6 hits
XFF4834R_chr09160 | XFF4834R_chr09750254_1056039_r1_XFF4834R-XFF4834R_chr09160 | XFF4834R_chr09160 | putative N-formylglutamate amidohydrolase |
XFF4834R_chr28680 | XFF4834R_chr31230591_3301961_r2_XFF4834R-XFF4834R_chr28680 | XFF4834R_chr28680 | putative N-formimino-L-glutamate deiminase |
XFF4834R_chr28690 | hutI | XFF4834R_chr28690 | probable imidazolonepropionase |
XFF4834R_chr28700 | hutH | XFF4834R_chr28700 | probable histidine ammonia-lyase |
XFF4834R_chr28710 | hutG | XFF4834R_chr28710 | probable N-formylglutamate amidohydrolase HutG |
XFF4834R_chr28720 | hutU | XFF4834R_chr28720 | probable urocanate hydratase HutU |
![]() XFF4834R_chr09150 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
![]() |
![]() |
![]() XFF4834R_chr09170 |
ID | XFF4834R_chr09750254_1056039_r1_XFF4834R-XFF4834R_chr09160 |
AC | XFF4834R_chr09160 |
LT | XFF4834R_chr09160 |
OR | XFF4834R_chr from 1055254 to 1056039 on strand - |
DE | putative N-formylglutamate amidohydrolase |
IP | N-formylglutamate amidohydrolase; Uncharacterized conserved protein UCP029730 |
CL | 1.1.3.11 Histidine degradation GO:0006548 |
EC | |
GO |
InterPro Curated
|
PM | |
AN | |
CC | COG: [E] Amino acid transport and metabolism; |
CC | MODEL: XFF4834R |
CC | STATUS: curated by darrasse (20120329) |
MW | 28593.1 Da |
SQ | 261 aa |
........10........20........30........40........50 |
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YP_362677.1 lcl|XCV0946 |
1 |
234 |
S=1153 I=95 E=1.00681e-132 |
putative N-formylglutamate amidohydrolase |
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NP_641262.1 lcl|XAC0910-XAC0910 |
20 |
234 |
S=1097 I=98 E=6.03659e-126 |
hypothetical protein |
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NP_636228.1 lcl|XCC0837 |
8 |
234 |
S=1011 I=87 E=1.54844e-115 |
hypothetical protein |
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2 |
234 |
S=822 I=68 E=1.35621e-92 |
putative n-formylglutamate amidohydrolase protein |
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18 |
234 |
S=347 I=34 E=1.39699e-33 |
Riorf59 protein ; Plasmid |
||
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28 |
234 |
S=337 I=40 E=2.23513e-32 |
Orf3; putative |
Pubmed 9244287 |
|
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30 |
234 |
S=289 I=31 E=1.66791e-26 |
Putative uncharacterized protein ipuJ |
Pubmed 11976110 |
|
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IPR011227 [PIRSF029730] | 1 |
258 |
Uncharacterised conserved protein UCP029730 |
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IPR007709 [PF05013] | 26 |
236 |
N-formylglutamate amidohydrolase |
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[seg] | 235 |
261 |
- |
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30 |
233 |
S=294 I=41 E=3.88358e-28 |
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1 |
29 |
S=129 I=86 E=3.35105e-08 |
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8 |
29 |
S=103 I=86 E=5.64005e-05 |
Access unfiltered results
![]() |
Set of Uniprot with relevant PubMed cross-references ncbi-blastp |
3 hits |
![]() |
Swiss-Prot ncbi-blastp |
0 hits |
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Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp |
0 hits |
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HAMAP scan |
0 hits |
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IprScan |
3 hits |
Miscellaneous analyses
![]() XFF4834R_chr28670 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
![]() |
![]() |
![]() XFF4834R_chr28690 |
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 |
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XFF4834R_chr23890 lcl|XFF4834R_chr26060767_2756116_r3_XFF4834R-XFF4834R_chr23890 |
209 |
307 |
S=96 I=28 E=5.27796e-05 |
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NP_641971.1 lcl|sdeB-XAC1639 |
6 |
456 |
S=1912 I=84 E=0 |
N-formimino-L-glutamate deiminase |
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YP_363411.1 lcl|XCV1680 |
1 |
456 |
S=1886 I=81 E=0 |
N-formimino-L-glutamate deiminase |
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NP_636952.2 lcl|sdeB-XCC1580 |
6 |
454 |
S=1635 I=73 E=0 |
N-formimino-L-glutamate deiminase |
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9 |
454 |
S=1414 I=63 E=4.48542e-164 |
putative metalo_dependent_hydrolase protein |
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209 |
307 |
S=102 I=29 E=3.69515e-05 |
hypothetical n-ethylammeline chlorohydrolase protein |
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NP_637625.1 lcl|XCC2270 |
209 |
307 |
S=101 I=29 E=5.10191e-05 |
N-ethylammeline chlorohydrolase |
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[G3DSA:3.20.20.140] | 55 |
