8 hits
XFF4834R_chr17230 | pyrB | XFF4834R_chr17230 | probable aspartate carbamoyltransferase, catalytic subunit |
XFF4834R_chr19340 | pyrD | XFF4834R_chr19340 | probable dihydro-orotate oxidase, FMN-linked |
XFF4834R_chr23650 | pyrC | XFF4834R_chr23650 | probable Dihydroorotase |
XFF4834R_chr27950 | pyrG | XFF4834R_chr27950 | probable CTP synthetase |
XFF4834R_chr30780 | pyrH | XFF4834R_chr30780 | probable uridylate kinase |
XFF4834R_chr37900 | pyrE | XFF4834R_chr37900 | probable orotate phosphoribosyltransferase |
XFF4834R_chr39340 | XFF4834R_chr42550972_4531916_f3_XFF4834R-XFF4834R_chr39340 | XFF4834R_chr39340 | putative 2-dehydropantoate 2-reductase |
XFF4834R_chr41420 | pyrF | XFF4834R_chr41420 | probable orotidine-5'-phosphate decarboxylase |
![]() XFF4834R_chr17230 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
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![]() 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: cellular amino acid metabolic process (GO:0006520) Biological Process: 'de novo' pyrimidine base biosynthetic process (GO:0006207) Molecular Function: amino acid binding (GO:0016597) Molecular Function: carboxyl- or carbamoyltransferase activity (GO:0016743) Molecular Function: aspartate carbamoyltransferase activity (GO:0004070) 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 |
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YP_364792.1 lcl|pyrB-XCV3061 |
1 |
315 |
S=1497 I=93 E=2.35438e-174 |
aspartate carbamoyltransferase catalytic subunit |
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NP_638094.1 lcl|pyrB-XCC2746 |
1 |
315 |
S=1480 I=92 E=2.70231e-172 |
aspartate carbamoyltransferase catalytic subunit |
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NP_643225.1 lcl|pyrB-XAC2916 |
1 |
315 |
S=1479 I=93 E=3.9659e-172 |
aspartate carbamoyltransferase catalytic subunit |
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1 |
315 |
S=1347 I=84 E=3.87929e-156 |
putative aspartate carbamoyltransferase, catalytic subunit protein |
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4 |
310 |
S=775 I=53 E=3.06731e-85 |
Aspartate carbamoyltransferase EC=2.1.3.2 ; Pyrimidine biosynthesis |
Pubmed 7896697 |
|
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3 |
313 |
S=768 I=54 E=2.1624e-84 |
Aspartate carbamoyltransferase EC=2.1.3.2 ; Pyrimidine biosynthesis |
Pubmed 19077236 |
|
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4 |
310 |
S=756 I=52 E=6.36941e-83 |
Aspartate carbamoyltransferase EC=2.1.3.2 ; Pyrimidine biosynthesis |
Pubmed 8234318 |
|
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5 |
310 |
S=683 I=47 E=4.34526e-74 |
Aspartate carbamoyltransferase EC=2.1.3.2 ; Pyrimidine biosynthesis |
Pubmed 9682487 |
|
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14 |
313 |
S=666 I=50 E=4.08117e-72 |
Aspartate carbamoyltransferase EC=2.1.3.2 ; Pyrimidine biosynthesis |
Pubmed 17965706 |
|
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14 |
314 |
S=642 I=51 E=3.44948e-69 |
Aspartate carbamoyltransferase EC=2.1.3.2 ; Pyrimidine biosynthesis |
Pubmed 9171389 |
|
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12 |
314 |
S=616 I=46 E=5.32096e-66 |
Aspartate carbamoyltransferase EC=2.1.3.2 ; Pyrimidine biosynthesis |
Pubmed 18367281 |
|
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15 |
315 |
S=616 I=46 E=5.65582e-66 |
Aspartate carbamoyltransferase EC=2.1.3.2 ; Pyrimidine biosynthesis |
Pubmed 18441057 |
|
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15 |
310 |
S=612 I=45 E=1.41279e-65 |
Aspartate carbamoyltransferase EC=2.1.3.2 ; Pyrimidine biosynthesis |
Pubmed 18391199 |
|
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15 |
315 |
S=611 I=46 E=2.147e-65 |
Aspartate carbamoyltransferase EC=2.1.3.2 |
Pubmed 12446909 |
|
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1 |
315 |
S=1497 I=93 E=6.14145e-173 |
Aspartate carbamoyltransferase EC=2.1.3.2 ; Pyrimidine biosynthesis |
||
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1 |
315 |
S=1481 I=93 E=5.28658e-171 |
Aspartate carbamoyltransferase EC=2.1.3.2 ; Pyrimidine biosynthesis |
||
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1 |
315 |
S=1481 I=93 E=5.28658e-171 |
