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O60135 (LCF1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:lcf1
ORF Names:SPBC18H10.02
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length676 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 fatty acid + CoA = AMP + diphosphate + an acyl-CoA.

Cofactor

Magnesium By similarity.

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 676676Long-chain-fatty-acid--CoA ligase 1
PRO_0000193118

Sequences

Sequence LengthMass (Da)Tools
O60135 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 98EF74D4A1C5AA41

FASTA67675,966
        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 

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329671 Genomic DNA. Translation: CAA18399.1.
PIRT39766.
RefSeqNP_595726.1. NM_001021624.2.

3D structure databases

ProteinModelPortalO60135.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid277254. 4 interactions.
MINTMINT-4677511.
STRING4896.SPBC18H10.02-1.

Proteomic databases

MaxQBO60135.
PaxDbO60135.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC18H10.02.1; SPBC18H10.02.1:pep; SPBC18H10.02.
GeneID2540731.
KEGGspo:SPBC18H10.02.

Organism-specific databases

PomBaseSPBC18H10.02.

Phylogenomic databases

eggNOGCOG1022.
HOGENOMHOG000159459.
KOK01897.
OMAGISVHNM.
OrthoDBEOG7CCC0K.
PhylomeDBO60135.

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

NextBio20801853.

Entry information

Entry nameLCF1_SCHPO
AccessionPrimary (citable) accession number: O60135
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: August 1, 1998
Last modified: May 14, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names