FABG_AQUAE
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 03-AUG-2022, entry version 134.
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; 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}.
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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 OMA; KMPERDY; -.
DR OrthoDB; 1601931at2; -.
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 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 PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01830; 3oxo_ACP_reduc; 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
