ACL1_SCHPO
ID ACL1_SCHPO Reviewed; 615 AA.
AC Q9P7W3; P78844;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Probable ATP-citrate synthase subunit 1;
DE EC=2.3.3.8;
DE AltName: Full=ATP-citrate (pro-S-)-lyase 1;
DE AltName: Full=Citrate cleavage enzyme subunit 1;
GN ORFNames=SPBC1703.07;
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 [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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 293-615.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Catalyzes the formation of cytosolic acetyl-CoA, which is
CC mainly used for the biosynthesis of fatty acids and sterols.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + ADP + oxaloacetate + phosphate = ATP + citrate +
CC CoA; Xref=Rhea:RHEA:21160, ChEBI:CHEBI:16452, ChEBI:CHEBI:16947,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:456216; EC=2.3.3.8;
CC -!- SUBUNIT: Composed of two subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit
CC family. {ECO:0000305}.
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DR EMBL; CU329671; CAB66451.1; -; Genomic_DNA.
DR EMBL; D89194; BAA13855.1; -; mRNA.
DR PIR; T42753; T42753.
DR PIR; T50320; T50320.
DR RefSeq; NP_596202.1; NM_001022121.2.
DR AlphaFoldDB; Q9P7W3; -.
DR SMR; Q9P7W3; -.
DR BioGRID; 276425; 7.
DR STRING; 4896.SPBC1703.07.1; -.
DR iPTMnet; Q9P7W3; -.
DR MaxQB; Q9P7W3; -.
DR PaxDb; Q9P7W3; -.
DR PRIDE; Q9P7W3; -.
DR EnsemblFungi; SPBC1703.07.1; SPBC1703.07.1:pep; SPBC1703.07.
DR GeneID; 2539879; -.
DR KEGG; spo:SPBC1703.07; -.
DR PomBase; SPBC1703.07; -.
DR VEuPathDB; FungiDB:SPBC1703.07; -.
DR eggNOG; KOG1254; Eukaryota.
DR HOGENOM; CLU_006587_4_1_1; -.
DR InParanoid; Q9P7W3; -.
DR OMA; IHVPDTF; -.
DR PhylomeDB; Q9P7W3; -.
DR PRO; PR:Q9P7W3; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003878; F:ATP citrate synthase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; ISS:PomBase.
DR GO; GO:0006101; P:citrate metabolic process; IC:PomBase.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; NAS:PomBase.
DR Gene3D; 1.10.230.10; -; 1.
DR Gene3D; 3.40.50.261; -; 1.
DR InterPro; IPR016143; Citrate_synth-like_sm_a-sub.
DR InterPro; IPR002020; Citrate_synthase.
DR InterPro; IPR036969; Citrate_synthase_sf.
DR InterPro; IPR033847; Citrt_syn/SCS-alpha_CS.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR005811; CoA_ligase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR Pfam; PF00285; Citrate_synt; 1.
DR Pfam; PF02629; CoA_binding; 1.
DR Pfam; PF00549; Ligase_CoA; 1.
DR SMART; SM00881; CoA_binding; 1.
DR SUPFAM; SSF48256; SSF48256; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
DR PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Lipid biosynthesis; Lipid metabolism; Magnesium;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..615
FT /note="Probable ATP-citrate synthase subunit 1"
FT /id="PRO_0000102786"
FT ACT_SITE 280
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 221..241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 272..298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 299..309
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 615 AA; 67204 MW; D9998607127639C4 CRC64;
MAGSVDKPSY ELFSKDTRAF VYGMQTKAVQ GMLDFDYMCG RTVPSVAAII YTFGSQSISK
LYWGTKEILL PVYRTIEEAC TKHPEVDVVV NFASSRSAYA STMELMEFPQ IRCIAIIAEG
VPERRAREIL VTSKEKNVVI IGPATVGGIK PGCFKIGNTG GMMDNIVASK LYRPGSVAYV
SKSGGMSNEL NNIISHTTDG VYEGIAIGGD RYPGTTFIDH LIRFEADPAC KLMVLLGEVG
GVEEYRVIEA VKNGTIKKPI VAWAIGTCSS MFKTEVQFGH AGSFANSELE TAVAKNQAMR
EAGIYVPETF EKLPALLQEV YEGLVKKGVI VPQPEVAPPN IPLDYAWAKE LGLVRKPSSF
ICTISNDRGS ELTYNNVPIS KVFEEELGIG GVISLLWLRR RLPSYATKFL EMVLQLTADH
GPCVSGAMNT IITTRAGKDL ISSLVAGLLT IGTRFGGALD GAAQEFSKAY DAGLSPRAFV
DSCRKANKLI PGIGHRIKSR NNPDLRVELV KGYVKKNFPS TKLLDYALAV ENVTTSKKDN
LILNVDGCIA VCFVDLLRNC GAFTLEEANE YINLGILNGM FVLGRSIGLI GHHLDQKRLR
APLYRHPWDD FLYLS