378 |
- |
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IPR010252 [PTHR11271:SF4] | 50 |
448 |
Formiminoglutamate deiminase |
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[PTHR11271] | 50 |
448 |
- |
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IPR006680 [PF01979] | 51 |
390 |
Amidohydrolase 1 |
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IPR010252 [TIGR02022] | 6 |
455 |
Formiminoglutamate deiminase |
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[seg] | 310 |
321 |
- |
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[seg] | 364 |
377 |
- |
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[seg] | 398 |
412 |
- |
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[seg] | 420 |
434 |
- |
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[SignalP-NN(euk)] | 1 |
21 |
- |
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[SSF51556] | 55 |
379 |
- |
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IPR011059 [SSF51338] | 358 |
455 |
Metal-dependent hydrolase, composite domain |
Access unfiltered results
![]() |
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 |
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IprScan |
12 hits |
Miscellaneous analyses
![]() XFF4834R_chr28680 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
![]() |
![]() |
![]() XFF4834R_chr28700 |
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 | |
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
|
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 |
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YP_363410.2 lcl|hutI-XCV1679 |
1 |
401 |
S=1708 I=83 E=0 |
imidazolonepropionase |
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NP_641970.2 lcl|hutI-XAC1638 |
1 |
401 |
S=1686 I=83 E=0 |
imidazolonepropionase |
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NP_636951.2 lcl|hutI-XCC1581 |
1 |
401 |
S=1563 I=76 E=0 |
imidazolonepropionase |
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1 |
399 |
S=1356 I=68 E=4.22115e-157 |
probable imidazolonepropionase (imidazolone-5-propionatehydrolase) protein |
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6 |
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 |
|
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6 |
399 |
S=911 I=47 E=1.15173e-101 |
Imidazolonepropionase EC=3.5.2.7 ; Cytoplasm Histidine metabolism Hydrolase Iron Metal-binding Plasmid Zinc |
||
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1 |
397 |
S=849 I=47 E=4.23435e-94 |
Imidazolonepropionase EC=3.5.2.7 ; Histidine metabolism Hydrolase Iron Metal-binding Zinc |
Pubmed 17564599 |
|
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5 |
401 |
S=520 I=32 E=2.9403e-54 |
Imidazolonepropionase EC=3.5.2.7 ; Cytoplasm Histidine metabolism Hydrolase Iron Metal-binding Zinc |
Pubmed 7704263 |
|
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60 |
396 |
S=511 I=36 E=3.49751e-53 |
HutI ; Histidine metabolism Hydrolase Iron Metal-binding Zinc |
||
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56 |
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 |
|
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56 |
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 |
|
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56 |
401 |
S=439 I=32 E=1.75852e-44 |
Imidazolonepropionase EC=3.5.2.7 ; Cytoplasm Histidine metabolism Hydrolase Iron Metal-binding Zinc |
Pubmed 17107561 |
|
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56 |
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 |
|
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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 |
|
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1 |
401 |
S=1708 I=83 E=0 |
Imidazolonepropionase EC=3.5.2.7 ; Cytoplasm Histidine metabolism Hydrolase Iron Metal-binding Zinc |
||
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1 |
401 |
S=1686 I=83 E=0 |
Imidazolonepropionase EC=3.5.2.7 ; Cytoplasm Histidine metabolism Hydrolase Iron Metal-binding Zinc |
||
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1 |
401 |
S=1645 I=80 E=0 |
Imidazolonepropionase EC=3.5.2.7 ; Cytoplasm Histidine metabolism Hydrolase Iron Metal-binding Zinc |
||
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1 |
401 |
S=1641 I=80 E=0 |
Imidazolonepropionase EC=3.5.2.7 ; Cytoplasm Histidine metabolism Hydrolase Iron Metal-binding Zinc |
||
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1 |
401 |
S=1641 I=80 E=0 |
Imidazolonepropionase EC=3.5.2.7 ; Cytoplasm Histidine metabolism Hydrolase Iron Metal-binding Zinc |
||
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[G3DSA:3.20.20.140] | 65 |
358 |
- |
![]() |
IPR005920 [MF_00372] | 4 |
