Xanthomonas fuscans subsp. fuscans

8 hits

  1. XFF4834R_chr17230pyrBXFF4834R_chr17230probable aspartate carbamoyltransferase, catalytic subunit
  2. XFF4834R_chr19340pyrDXFF4834R_chr19340 probable dihydro-orotate oxidase, FMN-linked
  3. XFF4834R_chr23650pyrCXFF4834R_chr23650probable Dihydroorotase
  4. XFF4834R_chr27950pyrGXFF4834R_chr27950probable CTP synthetase
  5. XFF4834R_chr30780pyrHXFF4834R_chr30780probable uridylate kinase
  6. XFF4834R_chr37900pyrEXFF4834R_chr37900probable orotate phosphoribosyltransferase
  7. XFF4834R_chr39340XFF4834R_chr42550972_4531916_f3_XFF4834R-XFF4834R_chr39340XFF4834R_chr39340putative 2-dehydropantoate 2-reductase
  8. XFF4834R_chr41420pyrFXFF4834R_chr41420probable orotidine-5'-phosphate decarboxylase

pyrB XFF4834R_chr17230
XFF4834R_chr17230
XFF4834R_chr17230 		Cluster
DrawMap 		XML file

FASTA file 		Extract
Sequence 		Codon
Usage 		Framed OrthoMCL XFF4834R_chr_1849
XFF4834R_chr_1849
ID pyrB
AC XFF4834R_chr17230
LT XFF4834R_chr17230
OR XFF4834R_chr from 1970257 to 1971204 on strand +
DE probable aspartate carbamoyltransferase, catalytic subunit
IP Aspartate carbamoyltransferase, eukaryotic; Aspartate/ornithine carbamoyltransferase, Asp/Orn-binding region; Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding
CL 1.5.2.2 Pyrimidine biosynthesis GO:0006221
EC
GO InterPro
Biological Process: 'de novo' pyrimidine base biosynthetic process (GO:0006207)
Biological Process: cellular amino acid metabolic process (GO:0006520)
Molecular Function: carboxyl- or carbamoyltransferase activity (GO:0016743)
Molecular Function: aspartate carbamoyltransferase activity (GO:0004070)
Molecular Function: amino acid binding (GO:0016597)

Curated
PM
AN blastp avec pyrB coli : 32% sur la totalite
CC COG: [F] Nucleotide transport and metabolism;
CC MODEL: XFF4834R
CC STATUS: curated by brin (20100906)
MW 33687.2 Da
SQ 315 aa
  
........10........20........30........40........50
         |         |         |         |         |
MTTMQLDSDGRLCHLLTLEGLPRTTLLQLLDRAGQIRDAAVGRVGKRSVL
AGTAVCTLFFEPSTRTRSSFHLAAQRLGADVLNFDASTSSTRKGETARDT
LKNLEAMGVRGFVVRHPDDGAVEALAAAAGEGTALINAGDGRSAHPTQGL
LDMLTLRQAKGTDFSKLKVVIVGDVKHSRVARSDLHALRTLGAGEIRVCG
PASLLPEDDMLEGCVVGQDFDAMLEGADALMMLRLQRERMEEGLLPSLEQ
YHTEYGLTRERLARAGRDAAVLHPGPINRGVEITDEVADGAQSCVLRQVA
NGVAVRMAVLETLLG

    






    

        
            
                X.species
            
                
        
YP_364792.1 lcl|pyrB-XCV3061

        
1

	
315

	
S=1497 I=93 E=2.35438e-174

	
aspartate carbamoyltransferase catalytic subunit

     	

   





    

        
            
                X.species
            
                
        
NP_638094.1 lcl|pyrB-XCC2746

        
1

	
315

	
S=1480 I=92 E=2.70231e-172

	
aspartate carbamoyltransferase catalytic subunit

     	

   





    

        
            
                X.species
            
                
        
NP_643225.1 lcl|pyrB-XAC2916

        
1

	
315

	
S=1479 I=93 E=3.9659e-172

	
aspartate carbamoyltransferase catalytic subunit

     	

   





    

        
            
                X.species
            
                
        
 lcl|PyrB-XALc_2155

        
1

	
315

	
S=1347 I=84 E=3.87929e-156

	
putative aspartate carbamoyltransferase, catalytic subunit protein

     	

   





    

        
                pubmed
        
        

        
4

	
310

	
S=775 I=53 E=3.06731e-85

	
Aspartate carbamoyltransferase EC=2.1.3.2 ; Pyrimidine biosynthesis

	
Pubmed 7896697

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
3

	
313

	
S=768 I=54 E=2.1624e-84

	
Aspartate carbamoyltransferase EC=2.1.3.2 ; Pyrimidine biosynthesis

	
Pubmed 19077236

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
4

	
310

	
S=756 I=52 E=6.36941e-83

	
Aspartate carbamoyltransferase EC=2.1.3.2 ; Pyrimidine biosynthesis

	
Pubmed 8234318

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
5

	
310

	
S=683 I=47 E=4.34526e-74

	
Aspartate carbamoyltransferase EC=2.1.3.2 ; Pyrimidine biosynthesis

	
Pubmed 9682487

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
14

	
313

	
S=666 I=50 E=4.08117e-72

	
Aspartate carbamoyltransferase EC=2.1.3.2 ; Pyrimidine biosynthesis

	
Pubmed 17965706

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
14

	
314

	
S=642 I=51 E=3.44948e-69

	
Aspartate carbamoyltransferase EC=2.1.3.2 ; Pyrimidine biosynthesis

	
Pubmed 9171389

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
12

	
314

	
S=616 I=46 E=5.32096e-66

	
Aspartate carbamoyltransferase EC=2.1.3.2 ; Pyrimidine biosynthesis

	
Pubmed 18367281

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
15

	
315

	
S=616 I=46 E=5.65582e-66

	
Aspartate carbamoyltransferase EC=2.1.3.2 ; Pyrimidine biosynthesis

	
Pubmed 18441057

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
15

	
310

	
S=612 I=45 E=1.41279e-65

	
Aspartate carbamoyltransferase EC=2.1.3.2 ; Pyrimidine biosynthesis

	
Pubmed 18391199

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
15

	
315

	
S=611 I=46 E=2.147e-65

	
Aspartate carbamoyltransferase EC=2.1.3.2

	
Pubmed 12446909

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
1

	
315

	
S=1497 I=93 E=6.14145e-173

	
Aspartate carbamoyltransferase EC=2.1.3.2 ; Pyrimidine biosynthesis

	

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
1

	
315

	
S=1481 I=93 E=5.28658e-171

	
Aspartate carbamoyltransferase EC=2.1.3.2 ; Pyrimidine biosynthesis

	

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
1

	
315

	
S=1481 I=93 E=5.28658e-171

	
Aspartate carbamoyltransferase EC=2.1.3.2 ; Pyrimidine biosynthesis

	

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
1

	
315

	
S=1480 I=92 E=7.04903e-171

	
Aspartate carbamoyltransferase EC=2.1.3.2 ; Pyrimidine biosynthesis

	

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
1

	
315

	
S=1480 I=92 E=7.04903e-171

	
Aspartate carbamoyltransferase EC=2.1.3.2 ; Pyrimidine biosynthesis

	

    

    

         
        
prodomImg

    





    

        
            
                
            
                
        
PD000708

        
14

	
96

	
S=151 I=43 E=9.35152e-11

    	
    





    

        
            
                
            
                
        
PD409592

        
255

	
315

	
S=139 I=52 E=2.27375e-09

    	
    





    

        
            
                
            
                
        
PDA4M8Y6

        
99

	
213

	
S=138 I=35 E=3.08511e-09

    	
    





    

        
            
                
            
                
        
PDA239L5

        
153

	
239

	
S=121 I=37 E=3.16159e-07

    	
    





    

        
            
                
            
                
        
PDA7V852

        
168

	
206

	
S=115 I=62 E=1.79234e-06

    	
    





    

        
            
                
            
                
        
PDA1F845

        
210

	
252

	
S=111 I=59 E=5.14738e-06

    	
    




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  Validation code (copy this one TtLxe1Yy)  
 
     



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                pubmed
            
        
	    
            
Set of Uniprot with relevant PubMed cross-references ncbi-blastp

        		
 	    
