ID FABG_AQUAE Reviewed; 248 AA. AC O67610; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 27-MAR-2024, entry version 141. 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=aq_1716; OS Aquifex aeolicus (strain VF5). OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Aquifex. OX NCBI_TaxID=224324; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VF5; RX PubMed=9537320; DOI=10.1038/32831; RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.; RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."; RL Nature 392:353-358(1998). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS), AND SUBUNIT. RG Southeast collaboratory for structural genomics (SECSG); RT "Crystal structure of aq_1716 from Aquifex aeolicus VF5."; RL Submitted (APR-2007) 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] + 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:0000269|Ref.2}. 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; AE000657; AAC07575.1; -; Genomic_DNA. DR PIR; H70447; H70447. DR RefSeq; NP_214176.1; NC_000918.1. DR RefSeq; WP_010881113.1; NC_000918.1. DR PDB; 2P68; X-ray; 1.84 A; A/B=1-248. DR PDB; 2PNF; X-ray; 1.80 A; A/B=1-248. DR PDBsum; 2P68; -. DR PDBsum; 2PNF; -. DR AlphaFoldDB; O67610; -. DR SMR; O67610; -. DR STRING; 224324.aq_1716; -. DR EnsemblBacteria; AAC07575; AAC07575; aq_1716. DR KEGG; aae:aq_1716; -. DR PATRIC; fig|224324.8.peg.1317; -. DR eggNOG; COG1028; Bacteria. DR HOGENOM; CLU_010194_1_3_0; -. DR InParanoid; O67610; -. DR OrthoDB; 9803333at2; -. DR UniPathway; UPA00094; -. DR EvolutionaryTrace; O67610; -. DR Proteomes; UP000000798; 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:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central. 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 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..248 FT /note="3-oxoacyl-[acyl-carrier-protein] reductase FabG" FT /id="PRO_0000054664" FT ACT_SITE 157 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001" FT BINDING 14..17 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 39 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 65..66 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 92 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 144 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 157..161 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 190 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT STRAND 9..12 FT /evidence="ECO:0007829|PDB:2PNF" FT HELIX 18..29 FT /evidence="ECO:0007829|PDB:2PNF" FT STRAND 33..40 FT /evidence="ECO:0007829|PDB:2PNF" FT HELIX 41..55 FT /evidence="ECO:0007829|PDB:2PNF" FT STRAND 59..63 FT /evidence="ECO:0007829|PDB:2PNF" FT HELIX 69..82 FT /evidence="ECO:0007829|PDB:2PNF" FT STRAND 87..91 FT /evidence="ECO:0007829|PDB:2PNF" FT HELIX 101..103 FT /evidence="ECO:0007829|PDB:2PNF" FT HELIX 106..116 FT /evidence="ECO:0007829|PDB:2PNF" FT HELIX 118..127 FT /evidence="ECO:0007829|PDB:2PNF" FT HELIX 129..134 FT /evidence="ECO:0007829|PDB:2PNF" FT STRAND 137..142 FT /evidence="ECO:0007829|PDB:2PNF" FT HELIX 145..149 FT /evidence="ECO:0007829|PDB:2PNF" FT HELIX 155..175 FT /evidence="ECO:0007829|PDB:2PNF" FT HELIX 176..178 FT /evidence="ECO:0007829|PDB:2PNF" FT STRAND 180..187 FT /evidence="ECO:0007829|PDB:2PNF" FT HELIX 193..197 FT /evidence="ECO:0007829|PDB:2PNF" FT HELIX 200..208 FT /evidence="ECO:0007829|PDB:2PNF" FT HELIX 218..229 FT /evidence="ECO:0007829|PDB:2PNF" FT HELIX 231..233 FT /evidence="ECO:0007829|PDB:2PNF" FT STRAND 240..244 FT /evidence="ECO:0007829|PDB:2PNF" SQ SEQUENCE 248 AA; 26867 MW; 5CFD9EB9AD83F2C5 CRC64; MEIKLQGKVS LVTGSTRGIG RAIAEKLASA GSTVIITGTS GERAKAVAEE IANKYGVKAH GVEMNLLSEE SINKAFEEIY NLVDGIDILV NNAGITRDKL FLRMSLLDWE EVLKVNLTGT FLVTQNSLRK MIKQRWGRIV NISSVVGFTG NVGQVNYSTT KAGLIGFTKS LAKELAPRNV LVNAVAPGFI ETDMTAVLSE EIKQKYKEQI PLGRFGSPEE VANVVLFLCS ELASYITGEV IHVNGGMF //