ID A7GPH6_BACCN Unreviewed; 350 AA.
AC A7GPH6;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=3-hydroxyisobutyryl-CoA hydrolase {ECO:0000256|ARBA:ARBA00011915};
DE EC=3.1.2.4 {ECO:0000256|ARBA:ARBA00011915};
GN OrderedLocusNames=Bcer98_1732 {ECO:0000313|EMBL:ABS22034.1};
OS Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315749 {ECO:0000313|EMBL:ABS22034.1, ECO:0000313|Proteomes:UP000002300};
RN [1] {ECO:0000313|EMBL:ABS22034.1, ECO:0000313|Proteomes:UP000002300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98
RC {ECO:0000313|Proteomes:UP000002300};
RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "Extending the Bacillus cereus group genomics to putative food-borne
RT pathogens of different toxicity.";
RL Chem. Biol. Interact. 171:236-249(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxy-2-methylpropanoyl-CoA + H2O = 3-hydroxy-2-
CC methylpropanoate + CoA + H(+); Xref=Rhea:RHEA:20888,
CC ChEBI:CHEBI:11805, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57340; EC=3.1.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00001709};
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DR EMBL; CP000764; ABS22034.1; -; Genomic_DNA.
DR RefSeq; WP_012094223.1; NC_009674.1.
DR AlphaFoldDB; A7GPH6; -.
DR STRING; 315749.Bcer98_1732; -.
DR GeneID; 56417306; -.
DR KEGG; bcy:Bcer98_1732; -.
DR eggNOG; COG1024; Bacteria.
DR HOGENOM; CLU_009834_22_1_9; -.
DR OrthoDB; 9775794at2; -.
DR Proteomes; UP000002300; Chromosome.
DR GO; GO:0003860; F:3-hydroxyisobutyryl-CoA hydrolase activity; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR CDD; cd06558; crotonase-like; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR045004; ECH_dom.
DR InterPro; IPR032259; HIBYL-CoA-H.
DR PANTHER; PTHR43176:SF3; 3-HYDROXYISOBUTYRYL-COA HYDROLASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43176; 3-HYDROXYISOBUTYRYL-COA HYDROLASE-RELATED; 1.
DR Pfam; PF16113; ECH_2; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Isomerase {ECO:0000313|EMBL:ABS22034.1}.
FT DOMAIN 15..345
FT /note="Enoyl-CoA hydratase/isomerase"
FT /evidence="ECO:0000259|Pfam:PF16113"
SQ SEQUENCE 350 AA; 39125 MW; C6836CEA4576EC2E CRC64;
MTENVLFSIG DHGVATITLN RPKALNSLSY DMLKSIGQKL KEWETNNQIA LIVLKGAGSK
GFCAGGDIKT LYEARSNEAA LQHAEKFFEE EYDIDTYIYR YPKPIIACLD GIVMGGGVGL
TNGATYRIVT EHTKWAMPEM NIGFFPDVGA AYFLNQAPGH TGRYVALTAA VLKAADVLYI
NAADYYMTTE SLSAFLTEIE NINWNIQDVH TTLKKIILTF ASTPNAESTL ASILENINTH
FSFHSIEEII DSLEKDGGTF ALQTKETLLS KSPFSLKVTL KQLSEGRNKS IEECFATDLI
LAKNFMRHDD FFEGVRSVVI DKDQNPQYKY KKLSDVSDED VNRFFHLLHV
//
