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HUTU_SHEPC
ID   HUTU_SHEPC              Reviewed;         555 AA.
AC   A4Y1I2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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};
GN   OrderedLocusNames=Sputcn32_0079;
OS   Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=319224;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CN-32 / ATCC BAA-453;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella putrefaciens CN-32.";
RL   Submitted (APR-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; CP000681; ABP73815.1; -; Genomic_DNA.
DR   RefSeq; WP_011918296.1; NC_009438.1.
DR   AlphaFoldDB; A4Y1I2; -.
DR   SMR; A4Y1I2; -.
DR   STRING; 319224.Sputcn32_0079; -.
DR   GeneID; 45040520; -.
DR   KEGG; spc:Sputcn32_0079; -.
DR   eggNOG; COG2987; Bacteria.
DR   HOGENOM; CLU_018868_0_1_6; -.
DR   OMA; MAKQHFN; -.
DR   UniPathway; UPA00379; UER00550.
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..555
FT                   /note="Urocanate hydratase"
FT                   /id="PRO_1000025151"
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   555 AA;  60271 MW;  1BA83DF8E94C0522 CRC64;
     MDKRHDPSRR IIAPHGTQLS CKSWLTEAPM RMLMNNLHPD VAERPEDLVV YGGIGRAARD
     WDCYDKIIEV LQRLEDDETL LVQSGKPVGV FRTHADAPRV LIANSNLVPH WANWEHFNEL
     DKLGLAMYGQ MTAGSWIYIG TQGIVQGTYE TFVSVAKQHF EGISKGKWIL TGGLGGMGGA
     QTLAGTMAGF SVLACEVDET RIDFRLRTRY VDKKATSLDE ALAMIEAANQ AGKPVSVGLL
     ANAADVFAEL VKRGVTPDVV TDQTSAHDPL NGYLPQGWTM AEAAAMRKTD EAAVIKAAKA
     SMAVQVQAML DLQTAGAATL DYGNNIRQMA FEMGVENAFD FPGFVPAYIR PLFCEGIGPF
     RWVALSGDPE DIYKTDAKVK ELIPDNPLLH NWLDMARERI AFQGLPARIC WVGLKDRARL
     ALAFNEMVKN GELSAPVVIG RDHLDSGSVA SPNRETESML DGSDAVSDWP LLNALLNTAS
     GATWVSLHHG GGVGMGFSQH SGVVIVCDGT DAAAKRVGRV LWNDPATGVM RHADAGYEIA
     KNCAKEQGLD LPMQD
 
 
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