COQ1_YEAST
ID COQ1_YEAST Reviewed; 473 AA.
AC P18900; D6VQ04;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Hexaprenyl pyrophosphate synthase, mitochondrial;
DE Short=HPS;
DE EC=2.5.1.-;
DE Flags: Precursor;
GN Name=COQ1; OrderedLocusNames=YBR003W; ORFNames=YBR0109;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=D273-10B/A1;
RX PubMed=2198286; DOI=10.1016/s0021-9258(19)38280-8;
RA Ashby M.N., Edwards P.A.;
RT "Elucidation of the deficiency in two yeast coenzyme Q mutants.
RT Characterization of the structural gene encoding hexaprenyl pyrophosphate
RT synthetase.";
RL J. Biol. Chem. 265:13157-13164(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-285.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091860; DOI=10.1002/yea.320100006;
RA Wolfe K.H., Lohan A.J.E.;
RT "Sequence around the centromere of Saccharomyces cerevisiae chromosome II:
RT similarity of CEN2 to CEN4.";
RL Yeast 10:S41-S46(1994).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Assembly of polyisoprenoid side chains. The polyprenyl
CC synthase of coenzyme Q biosynthesis catalyzes the formation from
CC isopentenyl diphosphate of all trans-polyprenyl pyrophosphates
CC generally ranging in length of between 6 and 10 isoprene units
CC depending on the species.
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 -!- INTERACTION:
CC P18900; P10592: SSA2; NbExp=2; IntAct=EBI-4912, EBI-8603;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane
CC protein; Matrix side.
CC -!- MISCELLANEOUS: Present with 1560 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; J05547; AAA34686.1; -; Genomic_DNA.
DR EMBL; Z35872; CAA84939.1; -; Genomic_DNA.
DR EMBL; AY558099; AAS56425.1; -; Genomic_DNA.
DR EMBL; Z26494; CAA81272.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07124.1; -; Genomic_DNA.
DR PIR; A36625; XUBYTP.
DR RefSeq; NP_009557.1; NM_001178351.1.
DR AlphaFoldDB; P18900; -.
DR SMR; P18900; -.
DR BioGRID; 32704; 49.
DR DIP; DIP-1103N; -.
DR IntAct; P18900; 8.
DR MINT; P18900; -.
DR STRING; 4932.YBR003W; -.
DR CarbonylDB; P18900; -.
DR MaxQB; P18900; -.
DR PaxDb; P18900; -.
DR PRIDE; P18900; -.
DR EnsemblFungi; YBR003W_mRNA; YBR003W; YBR003W.
DR GeneID; 852288; -.
DR KEGG; sce:YBR003W; -.
DR SGD; S000000207; COQ1.
DR VEuPathDB; FungiDB:YBR003W; -.
DR eggNOG; KOG0776; Eukaryota.
DR GeneTree; ENSGT00940000153498; -.
DR HOGENOM; CLU_014015_1_0_1; -.
DR InParanoid; P18900; -.
DR OMA; RVAKYYT; -.
DR BioCyc; MetaCyc:YBR003W-MON; -.
DR BioCyc; YEAST:YBR003W-MON; -.
DR Reactome; R-SCE-2142789; Ubiquinol biosynthesis.
DR UniPathway; UPA00232; -.
DR PRO; PR:P18900; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P18900; protein.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IDA:WormBase.
DR GO; GO:0005739; C:mitochondrion; IMP:SGD.
DR GO; GO:1990234; C:transferase complex; IBA:GO_Central.
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; IMP:SGD.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IBA:GO_Central.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IMP:SGD.
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; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..473
FT /note="Hexaprenyl pyrophosphate synthase, mitochondrial"
FT /id="PRO_0000016477"
FT BINDING 84
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 87
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:Q12051"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 197
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 197
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 202
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 323
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 324
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 361
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
SQ SEQUENCE 473 AA; 52560 MW; 676191C9DCA18E3A CRC64;
MFQRSGAAHH IKLISSRRCR FKSSFAVALN AASKLVTPKI LWNNPISLVS KEMNTLAKNI
VALIGSGHPV LNKVTSYYFE TEGKKVRPLL VLLLSRALSE IPMTERNHLK IDKSDVPEDP
IYSKPSQNQL FQRPASSISP LHILHGIKPL NPLTKGPEPL PEETFDKQRG ILPKQRRLAE
IVEMIHTASL LHDDVIDHSD TRRGRPSGNA AFTNKMAVLA GDFLLGRATV SISRLHNPEV
VELMSNSIAN LVEGEFMQLK NTSIDADIDT IENGHKLLPV PSKKLEVKEH DFRVPSRQQG
LQLSHDQIIE TAFEYYIHKT YLKTAALISK SCRCAAILSG ASPAVIDECY DFGRNLGICF
QLVDDMLDFT VSGKDLGKPS GADLKLGIAT APVLFAWKED PSLGPLISRN FSERGDVEKT
IDSVRLHNGI AKTKILAEEY RDKALQNLRD SLPESDARSA LEFLTNSILT RRK