401 |
Imidazolonepropionase |
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[PTHR22642] | 24 |
398 |
- |
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IPR006680 [PF01979] | 62 |
375 |
Amidohydrolase 1 |
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IPR005920 [TIGR01224] | 25 |
400 |
Imidazolonepropionase |
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[seg] | 40 |
54 |
- |
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[seg] | 88 |
120 |
- |
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[seg] | 268 |
281 |
- |
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128 |
212 |
S=277 I=63 E=4.16022e-26 |
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210 |
289 |
S=210 I=56 E=5.36796e-18 |
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293 |
364 |
S=196 I=56 E=2.88564e-16 |
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1 |
29 |
S=130 I=83 E=2.42883e-08 |
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[SSF51556] | 65 |
359 |
- |
![]() |
IPR011059 [SSF51338] | 1 |
401 |
Metal-dependent hydrolase, composite domain |
Access unfiltered results
Miscellaneous analyses
![]() XFF4834R_chr28690 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
![]() |
![]() |
![]() XFF4834R_chr_3028 |
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: histidine catabolic process (GO:0006548) Biological Process: biosynthetic process (GO:0009058) Cellular Component: cytoplasm (GO:0005737) Molecular Function: ammonia ligase activity (GO:0016211) Molecular Function: histidine ammonia-lyase activity (GO:0004397) Molecular Function: catalytic activity (GO:0003824) 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 |
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3 |
499 |
S=1633 I=68 E=0 |
Histidine ammonia-lyase EC=4.3.1.3 ; Cytoplasm metabolism |
Pubmed 18700039 |
|
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3 |
503 |
S=1400 I=57 E=1.07455e-160 |
Histidine ammonia-lyase EC=4.3.1.3 ; Cytoplasm metabolism Plasmid |
||
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3 |
511 |
S=1386 I=56 E=4.72682e-159 |
Histidine ammonia-lyase EC=4.3.1.3 ; Cytoplasm metabolism Plasmid |
Pubmed 11481431 |
|
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39 |
507 |
S=1246 I=58 E=4.701e-142 |
Histidine ammonia-lyase EC=4.3.1.3 ; metabolism |
Pubmed 17564599 |
|
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5 |
498 |
S=1174 I=51 E=2.09203e-133 |
Histidine ammonia-lyase EC=4.3.1.3 ; Cytoplasm metabolism |
||
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39 |
498 |
S=1130 I=54 E=4.5264e-128 |
Histidine ammonia-lyase EC=4.3.1.3 ; metabolism |
Pubmed 11133432 |
|
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43 |
502 |
S=1064 I=49 E=4.41854e-120 |
Histidine ammonia-lyase EC=4.3.1.3 ; Cytoplasm metabolism |
Pubmed 11182319 |
|
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38 |
486 |
S=975 I=45 E=2.98321e-109 |
Histidine ammonia-lyase EC=4.3.1.3 ; Cytoplasm metabolism |
||
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53 |
502 |
S=897 I=49 E=8.28375e-100 |
Histidine ammonia-lyase EC=4.3.1.3 ; Cytoplasm metabolism |
Pubmed 17965706 |
|
![]() |
146 |
502 |
S=870 I=52 E=1.77972e-96 |
HutH ; Histidine metabolism Lyase Plasmid |
Pubmed 12620823 |
|
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1 |
513 |
S=2367 I=90 E=0 |
Histidine ammonia-lyase EC=4.3.1.3 ; Cytoplasm metabolism |
||
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1 |
510 |
S=2277 I=88 E=0 |
Histidine ammonia-lyase EC=4.3.1.3 ; Cytoplasm metabolism |
||
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1 |
510 |
S=2277 I=88 E=0 |
Histidine ammonia-lyase EC=4.3.1.3 ; Cytoplasm metabolism |
||
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1 |
510 |
S=2277 I=88 E=0 |
Histidine ammonia-lyase EC=4.3.1.3 ; Cytoplasm metabolism |
||
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3 |
510 |
S=1855 I=72 E=0 |
Histidine ammonia-lyase EC=4.3.1.3 ; Cytoplasm metabolism |
||
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[G3DSA:1.10.275.10] | 3 |
197 |
- |
![]() |
[G3DSA:1.20.200.10] | 198 |
510 |
- |
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IPR001106 [PF00221] | 5 |
477 |
Phenylalanine/histidine ammonia-lyase |
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IPR005921 [TIGR01225] | 5 |
506 |
Histidine ammonia-lyase |
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[seg] | 24 |
37 |
- |
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[seg] | 252 |
265 |
- |
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[seg] | 456 |
471 |
- |
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39 |
498 |
S=1098 I=51 E=1.77021e-125 |