            96 hits
        
    

    

        
            
                swiss-prot
            
        
	    
            
Swiss-Prot ncbi-blastp

        		
 	    
            0 hits
        
    

    
    
    

        
            
                XFF4834R
            
        
    	
            
Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp

        		        
        
            0 hits
        
    

        
    

        
            
                hamap
            
        
	
            
HAMAP scan

        		        
        
            0 hits
        
    

    
    

	    
            
                Interpro Scan
            
            
	        
                
IprScan

            		        
            
                0 hits
            
    








Show or not Miscellaneous analyses




    
    
        
  • ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBtLmBeB/XFF4834R_chr17230.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

    • 
    
    
    
    
        
  • ERROR Tag PERLLIB Portal/Tools.pl GetNcbiBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBtLmBeB/XFF4834R_chr17230.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

    • 
    

    
    
        
  • ERROR Tag PERLLIB Portal/Tools.pl GetUniprotBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBtLmBeB/XFF4834R_chr17230.xml_fasta"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

    • 
    

    
    
        
  • ERROR Tag PERLLIB Portal/Tools.pl GetKeggBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBtLmBeB/XFF4834R_chr17230.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

    • 
    
    

    






pyrD XFF4834R_chr19340




    

         
             
            XFF4834R_chr19330
            
XFF4834R_chr19330
            
        		


       
           
	   Cluster
	   
DrawMap
	   
        		
	
        
            XML file
        	


	    FASTA file
        		
	
	
             
            Extract
Sequence
            
        		
	
	
             
            Codon
Usage
            
        		
    
    
            
            Framed
            
     
  	



	
            OrthoMCL
            
    
  	
    
    
    

     


	
             
            XFF4834R_chr19350
            
XFF4834R_chr19350
            
        		

    





    

        ID
        pyrD
    

    

        AC
        XFF4834R_chr19340
    

    

        LT
        XFF4834R_chr19340
    

    

        OR
        XFF4834R_chr from 2214328 to 2215383 on strand -
    

   

        DE
         probable dihydro-orotate oxidase, FMN-linked
  

   

        IP
        Dihydroorotate dehydrogenase, class 2; Aldolase-type TIM barrel
  
  
  
  

        CL
        1.5.2.2 Pyrimidine biosynthesis	GO:0006221 
    

  

        EC
        
    

    
    

        GO
        
            InterPro
Biological Process: 'de novo' pyrimidine base biosynthetic process (GO:0006207)
Biological Process: UMP biosynthetic process (GO:0006222)
Biological Process: oxidation reduction (GO:0055114)
Biological Process: metabolic process (GO:0008152)
Cellular Component: membrane (GO:0016020)
Molecular Function: catalytic activity (GO:0003824)
Molecular Function: dihydroorotate dehydrogenase activity (GO:0004152)
Molecular Function: dihydroorotate oxidase activity (GO:0004158)


            Curated

        		
    


  

        PM
        
    

  

        AN
        
    

  

        CC
        COG: [F] Nucleotide transport and metabolism; 
    

    

        CC
        MODEL: XFF4834R 
  
    
  

        CC
        STATUS: curated by brin (20100906)
  

  
  


    

        MW
        37553.7 Da
    


    

        SQ
        351 aa
    

    

         
        
........10........20........30........40........50
         |         |         |         |         |
MYSLARPFLFSLDAERAHALALRSIDTAYRTGTTALLARRPVPLPTPAFG
LMFPNPVGLGAGLDKNGEHIDALFALGFGFVEIGTVTPRAQEGNPKPRMF
RLPEYQAVINRMGFNNLGVDALVANVQRARRTAGLLGINIGKNKDTPNEE
ATSDYRYCMERVYPLADYITVNISSPNTAGLRELQEEQSLRRLISDLRET
QEALSAQHGKRVPMLVKVAPDLNDRDIDAAARVLADLAVDGVIATNTTVT
RTLVANHPLAAEAGGLSGAPLLGQSTLVLRRLRARLPESIPLIGVGGINS
GADAVAKMAAGASLVQCYSGLVYRGPQLIGECVNAIRRRREAPSGGAVSP
L

    






    

        
            
                X.species
            
                
        
NP_642132.1 lcl|pyrD-XAC1805

        
1

	
351

	
S=1584 I=91 E=0

	
dihydroorotate dehydrogenase 2

     	

   





    

        
            
                X.species
            
                
        
YP_363566.1 lcl|pyrD-XCV1835

        
1

	
351

	
S=1574 I=91 E=0

	
dihydroorotate dehydrogenase 2

     	

   





    

        
            
                X.species
            
                
        
NP_637154.1 lcl|pyrD-XCC1788

        
1

	
351

	
S=1498 I=85 E=2.0002e-174

	
dihydroorotate dehydrogenase 2

     	

   





    

        
            
                X.species
            
                
        
 lcl|XALc_1218

        
1

	
349

	
S=1246 I=72 E=7.73502e-144

	
putative dihydroorotate dehydrogenase (dihydroorotate oxidase) protein

     	

   





    

        
                pubmed
        
        

        
1

	
346

	
S=1274 I=71 E=1.19826e-145

	
Dihydroorotate dehydrogenase EC=1.3.3.1 ; Cell membrane Flavoprotein FMN Oxidoreductase Pyrimidine biosynthesis

	
Pubmed 11098140

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
1

	
338

	
S=851 I=49 E=1.85486e-94

	
Dihydroorotate dehydrogenase ; Cell membrane FMN Flavoprotein Oxidoreductase Pyrimidine biosynthesis

	
Pubmed 12517848

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
1

	
338

	
S=851 I=49 E=2.30661e-94

	
Dihydroorotate dehydrogenase ; Cell membrane FMN Flavoprotein Oxidoreductase Pyrimidine biosynthesis

	
Pubmed 12517848

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
1

	
338

	
S=850 I=49 E=2.34719e-94

	
Dihydroorotate dehydrogenase ; Cell membrane FMN Flavoprotein Oxidoreductase Pyrimidine biosynthesis

	
Pubmed 12517848

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
1

	
338

	
S=847 I=49 E=6.85943e-94

	
Dihydroorotate dehydrogenase ; Cell membrane FMN Flavoprotein Oxidoreductase Pyrimidine biosynthesis

	
Pubmed 12517848

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
1

	
338

	
S=846 I=49 E=7.95533e-94

	
Dihydroorotate dehydrogenase ; Cell membrane FMN Flavoprotein Oxidoreductase Pyrimidine biosynthesis

	
Pubmed 12517848

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
2

	
336

	
S=789 I=50 E=6.64339e-87

	
Dihydroorotate dehydrogenase EC=1.3.3.1 ; Cell membrane Flavoprotein FMN Oxidoreductase Pyrimidine biosynthesis

	
Pubmed 2992959

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
2

	
336

	
S=782 I=50 E=4.93498e-86

	
Dihydroorotate dehydrogenase EC=1.3.3.1 ; Cell membrane Flavoprotein FMN Oxidoreductase Pyrimidine biosynthesis

	
Pubmed 2269282

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
1

	
339

	
S=650 I=42 E=4.70259e-70

	
Dihydroorotate dehydrogenase EC=1.3.3.1 ; Cell membrane Flavoprotein FMN Oxidoreductase Pyrimidine biosynthesis

	
Pubmed 17107561

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
2

	
336

	
S=643 I=45 E=3.31523e-69

	
Dihydroorotate dehydrogenase EC=1.3.3.1 ; Cell membrane Flavoprotein FMN Oxidoreductase Pyrimidine biosynthesis

	
Pubmed 19077236

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
1

	
351

	
S=1584 I=91 E=0

	
Dihydroorotate dehydrogenase EC=1.3.3.1 ; Cell membrane Flavoprotein FMN Oxidoreductase Pyrimidine biosynthesis

	

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
1

	
351

	
S=1574 I=91 E=0

	
Dihydroorotate dehydrogenase EC=1.3.3.1 ; Cell membrane Flavoprotein FMN Oxidoreductase Pyrimidine biosynthesis

	

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
1

	
351

	
S=1539 I=88 E=5.43099e-178

	
Dihydroorotate dehydrogenase EC=1.3.3.1 ; Cell membrane Flavoprotein FMN Oxidoreductase Pyrimidine biosynthesis

	

