Xanthomonas fuscans subsp. fuscans

9 hits

XFF4834R_chr19710 hisS XFF4834R_chr19710 histidyl tRNA synthetase
XFF4834R_chr19730 hisG XFF4834R_chr19730 ATP phosphoribosyltransferase
XFF4834R_chr19740 hisD XFF4834R_chr19740 histidinol dehydrogenase
XFF4834R_chr19750 hisC XFF4834R_chr19750 histidinol-phosphate aminotransferase
XFF4834R_chr19760 hisB XFF4834R_chr19760 bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase protein
XFF4834R_chr19770 hisH XFF4834R_chr19770 imidazole glycerol phosphate synthase, glutamine amidotransferase subunit with HisF
XFF4834R_chr19780 hisA XFF4834R_chr19780 N-(5'-phospho-L-ribosyl-formimino)-5-amino-1-(5'-phosphoribosyl)-4-imidazolecarboxamide isomerase
XFF4834R_chr19790 hisF XFF4834R_chr19790 imidazole glycerol phosphate synthase, catalytic subunit with HisH
XFF4834R_chr19800 hisIE XFF4834R_chr19800 bifunctional phosphoribosyl-AMP cyclohydrolase-phosphoribosyl-ATP pyrophosphatase

hisS XFF4834R_chr19710

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: tRNA aminoacylation for protein translation (GO:0006418) Biological Process: histidyl-tRNA aminoacylation (GO:0006427) Biological Process: translation (GO:0006412) Cellular Component: cytoplasm (GO:0005737) Molecular Function: ATP binding (GO:0005524) Molecular Function: nucleotide binding (GO:0000166) Molecular Function: histidine-tRNA ligase activity (GO:0004821) 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

NP_642152.1 lcl|hisS-XAC1826

469

S=2281 I=94 E=0

histidyl-tRNA synthetase

NP_637171.1 lcl|hisS-XCC1806

469

S=2224 I=92 E=0

histidyl-tRNA synthetase

lcl|hisS-XALc_1250

469

S=2100 I=87 E=0

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

YP_363603.1 lcl|hisS-XCV1872

469

S=2025 I=84 E=0

histidyl-tRNA synthetase

B0S168 sp|B0S168|SYH_FINM2

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

B7GPS9 sp|B7GPS9|SYH_BIFLI

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

B8DU04 sp|B8DU04|SYH_BIFA0

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

B6YS23 sp|B6YS23|SYH_AZOPC

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

B2S3N0 sp|B2S3N0|SYH_TREPS

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|Q8PLH2|SYH_XANAC

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|Q5H0L6|SYH_XANOR

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|B2SKP3|SYH_XANOP

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|Q2P3K8|SYH_XANOM

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|Q4UU37|SYH_XANC8

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

[G3DSA:3.30.930.10]

364

IPR004154 [G3DSA:3.40.50.800]

368

459

Anticodon-binding

IPR015807 [MF_00127]

465

Histidyl-tRNA synthetase, class IIa, subgroup

IPR004516 [PIRSF001549]

463

Histidyl-tRNA synthetase, class IIa

IPR004516 [PTHR11476]

464

Histidyl-tRNA synthetase, class IIa

IPR002314 [PF00587]

184

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

IPR004154 [PF03129]

372

459

Anticodon-binding

IPR015807 [TIGR00442]

452

Histidyl-tRNA synthetase, class IIa, subgroup

IPR006195 [PS50862]

470

Aminoacyl-tRNA synthetase, class II, conserved domain

[seg]

[SignalP-NN(euk)]

PD001912

181

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

PD155307

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

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

PDA4V4X2

245

269

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

[SSF55681]

366

IPR004154 [SSF52954]

368

464

Anticodon-binding

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EC
GO
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	Your email
	Validation code (copy this one z5EYYHMj)

Access unfiltered results

	Set of Uniprot with relevant PubMed cross-references ncbi-blastp	78 hits
	Swiss-Prot ncbi-blastp	0 hits
	Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp	0 hits
	HAMAP scan	0 hits
	IprScan	13 hits

