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P39518

- LCF2_YEAST

UniProt

P39518 - LCF2_YEAST

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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

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

Mg2+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
Complete GO annotation...

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.
ReactomeiREACT_188942. Linoleic acid (LA) metabolism.
REACT_188947. alpha-linolenic acid (ALA) metabolism.
REACT_188984. PPARA activates gene expression.
REACT_239919. Synthesis of very long-chain fatty acyl-CoAs.

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-KW
  2. peroxisome Source: SGD
Complete GO annotation...

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.
InParanoidiP39518.
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

        10         20         30         40         50
MAAPDYALTD LIESDPRFES LKTRLAGYTK GSDEYIEELY SQLPLTSYPR
60 70 80 90 100
YKTFLKKQAV AISNPDNEAG FSSIYRSSLS SENLVSCVDK NLRTAYDHFM
110 120 130 140 150
FSARRWPQRD CLGSRPIDKA TGTWEETFRF ESYSTVSKRC HNIGSGILSL
160 170 180 190 200
VNTKRKRPLE ANDFVVAILS HNNPEWILTD LACQAYSLTN TALYETLGPN
210 220 230 240 250
TSEYILNLTE APILIFAKSN MYHVLKMVPD MKFVNTLVCM DELTHDELRM
260 270 280 290 300
LNESLLPVKC NSLNEKITFF SLEQVEQVGC FNKIPAIPPT PDSLYTISFT
310 320 330 340 350
SGTTGLPKGV EMSHRNIASG IAFAFSTFRI PPDKRNQQLY DMCFLPLAHI
360 370 380 390 400
FERMVIAYDL AIGFGIGFLH KPDPTVLVED LKILKPYAVA LVPRILTRFE
410 420 430 440 450
AGIKNALDKS TVQRNVANTI LDSKSARFTA RGGPDKSIMN FLVYHRVLID
460 470 480 490 500
KIRDSLGLSN NSFIITGSAP ISKDTLLFLR SALDIGIRQG YGLTETFAGV
510 520 530 540 550
CLSEPFEKDV GSCGAIGISA ECRLKSVPEM GYHADKDLKG ELQIRGPQVF
560 570 580 590 600
ERYFKNPNET SKAVDQDGWF STGDVAFIDG KGRISVIDRV KNFFKLAHGE
610 620 630 640 650
YIAPEKIENI YLSSCPYITQ IFVFGDPLKT FLVGIVGVDV DAAQPILAAK
660 670 680 690 700
HPEVKTWTKE VLVENLNRNK KLRKEFLNKI NKCTDGLQGF EKLHNIKVGL
710 720 730 740
EPLTLEDDVV TPTFKIKRAK ASKFFKDTLD QLYAEGSLVK TEKL
Length:744
Mass (Da):83,438
Last modified:February 1, 1995 - v1
Checksum:i1E023C18682805BC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
InParanoidi P39518.
KOi K01897.
OMAi CGYYKDE.
OrthoDBi EOG7TTQH5.

Enzyme and pathway databases

BioCyci MetaCyc:YER015W-MONOMER.
YEAST:YER015W-MONOMER.
BRENDAi 6.2.1.3. 984.
Reactomei REACT_188942. Linoleic acid (LA) metabolism.
REACT_188947. alpha-linolenic acid (ALA) metabolism.
REACT_188984. PPARA activates gene expression.
REACT_239919. Synthesis of very long-chain fatty acyl-CoAs.

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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 121 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