P39518 (LCF2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Long-chain-fatty-acid--CoA ligase 2
EC=6.2.1.3

Alternative name(s):
Fatty acid activator 2
Long-chain acyl-CoA synthetase 2

Gene names

Name:	FAA2
Synonyms:	FAM1
Ordered Locus Names:	YER015W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	744 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Preferentially acts on C9:0-C13:0 fatty acids although C7:0-C17:0 fatty acids are tolerated.
Catalytic activity	ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA.
Cofactor	Magnesium By similarity.
Subcellular location	Cytoplasm. Mitochondrion. Note: The FAM1-1 mutant is imported in the mitochondria.
Miscellaneous	The FAM1-1 suppressor mutant has a single base mutation that creates a new initiator methionine and adds 18 residues at the N-terminus of the protein. This extra sequence acts as a transit peptide and the resulting protein is imported in the mitochondria. Present with 358 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 25 degrees Celsius.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Cytoplasm Mitochondrion
Ligand	ATP-binding Magnesium Nucleotide-binding
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	long-chain fatty acid metabolic process Inferred from mutant phenotype. Source: SGD
Cellular component	mitochondrion Inferred from direct assay. Source: SGD peroxisome Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW long-chain fatty acid-CoA ligase activity Inferred from direct assay. Source: SGD medium-chain fatty acid-CoA ligase activity Inferred from direct assay. Source: SGD very long-chain fatty acid-CoA ligase activity Inferred from genetic interaction. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 744	744	Long-chain-fatty-acid--CoA ligase 2		PRO_0000193120
Amino acid modifications
	Modified residue	711	1	Phosphothreonine Ref.6
Experimental info
	Mutagenesis	1	1	M → MWKNAGYKKRIRTNLFRNM in FAM1-1. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P39518 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 1E023C18682805BC	FASTA	744	83,438
	10 20 30 40 50 60 MAAPDYALTD LIESDPRFES LKTRLAGYTK GSDEYIEELY SQLPLTSYPR YKTFLKKQAV 70 80 90 100 110 120 AISNPDNEAG FSSIYRSSLS SENLVSCVDK NLRTAYDHFM FSARRWPQRD CLGSRPIDKA 130 140 150 160 170 180 TGTWEETFRF ESYSTVSKRC HNIGSGILSL VNTKRKRPLE ANDFVVAILS HNNPEWILTD 190 200 210 220 230 240 LACQAYSLTN TALYETLGPN TSEYILNLTE APILIFAKSN MYHVLKMVPD MKFVNTLVCM 250 260 270 280 290 300 DELTHDELRM LNESLLPVKC NSLNEKITFF SLEQVEQVGC FNKIPAIPPT PDSLYTISFT 310 320 330 340 350 360 SGTTGLPKGV EMSHRNIASG IAFAFSTFRI PPDKRNQQLY DMCFLPLAHI FERMVIAYDL 370 380 390 400 410 420 AIGFGIGFLH KPDPTVLVED LKILKPYAVA LVPRILTRFE AGIKNALDKS TVQRNVANTI 430 440 450 460 470 480 LDSKSARFTA RGGPDKSIMN FLVYHRVLID KIRDSLGLSN NSFIITGSAP ISKDTLLFLR 490 500 510 520 530 540 SALDIGIRQG YGLTETFAGV CLSEPFEKDV GSCGAIGISA ECRLKSVPEM GYHADKDLKG 550 560 570 580 590 600 ELQIRGPQVF ERYFKNPNET SKAVDQDGWF STGDVAFIDG KGRISVIDRV KNFFKLAHGE 610 620 630 640 650 660 YIAPEKIENI YLSSCPYITQ IFVFGDPLKT FLVGIVGVDV DAAQPILAAK HPEVKTWTKE 670 680 690 700 710 720 VLVENLNRNK KLRKEFLNKI NKCTDGLQGF EKLHNIKVGL EPLTLEDDVV TPTFKIKRAK 730 740 ASKFFKDTLD QLYAEGSLVK TEKL

References

	« Hide 'large scale' referencesShow '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: 8027063] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	"Subcellular relocalization of a long-chain fatty acid CoA ligase by a suppressor mutation alleviates a respiration deficiency in Saccharomyces cerevisiae." Harington A., Schwarz E., Slonimski P.P., Herbert C.J. EMBO J. 13:5531-5538(1994) [PubMed: 7988550] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF MET-1. Strain: CW04.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W. Nature 387:78-81(1997) [PubMed: 9169868] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[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 THR-711, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X77783 Genomic DNA. Translation: CAA54817.1. X82364 Genomic DNA. Translation: CAA57780.1. U18778 Genomic DNA. Translation: AAB64548.1. BK006939 Genomic DNA. Translation: DAA07667.1.
PIR	A54901.
RefSeq	NP_010931.1. NM_001178906.1.
3D structure databases
ProteinModelPortal	P39518.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6565N.
IntAct	P39518. 5 interactions.
MINT	MINT-676865.
STRING	P39518.
Proteomic databases
PeptideAtlas	P39518.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YER015W; YER015W; YER015W.
GeneID	856734.
KEGG	sce:YER015W.
NMPDR	fig|4932.3.peg.1991.
Organism-specific databases
CYGD	YER015w.
SGD	S000000817. FAA2.
Phylogenomic databases
eggNOG	fuNOG04411.
GeneTree	EFGT00050000001161.
HOGENOM	HBG721674.
OMA	HIPPKPE.
OrthoDB	EOG4PP1R5.
Enzyme and pathway databases
BRENDA	6.2.1.3. 984.
Gene expression databases
ArrayExpress	P39518.
Genevestigator	P39518.
GermOnline	YER015W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. [Graphical view]
KO	K01897.
Pfam	PF00501. AMP-binding. 1 hit. [Graphical view]
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	982852.

Entry information

Entry name

LCF2_YEAST

Accession

Primary (citable) accession number: P39518
Secondary accession number(s): D3DLR3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	December 14, 2011
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program