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P30624 (LCF1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. 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 1

EC=6.2.1.3
Alternative name(s):
Fatty acid activator 1
Long-chain acyl-CoA synthetase 1
Gene names
Name:FAA1
Ordered Locus Names:YOR317W
ORF Names:O6136
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length700 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Esterification, concomitant with transport, of exogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. It may supplement intracellular myristoyl-CoA pools from exogenous myristate. Preferentially acts on C12:0-C16:0 fatty acids with myristic and pentadecanic acid (C15:0) having the highest activities.

Catalytic activity

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

Cofactor

Magnesium.

Miscellaneous

Present with 7470 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 30 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 700700Long-chain-fatty-acid--CoA ligase 1
PRO_0000193119

Sequences

Sequence LengthMass (Da)Tools
P30624 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 56EE7E04D95BC5C9

FASTA70077,866
        10         20         30         40         50         60 
MVAQYTVPVG KAANEHETAP RRNYQCREKP LVRPPNTKCS TVYEFVLECF QKNKNSNAMG 

        70         80         90        100        110        120 
WRDVKEIHEE SKSVMKKVDG KETSVEKKWM YYELSHYHYN SFDQLTDIMH EIGRGLVKIG 

       130        140        150        160        170        180 
LKPNDDDKLH LYAATSHKWM KMFLGAQSQG IPVVTAYDTL GEKGLIHSLV QTGSKAIFTD 

       190        200        210        220        230        240 
NSLLPSLIKP VQAAQDVKYI IHFDSISSED RRQSGKIYQS AHDAINRIKE VRPDIKTFSF 

       250        260        270        280        290        300 
DDILKLGKES CNEIDVHPPG KDDLCCIMYT SGSTGEPKGV VLKHSNVVAG VGGASLNVLK 

       310        320        330        340        350        360 
FVGNTDRVIC FLPLAHIFEL VFELLSFYWG ACIGYATVKT LTSSSVRNCQ GDLQEFKPTI 

       370        380        390        400        410        420 
MVGVAAVWET VRKGILNQID NLPFLTKKIF WTAYNTKLNM QRLHIPGGGA LGNLVFKKIR 

       430        440        450        460        470        480 
TATGGQLRYL LNGGSPISRD AQEFITNLIC PMLIGYGLTE TCASTTILDP ANFELGVAGD 

       490        500        510        520        530        540 
LTGCVTVKLV DVEELGYFAK NNQGEVWITG ANVTPEYYKN EEETSQALTS DGWFKTGDIG 

       550        560        570        580        590        600 
EWEANGHLKI IDRKKNLVKT MNGEYIALEK LESVYRSNEY VANICVYADQ SKTKPVGIIV 

       610        620        630        640        650        660 
PNHAPLTKLA KKLGIMEQKD SSINIENYLE DAKLIKAVYS DLLKTGKDQG LVGIELLAGI 

       670        680        690        700 
VFFDGEWTPQ NGFVTSAQKL KRKDILNAVK DKVDAVYSSS 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of a Saccharomyces cerevisiae long chain fatty acyl:CoA synthetase gene (FAA1) and assessment of its role in protein N-myristoylation."
Duronio R.J., Knoll L.J., Gordon J.I.
J. Cell Biol. 117:515-529(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 4-14.
Strain: ATCC 204508 / S288c.
[2]"Sequencing of a 35.71 kb DNA segment on the right arm of yeast chromosome XV reveals regions of similarity to chromosomes I and XIII."
Pearson B.M., Hernando Y., Payne J., Wolf S.S., Kalogeropoulos A., Schweizer M.
Yeast 12:1021-1031(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. expand/collapse author list , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
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 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].
[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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X66194 Genomic DNA. Translation: CAA46957.1.
X90565 Genomic DNA. Translation: CAA62172.1.
Z75225 Genomic DNA. Translation: CAA99637.1.
BK006948 Genomic DNA. Translation: DAA11082.1.
PIRS23052.
RefSeqNP_014962.3. NM_001183737.3.

3D structure databases

ProteinModelPortalP30624.
SMRP30624. Positions 112-604.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34704. 66 interactions.
DIPDIP-4654N.
IntActP30624. 1 interaction.
MINTMINT-541922.
STRING4932.YOR317W.

Proteomic databases

PaxDbP30624.
PeptideAtlasP30624.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOR317W; YOR317W; YOR317W.
GeneID854495.
KEGGsce:YOR317W.

Organism-specific databases

CYGDYOR317w.
SGDS000005844. FAA1.

Phylogenomic databases

eggNOGCOG1022.
GeneTreeENSGT00690000102168.
HOGENOMHOG000159459.
KOK01897.
OMAFELAFEC.
OrthoDBEOG7CCC0K.

Enzyme and pathway databases

BioCycYEAST:YOR317W-MONOMER.

Gene expression databases

GenevestigatorP30624.

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

NextBio976828.

Entry information

Entry nameLCF1_YEAST
AccessionPrimary (citable) accession number: P30624
Secondary accession number(s): D6W316
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: April 16, 2014
This is version 118 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 XV

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

Yeast

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

SIMILARITY comments

Index of protein domains and families