COQ5_YEAST
ID COQ5_YEAST Reviewed; 307 AA.
AC P49017; D6W0H4;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03191, ECO:0000303|PubMed:9083049};
DE EC=2.1.1.201 {ECO:0000255|HAMAP-Rule:MF_03191, ECO:0000269|PubMed:14701817, ECO:0000269|PubMed:9083049};
DE AltName: Full=2-hexaprenyl-6-methoxy-1,4-benzoquinol methyltransferase {ECO:0000303|PubMed:9083048};
DE AltName: Full=Ubiquinone biosynthesis methyltransferase COQ5 {ECO:0000255|HAMAP-Rule:MF_03191, ECO:0000303|PubMed:9083049};
DE Flags: Precursor;
GN Name=COQ5 {ECO:0000255|HAMAP-Rule:MF_03191, ECO:0000303|PubMed:9083048,
GN ECO:0000303|PubMed:9083049}; Synonyms=DBI56;
GN OrderedLocusNames=YML110C {ECO:0000312|SGD:S000004578};
GN ORFNames=YM8339.09C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
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 [3]
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 [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9083048; DOI=10.1074/jbc.272.14.9175;
RA Dibrov E., Robinson K.M., Lemire B.D.;
RT "The COQ5 gene encodes a yeast mitochondrial protein necessary for
RT ubiquinone biosynthesis and the assembly of the respiratory chain.";
RL J. Biol. Chem. 272:9175-9181(1997).
RN [5]
RP CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=9083049; DOI=10.1074/jbc.272.14.9182;
RA Barkovich R.J., Shtanko A., Shepherd J.A., Lee P.T., Myles D.C.,
RA Tzagoloff A., Clarke C.F.;
RT "Characterization of the COQ5 gene from Saccharomyces cerevisiae. Evidence
RT for a C-methyltransferase in ubiquinone biosynthesis.";
RL J. Biol. Chem. 272:9182-9188(1997).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
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).
RN [8]
RP CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=14701817; DOI=10.1074/jbc.m313712200;
RA Baba S.W., Belogrudov G.I., Lee J.C., Lee P.T., Strahan J., Shepherd J.N.,
RA Clarke C.F.;
RT "Yeast Coq5 C-methyltransferase is required for stability of other
RT polypeptides involved in coenzyme Q biosynthesis.";
RL J. Biol. Chem. 279:10052-10059(2004).
RN [9]
RP SUBUNIT.
RX PubMed=24406904; DOI=10.1016/j.bbalip.2013.12.017;
RA He C.H., Xie L.X., Allan C.M., Tran U.C., Clarke C.F.;
RT "Coenzyme Q supplementation or over-expression of the yeast Coq8 putative
RT kinase stabilizes multi-subunit Coq polypeptide complexes in yeast coq null
RT mutants.";
RL Biochim. Biophys. Acta 1841:630-644(2014).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 61-307.
RX PubMed=25084328; DOI=10.1107/s1399004714011559;
RA Dai Y.N., Zhou K., Cao D.D., Jiang Y.L., Meng F., Chi C.B., Ren Y.M.,
RA Chen Y., Zhou C.Z.;
RT "Crystal structures and catalytic mechanism of the C-methyltransferase Coq5
RT provide insights into a key step of the yeast coenzyme Q synthesis
RT pathway.";
RL Acta Crystallogr. D 70:2085-2092(2014).
CC -!- FUNCTION: Methyltransferase required for the conversion of 2-
CC polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-
CC 6-methoxy-1,4-benzoquinol (DMQH2). {ECO:0000255|HAMAP-Rule:MF_03191,
CC ECO:0000269|PubMed:9083048}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-methoxy-6-all-trans-polyprenyl-1,4-benzoquinol + S-
CC adenosyl-L-methionine = a 6-methoxy-3-methyl-2-all-trans-polyprenyl-
CC 1,4-benzoquinol + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:28286, Rhea:RHEA-COMP:10858, Rhea:RHEA-COMP:10859,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:84166, ChEBI:CHEBI:84167; EC=2.1.1.201;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03191,
CC ECO:0000269|PubMed:14701817, ECO:0000269|PubMed:9083049};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03191, ECO:0000305|PubMed:9083048,
CC ECO:0000305|PubMed:9083049}.
CC -!- SUBUNIT: Component of a multi-subunit COQ enzyme complex, composed of
CC at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9. Interacts with COQ3.
CC {ECO:0000255|HAMAP-Rule:MF_03191, ECO:0000269|PubMed:24406904}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_03191, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14701817, ECO:0000269|PubMed:9083049}; Peripheral
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_03191,
CC ECO:0000269|PubMed:14701817}; Matrix side {ECO:0000255|HAMAP-
CC Rule:MF_03191, ECO:0000269|PubMed:14701817,
CC ECO:0000269|PubMed:9083048}.
CC -!- MISCELLANEOUS: Present with 8100 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. MenG/UbiE family. {ECO:0000255|HAMAP-Rule:MF_03191,
CC ECO:0000305}.
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DR EMBL; Z49210; CAA89108.1; -; Genomic_DNA.
DR EMBL; AY693194; AAT93213.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09788.1; -; Genomic_DNA.
DR PIR; S53962; S53962.
