HUTU_BACAA
ID HUTU_BACAA Reviewed; 552 AA.
AC C3P4M1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-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=BAA_3738;
OS Bacillus anthracis (strain A0248).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=592021;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A0248;
RA Dodson R.J., Munk A.C., Bruce D., Detter C., Tapia R., Sutton G., Sims D.,
RA Brettin T.;
RT "Genome sequence of Bacillus anthracis A0248.";
RL Submitted (APR-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; CP001598; ACQ50025.1; -; Genomic_DNA.
DR RefSeq; WP_000416715.1; NC_012659.1.
DR AlphaFoldDB; C3P4M1; -.
DR SMR; C3P4M1; -.
DR GeneID; 45023432; -.
DR KEGG; bai:BAA_3738; -.
DR HOGENOM; CLU_018868_0_1_9; -.
DR OMA; LVGDWAN; -.
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..552
FT /note="Urocanate hydratase"
FT /id="PRO_1000199894"
FT ACT_SITE 407
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 49..50
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 127
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 173..175
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 193
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 239..240
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 260..264
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 270..271
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 319
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT BINDING 489
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
SQ SEQUENCE 552 AA; 60778 MW; 8F5161A0D89D916B CRC64;
MEKVKQTIRA PRGTELQTKG WVQEAALRML MNNLDPEVAE KPEELVVYGG IGRAARNWES
YQAIVDSLKT LESDETLLVQ SGKPVAIFKS HEDAPRVLLA NSNLVPKWAN WDHFRELEKK
GLMMYGQMTA GSWIYIGTQG ILQGTYETFG EAARQHFGGS LKGTLTLTAG LGGMGGAQPL
AVTMNGGVVI AIDVDKRSID RRIEKRYCDM YTESLEEALA VANEYKEKKE PISIGLLGNA
AEILPELVKR NITPDLVTDQ TSAHDPLNGY IPVGYTLEEA AKLREEDPER YVQLSKESMT
KHVEAMLAMQ EKGAITFDYG NNIRQVAFDE GLKNAFDFPG FVPAFIRPLF CEGKGPFRWV
ALSGDPEDIY KTDEVILREF ADNEHLCNWI RMARQQVEFQ GLPSRICWLG YGERAKFGRI
INEMVANGEL SAPIVIGRDH LDCGSVASPN RETEAMKDGS DSVADWPILN ALINSVNGAS
WVSVHHGGGV GMGYSLHAGM VIVADGTEAA AKRIERVLTS DPGMGVVRHV DAGYDLAVET
AKEKGVNIPM MK
