ID A0A0B8Y8P8_9SPHI Unreviewed; 247 AA. AC A0A0B8Y8P8; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 08-NOV-2023, entry version 26. DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase {ECO:0000256|RuleBase:RU366074}; DE EC=1.1.1.100 {ECO:0000256|RuleBase:RU366074}; GN Name=fabG_7 {ECO:0000313|EMBL:KHJ36950.1}; GN ORFNames=PBAC_28680 {ECO:0000313|EMBL:KHJ36950.1}; OS Pedobacter glucosidilyticus. OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pedobacter. OX NCBI_TaxID=1122941 {ECO:0000313|EMBL:KHJ36950.1, ECO:0000313|Proteomes:UP000031461}; RN [1] {ECO:0000313|EMBL:KHJ36950.1, ECO:0000313|Proteomes:UP000031461} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DD6b {ECO:0000313|EMBL:KHJ36950.1, RC ECO:0000313|Proteomes:UP000031461}; RA Poehlein A., Daniel R., Simeonova D.D.; RT "Draft genome sequence of Pedobacter glucosidilyticus DD6b."; RL Submitted (MAY-2014) 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|RuleBase:RU366074}; CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC {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|RuleBase:RU366074}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KHJ36950.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JMTN01000034; KHJ36950.1; -; Genomic_DNA. DR RefSeq; WP_039454302.1; NZ_JMTN01000034.1. DR AlphaFoldDB; A0A0B8Y8P8; -. DR STRING; 1122941.PBAC_28680; -. DR EnsemblBacteria; KHJ36950; KHJ36950; PBAC_28680. DR PATRIC; fig|1122941.3.peg.2876; -. DR OrthoDB; 9803333at2; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000031461; Unassembled WGS sequence. 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 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; NADPH-DEPENDENT REDUCTASE BACG; 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:KHJ36950.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000031461}. FT ACT_SITE 156 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR611284-1" FT BINDING 91 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR611284-2" FT BINDING 156..160 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR611284-2" FT BINDING 189 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR611284-2" SQ SEQUENCE 247 AA; 26495 MW; 23A63005C68B4F1F CRC64; MKLLQGKTAL ITGASKGIGK RIAEKFAEQG ANVAFTYLSS VEKGEALEKE LQQYGTQIKG YRSDASKFAE AEQLINAIVA DFGTIDIVVN NAGITKDGLL MRMSEENWDD VLEVNLKSIF NTTKAASKIM MKNRHGVFIN MSSVVGVQGN AGQSNYAASK AGIIGFSKSI AKELGSRNIR TNVVAPGFIR TEMTAVLDPK VVEGWEKDIP LKRAGETDDV ANVCVFLASD MSAYVNGQVI SVCGGML //