Miscellaneous analyses

ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBv4iTLS/XFF4834R_chr19710.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBv4iTLS/XFF4834R_chr19710.xml_fasta", "blastp"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBv4iTLS/XFF4834R_chr19710.xml_fasta"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBv4iTLS/XFF4834R_chr19710.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

hisG XFF4834R_chr19730

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: ATP phosphoribosyltransferase activity (GO:0003879) Molecular Function: magnesium ion binding (GO:0000287) 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

HIS1_MF_00079

raw_score=4976 norm_score=31.245

ATP phosphoribosyltransferase [hisG].

YP_363605.1 lcl|hisG-XCV1874

304

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

ATP phosphoribosyltransferase

NP_642154.1 lcl|hisG-XAC1828

304

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

ATP phosphoribosyltransferase

NP_637173.1 lcl|hisG-XCC1808

304

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

ATP phosphoribosyltransferase

lcl|hisG-XALc_1253

304

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

probable atp phosphoribosyltransferase (atp-prt) protein

P60757 sp|P60757|HIS1_ECOLI

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

P00499 sp|P00499|HIS1_SALTY

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

Q9RQ89 sp|Q9RQ89|HIS1_BUCDN

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

Q9ZHE7 sp|Q9ZHE7|HIS1_BUCAP

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

Q9RQ86 sp|Q9RQ86|HIS1_BUCSC

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

Q9RQ83 sp|Q9RQ83|HIS1_BUCMH

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

B6YQ21 sp|B6YQ21|HIS1_AZOPC

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

Q0W6K3 sp|Q0W6K3|HIS1_UNCMA

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

Q18EV8 sp|Q18EV8|HIS1_HALWD

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

O33771 sp|O33771|HIS1_SULSO

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|Q3BUF8|HIS1_XANC5

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|Q8PLH0|HIS1_XANAC

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|Q4UU39|HIS1_XANC8

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|Q5H0L2|HIS1_XANOR

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|B2SKN9|HIS1_XANOP

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

[G3DSA:3.40.190.10]

141

IPR015867 [G3DSA:3.30.70.120]

232

304

Nitrogen regulatory protein PII/ATP phosphoribosyltransferase, C-terminal

IPR020621 [MF_00079]

304

Histidine biosynthesis HisG, ATP phosphoribosyltransferase, subgroup

IPR013820 [PF01634]

227

ATP phosphoribosyltransferase, catalytic region

IPR013115 [PF08029]

228

302

Histidine biosynthesis HisG, C-terminal

IPR013820 [TIGR00070]

203

ATP phosphoribosyltransferase, catalytic region

IPR013115 [TIGR03455]

204

303

Histidine biosynthesis HisG, C-terminal

IPR018198 [PS01316]

162

183

ATP phosphoribosyltransferase, conserved site

[seg]

209

225

PD874462

202

304

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

PD003516

201

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

Suggestions

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Move your mouse over each field to get more informations
ID
DE
EC
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Access unfiltered results

	Set of Uniprot with relevant PubMed cross-references ncbi-blastp	31 hits
	Swiss-Prot ncbi-blastp	458 hits
	Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp	0 hits
	HAMAP scan	1 hits
	IprScan	10 hits

Miscellaneous analyses

ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBv4iTLS/XFF4834R_chr19730.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBv4iTLS/XFF4834R_chr19730.xml_fasta", "blastp"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBv4iTLS/XFF4834R_chr19730.xml_fasta"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBv4iTLS/XFF4834R_chr19730.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

hisD XFF4834R_chr19740

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: zinc ion binding (GO:0008270) Molecular Function: NAD or NADH binding (GO:0051287) Molecular Function: histidinol dehydrogenase activity (GO:0004399) 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

Domain decomposition

HISX_MF_01024

raw_score=9990 norm_score=41.075

Histidinol dehydrogenase [hisD].

