Xanthomonas fuscans subsp. fuscans

9 hits

  1. XFF4834R_chr19710hisSXFF4834R_chr19710histidyl tRNA synthetase
  2. XFF4834R_chr19730hisGXFF4834R_chr19730ATP phosphoribosyltransferase
  3. XFF4834R_chr19740hisDXFF4834R_chr19740histidinol dehydrogenase
  4. XFF4834R_chr19750hisCXFF4834R_chr19750histidinol-phosphate aminotransferase
  5. XFF4834R_chr19760hisBXFF4834R_chr19760bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase protein
  6. XFF4834R_chr19770hisHXFF4834R_chr19770imidazole glycerol phosphate synthase, glutamine amidotransferase subunit with HisF
  7. XFF4834R_chr19780hisAXFF4834R_chr19780N-(5'-phospho-L-ribosyl-formimino)-5-amino-1-(5'-phosphoribosyl)-4-imidazolecarboxamide isomerase
  8. XFF4834R_chr19790hisFXFF4834R_chr19790imidazole glycerol phosphate synthase, catalytic subunit with HisH
  9. XFF4834R_chr19800hisIEXFF4834R_chr19800bifunctional phosphoribosyl-AMP cyclohydrolase-phosphoribosyl-ATP pyrophosphatase

hisS XFF4834R_chr19710
XFF4834R_chr19700
XFF4834R_chr19700
Cluster
DrawMap
XML file

FASTA file
Extract
Sequence
Codon
Usage
Framed OrthoMCL XFF4834R_chr_2102
XFF4834R_chr_2102
ID hisS
AC XFF4834R_chr19710
LT XFF4834R_chr19710
OR XFF4834R_chr from 2263682 to 2265094 on strand +
DE histidyl tRNA synthetase
IP Histidyl-tRNA synthetase, class IIa
CL 1.5.1.16 Histidine GO:0000105
EC
GO InterPro
Biological Process: histidyl-tRNA aminoacylation (GO:0006427)
Biological Process: translation (GO:0006412)
Biological Process: tRNA aminoacylation for protein translation (GO:0006418)
Cellular Component: cytoplasm (GO:0005737)
Molecular Function: nucleotide binding (GO:0000166)
Molecular Function: histidine-tRNA ligase activity (GO:0004821)
Molecular Function: ATP binding (GO:0005524)
Molecular Function: aminoacyl-tRNA ligase activity (GO:0004812)

Curated
PM
AN
CC COG: [J] Translation, ribosomal structure and biogenesis;
CC MODEL: XFF4834R
CC STATUS: curated by jacques (20110309)
MW 51882.8 Da
SQ 470 aa
 
........10........20........30........40........50
| | | | |
MIKPRTPPGIMELLPREQIAFQRMLDVIRRNYERFGFLPVETPVFELSDV
LLTKSGGETERQVYFVQSTGALANAAAAADEGAENGGLPELALRFDLTVP
LARYVAEHEHDLSFPFRRYQMQRVYRGERAQRGRFREFYQCDIDVIGKDA
LSIRYDAEVLAVIHAVFAELGIGDFKVQLNNRKLLRGFFESLGVAEGELQ
LAVLREVDKIDKRGADYVHDTLVGEGFGIPAEQVARILAFVAVRSEGHAD
ALAQLQALEGSVGTSATLGEGIAELREVLELVKALGVPESAYCLNFSIAR
GLDYYTGTVYETTLTDHPQIGSICSGGRYESLASHYTKSKLPGVGISIGL
TRLFWQLREAGLIQGIAESSVQAMVALMDETRLDDALDIARRLRIGGINT
EVQMEPKKVGKQFQYAARAGIRFVVLAGDDELARGVVAVKDLVREQQFDV
ARDELASTLLVELEQAKAMP
XFF4834R

NP_642152.1 lcl|hisS-XAC1826

1

469

S=2281 I=94 E=0

histidyl-tRNA synthetase

XFF4834R

NP_637171.1 lcl|hisS-XCC1806

1

469

S=2224 I=92 E=0

histidyl-tRNA synthetase

XFF4834R

lcl|hisS-XALc_1250

1

469

S=2100 I=87 E=0

probable histidyl-trna synthetase (histidine--trna ligase)(hisrs) protein

XFF4834R

YP_363603.1 lcl|hisS-XCV1872

1

469

S=2025 I=84 E=0

histidyl-tRNA synthetase

pubmed

1

447

S=850 I=39 E=3.75738e-94

Histidyl-tRNA synthetase EC=6.1.1.21 ; Aminoacyl-tRNA ATP-binding Cytoplasm Ligase Nucleotide-binding Protein biosynthesis

Pubmed 18263572

 

prodomImg

pubmed

1

424

S=651 I=39 E=4.91061e-70

Histidyl-tRNA synthetase EC=6.1.1.21 ; Aminoacyl-tRNA ATP-binding Cytoplasm Ligase Nucleotide-binding Protein biosynthesis

Pubmed 19033196

 

prodomImg

pubmed

1

447

S=648 I=38 E=1.27018e-69

Histidyl-tRNA synthetase EC=6.1.1.21 ; Aminoacyl-tRNA ATP-binding Cytoplasm Ligase Nucleotide-binding Protein biosynthesis

Pubmed 19011029

 

prodomImg

pubmed

1

457

S=598 I=32 E=1.55799e-63

Histidyl-tRNA synthetase EC=6.1.1.21 ; Aminoacyl-tRNA ATP-binding Cytoplasm Ligase Nucleotide-binding Protein biosynthesis

Pubmed 19008447

 

prodomImg

pubmed

2

423

S=586 I=35 E=3.95693e-62

Histidyl-tRNA synthetase EC=6.1.1.21 ; Aminoacyl-tRNA ATP-binding Cytoplasm Ligase Nucleotide-binding Protein biosynthesis

Pubmed 18482458

 

prodomImg

sp_Pdown

sp|Q8PLH2|SYH_XANAC

1

469

S=2281 I=94 E=0

Histidyl-tRNA synthetase EC=6.1.1.21 ; Aminoacyl-tRNA ATP-binding Cytoplasm Ligase Nucleotide-binding Protein biosynthesis

sp_Pdown

sp|Q5H0L6|SYH_XANOR

1

470

S=2274 I=94 E=0

Histidyl-tRNA synthetase EC=6.1.1.21 ; Aminoacyl-tRNA ATP-binding Cytoplasm Ligase Nucleotide-binding Protein biosynthesis

sp_Pdown

sp|B2SKP3|SYH_XANOP

1

470

S=2274 I=94 E=0

Histidyl-tRNA synthetase EC=6.1.1.21 ; Aminoacyl-tRNA ATP-binding Cytoplasm Ligase Nucleotide-binding Protein biosynthesis

sp_Pdown

sp|Q2P3K8|SYH_XANOM

1

467

S=2254 I=94 E=0

Histidyl-tRNA synthetase EC=6.1.1.21 ; Aminoacyl-tRNA ATP-binding Cytoplasm Ligase Nucleotide-binding Protein biosynthesis

sp_Pdown

sp|Q4UU37|SYH_XANC8

1

469

S=2227 I=92 E=0

Histidyl-tRNA synthetase EC=6.1.1.21 ; Aminoacyl-tRNA ATP-binding Cytoplasm Ligase Nucleotide-binding Protein biosynthesis

Iprscan [G3DSA:3.30.930.10]

2

364

-

Iprscan IPR004154 [G3DSA:3.40.50.800]