Aspartate carbamoyltransferase EC=2.1.3.2 ; Pyrimidine biosynthesis |
||
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1 |
315 |
S=1480 I=92 E=7.04903e-171 |
Aspartate carbamoyltransferase EC=2.1.3.2 ; Pyrimidine biosynthesis |
||
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1 |
315 |
S=1480 I=92 E=7.04903e-171 |
Aspartate carbamoyltransferase EC=2.1.3.2 ; Pyrimidine biosynthesis |
||
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14 |
96 |
S=151 I=43 E=9.35152e-11 |
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255 |
315 |
S=139 I=52 E=2.27375e-09 |
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99 |
213 |
S=138 I=35 E=3.08511e-09 |
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153 |
239 |
S=121 I=37 E=3.16159e-07 |
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168 |
206 |
S=115 I=62 E=1.79234e-06 |
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210 |
252 |
S=111 I=59 E=5.14738e-06 |
Access unfiltered results
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Set of Uniprot with relevant PubMed cross-references ncbi-blastp |
96 hits |
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Swiss-Prot ncbi-blastp |
0 hits |
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Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp |
0 hits |
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HAMAP scan |
0 hits |
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IprScan |
0 hits |
Miscellaneous analyses
![]() XFF4834R_chr19330 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
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![]() 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: metabolic process (GO:0008152) Biological Process: UMP biosynthetic process (GO:0006222) Biological Process: oxidation reduction (GO:0055114) Biological Process: 'de novo' pyrimidine base biosynthetic process (GO:0006207) Cellular Component: membrane (GO:0016020) Molecular Function: dihydroorotate oxidase activity (GO:0004158) Molecular Function: dihydroorotate dehydrogenase activity (GO:0004152) Molecular Function: catalytic activity (GO:0003824) 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 |
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NP_642132.1 lcl|pyrD-XAC1805 |
1 |
351 |
S=1584 I=91 E=0 |
dihydroorotate dehydrogenase 2 |
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YP_363566.1 lcl|pyrD-XCV1835 |
1 |
351 |
S=1574 I=91 E=0 |
dihydroorotate dehydrogenase 2 |
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NP_637154.1 lcl|pyrD-XCC1788 |
1 |
351 |
S=1498 I=85 E=2.0002e-174 |
dihydroorotate dehydrogenase 2 |
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1 |
349 |
S=1246 I=72 E=7.73502e-144 |
putative dihydroorotate dehydrogenase (dihydroorotate oxidase) protein |
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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 |
|
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1 |
338 |
S=851 I=49 E=1.85486e-94 |
Dihydroorotate dehydrogenase ; Cell membrane FMN Flavoprotein Oxidoreductase Pyrimidine biosynthesis |
Pubmed 12517848 |
|
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1 |
338 |
S=851 I=49 E=2.30661e-94 |
Dihydroorotate dehydrogenase ; Cell membrane FMN Flavoprotein Oxidoreductase Pyrimidine biosynthesis |
Pubmed 12517848 |
|
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1 |
338 |
S=850 I=49 E=2.34719e-94 |
Dihydroorotate dehydrogenase ; Cell membrane FMN Flavoprotein Oxidoreductase Pyrimidine biosynthesis |
Pubmed 12517848 |
|
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1 |
338 |
S=847 I=49 E=6.85943e-94 |
Dihydroorotate dehydrogenase ; Cell membrane FMN Flavoprotein Oxidoreductase Pyrimidine biosynthesis |
Pubmed 12517848 |
|
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1 |
338 |
S=846 I=49 E=7.95533e-94 |
Dihydroorotate dehydrogenase ; Cell membrane FMN Flavoprotein Oxidoreductase Pyrimidine biosynthesis |
Pubmed 12517848 |
|
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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 |
|
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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 |
|
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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 |
