ID A0A6I6RV36_9ACTN Unreviewed; 554 AA.
AC A0A6I6RV36;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 18-JUN-2025, entry version 18.
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=GR130_04095 {ECO:0000313|EMBL:QHC20733.1};
OS Streptomyces sp. GS7.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2692234 {ECO:0000313|EMBL:QHC20733.1, ECO:0000313|Proteomes:UP000464558};
RN [1] {ECO:0000313|EMBL:QHC20733.1, ECO:0000313|Proteomes:UP000464558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS7 {ECO:0000313|EMBL:QHC20733.1,
RC ECO:0000313|Proteomes:UP000464558};
RA Li J., Ni J., Li Y.;
RT "Multiple polyene macrolides produced by antifungal Streptomyces from gut
RT of Macrotermes barneyi facilitates the termite-fungus mutualism.";
RL Submitted (DEC-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of urocanate to 4-imidazolone-5-
CC propionate. {ECO:0000256|ARBA:ARBA00056569, ECO:0000256|HAMAP-
CC 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}.
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DR EMBL; CP047146; QHC20733.1; -; Genomic_DNA.
DR RefSeq; WP_159503431.1; NZ_CP047146.1.
DR AlphaFoldDB; A0A6I6RV36; -.
DR UniPathway; UPA00379; UER00550.
DR Proteomes; UP000464558; 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: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; 3.40.50.10730:FF:000001; Urocanate hydratase; 1.
DR Gene3D; 3.40.50.10730; Urocanase like domains; 1.
DR Gene3D; 3.40.1770.10; Urocanase superfamily; 1.
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:SF4; 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:UP000464558}.
FT DOMAIN 7..133
FT /note="Urocanase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17391"
FT DOMAIN 136..343
FT /note="Urocanase Rossmann-like"
FT /evidence="ECO:0000259|Pfam:PF01175"
FT DOMAIN 346..540
FT /note="Urocanase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17392"
FT ACT_SITE 405
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT BINDING 48..49
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT BINDING 126
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT BINDING 172..174
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT BINDING 192
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT BINDING 238..239
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT BINDING 259..263
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT BINDING 268..269
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT BINDING 317
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT BINDING 487
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
SQ SEQUENCE 554 AA; 59775 MW; B6367769ADD4EB3E CRC64;
MSGPRPVRAP RGTELSARGW QQEAALRMLQ NNLDPEVAEH PDQLVVYGGT GKAARDWRSF
DAMVRTLTTL KQDETMLVQS GKPVGVMQTH EWAPRVLIAN SNLVGDWANW EEFRRLEALG
LTMYGQMTAG SWIYIGTQGI LQGTYETFAA VAAKKFGGSL AGTITLTAGL GGMGGAQPLA
VTMNDGVAIC IDCDPRAIER RIEHRYLDVK ADSLQHALQL AVEARDQRRP LSIGLLGNAA
ELLPQMLAEG APIDIVTDQT SAHDPLAYLP VGIDFADMAA YAAEKPADFT QRARESMARH
VEAMVGFMDA GAEVFDYGNS IRGEAQLAGY QRAFAFPGFV PAYIRPLFAE GKGPFRWAAL
SGDPADIAAT DRAILDLFPE NESLARWIKL AGERVHFQGL PARICWLGYG ERDKAGERFN
EMVADGTLKA PLAIGRDHLD CGSVASPYRE TEAMRDGSDA IADWPLLNAM VNVASGASWV
SLHHGGGVGM GRSIHAGQVT VADGTPLAGE KIRRVLTNDP GMGVIRHVDA GYERAEEVAA
ERGVRIPMRE GEGA
//