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
1

	
351

	
S=1539 I=88 E=5.43099e-178

	
Dihydroorotate dehydrogenase EC=1.3.3.1 ; Cell membrane Flavoprotein FMN Oxidoreductase Pyrimidine biosynthesis

	

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
1

	
351

	
S=1534 I=88 E=2.13482e-177

	
Dihydroorotate dehydrogenase EC=1.3.3.1 ; Cell membrane Flavoprotein FMN Oxidoreductase Pyrimidine biosynthesis

	

    

    

         
        
prodomImg

    





    

        
            
                
            
                
        
PD001761

        
50

	
171

	
S=358 I=55 E=6.85062e-36

    	
    





    

        
            
                
            
                
        
PD637720

        
133

	
193

	
S=246 I=70 E=2.25711e-22

    	
    





    

        
            
                
            
                
        
PDA1V3J9

        
325

	
351

	
S=120 I=85 E=4.67698e-07

    	
    





    

        
            
                
            
                
        
PD190440

        
1

	
45

	
S=115 I=56 E=1.95413e-06

    	
    





    

        
            
                
            
                
        
PDA4W7A3

        
210

	
275

	
S=111 I=41 E=6.45214e-06

    	
    




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Show or not Access unfiltered results






    

       
            
                pubmed
            
        
	    
            
Set of Uniprot with relevant PubMed cross-references ncbi-blastp

        		
 	    
            47 hits
        
    

    

        
            
                swiss-prot
            
        
	    
            
Swiss-Prot ncbi-blastp

        		
 	    
            360 hits
        
    

    
    
    

        
            
                XFF4834R
            
        
    	
            
Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp

        		        
        
            0 hits
        
    

        
    

        
            
                hamap
            
        
	
            
HAMAP scan

        		        
        
            0 hits
        
    

    
    

	    
            
                Interpro Scan
            
            
	        
                
IprScan

            		        
            
                0 hits
            
    








Show or not Miscellaneous analyses




    
    
        
  • ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBtLmBeB/XFF4834R_chr19340.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

    • 
    
    
    
    
        
  • ERROR Tag PERLLIB Portal/Tools.pl GetNcbiBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBtLmBeB/XFF4834R_chr19340.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

    • 
    

    
    
        
  • ERROR Tag PERLLIB Portal/Tools.pl GetUniprotBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBtLmBeB/XFF4834R_chr19340.xml_fasta"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

    • 
    

    
    
        
  • ERROR Tag PERLLIB Portal/Tools.pl GetKeggBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBtLmBeB/XFF4834R_chr19340.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

    • 
    
    

    






pyrC XFF4834R_chr23650




    

         
             
            XFF4834R_chr23640
            
XFF4834R_chr23640
            
        		


       
           
	   Cluster
	   
DrawMap
	   
        		
	
        
            XML file
        	


	    FASTA file
        		
	
	
             
            Extract
Sequence
            
        		
	
	
             
            Codon
Usage
            
        		
    
    
            
            Framed
            
     
  	



	
            OrthoMCL
            
    
  	
    
    
    

     


	
             
            XFF4834R_chr23660
            
XFF4834R_chr23660
            
        		

    





    

        ID
        pyrC
    

    

        AC
        XFF4834R_chr23650
    

    

        LT
        XFF4834R_chr23650
    

    

        OR
        XFF4834R_chr from 2734931 to 2736280 on strand +
    

   

        DE
        probable Dihydroorotase
  

   

        IP
        Amidohydrolase 1; Metal-dependent hydrolase, composite domain
  
  
  
  

        CL
        1.5.2.2 Pyrimidine biosynthesis	GO:0006221 
    

  

        EC
        
    

    
    

        GO
        
            InterPro
Molecular Function: hydrolase activity (GO:0016787)
acting on carbon-nitrogen (but not peptide) bonds (GO:0016810)
in cyclic amides (GO:0016812)


            Curated

        		
    


  

        PM
        
    

  

        AN
        nomme au depart allB comme chez coli Bsub ai plutot suivi les xantho
    

  

        CC
        COG: [F] Nucleotide transport and metabolism; 
    

    

        CC
        MODEL: XFF4834R 
  
    
  

        CC
        STATUS: curated by brin (20100907)
  

  
  


    

        MW
        49092.3 Da
    


    

        SQ
        449 aa
    

    

         
        
........10........20........30........40........50
         |         |         |         |         |
MSRTVIVNARLVNEGKEFDADLLIEGGRIAKIDSKIVPAPGDTVVDAAGR
WVLPGMIDDQVHFREPGLTHKGDIATESGAAVAGGLTSFMDMPNTNPPTL
DAPALQAKYDAAAGRAWANYGFYMGASNDNLAHIQSLAPKTAPGIKVFMG
ASTGNMLVDNPETLDAIFRDAPTPIITHCEDTPTIDATMAQYKEKYGDAL
TPEMHPDIRSRQACLKSSQLAVSLARKHNTRLHVLHISTADELSLFEAGP
LVDADGKLRKRITAETCIHFLRFDRSDYARLGNLIKCNPAIKDAEDRLAL
IDALAEDVIDVLATDHAPHTWEEKQKPYAQAPSGLPLVQYALVAALELVH
EGKLPITRIVQKFAHAPAQLFDVEERGFLREGYFADLVMIDNTPFTVKRE
QVLSKCGWSPFEGTTFRSRIAATWVNGQQVWDGEQLVGSAAGQRLTFDR

    






    

        
            
                X.species
            
                
        
NP_642676.1 pyrC-XAC2360

        
1

	
449

	
S=2386 I=100 E=0

	
dihydroorotase

     	

   





    

        
            
                X.species
            
                
        
YP_364290.1 pyrC-XCV2559

        
1

	
449

	
S=2361 I=98 E=0

	
dihydroorotase

     	

   





    

        
            
                X.species
            
                
        
NP_637612.1 pyrC-XCC2257

        
1

	
449

	
S=2300 I=96 E=0

	
dihydroorotase

     	

   





    

        
            
                X.species
            
                
        
XALc_1913 pyrC-XALc_1913

        
4

	
449

	
S=1866 I=79 E=0

	
putative dihydroorotase domain protein

     	

   





    

        
                pubmed
        
        

        
5

	
442

	
S=526 I=35 E=7.31824e-55

	
Putative allantoinase

	
Pubmed 20081001

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
16

	
440

	
S=468 I=31 E=7.5338e-48

	
Dihydroorotase EC=3.5.2.3 ; Hydrolase Metal-binding Pyrimidine biosynthesis Zinc

	
Pubmed 7929010

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
5

	
436

	
S=445 I=29 E=4.98839e-45

	
Allantoinase EC=3.5.2.5 ; Hydrolase Metal-binding Purine metabolism Zinc

	
Pubmed 11344136

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
3

	
431

	
S=425 I=30 E=1.22249e-42

	
Dihydroorotase EC=3.5.2.3 ; Hydrolase Metal-binding Pyrimidine biosynthesis Zinc

	
Pubmed 15780005

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
14

	
431

	
S=418 I=29 E=9.40345e-42

	
Dihydroorotase EC=3.5.2.3 ; Hydrolase Metal-binding Pyrimidine biosynthesis Zinc

	
Pubmed 18391199

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
1

	
416

	
S=479 I=30 E=2.2204e-49

	
Dihydroorotase EC=3.5.2.3 ; Hydrolase Metal-binding Pyrimidine biosynthesis Zinc

	

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
6

	
413

	
S=471 I=32 E=2.50656e-48

	
Dihydroorotase EC=3.5.2.3 ; Hydrolase Metal-binding Pyrimidine biosynthesis Zinc

	

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
1

	
445

	
S=470 I=32 E=2.80739e-48

	
Allantoinase EC=3.5.2.5 ; Hydrolase Metal-binding Purine metabolism Zinc

	

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
16

	
440

	
S=468 I=31 E=5.12356e-48

	
Dihydroorotase EC=3.5.2.3 ; Hydrolase Metal-binding Pyrimidine biosynthesis Zinc

	

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
6

	
413

	
S=465 I=32 E=1.23597e-47

	
Dihydroorotase EC=3.5.2.3 ; Hydrolase Metal-binding Pyrimidine biosynthesis Zinc

	

    

    

         
        
prodomImg

    





