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P0A6Q3

- FABA_ECOLI

UniProt

P0A6Q3 - FABA_ECOLI

Protein

3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase

Gene

fabA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length. Is inactive in the dehydration of long chain unsaturated beta-hydroxyacyl-ACP.1 Publication

    Catalytic activityi

    A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl-carrier protein] + H2O.1 Publication
    (3R)-3-hydroxydecanoyl-[acyl-carrier-protein] = trans-dec-2-enoyl-[acyl-carrier-protein] + H2O.1 Publication
    Trans-dec-2-enoyl-[acyl-carrier-protein] = cis-dec-3-enoyl-[acyl-carrier-protein].1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei71 – 711

    GO - Molecular functioni

    1. 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity Source: EcoCyc
    2. 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity Source: EcoCyc
    3. trans-2-decenoyl-acyl-carrier-protein isomerase activity Source: EcoCyc

    GO - Biological processi

    1. fatty acid biosynthetic process Source: EcoCyc
    2. lipid biosynthetic process Source: EcoliWiki

    Keywords - Molecular functioni

    Isomerase, Lyase

    Keywords - Biological processi

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

    Enzyme and pathway databases

    BioCyciEcoCyc:FABA-MONOMER.
    ECOL316407:JW0937-MONOMER.
    MetaCyc:FABA-MONOMER.
    BRENDAi5.3.3.14. 2026.
    UniPathwayiUPA00094.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase (EC:4.2.1.59)
    Alternative name(s):
    3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabA
    Beta-hydroxydecanoyl thioester dehydrase
    Trans-2-decenoyl-[acyl-carrier-protein] isomerase (EC:5.3.3.14)
    Gene namesi
    Name:fabA
    Ordered Locus Names:b0954, JW0937
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10273. fabA.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 1721713-hydroxydecanoyl-[acyl-carrier-protein] dehydratasePRO_0000091594Add
    BLAST

    Proteomic databases

    PaxDbiP0A6Q3.
    PRIDEiP0A6Q3.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A6Q3.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    DIPiDIP-31864N.
    IntActiP0A6Q3. 29 interactions.
    MINTiMINT-1218658.
    STRINGi511145.b0954.

    Structurei

    Secondary structure

    1
    172
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 178
    Beta strandi24 – 263
    Turni32 – 343
    Beta strandi38 – 469
    Turni48 – 514
    Beta strandi54 – 607
    Helixi66 – 705
    Turni71 – 744
    Helixi80 – 9718
    Beta strandi102 – 1109
    Beta strandi112 – 1143
    Beta strandi124 – 15027
    Beta strandi153 – 16614
    Helixi169 – 1713

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MKAX-ray2.00A/B2-172[»]
    1MKBX-ray2.00A/B2-172[»]
    4KEHX-ray1.90A/B2-172[»]
    ProteinModelPortaliP0A6Q3.
    SMRiP0A6Q3. Positions 2-167.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A6Q3.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0764.
    HOGENOMiHOG000277828.
    KOiK01716.
    OMAiMGIADAT.
    OrthoDBiEOG6VB6SH.
    PhylomeDBiP0A6Q3.

    Family and domain databases

    Gene3Di3.10.129.10. 1 hit.
    HAMAPiMF_00405. FabA.
    InterProiIPR010083. FabA.
    IPR013114. FabA_FabZ.
    IPR029069. HotDog_dom.
    [Graphical view]
    PfamiPF07977. FabA. 1 hit.
    [Graphical view]
    SUPFAMiSSF54637. SSF54637. 1 hit.
    TIGRFAMsiTIGR01749. fabA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0A6Q3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVDKRESYTK EDLLASGRGE LFGAKGPQLP APNMLMMDRV VKMTETGGNF    50
    DKGYVEAELD INPDLWFFGC HFIGDPVMPG CLGLDAMWQL VGFYLGWLGG 100
    EGKGRALGVG EVKFTGQVLP TAKKVTYRIH FKRIVNRRLI MGLADGEVLV 150
    DGRLIYTASD LKVGLFQDTS AF 172
    Length:172
    Mass (Da):18,969
    Last modified:January 23, 2007 - v2
    Checksum:iDFC508352D2DCF2C
    GO