368

459

Anticodon-binding

Iprscan IPR015807 [MF_00127]

2

465

Histidyl-tRNA synthetase, class IIa, subgroup

Iprscan IPR004516 [PIRSF001549]

1

463

Histidyl-tRNA synthetase, class IIa

Iprscan IPR004516 [PTHR11476]

1

464

Histidyl-tRNA synthetase, class IIa

Iprscan IPR002314 [PF00587]

22

184

Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved domain

Iprscan IPR004154 [PF03129]

372

459

Anticodon-binding

Iprscan IPR015807 [TIGR00442]

5

452

Histidyl-tRNA synthetase, class IIa, subgroup

Iprscan IPR006195 [PS50862]

22

470

Aminoacyl-tRNA synthetase, class II, conserved domain

Iprscan [seg]

70

88

-

Iprscan [SignalP-NN(euk)]

1

3

-

PD001912

91

181

S=184 I=46 E=8.45976e-15

PD155307

93

292

S=171 I=26 E=3.35168e-13

PD537931

321

412

S=125 I=38 E=1.5216e-07

PD481466

182

244

S=115 I=42 E=2.49902e-06

PDA1O3Y0

1

67

S=112 I=40 E=4.93307e-06

PDA4V4X2

245

269

S=107 I=92 E=1.79275e-05

Iprscan [SSF55681]

3

366

-

Iprscan IPR004154 [SSF52954]

368

464

Anticodon-binding

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 ka1mQ09R)
   

Show or not Access unfiltered results

pubmed

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

78 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

13 hits

Show or not Miscellaneous analyses

  • ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBSb00uX/XFF4834R_chr19710.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBSb00uX/XFF4834R_chr19710.xml_fasta", "blastp"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBSb00uX/XFF4834R_chr19710.xml_fasta"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBSb00uX/XFF4834R_chr19710.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.
hisG XFF4834R_chr19730
XFF4834R_chr19720
XFF4834R_chr19720
Cluster
DrawMap
XML file

FASTA file
Extract
Sequence
Codon
Usage
Framed OrthoMCL XFF4834R_chr19740
XFF4834R_chr19740
ID hisG
AC XFF4834R_chr19730
LT XFF4834R_chr19730
OR XFF4834R_chr from 2266046 to 2266960 on strand +
DE ATP phosphoribosyltransferase
IP Histidine biosynthesis HisG, C-terminal; ATP phosphoribosyltransferase, catalytic region; ATP phosphoribosyltransferase, conserved site;
CL 1.5.1.16 Histidine GO:0000105
EC
GO InterPro
Biological Process: histidine biosynthetic process (GO:0000105)
Cellular Component: cytoplasm (GO:0005737)
Molecular Function: magnesium ion binding (GO:0000287)
Molecular Function: ATP phosphoribosyltransferase activity (GO:0003879)

Curated
PM
AN
CC COG: [E] Amino acid transport and metabolism;
CC MODEL: XFF4834R
CC STATUS: curated by jacques (20110309)
MW 32743.4 Da
SQ 304 aa
 
........10........20........30........40........50
| | | | |
MSASTAAPARDRLRIAIQKSGRLAEPARSLLAACGLSWRQSRDKLFCYGE
SLPVDLLLVRDDDIPGLIADGVCDLGIVGQNELEEQAAERRRNGLPAAYH
AVRGVGFGQCRLMLAVPEEWDWHGVAQLAGKRIATSYPAILAHWLGRQGI
DAAVVELSGSVEIAPRLGTADLICDLVSSGATLAANQLKPVELVMESEAV
LAGAVREPADARAGLLAMLLRRMDGVLKLRDSKLLMFRAEHGNVDALRRL
LPDADPLVQLPDDGNGALRLQTMCHGAVTWQRLEELERAGAQGLMVLTVE
RSLA
Hamap HIS1_MF_00079 raw_score=4976 norm_score=31.245

ATP phosphoribosyltransferase [hisG].

XFF4834R

YP_363605.1 lcl|hisG-XCV1874

1

304

S=1342 I=88 E=1.40455e-155

ATP phosphoribosyltransferase

XFF4834R

NP_642154.1 lcl|hisG-XAC1828

1

304

S=1330 I=88 E=4.55357e-154

ATP phosphoribosyltransferase

XFF4834R

NP_637173.1 lcl|hisG-XCC1808

1

304

S=1314 I=87 E=3.09757e-152

ATP phosphoribosyltransferase

XFF4834R

lcl|hisG-XALc_1253

1

304

S=1133 I=75 E=3.20451e-130

probable atp phosphoribosyltransferase (atp-prt) protein

pubmed

12

303

S=501 I=40 E=4.74038e-52

ATP phosphoribosyltransferase EC=2.4.2.17 ; Amino-acid biosynthesis ATP-binding Cytoplasm Glycosyltransferase Histidine Magnesium Metal-binding Nu

Pubmed 3062174,8201624

 

prodomImg

pubmed

12

303

S=496 I=40 E=1.84717e-51

ATP phosphoribosyltransferase EC=2.4.2.17 ; Amino-acid biosynthesis ATP-binding Cytoplasm Glycosyltransferase Histidine Magnesium Metal-binding Nuc

Pubmed 377278,3062174

 

prodomImg

pubmed

11

303

S=461 I=36 E=3.419e-47

ATP phosphoribosyltransferase EC=2.4.2.17 ; Amino-acid biosynthesis ATP-binding Cytoplasm Glycosyltransferase Histidine Magnesium Metal-binding Nucleotid

Pubmed 10555290

 

prodomImg

pubmed

11

303

S=456 I=36 E=1.06205e-46

ATP phosphoribosyltransferase EC=2.4.2.17 ; Amino-acid biosynthesis ATP-binding Cytoplasm Glycosyltransferase Histidine Magnesium Metal-binding N

Pubmed 9767718

 

prodomImg

pubmed

11

303

S=452 I=34 E=3.72736e-46

ATP phosphoribosyltransferase EC=2.4.2.17 ; Amino-acid biosynthesis ATP-binding Cytoplasm Glycosyltransferase Histidine Magnesium Metal-binding Nucleotid

Pubmed 10555290

 

prodomImg

pubmed

11

303

S=436 I=33 E=3.68884e-44

ATP phosphoribosyltransferase EC=2.4.2.17 ; Amino-acid biosynthesis ATP-binding Cytoplasm Glycosyltransferase Histidine Magnesium Metal-binding Nucleotid

Pubmed 10555290

 

prodomImg

pubmed

13

303

S=396 I=31 E=2.2544e-39

ATP phosphoribosyltransferase EC=2.4.2.17 ; Amino-acid biosynthesis ATP-binding Cytoplasm Glycosyltransferase Histidine Magnesium Metal-binding Nucleotid

Pubmed 19008447

 

prodomImg

pubmed

13

301

S=298 I=28 E=1.63067e-27

ATP phosphoribosyltransferase EC=2.4.2.17 ; Amino-acid biosynthesis ATP-binding Cytoplasm Glycosyltransferase Histidine Magnesium Metal-binding Nucleotid

Pubmed 16857943

 

prodomImg

pubmed

13

301

S=262 I=26 E=4.46837e-23

ATP phosphoribosyltransferase EC=2.4.2.17 ; Amino-acid biosynthesis ATP-binding Cytoplasm Glycosyltransferase Histidine Magnesium Metal-binding Nucleotid

