ID FABG_BUCAP Reviewed; 244 AA. AC Q8K9J5; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 27-MAR-2024, entry version 127. DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase FabG; DE EC=1.1.1.100; DE AltName: Full=3-ketoacyl-acyl carrier protein reductase; DE AltName: Full=Beta-Ketoacyl-acyl carrier protein reductase; DE AltName: Full=Beta-ketoacyl-ACP reductase; GN Name=fabG; OrderedLocusNames=BUsg_339; OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Buchnera. OX NCBI_TaxID=198804; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sg; RX PubMed=12089438; DOI=10.1126/science.1071278; RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.; RT "50 million years of genomic stasis in endosymbiotic bacteria."; RL Science 296:2376-2379(2002). 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. {ECO:0000250}. 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 -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- MISCELLANEOUS: Calcium ions stabilize the structure, and may inhibit CC FabG activity by obstructing access to the active site. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) CC family. {ECO:0000305}. 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; AE013218; AAM67893.1; -; Genomic_DNA. DR RefSeq; WP_011053860.1; NC_004061.1. DR AlphaFoldDB; Q8K9J5; -. DR SMR; Q8K9J5; -. DR STRING; 198804.BUsg_339; -. DR GeneID; 75258781; -. DR KEGG; bas:BUsg_339; -. DR eggNOG; COG1028; Bacteria. DR HOGENOM; CLU_010194_1_3_6; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000000416; Chromosome. DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. 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; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] REDUCTASE FABG; 1. DR Pfam; PF13561; adh_short_C2; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00061; ADH_SHORT; 1. PE 3: Inferred from homology; KW Calcium; Fatty acid biosynthesis; Fatty acid metabolism; KW Lipid biosynthesis; Lipid metabolism; Metal-binding; NADP; Oxidoreductase. FT CHAIN 1..244 FT /note="3-oxoacyl-[acyl-carrier-protein] reductase FabG" FT /id="PRO_0000054667" FT ACT_SITE 151 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001" FT BINDING 12..15 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 37 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 50 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250" FT BINDING 53 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250" FT BINDING 59..60 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 86 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 138 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 145 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 151..155 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 184 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 233 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250" FT BINDING 234 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250" SQ SEQUENCE 244 AA; 26939 MW; 14526C91CDC54D5A CRC64; MKIEKKTALV TGANQGLGKE IAIKLSQKGI QVIGTSTTVD GVKTINKYLK KNGFGFILDL KDTDSILEKM KEICQKKYSI DILINNAGIT SDNLLVYMSN KEWENVIKIN LTSVFYMSKS VIRSMIKKRY GRIVTIGSVI GYLGNRGQIN YSASKSGLIG FHKSLALEVA QKGITVNIVS PGFIKTNLTK NLNVFQYKKH LSKIPMKRIG TAEEIANAVI FLSSEKASYI TGQTIHVNGG MYMT //