ID   PHAB_ACISR              Reviewed;         248 AA.
AC   P50203;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Acetoacetyl-CoA reductase;
DE            EC=1.1.1.36;
GN   Name=phaB;
OS   Acinetobacter sp. (strain RA3849).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=68994;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7635832; DOI=10.1128/jb.177.15.4501-4507.1995;
RA   Schembri M.A., Bayly R.C., Davies J.K.;
RT   "Phosphate concentration regulates transcription of the Acinetobacter
RT   polyhydroxyalkanoic acid biosynthetic genes.";
RL   J. Bacteriol. 177:4501-4507(1995).
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; L37761; AAA99472.1; -; Genomic_DNA.
DR   AlphaFoldDB; P50203; -.
DR   SMR; P50203; -.
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:InterPro.
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.
FT   CHAIN           1..248
FT                   /note="Acetoacetyl-CoA reductase"
FT                   /id="PRO_0000054746"
FT   ACT_SITE        155
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         14..16
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         42
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         90..94
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         149..152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         185..188
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         186..187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   248 AA;  26727 MW;  850E0DC659795123 CRC64;
     MSEQKVALVT GALGGIGSEI CRQLVTAGYK IIATVVPREE DREKQWLQSE GFQDSDVRFV
     LTDLNNHEAA TAAIQEAIAA EGRVDVLVNN AGITRDATFK KMSYEQWSQV IDTNLKTLFT
     VTQPVFNKML EQKSGRIVNI SSVNGLKGQF GQANYSASKA GIIGFTKALA QEGARSNICV
     NVVAPGYTAT PMVTAMREDV IKSIEAQIPL QRLAAPAEIA AAVMYLVSEH GAYVTGETLS
     INGGLYMH