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P39002 (LCF3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:FAA3
Ordered Locus Names:YIL009W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length694 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cofactor

Magnesium By similarity.

Subunit structure

Interacts with FRK1. Ref.7

Miscellaneous

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

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family.

Biophysicochemical properties

Temperature dependence:

Optimum temperature is 25 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 694693Long-chain-fatty-acid--CoA ligase 3
PRO_0000193121

Amino acid modifications

Modified residue21N-acetylserine Ref.8

Sequences

Sequence LengthMass (Da)Tools
P39002 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 7AB33044335A5295

FASTA69477,947
        10         20         30         40         50         60 
MSEQHSVAVG KAANEHETAP RRNVRVKKRP LIRPLNSSAS TLYEFALECF NKGGKRDGMA 

        70         80         90        100        110        120 
WRDVIEIHET KKTIVRKVDG KDKSIEKTWL YYEMSPYKMM TYQELIWVMH DMGRGLAKIG 

       130        140        150        160        170        180 
IKPNGEHKFH IFASTSHKWM KIFLGCISQG IPVVTAYDTL GESGLIHSMV ETESAAIFTD 

       190        200        210        220        230        240 
NQLLAKMIVP LQSAKDIKFL IHNEPIDPND RRQNGKLYKA AKDAINKIRE VRPDIKIYSF 

       250        260        270        280        290        300 
EEVVKIGKKS KDEVKLHPPE PKDLACIMYT SGSISAPKGV VLTHYNIVSG IAGVGHNVFG 

       310        320        330        340        350        360 
WIGSTDRVLS FLPLAHIFEL VFEFEAFYWN GILGYGSVKT LTNTSTRNCK GDLVEFKPTI 

       370        380        390        400        410        420 
MIGVAAVWET VRKAILEKIS DLTPVLQKIF WSAYSMKEKS VPCTGFLSRM VFKKVRQATG 

       430        440        450        460        470        480 
GHLKYIMNGG SAISIDAQKF FSIVLCPMII GYGLTETVAN ACVLEPDHFE YGIVGDLVGS 

       490        500        510        520        530        540 
VTAKLVDVKD LGYYAKNNQG ELLLKGAPVC SEYYKNPIET AVSFTYDGWF RTGDIVEWTP 

       550        560        570        580        590        600 
KGQLKIIDRR KNLVKTLNGE YIALEKLESV YRSNSYVKNI CVYADESRVK PVGIVVPNPG 

       610        620        630        640        650        660 
PLSKFAVKLR IMKKGEDIEN YIHDKALRNA VFKEMIATAK SQGLVGIELL CGIVFFDEEW 

       670        680        690 
TPENGFVTSA QKLKRREILA AVKSEVERVY KENS 

« Hide

References

« Hide 'large scale' references
[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]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX."
Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. expand/collapse author list , Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:84-87(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]"A global protein kinase and phosphatase interaction network in yeast."
Breitkreutz A., Choi H., Sharom J.R., Boucher L., Neduva V., Larsen B., Lin Z.Y., Breitkreutz B.J., Stark C., Liu G., Ahn J., Dewar-Darch D., Reguly T., Tang X., Almeida R., Qin Z.S., Pawson T., Gingras A.C., Nesvizhskii A.I., Tyers M.
Science 328:1043-1046(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH FRK1.
[8]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z29647 Genomic DNA. Translation: CAA82755.1.
Z38113 Genomic DNA. Translation: CAA86241.1.
AY558110 Genomic DNA. Translation: AAS56436.1.
BK006942 Genomic DNA. Translation: DAA08537.1.
PIRB54901.
RefSeqNP_012257.1. NM_001179359.1.

3D structure databases

ProteinModelPortalP39002.
SMRP39002. Positions 100-683.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34983. 32 interactions.
DIPDIP-4210N.
IntActP39002. 8 interactions.
MINTMINT-562678.
STRING4932.YIL009W.

Proteomic databases

MaxQBP39002.
PaxDbP39002.
PeptideAtlasP39002.
PRIDEP39002.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYIL009W; YIL009W; YIL009W.
GeneID854808.
KEGGsce:YIL009W.

Organism-specific databases

CYGDYIL009w.
SGDS000001271. FAA3.

Phylogenomic databases

eggNOGCOG1022.
GeneTreeENSGT00690000102168.
HOGENOMHOG000159459.
KOK01897.
OMATHENIMA.
OrthoDBEOG7CCC0K.

Enzyme and pathway databases

BioCycYEAST:YIL009W-MONOMER.

Gene expression databases

GenevestigatorP39002.

Family and domain databases

InterProIPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio977630.

Entry information

Entry nameLCF3_YEAST
AccessionPrimary (citable) accession number: P39002
Secondary accession number(s): D6VVS1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 14, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IX

Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families