ID   PHAB_ALLVD              Reviewed;         246 AA.
AC   P45375; D3RUY9;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Acetoacetyl-CoA reductase;
DE            EC=1.1.1.36;
GN   Name=phaB {ECO:0000303|PubMed:1476773};
GN   Synonyms=phbB {ECO:0000303|PubMed:1396692}; OrderedLocusNames=Alvin_0066;
OS   Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS   10441 / D) (Chromatium vinosum).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Allochromatium.
OX   NCBI_TaxID=572477;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX   PubMed=1396692; DOI=10.1111/j.1432-1033.1992.tb17270.x;
RA   Liebergesell M., Steinbuechel A.;
RT   "Cloning and nucleotide sequences of genes relevant for biosynthesis of
RT   poly(3-hydroxybutyric acid) in Chromatium vinosum strain D.";
RL   Eur. J. Biochem. 209:135-150(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX   PubMed=22675582; DOI=10.4056/sigs.2335270;
RA   Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA   Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT   "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL   Stand. Genomic Sci. 5:311-330(2011).
RN   [3]
RP   GENE NAME.
RX   PubMed=1476773; DOI=10.1111/j.1574-6968.1992.tb05841.x;
RA   Steinbuechel A., Hustede E., Liebergesell M., Pieper U., Timm A.,
RA   Valentin H.;
RT   "Molecular basis for biosynthesis and accumulation of polyhydroxyalkanoic
RT   acids in bacteria.";
RL   FEMS Microbiol. Rev. 9:217-230(1992).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3R)-3-hydroxyacyl-CoA + NADP(+) = a 3-oxoacyl-CoA + H(+) +
CC         NADPH; Xref=Rhea:RHEA:22256, ChEBI:CHEBI:15378, ChEBI:CHEBI:57319,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:90726; EC=1.1.1.36;
CC   -!- PATHWAY: Biopolymer metabolism; poly-(R)-3-hydroxybutanoate
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; L01112; AAA23325.1; -; Genomic_DNA.
DR   EMBL; CP001896; ADC61038.1; -; Genomic_DNA.
DR   PIR; S29279; S29279.
DR   RefSeq; WP_012969314.1; NC_013851.1.
DR   AlphaFoldDB; P45375; -.
DR   SMR; P45375; -.
DR   STRING; 572477.Alvin_0066; -.
DR   EnsemblBacteria; ADC61038; ADC61038; Alvin_0066.
DR   KEGG; alv:Alvin_0066; -.
DR   eggNOG; COG1028; Bacteria.
DR   HOGENOM; CLU_010194_1_3_6; -.
DR   OMA; EFHSCDV; -.
DR   OrthoDB; 1601931at2; -.
DR   UniPathway; UPA00917; -.
DR   Proteomes; UP000001441; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0018454; F:acetoacetyl-CoA reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042619; P:poly-hydroxybutyrate biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR011283; Acetoacetyl-CoA_reductase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01829; AcAcCoA_reduct; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; NADP; Oxidoreductase; PHB biosynthesis; Reference proteome.
FT   CHAIN           1..246
FT                   /note="Acetoacetyl-CoA reductase"
FT                   /id="PRO_0000054749"
FT   ACT_SITE        153
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         12..14
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P14697"
FT   BINDING         88..92
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P14697"
FT   BINDING         94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P14697"
FT   BINDING         147..150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P14697"
FT   BINDING         183..186
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P14697"
FT   BINDING         184..185
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P14697"
FT   CONFLICT        215
FT                   /note="D -> N (in Ref. 1; AAA23325)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   246 AA;  26124 MW;  C7FED7450A1F54E3 CRC64;
     MARIALVTGG IGGIGTSICT RLAKDGCTVV ANCHPSEAAA AEEWKQARAA EGFDIAVFTA
     DVSSFDDSAR MVREITEQVG PIDILVNCAG ITRDKTFKKM EQAHWEAVIN VNLNSVFNVT
     RQVWDGMLER GFGRIINISS VNGQRGQFGQ ANYSAAKAGM HGFTMALAQE GASKGVTVNT
     ISPGYVETAM TLAMNDDVRN SIISGIPMRR MAQPDEIAAA IAFLAGDESG YMTGANLPVN
     GGLFMH