|
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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 |
|
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1 |
351 |
S=1584 I=91 E=0 |
Dihydroorotate dehydrogenase EC=1.3.3.1 ; Cell membrane Flavoprotein FMN Oxidoreductase Pyrimidine biosynthesis |
||
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1 |
351 |
S=1574 I=91 E=0 |
Dihydroorotate dehydrogenase EC=1.3.3.1 ; Cell membrane Flavoprotein FMN Oxidoreductase Pyrimidine biosynthesis |
||
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1 |
351 |
S=1539 I=88 E=5.43099e-178 |
Dihydroorotate dehydrogenase EC=1.3.3.1 ; Cell membrane Flavoprotein FMN Oxidoreductase Pyrimidine biosynthesis |
||
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1 |
351 |
S=1539 I=88 E=5.43099e-178 |
Dihydroorotate dehydrogenase EC=1.3.3.1 ; Cell membrane Flavoprotein FMN Oxidoreductase Pyrimidine biosynthesis |
||
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1 |
351 |
S=1534 I=88 E=2.13482e-177 |
Dihydroorotate dehydrogenase EC=1.3.3.1 ; Cell membrane Flavoprotein FMN Oxidoreductase Pyrimidine biosynthesis |
||
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50 |
171 |
S=358 I=55 E=6.85062e-36 |
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133 |
193 |
S=246 I=70 E=2.25711e-22 |
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325 |
351 |
S=120 I=85 E=4.67698e-07 |
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1 |
45 |
S=115 I=56 E=1.95413e-06 |
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210 |
275 |
S=111 I=41 E=6.45214e-06 |
Access unfiltered results
Miscellaneous analyses
![]() XFF4834R_chr23640 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
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![]() 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 |
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NP_642676.1 pyrC-XAC2360 |
1 |
449 |
S=2386 I=100 E=0 |
dihydroorotase |
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YP_364290.1 pyrC-XCV2559 |
1 |
449 |
S=2361 I=98 E=0 |
dihydroorotase |
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NP_637612.1 pyrC-XCC2257 |
1 |
449 |
S=2300 I=96 E=0 |
dihydroorotase |
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XALc_1913 pyrC-XALc_1913 |
4 |
449 |
S=1866 I=79 E=0 |
putative dihydroorotase domain protein |
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5 |
442 |
S=526 I=35 E=7.31824e-55 |
Putative allantoinase |
Pubmed 20081001 |
|
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16 |
440 |
S=468 I=31 E=7.5338e-48 |
Dihydroorotase EC=3.5.2.3 ; Hydrolase Metal-binding Pyrimidine biosynthesis Zinc |
Pubmed 7929010 |
|
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5 |
436 |
S=445 I=29 E=4.98839e-45 |
Allantoinase EC=3.5.2.5 ; Hydrolase Metal-binding Purine metabolism Zinc |
Pubmed 11344136 |
|
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3 |
431 |
S=425 I=30 E=1.22249e-42 |
Dihydroorotase EC=3.5.2.3 ; Hydrolase Metal-binding Pyrimidine biosynthesis Zinc |
Pubmed 15780005 |
|
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14 |
431 |
S=418 I=29 E=9.40345e-42 |
Dihydroorotase EC=3.5.2.3 ; Hydrolase Metal-binding Pyrimidine biosynthesis Zinc |
Pubmed 18391199 |
|
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1 |
416 |
S=479 I=30 E=2.2204e-49 |
Dihydroorotase EC=3.5.2.3 ; Hydrolase Metal-binding Pyrimidine biosynthesis Zinc |
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6 |
413 |
S=471 I=32 E=2.50656e-48 |
Dihydroorotase EC=3.5.2.3 ; Hydrolase Metal-binding Pyrimidine biosynthesis Zinc |
||
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1 |
445 |
S=470 I=32 E=2.80739e-48 |
Allantoinase EC=3.5.2.5 ; Hydrolase Metal-binding Purine metabolism Zinc |
||
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16 |
440 |
S=468 I=31 E=5.12356e-48 |
Dihydroorotase EC=3.5.2.3 ; Hydrolase Metal-binding Pyrimidine biosynthesis Zinc |
||
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6 |
413 |
S=465 I=32 E=1.23597e-47 |
Dihydroorotase EC=3.5.2.3 ; Hydrolase Metal-binding Pyrimidine biosynthesis Zinc |
||
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[G3DSA:3.20.20.140] | 55 |
