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Entry: A0A1X6MUQ5_9APHY
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ID   A0A1X6MUQ5_9APHY        Unreviewed;       299 AA.
AC   A0A1X6MUQ5;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   13-SEP-2023, entry version 17.
DE   RecName: Full=2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03191};
DE            EC=2.1.1.201 {ECO:0000256|HAMAP-Rule:MF_03191};
DE   AltName: Full=Ubiquinone biosynthesis methyltransferase COQ5 {ECO:0000256|HAMAP-Rule:MF_03191};
GN   Name=COQ5 {ECO:0000256|HAMAP-Rule:MF_03191};
GN   ORFNames=POSPLADRAFT_1183724 {ECO:0000313|EMBL:OSX59990.1};
OS   Postia placenta MAD-698-R-SB12.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Postiaceae; Postia.
OX   NCBI_TaxID=670580 {ECO:0000313|EMBL:OSX59990.1, ECO:0000313|Proteomes:UP000194127};
RN   [1] {ECO:0000313|EMBL:OSX59990.1, ECO:0000313|Proteomes:UP000194127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAD-698-R-SB12 {ECO:0000313|EMBL:OSX59990.1,
RC   ECO:0000313|Proteomes:UP000194127};
RG   DOE Joint Genome Institute;
RA   Gaskell J., Kersten P., Larrondo L.F., Canessa P., Martinez D., Hibbett D.,
RA   Schmoll M., Kubicek C.P., Martinez A.T., Yadav J., Master E.,
RA   Magnuson J.K., James T., Yaver D., Berka R., Labutti K., Lipzen A.,
RA   Aerts A., Barry K., Henrissat B., Blanchette R., Grigoriev I., Cullen D.;
RT   "Genome Sequence of the Model Brown-Rot Fungus Postia placenta SB12.";
RL   Submitted (APR-2017) 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:0000256|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:0000256|HAMAP-Rule:MF_03191};
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000256|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:0000256|HAMAP-
CC       Rule:MF_03191}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_03191}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_03191}; Matrix side {ECO:0000256|HAMAP-Rule:MF_03191}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. MenG/UbiE family. {ECO:0000256|HAMAP-Rule:MF_03191}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03191}.
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DR   EMBL; KZ110601; OSX59990.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X6MUQ5; -.
DR   STRING; 670580.A0A1X6MUQ5; -.
DR   OrthoDB; 5487921at2759; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000194127; Unassembled WGS sequence.
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   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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   NCBIfam; TIGR01934; MenG_MenH_UbiE; 1.
DR   PANTHER; PTHR43591:SF24; 2-METHOXY-6-POLYPRENYL-1,4-BENZOQUINOL METHYLASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43591; METHYLTRANSFERASE; 1.
DR   Pfam; PF01209; Ubie_methyltran; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51608; SAM_MT_UBIE; 1.
DR   PROSITE; PS01183; UBIE_1; 1.
DR   PROSITE; PS01184; UBIE_2; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_03191};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_03191}; Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03191};
KW   Mitochondrion inner membrane {ECO:0000256|HAMAP-Rule:MF_03191};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194127};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_03191};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_03191}; Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_03191}.
FT   BINDING         104
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03191"
FT   BINDING         130
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03191"
FT   BINDING         160..161
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03191"
SQ   SEQUENCE   299 AA;  33306 MW;  7C9BEBB38DBBBF57 CRC64;
     MLSRTAGRRA CRSFSSLKQV RLNHNQPQNA QDNARTTHFG FQTVPEETKE SLVRNVFDSV
     ASSYDLMNDA MSLGVHRLWK DEYIALLKPG AKGPVKCIDV AGGTGDIALR ILDSARERYA
     DRETSVDVVD INTEMLKEGY KRFKKTMYHN TSQIAFHEGN AQALNEEKFP SNTYDLYTIA
     FGIRNCTSVP DVLKEAYRVL KPGGTFACLE FSRVNNPLFG ALYDQYSFSV IPLIGTILTG
     DRASYQYLVE SIRKFPPQPE FAKMIADAGF TTGGMFEGKG GAWRDLWGGI ASIHTGVKV
//
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