ID FABG_BUCBP Reviewed; 245 AA. AC Q89AG9; DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2003, sequence version 1. DT 27-MAR-2024, entry version 119. 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=bbp_321; OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Buchnera. OX NCBI_TaxID=224915; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bp; RX PubMed=12522265; DOI=10.1073/pnas.0235981100; RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.; RT "Reductive genome evolution in Buchnera aphidicola."; RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003). 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; AE016826; AAO27043.1; -; Genomic_DNA. DR RefSeq; WP_011091444.1; NC_004545.1. DR AlphaFoldDB; Q89AG9; -. DR SMR; Q89AG9; -. DR STRING; 224915.bbp_321; -. DR KEGG; bab:bbp_321; -. DR eggNOG; COG1028; Bacteria. DR HOGENOM; CLU_010194_1_3_6; -. DR OrthoDB; 9804774at2; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000000601; 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: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; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR InterPro; IPR002347; SDR_fam. 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; KW Reference proteome. FT CHAIN 1..245 FT /note="3-oxoacyl-[acyl-carrier-protein] reductase FabG" FT /id="PRO_0000054668" FT ACT_SITE 152 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 38 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 51 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 54 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 60..61 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 87 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 139 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 146 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 152..156 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 185 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" 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" FT BINDING 235 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 245 AA; 26788 MW; 6B94C5520D69157E CRC64; MKTTKKIAVI TGANRGLGKG IAEELSNTNN ITVIGTSTSQ KGCKIINKYL KNNGIGIKLD ITNPNEITKT MDFVYKNFGR VDILINNAGI IRDKLLINMK TQDWNSVLNV NLNSIFYMSK SVIRNMIKNK QGKIITIGSV IAHIGNCGQT NYSAAKLGLV GFHKSLALEL APKGITVNMI APGLIKTGMT NNLSQKQLSK YLSKIPMKRL GTIKEISKIT LFLISNDANY ITGQVIHVNG GMYMP //