Pubmed 16820047

 

prodomImg

pubmed

12

203

S=255 I=32 E=2.91238e-22

ATP phosphoribosyltransferase EC=2.4.2.17 ; Amino-acid biosynthesis ATP-binding Cytoplasm Glycosyltransferase Histidine Magnesium Metal-binding N

Pubmed 9209067,10701121

 

prodomImg

sp_Pdown

sp|Q3BUF8|HIS1_XANC5

1

304

S=1342 I=88 E=3.65013e-154

ATP phosphoribosyltransferase EC=2.4.2.17 ; Amino-acid biosynthesis ATP-binding Cytoplasm Glycosyltransferase Histidine Magnesium Metal-binding Nucleotid

sp_Pdown

sp|Q8PLH0|HIS1_XANAC

1

304

S=1330 I=88 E=1.18338e-152

ATP phosphoribosyltransferase EC=2.4.2.17 ; Amino-acid biosynthesis ATP-binding Cytoplasm Glycosyltransferase Histidine Magnesium Metal-binding Nucleotid

sp_Pdown

sp|Q4UU39|HIS1_XANC8

1

304

S=1323 I=87 E=7.84866e-152

ATP phosphoribosyltransferase EC=2.4.2.17 ; Amino-acid biosynthesis ATP-binding Cytoplasm Glycosyltransferase Histidine Magnesium Metal-binding Nucleotid

sp_Pdown

sp|Q5H0L2|HIS1_XANOR

1

304

S=1320 I=87 E=1.92666e-151

ATP phosphoribosyltransferase EC=2.4.2.17 ; Amino-acid biosynthesis ATP-binding Cytoplasm Glycosyltransferase Histidine Magnesium Metal-binding Nucleotid

sp_Pdown

sp|B2SKN9|HIS1_XANOP

1

304

S=1320 I=87 E=1.92666e-151

ATP phosphoribosyltransferase EC=2.4.2.17 ; Amino-acid biosynthesis ATP-binding Cytoplasm Glycosyltransferase Histidine Magnesium Metal-binding Nucleotid

Iprscan [G3DSA:3.40.190.10]

7

141

-

Iprscan IPR015867 [G3DSA:3.30.70.120]

232

304

Nitrogen regulatory protein PII/ATP phosphoribosyltransferase, C-terminal

Iprscan IPR020621 [MF_00079]

12

304

Histidine biosynthesis HisG, ATP phosphoribosyltransferase, subgroup

Iprscan IPR013820 [PF01634]

59

227

ATP phosphoribosyltransferase, catalytic region

Iprscan IPR013115 [PF08029]

228

302

Histidine biosynthesis HisG, C-terminal

Iprscan IPR013820 [TIGR00070]

13

203

ATP phosphoribosyltransferase, catalytic region

Iprscan IPR013115 [TIGR03455]

204

303

Histidine biosynthesis HisG, C-terminal

Iprscan IPR018198 [PS01316]

162

183

ATP phosphoribosyltransferase, conserved site

Iprscan [seg]

52

63

-

Iprscan [seg]

209

225

-

PD874462

202

304

S=379 I=77 E=2.01739e-38

PD003516

96

201

S=279 I=50 E=2.29626e-26

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Suggest an annotation

Move your mouse over each field to get more informations

ID
DE
EC
GO
PM
CC
CL
  Your email
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Show or not Access unfiltered results

pubmed

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

31 hits
swiss-prot

Swiss-Prot ncbi-blastp

458 hits
XFF4834R

Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp

0 hits
hamap

HAMAP scan

1 hits
Interpro Scan

IprScan

10 hits

Show or not Miscellaneous analyses

  • ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBSb00uX/XFF4834R_chr19730.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBSb00uX/XFF4834R_chr19730.xml_fasta", "blastp"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBSb00uX/XFF4834R_chr19730.xml_fasta"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBSb00uX/XFF4834R_chr19730.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.
hisD XFF4834R_chr19740
XFF4834R_chr19730
XFF4834R_chr19730
Cluster
DrawMap
XML file

FASTA file
Extract
Sequence
Codon
Usage
Framed OrthoMCL XFF4834R_chr19750
XFF4834R_chr19750
ID hisD
AC XFF4834R_chr19740
LT XFF4834R_chr19740
OR XFF4834R_chr from 2266957 to 2268252 on strand +
DE histidinol dehydrogenase
IP Histidinol dehydrogenase, conserved site
CL 1.5.1.16 Histidine GO:0000105
EC
GO InterPro
Biological Process: histidine biosynthetic process (GO:0000105)
Molecular Function: NAD or NADH binding (GO:0051287)
Molecular Function: histidinol dehydrogenase activity (GO:0004399)
Molecular Function: zinc ion binding (GO:0008270)

Curated
PM
AN
CC COG: [E] Amino acid transport and metabolism;
CC MODEL: XFF4834R
CC STATUS: curated by jacques (20110309)
MW 44741.4 Da
SQ 431 aa
 
........10........20........30........40........50
| | | | |
MKILDWSQLDGAARTDALTRPVQTVAARTRDAVAALIADVRTRGDAALRE
ITARFDGVSLDSFAVSEAEFVTAEAAVPPELRQAMQDAVARIDTFHRAGM
SQGYAVETAPGVVCEKIVRPIGRVGLYVPAGSAPLPSTALMLGVPARLAG
CREVVLCTPPRKDGSVDPAVLVAAQLTGVRRVFKLGGAQAIAAMAYGTES
LPSCDKLFGPGNSYVTEAKQQVAQSGAAAIDMPAGPSEVLVIADAGAQPA
FVAADLLSQAEHGPDSQVLLLSDSDALIDAVQAQLEVQLAQLSRADIARQ
ALAQSRLIKVQTLDEAFAISNRYAPEHLILALREPRAWLEHVEAAGSVFL
GDYTPEALGDYCSGTNHVLPTSGAARAYSGVSVASFQNMVSVQAASKAGI
DGIGECALLLARAEGLDAHANAVALRMGAAA
Show or not Domain decomposition
 
Hamap HISX_MF_01024 raw_score=9990 norm_score=41.075

Histidinol dehydrogenase [hisD].

XFF4834R

YP_363606.1 lcl|hisD-XCV1875

1

431

S=1872 I=88 E=0

histidinol dehydrogenase

XFF4834R

NP_642155.1 lcl|hisD-XAC1829

1

431

S=1857 I=89 E=0

histidinol dehydrogenase

XFF4834R

NP_637174.1 lcl|hisD-XCC1809

1

431

S=1826 I=84 E=0

histidinol dehydrogenase

XFF4834R

lcl|hisD-XALc_1254

1

427

S=1488 I=75 E=4.48512e-173

probable histidinol dehydrogenase (hdh) protein

pubmed

3

429

S=1039 I=50 E=4.16562e-117

Histidinol dehydrogenase EC=1.1.1.23 ; Amino-acid biosynthesis Histidine Manganese Metal-binding NAD Oxidoreductase Zinc

Pubmed 3062174

 

prodomImg

pubmed

3

429

S=1025 I=50 E=1.96478e-115

Histidinol dehydrogenase EC=1.1.1.23 ; Amino-acid biosynthesis Histidine Metal-binding NAD Oxidoreductase Zinc

Pubmed 10222209

 

prodomImg

pubmed

3

429

S=1024 I=49 E=3.1462e-115

Histidinol dehydrogenase EC=1.1.1.23 ; Amino-acid biosynthesis Histidine Metal-binding NAD Oxidoreductase Zinc

