(data stored in ACNUC7421 zone)

SWISSPROT: A0KF86_AERHH

ID   A0KF86_AERHH            Unreviewed;       569 AA.
AC   A0KF86;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   11-DEC-2019, entry version 101.
DE   RecName: Full=Urocanate hydratase {ECO:0000256|HAMAP-Rule:MF_00577, ECO:0000256|SAAS:SAAS00693702};
DE            Short=Urocanase {ECO:0000256|HAMAP-Rule:MF_00577};
DE            EC=4.2.1.49 {ECO:0000256|HAMAP-Rule:MF_00577, ECO:0000256|SAAS:SAAS00693702};
DE   AltName: Full=Imidazolonepropionate hydrolase {ECO:0000256|HAMAP-Rule:MF_00577};
GN   Name=hutU {ECO:0000256|HAMAP-Rule:MF_00577,
GN   ECO:0000313|EMBL:ABK37402.1};
GN   OrderedLocusNames=AHA_0379 {ECO:0000313|EMBL:ABK37402.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / JCM
OS   1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK37402.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK37402.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.,
RA   Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA   Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- FUNCTION: Catalyzes the conversion of urocanate to 4-imidazolone-5-
CC       propionate. {ECO:0000256|HAMAP-Rule:MF_00577}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-imidazolone-5-propanoate = H2O + trans-urocanate;
CC         Xref=Rhea:RHEA:13101, ChEBI:CHEBI:15377, ChEBI:CHEBI:17771,
CC         ChEBI:CHEBI:77893; EC=4.2.1.49; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00577, ECO:0000256|SAAS:SAAS01115074};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00577};
CC       Note=Binds 1 NAD(+) per subunit. {ECO:0000256|HAMAP-Rule:MF_00577};
CC   -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC       glutamate; N-formimidoyl-L-glutamate from L-histidine: step 2/3.
CC       {ECO:0000256|HAMAP-Rule:MF_00577, ECO:0000256|SAAS:SAAS00693692}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00577}.
CC   -!- SIMILARITY: Belongs to the urocanase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00577, ECO:0000256|SAAS:SAAS00693689}.
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DR   EMBL; CP000462; ABK37402.1; -; Genomic_DNA.
DR   RefSeq; WP_011704355.1; NC_008570.1.
DR   RefSeq; YP_854908.1; NC_008570.1.
DR   STRING; 380703.AHA_0379; -.
DR   EnsemblBacteria; ABK37402; ABK37402; AHA_0379.
DR   GeneID; 4486963; -.
DR   KEGG; aha:AHA_0379; -.
DR   PATRIC; fig|380703.7.peg.366; -.
DR   eggNOG; ENOG4105CGP; Bacteria.
DR   eggNOG; COG2987; LUCA.
DR   HOGENOM; HOG000237606; -.
DR   KO; K01712; -.
DR   OMA; AVQVKAM; -.
DR   BioCyc; AHYD380703:G1G7B-380-MONOMER; -.
DR   UniPathway; UPA00379; UER00550.
DR   Proteomes; UP000000756; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016153; F:urocanate hydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019556; P:histidine catabolic process to glutamate and formamide; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019557; P:histidine catabolic process to glutamate and formate; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.10730; -; 1.
DR   HAMAP; MF_00577; HutU; 1.
DR   InterPro; IPR023637; Urocanase.
DR   InterPro; IPR035401; Urocanase_C.
DR   InterPro; IPR038364; Urocanase_central_sf.
DR   InterPro; IPR023636; Urocanase_CS.
DR   InterPro; IPR035400; Urocanase_N.
DR   InterPro; IPR035085; Urocanase_Rossmann-like.
DR   InterPro; IPR036190; Urocanase_sf.
DR   PANTHER; PTHR12216; PTHR12216; 1.
DR   Pfam; PF01175; Urocanase; 1.
DR   Pfam; PF17392; Urocanase_C; 1.
DR   Pfam; PF17391; Urocanase_N; 1.
DR   PIRSF; PIRSF001423; Urocanate_hydrat; 1.
DR   SUPFAM; SSF111326; SSF111326; 1.
DR   TIGRFAMs; TIGR01228; hutU; 1.
DR   PROSITE; PS01233; UROCANASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0KF86.
DR   SWISS-2DPAGE; A0KF86.
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00577};
KW   Histidine metabolism {ECO:0000256|HAMAP-Rule:MF_00577,
KW   ECO:0000256|SAAS:SAAS00693681};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00577, ECO:0000256|SAAS:SAAS00693676,
KW   ECO:0000313|EMBL:ABK37402.1};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00577, ECO:0000256|SAAS:SAAS00693683};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756}.
FT   DOMAIN          16..142
FT                   /note="Urocanase_N"
FT                   /evidence="ECO:0000259|Pfam:PF17391"
FT   DOMAIN          145..353
FT                   /note="Urocanase"
FT                   /evidence="ECO:0000259|Pfam:PF01175"
FT   DOMAIN          356..550
FT                   /note="Urocanase_C"
FT                   /evidence="ECO:0000259|Pfam:PF17392"
FT   NP_BIND         57..58
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT   NP_BIND         181..183
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT   NP_BIND         247..248
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT   NP_BIND         268..272
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT   NP_BIND         278..279
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        415
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT   BINDING         135
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT   BINDING         201
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT   BINDING         206
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT   BINDING         327
FT                   /note="NAD; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT   BINDING         497
FT                   /note="NAD; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
SQ   SEQUENCE   569 AA;  62076 MW;  85EF6D00AA2060C1 CRC64;
     MSQQHQDPRH DPNRVIRAPR GTTLTAKSWL TEAPLRMLMN NLDPEVAEHP QSLVVYGGIG
     RAARNWACFD KIVEVLTRLE EDQTLLVQSG KPVGVFQTHK DAPRVLIANS NLVPHWANWE
     HFNELDKKGL MMYGQMTAGS WIYIGTQGIV QGTYETFFAV ANQHFNGEPK GRWILTGGLG
     GMGGAQPLAA TMAGFSMIAV ECDETRIDFR LRTRYVDKKA HSLDEALAMI EEAKQSGSAV
     SVGLLGNAAD VFAELVARGI TPDVVTDQTS AHDPVHGYLP QGWSVAQWRA LQKSAPQEVN
     VAARHSMARQ VEAMLTLQSR GAATLDYGNN IRQMALEEGV KNAFDFPGFV PAYIRPLFCE
     GIGPFRWVAL SGDPEDIYKT DQKVKELIPD DPHLHNWLDM ARDRIAFQGL PARICWVGVK
     DRVRLGLAFN EMVKNGELKA PIVIGRDHLD SGSVASPNRE TESMMDGSDA VSDWPLLNAL
     LNTAGGATWV SLHHGGGVGM GFSQHSGVVI VCDGSDDAAK RVGRVLRNDP ATGVMRHADA
     GYEIAINCAH EAKLDLPMID GANGVKGKV
//

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