YP_363606.1 lcl|hisD-XCV1875

431

S=1872 I=88 E=0

histidinol dehydrogenase

NP_642155.1 lcl|hisD-XAC1829

431

S=1857 I=89 E=0

histidinol dehydrogenase

NP_637174.1 lcl|hisD-XCC1809

431

S=1826 I=84 E=0

histidinol dehydrogenase

lcl|hisD-XALc_1254

427

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

probable histidinol dehydrogenase (hdh) protein

P10370 sp|P10370|HISX_SALTY

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

Q8X8T3 sp|Q8X8T3|HISX_ECO57

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

P06988 sp|P06988|HISX_ECOLI

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

P45353 sp|P45353|HIS2_PICPA

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

Q7ZA54 sp|Q7ZA54|Q7ZA54_HEBCY

427

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

HIS4

Pubmed 12723033

prodomImg

O13471 sp|O13471|HIS2_KLULA

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

P00815 sp|P00815|HIS2_YEAST

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

P24226 sp|P24226|HISX_BRAOC

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

O74712 sp|O74712|HIS2_CANAL

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

Q9C5U8 sp|Q9C5U8|HISX_ARATH

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|Q3BUF7|HISX_XANC5

431

S=1872 I=88 E=0

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

sp|Q8PLG9|HISX_XANAC

431

S=1857 I=89 E=0

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

sp|Q8P9P2|HISX_XANCP

431

S=1826 I=84 E=0

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

sp|Q4UU40|HISX_XANC8

431

S=1821 I=85 E=0

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

sp|Q5H0L1|HISX_XANOR

431

S=1777 I=87 E=0

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

[G3DSA:3.40.50.10270]

237

[G3DSA:3.40.50.1980]

236

397

IPR012131 [MF_01024]

427

Histidinol dehydrogenase, prokaryotic-type

IPR012131 [PF00815]

428

Histidinol dehydrogenase, prokaryotic-type

IPR012131 [TIGR00069]

426

Histidinol dehydrogenase, prokaryotic-type

IPR001692 [PS00611]

230

262

Histidinol dehydrogenase, conserved site

[seg]

269

292

PD002680

429

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

PDA8P1D3

197

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

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ID
DE
EC
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	Your email
	Validation code (copy this one 7GQZTkq0)

Access unfiltered results

	Set of Uniprot with relevant PubMed cross-references ncbi-blastp	33 hits
	Swiss-Prot ncbi-blastp	230 hits
	Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp	0 hits
	HAMAP scan	1 hits
	IprScan	8 hits

Miscellaneous analyses

ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBv4iTLS/XFF4834R_chr19740.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBv4iTLS/XFF4834R_chr19740.xml_fasta", "blastp"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBv4iTLS/XFF4834R_chr19740.xml_fasta"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBv4iTLS/XFF4834R_chr19740.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

hisC XFF4834R_chr19750

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: histidine biosynthetic process (GO:0000105) Biological Process: biosynthetic process (GO:0009058) Molecular Function: pyridoxal phosphate binding (GO:0030170) Molecular Function: catalytic activity (GO:0003824) 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

HIS8_MF_01023

raw_score=5199 norm_score=33.849

Histidinol-phosphate aminotransferase [hisC].

