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Protein

2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial

Gene

COQ5

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

Functioni

Methyltransferase required for the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).UniRule annotation1 Publication

Catalytic activityi

S-adenosyl-L-methionine + 2-methoxy-6-all-trans-polyprenyl-1,4-benzoquinol = S-adenosyl-L-homocysteine + 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol.UniRule annotation2 Publications

Pathwayi: ubiquinone 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei122 – 1221S-adenosyl-L-methionineUniRule annotation1 Publication
Binding sitei148 – 1481S-adenosyl-L-methionineUniRule annotation1 Publication
Binding sitei197 – 1971S-adenosyl-L-methionineUniRule annotation1 Publication

GO - Molecular functioni

GO - Biological processi

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

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Ubiquinone biosynthesis

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13704.
YEAST:YML110C-MONOMER.
BRENDAi2.1.1.201. 984.
ReactomeiR-SCE-2142789. Ubiquinol biosynthesis.
UniPathwayiUPA00232.

Names & Taxonomyi

Protein namesi
Recommended name:
2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial1 PublicationUniRule annotation (EC:2.1.1.201UniRule annotation2 Publications)
Alternative name(s):
2-hexaprenyl-6-methoxy-1,4-benzoquinol methyltransferase1 Publication
Ubiquinone biosynthesis methyltransferase COQ51 PublicationUniRule annotation
Gene namesi
Name:COQ52 PublicationsUniRule annotation
Synonyms:DBI56
Ordered Locus Names:YML110CImported
ORF Names:YM8339.09C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YML110C.
SGDiS000004578. COQ5.

Subcellular locationi

GO - Cellular componenti

  • extrinsic component of mitochondrial inner membrane Source: UniProtKB-HAMAP
  • mitochondrial matrix Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1919MitochondrionSequence analysisAdd
BLAST
Chaini20 – 3072882-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrialPRO_0000193361Add
BLAST

Proteomic databases

MaxQBiP49017.
PRIDEiP49017.

Interactioni

Subunit structurei

Component of a multi-subunit COQ enzyme complex, composed of at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9. Interacts with COQ3.UniRule annotation1 Publication

Protein-protein interaction databases

BioGridi35094. 20 interactions.
DIPiDIP-1639N.
IntActiP49017. 6 interactions.
MINTiMINT-408577.

Structurei

Secondary structure

1
307
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi74 – 8613Combined sources
Turni87 – 893Combined sources
Helixi90 – 10112Combined sources
Beta strandi114 – 1196Combined sources
Helixi124 – 13714Combined sources
Beta strandi143 – 1497Combined sources
Helixi151 – 16414Combined sources
Beta strandi166 – 1694Combined sources
Beta strandi173 – 1775Combined sources
Turni180 – 1823Combined sources
Beta strandi191 – 1988Combined sources
Helixi200 – 2023Combined sources
Helixi206 – 21611Combined sources
Beta strandi217 – 22812Combined sources
Helixi234 – 25522Combined sources
Helixi258 – 27013Combined sources
Helixi274 – 28310Combined sources
Beta strandi286 – 2949Combined sources
Helixi295 – 2973Combined sources
Beta strandi299 – 3068Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4OBWX-ray2.40A/B/C/D61-307[»]
4OBXX-ray2.20A/B/C/D61-307[»]
ProteinModelPortaliP49017.
SMRiP49017. Positions 73-307.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni179 – 1802S-adenosyl-L-methionine bindingUniRule annotation1 Publication

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. MenG/UbiE family.UniRule annotationCurated

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00390000001654.
HOGENOMiHOG000249463.
InParanoidiP49017.
KOiK06127.
OMAiGGLHRAW.
OrthoDBiEOG71ZPBN.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01813. MenG_UbiE_methyltr.
InterProiIPR029063. SAM-dependent_MTases.
IPR004033. UbiE/COQ5_MeTrFase.
IPR023576. UbiE/COQ5_MeTrFase_CS.
[Graphical view]
PfamiPF01209. Ubie_methyltran. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR01934. MenG_MenH_UbiE. 1 hit.
PROSITEiPS51608. SAM_MT_UBIE. 1 hit.
PS01183. UBIE_1. 1 hit.
PS01184. UBIE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P49017-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLISSRIVRS SLVNVPLRLS RCFTQAHRAC KEEEVNSPLS SAAEQPEQKY
60 70 80 90 100
THFGSKTVLK STKQKLVGDV FSSVANRYDL MNDVMSLGIH RLWKDHFINK
110 120 130 140 150
LDAGKRPNST TPLNFIDVAG GSGDIAFGLL DHAESKFGDT ESTMDIVDIN
160 170 180 190 200
PDMLKEGEKR AMEQGKYFKD PRVRFLVSNG EKLEEIDSDS KDIYTVSFGI
210 220 230 240 250
RNFTDIQKGL NTAYRVLKPG GIFYCLEFSK IENPLMDFAY QQWAKVLPVM
260 270 280 290 300
GSMIANDYDS YQYLVESIER FPDQETFKSM IEKAGFKSAG YESLTFGICA

IHWGIKV
Length:307
Mass (Da):34,685
Last modified:February 1, 1996 - v1
Checksum:iC8951F9C8FFF8F41
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49210 Genomic DNA. Translation: CAA89108.1.
AY693194 Genomic DNA. Translation: AAT93213.1.
BK006946 Genomic DNA. Translation: DAA09788.1.
PIRiS53962.
RefSeqiNP_013597.1. NM_001182472.1.

Genome annotation databases

EnsemblFungiiYML110C; YML110C; YML110C.
GeneIDi854930.
KEGGisce:YML110C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49210 Genomic DNA. Translation: CAA89108.1.
AY693194 Genomic DNA. Translation: AAT93213.1.
BK006946 Genomic DNA. Translation: DAA09788.1.
PIRiS53962.
RefSeqiNP_013597.1. NM_001182472.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4OBWX-ray2.40A/B/C/D61-307[»]
4OBXX-ray2.20A/B/C/D61-307[»]
ProteinModelPortaliP49017.
SMRiP49017. Positions 73-307.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35094. 20 interactions.
DIPiDIP-1639N.
IntActiP49017. 6 interactions.
MINTiMINT-408577.

Proteomic databases

MaxQBiP49017.
PRIDEiP49017.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYML110C; YML110C; YML110C.
GeneIDi854930.
KEGGisce:YML110C.

Organism-specific databases

EuPathDBiFungiDB:YML110C.
SGDiS000004578. COQ5.

Phylogenomic databases

GeneTreeiENSGT00390000001654.
HOGENOMiHOG000249463.
InParanoidiP49017.
KOiK06127.
OMAiGGLHRAW.
OrthoDBiEOG71ZPBN.

Enzyme and pathway databases

UniPathwayiUPA00232.
BioCyciMetaCyc:MONOMER-13704.
YEAST:YML110C-MONOMER.
BRENDAi2.1.1.201. 984.
ReactomeiR-SCE-2142789. Ubiquinol biosynthesis.

Miscellaneous databases

PROiP49017.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01813. MenG_UbiE_methyltr.
InterProiIPR029063. SAM-dependent_MTases.
IPR004033. UbiE/COQ5_MeTrFase.
IPR023576. UbiE/COQ5_MeTrFase_CS.
[Graphical view]
PfamiPF01209. Ubie_methyltran. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR01934. MenG_MenH_UbiE. 1 hit.
PROSITEiPS51608. SAM_MT_UBIE. 1 hit.
PS01183. UBIE_1. 1 hit.
PS01184. UBIE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "The COQ5 gene encodes a yeast mitochondrial protein necessary for ubiquinone biosynthesis and the assembly of the respiratory chain."
    Dibrov E., Robinson K.M., Lemire B.D.
    J. Biol. Chem. 272:9175-9181(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  5. "Characterization of the COQ5 gene from Saccharomyces cerevisiae. Evidence for a C-methyltransferase in ubiquinone biosynthesis."
    Barkovich R.J., Shtanko A., Shepherd J.A., Lee P.T., Myles D.C., Tzagoloff A., Clarke C.F.
    J. Biol. Chem. 272:9182-9188(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Yeast Coq5 C-methyltransferase is required for stability of other polypeptides involved in coenzyme Q biosynthesis."
    Baba S.W., Belogrudov G.I., Lee J.C., Lee P.T., Strahan J., Shepherd J.N., Clarke C.F.
    J. Biol. Chem. 279:10052-10059(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
  9. "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.
  10. "Crystal structures and catalytic mechanism of the C-methyltransferase Coq5 provide insights into a key step of the yeast coenzyme Q synthesis pathway."
    Dai Y.N., Zhou K., Cao D.D., Jiang Y.L., Meng F., Chi C.B., Ren Y.M., Chen Y., Zhou C.Z.
    Acta Crystallogr. D 70:2085-2092(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 61-307.

Entry informationi

Entry nameiCOQ5_YEAST
AccessioniPrimary (citable) accession number: P49017
Secondary accession number(s): D6W0H4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: July 6, 2016
This is version 137 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 8100 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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