DPS1_SCHPO
ID DPS1_SCHPO Reviewed; 378 AA.
AC O43091; P78914; Q96WV7;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Decaprenyl-diphosphate synthase subunit 1;
DE EC=2.5.1.91;
DE AltName: Full=All-trans-decaprenyl-diphosphate synthase subunit 1;
DE AltName: Full=Decaprenyl pyrophosphate synthase subunit 1;
GN Name=dps1; Synonyms=dps; ORFNames=SPBPJ4664.01, SPBPJ694.01;
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 [MRNA].
RX PubMed=9133618; DOI=10.1093/oxfordjournals.jbchem.a021614;
RA Suzuki K., Okada K., Kamiya Y., Zhu X.F., Nakagawa T., Kawamukai M.,
RA Matsuda H.;
RT "Analysis of the decaprenyl diphosphate synthase (dps) gene in fission
RT yeast suggests a role of ubiquinone as an antioxidant.";
RL J. Biochem. 121:496-505(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 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 [4]
RP SUBUNIT.
RX PubMed=14519123; DOI=10.1046/j.1432-1033.2003.03804.x;
RA Saiki R., Nagata A., Uchida N., Kainou T., Matsuda H., Kawamukai M.;
RT "Fission yeast decaprenyl diphosphate synthase consists of Dps1 and the
RT newly characterized Dlp1 protein in a novel heterotetrameric structure.";
RL Eur. J. Biochem. 270:4113-4121(2003).
CC -!- FUNCTION: Supplies decaprenyl diphosphate, the precursor for the side
CC chain of the isoprenoid quinones ubiquinone-10.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate =
CC all-trans-decaprenyl diphosphate + 7 diphosphate;
CC Xref=Rhea:RHEA:27802, ChEBI:CHEBI:33019, ChEBI:CHEBI:60721,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.91;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC -!- SUBUNIT: Heterotetramer of 2 dps1 and 2 dlp1 subunits.
CC {ECO:0000269|PubMed:14519123}.
CC -!- INTERACTION:
CC O43091; P0AD57: ispB; Xeno; NbExp=2; IntAct=EBI-7701164, EBI-1131851;
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13926.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D84311; BAA12314.1; -; mRNA.
DR EMBL; D89265; BAA13926.1; ALT_FRAME; mRNA.
DR EMBL; CU329671; CAB66154.1; -; Genomic_DNA.
DR PIR; JC5429; JC5429.
DR PIR; T43193; T43193.
DR RefSeq; NP_595276.1; NM_001021183.2.
DR AlphaFoldDB; O43091; -.
DR SMR; O43091; -.
DR BioGRID; 277911; 5.
DR IntAct; O43091; 1.
DR MINT; O43091; -.
DR STRING; 4896.SPBPJ4664.01.1; -.
DR MaxQB; O43091; -.
DR PaxDb; O43091; -.
DR EnsemblFungi; SPBPJ4664.01.1; SPBPJ4664.01.1:pep; SPBPJ4664.01.
DR GeneID; 2541402; -.
DR KEGG; spo:SPBPJ4664.01; -.
DR PomBase; SPBPJ4664.01; dps1.
DR VEuPathDB; FungiDB:SPBPJ4664.01; -.
DR eggNOG; KOG0776; Eukaryota.
DR HOGENOM; CLU_014015_1_0_1; -.
DR OMA; GKQMRPM; -.
DR PhylomeDB; O43091; -.
DR BRENDA; 2.5.1.91; 5613.
DR Reactome; R-SPO-2142789; Ubiquinol biosynthesis.
DR UniPathway; UPA00232; -.
DR PRO; PR:O43091; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0032476; C:decaprenyl diphosphate synthase complex; IPI:PomBase.
DR GO; GO:0005743; C:mitochondrial inner membrane; IC:PomBase.
DR GO; GO:0005739; C:mitochondrion; IDA:PomBase.
DR GO; GO:1990234; C:transferase complex; IBA:GO_Central.
DR GO; GO:0097269; F:all-trans-decaprenyl-diphosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004659; F:prenyltransferase activity; IBA:GO_Central.
DR GO; GO:0010142; P:farnesyl diphosphate biosynthetic process, mevalonate pathway; IMP:PomBase.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IBA:GO_Central.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IDA:PomBase.
DR CDD; cd00685; Trans_IPPS_HT; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR InterPro; IPR033749; Polyprenyl_synt_CS.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE 1: Evidence at protein level;
KW Isoprene biosynthesis; Magnesium; Metal-binding; Reference proteome;
KW Transferase; Ubiquinone biosynthesis.
FT CHAIN 1..378
FT /note="Decaprenyl-diphosphate synthase subunit 1"
FT /id="PRO_0000123977"
FT BINDING 72
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 75
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 130
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 137
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 137
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 141
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 141
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 146
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 229
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT CONFLICT 89
FT /note="C -> F (in Ref. 2; BAA13926)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="I -> T (in Ref. 2; BAA13926)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="A -> V (in Ref. 2; BAA13926)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="T -> S (in Ref. 2; BAA13926)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="T -> P (in Ref. 2; BAA13926)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="K -> I (in Ref. 2; BAA13926)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 378 AA; 42047 MW; 84B3300F84EBB06E CRC64;
MIQYVYLKHM RKLWSLGKVR STVLRFSTTN RNASHLIKNE LEQISPGIRQ MLNSNSEFLE
ECSKYYTIAQ GKQMRPSLVL LMSKATSLCH GIDRSVVGDK YIDDDDLRSF STGQILPSQL
RLAQITEMIH IASLLHDDVI DHANVRRGSP SSNVAFGNRR SILAGNFILA RASTAMARLR
NPQVTELLAT VIADLVRGEF LQLKNTMDPS SLEIKQSNFD YYIEKSFLKT ASLISKSCKA
STILGQCSPT VATAAGEYGR CIGTAFQLMD DVLDYTSKDD TLGKAAGADL KLGLATAPVL
FAWKKYPELG AMIVNRFNHP SDIQRARSLV ECTDAIEQTI TWAKEYIKKA KDSLLCLPDS
PARKALFALA DKVITRKK