DR RefSeq; NP_013597.1; NM_001182472.1.
DR PDB; 4OBW; X-ray; 2.40 A; A/B/C/D=61-307.
DR PDB; 4OBX; X-ray; 2.20 A; A/B/C/D=61-307.
DR PDBsum; 4OBW; -.
DR PDBsum; 4OBX; -.
DR AlphaFoldDB; P49017; -.
DR SMR; P49017; -.
DR BioGRID; 35094; 191.
DR ComplexPortal; CPX-1155; CoQ biosynthetic complex.
DR DIP; DIP-1639N; -.
DR IntAct; P49017; 8.
DR MINT; P49017; -.
DR STRING; 4932.YML110C; -.
DR MaxQB; P49017; -.
DR PaxDb; P49017; -.
DR PRIDE; P49017; -.
DR EnsemblFungi; YML110C_mRNA; YML110C; YML110C.
DR GeneID; 854930; -.
DR KEGG; sce:YML110C; -.
DR SGD; S000004578; COQ5.
DR VEuPathDB; FungiDB:YML110C; -.
DR eggNOG; KOG1540; Eukaryota.
DR GeneTree; ENSGT00390000001654; -.
DR HOGENOM; CLU_037990_0_1_1; -.
DR InParanoid; P49017; -.
DR OMA; VRNFENL; -.
DR BioCyc; MetaCyc:YML110C-MON; -.
DR BioCyc; YEAST:YML110C-MON; -.
DR BRENDA; 2.1.1.201; 984.
DR UniPathway; UPA00232; -.
DR PRO; PR:P49017; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P49017; protein.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0043334; F:2-hexaprenyl-6-methoxy-1,4-benzoquinone methyltransferase activity; IMP:SGD.
DR GO; GO:0043333; F:2-octaprenyl-6-methoxy-1,4-benzoquinone methylase activity; IMP:UniProtKB.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0009060; P:aerobic respiration; IMP:SGD.
DR GO; GO:0032259; P:methylation; IMP:UniProtKB.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IMP:SGD.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01813; MenG_UbiE_methyltr; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR004033; UbiE/COQ5_MeTrFase.
DR InterPro; IPR023576; UbiE/COQ5_MeTrFase_CS.
DR Pfam; PF01209; Ubie_methyltran; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR01934; MenG_MenH_UbiE; 1.
DR PROSITE; PS51608; SAM_MT_UBIE; 1.
DR PROSITE; PS01183; UBIE_1; 1.
DR PROSITE; PS01184; UBIE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; Methyltransferase; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; Transit peptide; Ubiquinone biosynthesis.
FT TRANSIT 1..19
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03191"
FT CHAIN 20..307
FT /note="2-methoxy-6-polyprenyl-1,4-benzoquinol methylase,
FT mitochondrial"
FT /id="PRO_0000193361"
FT BINDING 122
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03191,
FT ECO:0000269|PubMed:25084328"
FT BINDING 148
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03191,
FT ECO:0000269|PubMed:25084328"
FT BINDING 179..180
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03191,
FT ECO:0000269|PubMed:25084328"
FT BINDING 197
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03191,
FT ECO:0000269|PubMed:25084328"
FT HELIX 74..86
FT /evidence="ECO:0007829|PDB:4OBX"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:4OBX"
FT HELIX 90..101
FT /evidence="ECO:0007829|PDB:4OBX"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:4OBX"
FT HELIX 124..137
FT /evidence="ECO:0007829|PDB:4OBX"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:4OBX"
FT HELIX 151..164
FT /evidence="ECO:0007829|PDB:4OBX"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:4OBW"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:4OBX"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:4OBX"
FT STRAND 191..198
FT /evidence="ECO:0007829|PDB:4OBX"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:4OBX"
FT HELIX 206..216
FT /evidence="ECO:0007829|PDB:4OBX"
FT STRAND 217..228
FT /evidence="ECO:0007829|PDB:4OBX"
FT HELIX 234..255
FT /evidence="ECO:0007829|PDB:4OBX"
FT HELIX 258..270
FT /evidence="ECO:0007829|PDB:4OBX"
FT HELIX 274..283
FT /evidence="ECO:0007829|PDB:4OBX"
FT STRAND 286..294
FT /evidence="ECO:0007829|PDB:4OBX"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:4OBX"
FT STRAND 299..306
FT /evidence="ECO:0007829|PDB:4OBX"
SQ SEQUENCE 307 AA; 34685 MW; C8951F9C8FFF8F41 CRC64;
MLISSRIVRS SLVNVPLRLS RCFTQAHRAC KEEEVNSPLS SAAEQPEQKY THFGSKTVLK
STKQKLVGDV FSSVANRYDL MNDVMSLGIH RLWKDHFINK LDAGKRPNST TPLNFIDVAG
GSGDIAFGLL DHAESKFGDT ESTMDIVDIN PDMLKEGEKR AMEQGKYFKD PRVRFLVSNG
EKLEEIDSDS KDIYTVSFGI RNFTDIQKGL NTAYRVLKPG GIFYCLEFSK IENPLMDFAY
QQWAKVLPVM GSMIANDYDS YQYLVESIER FPDQETFKSM IEKAGFKSAG YESLTFGICA
IHWGIKV
