Reviewed, UniProtKB/Swiss-Prot P30624 (LCF1_YEAST)

Names and origin

Protein names

Recommended name:
    Long-chain-fatty-acid--CoA ligase 1
    EC=6.2.1.3
Alternative name(s):
    Long-chain acyl-CoA synthetase 1
    Fatty acid activator 1

Gene names

Name:	FAA1
Ordered Locus Names:	YOR317W
ORF Names:	O6136

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	700 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA.
Cofactor	Magnesium.
Miscellaneous	Present with 7470 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.
Biophysicochemical properties	Temperature dependence: Optimum temperature is 30 degrees Celsius.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Ligand	ATP-binding Magnesium Nucleotide-binding
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	N-terminal protein myristoylation Inferred from genetic interaction. Source: SGD fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW lipid transport Inferred from genetic interaction. Source: SGD
Cellular component	lipid particle Inferred from direct assay. Source: SGD mitochondrial outer membrane Inferred from direct assay. Source: SGD plasma membrane enriched fraction Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW long-chain-fatty-acid-CoA ligase activity Ref.4 Inferred from direct assay. Source: SGD magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
JSN1	P47135	1	EBI-10075,EBI-9422

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 700	700	Long-chain-fatty-acid--CoA ligase 1		PRO_0000193119
Amino acid modifications
	Modified residue	622	1	Phosphoserine Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P30624-1 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: 56EE7E04D95BC5C9	FASTA	700	77,866
	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

References

	« Hide 'large scale' referencesShow '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: 1572893] [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: 8896266] [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(1997) [PubMed: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	"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: 8206942] [Abstract] Cited for: CHARACTERIZATION.
[5]	"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: 14562106] [Abstract] 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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-622, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X66194 Genomic DNA. Translation: CAA46957.1. X90565 Genomic DNA. Translation: CAA62172.1. Z75225 Genomic DNA. Translation: CAA99637.1.
PIR	S23052.
RefSeq	NP_014962.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:4654N.
IntAct	P30624. 10 interactions.
Proteomic databases
PeptideAtlas	P30624.
Genome annotation databases
Ensembl	YOR317W. Saccharomyces cerevisiae. [Contig view]
GeneID	854495.
GenomeReviews	Gene locus YOR317W in contig Y13140_GR.
KEGG	sce:YOR317W.
NMPDR	fig|4932.3.peg.6077.
Organism-specific databases
CYGD	YOR317w.
SGD	S000005844. FAA1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P30624.
OMA	P30624. FITNLIC.
Enzyme and pathway databases
BRENDA	6.2.1.3. 250.
Gene expression databases
ArrayExpress	P30624.
GermOnline	YOR317W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000873. AMP-dep_Synth/Lig. [Graphical view]
Pfam	PF00501. AMP-binding. 2 hits. [Graphical view]
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	976828.

Entry information

Entry name

LCF1_YEAST

Accession

Primary (citable) accession number: P30624

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	June 16, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)