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P18900 (COQ1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hexaprenyl pyrophosphate synthase, mitochondrial
Short name=HPS
EC=2.5.1.-
Gene names
Name:COQ1
Ordered Locus Names:YBR003W
ORF Names:YBR0109
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Assembly of polyisoprenoid side chains. The polyprenyl synthase of coenzyme Q biosynthesis catalyzes the formation from isopentenyl diphosphate of all trans-polyprenyl pyrophosphates generally ranging in length of between 6 and 10 isoprene units depending on the species.

Cofactor

Binds 3 magnesium ions per subunit By similarity.

Pathway

Cofactor biosynthesis; ubiquinone biosynthesis.

Subcellular location

Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.

Miscellaneous

Present with 1560 molecules/cell in log phase SD medium. Ref.6

Sequence similarities

Belongs to the FPP/GGPP synthase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SSA2P105922EBI-4912,EBI-8603

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 473Hexaprenyl pyrophosphate synthase, mitochondrialPRO_0000016477

Sites

Metal binding1931Magnesium 1 By similarity
Metal binding1931Magnesium 2 By similarity
Metal binding1971Magnesium 1 By similarity
Metal binding1971Magnesium 2 By similarity
Metal binding3641Magnesium 3 By similarity
Binding site841Isopentenyl diphosphate By similarity
Binding site871Isopentenyl diphosphate By similarity
Binding site1861Isopentenyl diphosphate By similarity
Binding site2021Polyprenyl diphosphate By similarity
Binding site2031Isopentenyl diphosphate By similarity
Binding site3231Polyprenyl diphosphate By similarity
Binding site3241Polyprenyl diphosphate By similarity
Binding site3611Polyprenyl diphosphate By similarity
Binding site3781Polyprenyl diphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
P18900 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 676191C9DCA18E3A

FASTA47352,560
        10         20         30         40         50         60 
MFQRSGAAHH IKLISSRRCR FKSSFAVALN AASKLVTPKI LWNNPISLVS KEMNTLAKNI 

        70         80         90        100        110        120 
VALIGSGHPV LNKVTSYYFE TEGKKVRPLL VLLLSRALSE IPMTERNHLK IDKSDVPEDP 

       130        140        150        160        170        180 
IYSKPSQNQL FQRPASSISP LHILHGIKPL NPLTKGPEPL PEETFDKQRG ILPKQRRLAE 

       190        200        210        220        230        240 
IVEMIHTASL LHDDVIDHSD TRRGRPSGNA AFTNKMAVLA GDFLLGRATV SISRLHNPEV 

       250        260        270        280        290        300 
VELMSNSIAN LVEGEFMQLK NTSIDADIDT IENGHKLLPV PSKKLEVKEH DFRVPSRQQG 

       310        320        330        340        350        360 
LQLSHDQIIE TAFEYYIHKT YLKTAALISK SCRCAAILSG ASPAVIDECY DFGRNLGICF 

       370        380        390        400        410        420 
QLVDDMLDFT VSGKDLGKPS GADLKLGIAT APVLFAWKED PSLGPLISRN FSERGDVEKT 

       430        440        450        460        470 
IDSVRLHNGI AKTKILAEEY RDKALQNLRD SLPESDARSA LEFLTNSILT RRK

« Hide

References

« Hide 'large scale' references
[1]"Elucidation of the deficiency in two yeast coenzyme Q mutants. Characterization of the structural gene encoding hexaprenyl pyrophosphate synthetase."
Ashby M.N., Edwards P.A.
J. Biol. Chem. 265:13157-13164(1990) [PubMed: 2198286] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: D273-10B/A1.
[2]"Complete DNA sequence of yeast chromosome II."
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. expand/collapse author list , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"Sequence around the centromere of Saccharomyces cerevisiae chromosome II: similarity of CEN2 to CEN4."
Wolfe K.H., Lohan A.J.E.
Yeast 10:S41-S46(1994) [PubMed: 8091860] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-285.
Strain: ATCC 204508 / S288c.
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J05547 Genomic DNA. Translation: AAA34686.1.
Z35872 Genomic DNA. Translation: CAA84939.1.
AY558099 Genomic DNA. Translation: AAS56425.1.
Z26494 Genomic DNA. Translation: CAA81272.1.
BK006936 Genomic DNA. Translation: DAA07124.1.
PIRXUBYTP. A36625.
RefSeqNP_009557.1. NM_001178351.1.

3D structure databases

ProteinModelPortalP18900.
SMRP18900. Positions 42-472.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-1103N.
IntActP18900. 5 interactions.
MINTMINT-427151.
STRINGP18900.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR003W; YBR003W; YBR003W.
GeneID852288.
KEGGsce:YBR003W.
NMPDRfig|4932.3.peg.252.

Organism-specific databases

CYGDYBR003w.
SGDS000000207. COQ1.

Phylogenomic databases

eggNOGfuNOG07632.
GeneTreeEFGT00050000002298.
HOGENOMHBG732667.
OMADIDTIEN.
OrthoDBEOG4HB1V2.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13702.
BRENDA2.5.1.33. 984.

Gene expression databases

ArrayExpressP18900.
GenevestigatorP18900.
GermOnlineYBR003W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR000092. Polyprenyl_synt.
IPR017446. Polyprenyl_synth-rel.
IPR008949. Terpenoid_synth.
[Graphical view]
Gene3DG3DSA:1.10.600.10. Terpenoid_synth. 3 hits.
KOK05355.
PANTHERPTHR12001. Polyprenyl_synt. 1 hit.
PfamPF00348. polyprenyl_synt. 1 hit.
[Graphical view]
SUPFAMSSF48576. Terpenoid_synth. 1 hit.
PROSITEPS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio970928.

Entry information

Entry nameCOQ1_YEAST
AccessionPrimary (citable) accession number: P18900
Secondary accession number(s): D6VQ04
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: December 14, 2011
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents