Xanthomonas fuscans subsp. fuscans

235

261

PD117136

233

S=294 I=41 E=3.88358e-28

PDA3D8C9

S=129 I=86 E=3.35105e-08

PD665280

S=103 I=86 E=5.64005e-05

IPR010252 [PTHR11271:SF4]

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ID
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EC
GO
PM
CC
CL
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	Validation code (copy this one lV6KmmNl)

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	Set of Uniprot with relevant PubMed cross-references ncbi-blastp	3 hits
	Swiss-Prot ncbi-blastp	0 hits
	Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp	0 hits
	HAMAP scan	0 hits
	IprScan	3 hits

Miscellaneous analyses

ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBnyQIt7/XFF4834R_chr09160.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBnyQIt7/XFF4834R_chr09160.xml_fasta", "blastp"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBnyQIt7/XFF4834R_chr09160.xml_fasta"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBnyQIt7/XFF4834R_chr09160.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

XFF4834R_chr31230591_3301961_r2_XFF4834R-XFF4834R_chr28680 XFF4834R_chr28680

ID	XFF4834R_chr31230591_3301961_r2_XFF4834R-XFF4834R_chr28680
AC	XFF4834R_chr28680
LT	XFF4834R_chr28680
OR	XFF4834R_chr from 3300591 to 3301961 on strand -
DE	putative N-formimino-L-glutamate deiminase
IP	Formiminoglutamate deiminase
CL	1.1.3.11 Histidine degradation GO:0006548
EC
GO	InterPro Molecular Function: hydrolase activity (GO:0016787) acting on carbon-nitrogen (but not peptide) bonds (GO:0016810) Curated
PM
AN	In some species, histidine utilisation goes via urocanate to glutamate in four step, the last being removal of formamide. This entry describes an alternate fourth step, formiminoglutamate hydrolase, which leads to N-formyl-L-glutamate. This product may be acted on by formylglutamate amidohydrolase (IPR010247) and bypass glutamate as a product during its degradation. Alternatively, removal of formate (by EC: 3.5.1.68) would yield glutamate.
CC	COG: [FR] Nucleotide transport and metabolism;General function prediction only;
CC	MODEL: XFF4834R
CC	STATUS: curated by darrasse (20120404)
MW	48852 Da
SQ	456 aa
	........10........20........30........40........50 \| \| \| \| \| MADQQMQVFWAARALLPDGWASGVRIEVVQGRIGAVQVDAPAALTDTRCD VVLPGLGNLHSHAFQRGMAGLTEVGGRSGDSFWSWRELMYRFVDRLDPDS LQAIAEQAYVEMLESGFTRVGEFHYLHHAASGAPYAQAGEMSERIAAAAA STGIGLSLLPVFYAHSDFGGAAPSPAQRRLIHDVDGFARLLDDCRHSLKA LPDAVLGLAPHSLRAVTPQQLAALVPLTDGPIHLHIAEQQREVDACLAWS RQRPVQWLLANAPVDARWCLVHATHVDARELQAIVTSGAVVGLCPITEAN LGDGVFPMQAFAAAGGRFGVGSDSNVLIDAAEELRLLEYGQRLTLQARNV LAQGPVSSGRWLYGQAGIGAAQALGVAHTGIRTGAAADLIELDTAHPALL ARSDDALLDSWLFAARATAVRNVWRGGRWVVRNGQHVDRARIATRFAAVL RSLLGQ

Domain decomposition

XFF4834R_chr23890 lcl|XFF4834R_chr26060767_2756116_r3_XFF4834R-XFF4834R_chr23890

209

307

S=96 I=28 E=5.27796e-05

NP_641971.1 lcl|sdeB-XAC1639

456

S=1912 I=84 E=0

N-formimino-L-glutamate deiminase

YP_363411.1 lcl|XCV1680

456

S=1886 I=81 E=0

N-formimino-L-glutamate deiminase

NP_636952.2 lcl|sdeB-XCC1580

454

S=1635 I=73 E=0

N-formimino-L-glutamate deiminase

lcl|XALc_1715

454

S=1414 I=63 E=4.48542e-164

putative metalo_dependent_hydrolase protein

lcl|XALc_1920

209

307

S=102 I=29 E=3.69515e-05

hypothetical n-ethylammeline chlorohydrolase protein

NP_637625.1 lcl|XCC2270

209

307

S=101 I=29 E=5.10191e-05

N-ethylammeline chlorohydrolase

[G3DSA:3.20.20.140]