417 |
- |
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[PTHR11647:SF5] | 44 |
449 |
- |
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[PTHR11647] | 44 |
449 |
- |
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IPR006680 [PF01979] | 51 |
391 |
Amidohydrolase 1 |
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IPR002195 [PS00483] | 313 |
324 |
Dihydroorotase, conserved site |
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60 |
383 |
S=341 I=34 E=8.94818e-34 |
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384 |
449 |
S=143 I=40 E=8.61901e-10 |
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417 |
449 |
S=137 I=73 E=4.36262e-09 |
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426 |
449 |
S=131 I=100 E=2.15118e-08 |
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4 |
167 |
S=130 I=26 E=3.15707e-08 |
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6 |
66 |
S=113 I=41 E=4.16607e-06 |
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1 |
71 |
S=103 I=33 E=6.38121e-05 |
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1 |
99 |
S=102 I=28 E=7.73047e-05 |
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[SSF51556] | 55 |
379 |
- |
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IPR011059 [SSF51338] | 1 |
429 |
Metal-dependent hydrolase, composite domain |
Access unfiltered results
Miscellaneous analyses
![]() XFF4834R_chr27940 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
![]() |
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![]() 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: catalytic activity (GO:0003824) Molecular Function: CTP synthase activity (GO:0003883) 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 |
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NP_642047.1 pyrG-XAC1716 |
1 |
554 |
S=2839 I=97 E=0 |
CTP synthetase |
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YP_363480.1 pyrG-XCV1749 |
1 |
554 |
S=2836 I=97 E=0 |
CTP synthetase |
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NP_637067.2 pyrG-XCC1697 |
1 |
554 |
S=2796 I=95 E=0 |
CTP synthetase |
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XALc_1149 pyrG-XALc_1149 |
1 |
554 |
S=2672 I=90 E=0 |
probable ctp synthase (utp--ammonia ligase) protein |
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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 |
|
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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 |
|
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45 |
545 |
S=1684 I=61 E=0 |
Putative uncharacterized protein |
Pubmed 8790892 |
|
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47 |
541 |
S=1600 I=60 E=0 |
CTP synthetase |
Pubmed 12668143 |
|
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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 |
|
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1 |
554 |
S=2839 I=97 E=0 |
CTP synthase EC=6.3.4.2 ; ATP-binding Glutamine amidotransferase Ligase Nucleotide-binding Pyrimidine biosynthesis |
||
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1 |
554 |
S=2836 I=97 E=0 |
CTP synthase EC=6.3.4.2 ; ATP-binding Glutamine amidotransferase Ligase Nucleotide-binding Pyrimidine biosynthesis |
||
![]() |
1 |
554 |
S=2818 I=96 E=0 |
CTP synthase EC=6.3.4.2 ; ATP-binding Glutamine amidotransferase Ligase Nucleotide-binding Pyrimidine biosynthesis |
||
![]() |
1 |
554 |
S=2818 I=96 E=0 |
CTP synthase EC=6.3.4.2 ; ATP-binding Glutamine amidotransferase Ligase Nucleotide-binding Pyrimidine biosynthesis |
||
![]() |
1 |
554 |
S=2818 I=96 E=0 |
CTP synthase EC=6.3.4.2 ; ATP-binding Glutamine amidotransferase Ligase Nucleotide-binding Pyrimidine biosynthesis |
||
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[G3DSA:3.40.50.300] | 2 |
286 |
- |
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[G3DSA:3.40.50.880] | 287 |
548 |
- |
![]() |
IPR004468 [MF_01227] | 2 |
543 |
CTP synthase |
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[PTHR11550] | 117 |
542 |
- |
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IPR017456 [PF06418] | 4 |
269 |
CTP synthase, N-terminal |
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IPR000991 [PF00117] | 303 |