Pubmed 3062174,3018428

 

prodomImg

pubmed

4

427

S=1002 I=47 E=1.39493e-112

Histidine biosynthesis trifunctional protein EC=3.5.4.19 EC=3.6.1.31 EC=1.1.1.23 ; Amino-acid ATP-binding Hydrolase Metal-binding Multifunctional enzyme N

Pubmed 7874737

 

prodomImg

pubmed

1

427

S=991 I=49 E=3.19086e-111

HIS4

Pubmed 12723033

 

prodomImg

pubmed

10

427

S=979 I=48 E=8.17501e-110

Histidine biosynthesis trifunctional protein EC=3.5.4.19 EC=3.6.1.31 EC=1.1.1.23 ; Amino-acid ATP-binding Hydrolase Metal-binding Multifunctional

Pubmed 9639316

 

prodomImg

pubmed

10

427

S=934 I=46 E=2.50688e-104

Histidine biosynthesis trifunctional protein EC=3.5.4.19 EC=3.6.1.31 EC=1.1.1.23 ; Amino-acid ATP-binding Hydrolase Metal-binding Multifunctional e

Pubmed 7049842,1897318

 

prodomImg

pubmed

36

427

S=923 I=49 E=5.07549e-103

Histidinol dehydrogenase, chloroplastic EC=1.1.1.23 ; Amino-acid biosynthesis Histidine Metal-binding NAD Oxidoreductase Plastid Transit peptide Zinc

Pubmed 2034659

 

prodomImg

pubmed

10

427

S=919 I=46 E=1.6905e-102

Histidine biosynthesis trifunctional protein EC=3.5.4.19 EC=3.6.1.31 EC=1.1.1.23 ; Amino-acid ATP-binding Hydrolase Metal-binding Multifunctional enzyme N

Pubmed 9778800

 

prodomImg

pubmed

1

427

S=917 I=46 E=2.80306e-102

Histidinol dehydrogenase, chloroplastic EC=1.1.1.23 ; Alternative splicing Amino-acid biosynthesis Histidine Metal-binding NAD Oxidoreductase Pla

Pubmed 9501997

 

prodomImg

sp_Pdown

sp|Q3BUF7|HISX_XANC5

1

431

S=1872 I=88 E=0

Histidinol dehydrogenase EC=1.1.1.23 ; Amino-acid biosynthesis Histidine Metal-binding NAD Oxidoreductase Zinc

sp_Pdown

sp|Q8PLG9|HISX_XANAC

1

431

S=1857 I=89 E=0

Histidinol dehydrogenase EC=1.1.1.23 ; Amino-acid biosynthesis Histidine Metal-binding NAD Oxidoreductase Zinc

sp_Pdown

sp|Q8P9P2|HISX_XANCP

1

431

S=1826 I=84 E=0

Histidinol dehydrogenase EC=1.1.1.23 ; Amino-acid biosynthesis Histidine Metal-binding NAD Oxidoreductase Zinc

sp_Pdown

sp|Q4UU40|HISX_XANC8

1

431

S=1821 I=85 E=0

Histidinol dehydrogenase EC=1.1.1.23 ; Amino-acid biosynthesis Histidine Metal-binding NAD Oxidoreductase Zinc

sp_Pdown

sp|Q5H0L1|HISX_XANOR

1

431

S=1777 I=87 E=0

Histidinol dehydrogenase EC=1.1.1.23 ; Amino-acid biosynthesis Histidine Metal-binding NAD Oxidoreductase Zinc

Iprscan [G3DSA:3.40.50.10270]

25

237

-

Iprscan [G3DSA:3.40.50.1980]

236

397

-

Iprscan IPR012131 [MF_01024]

4

427

Histidinol dehydrogenase, prokaryotic-type

Iprscan IPR012131 [PF00815]

14

428

Histidinol dehydrogenase, prokaryotic-type

Iprscan IPR012131 [TIGR00069]

33

426

Histidinol dehydrogenase, prokaryotic-type

Iprscan IPR001692 [PS00611]

230

262

Histidinol dehydrogenase, conserved site

Iprscan [seg]

24

35

-

Iprscan [seg]

269

292

-

PD002680

6

429

S=973 I=48 E=1.9207e-110

PDA8P1D3

53

197

S=185 I=39 E=5.96114e-15

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 KlYAYaWS)
   

Show or not Access unfiltered results

pubmed

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

33 hits
swiss-prot

Swiss-Prot ncbi-blastp

230 hits
XFF4834R

Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp

0 hits
hamap

HAMAP scan

1 hits
Interpro Scan

IprScan

8 hits

Show or not Miscellaneous analyses

  • ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBSb00uX/XFF4834R_chr19740.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBSb00uX/XFF4834R_chr19740.xml_fasta", "blastp"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBSb00uX/XFF4834R_chr19740.xml_fasta"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBSb00uX/XFF4834R_chr19740.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.
hisC XFF4834R_chr19750
XFF4834R_chr19740
XFF4834R_chr19740
Cluster
DrawMap
XML file

FASTA file
Extract
Sequence
Codon
Usage
Framed OrthoMCL XFF4834R_chr19760
XFF4834R_chr19760
ID hisC
AC XFF4834R_chr19750
LT XFF4834R_chr19750
OR XFF4834R_chr from 2268249 to 2269340 on strand +
DE histidinol-phosphate aminotransferase
IP Aminotransferase, class I/II; Pyridoxal phosphate-dependent transferase, major region, subdomain 1
CL 1.5.1.16 Histidine GO:0000105
EC
GO InterPro
Biological Process: biosynthetic process (GO:0009058)
Biological Process: histidine biosynthetic process (GO:0000105)
Molecular Function: catalytic activity (GO:0003824)
Molecular Function: pyridoxal phosphate binding (GO:0030170)
Molecular Function: histidinol-phosphate transaminase activity (GO:0004400)
transferring nitrogenous groups (GO:0016769)

Curated
PM
AN
CC COG: [E] Amino acid transport and metabolism;
CC MODEL: XFF4834R
CC STATUS: curated by jacques (20110309)
MW 38594.6 Da
SQ 363 aa
 
........10........20........30........40........50
| | | | |
MSTSSILDLVREDLRAFAGYSSARTSALQGDVWLNANESAWANPADPAAS
TRRYPDPQPKGLRSALAALYGCASEQLLIGRGSDEAIDLLVRGLCVPERD
AVLVTPPVFGMYAVCARLQNAPLVDVPLVDGPDGFHADIPAIVAAALSSN
AKLVFLCSPSNPAGSAIALDEIEQALQALQGKALVVVDEAYGEFSDVPSA
VGLLGRYDNLAVLRTLSKAHALAAARIGTLIANADLIALLRRCQAPYPVP
TPCAAMAEQALSAPALEVTRRRIAEVRSERERVHKALVQLPGVRQVYPSQ
GNFLLVRFDDAEGAFQALLEAGVVVRDQRAVPRLADALRITLGTHEQNQR
VLSALQRTQEAAA
Hamap HIS8_MF_01023 raw_score=5199 norm_score=33.849

Histidinol-phosphate aminotransferase [hisC].