378

448

Formiminoglutamate deiminase

[PTHR11271]

448

IPR006680 [PF01979]

390

Amidohydrolase 1

IPR010252 [TIGR02022]

455

Formiminoglutamate deiminase

310

321

364

377

398

412

420

434

[SignalP-NN(euk)]

[SSF51556]

379

IPR011059 [SSF51338]

358

455

Metal-dependent hydrolase, composite domain

O31196 sp|O31196|HUTI_RHIME

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ID
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EC
GO
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	Your email
	Validation code (copy this one NTK8FwAA)

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	Set of Uniprot with relevant PubMed cross-references ncbi-blastp	2 hits
	Swiss-Prot ncbi-blastp	7 hits
	Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp	1 hits
	HAMAP scan	0 hits
	IprScan	12 hits

Miscellaneous analyses

ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBnyQIt7/XFF4834R_chr28680.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBnyQIt7/XFF4834R_chr28680.xml_fasta", "blastp"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBnyQIt7/XFF4834R_chr28680.xml_fasta"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBnyQIt7/XFF4834R_chr28680.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

hutI XFF4834R_chr28690

ID	hutI
AC	XFF4834R_chr28690
LT	XFF4834R_chr28690
OR	XFF4834R_chr from 3302022 to 3303227 on strand +
DE	probable imidazolonepropionase
IP	Imidazolonepropionase; D-hydantoinase
CL	1.1.3.11 Histidine degradation GO:0006548
EC	3.5.2.7
GO	InterPro Biological Process: histidine catabolic process to glutamate and formamide (GO:0019556) Cellular Component: cytoplasm (GO:0005737) Molecular Function: hydrolase activity (GO:0016787) acting on carbon-nitrogen (but not peptide) bonds (GO:0016810) in cyclic amides (GO:0016812) Curated : (GO:0050480)
PM
AN
CC	COG: [Q] Secondary metabolites biosynthesis, transport and catabolism;
CC	MODEL: XFF4834R
CC	STATUS: curated by darrasse (20120404)
MW	42483.1 Da
SQ	401 aa
	........10........20........30........40........50 \| \| \| \| \| MHCDVLWHNAQLMTLDAAAGGLGIVDDGIVACRHGHIVYAGAAAQAPALQ PDSAHDCQRRWISPGLIDCHTHLVYAGNRANEFEQRLRGASYADIAAAGG GIVATVRATRAADDAALLAASLPRLDAMLAEGVTTLEIKSGYGLTLDDEI KQLRVARQLAALRNVEVVPTFLGAHAVPPGGQAQHYIDQVCTQMIPAIAA QGLAEAVDVFCEHLAFSQAQAEQVFIAAQAHGLRIKIHAEQLSNQHGAEL AARYGALSADHIEYLDQAGVAAMATAGTVAVLLPGAFYFTRDTQLPPIAA LRTAGVPLALATDCNPGTSPLTSPLLAMNMAATLFRMTVDECIAGFTREA ARALGRSERLGQLRAGMDCDLAIWNIDAPADLVYRMGFNPLHARVWRGHL C

YP_363410.2 lcl|hutI-XCV1679

401

S=1708 I=83 E=0

imidazolonepropionase

NP_641970.2 lcl|hutI-XAC1638

401

S=1686 I=83 E=0

imidazolonepropionase

NP_636951.2 lcl|hutI-XCC1581

401

S=1563 I=76 E=0

imidazolonepropionase

lcl|hutI-XALc_1716

399

S=1356 I=68 E=4.22115e-157

probable imidazolonepropionase (imidazolone-5-propionatehydrolase) protein

399

S=947 I=50 E=6.38731e-106

Imidazolonepropionase EC=3.5.2.7 ; Cytoplasm Histidine metabolism Hydrolase Iron Metal-binding Plasmid Zinc

Pubmed 11481431

prodomImg

Q9KWE5 sp|Q9KWE5|HUTI_AGRRH

399

S=911 I=47 E=1.15173e-101

Imidazolonepropionase EC=3.5.2.7 ; Cytoplasm Histidine metabolism Hydrolase Iron Metal-binding Plasmid Zinc

Pubmed 10907845,11273700

prodomImg

A8KCI5 sp|A8KCI5|A8KCI5_9BURK

397

S=849 I=47 E=4.23435e-94

Imidazolonepropionase EC=3.5.2.7 ; Histidine metabolism Hydrolase Iron Metal-binding Zinc

Pubmed 17564599

prodomImg

P42084 sp|P42084|HUTI_BACSU

Q7BK24 sp|Q7BK24|Q7BK24_9RHIZ

S=520 I=32 E=2.9403e-54

Imidazolonepropionase EC=3.5.2.7 ; Cytoplasm Histidine metabolism Hydrolase Iron Metal-binding Zinc

Pubmed 7704263

prodomImg

396

S=511 I=36 E=3.49751e-53

HutI ; Histidine metabolism Hydrolase Iron Metal-binding Zinc

Pubmed 11133460,15240299

prodomImg

A6H0H4 sp|A6H0H4|HUTI_FLAPJ

389

S=465 I=33 E=1.33373e-47

Imidazolonepropionase EC=3.5.2.7 ; Cytoplasm Histidine metabolism Hydrolase Iron Metal-binding Zinc

Pubmed 17592475

prodomImg

B2RLA8 sp|B2RLA8|HUTI_PORG3

400

S=463 I=32 E=2.70256e-47

Imidazolonepropionase EC=3.5.2.7 ; Cytoplasm Histidine metabolism Hydrolase Iron Metal-binding Zinc

Pubmed 18524787

prodomImg

A0LZE0 sp|A0LZE0|HUTI_GRAFK

A7RX26 sp|A7RX26|HUTI_NEMVE

S=439 I=32 E=1.75852e-44

Imidazolonepropionase EC=3.5.2.7 ; Cytoplasm Histidine metabolism Hydrolase Iron Metal-binding Zinc

Pubmed 17107561

prodomImg

387

S=436 I=33 E=4.35456e-44

Probable imidazolonepropionase EC=3.5.2.7 ; Histidine metabolism Hydrolase Iron Metal-binding Zinc

Pubmed 17615350

prodomImg

P42358 sp|P42358|HUTI_STRGN

125

400

S=385 I=33 E=7.37472e-38

Probable imidazolonepropionase EC=3.5.2.7 ; Cytoplasm Histidine metabolism Hydrolase Iron Metal-binding Zinc

Pubmed 7927711

prodomImg

Q3BV03 sp|Q3BV03|HUTI_XANC5

Q8PLZ7 sp|Q8PLZ7|HUTI_XANAC

S=1708 I=83 E=0

Imidazolonepropionase EC=3.5.2.7 ; Cytoplasm Histidine metabolism Hydrolase Iron Metal-binding Zinc

prodomImg

Q5H071 sp|Q5H071|HUTI_XANOR

S=1686 I=83 E=0

Imidazolonepropionase EC=3.5.2.7 ; Cytoplasm Histidine metabolism Hydrolase Iron Metal-binding Zinc

prodomImg

B2SJI1 sp|B2SJI1|HUTI_XANOP

S=1645 I=80 E=0

Imidazolonepropionase EC=3.5.2.7 ; Cytoplasm Histidine metabolism Hydrolase Iron Metal-binding Zinc

prodomImg

Q2P345 sp|Q2P345|HUTI_XANOM

S=1641 I=80 E=0

Imidazolonepropionase EC=3.5.2.7 ; Cytoplasm Histidine metabolism Hydrolase Iron Metal-binding Zinc

prodomImg

S=1641 I=80 E=0

Imidazolonepropionase EC=3.5.2.7 ; Cytoplasm Histidine metabolism Hydrolase Iron Metal-binding Zinc

prodomImg

[G3DSA:3.20.20.140]

358

IPR005920 [MF_00372]

401

Imidazolonepropionase

[PTHR22642]

398

IPR006680 [PF01979]

375

Amidohydrolase 1

IPR005920 [TIGR01224]

400

Imidazolonepropionase

120

268

281

PD014595

128

212

S=277 I=63 E=4.16022e-26

PD690291

210

289

S=210 I=56 E=5.36796e-18

PD891632

293

364

S=196 I=56 E=2.88564e-16

PDA0Q5L3

S=130 I=83 E=2.42883e-08

[SSF51556]

359

IPR011059 [SSF51338]

401

Metal-dependent hydrolase, composite domain

B4RED8 sp|B4RED8|HUTH_PHEZH

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ID
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Access unfiltered results

	Set of Uniprot with relevant PubMed cross-references ncbi-blastp	22 hits
	Swiss-Prot ncbi-blastp	257 hits
	Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp	1 hits
	HAMAP scan	0 hits
	IprScan	10 hits

Miscellaneous analyses

ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBnyQIt7/XFF4834R_chr28690.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBnyQIt7/XFF4834R_chr28690.xml_fasta", "blastp"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBnyQIt7/XFF4834R_chr28690.xml_fasta"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBnyQIt7/XFF4834R_chr28690.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

hutH XFF4834R_chr28700

ID	hutH
AC	XFF4834R_chr28700
LT	XFF4834R_chr28700
OR	XFF4834R_chr from 3303241 to 3304782 on strand +
DE	probable histidine ammonia-lyase
IP	Phenylalanine/histidine ammonia-lyase; Histidine ammonia-lyase; L-Aspartase-like
CL	1.1.3.11 Histidine degradation GO:0006548
EC
GO	InterPro Biological Process: biosynthetic process (GO:0009058) Biological Process: histidine catabolic process (GO:0006548) Cellular Component: cytoplasm (GO:0005737) Molecular Function: catalytic activity (GO:0003824) Molecular Function: histidine ammonia-lyase activity (GO:0004397) Molecular Function: ammonia ligase activity (GO:0016211) Curated
PM
AN
CC	COG: [E] Amino acid transport and metabolism;
CC	MODEL: XFF4834R
CC	STATUS: curated by darrasse (20120404)
MW	53202.5 Da
SQ	513 aa
	........10........20........30........40........50 \| \| \| \| \| MSVSVVLQPGQVTLAQWRALYRGAEVALDDACAAAVLRSAQTVEAIVARG EPVYGVNTGFGKLASVRIEREDLQALQRNIVLSHAAGVGEPTPVPVVRLM MALKLTSLAQGASGVQPDTLALLDAMLRAGITPVVPCQGSVGASGDLAPL SHLAAVMIGVGEAFVGAQRLPAADALAHAQLQPRVLGAKEGLALLNGTQF STACALAGLFEIETILQAALVTGALSVEAAKGSDTPFDARIHALRGQPGQ IATAAALRALMADSAIRESHRLGDVRVQDPYCLRCQPQVMGAALDVMRQA ARTLEIEANGVSDNPLVFSDTSEALSGGNFHAEPVAFAADMLAMAVCEIG SISERRTAMLVDPALSGLPAFLTPRPGLNSGFMIPQVTAAALVSENKQRA YPASVDSIPTSANQEDHVSMAAHGARRLLAMAENAAHVIGIELLAAVQGC DFHAPLRSSTALEAARALLRAQVPTLQDDRYFHPDMLVASALVRSGALAQ AVAVPLPGVEQDV