537 |
Glutamine amidotransferase class-I, C-terminal |
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IPR004468 [TIGR00337] | 1 |
538 |
CTP synthase |
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IPR017926 [PS51273] | 292 |
545 |
Glutamine amidotransferase type 1 |
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[seg] | 13 |
28 |
- |
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[SignalP-NN(euk)] | 1 |
30 |
- |
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114 |
229 |
S=426 I=70 E=4.78809e-44 |
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319 |
421 |
S=311 I=52 E=3.48784e-30 |
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51 |
111 |
S=254 I=72 E=3.01602e-23 |
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428 |
495 |
S=219 I=64 E=5.63134e-19 |
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499 |
543 |
S=162 I=60 E=4.54147e-12 |
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1 |
49 |
S=142 I=59 E=1.16256e-09 |
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234 |
295 |
S=124 I=47 E=1.52079e-07 |
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295 |
331 |
S=123 I=57 E=2.27117e-07 |
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441 |
543 |
S=121 I=29 E=3.83213e-07 |
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33 |
111 |
S=103 I=28 E=5.91616e-05 |
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[SSF52540] | 1 |
270 |
- |
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[SSF52317] | 288 |
547 |
- |
Access unfiltered results
Miscellaneous analyses
![]() XFF4834R_chr30770 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
![]() |
![]() |
![]() 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: cellular amino acid biosynthetic process (GO:0008652) Biological Process: pyrimidine nucleotide biosynthetic process (GO:0006221) Biological Process: 'de novo' pyrimidine base biosynthetic process (GO:0006207) Cellular Component: cytoplasm (GO:0005737) Molecular Function: uridylate kinase activity (GO:0009041) Molecular Function: UMP kinase activity (GO:0033862) 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 |
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YP_363207.1 lcl|pyrH-XCV1476 |
1 |
240 |
S=1222 I=99 E=4.10237e-141 |
uridylate kinase |
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NP_641754.1 lcl|pyrH-XAC1419 |
1 |
240 |
S=1216 I=99 E=1.69916e-140 |
uridylate kinase |
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NP_636745.1 lcl|pyrH-XCC1371 |
1 |
240 |
S=1206 I=98 E=2.94051e-139 |
uridylate kinase |
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1 |
239 |
S=1118 I=90 E=1.31784e-128 |
probable uridylate kinase protein |
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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 |
|
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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 |
|
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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 |
|
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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 |
|
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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 |
||
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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 |
|
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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 |
|
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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 |
|
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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 |
|
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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 |
|
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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 |
||
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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 |
||
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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 |
||
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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 |
