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HUTU_BEUC1
ID   HUTU_BEUC1              Reviewed;         557 AA.
AC   C5C4W6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-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=Bcav_1838;
OS   Beutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / NBRC 16432).
OC   Bacteria; Actinobacteria; Micrococcales; Beutenbergiaceae; Beutenbergia.
OX   NCBI_TaxID=471853;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-8 / DSM 12333 / NBRC 16432;
RX   PubMed=21304633; DOI=10.4056/sigs.1162;
RA   Land M., Pukall R., Abt B., Goker M., Rohde M., Glavina Del Rio T.,
RA   Tice H., Copeland A., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D.,
RA   Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA   Pati A., Chen A., Palaniappan K., Hauser L., Chang Y.J., Jefferies C.C.,
RA   Saunders E., Brettin T., Detter J.C., Han C., Chain P., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Beutenbergia cavernae type strain (HKI
RT   0122).";
RL   Stand. Genomic Sci. 1:21-28(2009).
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; CP001618; ACQ80094.1; -; Genomic_DNA.
DR   RefSeq; WP_015882334.1; NC_012669.1.
DR   AlphaFoldDB; C5C4W6; -.
DR   SMR; C5C4W6; -.
DR   STRING; 471853.Bcav_1838; -.
DR   EnsemblBacteria; ACQ80094; ACQ80094; Bcav_1838.
DR   KEGG; bcv:Bcav_1838; -.
DR   eggNOG; COG2987; Bacteria.
DR   HOGENOM; CLU_018868_0_1_11; -.
DR   OMA; LVGDWAN; -.
DR   OrthoDB; 100619at2; -.
DR   UniPathway; UPA00379; UER00550.
DR   Proteomes; UP000007962; 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..557
FT                   /note="Urocanate hydratase"
FT                   /id="PRO_1000212099"
FT   ACT_SITE        411
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT   BINDING         48..49
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT   BINDING         126
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT   BINDING         178..180
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT   BINDING         198
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT   BINDING         203
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT   BINDING         244..245
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT   BINDING         265..269
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT   BINDING         274..275
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT   BINDING         323
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT   BINDING         493
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
SQ   SEQUENCE   557 AA;  59869 MW;  459D2727E9BAE8A1 CRC64;
     MDGAREVRSP RGSTLTARSW QTEAPLRMLM NNLDPDVAER PDDLVVYGGT GRAARDWASY
     DGIVRTLTTL GDDETLLVQS GRPVGVLRTH EWAPRVLIAN SNLVPDWATW PEFRRLEHLG
     LTMYGQMTAG SWIYIGTQGI LQGTYETFAA VAEKVGRPDD DGVASLAGTL TLTAGCGGMG
     GAQPLAVTLN GGVCLVVDVD PERLRRRVAT RYLDEVADGL DDAVARCEAA KLERRALSVG
     LVGNAATVYP ELLRRGVEID VVTDQTSAHD PLSYLPEGVE LGEWHEAAEA KPEEFTDRAR
     ESMARQVAAM VGFLDAGAEV FDYGNSIRDE ARQGGYDRAF AFPGFVPAYI RPLFSEGKGP
     FRWAALSGDP ADIAATDRAV LDLFPDDAKL HRWIRAAGER VAYQGLPARI CWLGYGERHL
     AGLRFNEMVA SGELSAPIVI GRDHLDAGSV ASPYRETEAM ADGSDAIADW PLLNALVNTA
     SGATWVSIHH GGGVGIGRSI HAGQVSVADG TELAAAKLER VLTNDPGMGV IRHVDAGYAR
     ADEVAAERGV RVPMRES
 
 
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