499

S=1633 I=68 E=0

Histidine ammonia-lyase EC=4.3.1.3 ; Cytoplasm metabolism

Pubmed 18700039

prodomImg

Q9KWE4 sp|Q9KWE4|HUTH_AGRRH

503

S=1400 I=57 E=1.07455e-160

Histidine ammonia-lyase EC=4.3.1.3 ; Cytoplasm metabolism Plasmid

Pubmed 10907845,11273700

prodomImg

O31197 sp|O31197|HUTH_RHIME

511

S=1386 I=56 E=4.72682e-159

Histidine ammonia-lyase EC=4.3.1.3 ; Cytoplasm metabolism Plasmid

Pubmed 11481431

prodomImg

A8KCI3 sp|A8KCI3|A8KCI3_9BURK

507

S=1246 I=58 E=4.701e-142

Histidine ammonia-lyase EC=4.3.1.3 ; metabolism

Pubmed 17564599

prodomImg

P21310 sp|P21310|HUTH_PSEPU

498

S=1174 I=51 E=2.09203e-133

Histidine ammonia-lyase EC=4.3.1.3 ; Cytoplasm metabolism

Pubmed 2332400,8239649

prodomImg

Q9APT1 sp|Q9APT1|Q9APT1_9BACT

498

S=1130 I=54 E=4.5264e-128

Histidine ammonia-lyase EC=4.3.1.3 ; metabolism

Pubmed 11133432

prodomImg

Q93TX3 sp|Q93TX3|HUTH_STIAU

502

S=1064 I=49 E=4.41854e-120

Histidine ammonia-lyase EC=4.3.1.3 ; Cytoplasm metabolism

Pubmed 11182319

prodomImg

P10944 sp|P10944|HUTH_BACSU

486

S=975 I=45 E=2.98321e-109

Histidine ammonia-lyase EC=4.3.1.3 ; Cytoplasm metabolism

Pubmed 2454913,7704263

prodomImg

A9GFW6 sp|A9GFW6|HUTH_SORC5

502

S=897 I=49 E=8.28375e-100

Histidine ammonia-lyase EC=4.3.1.3 ; Cytoplasm metabolism

Pubmed 17965706

prodomImg

Q848M8 sp|Q848M8|Q848M8_9BACT

146

502

S=870 I=52 E=1.77972e-96

HutH ; Histidine metabolism Lyase Plasmid

Pubmed 12620823

prodomImg

Q8PLZ8 sp|Q8PLZ8|HUTH_XANAC

513

S=2367 I=90 E=0

Histidine ammonia-lyase EC=4.3.1.3 ; Cytoplasm metabolism

prodomImg

Q8PAA7 sp|Q8PAA7|HUTH_XANCP

B0RUX3 sp|B0RUX3|HUTH_XANCB

S=2277 I=88 E=0

Histidine ammonia-lyase EC=4.3.1.3 ; Cytoplasm metabolism

prodomImg

Q4UTB9 sp|Q4UTB9|HUTH_XANC8

S=2277 I=88 E=0

Histidine ammonia-lyase EC=4.3.1.3 ; Cytoplasm metabolism

prodomImg

B0SYU6 sp|B0SYU6|HUTH_CAUSK

S=2277 I=88 E=0

Histidine ammonia-lyase EC=4.3.1.3 ; Cytoplasm metabolism

prodomImg

S=1855 I=72 E=0

Histidine ammonia-lyase EC=4.3.1.3 ; Cytoplasm metabolism

prodomImg

[G3DSA:1.10.275.10]

197

[G3DSA:1.20.200.10]

198

510

IPR001106 [PF00221]

477

Phenylalanine/histidine ammonia-lyase

IPR005921 [TIGR01225]

506

Histidine ammonia-lyase

252

265

456

471

PD001290

498

S=1098 I=51 E=1.77021e-125

PD737272

452

510

S=177 I=63 E=8.09599e-14

PDA9Q8M1

317

S=132 I=21 E=2.01391e-08

IPR008948 [SSF48557]

510

L-Aspartase-like

Q9KWE3 sp|Q9KWE3|Q9KWE3_AGRRH

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ID
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GO
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Access unfiltered results

	Set of Uniprot with relevant PubMed cross-references ncbi-blastp	124 hits
	Swiss-Prot ncbi-blastp	234 hits
	Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp	1 hits
	HAMAP scan	0 hits
	IprScan	8 hits

Miscellaneous analyses

ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBnyQIt7/XFF4834R_chr28700.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBnyQIt7/XFF4834R_chr28700.xml_fasta", "blastp"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBnyQIt7/XFF4834R_chr28700.xml_fasta"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBnyQIt7/XFF4834R_chr28700.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

hutG XFF4834R_chr28710

ID	hutG
AC	XFF4834R_chr28710
LT	XFF4834R_chr28710
OR	XFF4834R_chr from 3304964 to 3305821 on strand +
DE	probable N-formylglutamate amidohydrolase HutG
IP	N-formylglutamate amidohydrolase; N-formylglutamate deformylase
CL	1.1.3.11 Histidine degradation GO:0006548
EC
GO	InterPro Curated
PM
AN	Interpro : In some species, histidine is converted to via urocanate and then formimino-L-glutamate to glutamate in four steps, where the fourth step is conversion of N-formimino-L-glutamate to L-glutamate and formamide. In others, that pathway from formimino-L-glutamate may differ, with the next enzyme being formiminoglutamate hydrolase (HutF) yielding N-formyl-L-glutamate. This entry represents the enzyme N-formylglutamate deformylase, also called N-formylglutamate amidohydrolase, which then produces glutamate.
CC	COG: [E] Amino acid transport and metabolism;
CC	MODEL: XFF4834R
CC	STATUS: curated by darrasse (20120404)
MW	31971.6 Da
SQ	285 aa
	........10........20........30........40........50 \| \| \| \| \| MNALPDWLELHRGDAPLIISFPHTGTELPEDLADQFVSPWLARRDTDWWV HQLYDFAQGLGATTLRTAISRSVIDVNRDPSGASLYPGQNTTGLCPLTTF DNQPLYADGAAPDQAQIALRRMRWFDPYHAALAEEIARLRAQHAKIVVYD AHSIRSFIPHLFDGQLPQFNIGSNEDRSCDRRLVDAVERLCRSSGSSTVR NGRFKGGWITRHYAQPEHGVHTLQMELACRGYMREPDSLTPDNWPTPWQP VHAVALRAVLRHVLQACLHFANAPSSDTAPPAANR

