HUTU_FERNB
ID HUTU_FERNB Reviewed; 549 AA.
AC A7HN21;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Urocanate hydratase {ECO:0000255|HAMAP-Rule:MF_00577};
DE Short=Urocanase {ECO:0000255|HAMAP-Rule:MF_00577};
DE EC=4.2.1.49 {ECO:0000255|HAMAP-Rule:MF_00577};
DE AltName: Full=Imidazolonepropionate hydrolase {ECO:0000255|HAMAP-Rule:MF_00577};
GN Name=hutU {ECO:0000255|HAMAP-Rule:MF_00577}; OrderedLocusNames=Fnod_1461;
OS Fervidobacterium nodosum (strain ATCC 35602 / DSM 5306 / Rt17-B1).
OC Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Fervidobacterium.
OX NCBI_TaxID=381764;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Fervidobacterium nodosum Rt17-B1.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of urocanate to 4-imidazolone-5-
CC propionate. {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_00577};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00577};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00577}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00577}.
CC -!- SIMILARITY: Belongs to the urocanase family. {ECO:0000255|HAMAP-
CC Rule:MF_00577}.
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DR EMBL; CP000771; ABS61304.1; -; Genomic_DNA.
DR RefSeq; WP_011994609.1; NC_009718.1.
DR AlphaFoldDB; A7HN21; -.
DR SMR; A7HN21; -.
DR STRING; 381764.Fnod_1461; -.
DR EnsemblBacteria; ABS61304; ABS61304; Fnod_1461.
DR KEGG; fno:Fnod_1461; -.
DR eggNOG; COG2987; Bacteria.
DR HOGENOM; CLU_018868_0_1_0; -.
DR OMA; LVGDWAN; -.
DR OrthoDB; 100619at2; -.
DR UniPathway; UPA00379; UER00550.
DR Proteomes; UP000002415; 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;
KW Cytoplasm; Histidine metabolism; Lyase; NAD; Reference proteome.
FT CHAIN 1..549
FT /note="Urocanate hydratase"
FT /id="PRO_1000072580"
FT ACT_SITE 404
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 46..47
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 124
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 190
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 236..237
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 257..261
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 267..268
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 316
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 486
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
SQ SEQUENCE 549 AA; 61110 MW; 3C0956E9409BC7E5 CRC64;
MPEVIRAPRG TQLTCKSWQT EAAMRMLMNN LDPEVARDPA NLIVYGGKGK AARNWDCFYK
IVETLKKLEN DETLLIQSGK PVAVWKTHEW APRVLIANSN LVPKWATWEY FNELEVRGLI
MYGQMTAGSW IYIGTQGILQ GTYETFYAVA KKYFGGTLKG KLVLTAGLGE MGGAQPLAVT
MNDGVVIAVE VDKRMIDRRI QTGYLDTWTD NLDEALRLAK EALKEGRPLS IGLLGNAAEV
HPELVRRGII PDVVTDQTAA HDPLNGYVPA GISFEEALKL RKENPEKYLE MVYDSVVKHI
EAILEMQRQG AKVFEYGNNI RRLALDHGVK DAFNIPGYVP EYIRDLFSEG KGPFRWVALS
GKPEDIYKTD QKVLELFGED EHLRKWIDMA QKKVKWQGLP ARICWLGQGQ RAEMGLAMNE
MVRKGELEAP IVIGRDHHDT GSVASPYRET EAMKDGSDAI ADWPLLNAML NVASGATWVS
IHHGGGVGIG YSIHAGVVIV ADGTELTRQK LERVLTNDVG MGVVRHADAG YEIAIQTAKK
HGIRMPMMD
