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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: 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

  • ATP binding Source: UniProtKB-KW
  • long-chain fatty acid-CoA ligase activity Source: SGD
  • medium-chain fatty acid-CoA ligase activity Source: SGD
  • very long-chain fatty acid-CoA ligase activity Source: SGD

GO - Biological processi

  • fatty acid beta-oxidation Source: UniProtKB
  • fatty-acyl-CoA transport Source: UniProtKB
  • long-chain fatty acid metabolic process Source: SGD
  • peroxisomal long-chain fatty acid import Source: UniProtKB
  • 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_297847. Linoleic acid (LA) metabolism.
REACT_306569. alpha-linolenic acid (ALA) metabolism.
REACT_308531. 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 Componenti: Chromosome V

Organism-specific databases

CYGDiYER015w.
EuPathDBiFungiDB:YER015W.
SGDiS000000817. FAA2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: UniProtKB-SubCell
  • 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.

Interactioni

Protein-protein interaction databases

BioGridi36747. 8 interactions.
DIPiDIP-6565N.
IntActiP39518. 4 interactions.
MINTiMINT-676865.

Structurei

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1022.
GeneTreeiENSGT00690000101725.
HOGENOMiHOG000159459.
InParanoidiP39518.
KOiK01897.
OMAiVICENED.
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.
PIRiA54901.
RefSeqiNP_010931.3. NM_001178906.3.

3D structure databases

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

Protein-protein interaction databases

BioGridi36747. 8 interactions.
DIPiDIP-6565N.
IntActiP39518. 4 interactions.
MINTiMINT-676865.

Protein family/group databases

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

Proteomic databases

MaxQBiP39518.
PaxDbiP39518.
PeptideAtlasiP39518.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CYGDiYER015w.
EuPathDBiFungiDB:YER015W.
SGDiS000000817. FAA2.

Phylogenomic databases

eggNOGiCOG1022.
GeneTreeiENSGT00690000101725.
HOGENOMiHOG000159459.
InParanoidiP39518.
KOiK01897.
OMAiVICENED.
OrthoDBiEOG7TTQH5.

Enzyme and pathway databases

BioCyciMetaCyc:YER015W-MONOMER.
YEAST:YER015W-MONOMER.
BRENDAi6.2.1.3. 984.
ReactomeiREACT_297847. Linoleic acid (LA) metabolism.
REACT_306569. alpha-linolenic acid (ALA) metabolism.
REACT_308531. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

NextBioi982852.
PROiP39518.

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]
ProtoNetiSearch...

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: July 22, 2015
This is version 127 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.