LCF1_SCHPO
ID LCF1_SCHPO Reviewed; 676 AA.
AC O60135;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase 1;
DE EC=6.2.1.3;
DE AltName: Full=Fatty acid activator 1;
DE AltName: Full=Long-chain acyl-CoA synthetase 1;
GN Name=lcf1; ORFNames=SPBC18H10.02;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=12684881; DOI=10.1007/s00438-003-0841-3;
RA Oshiro T., Aiba H., Mizuno T.;
RT "A defect in a fatty acyl-CoA synthetase gene, lcf1+, results in a decrease
RT in viability after entry into the stationary phase in fission yeast.";
RL Mol. Genet. Genomics 269:437-442(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Esterification, concomitant with transport, of exogenous
CC long-chain fatty acids into metabolically active CoA thioesters for
CC subsequent degradation or incorporation into phospholipids. It may
CC supplement intracellular myristoyl-CoA pools from exogenous myristate.
CC Preferentially acts on C12:0-C16:0 fatty acids with myristic and
CC pentadecanic acid (C15:0) having the highest activities (By
CC similarity). Appears to play a role in the maintenance of cell
CC viability during stationary phase. {ECO:0000250,
CC ECO:0000269|PubMed:12684881}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-
CC CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- DOMAIN: The FACS motif is required for catalytic activity and substrate
CC specificity. {ECO:0000250|UniProtKB:P30624}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAA18399.1; -; Genomic_DNA.
DR PIR; T39766; T39766.
DR RefSeq; NP_595726.1; NM_001021624.2.
DR AlphaFoldDB; O60135; -.
DR SMR; O60135; -.
DR BioGRID; 277254; 6.
DR STRING; 4896.SPBC18H10.02.1; -.
DR iPTMnet; O60135; -.
DR MaxQB; O60135; -.
DR PaxDb; O60135; -.
DR PRIDE; O60135; -.
DR EnsemblFungi; SPBC18H10.02.1; SPBC18H10.02.1:pep; SPBC18H10.02.
DR GeneID; 2540731; -.
DR KEGG; spo:SPBC18H10.02; -.
DR PomBase; SPBC18H10.02; lcf1.
DR VEuPathDB; FungiDB:SPBC18H10.02; -.
DR eggNOG; KOG1180; Eukaryota.
DR HOGENOM; CLU_000022_45_2_1; -.
DR InParanoid; O60135; -.
DR OMA; KIFQWAA; -.
DR PhylomeDB; O60135; -.
DR Reactome; R-SPO-434313; Intracellular metabolism of fatty acids regulates insulin secretion.
DR Reactome; R-SPO-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR PRO; PR:O60135; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005811; C:lipid droplet; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IBA:GO_Central.
DR GO; GO:0090432; F:myristoyl-CoA ligase activity; IMP:PomBase.
DR GO; GO:0090434; F:oleoyl-CoA ligase activity; IMP:PomBase.
DR GO; GO:0090433; F:palmitoyl-CoA ligase activity; IMP:PomBase.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; IMP:PomBase.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW ATP-binding; Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..676
FT /note="Long-chain-fatty-acid--CoA ligase 1"
FT /id="PRO_0000193118"
FT MOTIF 511..560
FT /note="FACS"
FT /evidence="ECO:0000250|UniProtKB:P30624"
FT BINDING 246..257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69451"
SQ SEQUENCE 676 AA; 75966 MW; 98EF74D4A1C5AA41 CRC64;
MKVQSKAISK PKEHESAIYR NANFPDHLVE TYSDDVHTLF DVFRHSVKQF GNKKAMGYRN
LVKEHVETKM VTKVVDGEKK EVPKSWSYFE LSDYNYLSFN DIYDKALRYA GALRKLGLNK
GDKFELYAPT SAFWLLTAEA CLSQSMTIVT AYDTLGEEGL LHSLRESGVR GMYTEGHLLK
TLVNPLKEIE SLEVIIYRND AKEEDIKTIQ EIRPNLKLIK FADFEKMSPP VEPDPPSPEE
ICCIMYTSGS TGLPKGVILS HKNMVAIVTA IVKHVPEVTS KDYLLAYLPL AHILEFAFEN
ICLAWGGTIG YANVRTLVDT NCRNCKGDIN TFRPTIMVGV PAVWEMVRKG IMSKLNAASA
VKRSVFWTAY YTKAKLMRHN LPGSCVLDTA VFNKIRSMGT GGRLRYTLSG GSALSPDTKR
FLSIVLCPML IGYGLTEISA AAMVQNPACF NLDDSAGSLL PCTEMKLVDC EEGNYNSHGH
PPRGEIWLRG PSLTRGYLNR DKENKESFTP DGWFRTGDVG ELTPEGLLRI IDRKKNLVKT
QNGEYIALEK LESRYRTSSL VSNICVYADQ TKVKPLAIIV PNEPVVRKLA TEQAGLSPDA
SWEEVCHNKK VRQLVYDDLI RIGRSHHFAN IELIQNVVLV PIEFTPENGL VTAAQKLQRR
KILDRFKKEI DAAYAE