XFF4834R_chr28800 lcl|XFF4834R_chr31420498_3321556_f2_XFF4834R-XFF4834R_chr28800

359

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

XFF4834R_chr12240 lcl|XFF4834R_chr12890671_1386873_f1_XFF4834R-XFF4834R_chr12240

266

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

XFF4834R_chr06390 lcl|XFF4834R_chr06650106_0729290_r2_XFF4834R-XFF4834R_chr06390

131

305

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

XFF4834R_chr11530 lcl|XFF4834R_chr11990091_1285446_r1_XFF4834R-XFF4834R_chr11530

325

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

predicted aminotransferase

XFF4834R_chr23260 lcl|XFF4834R_chr25460880_2695028_r2_XFF4834R-XFF4834R_chr23260

244

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

methionine aminotransferase, PLP-dependent

NP_642156.1 lcl|hisC-XAC1830

363

S=1817 I=98 E=0

histidinol-phosphate aminotransferase

YP_363607.1 lcl|hisC2-XCV1876

363

S=1774 I=96 E=0

histidinol-phosphate aminotransferase

NP_637175.1 lcl|hisC-XCC1810

362

S=1638 I=87 E=0

histidinol-phosphate aminotransferase

lcl|hisC-XALc_1255

362

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

probable histidinol-phosphate aminotransferase (ihpat) protein

NP_636940.1 lcl|hisC-XCC1569

360

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

putative aminotransferase

lcl|XALc_1730

360

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

putative histidinol-phosphate aminotransferase protein

YP_363398.1 lcl|hisC-XCV1667

359

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

putative aminotransferase

NP_641958.1 lcl|hisC-XAC1626

359

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

putative aminotransferase

YP_365269.1 lcl|hisC3-XCV3538

355

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

putative aminotransferase

NP_643730.1 lcl|hisC-XAC3423

266

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

putative aminotransferase

P06986 sp|P06986|HIS8_ECOLI

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

Q9S5G6 sp|Q9S5G6|HIS8_ECO57

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

P10369 sp|P10369|HIS8_SALTY

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

Q9ZHE5 sp|Q9ZHE5|HIS8_BUCAP

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

A6GY79 sp|A6GY79|HIS8_FLAPJ

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

A0M287 sp|A0M287|HIS8_GRAFK

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

Q058A6 sp|Q058A6|HIS8_BUCCC

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

P07172 sp|P07172|HIS8_YEAST

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

P56099 sp|P56099|HIS8_CANMA

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

P36605 sp|P36605|HIS8_SCHPO

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

IPR015421 [G3DSA:3.40.640.10]

262

Pyridoxal phosphate-dependent transferase, major region, subdomain 1

[MF_01023]

359

IPR004839 [PF00155]

355

Aminotransferase, class I/II

IPR005861 [TIGR01141]

358

Histidinol-phosphate aminotransferase

PD021719

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

143

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

PD000087

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

Suggestions

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Move your mouse over each field to get more informations
ID
DE
EC
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PM
CC
CL
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	Validation code (copy this one Gvr7dYnT)

Access unfiltered results

	Set of Uniprot with relevant PubMed cross-references ncbi-blastp	103 hits
	Swiss-Prot ncbi-blastp	0 hits
	Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp	5 hits
	HAMAP scan	1 hits
	IprScan	4 hits

Miscellaneous analyses

ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBv4iTLS/XFF4834R_chr19750.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBv4iTLS/XFF4834R_chr19750.xml_fasta", "blastp"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBv4iTLS/XFF4834R_chr19750.xml_fasta"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBv4iTLS/XFF4834R_chr19750.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

hisB XFF4834R_chr19760

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: catalytic activity (GO:0003824) Molecular Function: histidinol-phosphatase activity (GO:0004401) Molecular Function: imidazoleglycerol-phosphate dehydratase activity (GO:0004424) 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

Domain decomposition

HIS7_MF_00076

raw_score=4622 norm_score=36.141

Imidazoleglycerol-phosphate dehydratase [hisB].

HIS7_MF_01022

raw_score=12083 norm_score=52.870

Histidine biosynthesis bifunctional protein hisB [hisB].

