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P69451

- LCFA_ECOLI

UniProt

P69451 - LCFA_ECOLI

Protein

Long-chain-fatty-acid--CoA ligase

Gene

fadD

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 80 (01 Oct 2014)
      Sequence version 1 (01 Mar 2005)
      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.

    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. fatty acid binding Source: EcoliWiki
    3. long-chain fatty acid-CoA ligase activity Source: EcoCyc
    4. oleic acid binding Source: EcoliWiki

    GO - Biological processi

    1. acyl-CoA metabolic process Source: EcoCyc
    2. fatty acid beta-oxidation Source: EcoCyc
    3. fatty acid metabolic process Source: EcoliWiki
    4. lipid metabolic process Source: EcoliWiki
    5. long-chain fatty acid metabolic process Source: GOC
    6. phospholipid biosynthetic process Source: EcoliWiki

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:ACYLCOASYN-MONOMER.
    ECOL316407:JW1794-MONOMER.
    MetaCyc:ACYLCOASYN-MONOMER.
    RETL1328306-WGS:GSTH-490-MONOMER.
    SABIO-RKP69451.

    Protein family/group databases

    TCDBi4.C.1.1.4. the proposed fatty acid transporter (fat) family.

    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:b1805, JW1794
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11530. fadD.

    Subcellular locationi

    Membrane By similarity; Peripheral membrane protein By similarity
    Note: Partially membrane-associated.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: EcoliWiki
    2. cytoplasmic side of plasma membrane Source: EcoCyc
    3. cytosol Source: EcoCyc

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi213 – 2131Y → A: Loss of activity. 1 Publication
    Mutagenesisi214 – 2141T → A: 10% of wild-type activity. 1 Publication
    Mutagenesisi216 – 2161G → A: Decreases activity. 1 Publication
    Mutagenesisi217 – 2171T → A: Decreases activity. 1 Publication
    Mutagenesisi219 – 2191G → A: Decreases activity. 1 Publication
    Mutagenesisi222 – 2221K → A: Decreases activity. 1 Publication
    Mutagenesisi361 – 3611E → A: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 561561Long-chain-fatty-acid--CoA ligasePRO_0000193125Add
    BLAST

    Proteomic databases

    PaxDbiP69451.
    PRIDEiP69451.

    Expressioni

    Gene expression databases

    GenevestigatoriP69451.

    Interactioni

    Subunit structurei

    Homodimer.Curated

    Protein-protein interaction databases

    IntActiP69451. 6 interactions.
    STRINGi511145.b1805.

    Structurei

    3D structure databases

    ProteinModelPortaliP69451.
    SMRiP69451. Positions 60-551.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0318.
    HOGENOMiHOG000229983.
    KOiK01897.
    OMAiVATRWHE.
    OrthoDBiEOG6MH5BV.
    PhylomeDBiP69451.

    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.

