COQ5_PONAB
ID COQ5_PONAB Reviewed; 327 AA.
AC Q5RBK6;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR858638; CAH90854.1; -; mRNA.
DR RefSeq; NP_001125488.1; NM_001132016.1.
DR AlphaFoldDB; Q5RBK6; -.
DR SMR; Q5RBK6; -.
DR STRING; 9601.ENSPPYP00000005736; -.
DR GeneID; 100172397; -.
DR KEGG; pon:100172397; -.
DR CTD; 84274; -.
DR eggNOG; KOG1540; Eukaryota.
DR InParanoid; Q5RBK6; -.
DR OrthoDB; 1125002at2759; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0043430; F:2-decaprenyl-6-methoxy-1,4-benzoquinone methyltransferase activity; 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..49
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03191"
FT CHAIN 50..327
FT /note="2-methoxy-6-polyprenyl-1,4-benzoquinol methylase,
FT mitochondrial"
FT /id="PRO_0000228630"
FT BINDING 117
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03191"
FT BINDING 171
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03191"
FT BINDING 199..200
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03191"
SQ SEQUENCE 327 AA; 37255 MW; 53C34CA0B1ECB479 CRC64;
MAAPRSCALW SYCGRGWSWA MRGCQLLGLR SSWPGAPLSA RLLPQEKRAT ETHFGSETVS
EEEKGGKVYQ VFESVAKKYD VMNDMMSLGI HRVWKDLLLW KMRPLPGTQL LDVAGGTGDI
AFRFLNYVQS QHQRKQKRQL RAQQNLSWEE IAKEYQNEED SLGGSRVVMC DINKEMLKVG
KQKALAQGYR AGLAWVLGDA EELPFDDDKF DIYTIAFGIR NVTHIDQALQ EAHRVLKPGG
RFLCLEFSQV NNPLISRLYD LYSFQVIPVL GEVIAGDWKS YQYLVESIRR FPSQEEFKEM
IEDAGFHKVT YESLTSGIVA IHSGFKL