YP_363608.1 lcl|hisB-XCV1877

375

S=1888 I=94 E=0

imidazole glycerol-phosphate dehydratase/histidinol phosphatase

NP_642157.1 lcl|hisB-XAC1831

375

S=1871 I=94 E=0

imidazole glycerol-phosphate dehydratase/histidinol phosphatase

NP_637176.1 lcl|hisB-XCC1811

375

S=1830 I=91 E=0

imidazole glycerol-phosphate dehydratase/histidinol phosphatase

lcl|hisB-XALc_1256

375

S=1564 I=79 E=0

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

Q9S5G5 sp|Q9S5G5|HIS7_ECO57

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

P06987 sp|P06987|HIS7_ECOLI

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

P10368 sp|P10368|HIS7_SALTY

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

Q9ZHE4 sp|Q9ZHE4|HIS7_BUCAP

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

Q50504 sp|Q50504|HIS7_METTH

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

A5UMI3 sp|A5UMI3|HIS7_METS3

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

P18787 sp|P18787|HIS7_AZOBR

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

A0JJW8 sp|A0JJW8|A0JJW8_9EUKA

167

375

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

Imidazoleglycerol-phosphate dehydratase EC=4.2.1.19 ; Histidine biosynthesis Lyase

Pubmed 18043670

prodomImg

Q845V1 sp|Q845V1|HIS7_BURM1

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

P34047 sp|P34047|HIS7A_ARATH

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|Q3BUF5|HIS7_XANC5

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|Q5H0K9|HIS7_XANOR

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|B2SKN6|HIS7_XANOP

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|Q2P3K1|HIS7_XANOM

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|P58881|HIS7_XANAC

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

[G3DSA:3.40.50.1000]

148

[G3DSA:3.30.230.40]

166

256

[G3DSA:3.30.230.40]

275

375

IPR000807 [MF_00076]

169

375

Imidazoleglycerol-phosphate dehydratase

IPR020566 [MF_01022]

375

Histidine biosynthesis bifunctional protein hisB

IPR013954 [PF08645]

151

Polynucleotide kinase 3 phosphatase, central region

IPR000807 [PF00475]

198

358

Imidazoleglycerol-phosphate dehydratase

IPR005954 [TIGR01261]

165

Histidinol-phosphatase

IPR006543 [TIGR01656]

151

Histidinol-phosphate phosphatase

IPR006549 [TIGR01662]

149

HAD-superfamily hydrolase, subfamily IIIA

IPR020565 [PS00954]

228

241

Imidazoleglycerol-phosphate dehydratase, conserved site

IPR020565 [PS00955]

339

351

Imidazoleglycerol-phosphate dehydratase, conserved site

[seg]

352

363

PDA20878

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

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

PDA1V165

175

259

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

PDA1L2G8

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

PDA1F7B9

169

211

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

Suggestions

Suggest an annotation
Move your mouse over each field to get more informations
ID
DE
EC
GO
PM
CC
CL
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	Validation code (copy this one IWMt1UMy)

Access unfiltered results

	Set of Uniprot with relevant PubMed cross-references ncbi-blastp	65 hits
	Swiss-Prot ncbi-blastp	520 hits
	Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp	0 hits
	HAMAP scan	2 hits
	IprScan	13 hits

Miscellaneous analyses

ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBv4iTLS/XFF4834R_chr19760.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBv4iTLS/XFF4834R_chr19760.xml_fasta", "blastp"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBv4iTLS/XFF4834R_chr19760.xml_fasta"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBv4iTLS/XFF4834R_chr19760.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

hisH XFF4834R_chr19770

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: transferase activity (GO:0016740) Molecular Function: catalytic activity (GO:0003824) 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

HIS5_MF_00278

raw_score=4101 norm_score=32.166

Imidazole glycerol phosphate synthase subunit hisH [hisH].

NP_642158.1 lcl|hisH-XAC1832

200

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

imidazole glycerol phosphate synthase subunit HisH

YP_363609.1 lcl|hisH-XCV1878

200

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

imidazole glycerol phosphate synthase subunit HisH

NP_637177.1 lcl|hisH-XCC1812

200

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

imidazole glycerol phosphate synthase subunit HisH

lcl|hisH-XALc_1257

200

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

probable imidazole glycerol phosphate synthase subunit hish protein

Q9ZHE3 sp|Q9ZHE3|HIS5_BUCAP

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

P60595 sp|P60595|HIS5_ECOLI

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

P58237 sp|P58237|HIS5_ECO57

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

P0A1R4 sp|P0A1R4|HIS5_SALTY

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

A1W0U9 sp|A1W0U9|HIS51_CAMJJ

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

Q9SZ30 sp|Q9SZ30|HIS5_ARATH

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

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Q845U9 sp|Q845U9|HIS5_BURM1

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

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P72138 sp|P72138|HIS52_PSEAE