    P69451-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKVWLNRYP ADVPTEINPD RYQSLVDMFE QSVARYADQP AFVNMGEVMT    50
    FRKLEERSRA FAAYLQQGLG LKKGDRVALM MPNLLQYPVA LFGILRAGMI 100
    VVNVNPLYTP RELEHQLNDS GASAIVIVSN FAHTLEKVVD KTAVQHVILT 150
    RMGDQLSTAK GTVVNFVVKY 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 LVDDDDNEVP 400
    PGQPGELCVK GPQVMLGYWQ RPDATDEIIK NGWLHTGDIA VMDEEGFLRI 450
    VDRKKDMILV SGFNVYPNEI EDVVMQHPGV QEVAAVGVPS GSSGEAVKIF 500
    VVKKDPSLTE ESLVTFCRRQ LTGYKVPKLV EFRDELPKSN VGKILRRELR 550
    DEARGKVDNK A 561
    Length:561
    Mass (Da):62,332
    Last modified:March 1, 2005 - v1
    Checksum:i249B0AA54B3DBFA5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti34 – 5118ARYAD…EVMTF → GALRRSTCVCEYGGGNDL in AAA23752. (PubMed:1460045)CuratedAdd
    BLAST
    Sequence conflicti468 – 49023NEIED…VGVPS → TRLKMSSCSMVAYRKSRLLA YLP in AAA23752. (PubMed:1460045)CuratedAdd
    BLAST
    Sequence conflicti496 – 4961A → G in AAA23752. (PubMed:1460045)Curated
    Sequence conflicti555 – 5617GKVDNKA → QSGQ in AAA23752. (PubMed:1460045)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X70994 Genomic DNA. Translation: CAA50321.1.
    L02649 Genomic DNA. Translation: AAA23752.1.
    U00096 Genomic DNA. Translation: AAC74875.1.
    AP009048 Genomic DNA. Translation: BAA15609.1.
    PIRiE64941. S41589.
    RefSeqiNP_416319.1. NC_000913.3.
    YP_490066.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74875; AAC74875; b1805.
    BAA15609; BAA15609; BAA15609.
    GeneIDi12930156.
    946327.
    KEGGiecj:Y75_p1780.
    eco:b1805.
    PATRICi32118927. VBIEscCol129921_1881.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X70994 Genomic DNA. Translation: CAA50321.1 .
    L02649 Genomic DNA. Translation: AAA23752.1 .
    U00096 Genomic DNA. Translation: AAC74875.1 .
    AP009048 Genomic DNA. Translation: BAA15609.1 .
    PIRi E64941. S41589.
    RefSeqi NP_416319.1. NC_000913.3.
    YP_490066.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P69451.
    SMRi P69451. Positions 60-551.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P69451. 6 interactions.
    STRINGi 511145.b1805.

    Protein family/group databases

    TCDBi 4.C.1.1.4. the proposed fatty acid transporter (fat) family.

    Proteomic databases

    PaxDbi P69451.
    PRIDEi P69451.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74875 ; AAC74875 ; b1805 .
    BAA15609 ; BAA15609 ; BAA15609 .
    GeneIDi 12930156.
    946327.
    KEGGi ecj:Y75_p1780.
    eco:b1805.
    PATRICi 32118927. VBIEscCol129921_1881.

    Organism-specific databases

    EchoBASEi EB1492.
    EcoGenei EG11530. fadD.

    Phylogenomic databases

    eggNOGi COG0318.
    HOGENOMi HOG000229983.
    KOi K01897.
    OMAi VATRWHE.
    OrthoDBi EOG6MH5BV.
    PhylomeDBi P69451.

    Enzyme and pathway databases

    BioCyci EcoCyc:ACYLCOASYN-MONOMER.
    ECOL316407:JW1794-MONOMER.
    MetaCyc:ACYLCOASYN-MONOMER.
    RETL1328306-WGS:GSTH-490-MONOMER.
    SABIO-RK P69451.

    Miscellaneous databases

    PROi P69451.

    Gene expression databases

    Genevestigatori P69451.

    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. "The fadD gene of Escherichia coli K12 is located close to rnd at 39.6 min of the chromosomal map and is a new member of the AMP-binding protein family."
      Fulda M., Heinz E., Wolter F.P.
      Mol. Gen. Genet. 242:241-249(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Cloning, sequencing, and expression of the fadD gene of Escherichia coli encoding acyl coenzyme A synthetase."
      Black P.N., Dirusso C.C., Metzger A.K., Heimert T.L.
      J. Biol. Chem. 267:25513-25520(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10.
      Strain: K12.
    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. "Functional role of fatty acyl-coenzyme A synthetase in the transmembrane movement and activation of exogenous long-chain fatty acids. Amino acid residues within the ATP/AMP signature motif of Escherichia coli FadD are required for enzyme activity and fatty acid transport."
      Weimar J.D., DiRusso C.C., Delio R., Black P.N.
      J. Biol. Chem. 277:29369-29376(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF ATP-BINDING MOTIF, MUTAGENESIS OF TYR-213; THR-214; GLY-216; THR-217; GLY-219; LYS-222 AND GLU-361.

    Entry informationi

    Entry nameiLCFA_ECOLI
    AccessioniPrimary (citable) accession number: P69451
    Secondary accession number(s): P29212
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 2005
    Last sequence update: March 1, 2005
    Last modified: October 1, 2014
    This is version 80 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.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3