ID   PHAB_PARDE              Reviewed;         242 AA.
AC   P50204;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JUN-2009, entry version 49.
DE   RecName: Full=Acetoacetyl-CoA reductase;
DE            EC=1.1.1.36;
GN   Name=phaB;
OS   Paracoccus denitrificans.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=266;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=96079497; PubMed=8566717; DOI=10.1016/0378-1097(95)00341-2;
RA   Yabutani T., Maehara A., Ueda S., Yamane T.;
RT   "Analysis of beta-ketothiolase and acetoacetyl-CoA reductase genes of
RT   a methylotrophic bacterium, Paracoccus denitrificans, and their
RT   expression in Escherichia coli.";
RL   FEMS Microbiol. Lett. 133:85-90(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   -!- MISCELLANEOUS: NADH was preferred to NADPH as a substrate.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family.
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DR   EMBL; D49362; BAA08358.1; -; Genomic_DNA.
DR   HSSP; Q93X62; 1EDO.
DR   BRENDA; 1.1.1.36; 59.
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:UniProtKB-KW.
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; NAD; NADP; Oxidoreductase; PHB biosynthesis.
FT   CHAIN         1    242       Acetoacetyl-CoA reductase.
FT                                /FTId=PRO_0000054747.
FT   NP_BIND       7     31       NAD (By similarity).
FT   ACT_SITE    147    147       Proton acceptor (By similarity).
FT   BINDING     134    134       Substrate (By similarity).
SQ   SEQUENCE   242 AA;  25615 MW;  3CD4B9BD23FC98FD CRC64;
     MAKVALVTGG SRGIGAAISK ALKEAGYTVA ANYAGNDDAA RAFTEETGIK TYKWSVADYD
     ACAAGIKQVE EELGPIAVLV NNAGITRDAM FHKMTPQQWK EVIDTNLTGL FNMTHPVWSG
     MRDRKYGRIV NISSINGQKG QAGQANYSAA KAGDLGFTKA LAQEGARAGI TVNAICPGYI
     GTEMVRAIDE KVLNEGIIPQ IPVAAWAEPE EIARCVVFLA SEDAGFITGS THQAPNGGQF
     FV
//