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   16-JUN-2009, entry version 46.
DE   RecName: Full=Acetoacetyl-CoA reductase;
DE            EC=1.1.1.36;
GN   Name=phaB;
OS   Acinetobacter sp. (strain RA3849).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=68994;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=95362679; PubMed=7635832;
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: (R)-3-hydroxyacyl-CoA + NADP(+) = 3-oxoacyl-
CC       CoA + NADPH.
CC   -!- PATHWAY: Biopolymer metabolism; poly-(R)-3-hydroxybutyric acid
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family.
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DR   EMBL; L37761; AAA99472.1; -; Genomic_DNA.
DR   HSSP; Q01782; 1E7W.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0018454; F:acetoacetyl-CoA reductase activity; IEA:EC.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0042619; P:poly-hydroxybutyrate biosynthetic process; IEA:InterPro.
DR   InterPro; IPR011283; Acetoacetyl-CoA_reductase.
DR   InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR   InterPro; IPR002347; Glc/ribitol_DH.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR19410; ADH_short_C2; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
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       Acetoacetyl-CoA reductase.
FT                                /FTId=PRO_0000054746.
FT   NP_BIND       9     33       NADP (By similarity).
FT   ACT_SITE    155    155       Proton acceptor (By similarity).
FT   BINDING     142    142       Substrate (By similarity).
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
//