FABG_SALTY
ID FABG_SALTY Reviewed; 244 AA.
AC P0A2C9; O85141;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=STM1195;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=9642179; DOI=10.1128/jb.180.13.3295-3303.1998;
RA Zhang Y., Cronan J.E. Jr.;
RT "Transcriptional analysis of essential genes of the Escherichia coli fatty
RT acid biosynthesis gene cluster by functional replacement with the analogous
RT Salmonella typhimurium gene cluster.";
RL J. Bacteriol. 180:3295-3303(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION IN FATTY ACID BIOSYNTHESIS, AND MUTAGENESIS OF MET-125; ALA-223
RP AND SER-224.
RX PubMed=14996818; DOI=10.1128/jb.186.6.1869-1878.2004;
RA Lai C.Y., Cronan J.E.;
RT "Isolation and characterization of beta-ketoacyl-acyl carrier protein
RT reductase (fabG) mutants of Escherichia coli and Salmonella enterica
RT serovar Typhimurium.";
RL J. Bacteriol. 186:1869-1878(2004).
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.
CC {ECO:0000269|PubMed:14996818}.
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 -!- MISCELLANEOUS: Calcium ions stabilize the structure, and may inhibit
CC FabG activity by obstructing access to the active site. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AF044668; AAC38650.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20124.1; -; Genomic_DNA.
DR RefSeq; NP_460165.1; NC_003197.2.
DR RefSeq; WP_000007236.1; NC_003197.2.
DR PDB; 6T5X; X-ray; 1.50 A; A/B=1-244.
DR PDB; 6T7M; X-ray; 2.65 A; A/B/C/D=1-244.
DR PDBsum; 6T5X; -.
DR PDBsum; 6T7M; -.
DR AlphaFoldDB; P0A2C9; -.
DR SMR; P0A2C9; -.
DR STRING; 99287.STM1195; -.
DR PaxDb; P0A2C9; -.
DR PRIDE; P0A2C9; -.
DR EnsemblBacteria; AAL20124; AAL20124; STM1195.
DR GeneID; 1252713; -.
DR GeneID; 66755598; -.
DR KEGG; stm:STM1195; -.
DR PATRIC; fig|99287.12.peg.1264; -.
DR HOGENOM; CLU_010194_1_3_6; -.
DR OMA; KMPERDY; -.
DR PhylomeDB; P0A2C9; -.
DR BioCyc; SENT99287:STM1195-MON; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IMP: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; Calcium; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Metal-binding; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..244
FT /note="3-oxoacyl-[acyl-carrier-protein] reductase FabG"
FT /id="PRO_0000054681"
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 50
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="ligand shared between dimeric partners"
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 145
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 BINDING 233
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT MUTAGEN 125
FT /note="M->I: Loss of the temperature-sensitive phenotype;
FT when associated with T-223."
FT /evidence="ECO:0000269|PubMed:14996818"
FT MUTAGEN 223
FT /note="A->T: Loss of the temperature-sensitive phenotype;
FT when associated with I-125."
FT /evidence="ECO:0000269|PubMed:14996818"
FT MUTAGEN 224
FT /note="S->F: Distorts the local conformation and prevent
FT stacking around Phe-221. The S224F mutation would
FT additionally disrupt the hydrogen bond formed between Ser-
FT 224 and Glu-226."
FT /evidence="ECO:0000269|PubMed:14996818"
FT TURN 2..5
FT /evidence="ECO:0007829|PDB:6T7M"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:6T5X"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:6T5X"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:6T5X"
FT HELIX 39..49
FT /evidence="ECO:0007829|PDB:6T5X"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:6T5X"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:6T5X"
FT HELIX 63..76
FT /evidence="ECO:0007829|PDB:6T5X"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:6T5X"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:6T5X"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:6T5X"
FT HELIX 112..128
FT /evidence="ECO:0007829|PDB:6T5X"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:6T5X"
FT HELIX 139..143
FT /evidence="ECO:0007829|PDB:6T5X"
FT HELIX 149..169
FT /evidence="ECO:0007829|PDB:6T5X"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:6T5X"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:6T5X"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:6T5X"
FT TURN 187..191
FT /evidence="ECO:0007829|PDB:6T5X"
FT HELIX 194..202
FT /evidence="ECO:0007829|PDB:6T5X"
FT HELIX 212..223
FT /evidence="ECO:0007829|PDB:6T5X"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:6T5X"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:6T5X"
SQ SEQUENCE 244 AA; 25545 MW; 86D71DA3E9AF0363 CRC64;
MSFEGKIALV TGASRGIGRA IAETLVARGA KVIGTATSEN GAKNISDYLG ANGKGLMLNV
TDPASIESVL ENIRAEFGEV DILVNNAGIT RDNLLMRMKD DEWNDIIETN LSSVFRLSKA
VMRAMMKKRC GRIITIGSVV GTMGNAGQAN YAAAKAGLIG FSKSLAREVA SRGITVNVVA
PGFIETDMTR ALSDDQRAGI LAQVPAGRLG GAQEIASAVA FLASDEASYI TGETLHVNGG
MYMV
