ID FABG_RICPR Reviewed; 241 AA. AC P50941; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 10-JUN-2026, entry version 138. 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=RP762; OS Rickettsia prowazekii (strain Madrid E). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; typhus group. OX NCBI_TaxID=272947; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Madrid E; RX PubMed=9823893; DOI=10.1038/24094; RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., RA Kurland C.G.; RT "The genome sequence of Rickettsia prowazekii and the origin of RT mitochondria."; RL Nature 396:133-140(1998). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41. RC STRAIN=Madrid E; RX PubMed=8132476; DOI=10.1128/jb.176.6.1777-1781.1994; RA Dunkin S.M., Winkler H.H., Wood D.O.; RT "Isolation and characterization of the Rickettsia prowazekii recA gene."; RL J. Bacteriol. 176:1777-1781(1994). RN [3] RP IDENTIFICATION. RX PubMed=8662004; DOI=10.1007/bf02352282; RA Andersson S.G.E., Sharp P.M.; RT "Codon usage and base composition in Rickettsia prowazekii."; RL J. Mol. Evol. 42:525-536(1996). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS), AND SUBUNIT. RG Joint center for structural genomics (JCSG); RT "Crystal structure of 3-ketoacyl-(acyl-carrier-protein) reductase RT Rickettsia prowazekii."; RL Submitted (FEB-2009) to the PDB data bank. 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:0000269|Ref.4}. 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; AJ235273; CAA15190.1; -; Genomic_DNA. DR EMBL; U01959; -; NOT_ANNOTATED_CDS; Unassigned_DNA. DR PIR; F71636; F71636. DR RefSeq; WP_010886363.1; NC_000963.1. DR PDB; 3F9I; X-ray; 2.25 A; A/B=1-241. DR AlphaFoldDB; P50941; -. DR SMR; P50941; -. DR STRING; 272947.gene:17555832; -. DR EnsemblBacteria; CAA15190; CAA15190; CAA15190. DR KEGG; rpr:RP762; -. DR PATRIC; fig|272947.5.peg.798; -. DR eggNOG; COG1028; Bacteria. DR HOGENOM; CLU_010194_1_3_5; -. DR OrthoDB; 9804774at2; -. DR BRENDA; 1.1.1.100; 5447. DR UniPathway; UPA00094; -. DR EvolutionaryTrace; P50941; -. DR Proteomes; UP000002480; Chromosome. 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:000806; 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; NF004199; PRK05653.1-4; 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. DR PDBsum; 3F9I; -. PE 1: Evidence at protein level; KW 3D-structure; Fatty acid biosynthesis; Fatty acid metabolism; KW Lipid biosynthesis; Lipid metabolism; NADP; Oxidoreductase; KW Reference proteome. FT CHAIN 1..241 FT /note="3-oxoacyl-[acyl-carrier-protein] reductase FabG" FT /id="PRO_0000054679" FT ACT_SITE 148 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001" FT BINDING 13..16 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 57..58 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 83 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 135 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 148..152 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 181 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT STRAND 8..11 FT /evidence="ECO:0007829|PDB:3F9I" FT TURN 12..15 FT /evidence="ECO:0007829|PDB:3F9I" FT HELIX 17..28 FT /evidence="ECO:0007829|PDB:3F9I" FT STRAND 32..38 FT /evidence="ECO:0007829|PDB:3F9I" FT HELIX 40..50 FT /evidence="ECO:0007829|PDB:3F9I" FT STRAND 52..58 FT /evidence="ECO:0007829|PDB:3F9I" FT HELIX 64..72 FT /evidence="ECO:0007829|PDB:3F9I" FT STRAND 78..82 FT /evidence="ECO:0007829|PDB:3F9I" FT HELIX 100..104 FT /evidence="ECO:0007829|PDB:3F9I" FT HELIX 105..109 FT /evidence="ECO:0007829|PDB:3F9I" FT HELIX 110..125 FT /evidence="ECO:0007829|PDB:3F9I" FT STRAND 128..133 FT /evidence="ECO:0007829|PDB:3F9I" FT HELIX 134..137 FT /evidence="ECO:0007829|PDB:3F9I" FT HELIX 146..166 FT /evidence="ECO:0007829|PDB:3F9I" FT HELIX 167..169 FT /evidence="ECO:0007829|PDB:3F9I" FT STRAND 171..178 FT /evidence="ECO:0007829|PDB:3F9I" FT HELIX 191..200 FT /evidence="ECO:0007829|PDB:3F9I" FT HELIX 209..220 FT /evidence="ECO:0007829|PDB:3F9I" FT HELIX 222..224 FT /evidence="ECO:0007829|PDB:3F9I" FT STRAND 231..235 FT /evidence="ECO:0007829|PDB:3F9I" SQ SEQUENCE 241 AA; 25759 MW; E43B8711545B8295 CRC64; MIDLTGKTSL ITGASSGIGS AIARLLHKLG SKVIISGSNE EKLKSLGNAL KDNYTIEVCN LANKEECSNL ISKTSNLDIL VCNAGITSDT LAIRMKDQDF DKVIDINLKA NFILNREAIK KMIQKRYGRI INISSIVGIA GNPGQANYCA SKAGLIGMTK SLSYEVATRG ITVNAVAPGF IKSDMTDKLN EKQREAIVQK IPLGTYGIPE DVAYAVAFLA SNNASYITGQ TLHVNGGMLM V //