Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P0AEK2

- FABG_ECOLI

UniProt

P0AEK2 - FABG_ECOLI

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (20 Dec 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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.
    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

    MNFEGKIALV TGASRGIGRA IAETLAARGA KVIGTATSEN GAQAISDYLG    50
    ANGKGLMLNV TDPASIESVL EKIRAEFGEV DILVNNAGIT RDNLLMRMKD 100
    EEWNDIIETN LSSVFRLSKA VMRAMMKKRH GRIITIGSVV GTMGNGGQAN 150
    YAAAKAGLIG FSKSLAREVA SRGITVNVVA PGFIETDMTR ALSDDQRAGI 200
    LAQVPAGRLG GAQEIANAVA FLASDEAAYI TGETLHVNGG MYMV 244
    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.
    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

    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 1, 2014
    This is version 83 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