YP_363408.1 lcl|hutG-XCV1677

285

S=1403 I=92 E=4.79059e-163

N-formylglutamate amidohydrolase

NP_641968.1 lcl|hutG-XAC1636

285

S=1395 I=92 E=5.26839e-162

formylglutamate amidohydrolase

NP_636949.1 lcl|hutG-XCC1578

285

S=1145 I=76 E=9.21497e-132

formylglutamate amidohydrolase

lcl|hutG-XALc_1718

280

S=1010 I=67 E=2.15553e-115

probable n-formylglutamate_deformylase protein

264

S=542 I=44 E=3.86189e-57

Riorf41 protein ; Plasmid

Pubmed 10907845,11273700

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IPR007709 [PF05013]

233

N-formylglutamate amidohydrolase

IPR010247 [TIGR02017]

273

N-formylglutamate deformylase

130

141

PD117136

235

S=324 I=37 E=9.89405e-32

PDA92322

236

285

S=250 I=96 E=8.61613e-23

PDA9C6Y4

129

S=142 I=31 E=1.14641e-09

PDA1G6N3

162

208

S=141 I=56 E=1.47621e-09

PD123728

208

273

S=131 I=47 E=1.91593e-08

PD463862

S=126 I=60 E=8.58339e-08

B4REE0 sp|B4REE0|HUTU_PHEZH

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ID
DE
EC
GO
PM
CC
CL
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	Validation code (copy this one 7OXSPNhe)

Access unfiltered results

	Set of Uniprot with relevant PubMed cross-references ncbi-blastp	1 hits
	Swiss-Prot ncbi-blastp	0 hits
	Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp	1 hits
	HAMAP scan	0 hits
	IprScan	3 hits

Miscellaneous analyses

ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBnyQIt7/XFF4834R_chr28710.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBnyQIt7/XFF4834R_chr28710.xml_fasta", "blastp"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBnyQIt7/XFF4834R_chr28710.xml_fasta"\) - 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\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBnyQIt7/XFF4834R_chr28710.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

hutU XFF4834R_chr28720

ID	hutU
AC	XFF4834R_chr28720
LT	XFF4834R_chr28720
OR	XFF4834R_chr from 3305838 to 3307505 on strand +
DE	probable urocanate hydratase HutU
IP	Urocanase
CL	1.1.3.11 Histidine degradation GO:0006548
EC
GO	InterPro Biological Process: histidine catabolic process (GO:0006548) Molecular Function: urocanate hydratase activity (GO:0016153) Curated
PM
AN	Interpro : Urocanase [1] (also known as imidazolonepropionate hydrolase or urocanate hydratase) is the enzyme that catalyzes the second step in the degradation of histidine, the hydration of urocanate into imidazolonepropionate. urocanate + H2O = 4,5-dihydro-4-oxo-5-imidazolepropanoate Urocanase is found in some bacteria (gene hutU), in the liver of many vertebrates and has also been found in the plant Trifolium repens (white clover). Urocanase is a protein of about 60 Kd, it binds tightly to NAD+ and uses it as an electrophil cofactor. A conserved cysteine has been found to be important for the catalytic mechanism and could be involved in the binding of the NAD+.
CC	COG: [E] Amino acid transport and metabolism;
CC	MODEL: acur
CC	STATUS: curated by darrasse (20120404)
MW	60054.8 Da
SQ	555 aa
	........10........20........30........40........50 \| \| \| \| \| MTRHDATRVIRAATGTTLTAKSWLTEAPLRMLMNNLDPDVAERPQELVVY GGIGRAARDWESFDAIVAALTRLDEDQTLLVQSGKPVGVFRTHADAPRVL IANSNLVPRWANWDHFNALDKKGLAMYGQMTAGSWIYIGAQGIVQGTYET FVEMGRQHYAGNLAGKWLFTGGLGGMGGAQPLAAVMAGASCLAVECRRSS IDMRLRTGYLDTWTDSLDDALRLIEESCTARKPLSVGLLGNVADVLDELL LRGIKPDLLTDQTSAHDPVNGYLPQGWSVEEWDAKRMSAPKEVEAAARDS MANHIRAMLAFHALGVPTVDYGNNLRQMALEAGVDDAFDFPGFVPAYIRP LFCRGIGPFRWVALSGDPDDIAKTDAKVKELIPDDAHLHRWLDMAAEKIA FQGLPARICWVGLGDRHRLGLAFNAMVRSGELKAPVVIGRDHLDSGSVAS PNRETEAMADGSDAVSDWPLLNALLNTASGATWVSLHHGGGVGMGFSQHA GMVIVCDGSQAADRRLERVLWNDPATGVMRHADAGYAIATDCAKEKGLDL PGIVR