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

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Q5ISX2 sp|Q5ISX2|Q5ISX2_ECOLX

197

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

WbuY ; Amino-acid biosynthesis Glutamine amidotransferase Histidine

Pubmed 15629947

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Q02132 sp|Q02132|HIS5_LACLA

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

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sp|Q8PLG8|HIS5_XANAC

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|Q3BUF4|HIS5_XANC5

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|Q5H0K8|HIS5_XANOR

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|Q2P3K0|HIS5_XANOM

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|Q8P9P1|HIS5_XANCP

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

[G3DSA:3.40.50.880]

196

IPR010139 [MF_00278]

197

Imidazole glycerol phosphate synthase, subunit H

IPR016226 [PIRSF000495]

200

Imidazole glycerol phosphate synthase, glutamine amidotransferase subunit H

IPR000991 [PF00117]

198

Glutamine amidotransferase class-I, C-terminal

IPR010139 [TIGR01855]

197

Imidazole glycerol phosphate synthase, subunit H

IPR017926 [PS51273]

200

Glutamine amidotransferase type 1

PD988683

162

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

PD329941

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

PD579466

116

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

Suggestions

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ID
DE
EC
GO
PM
CC
CL
	Your email
	Validation code (copy this one uEL2LWdh)

Access unfiltered results

	Set of Uniprot with relevant PubMed cross-references ncbi-blastp	23 hits
	Swiss-Prot ncbi-blastp	262 hits
	Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp	0 hits
	HAMAP scan	1 hits
	IprScan	6 hits

Miscellaneous analyses

ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBv4iTLS/XFF4834R_chr19770.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBv4iTLS/XFF4834R_chr19770.xml_fasta", "blastp"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBv4iTLS/XFF4834R_chr19770.xml_fasta"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBv4iTLS/XFF4834R_chr19770.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

hisA XFF4834R_chr19780

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: catalytic activity (GO:0003824) Molecular Function: 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity (GO:0003949) 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

HIS4_MF_01014

raw_score=4527 norm_score=31.624

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

XFF4834R_chr19790 lcl|hisF-XFF4834R_chr19790

207

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

imidazole glycerol phosphate synthase, catalytic subunit with HisH

YP_363610.1 lcl|hisA-XCV1879

244

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

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

NP_642159.1 lcl|hisA-XAC1833

244

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

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

NP_637178.1 lcl|hisA-XCC1813

244

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

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

lcl|hisA-XALc_1258

244

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

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

NP_637179.1 lcl|hisF-XCC1814

207

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

imidazole glycerol phosphate synthase subunit HisF

NP_642160.1 lcl|hisF-XAC1834

207

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

imidazole glycerol phosphate synthase subunit HisF

YP_363611.1 lcl|hisF-XCV1880

207

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

imidazole glycerol phosphate synthase subunit HisF

lcl|hisF-XALc_1259

207

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

probable imidazole glycerol phosphate synthase subunit hisf protein

Q9S5G4 sp|Q9S5G4|HIS4_ECO57

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

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P10371 sp|P10371|HIS4_ECOLI

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

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P10372 sp|P10372|HIS4_SALTY

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

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Q9ZHE2 sp|Q9ZHE2|HIS4_BUCAP

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

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Q058A3 sp|Q058A3|HIS4_BUCCC

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

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A0M284 sp|A0M284|HIS4_GRAFK

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

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A6GY76 sp|A6GY76|HIS4_FLAPJ

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

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hisS XFF4834R_chr19710

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hisG XFF4834R_chr19730

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hisD XFF4834R_chr19740

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hisC XFF4834R_chr19750

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hisB XFF4834R_chr19760

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hisH XFF4834R_chr19770

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hisA XFF4834R_chr19780