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UniProtKB - O60135 (LCF1_SCHPO)
Protein
Long-chain-fatty-acid--CoA ligase 1
Gene
lcf1
Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
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 PublicationCatalytic activityi
- EC:6.2.1.3
Cofactori
Mg2+By similarity
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 246 – 257 | ATPBy similarityAdd BLAST | 12 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- long-chain fatty acid-CoA ligase activity Source: GO_Central
- 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: GO_Central
- long-chain fatty-acyl-CoA metabolic process Source: PomBase
Keywordsi
Molecular function | Ligase |
Biological process | Fatty acid metabolism, Lipid metabolism |
Ligand | ATP-binding, Magnesium, Nucleotide-binding |
Enzyme and pathway databases
Reactomei | R-SPO-434313, Intracellular metabolism of fatty acids regulates insulin secretion R-SPO-75876, 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 |
Organismi | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
Taxonomic identifieri | 284812 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › |
Proteomesi |
|
Organism-specific databases
PomBasei | SPBC18H10.02, lcf1 |
VEuPathDBi | FungiDB:SPBC18H10.02 |
Subcellular locationi
Endoplasmic reticulum
- endoplasmic reticulum Source: PomBase
Plasma Membrane
- plasma membrane Source: GO_Central
Other locations
- lipid droplet Source: GO_Central
- membrane Source: GO_Central
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000193118 | 1 – 676 | Long-chain-fatty-acid--CoA ligase 1Add BLAST | 676 |
Proteomic databases
MaxQBi | O60135 |
PaxDbi | O60135 |
PTM databases
iPTMneti | O60135 |
Interactioni
Protein-protein interaction databases
BioGRIDi | 277254, 6 interactors |
STRINGi | 4896.SPBC18H10.02.1 |
Family & Domainsi
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 511 – 560 | FACSBy similarityAdd BLAST | 50 |
Domaini
The FACS motif is required for catalytic activity and substrate specificity.By similarity
Sequence similaritiesi
Belongs to the ATP-dependent AMP-binding enzyme family.Curated
Phylogenomic databases
eggNOGi | KOG1180, Eukaryota |
HOGENOMi | CLU_000022_45_2_1 |
InParanoidi | O60135 |
OMAi | KIFQWAA |
PhylomeDBi | O60135 |
Family and domain databases
Gene3Di | 3.40.50.12780, 1 hit |
InterProi | View protein in InterPro IPR020845, AMP-binding_CS IPR000873, AMP-dep_Synth/Lig IPR042099, ANL_N_sf |
Pfami | View protein in Pfam PF00501, AMP-binding, 1 hit |
PROSITEi | View protein in PROSITE PS00455, AMP_BINDING, 1 hit |
i Sequence
Sequence statusi: Complete.
O60135-1 [UniParc]FASTAAdd to basket
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CU329671 Genomic DNA Translation: CAA18399.1 |
PIRi | T39766 |
RefSeqi | NP_595726.1, NM_001021624.2 |
Genome annotation databases
EnsemblFungii | SPBC18H10.02.1; SPBC18H10.02.1:pep; SPBC18H10.02 |
GeneIDi | 2540731 |
KEGGi | spo:SPBC18H10.02 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CU329671 Genomic DNA Translation: CAA18399.1 |
PIRi | T39766 |
RefSeqi | NP_595726.1, NM_001021624.2 |
3D structure databases
AlphaFoldDBi | O60135 |
SMRi | O60135 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 277254, 6 interactors |
STRINGi | 4896.SPBC18H10.02.1 |
PTM databases
iPTMneti | O60135 |
Proteomic databases
MaxQBi | O60135 |
PaxDbi | O60135 |
Genome annotation databases
EnsemblFungii | SPBC18H10.02.1; SPBC18H10.02.1:pep; SPBC18H10.02 |
GeneIDi | 2540731 |
KEGGi | spo:SPBC18H10.02 |
Organism-specific databases
PomBasei | SPBC18H10.02, lcf1 |
VEuPathDBi | FungiDB:SPBC18H10.02 |
Phylogenomic databases
eggNOGi | KOG1180, Eukaryota |
HOGENOMi | CLU_000022_45_2_1 |
InParanoidi | O60135 |
OMAi | KIFQWAA |
PhylomeDBi | O60135 |
Enzyme and pathway databases
Reactomei | R-SPO-434313, Intracellular metabolism of fatty acids regulates insulin secretion R-SPO-75876, Synthesis of very long-chain fatty acyl-CoAs |
Miscellaneous databases
PROi | PR:O60135 |
Family and domain databases
Gene3Di | 3.40.50.12780, 1 hit |
InterProi | View protein in InterPro IPR020845, AMP-binding_CS IPR000873, AMP-dep_Synth/Lig IPR042099, ANL_N_sf |
Pfami | View protein in Pfam PF00501, AMP-binding, 1 hit |
PROSITEi | View protein in PROSITE PS00455, AMP_BINDING, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | LCF1_SCHPO | |
Accessioni | O60135Primary (citable) accession number: O60135 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | September 13, 2005 |
Last sequence update: | August 1, 1998 | |
Last modified: | May 25, 2022 | |
This is version 131 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- Schizosaccharomyces pombe
Schizosaccharomyces pombe: entries and gene names - SIMILARITY comments
Index of protein domains and families