ID A0A4Y9J493_9LACT Unreviewed; 674 AA.
AC A0A4Y9J493;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 18-JUN-2025, entry version 21.
DE RecName: Full=Urocanate hydratase {ECO:0000256|ARBA:ARBA00011992, ECO:0000256|HAMAP-Rule:MF_00577};
DE Short=Urocanase {ECO:0000256|HAMAP-Rule:MF_00577};
DE EC=4.2.1.49 {ECO:0000256|ARBA:ARBA00011992, ECO:0000256|HAMAP-Rule:MF_00577};
DE AltName: Full=Imidazolonepropionate hydrolase {ECO:0000256|ARBA:ARBA00031640, ECO:0000256|HAMAP-Rule:MF_00577};
GN Name=hutU {ECO:0000256|HAMAP-Rule:MF_00577};
GN ORFNames=E4T68_03205 {ECO:0000313|EMBL:TFU95820.1};
OS Granulicatella sp. WM01.
OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
OC Carnobacteriaceae; Granulicatella.
OX NCBI_TaxID=2558277 {ECO:0000313|EMBL:TFU95820.1, ECO:0000313|Proteomes:UP000298203};
RN [1] {ECO:0000313|EMBL:TFU95820.1, ECO:0000313|Proteomes:UP000298203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM01 {ECO:0000313|EMBL:TFU95820.1,
RC ECO:0000313|Proteomes:UP000298203};
RA Joseph S., Aduse-Opoku J., Curtis M., Wade W., Hashim A.;
RT "Diversity of the mouse oral microbiome.";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
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 = trans-urocanate + H2O;
CC Xref=Rhea:RHEA:13101, ChEBI:CHEBI:15377, ChEBI:CHEBI:17771,
CC ChEBI:CHEBI:77893; EC=4.2.1.49;
CC Evidence={ECO:0000256|ARBA:ARBA00047623, ECO:0000256|HAMAP-
CC Rule:MF_00577};
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|ARBA:ARBA00004794, ECO:0000256|HAMAP-Rule:MF_00577}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00577}.
CC -!- SIMILARITY: Belongs to the urocanase family.
CC {ECO:0000256|ARBA:ARBA00007578, ECO:0000256|HAMAP-Rule:MF_00577}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00577}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TFU95820.1}.
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DR EMBL; SPPB01000013; TFU95820.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Y9J493; -.
DR OrthoDB; 9764874at2; -.
DR UniPathway; UPA00379; UER00550.
DR Proteomes; UP000298203; Unassembled WGS sequence.
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:L-histidine catabolic process to glutamate and formamide; IEA:UniProtKB-UniPathway.
DR GO; GO:0019557; P:L-histidine catabolic process to glutamate and formate; IEA:UniProtKB-UniPathway.
DR FunFam; 3.40.1770.10:FF:000002; Urocanate hydratase 1; 1.
DR Gene3D; 3.40.50.10730; Urocanase like domains; 1.
DR Gene3D; 3.40.1770.10; Urocanase superfamily; 2.
DR HAMAP; MF_00577; HutU; 1.
DR InterPro; IPR055351; Urocanase.
DR InterPro; IPR023637; Urocanase-like.
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 NCBIfam; TIGR01228; hutU; 1.
DR NCBIfam; NF003820; PRK05414.1; 1.
DR PANTHER; PTHR12216; UROCANATE HYDRATASE; 1.
DR PANTHER; PTHR12216:SF3; UROCANATE HYDRATASE; 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; Urocanase; 1.
DR PROSITE; PS01233; UROCANASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00577};
KW Histidine metabolism {ECO:0000256|ARBA:ARBA00022808, ECO:0000256|HAMAP-
KW Rule:MF_00577};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00577};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00577};
KW Reference proteome {ECO:0000313|Proteomes:UP000298203}.
FT DOMAIN 89..214
FT /note="Urocanase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17391"
FT DOMAIN 217..440
FT /note="Urocanase Rossmann-like"
FT /evidence="ECO:0000259|Pfam:PF01175"
FT DOMAIN 445..640
FT /note="Urocanase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17392"
FT BINDING 207
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT BINDING 277
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT BINDING 282
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT BINDING 404
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT BINDING 589
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
SQ SEQUENCE 674 AA; 75561 MW; C64E5D09F0C4D50C CRC64;
MINYKDIEAA MTIKLDDVLP EKTVFEPGIR RAPDRGFRLT PAQTEIALKN ALRYIPSKYH
EEIIPEFLEE LKTRGRIYGY RWYPKERIYG KPIDEYKGKC TAAKAMQVMI DNNLDFRVAL
YPYELVTYGE TGQVCSNWMQ YHLIMKYLEE MTDEQTLVVE SGHPLGLFKS KKDAPRVIIT
NGLLVGEYDN MHDWEIAEQM GVTNYGQMTA GGWMYIGPQG IVHGTFNTLL NAGRLKLGIA
DEGDLRGKLF ISSGLGGMSG AQGKAGEIAN AVAIVAEVDE SRIETRHSQG WISQVCQTPE
DTMALAKEYL DKQESTSIAY HGNIVDLLEY IDRENIHVDL LSDQTSCHNV YTGGYCPVGI
SFEERTRLLG EDQGTFKRLV DETLARHYKV IKSLTEKGTY FFDYGNAFMK SVYDSGIKEI
SKNGIDDKDG FIWPSYVEDI MGPMLFDYGY GPFRWVCLSG KHEDLMATDK AAMEVIDPTR
RYQDRDNYNW IRDAEKNQLV VGTQARILYQ DAMGRVNIAL KFNQLIREGK IGPVMLGRDH
HDVSGTDSPF RETSNIKDGS NVTADMATQC YAGNAARGMS LIALHNGGGV GIGKSINGGF
GLVLDGSELC DDIIKSAIAW DTMGGVARRN WARNEHAIET SIEYNKMREG SDHITIPYLA
DEEAVKAAVS KLFN
//
