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Protein

Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial

Gene

COQ6

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

FAD-dependent monooxygenase required for the C5-ring hydroxylation during ubiquinone biosynthesis. Catalyzes the hydroxylation of 3-hexaprenyl-4-hydroxybenzoic acid (HHB) to 3-hexaprenyl-4,5-dihydroxybenzoic acid (DHHB). The electrons required for the hydroxylation reaction may be funneled indirectly from NADPH via ferredoxin (YAH1) and ferredoxin reductase (ARH1) to COQ6. Can also use 3-hexaprenyl-4-aminobenzoic acid (HAB) as substrate.UniRule annotation1 Publication

Cofactori

FADUniRule annotation1 Publication

Pathway:iubiquinone biosynthesis

This protein is involved in the pathway ubiquinone biosynthesis, which is part of Cofactor biosynthesis.UniRule annotation2 Publications
View all proteins of this organism that are known to be involved in the pathway ubiquinone biosynthesis and in Cofactor biosynthesis.

GO - Molecular functioni

GO - Biological processi

  • ubiquinone biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Ubiquinone biosynthesis

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16019.
YEAST:YGR255C-MONOMER.
ReactomeiREACT_293512. Ubiquinol biosynthesis.
UniPathwayiUPA00232.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquinone biosynthesis monooxygenase COQ6, mitochondrialUniRule annotation1 Publication (EC:1.14.13.-UniRule annotation1 Publication)
Gene namesi
Name:COQ61 PublicationUniRule annotation
Ordered Locus Names:YGR255CImported
ORF Names:G9165
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome VII

Organism-specific databases

CYGDiYGR255c.
EuPathDBiFungiDB:YGR255C.
SGDiS000003487. COQ6.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi202 – 2021G → A: Accumulates ubiquinone biosynthesis intermediates lacking the C5-ring hydroxyl. 1 Publication
Mutagenesisi386 – 3861G → A: Accumulates ubiquinone biosynthesis intermediates lacking the C5-ring hydroxyl; when associated with D-388. 1 Publication
Mutagenesisi388 – 3881N → D: Accumulates ubiquinone biosynthesis intermediates lacking the C5-ring hydroxyl; when associated with A-386. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1717MitochondrionSequence AnalysisAdd
BLAST
Chaini18 – 479462Ubiquinone biosynthesis monooxygenase COQ6, mitochondrialPRO_0000207581Add
BLAST

Proteomic databases

MaxQBiP53318.
PaxDbiP53318.

Interactioni

Subunit structurei

Component of a multi-subunit COQ enzyme complex, composed of at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9.UniRule annotation2 Publications

Protein-protein interaction databases

BioGridi33506. 17 interactions.
IntActiP53318. 7 interactions.
MINTiMINT-619446.

Structurei

3D structure databases

ProteinModelPortaliP53318.
SMRiP53318. Positions 29-447.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the UbiH/COQ6 family.UniRule annotationCurated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0654.
GeneTreeiENSGT00390000015152.
HOGENOMiHOG000255772.
InParanoidiP53318.
KOiK06126.
OMAiIDEIYPP.
OrthoDBiEOG747PT4.

Family and domain databases

HAMAPiMF_03193. COQ6_monooxygenase.
InterProiIPR002938. mOase_FAD-bd.
IPR018168. Ubi_Hdrlase_CS.
IPR010971. UbiH/COQ6.
IPR000689. UbQ_mOase_COQ6.
[Graphical view]
PfamiPF01494. FAD_binding_3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01989. COQ6. 1 hit.
TIGR01988. Ubi-OHases. 1 hit.
PROSITEiPS01304. UBIH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P53318-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFFSKVMLTR RILVRGLATA KSSAPKLTDV LIVGGGPAGL TLAASIKNSP
60 70 80 90 100
QLKDLKTTLV DMVDLKDKLS DFYNSPPDYF TNRIVSVTPR SIHFLENNAG
110 120 130 140 150
ATLMHDRIQS YDGLYVTDGC SKATLDLARD SMLCMIEIIN IQASLYNRIS
160 170 180 190 200
QYDSKKDSID IIDNTKVVNI KHSDPNDPLS WPLVTLSNGE VYKTRLLVGA
210 220 230 240 250
DGFNSPTRRF SQIPSRGWMY NAYGVVASMK LEYPPFKLRG WQRFLPTGPI
260 270 280 290 300
AHLPMPENNA TLVWSSSERL SRLLLSLPPE SFTALINAAF VLEDADMNYY
310 320 330 340 350
YRTLEDGSMD TDKLIEDIKF RTEEIYATLK DESDIDEIYP PRVVSIIDKT
360 370 380 390 400
RARFPLKLTH ADRYCTDRVA LVGDAAHTTH PLAGQGLNMG QTDVHGLVYA
410 420 430 440 450
LEKAMERGLD IGSSLSLEPF WAERYPSNNV LLGMADKLFK LYHTNFPPVV
460 470
ALRTFGLNLT NKIGPVKNMI IDTLGGNEK
Length:479
Mass (Da):53,527
Last modified:October 1, 1996 - v1
Checksum:iB6D4286545CCE695
GO

