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Protein

Long-chain-fatty-acid--CoA ligase 1

Gene

FAA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

Temperature dependencei

Optimum temperature is 30 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

GO - Biological processi

  1. long-chain fatty acid metabolic process Source: GOC
  2. long-chain fatty acid transport Source: SGD
  3. long-chain fatty-acyl-CoA 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:YOR317W-MONOMER.
ReactomeiREACT_308531. Synthesis of very long-chain fatty acyl-CoAs.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:FAA1
Ordered Locus Names:YOR317W
ORF Names:O6136
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XV

Organism-specific databases

CYGDiYOR317w.
SGDiS000005844. FAA1.

Subcellular locationi

GO - Cellular componenti

  1. lipid particle Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 700699Long-chain-fatty-acid--CoA ligase 1PRO_0000193119Add
BLAST

Proteomic databases

MaxQBiP30624.
PaxDbiP30624.
PeptideAtlasiP30624.

Expressioni

Gene expression databases

GenevestigatoriP30624.

Interactioni

Protein-protein interaction databases

BioGridi34704. 69 interactions.
DIPiDIP-4654N.
IntActiP30624. 1 interaction.
MINTiMINT-541922.
STRINGi4932.YOR317W.

Structurei

3D structure databases

SMRiP30624. Positions 112-604.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1022.
GeneTreeiENSGT00690000102168.
HOGENOMiHOG000159459.
InParanoidiP30624.
KOiK01897.
OMAiFITNLIC.
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.

P30624-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVAQYTVPVG KAANEHETAP RRNYQCREKP LVRPPNTKCS TVYEFVLECF
60 70 80 90 100
QKNKNSNAMG WRDVKEIHEE SKSVMKKVDG KETSVEKKWM YYELSHYHYN
110 120 130 140 150
SFDQLTDIMH EIGRGLVKIG LKPNDDDKLH LYAATSHKWM KMFLGAQSQG
160 170 180 190 200
IPVVTAYDTL GEKGLIHSLV QTGSKAIFTD NSLLPSLIKP VQAAQDVKYI
210 220 230 240 250
IHFDSISSED RRQSGKIYQS AHDAINRIKE VRPDIKTFSF DDILKLGKES
260 270 280 290 300
CNEIDVHPPG KDDLCCIMYT SGSTGEPKGV VLKHSNVVAG VGGASLNVLK
310 320 330 340 350
FVGNTDRVIC FLPLAHIFEL VFELLSFYWG ACIGYATVKT LTSSSVRNCQ
360 370 380 390 400
GDLQEFKPTI MVGVAAVWET VRKGILNQID NLPFLTKKIF WTAYNTKLNM
410 420 430 440 450
QRLHIPGGGA LGNLVFKKIR TATGGQLRYL LNGGSPISRD AQEFITNLIC
460 470 480 490 500
PMLIGYGLTE TCASTTILDP ANFELGVAGD LTGCVTVKLV DVEELGYFAK
510 520 530 540 550
NNQGEVWITG ANVTPEYYKN EEETSQALTS DGWFKTGDIG EWEANGHLKI
560 570 580 590 600
IDRKKNLVKT MNGEYIALEK LESVYRSNEY VANICVYADQ SKTKPVGIIV
610 620 630 640 650
PNHAPLTKLA KKLGIMEQKD SSINIENYLE DAKLIKAVYS DLLKTGKDQG
660 670 680 690 700
LVGIELLAGI VFFDGEWTPQ NGFVTSAQKL KRKDILNAVK DKVDAVYSSS
Length:700
Mass (Da):77,866
Last modified:March 31, 1993 - v1
Checksum:i56EE7E04D95BC5C9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66194 Genomic DNA. Translation: CAA46957.1.
X90565 Genomic DNA. Translation: CAA62172.1.
Z75225 Genomic DNA. Translation: CAA99637.1.
BK006948 Genomic DNA. Translation: DAA11082.1.
PIRiS23052.
RefSeqiNP_014962.3. NM_001183737.3.

Genome annotation databases

EnsemblFungiiYOR317W; YOR317W; YOR317W.
GeneIDi854495.
KEGGisce:YOR317W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66194 Genomic DNA. Translation: CAA46957.1.
X90565 Genomic DNA. Translation: CAA62172.1.
Z75225 Genomic DNA. Translation: CAA99637.1.
BK006948 Genomic DNA. Translation: DAA11082.1.
PIRiS23052.
RefSeqiNP_014962.3. NM_001183737.3.

3D structure databases

SMRiP30624. Positions 112-604.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34704. 69 interactions.
DIPiDIP-4654N.
IntActiP30624. 1 interaction.
MINTiMINT-541922.
STRINGi4932.YOR317W.

Proteomic databases

MaxQBiP30624.
PaxDbiP30624.
PeptideAtlasiP30624.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR317W; YOR317W; YOR317W.
GeneIDi854495.
KEGGisce:YOR317W.

Organism-specific databases

CYGDiYOR317w.
SGDiS000005844. FAA1.

Phylogenomic databases

eggNOGiCOG1022.
GeneTreeiENSGT00690000102168.
HOGENOMiHOG000159459.
InParanoidiP30624.
KOiK01897.
OMAiFITNLIC.
OrthoDBiEOG7CCC0K.

Enzyme and pathway databases

BioCyciYEAST:YOR317W-MONOMER.
ReactomeiREACT_308531. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

NextBioi976828.

Gene expression databases

GenevestigatoriP30624.

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. "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(1991) [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(1995) [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.
    , 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(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. 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(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. 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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. 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(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiLCF1_YEAST
AccessioniPrimary (citable) accession number: P30624
Secondary accession number(s): D6W316
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 31, 1993
Last sequence update: March 31, 1993
Last modified: March 31, 2015
This is version 126 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 7470 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: 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.