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Q8XDR6

- LCFA_ECO57

UniProt

Q8XDR6 - LCFA_ECO57

Protein

Long-chain-fatty-acid--CoA ligase

Gene

fadD

Organism
Escherichia coli O157:H7
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      Previous versions | rss
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    Functioni

    Catalyzes the esterification, concomitant with transport, of exogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids.By similarity

    Catalytic activityi

    ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi213 – 22412ATPCuratedAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. long-chain fatty acid-CoA ligase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciECOL386585:GJFA-2487-MONOMER.
    ECOO157:FADD-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Long-chain-fatty-acid--CoA ligase (EC:6.2.1.3)
    Alternative name(s):
    Long-chain acyl-CoA synthetase
    Short name:
    Acyl-CoA synthetase
    Gene namesi
    Name:fadD
    Synonyms:oldD
    Ordered Locus Names:Z2848, ECs2514
    OrganismiEscherichia coli O157:H7
    Taxonomic identifieri83334 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

    Subcellular locationi

    Membrane Curated; Peripheral membrane protein Curated
    Note: Partially membrane-associated.Curated

    GO - Cellular componenti

    1. membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 561561Long-chain-fatty-acid--CoA ligasePRO_0000193127Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.Curated

    Protein-protein interaction databases

    STRINGi155864.Z2848.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8XDR6.
    SMRiQ8XDR6. Positions 23-551.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0318.
    HOGENOMiHOG000229983.
    KOiK01897.
    OMAiVATRWHE.
    OrthoDBiEOG6MH5BV.

    Family and domain databases

    InterProiIPR025110. AMP-bd_C.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    [Graphical view]
    PfamiPF00501. AMP-binding. 1 hit.
    PF13193. AMP-binding_C. 1 hit.
    [Graphical view]
    PROSITEiPS00455. AMP_BINDING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8XDR6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKVWLNRYP ADVPTEINPD RYQSLVDMFE QSVARYADQP AFVNMGEVMT    50
    FRKLEERSRA FAAYLQQGLG LKKGDRVALM MPNLLQYPVA LFGILRAGMI 100
    VVNVNPLYTP RELEHQLNDS GASAIVIVSN FAHTLEKVVD KTAVQHVILT 150
    RMGDQLSTAK GTLVNFVVKY IKRLVPKYHL PDAISFRSAL HNGYRMQYVK 200
    PELVPEDLAF LQYTGGTTGV AKGAMLTHRN MLANLEQVNA TYGPLLHPGK 250
    ELVVTALPLY HIFALTINCL LFIELGGQNL LITNPRDIPG LVKELAKYPF 300
    TAITGVNTLF NALLNNKEFQ QLDFSSLHLS AGGGMPVQQV VAERWVKLTG 350
    QYLLEGYGLT ECAPLVSVNP YDIDYHSGSI GLPVPSTEAK LVDDDDNEVS 400
    PGQPGELCVR GPQVMLGYWQ RPDATDEIIK NGWLHTGDIA VMDEEGFLRI 450
    VDRKKDMILV SGFNVYPNEI EDVVMQHPGV QEVAAVGVPS GSSGEAVKIF 500
    VVKKDPSLTE ESLVTFCRRQ LTGYKVPKLV EFRDELPKSN VGKILRRELR 550
    DEARGKVDNK A 561
    Length:561
    Mass (Da):62,364
    Last modified:March 1, 2002 - v1
    Checksum:i4DE944AB7DF40CF2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005174 Genomic DNA. Translation: AAG56794.1.
    BA000007 Genomic DNA. Translation: BAB35937.1.
    PIRiB90943.
    F85791.
    RefSeqiNP_288241.1. NC_002655.2.
    NP_310541.1. NC_002695.1.

    Genome annotation databases

    EnsemblBacteriaiAAG56794; AAG56794; Z2848.
    BAB35937; BAB35937; BAB35937.
    GeneIDi912449.
    961778.
    KEGGiece:Z2848.
    ecs:ECs2514.
    PATRICi18354390. VBIEscCol44059_2406.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005174 Genomic DNA. Translation: AAG56794.1 .
    BA000007 Genomic DNA. Translation: BAB35937.1 .
    PIRi B90943.
    F85791.
    RefSeqi NP_288241.1. NC_002655.2.
    NP_310541.1. NC_002695.1.

    3D structure databases

    ProteinModelPortali Q8XDR6.
    SMRi Q8XDR6. Positions 23-551.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 155864.Z2848.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG56794 ; AAG56794 ; Z2848 .
    BAB35937 ; BAB35937 ; BAB35937 .
    GeneIDi 912449.
    961778.
    KEGGi ece:Z2848.
    ecs:ECs2514.
    PATRICi 18354390. VBIEscCol44059_2406.

    Phylogenomic databases

    eggNOGi COG0318.
    HOGENOMi HOG000229983.
    KOi K01897.
    OMAi VATRWHE.
    OrthoDBi EOG6MH5BV.

    Enzyme and pathway databases

    BioCyci ECOL386585:GJFA-2487-MONOMER.
    ECOO157:FADD-MONOMER.

    Family and domain databases

    InterProi IPR025110. AMP-bd_C.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    [Graphical view ]
    Pfami PF00501. AMP-binding. 1 hit.
    PF13193. AMP-binding_C. 1 hit.
    [Graphical view ]
    PROSITEi PS00455. AMP_BINDING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
    2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
      Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
      , Kuhara S., Shiba T., Hattori M., Shinagawa H.
      DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

    Entry informationi

    Entry nameiLCFA_ECO57
    AccessioniPrimary (citable) accession number: Q8XDR6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 2002
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 73 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Activity is the highest with fatty acid substrates of > 10 carbon atoms.By similarity

    Keywords - Technical termi

    Complete proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3