FABG_VIBCH
ID FABG_VIBCH Reviewed; 244 AA.
AC Q9KQH7;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 133.
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=VC_2021;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(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 -!- SEQUENCE CAUTION:
CC Sequence=AAF95169.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE003852; AAF95169.1; ALT_INIT; Genomic_DNA.
DR PIR; F82128; F82128.
DR RefSeq; NP_231655.1; NC_002505.1.
DR RefSeq; WP_001918744.1; NZ_LT906614.1.
DR PDB; 3RRO; X-ray; 2.00 A; A/B=1-244.
DR PDB; 3RSH; X-ray; 1.95 A; A/B=1-244.
DR PDB; 3U09; X-ray; 1.75 A; A/B=1-244.
DR PDB; 4I08; X-ray; 2.06 A; A/B=1-244.
DR PDB; 4WJZ; X-ray; 2.40 A; A/B/C/D=1-244.
DR PDB; 5END; X-ray; 2.55 A; A/B=1-244.
DR PDBsum; 3RRO; -.
DR PDBsum; 3RSH; -.
DR PDBsum; 3U09; -.
DR PDBsum; 4I08; -.
DR PDBsum; 4WJZ; -.
DR PDBsum; 5END; -.
DR AlphaFoldDB; Q9KQH7; -.
DR SMR; Q9KQH7; -.
DR STRING; 243277.VC_2021; -.
DR PRIDE; Q9KQH7; -.
DR DNASU; 2613400; -.
DR EnsemblBacteria; AAF95169; AAF95169; VC_2021.
DR GeneID; 57740642; -.
DR GeneID; 66940451; -.
DR KEGG; vch:VC_2021; -.
DR PATRIC; fig|243277.26.peg.1931; -.
DR eggNOG; COG1028; Bacteria.
DR HOGENOM; CLU_010194_1_3_6; -.
DR OMA; KMPERDY; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000000584; Chromosome 1.
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..244
FT /note="3-oxoacyl-[acyl-carrier-protein] reductase FabG"
FT /id="PRO_0000054694"
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 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 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 STRAND 7..12
FT /evidence="ECO:0007829|PDB:3U09"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:3U09"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:3U09"
FT HELIX 39..49
FT /evidence="ECO:0007829|PDB:3U09"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:3U09"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:3U09"
FT HELIX 63..77
FT /evidence="ECO:0007829|PDB:3U09"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:3U09"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:3U09"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:3U09"
FT HELIX 112..128
FT /evidence="ECO:0007829|PDB:3U09"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:3U09"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:3U09"
FT HELIX 149..169
FT /evidence="ECO:0007829|PDB:3U09"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:3U09"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:3U09"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:4I08"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:3U09"
FT HELIX 194..201
FT /evidence="ECO:0007829|PDB:3U09"
FT HELIX 212..223
FT /evidence="ECO:0007829|PDB:3U09"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:3U09"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:3U09"
SQ SEQUENCE 244 AA; 25566 MW; 9FB2E8278D7CC3CE CRC64;
MNLEGKVALV TGASRGIGKA IAELLAERGA KVIGTATSES GAQAISDYLG DNGKGMALNV
TNPESIEAVL KAITDEFGGV DILVNNAGIT RDNLLMRMKE EEWSDIMETN LTSIFRLSKA
VLRGMMKKRQ GRIINVGSVV GTMGNAGQAN YAAAKAGVIG FTKSMAREVA SRGVTVNTVA
PGFIETDMTK ALNDEQRTAT LAQVPAGRLG DPREIASAVA FLASPEAAYI TGETLHVNGG
MYMI
