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P0AEK2

- FABG_ECOLI

UniProt

P0AEK2 - FABG_ECOLI

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Protein

3-oxoacyl-[acyl-carrier-protein] reductase FabG

Gene

fabG

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH.1 Publication

Enzyme regulationi

Inhibited by cinnamic acid derivatives.1 Publication

pH dependencei

Optimum pH is between 6.0 and 7.0.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei37 – 371NADP1 Publication
Metal bindingi50 – 501Calcium 1; via carbonyl oxygen; shared with dimeric partner
Metal bindingi53 – 531Calcium 1; via carbonyl oxygen; shared with dimeric partner
Binding sitei86 – 861NADP; via carbonyl oxygen1 Publication
Binding sitei138 – 1381SubstrateBy similarity
Metal bindingi145 – 1451Calcium 2
Active sitei151 – 1511Proton acceptorPROSITE-ProRule annotation
Binding sitei184 – 1841NADP; via amide nitrogen and carbonyl oxygen1 Publication
Metal bindingi233 – 2331Calcium 3; shared with dimeric partner
Metal bindingi234 – 2341Calcium 3; via carbonyl oxygen; shared with dimeric partner

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 154NADP1 Publication
Nucleotide bindingi59 – 602NADP1 Publication
Nucleotide bindingi151 – 1555NADP1 Publication

GO - Molecular functioni

  1. 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity Source: UniProtKB
  2. identical protein binding Source: EcoCyc
  3. metal ion binding Source: UniProtKB-KW
  4. NAD binding Source: InterPro
  5. NADP binding Source: UniProtKB

GO - Biological processi

  1. biotin biosynthetic process Source: EcoCyc
  2. fatty acid biosynthetic process Source: EcoCyc
  3. fatty acid elongation Source: UniProtKB
  4. lipid biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding, NADP

Enzyme and pathway databases

BioCyciEcoCyc:3-OXOACYL-ACP-REDUCT-MONOMER.
ECOL316407:JW1079-MONOMER.
MetaCyc:3-OXOACYL-ACP-REDUCT-MONOMER.
UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:fabG
Ordered Locus Names:b1093, JW1079
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11318. fabG.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi151 – 1511Y → F: Defect in the affinity for NADPH. 1 Publication
Mutagenesisi154 – 1541A → T: Decreases in the thermolability of the reductase; when associated with K-233. 1 Publication
Mutagenesisi155 – 1551K → A: Defect in the affinity for NADPH. 1 Publication
Mutagenesisi233 – 2331E → K: Decreases in the thermolability of the reductase; when associated with T-154. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2442443-oxoacyl-[acyl-carrier-protein] reductase FabGPRO_0000054672Add
BLAST

Proteomic databases

PaxDbiP0AEK2.
PRIDEiP0AEK2.

Expressioni

Gene expression databases

GenevestigatoriP0AEK2.

Interactioni

Subunit structurei

Homotetramer.2 Publications

Protein-protein interaction databases

DIPiDIP-31869N.
IntActiP0AEK2. 6 interactions.
MINTiMINT-1232516.
STRINGi511145.b1093.

Structurei

Secondary structure

1
244
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 126
Helixi16 – 2712
Beta strandi31 – 388
Helixi39 – 4911
Helixi50 – 523
Beta strandi53 – 575
Helixi63 – 7614
Beta strandi81 – 855
Helixi95 – 973
Helixi100 – 11011
Helixi112 – 12817
Beta strandi131 – 1366
Helixi139 – 1435
Helixi149 – 16921
Helixi170 – 1723
Beta strandi174 – 1818
Helixi187 – 1904
Helixi194 – 2018
Helixi212 – 22312
Helixi225 – 2273
Beta strandi234 – 2385

