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P0A2C9 (FABG_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-oxoacyl-[acyl-carrier-protein] reductase FabG
EC=1.1.1.100
Alternative name(s):
3-ketoacyl-acyl carrier protein reductase
Beta-Ketoacyl-acyl carrier protein reductase
Beta-ketoacyl-ACP reductase
Gene names
Name:fabG
Ordered Locus Names:STM1195
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella ›

Protein attributes

Sequence length244 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis. Ref.3

Catalytic activity

(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH.

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subunit structure

Homotetramer By similarity.

Miscellaneous

Calcium ions stabilize the structure, and may inhibit FabG activity by obstructing access to the active site By similarity.

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2442443-oxoacyl-[acyl-carrier-protein] reductase FabG
PRO_0000054681

Regions

Nucleotide binding12 – 154NADP By similarity
Nucleotide binding59 – 602NADP By similarity
Nucleotide binding151 – 1555NADP By similarity

Sites

Active site1511Proton acceptor By similarity
Metal binding501Calcium 1; via carbonyl oxygen; shared with dimeric partner By similarity
Metal binding531Calcium 1; via carbonyl oxygen; shared with dimeric partner By similarity
Metal binding1451Calcium 2 By similarity
Metal binding2331Calcium 3; shared with dimeric partner By similarity
Metal binding2341Calcium 3; via carbonyl oxygen; shared with dimeric partner By similarity
Binding site371NADP By similarity
Binding site861NADP; via carbonyl oxygen By similarity
Binding site1381Substrate By similarity
Binding site1841NADP; via amide nitrogen and carbonyl oxygen By similarity

Experimental info

Mutagenesis1251M → I: Loss of the temperature-sensitive phenotype; when associated with T-223. Ref.3
Mutagenesis2231A → T: Loss of the temperature-sensitive phenotype; when associated with I-125. Ref.3
Mutagenesis2241S → F: Distorts the local conformation and prevent stacking around Phe-221. The S224F mutation would additionally disrupt the hydrogen bond formed between Ser-224 and Glu-226. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P0A2C9 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 86D71DA3E9AF0363

FASTA24425,545
        10         20         30         40         50         60 
MSFEGKIALV TGASRGIGRA IAETLVARGA KVIGTATSEN GAKNISDYLG ANGKGLMLNV 

        70         80         90        100        110        120 
TDPASIESVL ENIRAEFGEV DILVNNAGIT RDNLLMRMKD DEWNDIIETN LSSVFRLSKA 

       130        140        150        160        170        180 
VMRAMMKKRC GRIITIGSVV GTMGNAGQAN YAAAKAGLIG FSKSLAREVA SRGITVNVVA 

       190        200        210        220        230        240 
PGFIETDMTR ALSDDQRAGI LAQVPAGRLG GAQEIASAVA FLASDEASYI TGETLHVNGG 


MYMV

« Hide

References

« Hide 'large scale' references
[1]"Transcriptional analysis of essential genes of the Escherichia coli fatty acid biosynthesis gene cluster by functional replacement with the analogous Salmonella typhimurium gene cluster."
Zhang Y., Cronan J.E. Jr.
J. Bacteriol. 180:3295-3303(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: LT2.
[2]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[3]"Isolation and characterization of beta-ketoacyl-acyl carrier protein reductase (fabG) mutants of Escherichia coli and Salmonella enterica serovar Typhimurium."
Lai C.Y., Cronan J.E.
J. Bacteriol. 186:1869-1878(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN FATTY ACID BIOSYNTHESIS, MUTAGENESIS OF MET-125; ALA-223 AND SER-224.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF044668 Genomic DNA. Translation: AAC38650.1.
AE006468 Genomic DNA. Translation: AAL20124.1.
RefSeqNP_460165.1. NC_003197.1.

3D structure databases

ProteinModelPortalP0A2C9.
SMRP0A2C9. Positions 2-244.
ModBaseSearch...

Protein-protein interaction databases

STRING99287.STM1195.

Proteomic databases

PaxDbP0A2C9.
PRIDEP0A2C9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL20124; AAL20124; STM1195.
GeneID1252713.
KEGGstm:STM1195.
PATRIC32380839. VBISalEnt20916_1264.

Phylogenomic databases

eggNOGCOG1028.
KOK00059.
OMAMSKAVMR.
ProtClustDBPRK05557.

Enzyme and pathway databases

UniPathwayUPA00094.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR011284. 3oxo_ACP_reduc.
IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
TIGRFAMsTIGR01830. 3oxo_ACP_reduc. 1 hit.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFABG_SALTY
AccessionPrimary (citable) accession number: P0A2C9
Secondary accession number(s): O85141
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: May 1, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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