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452 |
510 |
S=177 I=63 E=8.09599e-14 |
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98 |
317 |
S=132 I=21 E=2.01391e-08 |
![]() |
IPR008948 [SSF48557] | 3 |
510 |
L-Aspartase-like |
Access unfiltered results
Miscellaneous analyses
![]() XFF4834R_chr_3028 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
![]() |
![]() |
![]() XFF4834R_chr28720 |
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 |
![]() |
YP_363408.1 lcl|hutG-XCV1677 |
1 |
285 |
S=1403 I=92 E=4.79059e-163 |
N-formylglutamate amidohydrolase |
![]() |
NP_641968.1 lcl|hutG-XAC1636 |
1 |
285 |
S=1395 I=92 E=5.26839e-162 |
formylglutamate amidohydrolase |
![]() |
NP_636949.1 lcl|hutG-XCC1578 |
1 |
285 |
S=1145 I=76 E=9.21497e-132 |
formylglutamate amidohydrolase |
![]() |
1 |
280 |
S=1010 I=67 E=2.15553e-115 |
probable n-formylglutamate_deformylase protein |
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9 |
264 |
S=542 I=44 E=3.86189e-57 |
Riorf41 protein ; Plasmid |
||
![]() |
IPR007709 [PF05013] | 15 |
233 |
N-formylglutamate amidohydrolase |
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IPR010247 [TIGR02017] | 6 |
273 |
N-formylglutamate deformylase |
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[seg] | 130 |
141 |
- |
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17 |
235 |
S=324 I=37 E=9.89405e-32 |
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236 |
285 |
S=250 I=96 E=8.61613e-23 |
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16 |
129 |
S=142 I=31 E=1.14641e-09 |
![]() |
162 |
208 |
S=141 I=56 E=1.47621e-09 |
![]() |
208 |
273 |
S=131 I=47 E=1.91593e-08 |
![]() |
10 |
51 |
S=126 I=60 E=8.58339e-08 |
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
![]() XFF4834R_chr28710 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
![]() |
![]() |
![]() XFF4834R_chr28730 |
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 |
![]() |
1 |
554 |
S=2290 I=77 E=0 |
Urocanate hydratase EC=4.2.1.49 ; Cytoplasm Histidine metabolism Lyase NAD |
Pubmed 18700039 |
|
![]() |
3 |
554 |
S=2216 I=75 E=0 |
Urocanate hydratase EC=4.2.1.49 ; Cytoplasm Histidine metabolism Lyase NAD Plasmid |
Pubmed 11481431 |
|
![]() |
3 |
554 |
S=2114 I=73 E=0 |
Riorf42 protein ; Histidine metabolism Lyase NAD Plasmid |
||
![]() |
10 |
554 |
S=2089 I=72 E=0 |
Urocanate hydratase EC=4.2.1.49 ; Cytoplasm Histidine metabolism Lyase NAD |
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1 |
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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8 |
551 |
S=2037 I=70 E=0 |
Urocanate hydratase EC=4.2.1.49 ; Histidine metabolism Lyase NAD |
Pubmed 1356832 |
|
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6 |
551 |
S=1979 I=69 E=0 |
Urocanase EC=4.2.1.49 ; Histidine metabolism Lyase NAD |
Pubmed 17564599 |
|
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8 |
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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5 |
551 |
S=1754 I=61 E=0 |
Urocanate hydratase EC=4.2.1.49 ; Cytoplasm Histidine metabolism Lyase NAD |
Pubmed 7704263 |
|
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8 |
551 |
S=1719 I=58 E=0 |
Urocanate hydratase EC=4.2.1.49 ; Cytoplasm Histidine metabolism Lyase NAD |
Pubmed 19124572 |
|
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1 |
555 |
S=2738 I=94 E=0 |
Urocanate hydratase EC=4.2.1.49 ; Cytoplasm Histidine metabolism Lyase NAD |
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1 |
555 |
S=2734 I=93 E=0 |
Urocanate hydratase EC=4.2.1.49 ; Cytoplasm Histidine metabolism Lyase NAD |
||
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1 |
554 |
S=2698 I=92 E=0 |
Urocanate hydratase EC=4.2.1.49 ; Cytoplasm Histidine metabolism Lyase NAD |
||
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1 |
554 |
S=2523 I=86 E=0 |
Urocanate hydratase EC=4.2.1.49 ; Cytoplasm Histidine metabolism Lyase NAD |
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1 |
554 |
S=2522 I=86 E=0 |
Urocanate hydratase EC=4.2.1.49 ; Cytoplasm Histidine metabolism Lyase NAD |
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IPR000193 [PIRSF001423] | 6 |
555 |
Urocanase |
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IPR000193 [PF01175] | 10 |
552 |
Urocanase |
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IPR000193 [TIGR01228] | 8 |
552 |
Urocanase |
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[seg] | 164 |
184 |
- |
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10 |
551 |
S=1961 I=67 E=0 |
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IPR000193 [SSF111326] | 2 |
555 |
Urocanase |
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