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP0AEK2.
SMRiP0AEK2. Positions 2-244.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AEK2.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1028.
InParanoidiP0AEK2.
KOiK00059.
OMAiDEFGAID.
OrthoDBiEOG6N3CR8.
PhylomeDBiP0AEK2.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR011284. 3oxo_ACP_reduc.
IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
TIGRFAMsiTIGR01830. 3oxo_ACP_reduc. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AEK2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNFEGKIALV TGASRGIGRA IAETLAARGA KVIGTATSEN GAQAISDYLG
60 70 80 90 100
ANGKGLMLNV TDPASIESVL EKIRAEFGEV DILVNNAGIT RDNLLMRMKD
110 120 130 140 150
EEWNDIIETN LSSVFRLSKA VMRAMMKKRH GRIITIGSVV GTMGNGGQAN
160 170 180 190 200
YAAAKAGLIG FSKSLAREVA SRGITVNVVA PGFIETDMTR ALSDDQRAGI
210 220 230 240
LAQVPAGRLG GAQEIANAVA FLASDEAAYI TGETLHVNGG MYMV
Length:244
Mass (Da):25,560
Last modified:December 20, 2005 - v1
Checksum:i48EC1F2A7F7EEFD9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301A → G in AAA23739. (PubMed:1556094)Curated
Sequence conflicti43 – 431Q → R in AAA23739. (PubMed:1556094)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M84991 Genomic DNA. Translation: AAA23739.1.
U00096 Genomic DNA. Translation: AAC74177.1.
AP009048 Genomic DNA. Translation: BAA35901.1.
M87040 Genomic DNA. Translation: AAA23743.1.
PIRiB64853. B42147.
RefSeqiNP_415611.1. NC_000913.3.
YP_489361.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74177; AAC74177; b1093.
BAA35901; BAA35901; BAA35901.
GeneIDi12931086.
945645.
KEGGiecj:Y75_p1063.
eco:b1093.
PATRICi32117427. VBIEscCol129921_1136.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M84991 Genomic DNA. Translation: AAA23739.1 .
U00096 Genomic DNA. Translation: AAC74177.1 .
AP009048 Genomic DNA. Translation: BAA35901.1 .
M87040 Genomic DNA. Translation: AAA23743.1 .
PIRi B64853. B42147.
RefSeqi NP_415611.1. NC_000913.3.
YP_489361.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1I01 X-ray 2.60 A/B/C/D/E/F/G/H 1-244 [» ]
1Q7B X-ray 2.05 A/B/C/D 1-244 [» ]
1Q7C X-ray 2.50 A/B 1-244 [» ]
ProteinModelPortali P0AEK2.
SMRi P0AEK2. Positions 2-244.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-31869N.
IntActi P0AEK2. 6 interactions.
MINTi MINT-1232516.
STRINGi 511145.b1093.

Proteomic databases

PaxDbi P0AEK2.
PRIDEi P0AEK2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74177 ; AAC74177 ; b1093 .
BAA35901 ; BAA35901 ; BAA35901 .
GeneIDi 12931086.
945645.
KEGGi ecj:Y75_p1063.
eco:b1093.
PATRICi 32117427. VBIEscCol129921_1136.

Organism-specific databases

EchoBASEi EB1294.
EcoGenei EG11318. fabG.

Phylogenomic databases

eggNOGi COG1028.
InParanoidi P0AEK2.
KOi K00059.
OMAi DEFGAID.
OrthoDBi EOG6N3CR8.
PhylomeDBi P0AEK2.

Enzyme and pathway databases

UniPathwayi UPA00094 .
BioCyci EcoCyc:3-OXOACYL-ACP-REDUCT-MONOMER.
ECOL316407:JW1079-MONOMER.
MetaCyc:3-OXOACYL-ACP-REDUCT-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0AEK2.
PROi P0AEK2.

Gene expression databases

Genevestigatori P0AEK2.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR011284. 3oxo_ACP_reduc.
IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view ]
Pfami PF00106. adh_short. 1 hit.
[Graphical view ]
PRINTSi PR00081. GDHRDH.
PR00080. SDRFAMILY.
TIGRFAMsi TIGR01830. 3oxo_ACP_reduc. 1 hit.
PROSITEi PS00061. ADH_SHORT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. 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.

Entry informationi

Entry nameiFABG_ECOLI
AccessioniPrimary (citable) accession number: P0AEK2
Secondary accession number(s): P25716, P78221, Q47202
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: October 29, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3