ID A4J686_DESRM Unreviewed; 247 AA.
AC A4J686;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase {ECO:0000256|RuleBase:RU366074};
DE EC=1.1.1.100 {ECO:0000256|RuleBase:RU366074};
GN OrderedLocusNames=Dred_2072 {ECO:0000313|EMBL:ABO50589.1};
OS Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS (Desulfotomaculum reducens).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=349161 {ECO:0000313|EMBL:ABO50589.1, ECO:0000313|Proteomes:UP000001556};
RN [1] {ECO:0000313|EMBL:ABO50589.1, ECO:0000313|Proteomes:UP000001556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MI-1 {ECO:0000313|EMBL:ABO50589.1,
RC ECO:0000313|Proteomes:UP000001556};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT "Complete sequence of Desulfotomaculum reducens MI-1.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP
CC substrates to beta-hydroxyacyl-ACP products, the first reductive step
CC in the elongation cycle of fatty acid biosynthesis.
CC {ECO:0000256|RuleBase:RU366074}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+)
CC + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-
CC COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;
CC Evidence={ECO:0000256|ARBA:ARBA00001572,
CC ECO:0000256|RuleBase:RU366074};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194, ECO:0000256|RuleBase:RU366074}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU366074}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484, ECO:0000256|RuleBase:RU366074}.
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DR EMBL; CP000612; ABO50589.1; -; Genomic_DNA.
DR RefSeq; WP_011878395.1; NC_009253.1.
DR AlphaFoldDB; A4J686; -.
DR STRING; 349161.Dred_2072; -.
DR KEGG; drm:Dred_2072; -.
DR eggNOG; COG1028; Bacteria.
DR HOGENOM; CLU_010194_1_3_9; -.
DR OrthoDB; 9803333at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001556; Chromosome.
DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008202; P:steroid metabolic process; IEA:UniProtKB-KW.
DR CDD; cd05333; BKR_SDR_c; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR011284; 3oxo_ACP_reduc.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR NCBIfam; TIGR01830; 3oxo_ACP_reduc; 1.
DR PANTHER; PTHR42879; 3-OXOACYL-(ACYL-CARRIER-PROTEIN) REDUCTASE; 1.
DR PANTHER; PTHR42879:SF2; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] REDUCTASE FABG; 1.
DR Pfam; PF13561; adh_short_C2; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SMART; SM00822; PKS_KR; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|RuleBase:RU366074};
KW Fatty acid metabolism {ECO:0000256|RuleBase:RU366074};
KW Lipid biosynthesis {ECO:0000256|RuleBase:RU366074};
KW Lipid metabolism {ECO:0000256|RuleBase:RU366074};
KW NADP {ECO:0000256|PIRSR:PIRSR611284-2, ECO:0000256|RuleBase:RU366074};
KW Oxidoreductase {ECO:0000256|RuleBase:RU366074,
KW ECO:0000313|EMBL:ABO50589.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001556};
KW Steroid metabolism {ECO:0000256|ARBA:ARBA00023221}.
FT ACT_SITE 155
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR611284-1"
FT BINDING 12..15
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
FT BINDING 90
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
FT BINDING 155..159
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
FT BINDING 188
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
SQ SEQUENCE 247 AA; 25940 MW; 0047365B4F7638BB CRC64;
MFLNGKVAIV TGASRGIGKA IALALAGAQA DIVVNYAGRT EAAEETAAAI REMGRRVLVY
KADVSDAQQV QEMVAATLAE FGKVNILVNN AGITRDNLIL RMKEEDWDSV LSVNLKSAFN
TIKAVARPMV KARSGRIINV SSVVGQYGNA GQANYSAAKA GLIGLTKSMA KELGPRNITV
NAVAPGFIMT DMTEHLTSEA REKMVSSIAL NRLGSPEDVA SMVAFLASDF CGYITGQVIG
IDGGIAM
//
