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Protein

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

Gene

FAA3

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. 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

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

GO - Biological processi

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

BioCyciYEAST:YIL009W-MONOMER.
ReactomeiREACT_308531. Synthesis of very long-chain fatty acyl-CoAs.

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 Componenti: 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. 33 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.
InParanoidiP39002.
KOiK01897.
OMAiLICSEIK.
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

« Hide

        10         20         30         40         50
MSEQHSVAVG KAANEHETAP RRNVRVKKRP LIRPLNSSAS TLYEFALECF
60 70 80 90 100
NKGGKRDGMA WRDVIEIHET KKTIVRKVDG KDKSIEKTWL YYEMSPYKMM
110 120 130 140 150
TYQELIWVMH DMGRGLAKIG IKPNGEHKFH IFASTSHKWM KIFLGCISQG
160 170 180 190 200
IPVVTAYDTL GESGLIHSMV ETESAAIFTD NQLLAKMIVP LQSAKDIKFL
210 220 230 240 250
IHNEPIDPND RRQNGKLYKA AKDAINKIRE VRPDIKIYSF EEVVKIGKKS
260 270 280 290 300
KDEVKLHPPE PKDLACIMYT SGSISAPKGV VLTHYNIVSG IAGVGHNVFG
310 320 330 340 350
WIGSTDRVLS FLPLAHIFEL VFEFEAFYWN GILGYGSVKT LTNTSTRNCK
360 370 380 390 400
GDLVEFKPTI MIGVAAVWET VRKAILEKIS DLTPVLQKIF WSAYSMKEKS
410 420 430 440 450
VPCTGFLSRM VFKKVRQATG GHLKYIMNGG SAISIDAQKF FSIVLCPMII
460 470 480 490 500
GYGLTETVAN ACVLEPDHFE YGIVGDLVGS VTAKLVDVKD LGYYAKNNQG
510 520 530 540 550
ELLLKGAPVC SEYYKNPIET AVSFTYDGWF RTGDIVEWTP KGQLKIIDRR
560 570 580 590 600
KNLVKTLNGE YIALEKLESV YRSNSYVKNI CVYADESRVK PVGIVVPNPG
610 620 630 640 650
PLSKFAVKLR IMKKGEDIEN YIHDKALRNA VFKEMIATAK SQGLVGIELL
660 670 680 690
CGIVFFDEEW TPENGFVTSA QKLKRREILA AVKSEVERVY KENS
Length:694
Mass (Da):77,947
Last modified:February 1, 1995 - v1
Checksum:i7AB33044335A5295
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi34983. 33 interactions.
DIPiDIP-4210N.
IntActiP39002. 8 interactions.
MINTiMINT-562678.
STRINGi4932.YIL009W.

Proteomic databases

MaxQBiP39002.
PaxDbiP39002.
PeptideAtlasiP39002.
PRIDEiP39002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CYGDiYIL009w.
SGDiS000001271. FAA3.

Phylogenomic databases

eggNOGiCOG1022.
GeneTreeiENSGT00690000102168.
HOGENOMiHOG000159459.
InParanoidiP39002.
KOiK01897.
OMAiLICSEIK.
OrthoDBiEOG7CCC0K.

Enzyme and pathway databases

BioCyciYEAST:YIL009W-MONOMER.
ReactomeiREACT_308531. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

NextBioi977630.

Gene expression databases

GenevestigatoriP39002.

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(1993) [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(1993) [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: April 1, 2015
This is version 128 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

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.