ID S8AG23_DACHA Unreviewed; 300 AA.
AC S8AG23;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=H072_4008 {ECO:0000313|EMBL:EPS42015.1};
OS Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS (Monacrosporium haptotylum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS42015.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS42015.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS42015.1,
RC ECO:0000313|Proteomes:UP000015100};
RX PubMed=24244185;
RA Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL PLoS Genet. 9:E1003909-E1003909(2013).
RN [2] {ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA Ahren D.G.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL Submitted (APR-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPS42015.1}.
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DR EMBL; AQGS01000130; EPS42015.1; -; Genomic_DNA.
DR RefSeq; XP_011109968.1; XM_011111666.1.
DR AlphaFoldDB; S8AG23; -.
DR STRING; 1284197.S8AG23; -.
DR eggNOG; KOG1540; Eukaryota.
DR HOGENOM; CLU_037990_0_1_1; -.
DR OMA; MNDVMSM; -.
DR OrthoDB; 5487921at2759; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000015100; 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:UP000015100};
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};
KW Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688, ECO:0000256|HAMAP-
KW Rule:MF_03191}.
FT BINDING 116
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03191"
FT BINDING 142
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03191"
FT BINDING 175..176
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03191"
SQ SEQUENCE 300 AA; 33576 MW; 300380A908FF6A97 CRC64;
MSMRGAGRVL RLRPSRAWAT VYPRSFSTAG ARFQDGKSAA EERTTHFGFQ NITESMKESK
VREVFDSVAK NYDTMNDVMS FGIHRLWKDQ FVQQLNPGKK SIFSEPMTIL DLAGGTGDIA
FRMLNHARTV NGDSETRVKV VDINEEMLKE GVKRAHALGY RTEGEDAPIS FMVQNGETLE
AIPDNSIDLL TIAFGIRNFT DKEKALSTAH RVLKKGGVFA CLEFSKVNNF ILDQIYRRYS
FSVIPMMGQL IAGDRDSYQY LFPSQKDFAG MIRDAGFQLA GKGWQDLTFG VAAVHTGVKL
//
