ID FABG_SHIFL Reviewed; 244 AA. AC P0AEK3; P25716; P78221; Q47202; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 1. DT 27-MAR-2024, entry version 118. 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=SF1097, S1177; OS Shigella flexneri. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=623; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=301 / Serotype 2a; RX PubMed=12384590; DOI=10.1093/nar/gkf566; RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.; RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity RT through comparison with genomes of Escherichia coli K12 and O157."; RL Nucleic Acids Res. 30:4432-4441(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700930 / 2457T / Serotype 2a; RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003; RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.; RT "Complete genome sequence and comparative genomics of Shigella flexneri RT serotype 2a strain 2457T."; RL Infect. Immun. 71:2775-2786(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; AE005674; AAN42716.1; -; Genomic_DNA. DR EMBL; AE014073; AAP16604.1; -; Genomic_DNA. DR RefSeq; NP_707009.1; NC_004337.2. DR RefSeq; WP_001008535.1; NZ_WPGW01000001.1. DR AlphaFoldDB; P0AEK3; -. DR SMR; P0AEK3; -. DR STRING; 198214.SF1097; -. DR PaxDb; 198214-SF1097; -. DR GeneID; 1026267; -. DR GeneID; 75203679; -. DR KEGG; sfl:SF1097; -. DR KEGG; sfx:S1177; -. DR PATRIC; fig|198214.7.peg.1285; -. DR HOGENOM; CLU_010194_1_3_6; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000001006; Chromosome. DR Proteomes; UP000002673; Chromosome. DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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 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 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 Calcium; Fatty acid biosynthesis; Fatty acid metabolism; KW Lipid biosynthesis; Lipid metabolism; Metal-binding; NADP; Oxidoreductase; KW Reference proteome. FT CHAIN 1..244 FT /note="3-oxoacyl-[acyl-carrier-protein] reductase FabG" FT /id="PRO_0000054682" 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; 25560 MW; 48EC1F2A7F7EEFD9 CRC64; MNFEGKIALV TGASRGIGRA IAETLAARGA KVIGTATSEN GAQAISDYLG ANGKGLMLNV TDPASIESVL EKIRAEFGEV DILVNNAGIT RDNLLMRMKD EEWNDIIETN LSSVFRLSKA VMRAMMKKRH GRIITIGSVV GTMGNGGQAN YAAAKAGLIG FSKSLAREVA SRGITVNVVA PGFIETDMTR ALSDDQRAGI LAQVPAGRLG GAQEIANAVA FLASDEAAYI TGETLHVNGG MYMV //