O60135 (LCF1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	lcf1
ORF Names:	SPBC18H10.02

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	676 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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 By similarity. Appears to play a role in the maintenance of cell viability during stationary phase. Ref.1
Catalytic activity	ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA.
Cofactor	Magnesium By similarity.
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Ligand	ATP-binding Magnesium Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	chronological cell aging Inferred from mutant phenotype. Source: GeneDB_Spombe long-chain fatty acid metabolic process Inferred from genetic interaction. Source: GeneDB_Spombe negative regulation of G0 to G1 transition Inferred from mutant phenotype. Source: GeneDB_Spombe
Cellular component	endoplasmic reticulum Inferred from direct assay. Source: GeneDB_Spombe
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW long-chain fatty acid-CoA ligase activity Inferred from genetic interaction. Source: GeneDB_Spombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 676	676	Long-chain-fatty-acid--CoA ligase 1		PRO_0000193118

Sequences

	Sequence		Length	Mass (Da)
	O60135 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 98EF74D4A1C5AA41	FASTA	676	75,966
	10 20 30 40 50 60 MKVQSKAISK PKEHESAIYR NANFPDHLVE TYSDDVHTLF DVFRHSVKQF GNKKAMGYRN 70 80 90 100 110 120 LVKEHVETKM VTKVVDGEKK EVPKSWSYFE LSDYNYLSFN DIYDKALRYA GALRKLGLNK 130 140 150 160 170 180 GDKFELYAPT SAFWLLTAEA CLSQSMTIVT AYDTLGEEGL LHSLRESGVR GMYTEGHLLK 190 200 210 220 230 240 TLVNPLKEIE SLEVIIYRND AKEEDIKTIQ EIRPNLKLIK FADFEKMSPP VEPDPPSPEE 250 260 270 280 290 300 ICCIMYTSGS TGLPKGVILS HKNMVAIVTA IVKHVPEVTS KDYLLAYLPL AHILEFAFEN 310 320 330 340 350 360 ICLAWGGTIG YANVRTLVDT NCRNCKGDIN TFRPTIMVGV PAVWEMVRKG IMSKLNAASA 370 380 390 400 410 420 VKRSVFWTAY YTKAKLMRHN LPGSCVLDTA VFNKIRSMGT GGRLRYTLSG GSALSPDTKR 430 440 450 460 470 480 FLSIVLCPML IGYGLTEISA AAMVQNPACF NLDDSAGSLL PCTEMKLVDC EEGNYNSHGH 490 500 510 520 530 540 PPRGEIWLRG PSLTRGYLNR DKENKESFTP DGWFRTGDVG ELTPEGLLRI IDRKKNLVKT 550 560 570 580 590 600 QNGEYIALEK LESRYRTSSL VSNICVYADQ TKVKPLAIIV PNEPVVRKLA TEQAGLSPDA 610 620 630 640 650 660 SWEEVCHNKK VRQLVYDDLI RIGRSHHFAN IELIQNVVLV PIEFTPENGL VTAAQKLQRR 670 KILDRFKKEI DAAYAE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A defect in a fatty acyl-CoA synthetase gene, lcf1+, results in a decrease in viability after entry into the stationary phase in fission yeast." Oshiro T., Aiba H., Mizuno T. Mol. Genet. Genomics 269:437-442(2003) [PubMed: 12684881] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329671 Genomic DNA. Translation: CAA18399.1.
PIR	T39766.
RefSeq	NP_595726.1. NM_001021624.1.
3D structure databases
ProteinModelPortal	O60135.
ModBase	Search...
Protein-protein interaction databases
STRING	O60135.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC18H10.02.1; SPBC18H10.02.1:pep; SPBC18H10.02.
GeneID	2540731.
GenomeReviews	Gene locus lcf1 in contig CU329671_GR.
KEGG	spo:SPBC18H10.02.
NMPDR	fig|4896.1.peg.1592.
Organism-specific databases
GeneDB_Spombe	SPBC18H10.02.
Phylogenomic databases
eggNOG	fuNOG04652.
GeneTree	EFGT00050000001161.
HOGENOM	HBG721674.
OMA	FRELAIN.
OrthoDB	EOG4WDHM9.
Gene expression databases
ArrayExpress	O60135.
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...

Entry information

Entry name

LCF1_SCHPO

Accession

Primary (citable) accession number: O60135

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	August 1, 1998
Last modified:	December 14, 2011
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program