    

        Iprscan
        
	[G3DSA:3.20.20.140]
	
55

	
417

	
	
-

    





    

        Iprscan
        
	[PTHR11647:SF5]
	
44

	
449

	
	
-

    





    

        Iprscan
        
	[PTHR11647]
	
44

	
449

	
	
-

    





    

        Iprscan
        IPR006680
	[PF01979]
	
51

	
391

	
	
Amidohydrolase 1

    





    

        Iprscan
        IPR002195
	[PS00483]
	
313

	
324

	
	
Dihydroorotase, conserved site

    





    

        
            
                
            
                
        
PD001085

        
60

	
383

	
S=341 I=34 E=8.94818e-34

    	
    





    

        
            
                
            
                
        
PD684713

        
384

	
449

	
S=143 I=40 E=8.61901e-10

    	
    





    

        
            
                
            
                
        
PDA1S5B3

        
417

	
449

	
S=137 I=73 E=4.36262e-09

    	
    





    

        
            
                
            
                
        
PDA1S5B2

        
426

	
449

	
S=131 I=100 E=2.15118e-08

    	
    





    

        
            
                
            
                
        
PD840262

        
4

	
167

	
S=130 I=26 E=3.15707e-08

    	
    





    

        
            
                
            
                
        
PD929867

        
6

	
66

	
S=113 I=41 E=4.16607e-06

    	
    





    

        
            
                
            
                
        
PDA7B699

        
1

	
71

	
S=103 I=33 E=6.38121e-05

    	
    





    

        
            
                
            
                
        
PD613779

        
1

	
99

	
S=102 I=28 E=7.73047e-05

    	
    





    

        Iprscan
        
	[SSF51556]
	
55

	
379

	
	
-

    





    

        Iprscan
        IPR011059
	[SSF51338]
	
1

	
429

	
	
Metal-dependent hydrolase, composite domain

    




Show or not Suggestions
Suggest an annotation


Move your mouse over each field to get more informations


ID


DE


EC


GO


PM



CC


CL

 
  Your email  
 
  Validation code (copy this one SJxGJCV8)  
 
     



Show or not Access unfiltered results






    

       
            
                pubmed
            
        
	    
            
Set of Uniprot with relevant PubMed cross-references ncbi-blastp

        		
 	    
            103 hits
        
    

    

        
            
                swiss-prot
            
        
	    
            
Swiss-Prot ncbi-blastp

        		
 	    
            259 hits
        
    

    
    
    

        
            
                XFF4834R
            
        
    	
            
Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp

        		        
        
            1 hits
        
    

        
    

        
            
                hamap
            
        
	
            
HAMAP scan

        		        
        
            0 hits
        
    

    
    

	    
            
                Interpro Scan
            
            
	        
                
IprScan

            		        
            
                7 hits
            
    








Show or not Miscellaneous analyses




    
    
        
  • ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBtLmBeB/XFF4834R_chr23650.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

    • 
    
    
    
    
        
  • ERROR Tag PERLLIB Portal/Tools.pl GetNcbiBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBtLmBeB/XFF4834R_chr23650.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

    • 
    

    
    
        
  • ERROR Tag PERLLIB Portal/Tools.pl GetUniprotBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBtLmBeB/XFF4834R_chr23650.xml_fasta"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

    • 
    

    
    
        
  • ERROR Tag PERLLIB Portal/Tools.pl GetKeggBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBtLmBeB/XFF4834R_chr23650.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

    • 
    
    

    






pyrG XFF4834R_chr27950




    

         
             
            XFF4834R_chr27940
            
XFF4834R_chr27940
            
        		


       
           
	   Cluster
	   
DrawMap
	   
        		
	
        
            XML file
        	


	    FASTA file
        		
	
	
             
            Extract
Sequence
            
        		
	
	
             
            Codon
Usage
            
        		
    
    
            
            Framed
            
     
  	



	
            OrthoMCL
            
    
  	
    
    
    

     


	
             
            XFF4834R_chr27960
            
XFF4834R_chr27960
            
        		

    





    

        ID
        pyrG
    

    

        AC
        XFF4834R_chr27950
    

    

        LT
        XFF4834R_chr27950
    

    

        OR
        XFF4834R_chr from 3221501 to 3223165 on strand -
    

   

        DE
        probable CTP synthetase
  

   

        IP
        CTP synthase
  
  
  
  

        CL
        1.5.2.2 Pyrimidine biosynthesis	GO:0006221 
    

  

        EC
        
    

    
    

        GO
        
            InterPro
Biological Process: pyrimidine nucleotide biosynthetic process (GO:0006221)
Molecular Function: CTP synthase activity (GO:0003883)
Molecular Function: catalytic activity (GO:0003824)


            Curated

        		
    


  

        PM
        
    

  

        AN
        
    

  

        CC
        COG: [F] Nucleotide transport and metabolism; 
    

    

        CC
        MODEL: XFF4834R 
  
    
  

        CC
        STATUS: curated by brin (20100907)
  

  
  


    

        MW
        61490.5 Da
    


    

        SQ
        554 aa
    

    

         
        
........10........20........30........40........50
         |         |         |         |         |
MTPLIFVTGGVVSSLGKGIAAASLASILEARGLKVTMMKLDPYINVDPGT
MSPFQHGEVYVTDDGAETDLDLGHYERYVRTRLSRKNSVTTGRIYENVIR
KERRGDYLGATVQVIPHITDEIRRCIDEATAGFDVALIEIGGTVGDIESL
PFLEAIRQVRTERGAEKAMFMHLTLVPYIAAAGELKTKPTQHSVKELRSI
GIQPDVLLCRSEQAVPDSERRKIALFTNVSERAVISCPDIDVLYGMPLEL
LRQGLDELVIDQFKLRDKVAAADLSEWAAVVDAVKHPLDEVNIAVVGKYV
DHQDAYKSVAEALRHGGLRQRTKVNLKWLEAQDLEGSDMSALQDIDGILV
PGGFGDRGFEGKVQTSKFAREHKVPYFGICYGMQAAVVDYARHVADLDAA
NSTENDRQSPHPVIGLITEWRTATGEVEKRDEKSDLGGTMRLGLQEQRLK
PGTLAREVYGKDVVAERHRHRYEFNNRYRTQLEDAGLVISGKSMDDTLVE
VVELPRDTHPWFLACQAHPEFLSTPRDGHPLFIGFVRAAREKKAGGKLLK
EARA

    






    

        
            
                X.species
            
                
        
NP_642047.1 pyrG-XAC1716

        
1

	
554

	
S=2839 I=97 E=0

	
CTP synthetase

     	

   





    

        
            
                X.species
            
                
        
YP_363480.1 pyrG-XCV1749

        
1

	
554

	
S=2836 I=97 E=0

	
CTP synthetase

     	

   





    

        
            
                X.species
            
                
        
NP_637067.2 pyrG-XCC1697

        
1

	
554

	
S=2796 I=95 E=0

	
CTP synthetase

     	

   





    

        
            
                X.species
            
                
        
XALc_1149 pyrG-XALc_1149

        
1

	
554

	
S=2672 I=90 E=0

	
probable ctp synthase (utp--ammonia ligase) protein

     	

   





    

        
                pubmed
        
        

        
2

	
541

	
S=1776 I=62 E=0

	
CTP synthase EC=6.3.4.2 ; ATP-binding Glutamine amidotransferase Ligase Nucleotide-binding Pyrimidine biosynthesis

	
Pubmed 3514618

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
1

	
539

	
S=1712 I=58 E=0

	
CTP synthase EC=6.3.4.2 ; ATP-binding Glutamine amidotransferase Ligase Nucleotide-binding Pyrimidine biosynthesis

	
Pubmed 9711852

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
45

	
545

	
S=1684 I=61 E=0

	
Putative uncharacterized protein

	
Pubmed 8790892

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
47

	
541

	
S=1600 I=60 E=0

	
CTP synthetase

	
Pubmed 12668143

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
1

	
543

	
S=1508 I=54 E=1.04484e-173

	
CTP synthase EC=6.3.4.2 ; ATP-binding Glutamine amidotransferase Ligase Nucleotide-binding Pyrimidine biosynthesis