XFF4834R

XFF4834R_chr28800 lcl|XFF4834R_chr31420498_3321556_f2_XFF4834R-XFF4834R_chr28800

26

359

S=207 I=29 E=1.68896e-18

XFF4834R

XFF4834R_chr12240 lcl|XFF4834R_chr12890671_1386873_f1_XFF4834R-XFF4834R_chr12240

62

266

S=192 I=32 E=1.06221e-16

XFF4834R

XFF4834R_chr06390 lcl|XFF4834R_chr06650106_0729290_r2_XFF4834R-XFF4834R_chr06390

131

305

S=131 I=29 E=2.27448e-09

XFF4834R

XFF4834R_chr11530 lcl|XFF4834R_chr11990091_1285446_r1_XFF4834R-XFF4834R_chr11530

75

325

S=120 I=28 E=5.24837e-08

predicted aminotransferase

XFF4834R

XFF4834R_chr23260 lcl|XFF4834R_chr25460880_2695028_r2_XFF4834R-XFF4834R_chr23260

73

244

S=95 I=25 E=5.81265e-05

methionine aminotransferase, PLP-dependent

XFF4834R

NP_642156.1 lcl|hisC-XAC1830

1

363

S=1817 I=98 E=0

histidinol-phosphate aminotransferase

XFF4834R

YP_363607.1 lcl|hisC2-XCV1876

1

363

S=1774 I=96 E=0

histidinol-phosphate aminotransferase

XFF4834R

NP_637175.1 lcl|hisC-XCC1810

1

362

S=1638 I=87 E=0

histidinol-phosphate aminotransferase

XFF4834R

lcl|hisC-XALc_1255

3

362

S=1276 I=71 E=1.77574e-147

probable histidinol-phosphate aminotransferase (ihpat) protein

XFF4834R

NP_636940.1 lcl|hisC-XCC1569

30

360

S=244 I=30 E=2.04206e-22

putative aminotransferase

XFF4834R

lcl|XALc_1730

53

360

S=211 I=29 E=2.07105e-18

putative histidinol-phosphate aminotransferase protein

XFF4834R

YP_363398.1 lcl|hisC-XCV1667

30

359

S=206 I=29 E=7.20543e-18

putative aminotransferase

XFF4834R

NP_641958.1 lcl|hisC-XAC1626

26

359

S=203 I=29 E=2.01589e-17

putative aminotransferase

XFF4834R

YP_365269.1 lcl|hisC3-XCV3538

62

355

S=193 I=30 E=2.63929e-16

putative aminotransferase

XFF4834R

NP_643730.1 lcl|hisC-XAC3423

62

266

S=192 I=32 E=4.26328e-16

putative aminotransferase

pubmed

1

359

S=716 I=43 E=5.26977e-78

Histidinol-phosphate aminotransferase EC=2.6.1.9 ; Amino-acid biosynthesis Histidine Pyridoxal

Pubmed 3062174,2999081

 

prodomImg

pubmed

1

359

S=711 I=43 E=2.10788e-77

Histidinol-phosphate aminotransferase EC=2.6.1.9 ; Amino-acid biosynthesis Histidine Pyridoxal

Pubmed 10222209

 

prodomImg

pubmed

2

356

S=667 I=41 E=3.86445e-72

Histidinol-phosphate aminotransferase EC=2.6.1.9 ; Amino-acid biosynthesis Histidine Pyridoxal

Pubmed 3062174

 

prodomImg

pubmed

3

357

S=619 I=34 E=2.46491e-66

Histidinol-phosphate aminotransferase EC=2.6.1.9 ; Amino-acid biosynthesis Histidine Pyridoxal

Pubmed 9767718

 

prodomImg

pubmed

1

356

S=607 I=35 E=7.99127e-65

Histidinol-phosphate aminotransferase EC=2.6.1.9 ; Amino-acid biosynthesis Histidine Pyridoxal

Pubmed 17592475

 

prodomImg

pubmed

1

359

S=584 I=35 E=5.19983e-62

Histidinol-phosphate aminotransferase EC=2.6.1.9 ; Amino-acid biosynthesis Histidine Pyridoxal

Pubmed 17107561

 

prodomImg

pubmed

9

355

S=536 I=31 E=2.98719e-56

Histidinol-phosphate aminotransferase EC=2.6.1.9 ; Amino-acid biosynthesis Histidine Pyridoxal

Pubmed 17038625

 

prodomImg

pubmed

9

358

S=448 I=32 E=1.56624e-45

Histidinol-phosphate aminotransferase EC=2.6.1.9 ; Amino-acid biosynthesis Histidine Pyridoxal

Pubmed 3302607

 

prodomImg

pubmed

6

356

S=445 I=33 E=3.68075e-45

Histidinol-phosphate aminotransferase EC=2.6.1.9 ; Amino-acid biosynthesis Histidine Pyridoxal

Pubmed 2697466

 

prodomImg

pubmed

10

356

S=421 I=32 E=2.37423e-42

Histidinol-phosphate aminotransferase EC=2.6.1.9 ; Amino-acid biosynthesis Histidine Pyridoxal

Pubmed 8159167,10620777

 

prodomImg

Iprscan IPR015421 [G3DSA:3.40.640.10]

53

262

Pyridoxal phosphate-dependent transferase, major region, subdomain 1

Iprscan [MF_01023]

9

359

-

Iprscan IPR004839 [PF00155]

29

355

Aminotransferase, class I/II

Iprscan IPR005861 [TIGR01141]

11

358

Histidinol-phosphate aminotransferase

PD021719

6

88

S=155 I=43 E=2.95586e-11

PDA2A5Q6

146

174

S=136 I=93 E=5.57666e-09

PDA245V0

271

355

S=133 I=34 E=1.44246e-08

PDA1L187

175

206

S=128 I=84 E=4.76271e-08

PDA5Q058

203

356

S=128 I=33 E=5.15149e-08

PDA23983

266

356

S=123 I=31 E=1.85588e-07

PD948751

87

143

S=123 I=40 E=1.95555e-07

PD000087

71

143

S=123 I=42 E=2.04268e-07

PD975123

263

359

S=119 I=33 E=6.80359e-07

PD164716

316

356

S=114 I=59 E=2.918e-06

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 nVlQKfXK)
   

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

0 hits
XFF4834R

Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp

5 hits
hamap

HAMAP scan

1 hits
Interpro Scan

IprScan

4 hits

Show or not Miscellaneous analyses

  • ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBSb00uX/XFF4834R_chr19750.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBSb00uX/XFF4834R_chr19750.xml_fasta", "blastp"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBSb00uX/XFF4834R_chr19750.xml_fasta"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBSb00uX/XFF4834R_chr19750.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.
hisB XFF4834R_chr19760
XFF4834R_chr19750
XFF4834R_chr19750
Cluster
DrawMap
XML file

FASTA file
Extract
Sequence
Codon
Usage
Framed OrthoMCL XFF4834R_chr19770
XFF4834R_chr19770
ID hisB
AC XFF4834R_chr19760
LT XFF4834R_chr19760
OR XFF4834R_chr from 2269337 to 2270464 on strand +
DE bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase protein
IP Imidazoleglycerol-phosphate dehydratase; Histidinol-phosphatase; HAD-superfamily hydrolase, subfamily IIIA; Polynucleotide kinase 3 phosphatase, central region; Imidazoleglycerol-phosphate dehydratase, conserved site
CL 1.5.1.16 Histidine GO:0000105
EC
GO InterPro
Biological Process: histidine biosynthetic process (GO:0000105)
Cellular Component: cytoplasm (GO:0005737)
Molecular Function: imidazoleglycerol-phosphate dehydratase activity (GO:0004424)
Molecular Function: histidinol-phosphatase activity (GO:0004401)
Molecular Function: catalytic activity (GO:0003824)

