FABG_PSEAE
ID FABG_PSEAE Reviewed; 247 AA.
AC O54438;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
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=PA2967;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10464226; DOI=10.1128/jb.181.17.5498-5504.1999;
RA Kutchma A.J., Hoang T.T., Schweizer H.P.;
RT "Characterization of a Pseudomonas aeruginosa fatty acid biosynthetic gene
RT cluster: purification of acyl carrier protein (ACP) and malonyl-coenzyme
RT A:ACP transacylase (fabD).";
RL J. Bacteriol. 181:5498-5504(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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 -!- 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; U91631; AAB94395.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06355.1; -; Genomic_DNA.
DR PIR; T12020; T12020.
DR RefSeq; NP_251657.1; NC_002516.2.
DR RefSeq; WP_003091137.1; NZ_QZGE01000009.1.
DR PDB; 4AFN; X-ray; 2.30 A; A/B/C/D=1-247.
DR PDB; 4AG3; X-ray; 1.80 A; A/B/C/D=1-247.
DR PDB; 4BNT; X-ray; 2.30 A; A/B/C/D=1-247.
DR PDB; 4BNU; X-ray; 2.00 A; A/B/C/D=1-247.
DR PDB; 4BNV; X-ray; 2.50 A; A/B/C/D=1-247.
DR PDB; 4BNW; X-ray; 1.60 A; A/B/C/D=1-247.
DR PDB; 4BNX; X-ray; 2.30 A; A/B/C/D=1-247.
DR PDB; 4BNY; X-ray; 1.80 A; A/B/C/D=1-247.
DR PDB; 4BNZ; X-ray; 2.50 A; A/B/C/D=1-247.
DR PDB; 4BO0; X-ray; 2.40 A; A/B/C/D=1-247.
DR PDB; 4BO1; X-ray; 2.20 A; A/B/C/D=1-247.
DR PDB; 4BO2; X-ray; 1.90 A; A/B/C/D=1-247.
DR PDB; 4BO3; X-ray; 2.50 A; A/B/C/D=1-247.
DR PDB; 4BO4; X-ray; 2.70 A; A/B/C/D=1-247.
DR PDB; 4BO5; X-ray; 2.60 A; A/B/C/D=1-247.
DR PDB; 4BO6; X-ray; 2.80 A; A/B/C/D=1-247.
DR PDB; 4BO7; X-ray; 2.60 A; A/B/C/D=1-247.
DR PDB; 4BO8; X-ray; 2.70 A; A/B/C/D=1-247.
DR PDB; 4BO9; X-ray; 2.90 A; A/B/C/D=1-247.
DR PDBsum; 4AFN; -.
DR PDBsum; 4AG3; -.
DR PDBsum; 4BNT; -.
DR PDBsum; 4BNU; -.
DR PDBsum; 4BNV; -.
DR PDBsum; 4BNW; -.
DR PDBsum; 4BNX; -.
DR PDBsum; 4BNY; -.
DR PDBsum; 4BNZ; -.
DR PDBsum; 4BO0; -.
DR PDBsum; 4BO1; -.
DR PDBsum; 4BO2; -.
DR PDBsum; 4BO3; -.
DR PDBsum; 4BO4; -.
DR PDBsum; 4BO5; -.
DR PDBsum; 4BO6; -.
DR PDBsum; 4BO7; -.
DR PDBsum; 4BO8; -.
DR PDBsum; 4BO9; -.
DR AlphaFoldDB; O54438; -.
DR SMR; O54438; -.
DR STRING; 287.DR97_4972; -.
DR PaxDb; O54438; -.
DR PRIDE; O54438; -.
DR DNASU; 880433; -.
DR EnsemblBacteria; AAG06355; AAG06355; PA2967.
DR GeneID; 880433; -.
DR KEGG; pae:PA2967; -.
DR PATRIC; fig|208964.12.peg.3113; -.
DR PseudoCAP; PA2967; -.
DR HOGENOM; CLU_010194_1_3_6; -.
DR InParanoid; O54438; -.
DR OMA; KMPERDY; -.
DR PhylomeDB; O54438; -.
DR BioCyc; PAER208964:G1FZ6-3019-MON; -.
DR BRENDA; 1.1.1.100; 5087.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000002438; 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..247
FT /note="3-oxoacyl-[acyl-carrier-protein] reductase FabG"
FT /id="PRO_0000054678"
FT ACT_SITE 154
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 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"
FT TURN 2..5
FT /evidence="ECO:0007829|PDB:4AG3"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:4BNW"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:4BNW"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:4BNW"
FT HELIX 39..50
FT /evidence="ECO:0007829|PDB:4BNW"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:4BNW"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:4BNW"
FT HELIX 66..79
FT /evidence="ECO:0007829|PDB:4BNW"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:4BNW"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:4AG3"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:4BNT"
FT HELIX 106..131
FT /evidence="ECO:0007829|PDB:4BNW"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:4BNW"
FT HELIX 142..146
FT /evidence="ECO:0007829|PDB:4AG3"
FT HELIX 147..172
FT /evidence="ECO:0007829|PDB:4BNW"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:4BNW"
FT STRAND 177..184
FT /evidence="ECO:0007829|PDB:4BNW"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:4AG3"
FT TURN 190..194
FT /evidence="ECO:0007829|PDB:4BNW"
FT HELIX 197..205
FT /evidence="ECO:0007829|PDB:4BNW"
FT HELIX 215..226
FT /evidence="ECO:0007829|PDB:4BNW"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:4BNW"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:4BNW"
SQ SEQUENCE 247 AA; 25585 MW; AB83A2B95027445B CRC64;
MSLQGKVALV TGASRGIGQA IALELGRLGA VVIGTATSAS GAEKIAETLK ANGVEGAGLV
LDVSSDESVA ATLEHIQQHL GQPLIVVNNA GITRDNLLVR MKDDEWFDVV NTNLNSLYRL
SKAVLRGMTK ARWGRIINIG SVVGAMGNAG QTNYAAAKAG LEGFTRALAR EVGSRAITVN
AVAPGFIDTD MTRELPEAQR EALLGQIPLG RLGQAEEIAK VVGFLASDGA AYVTGATVPV
NGGMYMS
