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Protein

5-demethoxyubiquinone hydroxylase, mitochondrial

Gene

CAT5

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

Catalyzes the hydroxylation of 2-hexaprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2) during ubiquinone biosynthesis (PubMed:8621692, PubMed:9452453, PubMed:16624818). Has also a structural role in the COQ enzyme complex, stabilizing COQ3 and COQ4 polypeptides (PubMed:16624818).UniRule annotation3 Publications

Cofactori

Fe cationUniRule annotationNote: Binds 2 iron ions per subunit.UniRule annotation

Pathwayi: ubiquinone biosynthesis

This protein is involved in the pathway ubiquinone biosynthesis, which is part of Cofactor biosynthesis.UniRule annotation1 Publication
View all proteins of this organism that are known to be involved in the pathway ubiquinone biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi63 – 631Iron 1UniRule annotation
Metal bindingi95 – 951Iron 1UniRule annotation
Metal bindingi95 – 951Iron 2UniRule annotation
Metal bindingi98 – 981Iron 1UniRule annotation
Metal bindingi147 – 1471Iron 2UniRule annotation
Metal bindingi194 – 1941Iron 1UniRule annotation
Metal bindingi194 – 1941Iron 2UniRule annotation
Metal bindingi197 – 1971Iron 2UniRule annotation

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

Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13703.
ReactomeiR-SCE-2142789. Ubiquinol biosynthesis.
UniPathwayiUPA00232.

Names & Taxonomyi

Protein namesi
Recommended name:
5-demethoxyubiquinone hydroxylase, mitochondrialUniRule annotation1 Publication (EC:1.14.13.-UniRule annotation1 Publication)
Short name:
DMQ hydroxylaseUniRule annotation
Alternative name(s):
Catabolite repression protein 51 Publication
Ubiquinone biosynthesis monooxygenase COQ7UniRule annotation1 Publication
Gene namesi
Name:CAT51 Publication
Synonyms:COQ71 PublicationUniRule annotation
Ordered Locus Names:YOR125CImported
ORF Names:O3284, YOR3284C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR125C.
SGDiS000005651. CAT5.

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
Mutagenesisi194 – 1941E → K: Lacks ubiquinone and accumulates the intermediate DMQH2, causing respiratory deficiency. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1515MitochondrionSequence analysisAdd
BLAST
Chaini16 – 2332185-demethoxyubiquinone hydroxylase, mitochondrialPRO_0000089330Add
BLAST

Proteomic databases

MaxQBiP41735.
PeptideAtlasiP41735.

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

BioGridi34520. 119 interactions.
DIPiDIP-6435N.
IntActiP41735. 1 interaction.
MINTiMINT-698516.

Structurei

3D structure databases

ProteinModelPortaliP41735.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the COQ7 family.UniRule annotationCurated

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00390000014520.
HOGENOMiHOG000184972.
InParanoidiP41735.
KOiK06134.
OMAiHYNDQVR.
OrthoDBiEOG7WT4C2.

Family and domain databases

HAMAPiMF_01658. COQ7.
InterProiIPR009078. Ferritin-like_SF.
IPR011566. Ubq_synth_Coq7.
[Graphical view]
PANTHERiPTHR11237. PTHR11237. 1 hit.
PfamiPF03232. COQ7. 1 hit.
[Graphical view]
SUPFAMiSSF47240. SSF47240. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P41735-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSRVSVFKP ASRGFSVLSS LKITEHTSAK HTEKPEHAPK CQNLSDAQAA
60 70 80 90 100
FLDRVIRVDQ AGELGADYIY AGQYFVLAHR YPHLKPVLKH IWDQEIHHHN
110 120 130 140 150
TFNNLQLKRR VRPSLLTPLW KAGAFAMGAG TALISPEAAM ACTEAVETVI
160 170 180 190 200
GGHYNGQLRN LANQFNLERT DGTKGPSEEI KSLTSTIQQF RDDELEHLDT
210 220 230
AIKHDSYMAV PYTVITEGIK TICRVAIWSA ERI
Length:233
Mass (Da):26,060
Last modified:November 22, 2005 - v2
Checksum:i2686F44C5F17EFE5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82930 Genomic DNA. Translation: CAA58105.1.
S81938 mRNA. Translation: AAB36435.1.
X90518 Genomic DNA. Translation: CAA62119.1.
X94335 Genomic DNA. Translation: CAA64044.1.
Z75033 Genomic DNA. Translation: CAA99324.1.
BK006948 Genomic DNA. Translation: DAA10899.1.
PIRiS49912.
RefSeqiNP_014768.2. NM_001183544.1.