Curated
PM
AN
CC COG: [E] Amino acid transport and metabolism;
CC MODEL: XFF4834R
CC STATUS: curated by jacques (20110309)
MW 41857.9 Da
SQ 375 aa
 
........10........20........30........40........50
| | | | |
MTPILFVDRDGTLITEPADYQIDAYEKLRFVDHVIPAMLKLRDAGYQFVI
VSNQDGLGSESYPRASFDGPNNLMLQIFASQGIVFREVLIDCSWPADNAP
TRKPGVGLMVPYLQDRSIDWARSAMVGDRITDIQFAQNLNIRGFQLRTDE
FGGEWDWPGIAHELADAPRRAVVQRNTKETKIRVELDLDRVAEPKTATGL
PFFDHMLEQIGKHGGFALEIRAEGDLHIDEHHTIEDTGLALGQALREALG
DKRGIGRYGFDPESSPWQVAGDTAQHGFTLPMDETIASAALDFSGRPYFV
FDGEFKRERVGDMPTELVPHFFRSICDASGLNLHLTVRGENDHHKVEACF
KALARALRQAIRREGTALPTTKGAL
Show or not Domain decomposition
 
Hamap HIS7_MF_00076 raw_score=4622 norm_score=36.141

Imidazoleglycerol-phosphate dehydratase [hisB].

Hamap HIS7_MF_01022 raw_score=12083 norm_score=52.870

Histidine biosynthesis bifunctional protein hisB [hisB].

XFF4834R

YP_363608.1 lcl|hisB-XCV1877

1

375

S=1888 I=94 E=0

imidazole glycerol-phosphate dehydratase/histidinol phosphatase

XFF4834R

NP_642157.1 lcl|hisB-XAC1831

1

375

S=1871 I=94 E=0

imidazole glycerol-phosphate dehydratase/histidinol phosphatase

XFF4834R

NP_637176.1 lcl|hisB-XCC1811

1

375

S=1830 I=91 E=0

imidazole glycerol-phosphate dehydratase/histidinol phosphatase

XFF4834R

lcl|hisB-XALc_1256

1

375

S=1564 I=79 E=0

probable histidine biosynthesis bifunctional protein hisb (includes:histidinol-phosphatase / imidazoleglycerol-phosphate dehydratase (igpd)).

pubmed

5

375

S=941 I=51 E=2.43973e-105

Histidine biosynthesis bifunctional protein hisB EC=3.1.3.15 EC=4.2.1.19 ; Amino-acid Cytoplasm Hydrolase Lyase Multifunctional enzyme

Pubmed 10222209

 

prodomImg

pubmed

5

375

S=940 I=51 E=3.51864e-105

Histidine biosynthesis bifunctional protein hisB EC=3.1.3.15 EC=4.2.1.19 ; Amino-acid Cytoplasm Hydrolase Lyase Multifunctional enzyme

Pubmed 3062174,3007936

 

prodomImg

pubmed

5

375

S=935 I=50 E=1.5491e-104

Histidine biosynthesis bifunctional protein hisB EC=3.1.3.15 EC=4.2.1.19 ; Amino-acid Cytoplasm Hydrolase Lyase Multifunctional enzyme

Pubmed 3062174

 

prodomImg

pubmed

3

375

S=852 I=45 E=1.73566e-94

Histidine biosynthesis bifunctional protein hisB EC=3.1.3.15 EC=4.2.1.19 ; Amino-acid Cytoplasm Hydrolase Lyase Multifunctional enzyme

Pubmed 9767718

 

prodomImg

pubmed

169

375

S=430 I=43 E=2.17947e-43

Imidazoleglycerol-phosphate dehydratase EC=4.2.1.19 ; Amino-acid biosynthesis Cytoplasm Histidine Lyase

Pubmed 7730278

 

prodomImg

pubmed

169

375

S=426 I=42 E=6.42506e-43

Imidazoleglycerol-phosphate dehydratase EC=4.2.1.19 ; Amino-acid biosynthesis Cytoplasm Histidine Lyase

Pubmed 17563350

 

prodomImg

pubmed

163

375

S=420 I=41 E=3.51759e-42

Imidazoleglycerol-phosphate dehydratase EC=4.2.1.19 ; Amino-acid biosynthesis Cytoplasm Histidine Lyase

Pubmed 2664449

 

prodomImg

pubmed

167

375

S=414 I=42 E=2.13822e-41

Imidazoleglycerol-phosphate dehydratase EC=4.2.1.19 ; Histidine biosynthesis Lyase

Pubmed 18043670

 

prodomImg

pubmed

169

375

S=414 I=44 E=2.19488e-41

Imidazoleglycerol-phosphate dehydratase EC=4.2.1.19 ; Amino-acid biosynthesis Cytoplasm Histidine Lyase

Pubmed 12754231

 

prodomImg

pubmed

173

375

S=413 I=41 E=2.56784e-41

Imidazoleglycerol-phosphate dehydratase 1 EC=4.2.1.19 ; Alternative splicing Amino-acid biosynthesis Histidine Lyase

Pubmed 8066131

 

prodomImg

sp_Pdown

sp|Q3BUF5|HIS7_XANC5

1

375

S=1888 I=94 E=0

Histidine biosynthesis bifunctional protein hisB EC=3.1.3.15 EC=4.2.1.19 ; Amino-acid Cytoplasm Hydrolase Lyase Multifunctional enzyme

sp_Pdown

sp|Q5H0K9|HIS7_XANOR

1

375

S=1882 I=94 E=0

Histidine biosynthesis bifunctional protein hisB EC=3.1.3.15 EC=4.2.1.19 ; Amino-acid Cytoplasm Hydrolase Lyase Multifunctional enzyme

sp_Pdown

sp|B2SKN6|HIS7_XANOP

1

375

S=1882 I=94 E=0

Histidine biosynthesis bifunctional protein hisB EC=3.1.3.15 EC=4.2.1.19 ; Amino-acid Cytoplasm Hydrolase Lyase Multifunctional enzyme

sp_Pdown

sp|Q2P3K1|HIS7_XANOM

1

375

S=1882 I=94 E=0

Histidine biosynthesis bifunctional protein hisB EC=3.1.3.15 EC=4.2.1.19 ; Amino-acid Cytoplasm Hydrolase Lyase Multifunctional enzyme

sp_Pdown

sp|P58881|HIS7_XANAC

1

375

S=1871 I=94 E=0

Histidine biosynthesis bifunctional protein hisB EC=3.1.3.15 EC=4.2.1.19 ; Amino-acid Cytoplasm Hydrolase Lyase Multifunctional enzyme

Iprscan [G3DSA:3.40.50.1000]

2

148

-

Iprscan [G3DSA:3.30.230.40]

166

256

-

Iprscan [G3DSA:3.30.230.40]

275

375

-

Iprscan IPR000807 [MF_00076]

169

375

Imidazoleglycerol-phosphate dehydratase

Iprscan IPR020566 [MF_01022]

1

375

Histidine biosynthesis bifunctional protein hisB

Iprscan IPR013954 [PF08645]

3

151

Polynucleotide kinase 3 phosphatase, central region

Iprscan IPR000807 [PF00475]

198

358

Imidazoleglycerol-phosphate dehydratase

Iprscan IPR005954 [TIGR01261]

2

165

Histidinol-phosphatase

Iprscan IPR006543 [TIGR01656]

3

151

Histidinol-phosphate phosphatase

Iprscan IPR006549 [TIGR01662]

