ID   HUTU_TRIRP              Reviewed;         564 AA.
AC   P53385; P81170;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Urocanate hydratase;
DE            Short=Urocanase;
DE            EC=4.2.1.49;
DE   AltName: Full=Imidazolonepropionate hydrolase;
OS   Trifolium repens (Creeping white clover).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Trifolium.
OX   NCBI_TaxID=3899;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Huia;
RX   PubMed=1356832; DOI=10.1016/0014-5793(92)81103-s;
RA   Koberstaedt A., Lenz M., Retey J.;
RT   "Isolation, sequencing and expression in E. coli of the urocanase gene from
RT   white clover (Trifolium repens).";
RL   FEBS Lett. 311:206-208(1992).
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;
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC       Note=Binds 1 NAD(+) per subunit.;
CC   -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC       glutamate; N-formimidoyl-L-glutamate from L-histidine: step 2/3.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the urocanase family. {ECO:0000305}.
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DR   EMBL; X68950; CAA48765.1; -; Genomic_DNA.
DR   PIR; S29246; S29246.
DR   AlphaFoldDB; P53385; -.
DR   SMR; P53385; -.
DR   UniPathway; UPA00379; UER00550.
DR   GO; GO:0016153; F:urocanate hydratase activity; IEA:UniProtKB-EC.
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   Histidine metabolism; Lyase; NAD.
FT   CHAIN           1..564
FT                   /note="Urocanate hydratase"
FT                   /id="PRO_0000207373"
FT   ACT_SITE        416
FT                   /evidence="ECO:0000250"
FT   BINDING         54..55
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P25503"
FT   BINDING         132
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P25503"
FT   BINDING         178..180
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P25503"
FT   BINDING         198
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P25503"
FT   BINDING         203
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P25503"
FT   BINDING         244..245
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P25503"
FT   BINDING         269..273
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P25503"
FT   BINDING         279..280
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P25503"
FT   BINDING         328
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P25503"
FT   BINDING         498
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P25503"
SQ   SEQUENCE   564 AA;  61402 MW;  5A5E0FAC91622DC3 CRC64;
     MTDSVSKAVA RTIRAPHGSE LHCANWLIEA AYRMIQNNLD PDVAERPEDL VVYGGIGKAA
     RNWACFEQIL RSLQALQPEE TLLVQSGKPV GVFRTHADAP RVLIANSNLV PHWATWDHFH
     ELDKAGLMMY GQMTAGSWIY IGAQGIVQGT FETFVEAGRK HYNGDLTGKW ILTAGLGGMG
     GAQPLAGVLA GACVLAVECQ ESRIDFRLRT RYLDHKAFSV DEALAIIDKA CKEKRAISVG
     LLGNAAEILP ELVQRAKAGG MKPDIVTDQT SAHDPINGYL PAGWDLARWE SSRQSDPKAV
     EKAARASMAV HVQAMLDFCH MGIPTVDYGN NIRQVALDEG VKNAFDFPGF VPAYIRPLFC
     EGKGPFRWVA LSGDPEDIYK TDAKLKALFP EHTNLHRWLD MAQERIAFQG LPARICWLGL
     GERHLAGLAF NEMVRNGELK APVVIGRDHL DCGSVASPNR ETEAMMDGSD AVSDWPLLNA
     LLNTAGGATW VSLHHGGGVG MGFSQHAGVV IVADGTAEAD ARLSRVLWND PATGVMRHAD
     AGYEVARDCA RRHELTLPMA KELP