Genome annotation databases

EnsemblFungiiYOR125C; YOR125C; YOR125C.
GeneIDi854292.
KEGGisce:YOR125C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82930 Genomic DNA. Translation: CAA58105.1.
S81938 mRNA. Translation: AAB36435.1.
X90518 Genomic DNA. Translation: CAA62119.1.
X94335 Genomic DNA. Translation: CAA64044.1.
Z75033 Genomic DNA. Translation: CAA99324.1.
BK006948 Genomic DNA. Translation: DAA10899.1.
PIRiS49912.
RefSeqiNP_014768.2. NM_001183544.1.

3D structure databases

ProteinModelPortaliP41735.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34520. 119 interactions.
DIPiDIP-6435N.
IntActiP41735. 1 interaction.
MINTiMINT-698516.

Proteomic databases

MaxQBiP41735.
PeptideAtlasiP41735.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR125C; YOR125C; YOR125C.
GeneIDi854292.
KEGGisce:YOR125C.

Organism-specific databases

EuPathDBiFungiDB:YOR125C.
SGDiS000005651. CAT5.

Phylogenomic databases

GeneTreeiENSGT00390000014520.
HOGENOMiHOG000184972.
InParanoidiP41735.
KOiK06134.
OMAiHYNDQVR.
OrthoDBiEOG7WT4C2.

Enzyme and pathway databases

UniPathwayiUPA00232.
BioCyciMetaCyc:MONOMER-13703.
ReactomeiR-SCE-2142789. Ubiquinol biosynthesis.

Miscellaneous databases

PROiP41735.

Family and domain databases

HAMAPiMF_01658. COQ7.
InterProiIPR009078. Ferritin-like_SF.
IPR011566. Ubq_synth_Coq7.
[Graphical view]
PANTHERiPTHR11237. PTHR11237. 1 hit.
PfamiPF03232. COQ7. 1 hit.
[Graphical view]
SUPFAMiSSF47240. SSF47240. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "CAT5, a new gene necessary for derepression of gluconeogenic enzymes in Saccharomyces cerevisiae."
    Proft M., Koetter P., Hedges D., Bojunga N., Entian K.-D.
    EMBO J. 14:6116-6126(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The COQ7 gene encodes a protein in Saccharomyces cerevisiae necessary for ubiquinone biosynthesis."
    Marbois B.N., Clarke C.F.
    J. Biol. Chem. 271:2995-3004(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PATHWAY.
  3. "Sequencing and analysis of 51 kb on the right arm of chromosome XV from Saccharomyces cerevisiae reveals 30 open reading frames."
    Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C., Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.
    Yeast 12:281-288(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  7. "Yeast Clk-1 homologue (Coq7/Cat5) is a mitochondrial protein in coenzyme Q synthesis."
    Jonassen T., Proft M., Randez-Gil F., Schultz J.R., Marbois B.N., Entian K.-D., Clarke C.F.
    J. Biol. Chem. 273:3351-3357(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "Sequencing and comparison of yeast species to identify genes and regulatory elements."
    Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.
    Nature 423:241-254(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
  9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.
  10. "Complementation of Saccharomyces cerevisiae coq7 mutants by mitochondrial targeting of the Escherichia coli UbiF polypeptide: two functions of yeast Coq7 polypeptide in coenzyme Q biosynthesis."
    Tran U.C., Marbois B.N., Gin P., Gulmezian M., Jonassen T., Clarke C.F.
    J. Biol. Chem. 281:16401-16409(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLU-194.
  11. "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.
  12. "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, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiCOQ7_YEAST
AccessioniPrimary (citable) accession number: P41735
Secondary accession number(s): D6W2I3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 22, 2005
Last modified: June 8, 2016
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to be involved in carbon catabolite repression (PubMed:8557031). It has later been demonstrated that the catabolite-regulation defect in COQ7 mutants was a secondary effect of the respiration deficieny in ubiquinone-deficient mutants and could be rescued by the addition of exogenous ubiquinone (PubMed:9452453).2 Publications

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

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 one 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.