3

149

HAD-superfamily hydrolase, subfamily IIIA

Iprscan IPR020565 [PS00954]

228

241

Imidazoleglycerol-phosphate dehydratase, conserved site

Iprscan IPR020565 [PS00955]

339

351

Imidazoleglycerol-phosphate dehydratase, conserved site

Iprscan [seg]

352

363

-

PDA20878

93

147

S=289 I=96 E=1.65261e-27

PD002282

280

351

S=220 I=56 E=3.62945e-19

PDA1F7A6

212

259

S=198 I=75 E=1.91575e-16

PDA1K9Q3

251

280

S=153 I=93 E=4.48335e-11

PDA1V354

148

172

S=135 I=100 E=8.31226e-09

PD007329

28

83

S=125 I=39 E=1.07883e-07

PDA1V165

175

259

S=121 I=38 E=4.31525e-07

PDA1L2G8

1

27

S=120 I=81 E=4.50753e-07

PDA1F7B9

169

211

S=112 I=51 E=4.82912e-06

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 tFByVsPx)
   

Show or not Access unfiltered results

pubmed

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

65 hits
swiss-prot

Swiss-Prot ncbi-blastp

520 hits
XFF4834R

Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp

0 hits
hamap

HAMAP scan

2 hits
Interpro Scan

IprScan

13 hits

Show or not Miscellaneous analyses

  • ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBSb00uX/XFF4834R_chr19760.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBSb00uX/XFF4834R_chr19760.xml_fasta", "blastp"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBSb00uX/XFF4834R_chr19760.xml_fasta"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBSb00uX/XFF4834R_chr19760.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.
hisH XFF4834R_chr19770
XFF4834R_chr19760
XFF4834R_chr19760
Cluster
DrawMap
XML file

FASTA file
Extract
Sequence
Codon
Usage
Framed OrthoMCL XFF4834R_chr19780
XFF4834R_chr19780
ID hisH
AC XFF4834R_chr19770
LT XFF4834R_chr19770
OR XFF4834R_chr from 2270461 to 2271063 on strand +
DE imidazole glycerol phosphate synthase, glutamine amidotransferase subunit with HisF
IP Glutamine amidotransferase class-I, C-terminal; Imidazole glycerol phosphate synthase, glutamine amidotransferase subunit H; Glutamine amidotransferase type 1
CL 1.5.1.16 Histidine GO:0000105
EC
GO InterPro
Biological Process: histidine biosynthetic process (GO:0000105)
Cellular Component: cytoplasm (GO:0005737)
Molecular Function: catalytic activity (GO:0003824)
Molecular Function: transferase activity (GO:0016740)
transferring pentosyl groups (GO:0016763)

Curated
PM
AN
CC COG: [E] Amino acid transport and metabolism;
CC MODEL: XFF4834R
CC STATUS: curated by jacques (20110309)
MW 21227.4 Da
SQ 200 aa
 
........10........20........30........40........50
| | | | |
MTDVALIDAGGANLGSVRYALERLGVDARVVRDAAGLQGAQRVILPGVGA
APEAMSRLRAQGLVEPLRELQVPLIGICLGMQLLFEHSEEGDVECLGLLP
GIVRHMTPALGIRVPHMGWNQLVPMRDSALLAGLPERASAYFVHGYAAPV
TADTVAACDHGGLFTAVVQNGLRCGAQFHPERSADTGARILRNFLEMSFP
Hamap HIS5_MF_00278 raw_score=4101 norm_score=32.166

Imidazole glycerol phosphate synthase subunit hisH [hisH].

XFF4834R

NP_642158.1 lcl|hisH-XAC1832

1

200

S=1020 I=99 E=9.51865e-117

imidazole glycerol phosphate synthase subunit HisH

XFF4834R

YP_363609.1 lcl|hisH-XCV1878

1

200

S=1009 I=98 E=1.60473e-115

imidazole glycerol phosphate synthase subunit HisH

XFF4834R

NP_637177.1 lcl|hisH-XCC1812

1

200

S=990 I=95 E=3.54201e-113

imidazole glycerol phosphate synthase subunit HisH

XFF4834R

lcl|hisH-XALc_1257

1

200

S=866 I=84 E=4.05677e-98

probable imidazole glycerol phosphate synthase subunit hish protein

pubmed

3

197

S=422 I=38 E=7.96752e-43

Imidazole glycerol phosphate synthase subunit hisH EC=2.4.2.- ; Amino-acid biosynthesis Cytoplasm Glutamine amidotransferase Histidine

Pubmed 9767718

 

prodomImg

pubmed

3

197

S=421 I=45 E=1.04401e-42

Imidazole glycerol phosphate synthase subunit hisH EC=2.4.2.- ; Amino-acid biosynthesis Cytoplasm Glutamine amidotransferase Histidine

Pubmed 3062174

 

prodomImg

pubmed

3

197

S=412 I=44 E=1.27477e-41

Imidazole glycerol phosphate synthase subunit hisH EC=2.4.2.- ; Amino-acid biosynthesis Cytoplasm Glutamine amidotransferase Histidine

Pubmed 10222209

 

prodomImg

pubmed

3

197

S=409 I=45 E=3.3847e-41

Imidazole glycerol phosphate synthase subunit hisH EC=2.4.2.- ; Amino-acid biosynthesis Cytoplasm Glutamine amidotransferase Histidine

Pubmed 3062174

 

prodomImg

pubmed

4

194

S=374 I=38 E=5.08201e-37

Imidazole glycerol phosphate synthase subunit hisH 1 EC=2.4.2.- ; Amino-acid biosynthesis Cytoplasm Glutamine amidotransferase Histidine

Pubmed 11461915

 

prodomImg

pubmed

4

200

S=363 I=42 E=1.04701e-35

Imidazole glycerol phosphate synthase hisHF, chloroplastic EC=2.4.2.- EC=4.1.3.- ; Amino-acid biosynthesis Glutamine amidotransferase Histidine Lyase

Pubmed 9654139

 

prodomImg

pubmed

2

198

S=339 I=40 E=1.08146e-32

Imidazole glycerol phosphate synthase subunit hisH EC=2.4.2.- ; Amino-acid biosynthesis Cytoplasm Glutamine amidotransferase Histidine

Pubmed 12754231

 

prodomImg

pubmed

4

197

S=333 I=38 E=5.47394e-32

Imidazole glycerol phosphate synthase subunit hisH 2 EC=2.4.2.- ; Amino-acid biosynthesis Cytoplasm Glutamine amidotransferase Histidine

Pubmed 8939432,12057956

 

prodomImg

pubmed

4

197

S=331 I=35 E=8.68931e-32

WbuY ; Amino-acid biosynthesis Glutamine amidotransferase Histidine

Pubmed 15629947

 

prodomImg

pubmed

1

196

S=330 I=39 E=1.13859e-31

Imidazole glycerol phosphate synthase subunit hisH EC=2.4.2.- ; Amino-acid biosynthesis Cytoplasm Glutamine amidotransferase Histidine