    Sequence cautioni

    The sequence AAA96496.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti76 – 761P → L in allele FABA6; TS.
    Natural varianti102 – 1021G → D in allele FABA2; TS.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03186 Genomic DNA. Translation: AAA96496.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC74040.1.
    AP009048 Genomic DNA. Translation: BAA35712.1.
    U37057 Genomic DNA. Translation: AAC44389.1.
    U56977 Genomic DNA. Translation: AAC44399.1.
    PIRiA64836. DWECHD.
    RefSeqiNP_415474.1. NC_000913.3.
    YP_489226.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74040; AAC74040; b0954.
    BAA35712; BAA35712; BAA35712.
    GeneIDi12934245.
    945568.
    KEGGiecj:Y75_p0926.
    eco:b0954.
    PATRICi32117127. VBIEscCol129921_0988.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03186 Genomic DNA. Translation: AAA96496.1 . Different initiation.
    U00096 Genomic DNA. Translation: AAC74040.1 .
    AP009048 Genomic DNA. Translation: BAA35712.1 .
    U37057 Genomic DNA. Translation: AAC44389.1 .
    U56977 Genomic DNA. Translation: AAC44399.1 .
    PIRi A64836. DWECHD.
    RefSeqi NP_415474.1. NC_000913.3.
    YP_489226.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MKA X-ray 2.00 A/B 2-172 [» ]
    1MKB X-ray 2.00 A/B 2-172 [» ]
    4KEH X-ray 1.90 A/B 2-172 [» ]
    ProteinModelPortali P0A6Q3.
    SMRi P0A6Q3. Positions 2-167.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-31864N.
    IntActi P0A6Q3. 29 interactions.
    MINTi MINT-1218658.
    STRINGi 511145.b0954.

    Proteomic databases

    PaxDbi P0A6Q3.
    PRIDEi P0A6Q3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74040 ; AAC74040 ; b0954 .
    BAA35712 ; BAA35712 ; BAA35712 .
    GeneIDi 12934245.
    945568.
    KEGGi ecj:Y75_p0926.
    eco:b0954.
    PATRICi 32117127. VBIEscCol129921_0988.

    Organism-specific databases

    EchoBASEi EB0269.
    EcoGenei EG10273. fabA.

    Phylogenomic databases

    eggNOGi COG0764.
    HOGENOMi HOG000277828.
    KOi K01716.
    OMAi MGIADAT.
    OrthoDBi EOG6VB6SH.
    PhylomeDBi P0A6Q3.

    Enzyme and pathway databases

    UniPathwayi UPA00094 .
    BioCyci EcoCyc:FABA-MONOMER.
    ECOL316407:JW0937-MONOMER.
    MetaCyc:FABA-MONOMER.
    BRENDAi 5.3.3.14. 2026.

    Miscellaneous databases

    EvolutionaryTracei P0A6Q3.
    PROi P0A6Q3.

    Gene expression databases

    Genevestigatori P0A6Q3.

    Family and domain databases

    Gene3Di 3.10.129.10. 1 hit.
    HAMAPi MF_00405. FabA.
    InterProi IPR010083. FabA.
    IPR013114. FabA_FabZ.
    IPR029069. HotDog_dom.
    [Graphical view ]
    Pfami PF07977. FabA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54637. SSF54637. 1 hit.
    TIGRFAMsi TIGR01749. fabA. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Derived amino acid sequence and identification of active site residues of Escherichia coli beta-hydroxydecanoyl thioester dehydrase."
      Cronan J.E. Jr., Li W.-B., Coleman R., Narasimhan M., de Mendoza D., Schwab J.M.
      J. Biol. Chem. 263:4641-4646(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: K12.
    2. "A new mechanism of transcriptional regulation: release of an activator triggered by small molecule binding."
      Henry M.F., Cronan J.E. Jr.
      Cell 70:671-679(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 170-172.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "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.
    6. "Increased unsaturated fatty acid production associated with a suppressor of the fabA6(Ts) mutation in Escherichia coli."
      Rock C.O., Tsay J.-T., Heath R., Jackowski S.
      J. Bacteriol. 178:5382-5387(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTANTS FABA6 AND FABA2.
      Strain: K12.
    7. "Roles of the FabA and FabZ beta-hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis."
      Heath R.J., Rock C.O.
      J. Biol. Chem. 271:27795-27801(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
    8. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    9. "Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site."
      Leesong M., Henderson B.S., Gillig J.R., Schwab J.M., Smith J.L.
      Structure 4:253-264(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

    Entry informationi

    Entry nameiFABA_ECOLI
    AccessioniPrimary (citable) accession number: P0A6Q3
    Secondary accession number(s): P18391, Q59383
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 91 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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