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P39002

- LCF3_YEAST

UniProt

P39002 - LCF3_YEAST

Protein

Long-chain-fatty-acid--CoA ligase 3

Gene

FAA3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Esterification, concomitant with transport, of endogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. This enzyme acts preferentially on C16 and C18 fatty acids with a cis-double bond at C-9-C-10.

    Catalytic activityi

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

    Cofactori

    Magnesium.By similarity

    Temperature dependencei

    Optimum temperature is 25 degrees Celsius.

    GO - Molecular functioni

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

    GO - Biological processi

    1. long-chain fatty acid metabolic process Source: SGD

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    ATP-binding, Magnesium, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:YIL009W-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Long-chain-fatty-acid--CoA ligase 3 (EC:6.2.1.3)
    Alternative name(s):
    Fatty acid activator 3
    Long-chain acyl-CoA synthetase 3
    Gene namesi
    Name:FAA3
    Ordered Locus Names:YIL009W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IX

    Organism-specific databases

    CYGDiYIL009w.
    SGDiS000001271. FAA3.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 694693Long-chain-fatty-acid--CoA ligase 3PRO_0000193121Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP39002.
    PaxDbiP39002.
    PeptideAtlasiP39002.
    PRIDEiP39002.

    Expressioni

    Gene expression databases

    GenevestigatoriP39002.

    Interactioni

    Subunit structurei

    Interacts with FRK1.1 Publication

    Protein-protein interaction databases

    BioGridi34983. 32 interactions.
    DIPiDIP-4210N.
    IntActiP39002. 8 interactions.
    MINTiMINT-562678.
    STRINGi4932.YIL009W.

    Structurei

    3D structure databases

    ProteinModelPortaliP39002.
    SMRiP39002. Positions 100-683.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1022.
    GeneTreeiENSGT00690000102168.
    HOGENOMiHOG000159459.
    KOiK01897.
    OMAiTHENIMA.
    OrthoDBiEOG7CCC0K.

    Family and domain databases

    InterProiIPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    [Graphical view]
    PfamiPF00501. AMP-binding. 1 hit.
    [Graphical view]
    PROSITEiPS00455. AMP_BINDING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P39002-1 [UniParc]FASTAAdd to Basket

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    MSEQHSVAVG KAANEHETAP RRNVRVKKRP LIRPLNSSAS TLYEFALECF    50
    NKGGKRDGMA WRDVIEIHET KKTIVRKVDG KDKSIEKTWL YYEMSPYKMM 100
    TYQELIWVMH DMGRGLAKIG IKPNGEHKFH IFASTSHKWM KIFLGCISQG 150
    IPVVTAYDTL GESGLIHSMV ETESAAIFTD NQLLAKMIVP LQSAKDIKFL 200
    IHNEPIDPND RRQNGKLYKA AKDAINKIRE VRPDIKIYSF EEVVKIGKKS 250
    KDEVKLHPPE PKDLACIMYT SGSISAPKGV VLTHYNIVSG IAGVGHNVFG 300
    WIGSTDRVLS FLPLAHIFEL VFEFEAFYWN GILGYGSVKT LTNTSTRNCK 350
    GDLVEFKPTI MIGVAAVWET VRKAILEKIS DLTPVLQKIF WSAYSMKEKS 400
    VPCTGFLSRM VFKKVRQATG GHLKYIMNGG SAISIDAQKF FSIVLCPMII 450
    GYGLTETVAN ACVLEPDHFE YGIVGDLVGS VTAKLVDVKD LGYYAKNNQG 500
    ELLLKGAPVC SEYYKNPIET AVSFTYDGWF RTGDIVEWTP KGQLKIIDRR 550
    KNLVKTLNGE YIALEKLESV YRSNSYVKNI CVYADESRVK PVGIVVPNPG 600
    PLSKFAVKLR IMKKGEDIEN YIHDKALRNA VFKEMIATAK SQGLVGIELL 650
    CGIVFFDEEW TPENGFVTSA QKLKRREILA AVKSEVERVY KENS 694
    Length:694
    Mass (Da):77,947
    Last modified:February 1, 1995 - v1
    Checksum:i7AB33044335A5295
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z29647 Genomic DNA. Translation: CAA82755.1.
    Z38113 Genomic DNA. Translation: CAA86241.1.
    AY558110 Genomic DNA. Translation: AAS56436.1.
    BK006942 Genomic DNA. Translation: DAA08537.1.
    PIRiB54901.
    RefSeqiNP_012257.1. NM_001179359.1.

    Genome annotation databases

    EnsemblFungiiYIL009W; YIL009W; YIL009W.
    GeneIDi854808.
    KEGGisce:YIL009W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z29647 Genomic DNA. Translation: CAA82755.1 .
    Z38113 Genomic DNA. Translation: CAA86241.1 .
    AY558110 Genomic DNA. Translation: AAS56436.1 .
    BK006942 Genomic DNA. Translation: DAA08537.1 .
    PIRi B54901.
    RefSeqi NP_012257.1. NM_001179359.1.

    3D structure databases

    ProteinModelPortali P39002.
    SMRi P39002. Positions 100-683.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34983. 32 interactions.
    DIPi DIP-4210N.
    IntActi P39002. 8 interactions.
    MINTi MINT-562678.
    STRINGi 4932.YIL009W.

    Proteomic databases

    MaxQBi P39002.
    PaxDbi P39002.
    PeptideAtlasi P39002.
    PRIDEi P39002.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YIL009W ; YIL009W ; YIL009W .
    GeneIDi 854808.
    KEGGi sce:YIL009W.

    Organism-specific databases

    CYGDi YIL009w.
    SGDi S000001271. FAA3.

    Phylogenomic databases

    eggNOGi COG1022.
    GeneTreei ENSGT00690000102168.
    HOGENOMi HOG000159459.
    KOi K01897.
    OMAi THENIMA.
    OrthoDBi EOG7CCC0K.

    Enzyme and pathway databases

    BioCyci YEAST:YIL009W-MONOMER.

    Miscellaneous databases

    NextBioi 977630.

    Gene expression databases

    Genevestigatori P39002.

    Family and domain databases

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

    Publicationsi

    1. "Genetic analysis of the role of Saccharomyces cerevisiae acyl-CoA synthetase genes in regulating protein N-myristoylation."
      Johnson D.R., Knoll L.J., Rowley N., Gordon J.I.
      J. Biol. Chem. 269:18037-18046(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204511 / S288c / AB972.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. "Biochemical studies of three Saccharomyces cerevisiae acyl-CoA synthetases, Faa1p, Faa2p, and Faa3p."
      Knoll L.J., Johnson D.R., Gordon J.I.
      J. Biol. Chem. 269:16348-16356(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH FRK1.
    8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiLCF3_YEAST
    AccessioniPrimary (citable) accession number: P39002
    Secondary accession number(s): D6VVS1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 124 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 6440 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome IX
      Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

    External Data

    Dasty 3