||
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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 |
||
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19 |
75 |
S=175 I=60 E=1.03676e-13 |
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4 |
75 |
S=145 I=51 E=4.1007e-10 |
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102 |
133 |
S=129 I=75 E=3.37932e-08 |
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197 |
240 |
S=124 I=50 E=1.55406e-07 |
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76 |
131 |
S=119 I=45 E=6.1622e-07 |
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76 |
124 |
S=111 I=42 E=6.26536e-06 |
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133 |
190 |
S=103 I=53 E=5.21275e-05 |
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76 |
132 |
S=102 I=42 E=7.78478e-05 |
Access unfiltered results
Miscellaneous analyses
![]() XFF4834R_chr37890 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
![]() |
![]() |
![]() 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 |
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YP_365747.1 lcl|pyrE-XCV4016 |
1 |
219 |
S=1033 I=94 E=2.27559e-118 |
orotate phosphoribosyltransferase |
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NP_644204.1 lcl|pyrE-XAC3903 |
1 |
219 |
S=1026 I=93 E=1.7352e-117 |
orotate phosphoribosyltransferase |
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NP_639187.1 lcl|pyrE-XCC3847 |
1 |
219 |
S=1010 I=91 E=1.41754e-115 |
orotate phosphoribosyltransferase |
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1 |
216 |
S=842 I=80 E=3.57458e-95 |
probable orotate phosphoribosyltransferase protein |
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1 |
214 |
S=523 I=53 E=5.14762e-55 |
Orotate phosphoribosyltransferase EC=2.4.2.10 ; Glycosyltransferase Magnesium Pyrimidine biosynthesis |
Pubmed 8824606 |
|
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1 |
214 |
S=519 I=48 E=1.75996e-54 |
Orotate phosphoribosyltransferase EC=2.4.2.10 ; Glycosyltransferase Pyrimidine biosynthesis |
Pubmed 10509020 |
|
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1 |
215 |
S=515 I=50 E=5.96506e-54 |
Orotate phosphoribosyltransferase EC=2.4.2.10 ; Glycosyltransferase Magnesium Pyrimidine biosynthesis |
Pubmed 11889481 |
|
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1 |
215 |
S=512 I=49 E=1.07919e-53 |
Orotate phosphoribosyltransferase EC=2.4.2.10 ; Glycosyltransferase Magnesium Pyrimidine biosynthesis |
Pubmed 8487307 |
|
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1 |
215 |
S=496 I=48 E=1.07739e-51 |
Orotate phosphoribosyltransferase EC=2.4.2.10 ; Glycosyltransferase Magnesium Pyrimidine biosynthesis |
||
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1 |
195 |
S=489 I=50 E=6.96119e-51 |
Orotate phosphoribosyltransferase EC=2.4.2.10 ; Glycosyltransferase Pyrimidine biosynthesis |
Pubmed 7597846 |
|
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1 |
215 |
S=486 I=43 E=1.59368e-50 |
Orotate phosphoribosyl transferase |
Pubmed 14981288 |
|
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1 |
195 |
S=485 I=48 E=2.46449e-50 |
Orotate phosphoribosyltransferase 1 EC=2.4.2.10 ; Glycosyltransferase Pyrimidine biosynthesis |
Pubmed 2651891 |
|
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1 |
215 |
S=478 I=45 E=1.44673e-49 |
Orotate phosphoribosyltransferase EC=2.4.2.10 ; Glycosyltransferase Magnesium Pyrimidine biosynthesis |
Pubmed 10675023 |
|
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1 |
214 |
S=474 I=43 E=4.6131e-49 |
Orotate phosphoribosyltransferase EC=2.4.2.10 ; Glycosyltransferase |
Pubmed 9862479 |
|
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1 |
219 |
S=1033 I=94 E=5.64396e-117 |
Orotate phosphoribosyltransferase EC=2.4.2.10 ; Glycosyltransferase Magnesium Pyrimidine biosynthesis |
||
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1 |
219 |
S=1026 I=93 E=4.30367e-116 |
Orotate phosphoribosyltransferase EC=2.4.2.10 ; Glycosyltransferase Magnesium Pyrimidine biosynthesis |
||
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1 |
219 |
S=1010 I=91 E=3.5158e-114 |
Orotate phosphoribosyltransferase EC=2.4.2.10 ; Glycosyltransferase Magnesium Pyrimidine biosynthesis |
