PHAB_RHIME
ID PHAB_RHIME Reviewed; 241 AA.
AC P50205;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Acetoacetyl-CoA reductase;
DE EC=1.1.1.36;
GN Name=phaB {ECO:0000303|PubMed:7582015}; OrderedLocusNames=R03261;
GN ORFNames=SMc03878;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=41;
RX PubMed=7582015; DOI=10.1099/13500872-141-10-2553;
RA Tombolini R., Povolo S., Buson A., Squartini A., Nuti M.P.;
RT "Poly-beta-hydroxybutyrate (PHB) biosynthetic genes in Rhizobium meliloti
RT 41.";
RL Microbiology 141:2553-2559(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
RN [4]
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; U17226; AAA90983.1; -; Genomic_DNA.
DR EMBL; AL591688; CAC47840.1; -; Genomic_DNA.
DR RefSeq; NP_387367.1; NC_003047.1.
DR RefSeq; WP_003535773.1; NC_003047.1.
DR AlphaFoldDB; P50205; -.
DR SMR; P50205; -.
DR STRING; 266834.SMc03878; -.
DR EnsemblBacteria; CAC47840; CAC47840; SMc03878.
DR GeneID; 61604720; -.
DR KEGG; sme:SMc03878; -.
DR PATRIC; fig|266834.11.peg.4815; -.
DR eggNOG; COG1028; Bacteria.
DR HOGENOM; CLU_010194_1_3_5; -.
DR OMA; KGAFYCA; -.
DR UniPathway; UPA00917; -.
DR Proteomes; UP000001976; Chromosome.
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; Reference proteome.
FT CHAIN 1..241
FT /note="Acetoacetyl-CoA reductase"
FT /id="PRO_0000054750"
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 39
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; 25370 MW; 025C43AF1900B1F0 CRC64;
MSRVALVTGG SRGIGAAICV ALKAAGYKVA ANYAGNDERA KAFEQESGIP VYKWDVSSYQ
ACVDGIARVE ADLGPVDILV NNAGITRDAM FHKMTPEQWG EVIGTNLTGV FNMTHPLWSG
MRDRGFGRIV NISSINGQKG QMGQVNYSAA KAGDLGLTKA LAQEGAAKGI TVNAICPGYI
GTEMVRAVPE KVLNERIIPQ IPVGRLGEPE EVARCVVFLA SDDAGFITGS TISANGGQYF
A
