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HUTU_BRUMB
ID   HUTU_BRUMB              Reviewed;         557 AA.
AC   C0RM77;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 66.
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=BMEA_B0916;
OS   Brucella melitensis biotype 2 (strain ATCC 23457).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=546272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23457;
RA   Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., Lu J.,
RA   Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., Snyder E.E.,
RA   Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Munk C., Tapia R.,
RA   Han C., Detter J.C., Bruce D., Brettin T.S.;
RT   "Brucella melitensis ATCC 23457 whole genome shotgun sequencing project.";
RL   Submitted (MAR-2009) 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; CP001489; ACO02710.1; -; Genomic_DNA.
DR   RefSeq; WP_004685970.1; NC_012442.1.
DR   AlphaFoldDB; C0RM77; -.
DR   SMR; C0RM77; -.
DR   EnsemblBacteria; ACO02710; ACO02710; BMEA_B0916.
DR   KEGG; bmi:BMEA_B0916; -.
DR   HOGENOM; CLU_018868_0_1_5; -.
DR   OMA; LVGDWAN; -.
DR   UniPathway; UPA00379; UER00550.
DR   Proteomes; UP000001748; Chromosome II.
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; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; Histidine metabolism; Lyase; NAD.
FT   CHAIN           1..557
FT                   /note="Urocanate hydratase"
FT                   /id="PRO_1000199898"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   557 AA;  61213 MW;  577D635BF06C0A1A CRC64;
     MSNPRHNERE VRSPRGDELN AKSWLTEAPL RMLMNNLDPD VAERPHELVV YGGIGRAART
     WDDFDRIVAT LKTLNDDETL LVQSGKPVGV FRTHKDAPRV LIANSNLVPH WANWDHFNEL
     DKKGLAMYGQ MTAGSWIYIG AQGIVQGTYE TFVEAGRQHY GGNLKGRWIL TGGLGGMGGA
     QPLAAVMAGA CCLAVECDET RADFRLRTRY VDEKTHSLDE ALAKIDAWTK AGEAKSIALI
     GNAAEIFPEL VKRGVKPDIV TDQTSAHDPV HGYLPLGWTV AEWRAKQEND PKAVEKAARA
     SMKVQVQAML DFWNAGIPTV DYGNNIRQMA LEEGLENAFA FPGFVPAYIR PLFCRGIGPF
     RWAALSGDPE DIAKTDAKVK ELLPDNKHLH NWLDMAKERI AFQGLPARIC WVGLGDRHRL
     GLAFNEMVRN GELKAPIVIG RDHLDSGSVA SPNRKTEAMK DGSDAVSDWP LLNALLNTAS
     GATWVSLHHG GGVGMGFSQH AGMVICCDGT EDADRRLERV LWNDPATGVM RHADAGYDIA
     LDWARKQGLR LPAILGN
 
 
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