	
Pubmed 8138139

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
1

	
554

	
S=2839 I=97 E=0

	
CTP synthase EC=6.3.4.2 ; ATP-binding Glutamine amidotransferase Ligase Nucleotide-binding Pyrimidine biosynthesis

	

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
1

	
554

	
S=2836 I=97 E=0

	
CTP synthase EC=6.3.4.2 ; ATP-binding Glutamine amidotransferase Ligase Nucleotide-binding Pyrimidine biosynthesis

	

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
1

	
554

	
S=2818 I=96 E=0

	
CTP synthase EC=6.3.4.2 ; ATP-binding Glutamine amidotransferase Ligase Nucleotide-binding Pyrimidine biosynthesis

	

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
1

	
554

	
S=2818 I=96 E=0

	
CTP synthase EC=6.3.4.2 ; ATP-binding Glutamine amidotransferase Ligase Nucleotide-binding Pyrimidine biosynthesis

	

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
1

	
554

	
S=2818 I=96 E=0

	
CTP synthase EC=6.3.4.2 ; ATP-binding Glutamine amidotransferase Ligase Nucleotide-binding Pyrimidine biosynthesis

	

    

    

         
        
prodomImg

    





    

        Iprscan
        
	[G3DSA:3.40.50.300]
	
2

	
286

	
	
-

    





    

        Iprscan
        
	[G3DSA:3.40.50.880]
	
287

	
548

	
	
-

    





    

        Iprscan
        IPR004468
	[MF_01227]
	
2

	
543

	
	
CTP synthase

    





    

        Iprscan
        
	[PTHR11550]
	
117

	
542

	
	
-

    





    

        Iprscan
        IPR017456
	[PF06418]
	
4

	
269

	
	
CTP synthase, N-terminal

    





    

        Iprscan
        IPR000991
	[PF00117]
	
303

	
537

	
	
Glutamine amidotransferase class-I, C-terminal

    





    

        Iprscan
        IPR004468
	[TIGR00337]
	
1

	
538

	
	
CTP synthase

    





    

        Iprscan
        IPR017926
	[PS51273]
	
292

	
545

	
	
Glutamine amidotransferase type 1

    





    

        Iprscan
        
	[seg]
	
13

	
28

	
	
-

    





    

        Iprscan
        
	[SignalP-NN(euk)]
	
1

	
30

	
	
-

    





    

        
            
                
            
                
        
PD002309

        
114

	
229

	
S=426 I=70 E=4.78809e-44

    	
    





    

        
            
                
            
                
        
PD962121

        
319

	
421

	
S=311 I=52 E=3.48784e-30

    	
    





    

        
            
                
            
                
        
PDA1F6Q9

        
51

	
111

	
S=254 I=72 E=3.01602e-23

    	
    





    

        
            
                
            
                
        
PD888152

        
428

	
495

	
S=219 I=64 E=5.63134e-19

    	
    





    

        
            
                
            
                
        
PD002477

        
499

	
543

	
S=162 I=60 E=4.54147e-12

    	
    





    

        
            
                
            
                
        
PDA0B0B4

        
1

	
49

	
S=142 I=59 E=1.16256e-09

    	
    





    

        
            
                
            
                
        
PDA1F6S3

        
234

	
295

	
S=124 I=47 E=1.52079e-07

    	
    





    

        
            
                
            
                
        
PD845300

        
295

	
331

	
S=123 I=57 E=2.27117e-07

    	
    





    

        
            
                
            
                
        
PD845301

        
441

	
543

	
S=121 I=29 E=3.83213e-07

    	
    





    

        
            
                
            
                
        
PDA0G8M3

        
33

	
111

	
S=103 I=28 E=5.91616e-05

    	
    





    

        Iprscan
        
	[SSF52540]
	
1

	
270

	
	
-

    





    

        Iprscan
        
	[SSF52317]
	
288

	
547

	
	
-

    




Show or not Suggestions
Suggest an annotation


Move your mouse over each field to get more informations


ID


DE


EC


GO


PM



CC


CL

 
  Your email  
 
  Validation code (copy this one iSlkuv1S)  
 
     



Show or not Access unfiltered results






    

       
            
                pubmed
            
        
	    
            
Set of Uniprot with relevant PubMed cross-references ncbi-blastp

        		
 	    
            159 hits
        
    

    

        
            
                swiss-prot
            
        
	    
            
Swiss-Prot ncbi-blastp

        		
 	    
            0 hits
        
    

    
    
    

        
            
                XFF4834R
            
        
    	
            
Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp

        		        
        
            0 hits
        
    

        
    

        
            
                hamap
            
        
	
            
HAMAP scan

        		        
        
            0 hits
        
    

    
    

	    
            
                Interpro Scan
            
            
	        
                
IprScan

            		        
            
                12 hits
            
    








Show or not Miscellaneous analyses




    
    
        
  • ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBtLmBeB/XFF4834R_chr27950.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

    • 
    
    
    
    
        
  • ERROR Tag PERLLIB Portal/Tools.pl GetNcbiBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBtLmBeB/XFF4834R_chr27950.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

    • 
    

    
    
        
  • ERROR Tag PERLLIB Portal/Tools.pl GetUniprotBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBtLmBeB/XFF4834R_chr27950.xml_fasta"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

    • 
    

    
    
        
  • ERROR Tag PERLLIB Portal/Tools.pl GetKeggBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBtLmBeB/XFF4834R_chr27950.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

    • 
    
    

    






pyrH XFF4834R_chr30780




    

         
             
            XFF4834R_chr30770
            
XFF4834R_chr30770
            
        		


       
           
	   Cluster
	   
DrawMap
	   
        		
	
        
            XML file
        	


	    FASTA file
        		
	
	
             
            Extract
Sequence
            
        		
	
	
             
            Codon
Usage
            
        		
    
    
            
            Framed
            
     
  	



	
            OrthoMCL
            
    
  	
    
    
    

     


	
             
            XFF4834R_chr30790
            
XFF4834R_chr30790
            
        		

    





    

        ID
        pyrH
    

    

        AC
        XFF4834R_chr30780
    

    

        LT
        XFF4834R_chr30780
    

    

        OR
        XFF4834R_chr from 3542204 to 3542926 on strand +
    

   

        DE
        probable uridylate kinase
  

   

        IP
        Aspartate/glutamate/uridylate kinase
  
  
  
  

        CL
        1.5.2.2 Pyrimidine biosynthesis	GO:0006221 
    

  

        EC
        
    

    
    

        GO
        
            InterPro
Biological Process: pyrimidine nucleotide biosynthetic process (GO:0006221)
Biological Process: cellular amino acid biosynthetic process (GO:0008652)
Biological Process: 'de novo' pyrimidine base biosynthetic process (GO:0006207)
Cellular Component: cytoplasm (GO:0005737)
Molecular Function: UMP kinase activity (GO:0033862)
Molecular Function: uridylate kinase activity (GO:0009041)


            Curated

        		
    


  

        PM
        
    

  

        AN
        
    

  

        CC
        COG: [F] Nucleotide transport and metabolism; 
    

    

        CC
        MODEL: XFF4834R 
  
    
  

        CC
        STATUS: curated by brin (20100907)
  

  
  


    

        MW
        25767.4 Da
    


    

        SQ
        240 aa
    

    

         
        
........10........20........30........40........50
         |         |         |         |         |
MSELSYRRILLKLSGEALMGDGDYGIDPKVINRLAHEVIEAQQAGAQVAL
VIGGGNIFRGAGLAASGMDRVTGDHMGMLATVINALAMQDALETLGAKVR
VMSAIKINDVCEDFIRRRAIRHLEKGRIAIFAAGTGNPFFTTDSGAALRA
IEIGADLLLKATKVDGVYDKDPKKHTDAVRYDSLTYDQVILQGLEVMDTA
AFALARDSDLPLRIFGMSESGVLLRILHGEQIGTLVQGRS

    






    

        
            
                X.species
            
                
        
YP_363207.1 lcl|pyrH-XCV1476

        
1

	
240

	
S=1222 I=99 E=4.10237e-141

	
uridylate kinase

     	

   





    

        
            
                X.species
            
                
        
NP_641754.1 lcl|pyrH-XAC1419

        
1

	
240

	
S=1216 I=99 E=1.69916e-140

	
uridylate kinase

     	

   





    

        
            
                X.species
            
                
        