||
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1 |
219 |
S=1010 I=91 E=3.5158e-114 |
Orotate phosphoribosyltransferase EC=2.4.2.10 ; Glycosyltransferase Magnesium Pyrimidine biosynthesis |
||
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1 |
219 |
S=1010 I=91 E=3.5158e-114 |
Orotate phosphoribosyltransferase EC=2.4.2.10 ; Glycosyltransferase Magnesium Pyrimidine biosynthesis |
||
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[G3DSA:3.40.50.2020] | 1 |
215 |
- |
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IPR000836 [PF00156] | 45 |
153 |
Phosphoribosyltransferase |
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IPR004467 [TIGR00336] | 10 |
189 |
Orotate phosphoribosyl transferase |
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[seg] | 168 |
176 |
- |
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42 |
117 |
S=222 I=60 E=2.22558e-19 |
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190 |
219 |
S=145 I=97 E=3.75972e-10 |
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8 |
41 |
S=131 I=65 E=1.93489e-08 |
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[SSF53271] | 1 |
215 |
- |
Access unfiltered results
Miscellaneous analyses
![]() XFF4834R_chr39330 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
![]() |
![]() |
![]() 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: metabolic process (GO:0008152) Biological Process: oxidation reduction (GO:0055114) Biological Process: pantothenate biosynthetic process (GO:0015940) Cellular Component: cytoplasm (GO:0005737) Molecular Function: binding (GO:0005488) Molecular Function: coenzyme binding (GO:0050662) Molecular Function: oxidoreductase activity (GO:0016491) Molecular Function: NADP or NADPH binding (GO:0050661) Molecular Function: catalytic activity (GO:0003824) 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 |
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NP_644367.1 lcl|apbA-XAC4068 |
3 |
314 |
S=1439 I=90 E=2.63342e-167 |
2-dehydropantoate 2-reductase |
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YP_365885.1 lcl|XCV4154 |
1 |
313 |
S=1397 I=88 E=3.14937e-162 |
2-dehydropantoate 2-reductase |
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NP_639319.1 lcl|apbA-XCC3980 |
3 |
313 |
S=1341 I=86 E=2.17096e-155 |
2-dehydropantoate 2-reductase |
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3 |
309 |
S=925 I=60 E=5.15602e-105 |
probable 2-dehydropantoate 2-reductase (ketopantoate reductase) protein |
![]() |
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 |
|
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20 |
309 |
S=410 I=34 E=3.02653e-41 |
Uncharacterized oxidoreductase ykpB EC=1.1.1.- ; NADP |
||
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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 |
||
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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 |
||
![]() |
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 |
||
![]() |
IPR016040 [G3DSA:3.40.50.720] | 3 |
147 |
NAD(P)-binding domain |
![]() |
IPR013328 [G3DSA:1.10.1040.10] | 185 |
309 |
Dehydrogenase, multihelical |
![]() |
IPR013332 [PF02558] | 5 |
159 |
Ketopantoate reductase ApbA/PanE, N-terminal |
![]() |
IPR013752 [PF08546] | 185 |
309 |
Ketopantoate reductase ApbA/PanE, C-terminal |
![]() |
IPR003710 [TIGR00745] | 4 |
312 |
Ketopantoate reductase ApbA/PanE |
![]() |
[seg] | 9 |
19 |
- |
![]() |
[seg] | 164 |
176 |
- |
![]() |
194 |
268 |
S=195 I=56 E=4.15622e-16 |
![]() |
41 |
73 |
S=149 I=94 E=1.46531e-10 |
![]() |
194 |
313 |
S=133 I=28 E=1.30611e-08 |
![]() |
44 |
113 |
S=106 I=40 E=2.63996e-05 |
![]() |
116 |
193 |
S=104 I=35 E=4.15428e-05 |
Access unfiltered results
![]() |
Set of Uniprot with relevant PubMed cross-references ncbi-blastp |
1 hits |
![]() |
Swiss-Prot ncbi-blastp |
4 hits |
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Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp |
0 hits |
![]() |
HAMAP scan |
0 hits |
![]() |
IprScan |
7 hits |
Miscellaneous analyses
![]() XFF4834R_chr41410 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
![]() |
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