ID   DLP1_SCHPO              Reviewed;         294 AA.
AC   O13851;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 130.
DE   RecName: Full=Decaprenyl-diphosphate synthase subunit 2;
DE            EC=2.5.1.91;
DE   AltName: Full=All-trans-decaprenyl-diphosphate synthase subunit 2;
DE   AltName: Full=Decaprenyl pyrophosphate synthase subunit 2;
GN   Name=dlp1; ORFNames=SPAC19G12.12;
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], FUNCTION, AND 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).
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: Supplies decaprenyl diphosphate, the precursor for the side
CC       chain of the isoprenoid quinones ubiquinone-10.
CC       {ECO:0000269|PubMed:14519123}.
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   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC   -!- SUBUNIT: Heterotetramer of 2 dps1 and 2 dlp1 subunits.
CC       {ECO:0000269|PubMed:14519123}.
CC   -!- INTERACTION:
CC       O13851; P0AD57: ispB; Xeno; NbExp=2; IntAct=EBI-7701234, EBI-1131851;
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR   EMBL; AB118853; BAC82458.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB10123.1; -; Genomic_DNA.
DR   PIR; T37999; T37999.
DR   RefSeq; NP_594427.1; NM_001019856.2.
DR   AlphaFoldDB; O13851; -.
DR   SMR; O13851; -.
DR   BioGRID; 279062; 3.
DR   IntAct; O13851; 1.
DR   MINT; O13851; -.
DR   STRING; 4896.SPAC19G12.12.1; -.
DR   MaxQB; O13851; -.
DR   PaxDb; O13851; -.
DR   EnsemblFungi; SPAC19G12.12.1; SPAC19G12.12.1:pep; SPAC19G12.12.
DR   GeneID; 2542608; -.
DR   KEGG; spo:SPAC19G12.12; -.
DR   PomBase; SPAC19G12.12; dlp1.
DR   VEuPathDB; FungiDB:SPAC19G12.12; -.
DR   eggNOG; KOG0776; Eukaryota.
DR   HOGENOM; CLU_947168_0_0_1; -.
DR   InParanoid; O13851; -.
DR   OMA; IHINIRE; -.
DR   PhylomeDB; O13851; -.
DR   BRENDA; 2.5.1.91; 5613.
DR   Reactome; R-SPO-2142789; Ubiquinol biosynthesis.
DR   UniPathway; UPA00232; -.
DR   PRO; PR:O13851; -.
DR   Proteomes; UP000002485; Chromosome I.
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:0004659; F:prenyltransferase activity; IBA:GO_Central.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IMP:PomBase.
DR   Gene3D; 1.10.600.10; -; 1.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR000092; Polyprenyl_synt.
DR   Pfam; PF00348; polyprenyl_synt; 1.
DR   SUPFAM; SSF48576; SSF48576; 1.
PE   1: Evidence at protein level;
KW   Isoprene biosynthesis; Reference proteome; Transferase;
KW   Ubiquinone biosynthesis.
FT   CHAIN           1..294
FT                   /note="Decaprenyl-diphosphate synthase subunit 2"
FT                   /id="PRO_0000123981"
SQ   SEQUENCE   294 AA;  32411 MW;  F861EA3812D4A54D CRC64;
     MSFPFASLLK RPSAISSLLS LKKPGSWSSI LLKAVGVLSR DSRWHSDLLK MLTEEMDSLN
     GQINTWTDNN PLLDEITKPY RKSSTRFFHP LLVLLMSRAS VNGDPPSQQL FQRYKQLARV
     TELIHAANII HINIGEEQSN EQIKLATLVG DYLLGKASVD LAHLENNAIT EIMASVIANL
     VEGHFGSRQN GSVGLSNERT ILLQSAFMPA KACLCASILN NSSQYINDAC FNYGKFLGLS
     LQLAHKPVSP DAQVLQKNND ILKTYVENAK SSLSVFPDIE AKQALMEIAN SVSK