NP_636745.1 lcl|pyrH-XCC1371

        
1

	
240

	
S=1206 I=98 E=2.94051e-139

	
uridylate kinase

     	

   





    

        
            
                X.species
            
                
        
 lcl|pyrH-XALc_2028

        
1

	
239

	
S=1118 I=90 E=1.31784e-128

	
probable uridylate kinase protein

     	

   





    

        
                pubmed
        
        

        
4

	
237

	
S=738 I=59 E=6.28178e-81

	
Uridylate kinase EC=2.7.4.22 ; ATP-binding Cytoplasm Nucleotide-binding Pyrimidine biosynthesis Transferase

	
Pubmed 17107561

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
4

	
237

	
S=724 I=56 E=2.96291e-79

	
Uridylate kinase EC=2.7.4.22 ; ATP-binding Cytoplasm Nucleotide-binding Pyrimidine biosynthesis Transferase

	
Pubmed 17592475

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
6

	
237

	
S=706 I=60 E=4.11983e-77

	
Uridylate kinase EC=2.7.4.22 ; ATP-binding Cytoplasm Nucleotide-binding Pyrimidine biosynthesis Transferase

	
Pubmed 9973356

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
6

	
236

	
S=692 I=58 E=2.37468e-75

	
Uridylate kinase EC=2.7.4.22 ; Allosteric enzyme ATP-binding Cytoplasm Nucleotide-binding Pyrimidine biosynthesis Transferase

	
Pubmed 17210578

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
6

	
236

	
S=687 I=57 E=9.49859e-75

	
Uridylate kinase EC=2.7.4.22 ; Allosteric enzyme ATP-binding Cytoplasm Nucleotide-binding Pyrimidine biosynthesis Transferase

	
Pubmed 1447125,7711027

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
1

	
228

	
S=675 I=53 E=2.43354e-73

	
Uridylate kinase EC=2.7.4.22 ; ATP-binding Cytoplasm Nucleotide-binding Pyrimidine biosynthesis Transferase

	
Pubmed 17916642

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
1

	
236

	
S=671 I=54 E=6.92818e-73

	
Uridylate kinase EC=2.7.4.22 ; Allosteric enzyme ATP-binding Cytoplasm Nucleotide-binding Pyrimidine biosynthesis Transferase

	
Pubmed 17210578

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
2

	
236

	
S=667 I=53 E=2.22849e-72

	
Uridylate kinase EC=2.7.4.22 ; Allosteric enzyme ATP-binding Cytoplasm Nucleotide-binding Pyrimidine biosynthesis Transferase

	
Pubmed 15637156

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
4

	
237

	
S=657 I=54 E=4.24473e-71

	
Uridylate kinase EC=2.7.4.22 ; ATP-binding Cytoplasm Nucleotide-binding Pyrimidine biosynthesis Transferase

	
Pubmed 8617268

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
3

	
236

	
S=649 I=51 E=3.78671e-70

	
Uridylate kinase EC=2.7.4.22 ; Allosteric enzyme ATP-binding Cytoplasm Nucleotide-binding Pyrimidine biosynthesis Transferase

	
Pubmed 16707693

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
1

	
240

	
S=1222 I=99 E=1.0338e-139

	
Uridylate kinase EC=2.7.4.22 ; ATP-binding Cytoplasm Nucleotide-binding Pyrimidine biosynthesis Transferase

	

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
1

	
240

	
S=1216 I=99 E=4.28191e-139

	
Uridylate kinase EC=2.7.4.22 ; ATP-binding Cytoplasm Nucleotide-binding Pyrimidine biosynthesis Transferase

	

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
1

	
240

	
S=1214 I=98 E=9.54983e-139

	
Uridylate kinase EC=2.7.4.22 ; ATP-binding Cytoplasm Nucleotide-binding Pyrimidine biosynthesis Transferase

	

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
1

	
240

	
S=1214 I=98 E=9.54983e-139

	
Uridylate kinase EC=2.7.4.22 ; ATP-binding Cytoplasm Nucleotide-binding Pyrimidine biosynthesis Transferase

	

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
1

	
240

	
S=1206 I=98 E=7.4101e-138

	
Uridylate kinase EC=2.7.4.22 ; ATP-binding Cytoplasm Nucleotide-binding Pyrimidine biosynthesis Transferase

	

    

    

         
        
prodomImg

    





    

        
            
                
            
                
        
PD421181

        
19

	
75

	
S=175 I=60 E=1.03676e-13

    	
    





    

        
            
                
            
                
        
PDA7C3S9

        
4

	
75

	
S=145 I=51 E=4.1007e-10

    	
    





    

        
            
                
            
                
        
PDA0T8W4

        
102

	
133

	
S=129 I=75 E=3.37932e-08

    	
    





    

        
            
                
            
                
        
PD875552

        
197

	
240

	
S=124 I=50 E=1.55406e-07

    	
    





    

        
            
                
            
                
        
PDA707L1

        
76

	
131

	
S=119 I=45 E=6.1622e-07

    	
    





    

        
            
                
            
                
        
PDA2A285

        
76

	
124

	
S=111 I=42 E=6.26536e-06

    	
    





    

        
            
                
            
                
        
PD000447

        
133

	
190

	
S=103 I=53 E=5.21275e-05

    	
    





    

        
            
                
            
                
        
PDA310K8

        
76

	
132

	
S=102 I=42 E=7.78478e-05

    	
    




Show or not Suggestions
Suggest an annotation


Move your mouse over each field to get more informations


ID


DE


EC


GO


PM



CC


CL

 
  Your email  
 
  Validation code (copy this one IuJhVR2C)  
 
     



Show or not Access unfiltered results






    

       
            
                pubmed
            
        
	    
            
Set of Uniprot with relevant PubMed cross-references ncbi-blastp

        		
 	    
            119 hits
        
    

    

        
            
                swiss-prot
            
        
	    
            
Swiss-Prot ncbi-blastp

        		
 	    
            529 hits
        
    

    
    
    

        
            
                XFF4834R
            
        
    	
            
Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp

        		        
        
            0 hits
        
    

        
    

        
            
                hamap
            
        
	
            
HAMAP scan

        		        
        
            0 hits
        
    

    
    

	    
            
                Interpro Scan
            
            
	        
                
IprScan

            		        
            
                0 hits
            
    








Show or not Miscellaneous analyses




    
    
        
  • ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBtLmBeB/XFF4834R_chr30780.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

    • 
    
    
    
    
        
  • ERROR Tag PERLLIB Portal/Tools.pl GetNcbiBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBtLmBeB/XFF4834R_chr30780.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

    • 
    

    
    
        
  • ERROR Tag PERLLIB Portal/Tools.pl GetUniprotBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBtLmBeB/XFF4834R_chr30780.xml_fasta"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

    • 
    

    
    
        
  • ERROR Tag PERLLIB Portal/Tools.pl GetKeggBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBtLmBeB/XFF4834R_chr30780.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

    • 
    
    

    






pyrE XFF4834R_chr37900




    

         
             
            XFF4834R_chr37890
            
XFF4834R_chr37890
            
        		


       
           
	   Cluster
	   
DrawMap
	   
        		
	
        
            XML file
        	


	    FASTA file
        		
	
	
             
            Extract
Sequence
            
        		
	
	
             
            Codon
Usage
            
        		
    
    
            
            Framed
            
     
  	



	
            OrthoMCL
            
    
  	
    
    
    

     


	
             
            XFF4834R_chr37910
            
XFF4834R_chr37910
            
        		

    





    

        ID
        pyrE
    

    

        AC
        XFF4834R_chr37900
    

    

        LT
        XFF4834R_chr37900
    

    

        OR
        XFF4834R_chr from 4381247 to 4381906 on strand +
    

   

        DE
        probable orotate phosphoribosyltransferase
  

   

        IP
        Phosphoribosyltransferase
  
  
  
  

        CL
        1.5.2.2 Pyrimidine biosynthesis	GO:0006221 
    

  

        EC
        
    

    
    

        GO
        
            InterPro
Biological Process: pyrimidine nucleotide biosynthetic process (GO:0006221)
Biological Process: nucleoside metabolic process (GO:0009116)
Molecular Function: orotate phosphoribosyltransferase activity (GO:0004588)


            Curated

        		
    