Sequence cautioni

The sequence CAA56704.1 differs from that shown. Reason: Frameshift at positions 212 and 434. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti60 – 601V → I in CAA56704 (Ref. 5) Curated
Sequence conflicti68 – 681K → R in CAA56704 (Ref. 5) Curated
Sequence conflicti313 – 3131K → E in CAA56705 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF003698 Genomic DNA. Translation: AAB61341.1.
X99228 Genomic DNA. Translation: CAA67617.1.
Z73040 Genomic DNA. Translation: CAA97284.1.
X80690 Genomic DNA. Translation: CAA56704.1. Frameshift.
X80690 Genomic DNA. Translation: CAA56705.1.
BK006941 Genomic DNA. Translation: DAA08346.1.
PIRiS64587.
RefSeqiNP_011771.1. NM_001181384.1.

Genome annotation databases

EnsemblFungiiYGR255C; YGR255C; YGR255C.
GeneIDi853170.
KEGGisce:YGR255C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF003698 Genomic DNA. Translation: AAB61341.1.
X99228 Genomic DNA. Translation: CAA67617.1.
Z73040 Genomic DNA. Translation: CAA97284.1.
X80690 Genomic DNA. Translation: CAA56704.1. Frameshift.
X80690 Genomic DNA. Translation: CAA56705.1.
BK006941 Genomic DNA. Translation: DAA08346.1.
PIRiS64587.
RefSeqiNP_011771.1. NM_001181384.1.

3D structure databases

ProteinModelPortaliP53318.
SMRiP53318. Positions 29-447.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33506. 17 interactions.
IntActiP53318. 7 interactions.
MINTiMINT-619446.

Proteomic databases

MaxQBiP53318.
PaxDbiP53318.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR255C; YGR255C; YGR255C.
GeneIDi853170.
KEGGisce:YGR255C.

Organism-specific databases

CYGDiYGR255c.
EuPathDBiFungiDB:YGR255C.
SGDiS000003487. COQ6.

Phylogenomic databases

eggNOGiCOG0654.
GeneTreeiENSGT00390000015152.
HOGENOMiHOG000255772.
InParanoidiP53318.
KOiK06126.
OMAiIDEIYPP.
OrthoDBiEOG747PT4.

Enzyme and pathway databases

UniPathwayiUPA00232.
BioCyciMetaCyc:MONOMER-16019.
YEAST:YGR255C-MONOMER.
ReactomeiREACT_293512. Ubiquinol biosynthesis.

Miscellaneous databases

NextBioi973291.
PROiP53318.

Family and domain databases

HAMAPiMF_03193. COQ6_monooxygenase.
InterProiIPR002938. mOase_FAD-bd.
IPR018168. Ubi_Hdrlase_CS.
IPR010971. UbiH/COQ6.
IPR000689. UbQ_mOase_COQ6.
[Graphical view]
PfamiPF01494. FAD_binding_3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01989. COQ6. 1 hit.
TIGR01988. Ubi-OHases. 1 hit.
PROSITEiPS01304. UBIH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Saccharomyces cerevisiae COQ6 gene encodes a mitochondrial flavin-dependent monooxygenase required for coenzyme Q biosynthesis."
    Gin P., Hsu A.Y., Rothman S.C., Jonassen T., Lee P.T., Tzagoloff A., Clarke C.F.
    J. Biol. Chem. 278:25308-25316(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, COFACTOR, PATHWAY.
  2. "Sequence analysis of a 10.5 kb DNA fragment from the yeast chromosome VII reveals the presence of three new open reading frames and of a tRNAThr gene."
    Mazzoni C., Ruzzi M., Rinaldi T., Solinas F., Montebove F., Frontali L.
    Yeast 13:369-372(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Miosga T.
    Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Saccharomyces cerevisiae Coq9 polypeptide is a subunit of the mitochondrial coenzyme Q biosynthetic complex."
    Hsieh E.J., Gin P., Gulmezian M., Tran U.C., Saiki R., Marbois B.N., Clarke C.F.
    Arch. Biochem. Biophys. 463:19-26(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN COQ ENZYME COMPLEX, INTERACTION WITH COQ9.
  9. "Coenzyme Q biosynthesis: Coq6 is required for the C5-hydroxylation reaction and substrate analogs rescue Coq6 deficiency."
    Ozeir M., Muhlenhoff U., Webert H., Lill R., Fontecave M., Pierrel F.
    Chem. Biol. 18:1134-1142(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLY-202; GLY-386 AND ASN-388.
  10. "Coenzyme Q supplementation or over-expression of the yeast Coq8 putative kinase stabilizes multi-subunit Coq polypeptide complexes in yeast coq null mutants."
    He C.H., Xie L.X., Allan C.M., Tran U.C., Clarke C.F.
    Biochim. Biophys. Acta 1841:630-644(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.

Entry informationi

Entry nameiCOQ6_YEAST
AccessioniPrimary (citable) accession number: P53318
Secondary accession number(s): D6VV35, Q05674, Q05675
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 22, 2015
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2940 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.