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: histidyl-tRNA aminoacylation (GO:0006427) Biological Process: tRNA aminoacylation for protein translation (GO:0006418) Biological Process: translation (GO:0006412) Cellular Component: cytoplasm (GO:0005737) Molecular Function: nucleotide binding (GO:0000166) Molecular Function: ATP binding (GO:0005524) Molecular Function: aminoacyl-tRNA ligase activity (GO:0004812) Molecular Function: histidine-tRNA ligase activity (GO:0004821) 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

Q8PLH2 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

prodomImg

Q5H0L6 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

prodomImg

B2SKP3 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

prodomImg

Q2P3K8 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

prodomImg

Q4UU37 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

prodomImg

[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

Suggestions

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Move your mouse over each field to get more informations
ID
DE
EC
GO
PM
CC
CL
	Your email
	Validation code (copy this one QqNE9TCO)

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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBjTFgxp/XFF4834R_chr19710.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBjTFgxp/XFF4834R_chr19710.xml_fasta", "blastp"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBjTFgxp/XFF4834R_chr19710.xml_fasta"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBjTFgxp/XFF4834R_chr19710.xml_fasta", "blastp"\) - 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

Q3BUF8 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

prodomImg

Q8PLH0 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

prodomImg

Q4UU39 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

prodomImg

Q5H0L2 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

prodomImg

B2SKN9 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

prodomImg

[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
GO
PM
CC
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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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBjTFgxp/XFF4834R_chr19730.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBjTFgxp/XFF4834R_chr19730.xml_fasta", "blastp"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBjTFgxp/XFF4834R_chr19730.xml_fasta"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBjTFgxp/XFF4834R_chr19730.xml_fasta", "blastp"\) - 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: NAD or NADH binding (GO:0051287) Molecular Function: zinc ion binding (GO:0008270) 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

Q3BUF7 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

prodomImg

Q8PLG9 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

prodomImg

Q8P9P2 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

prodomImg

Q4UU40 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

prodomImg

Q5H0L1 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

prodomImg

[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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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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBjTFgxp/XFF4834R_chr19740.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBjTFgxp/XFF4834R_chr19740.xml_fasta", "blastp"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBjTFgxp/XFF4834R_chr19740.xml_fasta"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBjTFgxp/XFF4834R_chr19740.xml_fasta", "blastp"\) - 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: biosynthetic process (GO:0009058) Biological Process: histidine biosynthetic process (GO:0000105) Molecular Function: histidinol-phosphate transaminase activity (GO:0004400) Molecular Function: catalytic activity (GO:0003824) Molecular Function: pyridoxal phosphate binding (GO:0030170) 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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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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBjTFgxp/XFF4834R_chr19750.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBjTFgxp/XFF4834R_chr19750.xml_fasta", "blastp"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBjTFgxp/XFF4834R_chr19750.xml_fasta"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBjTFgxp/XFF4834R_chr19750.xml_fasta", "blastp"\) - 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: histidinol-phosphatase activity (GO:0004401) Molecular Function: imidazoleglycerol-phosphate dehydratase activity (GO:0004424) 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

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

Q3BUF5 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

prodomImg

Q5H0K9 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

prodomImg

B2SKN6 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

prodomImg

Q2P3K1 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

prodomImg

P58881 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

prodomImg

[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

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

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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBjTFgxp/XFF4834R_chr19760.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBjTFgxp/XFF4834R_chr19760.xml_fasta", "blastp"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBjTFgxp/XFF4834R_chr19760.xml_fasta"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBjTFgxp/XFF4834R_chr19760.xml_fasta", "blastp"\) - 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: 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

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

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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

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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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Q8PLG8 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

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Q3BUF4 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

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Q5H0K8 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

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Q2P3K0 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

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Q8P9P1 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

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[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

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ID
DE
EC
GO
PM
CC
CL
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	Validation code (copy this one urQvxPPl)

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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBjTFgxp/XFF4834R_chr19770.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBjTFgxp/XFF4834R_chr19770.xml_fasta", "blastp"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBjTFgxp/XFF4834R_chr19770.xml_fasta"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBjTFgxp/XFF4834R_chr19770.xml_fasta", "blastp"\) - 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: histidine biosynthetic process (GO:0000105) Biological Process: metabolic process (GO:0008152) 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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Q9RPQ5 sp|Q9RPQ5|HIS4_THEP3

242

S=345 I=33 E=2.75593e-33

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

Pubmed 10594232

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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