DPS1_DICDI
ID DPS1_DICDI Reviewed; 456 AA.
AC Q54VJ9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Decaprenyl-diphosphate synthase;
DE EC=2.5.1.91;
DE AltName: Full=All-trans-decaprenyl-diphosphate synthase subunit 1;
DE AltName: Full=Coenzyme Q biosynthesis protein 1;
DE AltName: Full=Decaprenyl pyrophosphate synthase;
DE AltName: Full=Trans-prenyltransferase;
DE Short=TPT;
GN Name=coq1; ORFNames=DDB_G0280293;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Supplies decaprenyl diphosphate, the precursor for the side
CC chain of the isoprenoid quinones ubiquinone-10. {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; AAFI02000035; EAL67373.1; -; Genomic_DNA.
DR RefSeq; XP_641356.1; XM_636264.1.
DR AlphaFoldDB; Q54VJ9; -.
DR SMR; Q54VJ9; -.
DR STRING; 44689.DDB0231590; -.
DR PaxDb; Q54VJ9; -.
DR EnsemblProtists; EAL67373; EAL67373; DDB_G0280293.
DR GeneID; 8622490; -.
DR KEGG; ddi:DDB_G0280293; -.
DR dictyBase; DDB_G0280293; coq1.
DR eggNOG; KOG0776; Eukaryota.
DR HOGENOM; CLU_014015_2_2_1; -.
DR InParanoid; Q54VJ9; -.
DR OMA; RVAKYYT; -.
DR PhylomeDB; Q54VJ9; -.
DR Reactome; R-DDI-2142789; Ubiquinol biosynthesis.
DR UniPathway; UPA00232; -.
DR PRO; PR:Q54VJ9; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005739; C:mitochondrion; ISS:dictyBase.
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:0000010; F:trans-hexaprenyltranstransferase activity; ISS:dictyBase.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IBA:GO_Central.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central.
DR GO; GO:0006743; P:ubiquinone metabolic process; ISS:dictyBase.
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; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE 3: Inferred from homology;
KW Isoprene biosynthesis; Magnesium; Metal-binding; Reference proteome;
KW Transferase; Ubiquinone biosynthesis.
FT CHAIN 1..456
FT /note="Decaprenyl-diphosphate synthase"
FT /id="PRO_0000328212"
FT BINDING 183
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 186
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 216
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 227
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 227
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 232
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 307
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 308
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
SQ SEQUENCE 456 AA; 51089 MW; 756C1AD338D59C32 CRC64;
MSRLIINKSN SRICNTIVKN YLIQTKYTLQ QQQHQQQQQQ QQYVRSYCSL QQPKPSKPNM
IEIVTHFFDK VKNKSFIIEN YLNNPIPEQQ QQLNKNIKIN NTDKDNDTLE QIQLLDPLNN
LGKRKGNEIF KVVENDLSNM THNIMKTITD GVSANSTYSP SPSKKTHPIL SSISSYYFEL
KGKRIRPTIV LLLSKALSST VHGSQLKLAE IVEMIHTASL VHDDVIDEAS TRRDVISINH
SYTNKLAILC GDYLLARASV VLSTIRNPDV TECMSTALAE LVEGEFMQAK SNGVVSFDNY
LQKTYLKTGS LITNSCRSAA ILSGADSNII NISTEFGKNL GLAFQIVDDL LDYTGSAEEC
GKATSVDLTL GLATAPVLYA TQEFPQLEKL IKRKFSEIGD VEEAKRLVAL SKGIEKTRNL
AIEYCNRAIQ SLLKLPQSES RDLLITLSHI VVTRTK
