ID FABG_STAAN Reviewed; 246 AA. AC P99093; Q99QK7; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 04-NOV-2026, entry version 116. 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=SA1074; OS Staphylococcus aureus (strain N315). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=158879; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=11181367; DOI=10.1128/aac.45.3.815-824.2001; RA Kondo N., Kuwahara-Arai K., Kuroda-Murakami H., Tateda-Suzuki E., RA Hiramatsu K.; RT "Eagle-type methicillin resistance: new phenotype of high methicillin RT resistance under mec regulator gene control."; RL Antimicrob. Agents Chemother. 45:815-824(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=N315; RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2; RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y., RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., RA Hiramatsu K.; RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus."; RL Lancet 357:1225-1240(2001). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=N315; RX PubMed=15590099; DOI=10.1016/j.mimet.2004.09.017; RA Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y., RA Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C., RA Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J.; RT "Correlation of proteomic and transcriptomic profiles of Staphylococcus RT aureus during the post-exponential phase of growth."; RL J. Microbiol. Methods 60:247-257(2005). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=N315; RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.; RT "Shotgun proteomic analysis of total and membrane protein extracts of S. RT aureus strain N315."; RL Submitted (OCT-2007) to UniProtKB. 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] + 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 -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC -!- SUBUNIT: Homotetramer. {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; D85817; BAB20935.2; -; Genomic_DNA. DR EMBL; BA000018; BAB42326.1; -; Genomic_DNA. DR PIR; B89896; B89896. DR AlphaFoldDB; P99093; -. DR SMR; P99093; -. DR EnsemblBacteria; BAB42326; BAB42326; BAB42326. DR KEGG; sau:SA1074; -. DR HOGENOM; CLU_010194_1_3_9; -. DR OMA; AAAWKIY; -. DR UniPathway; UPA00094; -. DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; ISS:UniProtKB. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; ISS:UniProtKB. DR GO; GO:0030497; P:fatty acid elongation; ISS:UniProtKB. 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; fabG; 1. DR NCBIfam; NF004198; fabG; 1. DR NCBIfam; NF004199; fabG; 1. DR NCBIfam; NF004200; fabG; 1. DR NCBIfam; NF009466; fabG; 1. DR NCBIfam; NF005559; PRK07231.1; 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 1: Evidence at protein level; KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis; KW Lipid metabolism; NADP; Oxidoreductase. FT CHAIN 1..246 FT /note="3-oxoacyl-[acyl-carrier-protein] reductase FabG" FT /id="PRO_0000054685" FT ACT_SITE 154 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001" FT BINDING 11..14 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 62..63 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 89 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 141 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 154..158 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 187 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" SQ SEQUENCE 246 AA; 26146 MW; 2BD7CA319D3A37C5 CRC64; MKMTKSALVT GASRGIGRSI ALQLAEEGYN VAVNYAGSKE KAEAVVEEIK AKGVDSFAIQ ANVADADEVK AMIKEVVSQF GSLDVLVNNA GITRDNLLMR MKEQEWDDVI DTNLKGVFNC IQKATPQMLR QRSGAIINLS SVVGAVGNPG QANYVATKAG VIGLTKSAAR ELASRGITVN AVAPGFIVSD MTDALSDELK EQMLTQIPLA RFGQDTDIAN TVAFLASDKA KYITGQTIHV NGGMYM //