  

        PM
        
    

  

        AN
        changement de start de 14 aa en moins
    

  

        CC
        COG: [F] Nucleotide transport and metabolism; 
    

    

        CC
        MODEL: XFF4834R 
  
    
  

        CC
        STATUS: curated by brin (20100907)
  

  
  


    

        MW
        22859.6 Da
    


    

        SQ
        219 aa
    

    

         
        
........10........20........30........40........50
         |         |         |         |         |
MTDHRTRFLQLALDADALRFGEFTLKSGRLSPYFFNAGRFDSGAKTAQLA
QCYADAIDAAGLDFDLLFGPAYKGIPLATALACTYAGRGRDLPLAFNRKE
AKDHGEGGTLIGAPLAGRKVLIIDDVITAGTATREALAIIRAAGGTPSGI
VVALDRQEIASDQDRRSAAQAVAAEAGIPVIAVANLGDLLAFAAGNADLV
GFQEPLLAYRGRYGTDTTG

    






    

        
            
                X.species
            
                
        
YP_365747.1 lcl|pyrE-XCV4016

        
1

	
219

	
S=1033 I=94 E=2.27559e-118

	
orotate phosphoribosyltransferase

     	

   





    

        
            
                X.species
            
                
        
NP_644204.1 lcl|pyrE-XAC3903

        
1

	
219

	
S=1026 I=93 E=1.7352e-117

	
orotate phosphoribosyltransferase

     	

   





    

        
            
                X.species
            
                
        
NP_639187.1 lcl|pyrE-XCC3847

        
1

	
219

	
S=1010 I=91 E=1.41754e-115

	
orotate phosphoribosyltransferase

     	

   





    

        
            
                X.species
            
                
        
 lcl|pyrE-XALc_0377

        
1

	
216

	
S=842 I=80 E=3.57458e-95

	
probable orotate phosphoribosyltransferase protein

     	

   





    

        
                pubmed
        
        

        
1

	
214

	
S=523 I=53 E=5.14762e-55

	
Orotate phosphoribosyltransferase EC=2.4.2.10 ; Glycosyltransferase Magnesium Pyrimidine biosynthesis

	
Pubmed 8824606

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
1

	
214

	
S=519 I=48 E=1.75996e-54

	
Orotate phosphoribosyltransferase EC=2.4.2.10 ; Glycosyltransferase Pyrimidine biosynthesis

	
Pubmed 10509020

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
1

	
215

	
S=515 I=50 E=5.96506e-54

	
Orotate phosphoribosyltransferase EC=2.4.2.10 ; Glycosyltransferase Magnesium Pyrimidine biosynthesis

	
Pubmed 11889481

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
1

	
215

	
S=512 I=49 E=1.07919e-53

	
Orotate phosphoribosyltransferase EC=2.4.2.10 ; Glycosyltransferase Magnesium Pyrimidine biosynthesis

	
Pubmed 8487307

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
1

	
215

	
S=496 I=48 E=1.07739e-51

	
Orotate phosphoribosyltransferase EC=2.4.2.10 ; Glycosyltransferase Magnesium Pyrimidine biosynthesis

	
Pubmed 6349999,6207018

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
1

	
195

	
S=489 I=50 E=6.96119e-51

	
Orotate phosphoribosyltransferase EC=2.4.2.10 ; Glycosyltransferase Pyrimidine biosynthesis

	
Pubmed 7597846

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
1

	
215

	
S=486 I=43 E=1.59368e-50

	
Orotate phosphoribosyl transferase

	
Pubmed 14981288

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
1

	
195

	
S=485 I=48 E=2.46449e-50

	
Orotate phosphoribosyltransferase 1 EC=2.4.2.10 ; Glycosyltransferase Pyrimidine biosynthesis

	
Pubmed 2651891

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
1

	
215

	
S=478 I=45 E=1.44673e-49

	
Orotate phosphoribosyltransferase EC=2.4.2.10 ; Glycosyltransferase Magnesium Pyrimidine biosynthesis

	
Pubmed 10675023

    

    

         
        
prodomImg

    





    

        
                pubmed
        
        

        
1

	
214

	
S=474 I=43 E=4.6131e-49

	
Orotate phosphoribosyltransferase EC=2.4.2.10 ; Glycosyltransferase

	
Pubmed 9862479

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
1

	
219

	
S=1033 I=94 E=5.64396e-117

	
Orotate phosphoribosyltransferase EC=2.4.2.10 ; Glycosyltransferase Magnesium Pyrimidine biosynthesis

	

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
1

	
219

	
S=1026 I=93 E=4.30367e-116

	
Orotate phosphoribosyltransferase EC=2.4.2.10 ; Glycosyltransferase Magnesium Pyrimidine biosynthesis

	

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
1

	
219

	
S=1010 I=91 E=3.5158e-114

	
Orotate phosphoribosyltransferase EC=2.4.2.10 ; Glycosyltransferase Magnesium Pyrimidine biosynthesis

	

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
1

	
219

	
S=1010 I=91 E=3.5158e-114

	
Orotate phosphoribosyltransferase EC=2.4.2.10 ; Glycosyltransferase Magnesium Pyrimidine biosynthesis

	

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
1

	
219

	
S=1010 I=91 E=3.5158e-114

	
Orotate phosphoribosyltransferase EC=2.4.2.10 ; Glycosyltransferase Magnesium Pyrimidine biosynthesis

	

    

    

         
        
prodomImg

    





    

        Iprscan
        
	[G3DSA:3.40.50.2020]
	
1

	
215

	
	
-

    





    

        Iprscan
        IPR000836
	[PF00156]
	
45

	
153

	
	
Phosphoribosyltransferase

    





    

        Iprscan
        IPR004467
	[TIGR00336]
	
10

	
189

	
	
Orotate phosphoribosyl transferase

    





    

        Iprscan
        
	[seg]
	
168

	
176

	
	
-

    





    

        
            
                
            
                
        
PDA1F8D3

        
42

	
117

	
S=222 I=60 E=2.22558e-19

    	
    





    

        
            
                
            
                
        
PD868993

        
190

	
219

	
S=145 I=97 E=3.75972e-10

    	
    





    

        
            
                
            
                
        
PDA1F8G2

        
8

	
41

	
S=131 I=65 E=1.93489e-08

    	
    





    

        Iprscan
        
	[SSF53271]
	
1

	
215

	
	
-

    




Show or not Suggestions
Suggest an annotation


Move your mouse over each field to get more informations


ID


DE


EC


GO


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CC


CL

 
  Your email  
 
  Validation code (copy this one xRlsTtIz)  
 
     



Show or not Access unfiltered results






    

       
            
                pubmed
            
        
	    
            
Set of Uniprot with relevant PubMed cross-references ncbi-blastp

        		
 	    
            120 hits
        
    

    

        
            
                swiss-prot
            
        
	    
            
Swiss-Prot ncbi-blastp

        		
 	    
            342 hits
        
    

    
    
    

        
            
                XFF4834R
            
        
    	
            
Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp

        		        
        
            1 hits
        
    

        
    

        
            
                hamap
            
        
	
            
HAMAP scan

        		        
        
            0 hits
        
    

    
    

	    
            
                Interpro Scan
            
            
	        
                
IprScan

            		        
            
                5 hits
            
    








Show or not Miscellaneous analyses




    
    
        
  • ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBtLmBeB/XFF4834R_chr37900.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

    • 
    
    
    
    
        
  • ERROR Tag PERLLIB Portal/Tools.pl GetNcbiBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBtLmBeB/XFF4834R_chr37900.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

    • 
    

    
    
        
  • ERROR Tag PERLLIB Portal/Tools.pl GetUniprotBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBtLmBeB/XFF4834R_chr37900.xml_fasta"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

    • 
    

    
    
        
  • ERROR Tag PERLLIB Portal/Tools.pl GetKeggBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBtLmBeB/XFF4834R_chr37900.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

    • 
    
    

    






XFF4834R_chr42550972_4531916_f3_XFF4834R-XFF4834R_chr39340 XFF4834R_chr39340




    

         
             
            XFF4834R_chr39330
            
XFF4834R_chr39330
            
        		


       
           
	   Cluster
	   
DrawMap
	   
        		
	
        
            XML file
        	


	    FASTA file
        		
	
	
