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   03-AUG-2022, entry version 96.
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   PubMed=8566717; DOI=10.1111/j.1574-6968.1995.tb07865.x;
RA   Yabutani T., Maehara A., Ueda S., Yamane T.;
RT   "Analysis of beta-ketothiolase and acetoacetyl-CoA reductase genes of a
RT   methylotrophic bacterium, Paracoccus denitrificans, and their expression in
RT   Escherichia coli.";
RL   FEMS Microbiol. Lett. 133:85-90(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   -!- MISCELLANEOUS: NADH was preferred to NADPH as a substrate.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; D49362; BAA08358.1; -; Genomic_DNA.
DR   AlphaFoldDB; P50204; -.
DR   SMR; P50204; -.
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   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; NAD; NADP; Oxidoreductase; PHB biosynthesis.
FT   CHAIN           1..242
FT                   /note="Acetoacetyl-CoA reductase"
FT                   /id="PRO_0000054747"
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"
FT   BINDING         82..86
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         141..144
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         177..180
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         178..179
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
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