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P39518

- LCF2_YEAST

UniProt

P39518 - LCF2_YEAST

Protein

Long-chain-fatty-acid--CoA ligase 2

Gene

FAA2

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 119 (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. Preferentially acts on C9:0-C13:0 fatty acids although C7:0-C17:0 fatty acids are tolerated.

    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. medium-chain fatty acid-CoA ligase activity Source: SGD
    4. very long-chain fatty acid-CoA ligase activity Source: SGD

    GO - Biological processi

    1. fatty acid beta-oxidation Source: UniProtKB
    2. fatty-acyl-CoA transport Source: UniProtKB
    3. long-chain fatty acid metabolic process Source: SGD
    4. peroxisomal long-chain fatty acid import Source: UniProtKB
    5. very long-chain fatty acid catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    ATP-binding, Magnesium, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:YER015W-MONOMER.
    YEAST:YER015W-MONOMER.
    BRENDAi6.2.1.3. 984.

    Protein family/group databases

    TCDBi4.C.1.1.15. the proposed fatty acid transporter (fat) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Long-chain-fatty-acid--CoA ligase 2 (EC:6.2.1.3)
    Alternative name(s):
    Fatty acid activator 2
    Long-chain acyl-CoA synthetase 2
    Gene namesi
    Name:FAA2
    Synonyms:FAM1
    Ordered Locus Names:YER015W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome V

    Organism-specific databases

    CYGDiYER015w.
    SGDiS000000817. FAA2.

    Subcellular locationi

    Cytoplasm. Mitochondrion
    Note: The FAM1-1 mutant is imported in the mitochondria.

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB-SubCell
    2. peroxisome Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1 – 11M → MWKNAGYKKRIRTNLFRNM in FAM1-1. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 744744Long-chain-fatty-acid--CoA ligase 2PRO_0000193120Add
    BLAST

    Proteomic databases

    MaxQBiP39518.
    PaxDbiP39518.
    PeptideAtlasiP39518.

    Expressioni

    Gene expression databases

    GenevestigatoriP39518.

    Interactioni

    Protein-protein interaction databases

    BioGridi36747. 9 interactions.
    DIPiDIP-6565N.
    IntActiP39518. 4 interactions.
    MINTiMINT-676865.
    STRINGi4932.YER015W.

    Structurei

    3D structure databases

    ProteinModelPortaliP39518.
    SMRiP39518. Positions 162-682.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1022.
    GeneTreeiENSGT00690000101725.
    HOGENOMiHOG000159459.
    KOiK01897.
    OMAiCGYYKDE.
    OrthoDBiEOG7TTQH5.

    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.

    P39518-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAPDYALTD LIESDPRFES LKTRLAGYTK GSDEYIEELY SQLPLTSYPR    50
    YKTFLKKQAV AISNPDNEAG FSSIYRSSLS SENLVSCVDK NLRTAYDHFM 100
    FSARRWPQRD CLGSRPIDKA TGTWEETFRF ESYSTVSKRC HNIGSGILSL 150
    VNTKRKRPLE ANDFVVAILS HNNPEWILTD LACQAYSLTN TALYETLGPN 200
    TSEYILNLTE APILIFAKSN MYHVLKMVPD MKFVNTLVCM DELTHDELRM 250
    LNESLLPVKC NSLNEKITFF SLEQVEQVGC FNKIPAIPPT PDSLYTISFT 300
    SGTTGLPKGV EMSHRNIASG IAFAFSTFRI PPDKRNQQLY DMCFLPLAHI 350
    FERMVIAYDL AIGFGIGFLH KPDPTVLVED LKILKPYAVA LVPRILTRFE 400
    AGIKNALDKS TVQRNVANTI LDSKSARFTA RGGPDKSIMN FLVYHRVLID 450
    KIRDSLGLSN NSFIITGSAP ISKDTLLFLR SALDIGIRQG YGLTETFAGV 500
    CLSEPFEKDV GSCGAIGISA ECRLKSVPEM GYHADKDLKG ELQIRGPQVF 550
    ERYFKNPNET SKAVDQDGWF STGDVAFIDG KGRISVIDRV KNFFKLAHGE 600
    YIAPEKIENI YLSSCPYITQ IFVFGDPLKT FLVGIVGVDV DAAQPILAAK 650
    HPEVKTWTKE VLVENLNRNK KLRKEFLNKI NKCTDGLQGF EKLHNIKVGL 700
    EPLTLEDDVV TPTFKIKRAK ASKFFKDTLD QLYAEGSLVK TEKL 744
    Length:744
    Mass (Da):83,438
    Last modified:February 1, 1995 - v1
    Checksum:i1E023C18682805BC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X77783 Genomic DNA. Translation: CAA54817.1.
    X82364 Genomic DNA. Translation: CAA57780.1.
    U18778 Genomic DNA. Translation: AAB64548.1.
    BK006939 Genomic DNA. Translation: DAA07667.1.
    PIRiA54901.
    RefSeqiNP_010931.3. NM_001178906.3.

    Genome annotation databases

    EnsemblFungiiYER015W; YER015W; YER015W.
    GeneIDi856734.
    KEGGisce:YER015W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X77783 Genomic DNA. Translation: CAA54817.1 .
    X82364 Genomic DNA. Translation: CAA57780.1 .
    U18778 Genomic DNA. Translation: AAB64548.1 .
    BK006939 Genomic DNA. Translation: DAA07667.1 .
    PIRi A54901.
    RefSeqi NP_010931.3. NM_001178906.3.

    3D structure databases

    ProteinModelPortali P39518.
    SMRi P39518. Positions 162-682.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36747. 9 interactions.
    DIPi DIP-6565N.
    IntActi P39518. 4 interactions.
    MINTi MINT-676865.
    STRINGi 4932.YER015W.

    Protein family/group databases

    TCDBi 4.C.1.1.15. the proposed fatty acid transporter (fat) family.

    Proteomic databases

    MaxQBi P39518.
    PaxDbi P39518.
    PeptideAtlasi P39518.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YER015W ; YER015W ; YER015W .
    GeneIDi 856734.
    KEGGi sce:YER015W.

    Organism-specific databases

    CYGDi YER015w.
    SGDi S000000817. FAA2.

    Phylogenomic databases

    eggNOGi COG1022.
    GeneTreei ENSGT00690000101725.
    HOGENOMi HOG000159459.
    KOi K01897.
    OMAi CGYYKDE.
    OrthoDBi EOG7TTQH5.

    Enzyme and pathway databases

    BioCyci MetaCyc:YER015W-MONOMER.
    YEAST:YER015W-MONOMER.
    BRENDAi 6.2.1.3. 984.

    Miscellaneous databases

    NextBioi 982852.

    Gene expression databases

    Genevestigatori P39518.

    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. "Subcellular relocalization of a long-chain fatty acid CoA ligase by a suppressor mutation alleviates a respiration deficiency in Saccharomyces cerevisiae."
      Harington A., Schwarz E., Slonimski P.P., Herbert C.J.
      EMBO J. 13:5531-5538(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF MET-1.
      Strain: CW04.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    6. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiLCF2_YEAST
    AccessioniPrimary (citable) accession number: P39518
    Secondary accession number(s): D3DLR3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 119 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The FAM1-1 suppressor mutant has a single base mutation that creates a new initiator methionine and adds 18 residues at the N-terminus of the protein. This extra sequence acts as a transit peptide and the resulting protein is imported in the mitochondria.
    Present with 358 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 V
      Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

    External Data

    Dasty 3