Pubmed 1400209

 

prodomImg

sp_Pdown

sp|Q8PLG8|HIS5_XANAC

1

200

S=1020 I=99 E=2.28677e-115

Imidazole glycerol phosphate synthase subunit hisH EC=2.4.2.- ; Amino-acid biosynthesis Cytoplasm Glutamine amidotransferase Histidine

sp_Pdown

sp|Q3BUF4|HIS5_XANC5

1

200

S=1009 I=98 E=3.85522e-114

Imidazole glycerol phosphate synthase subunit hisH EC=2.4.2.- ; Amino-acid biosynthesis Cytoplasm Glutamine amidotransferase Histidine

sp_Pdown

sp|Q5H0K8|HIS5_XANOR

1

200

S=998 I=97 E=9.13168e-113

Imidazole glycerol phosphate synthase subunit hisH EC=2.4.2.- ; Amino-acid biosynthesis Cytoplasm Glutamine amidotransferase Histidine

sp_Pdown

sp|Q2P3K0|HIS5_XANOM

1

200

S=998 I=97 E=9.13168e-113

Imidazole glycerol phosphate synthase subunit hisH EC=2.4.2.- ; Amino-acid biosynthesis Cytoplasm Glutamine amidotransferase Histidine

sp_Pdown

sp|Q8P9P1|HIS5_XANCP

1

200

S=990 I=95 E=8.50934e-112

Imidazole glycerol phosphate synthase subunit hisH EC=2.4.2.- ; Amino-acid biosynthesis Cytoplasm Glutamine amidotransferase Histidine

Iprscan [G3DSA:3.40.50.880]

4

196

-

Iprscan IPR010139 [MF_00278]

3

197

Imidazole glycerol phosphate synthase, subunit H

Iprscan IPR016226 [PIRSF000495]

2

200

Imidazole glycerol phosphate synthase, glutamine amidotransferase subunit H

Iprscan IPR000991 [PF00117]

5

198

Glutamine amidotransferase class-I, C-terminal

Iprscan IPR010139 [TIGR01855]

4

197

Imidazole glycerol phosphate synthase, subunit H

Iprscan IPR017926 [PS51273]

3

200

Glutamine amidotransferase type 1

PD988683

94

162

S=138 I=38 E=3.20641e-09

PD329941

4

59

S=125 I=49 E=1.05781e-07

PD579466

61

116

S=111 I=42 E=5.99183e-06

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 KFHoeKhb)
   

Show or not Access unfiltered results

pubmed

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

23 hits
swiss-prot

Swiss-Prot ncbi-blastp

262 hits
XFF4834R

Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp

0 hits
hamap

HAMAP scan

1 hits
Interpro Scan

IprScan

6 hits

Show or not Miscellaneous analyses

  • ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBSb00uX/XFF4834R_chr19770.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBSb00uX/XFF4834R_chr19770.xml_fasta", "blastp"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBSb00uX/XFF4834R_chr19770.xml_fasta"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBSb00uX/XFF4834R_chr19770.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.
hisA XFF4834R_chr19780
XFF4834R_chr19770
XFF4834R_chr19770
Cluster
DrawMap
XML file

FASTA file
Extract
Sequence
Codon
Usage
Framed OrthoMCL XFF4834R_chr19790
XFF4834R_chr19790
ID hisA
AC XFF4834R_chr19780
LT XFF4834R_chr19780
OR XFF4834R_chr from 2271060 to 2271794 on strand +
DE N-(5'-phospho-L-ribosyl-formimino)-5-amino-1-(5'-phosphoribosyl)-4-imidazolecarboxamide isomerase
IP Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; Ribulose-phosphate binding barrel
CL 1.5.1.16 Histidine GO:0000105
EC
GO InterPro
Biological Process: metabolic process (GO:0008152)
Biological Process: histidine biosynthetic process (GO:0000105)
Molecular Function: 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity (GO:0003949)
Molecular Function: catalytic activity (GO:0003824)

Curated
PM
AN
CC COG: [E] Amino acid transport and metabolism;
CC MODEL: XFF4834R
CC STATUS: curated by jacques (20110309)
MW 25757.1 Da
SQ 244 aa
 
........10........20........30........40........50
| | | | |
MSFTVYPALDIRNGRVVRLLQGDYARETQYGDDVLPRAQAFAAAGAQWMH
LVDLDAAKAGGYTLASTLGEIARATGLRVQTGGGVRSREDVARILDAGAA
RVVIGSLAVRDSEMVIGWLQEFGADRLTIALDTRQDANGVWQLPVHGWTE
AADATLDQLAVRYAQAGLQHLLCTDIARDGMLSGPNMALYAHLRALTPQL
QVQVSGGARNLADVAAAKAAGCAGIVLGKALLEGHLNLDEALAC
Hamap HIS4_MF_01014 raw_score=4527 norm_score=31.624

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase [hisA].

XFF4834R

XFF4834R_chr19790 lcl|hisF-XFF4834R_chr19790

1

207

S=103 I=24 E=4.15382e-06

imidazole glycerol phosphate synthase, catalytic subunit with HisH

XFF4834R

YP_363610.1 lcl|hisA-XCV1879

1

244

S=1057 I=86 E=4.0608e-121

1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase

XFF4834R

NP_642159.1 lcl|hisA-XAC1833

1

244

S=1052 I=86 E=1.37633e-120

1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase

XFF4834R

NP_637178.1 lcl|hisA-XCC1813

1

244

S=982 I=80 E=4.35939e-112

1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino] imidazole-4- carboxamide isomerase

XFF4834R

lcl|hisA-XALc_1258

1

244

S=802 I=67 E=2.71987e-90

probable1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino) imidazole-4-carboxamide isomerase protein

XFF4834R

NP_637179.1 lcl|hisF-XCC1814

1

207

S=110 I=25 E=1.85255e-06

imidazole glycerol phosphate synthase subunit HisF

XFF4834R

NP_642160.1 lcl|hisF-XAC1834

1

207

S=105 I=24 E=7.74027e-06

imidazole glycerol phosphate synthase subunit HisF

XFF4834R

YP_363611.1 lcl|hisF-XCV1880

1

207

S=103 I=24 E=1.47556e-05

imidazole glycerol phosphate synthase subunit HisF

XFF4834R

lcl|hisF-XALc_1259

1

207

S=100 I=23 E=3.65388e-05

probable imidazole glycerol phosphate synthase subunit hisf protein

pubmed

5

244

S=520 I=45 E=1.6768e-54

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase EC=5.3.1.16 ; Amino-acid biosynthesis Cytoplasm H

Pubmed 10222209

 

prodomImg

pubmed

5

244

S=516 I=45 E=4.18854e-54

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase EC=5.3.1.16 ; Amino-acid biosynthesis Cytoplasm His

Pubmed 3062174

 

prodomImg

pubmed

5

244

S=507 I=44 E=5.53183e-53

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase EC=5.3.1.16 ; Amino-acid biosynthesis Cytoplasm Hi

Pubmed 3062174

 

prodomImg

pubmed

5

244

S=425 I=33 E=4.89798e-43

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase EC=5.3.1.16 ; Amino-acid biosynthesis Cytoplasm Hi

Pubmed 9767718

 

prodomImg

pubmed

5

244

S=406 I=29 E=8.92403e-41

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase EC=5.3.1.16 ; Amino-acid biosynthesis Cytoplasm Histidine

Pubmed 17038625

 

prodomImg

pubmed

5

240

S=377 I=31 E=3.4386e-37

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase EC=5.3.1.16 ; Amino-acid biosynthesis Cytoplasm Histidine

Pubmed 17107561

 

prodomImg

pubmed

5

240

S=364 I=31 E=1.41069e-35

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase EC=5.3.1.16 ; Amino-acid biosynthesis Cytoplasm Histidine

Pubmed 17592475

 

prodomImg