ID   COQ5_XENLA              Reviewed;         310 AA.
AC   Q4V7R3;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03191};
DE            EC=2.1.1.201 {ECO:0000255|HAMAP-Rule:MF_03191};
DE   AltName: Full=Ubiquinone biosynthesis methyltransferase COQ5 {ECO:0000255|HAMAP-Rule:MF_03191};
DE   Flags: Precursor;
GN   Name=coq5 {ECO:0000255|HAMAP-Rule:MF_03191};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- 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   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_03191}.
CC   -!- SUBUNIT: Component of a multi-subunit COQ enzyme complex, composed of
CC       at least coq3, coq4, coq5, coq6, coq7 and coq9. {ECO:0000255|HAMAP-
CC       Rule:MF_03191}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_03191}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_03191}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03191}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. MenG/UbiE family. {ECO:0000255|HAMAP-Rule:MF_03191}.
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DR   EMBL; BC097761; AAH97761.1; -; mRNA.
DR   RefSeq; NP_001089511.1; NM_001096042.1.
DR   AlphaFoldDB; Q4V7R3; -.
DR   SMR; Q4V7R3; -.
DR   DNASU; 734563; -.
DR   GeneID; 734563; -.
DR   KEGG; xla:734563; -.
DR   CTD; 734563; -.
DR   Xenbase; XB-GENE-981150; coq5.L.
DR   OMA; VRNFENL; -.
DR   OrthoDB; 1125002at2759; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 734563; Expressed in muscle tissue and 19 other tissues.
DR   GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0043333; F:2-octaprenyl-6-methoxy-1,4-benzoquinone methylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniRule.
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   2: Evidence at transcript level;
KW   Membrane; Methyltransferase; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase; Transit peptide;
KW   Ubiquinone biosynthesis.
FT   TRANSIT         1..6
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03191"
FT   CHAIN           7..310
FT                   /note="2-methoxy-6-polyprenyl-1,4-benzoquinol methylase,
FT                   mitochondrial"
FT                   /id="PRO_0000228634"
FT   BINDING         99
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03191"
FT   BINDING         154
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03191"
FT   BINDING         182..183
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03191"
SQ   SEQUENCE   310 AA;  35838 MW;  8EB5A0A45F6B4B37 CRC64;
     MAHMRSVLRG RLCGMREILR CQKASYTEAS RKETHFGFQA VSEEEKRERV YKVFENVAHN
     YDIMNDAMSL GVHRFWKDWL LQLMKPTPGM QLLDMAGGTG DISFRFINYI RAQREKWIRQ
     ELKFQQDLSW PDISKTYQNK EEGSLMGSRA VICDINKEML KVGLQKSLRL GYSEGLSWVA
     GDAEELPFGD DKFDVYTIAF GIRNVTHIEQ ALQEAYRVLK PGGRFLCLEF SHVNNPLLSK
     IYDVYSFQVI PVLGEVIAKD WKSYQYLVES IRRFPSQEEF KAMIEDAGFS KVNYHNLTSG
     VVAVHSGFKL