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P0AEK2 (FABG_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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

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:b1093, JW1079
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

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.7 Ref.8

Catalytic activity

(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH. Ref.7

Enzyme regulation

Inhibited by cinnamic acid derivatives. Ref.9

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subunit structure

Homotetramer. Ref.10 Ref.11

Miscellaneous

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

Sequence similarities

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

Biophysicochemical properties

pH dependence:

Optimum pH is between 6.0 and 7.0. Ref.6

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2442443-oxoacyl-[acyl-carrier-protein] reductase FabG
PRO_0000054672

Regions

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

Sites

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

Experimental info

Mutagenesis1511Y → F: Defect in the affinity for NADPH. Ref.11
Mutagenesis1541A → T: Decreases in the thermolability of the reductase; when associated with K-233. Ref.8
Mutagenesis1551K → A: Defect in the affinity for NADPH. Ref.11
Mutagenesis2331E → K: Decreases in the thermolability of the reductase; when associated with T-154. Ref.8
Sequence conflict301A → G in AAA23739. Ref.1
Sequence conflict431Q → R in AAA23739. Ref.1

Secondary structure

....................................... 244
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AEK2 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 48EC1F2A7F7EEFD9

FASTA24425,560
        10         20         30         40         50         60 
MNFEGKIALV TGASRGIGRA IAETLAARGA KVIGTATSEN GAQAISDYLG ANGKGLMLNV 

        70         80         90        100        110        120 
TDPASIESVL EKIRAEFGEV DILVNNAGIT RDNLLMRMKD EEWNDIIETN LSSVFRLSKA 

       130        140        150        160        170        180 
VMRAMMKKRH GRIITIGSVV GTMGNGGQAN YAAAKAGLIG FSKSLAREVA SRGITVNVVA 

       190        200        210        220        230        240 
PGFIETDMTR ALSDDQRAGI LAQVPAGRLG GAQEIANAVA FLASDEAAYI TGETLHVNGG 


MYMV 

« Hide

References

« Hide 'large scale' references
[1]"The gene encoding Escherichia coli acyl carrier protein lies within a cluster of fatty acid biosynthetic genes."
Rawlings M., Cronan J.E. Jr.
J. Biol. Chem. 267:5751-5754(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], NOMENCLATURE.
Strain: K12.
[2]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Cloning, nucleotide sequence, and expression of the Escherichia coli fabD gene, encoding malonyl coenzyme A-acyl carrier protein transacylase."
Verwoert I.I.G.S., Verbree E.C., van der Linden K.H., Nijkamp H.J., Stuitje A.R.
J. Bacteriol. 174:2851-2857(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
Strain: K12.
[6]"Studies on the mechanism of fatty acid synthesis. XV. Preparation and general properties of beta-ketoacyl acyl carrier protein reductase from Escherichia coli."
Toomey R.E., Wakil S.J.
Biochim. Biophys. Acta 116:189-197(1966) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
[7]"Inhibition of beta-ketoacyl-acyl carrier protein synthase III (FabH) by acyl-acyl carrier protein in Escherichia coli."
Heath R.J., Rock C.O.
J. Biol. Chem. 271:10996-11000(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A BETA-KETOACYL-ACP REDUCTASE, CATALYTIC ACTIVITY.
[8]"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 AND AS A BETA-KETOACYL-ACP REDUCTASE, MUTAGENESIS OF ALA-154 AND GLU-233.
[9]"Novel inhibitors of beta-ketoacyl-ACP reductase from Escherichia coli."
Kristan K., Bratkovic T., Sova M., Gobec S., Prezelj A., Urleb U.
Chem. Biol. Interact. 178:310-316(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[10]"Structure of beta-ketoacyl-[acyl carrier-protein] reductase from Escherichia coli: negative cooperativity and its structural basis."
Price A.C., Zhang Y.-M., Rock C.O., White S.W.
Biochemistry 40:12772-12781(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), SUBUNIT.
[11]"Cofactor-induced conformational rearrangements establish a catalytically competent active site and a proton relay conduit in FabG."
Price A.C., Zhang Y.M., Rock C.O., White S.W.
Structure 12:417-428(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH NADP, MUTAGENESIS OF TYR-151 AND LYS-155, REACTION MECHANISM, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M84991 Genomic DNA. Translation: AAA23739.1.
U00096 Genomic DNA. Translation: AAC74177.1.
AP009048 Genomic DNA. Translation: BAA35901.1.
M87040 Genomic DNA. Translation: AAA23743.1.
PIRB42147. B64853.
RefSeqNP_415611.1. NC_000913.3.
YP_489361.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1I01X-ray2.60A/B/C/D/E/F/G/H1-244[»]
1Q7BX-ray2.05A/B/C/D1-244[»]
1Q7CX-ray2.50A/B1-244[»]
ProteinModelPortalP0AEK2.
SMRP0AEK2. Positions 2-244.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-31869N.
IntActP0AEK2. 6 interactions.
MINTMINT-1232516.
STRING511145.b1093.

Proteomic databases

PaxDbP0AEK2.
PRIDEP0AEK2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74177; AAC74177; b1093.
BAA35901; BAA35901; BAA35901.
GeneID12931086.
945645.
KEGGecj:Y75_p1063.
eco:b1093.
PATRIC32117427. VBIEscCol129921_1136.

Organism-specific databases

EchoBASEEB1294.
EcoGeneEG11318. fabG.

Phylogenomic databases

eggNOGCOG1028.
KOK00059.
OMATGQELHV.
OrthoDBEOG6N3CR8.
PhylomeDBP0AEK2.
ProtClustDBPRK05557.

Enzyme and pathway databases

BioCycEcoCyc:3-OXOACYL-ACP-REDUCT-MONOMER.
ECOL316407:JW1079-MONOMER.
MetaCyc:3-OXOACYL-ACP-REDUCT-MONOMER.
UniPathwayUPA00094.

Gene expression databases

GenevestigatorP0AEK2.

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...

Other

EvolutionaryTraceP0AEK2.
PROP0AEK2.

Entry information

Entry nameFABG_ECOLI
AccessionPrimary (citable) accession number: P0AEK2
Secondary accession number(s): P25716, P78221, Q47202
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: April 16, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene