ID   PHAB_SHIZO              Reviewed;         241 AA.
AC   P23238;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-AUG-2022, entry version 104.
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:2546004};
OS   Shinella zoogloeoides (Crabtreella saccharophila).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Shinella.
OX   NCBI_TaxID=352475;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC   STRAIN=ATCC 19623 / DSM 287 / JCM 20728 / IAM 12669 / NBRC 102405 / NCIMB
RC   10340 / NCTC 10482 / NRRL B-3303 / I-16-M;
RX   PubMed=2546004; DOI=10.1111/j.1365-2958.1989.tb00180.x;
RA   Peoples O.P., Sinskey A.J.;
RT   "Fine structural analysis of the Zoogloea ramigera phbA-phbB locus encoding
RT   beta-ketothiolase and acetoacetyl-CoA reductase: nucleotide sequence of
RT   phbB.";
RL   Mol. Microbiol. 3:349-357(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-31.
RX   PubMed=3286259; DOI=10.1111/j.1432-1033.1988.tb14079.x;
RA   Ploux O., Masamune S., Walsh C.T.;
RT   "The NADPH-linked acetoacetyl-CoA reductase from Zoogloea ramigera.
RT   Characterization and mechanistic studies of the cloned enzyme over-produced
RT   in Escherichia coli.";
RL   Eur. J. Biochem. 174:177-182(1988).
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. {ECO:0000269|PubMed:2546004}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   PIR; S06998; S06998.
DR   AlphaFoldDB; P23238; -.
DR   SMR; P23238; -.
DR   BioCyc; MetaCyc:MON-13089; -.
DR   UniPathway; UPA00917; -.
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   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.
FT   CHAIN           1..241
FT                   /note="Acetoacetyl-CoA reductase"
FT                   /id="PRO_0000054751"
FT   ACT_SITE        147
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         82..86
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P14697"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P14697"
FT   BINDING         141..144
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P14697"
FT   BINDING         177..180
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P14697"
FT   BINDING         178..179
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P14697"
SQ   SEQUENCE   241 AA;  25285 MW;  8FDD489C0D816804 CRC64;
     MSRVALVTGG SRGIGAAISI ALKAAGYKVA ASYAGNDDAA KPFKAETGIA VYKWDVSSYE
     ACVEGIAKVE ADLGPIDVLV NNAGITKDAM FHKMTPDQWN AVINTNLTGL FNMTHPVWSG
     MRDRSFGRIV NISSINGQKG QMGQANYSAA KAGDLGFTKA LAQEGAAKGI TVNAICPGYI
     GTEMVRAIPE KVLNERIIPQ IPVGRLGEPD EIARIVVFLA SDEAGFITGS TISANGGQFF
     V