ID A2SDG1_METPP Unreviewed; 249 AA. AC A2SDG1; DT 06-MAR-2007, integrated into UniProtKB/TrEMBL. DT 06-MAR-2007, sequence version 1. DT 02-SEP-2026, entry version 107. DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase {ECO:0000256|ARBA:ARBA00012948, ECO:0000256|RuleBase:RU366074}; DE EC=1.1.1.100 {ECO:0000256|ARBA:ARBA00012948, ECO:0000256|RuleBase:RU366074}; GN OrderedLocusNames=Mpe_A0638 {ECO:0000313|EMBL:ABM93600.1}; OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; Sphaerotilaceae; Methylibium. OX NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM93600.1, ECO:0000313|Proteomes:UP000000366}; RN [1] {ECO:0000313|EMBL:ABM93600.1, ECO:0000313|Proteomes:UP000000366} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1 RC {ECO:0000313|Proteomes:UP000000366}; RX PubMed=17158667; DOI=10.1128/JB.01259-06; RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W., RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M., RA Hristova K.R.; RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta- RT proteobacterium Methylibium petroleiphilum PM1."; RL J. Bacteriol. 189:1931-1945(2007). 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] + NADPH CC + H(+); 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|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}. 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; CP000555; ABM93600.1; -; Genomic_DNA. DR RefSeq; WP_011828238.1; NC_008825.1. DR AlphaFoldDB; A2SDG1; -. DR STRING; 420662.Mpe_A0638; -. DR KEGG; mpt:Mpe_A0638; -. DR eggNOG; COG1028; Bacteria. DR HOGENOM; CLU_010194_1_3_4; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000000366; 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:0030497; P:fatty acid elongation; IEA:UniProtKB-ARBA. DR CDD; cd05333; BKR_SDR_c; 1. DR FunFam; 3.40.50.720:FF:000037; 3-oxoacyl-[acyl-carrier-protein] reductase FabG; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR011284; 3oxo_ACP_reduc. DR InterPro; IPR057326; KR_dom. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR InterPro; IPR050259; SDR. DR InterPro; IPR002347; SDR_fam. DR NCBIfam; TIGR01830; 3oxo_ACP_reduc; 1. DR NCBIfam; NF004197; PRK05653.1-1; 1. DR NCBIfam; NF005559; PRK07231.1; 1. DR NCBIfam; NF009466; PRK12826.1-2; 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|ARBA:ARBA00023160, KW ECO:0000256|RuleBase:RU366074}; KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, KW ECO:0000256|RuleBase:RU366074}; KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, KW ECO:0000256|RuleBase:RU366074}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, KW ECO:0000256|RuleBase:RU366074}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR611284-2}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU366074}; KW Reference proteome {ECO:0000313|Proteomes:UP000000366}. FT DOMAIN 10..192 FT /note="Ketoreductase" FT /evidence="ECO:0000259|SMART:SM00822" FT ACT_SITE 156 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR611284-1, FT ECO:0000256|PROSITE-ProRule:PRU10001" FT BINDING 16..19 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR611284-2" FT BINDING 41 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR611284-2" FT BINDING 64..65 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR611284-2" 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 249 AA; 25450 MW; 761B9319B913BAEC CRC64; MSADASVTTQ VALVTGASRG IGRAIATTLA ERGFKVVGTA TSESGAAAIG EALAPLGGRG LVLNVNDGAA LEAAVDTIVK QDGGLHVLVN NAGITRDTLS MRMKDDDWDA VLDTNLKAVF RASRAVIRPM MKQRYGRIVN ITSVVGASGN PGQANYAAAK AGVAGMTRSL ARELGSRGIT VNCVAPGFIA TDMTDGLPEA QKAALLGQIP LGRLGAPEEI ADAVAFLASR QAGYITGTEL HVNGGMFMN //