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Protein

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

Gene

lcf1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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 (By similarity). Appears to play a role in the maintenance of cell viability during stationary phase.By similarity1 Publication

Catalytic activityi

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

Cofactori

Mg2+By similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • myristoyl-CoA ligase activity Source: PomBase
  • oleoyl-CoA ligase activity Source: PomBase
  • palmitoyl-CoA ligase activity Source: PomBase

GO - Biological processi

  • long-chain fatty acid metabolic process Source: PomBase
  • long-chain fatty-acyl-CoA metabolic process Source: PomBase
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

ReactomeiREACT_350968. 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:lcf1
ORF Names:SPBC18H10.02
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC18H10.02.
PomBaseiSPBC18H10.02. lcf1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • endoplasmic reticulum Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 676676Long-chain-fatty-acid--CoA ligase 1PRO_0000193118Add
BLAST

Proteomic databases

MaxQBiO60135.
PaxDbiO60135.

Interactioni

Protein-protein interaction databases

BioGridi277254. 1 interaction.
MINTiMINT-4677511.

Structurei

3D structure databases

ProteinModelPortaliO60135.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1022.
HOGENOMiHOG000159459.
InParanoidiO60135.
KOiK01897.
OMAiENICLAW.
OrthoDBiEOG7CCC0K.
PhylomeDBiO60135.

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.

O60135-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVQSKAISK PKEHESAIYR NANFPDHLVE TYSDDVHTLF DVFRHSVKQF
60 70 80 90 100
GNKKAMGYRN LVKEHVETKM VTKVVDGEKK EVPKSWSYFE LSDYNYLSFN
110 120 130 140 150
DIYDKALRYA GALRKLGLNK GDKFELYAPT SAFWLLTAEA CLSQSMTIVT
160 170 180 190 200
AYDTLGEEGL LHSLRESGVR GMYTEGHLLK TLVNPLKEIE SLEVIIYRND
210 220 230 240 250
AKEEDIKTIQ EIRPNLKLIK FADFEKMSPP VEPDPPSPEE ICCIMYTSGS
260 270 280 290 300
TGLPKGVILS HKNMVAIVTA IVKHVPEVTS KDYLLAYLPL AHILEFAFEN
310 320 330 340 350
ICLAWGGTIG YANVRTLVDT NCRNCKGDIN TFRPTIMVGV PAVWEMVRKG
360 370 380 390 400
IMSKLNAASA VKRSVFWTAY YTKAKLMRHN LPGSCVLDTA VFNKIRSMGT
410 420 430 440 450
GGRLRYTLSG GSALSPDTKR FLSIVLCPML IGYGLTEISA AAMVQNPACF
460 470 480 490 500
NLDDSAGSLL PCTEMKLVDC EEGNYNSHGH PPRGEIWLRG PSLTRGYLNR
510 520 530 540 550
DKENKESFTP DGWFRTGDVG ELTPEGLLRI IDRKKNLVKT QNGEYIALEK
560 570 580 590 600
LESRYRTSSL VSNICVYADQ TKVKPLAIIV PNEPVVRKLA TEQAGLSPDA
610 620 630 640 650
SWEEVCHNKK VRQLVYDDLI RIGRSHHFAN IELIQNVVLV PIEFTPENGL
660 670
VTAAQKLQRR KILDRFKKEI DAAYAE
Length:676
Mass (Da):75,966
Last modified:August 1, 1998 - v1
Checksum:i98EF74D4A1C5AA41
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA18399.1.
PIRiT39766.
RefSeqiNP_595726.1. NM_001021624.2.

Genome annotation databases

EnsemblFungiiSPBC18H10.02.1; SPBC18H10.02.1:pep; SPBC18H10.02.
GeneIDi2540731.
KEGGispo:SPBC18H10.02.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA18399.1.
PIRiT39766.
RefSeqiNP_595726.1. NM_001021624.2.

3D structure databases

ProteinModelPortaliO60135.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277254. 1 interaction.
MINTiMINT-4677511.

Proteomic databases

MaxQBiO60135.
PaxDbiO60135.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC18H10.02.1; SPBC18H10.02.1:pep; SPBC18H10.02.
GeneIDi2540731.
KEGGispo:SPBC18H10.02.

Organism-specific databases

EuPathDBiFungiDB:SPBC18H10.02.
PomBaseiSPBC18H10.02. lcf1.

Phylogenomic databases

eggNOGiCOG1022.
HOGENOMiHOG000159459.
InParanoidiO60135.
KOiK01897.
OMAiENICLAW.
OrthoDBiEOG7CCC0K.
PhylomeDBiO60135.

Enzyme and pathway databases

ReactomeiREACT_350968. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

NextBioi20801853.
PROiO60135.

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. "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.
    , 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.

Entry informationi

Entry nameiLCF1_SCHPO
AccessioniPrimary (citable) accession number: O60135
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: August 1, 1998
Last modified: July 22, 2015
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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.