             
            Extract
Sequence
            
        		
	
	
             
            Codon
Usage
            
        		
    
    
            
            Framed
            
     
  	



	
            OrthoMCL
            
    
  	
    
    
    

     


	
             
            XFF4834R_chr39350
            
XFF4834R_chr39350
            
        		

    





    

        ID
        XFF4834R_chr42550972_4531916_f3_XFF4834R-XFF4834R_chr39340
    

    

        AC
        XFF4834R_chr39340
    

    

        LT
        XFF4834R_chr39340
    

    

        OR
        XFF4834R_chr from 4530972 to 4531916 on strand +
    

   

        DE
        putative 2-dehydropantoate 2-reductase
  

   

        IP
        Ketopantoate reductase ApbA/PanE; Dehydrogenase, multihelical; Ketopantoate reductase ApbA/PanE, C-terminal; NAD(P)-binding domain
  
  
  
  

        CL
        1.5.2.2 Pyrimidine biosynthesis	GO:0006221 
    

  

        EC
        
    

    
    

        GO
        
            InterPro
Biological Process: oxidation reduction (GO:0055114)
Biological Process: pantothenate biosynthetic process (GO:0015940)
Biological Process: metabolic process (GO:0008152)
Cellular Component: cytoplasm (GO:0005737)
Molecular Function: oxidoreductase activity (GO:0016491)
Molecular Function: coenzyme binding (GO:0050662)
Molecular Function: catalytic activity (GO:0003824)
Molecular Function: NADP or NADPH binding (GO:0050661)
Molecular Function: binding (GO:0005488)


            Curated

        		
    


  

        PM
        
    

  

        AN
        
    

  

        CC
        COG: [H] Coenzyme transport and metabolism; 
    

    

        CC
        MODEL: XFF4834R 
  
    
  

        CC
        STATUS: curated by pieretti (20100412)
  

  
  


    

        MW
        33037.5 Da
    


    

        SQ
        314 aa
    

    

         
        
........10........20........30........40........50
         |         |         |         |         |
MAVRILILGAGGTGGYFGGRLAQAGVDVTFLVREARAAQLQADGLRIRSP
LGDADLQVAHVTAQDLPALVAQQPFDLVILSCKAYDLDSAIDAIAPAVGE
HTTVLPILNGLRHYAALDARFGAARVLGGLCFISATKGEHGEILHLGKPA
AITFGERSGDAHSARVQAFAAACAQADITHVASEKIAQEQWIKYSFLTAL
AAATCLMRAPVGAIVATDDGRALINGLYNECLWAADAAGQSIPEPARAKA
LQTLLQVDSPLKASMLRDLEAGQDVEAAQIVGDMLARVRETGRNAPLLMA
ANVHLQAYQVLRHR

    





Show or not Domain decomposition
 

    

        
            
                X.species
            
                
        
NP_644367.1 lcl|apbA-XAC4068

        
3

	
314

	
S=1439 I=90 E=2.63342e-167

	
2-dehydropantoate 2-reductase

     	

   





    

        
            
                X.species
            
                
        
YP_365885.1 lcl|XCV4154

        
1

	
313

	
S=1397 I=88 E=3.14937e-162

	
2-dehydropantoate 2-reductase

     	

   





    

        
            
                X.species
            
                
        
NP_639319.1 lcl|apbA-XCC3980

        
3

	
313

	
S=1341 I=86 E=2.17096e-155

	
2-dehydropantoate 2-reductase

     	

   





    

        
            
                X.species
            
                
        
 lcl|panE-XALc_3010

        
3

	
309

	
S=925 I=60 E=5.15602e-105

	
probable 2-dehydropantoate 2-reductase (ketopantoate reductase) protein

     	

   





    

        
                pubmed
        
        

        
21

	
307

	
S=126 I=25 E=1.30417e-06

	
2-dehydropantoate 2-reductase EC=1.1.1.169 ; NADP Oxidoreductase Pantothenate biosynthesis

	
Pubmed 17372221

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
20

	
309

	
S=410 I=34 E=3.02653e-41

	
Uncharacterized oxidoreductase ykpB EC=1.1.1.- ; NADP

	

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
20

	
296

	
S=167 I=25 E=9.0178e-12

	
Putative 2-dehydropantoate 2-reductase EC=1.1.1.169 ; Cytoplasm NADP Oxidoreductase Pantothenate biosynthesis

	

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
20

	
293

	
S=140 I=27 E=1.76025e-08

	
Putative 2-dehydropantoate 2-reductase EC=1.1.1.169 ; Cytoplasm NADP Oxidoreductase Pantothenate biosynthesis

	

    

    

         
        
prodomImg

    





    

        
                sp
        
        

        
39

	
290

	
S=110 I=26 E=8.43444e-05

	
Putative 2-dehydropantoate 2-reductase EC=1.1.1.169 ; Cytoplasm NADP Oxidoreductase Pantothenate biosynthesis

	

    

    

         
        
prodomImg

    





    

        Iprscan
        IPR016040
	[G3DSA:3.40.50.720]
	
3

	
147

	
	
NAD(P)-binding domain

    





    

        Iprscan
        IPR013328
	[G3DSA:1.10.1040.10]
	
185

	
309

	
	
Dehydrogenase, multihelical

    





    

        Iprscan
        IPR013332
	[PF02558]
	
5

	
159

	
	
Ketopantoate reductase ApbA/PanE, N-terminal

    





    

        Iprscan
        IPR013752
	[PF08546]
	
185

	
309

	
	
Ketopantoate reductase ApbA/PanE, C-terminal

    





    

        Iprscan
        IPR003710
	[TIGR00745]
	
4

	
312

	
	
Ketopantoate reductase ApbA/PanE

    





    

        Iprscan
        
	[seg]
	
9

	
19

	
	
-

    





    

        Iprscan
        
	[seg]
	
164

	
176

	
	
-

    





    

        
            
                
            
                
        
PDA1J0P3

        
194

	
268

	
S=195 I=56 E=4.15622e-16

    	
    





    

        
            
                
            
                
        
PDA203T1

        
41

	
73

	
S=149 I=94 E=1.46531e-10

    	
    





    

        
            
                
            
                
        
PDA4Q0J5

        
194

	
313

	
S=133 I=28 E=1.30611e-08

    	
    





    

        
            
                
            
                
        
PDA7I0R8

        
44

	
113

	
S=106 I=40 E=2.63996e-05

    	
    





    

        
            
                
            
                
        
PDA1F7W5

        
116

	
193

	
S=104 I=35 E=4.15428e-05

    	
    




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                pubmed
            
        
	    
            
Set of Uniprot with relevant PubMed cross-references ncbi-blastp

        		
 	    
            1 hits
        
    

    

        
            
                swiss-prot
            
        
	    
            
Swiss-Prot ncbi-blastp

        		
 	    
            4 hits
        
    

    
    
    

        
            
                XFF4834R
            
        
    	
            
Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp

        		        
        
            0 hits
        
    

        
    

        
            
                hamap
            
        
	
            
HAMAP scan

        		        
        
            0 hits
        
    

    
    

	    
            
                Interpro Scan
            
            
	        
                
IprScan

            		        
            
                7 hits
            
    








Show or not Miscellaneous analyses




    
    
        
  • ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBtLmBeB/XFF4834R_chr39340.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

    • 
    
    
    
    
        
  • ERROR Tag PERLLIB Portal/Tools.pl GetNcbiBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBtLmBeB/XFF4834R_chr39340.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

    • 
    

    
    
        
  • ERROR Tag PERLLIB Portal/Tools.pl GetUniprotBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBtLmBeB/XFF4834R_chr39340.xml_fasta"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

    • 
    

    
    
        
  • ERROR Tag PERLLIB Portal/Tools.pl GetKeggBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBtLmBeB/XFF4834R_chr39340.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

    • 
    
    

    






pyrF XFF4834R_chr41420




    

         
             
            XFF4834R_chr41410
            
XFF4834R_chr41410
            
        		


       
           
	   Cluster
	   
DrawMap
	   
        		
	
        
            XML file
        	


	    FASTA file
        		
	
	
             
            Extract
Sequence
            
        		
	
	
             
            Codon
Usage
            
        		
    
    
            
            Framed
            
     
  	



	
            OrthoMCL