HUTU_SHEPW
ID HUTU_SHEPW Reviewed; 556 AA.
AC B8CGY4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=swp_0133;
OS Shewanella piezotolerans (strain WP3 / JCM 13877).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=225849;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP3 / JCM 13877;
RX PubMed=18398463; DOI=10.1371/journal.pone.0001937;
RA Wang F., Wang J., Jian H., Zhang B., Li S., Wang F., Zeng X., Gao L.,
RA Bartlett D.H., Yu J., Hu S., Xiao X.;
RT "Environmental adaptation: genomic analysis of the piezotolerant and
RT psychrotolerant deep-sea iron reducing bacterium Shewanella piezotolerans
RT WP3.";
RL PLoS ONE 3:E1937-E1937(2008).
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; CP000472; ACJ26977.1; -; Genomic_DNA.
DR RefSeq; WP_020910361.1; NC_011566.1.
DR AlphaFoldDB; B8CGY4; -.
DR SMR; B8CGY4; -.
DR STRING; 225849.swp_0133; -.
DR EnsemblBacteria; ACJ26977; ACJ26977; swp_0133.
DR KEGG; swp:swp_0133; -.
DR eggNOG; COG2987; Bacteria.
DR HOGENOM; CLU_018868_0_1_6; -.
DR OMA; MAKQHFN; -.
DR OrthoDB; 100619at2; -.
DR UniPathway; UPA00379; UER00550.
DR Proteomes; UP000000753; 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.
FT CHAIN 1..556
FT /note="Urocanate hydratase"
FT /id="PRO_1000129576"
FT ACT_SITE 410
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 52..53
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 130
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 176..178
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 196
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 201
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 242..243
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 263..267
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 273..274
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 322
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 492
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
SQ SEQUENCE 556 AA; 60366 MW; 7A003BB5CEA2CF75 CRC64;
MDKRHDPSRR IIAPTGTKLS CKSWLTEAPM RMLMNNLHPD VAERPEDLVV YGGIGRAARD
WECYDKIVEV LQRLEDDETL LVQSGKPVGV FKTHSNAPRV IIANSNLVPH WANWEHFNEL
DKKGLAMYGQ MTAGSWIYIG SQGIVQGTYE TFVAMAKQHF GGSSKGKWIL TGGLGGMGGA
QPLAGTMAGY SVLTCEVDET RIDFRLRTRY VDKKATTLDE ALAMIDEANA SGKPVSVGLL
ANAADVFAEL VERGITPDVV TDQTSAHDPL NGYLPQGWTL EQAAQMRKTD EAAVVKAAKQ
SMAVQVKAML ALQAAGSATT DYGNNIRQMA FEEGVENAFD FPGFVPAYVR PLFCEGIGPF
RWAALSGDPE DIYKTDAKVK ELIPDNPHLH NWLDMARERI AFQGLPSRIC WVGLKDRARL
ALAFNEMVNN GELSAPVVIG RDHLDSGSVA SPNRETESML DGSDAVSDWP LMNALLNTAS
GATWVSLHHG GGVGMGFSQH SGVVIVADGT DDAAARLGRV LWNDPATGVM RHADAGYDIA
KDCAKEQGLD LPMLEK