Domain decomposition

Q92V80 sp|Q92V80|HUTU_RHIME

S=2290 I=77 E=0

Urocanate hydratase EC=4.2.1.49 ; Cytoplasm Histidine metabolism Lyase NAD

Pubmed 18700039

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Q9KWE2 sp|Q9KWE2|Q9KWE2_AGRRH

S=2216 I=75 E=0

Urocanate hydratase EC=4.2.1.49 ; Cytoplasm Histidine metabolism Lyase NAD Plasmid

Pubmed 11481431

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P25080 sp|P25080|HUTU_PSEPU

S=2114 I=73 E=0

Riorf42 protein ; Histidine metabolism Lyase NAD Plasmid

Pubmed 10907845,11273700

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Q9AGU4 sp|Q9AGU4|HUTU_PSESX

S=2089 I=72 E=0

Urocanate hydratase EC=4.2.1.49 ; Cytoplasm Histidine metabolism Lyase NAD

Pubmed 1677899,7901006

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553

S=2064 I=70 E=0

Urocanate hydratase EC=4.2.1.49 ; Cytoplasm Histidine metabolism Lyase NAD Stress response

Pubmed 11772602

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P53385 sp|P53385|HUTU_TRIRP

A8KCI2 sp|A8KCI2|A8KCI2_9BURK

S=2037 I=70 E=0

Urocanate hydratase EC=4.2.1.49 ; Histidine metabolism Lyase NAD

Pubmed 1356832

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P67417 sp|P67417|HUTU_STAAN

S=1979 I=69 E=0

Urocanase EC=4.2.1.49 ; Histidine metabolism Lyase NAD

Pubmed 17564599

prodomImg

553

S=1771 I=59 E=0

Urocanate hydratase EC=4.2.1.49 ; Cytoplasm Histidine metabolism Lyase NAD

Pubmed 15590099

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P25503 sp|P25503|HUTU_BACSU

B7IF30 sp|B7IF30|HUTU_THEAB

S=1754 I=61 E=0

Urocanate hydratase EC=4.2.1.49 ; Cytoplasm Histidine metabolism Lyase NAD

Pubmed 7704263

prodomImg

P58987 sp|P58987|HUTU_XANAC

S=1719 I=58 E=0

Urocanate hydratase EC=4.2.1.49 ; Cytoplasm Histidine metabolism Lyase NAD

Pubmed 19124572

prodomImg

555

S=2738 I=94 E=0

Urocanate hydratase EC=4.2.1.49 ; Cytoplasm Histidine metabolism Lyase NAD

prodomImg

Q3BV06 sp|Q3BV06|HUTU_XANC5

555

S=2734 I=93 E=0

Urocanate hydratase EC=4.2.1.49 ; Cytoplasm Histidine metabolism Lyase NAD

prodomImg

P58988 sp|P58988|HUTU_XANCP

B4SP57 sp|B4SP57|HUTU_STRM5

S=2698 I=92 E=0

Urocanate hydratase EC=4.2.1.49 ; Cytoplasm Histidine metabolism Lyase NAD

prodomImg

B2FKG1 sp|B2FKG1|HUTU_STRMK

S=2523 I=86 E=0

Urocanate hydratase EC=4.2.1.49 ; Cytoplasm Histidine metabolism Lyase NAD

prodomImg

S=2522 I=86 E=0

Urocanate hydratase EC=4.2.1.49 ; Cytoplasm Histidine metabolism Lyase NAD

prodomImg

IPR000193 [PIRSF001423]

555

Urocanase

IPR000193 [PF01175]

552

Urocanase

IPR000193 [TIGR01228]

552

Urocanase

164

184

PD025423

551

S=1961 I=67 E=0

IPR000193 [SSF111326]

555

Urocanase