ID A0A0E0A556_9ORYZ Unreviewed; 316 AA.
AC A0A0E0A556;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Ubiquinone biosynthesis O-methyltransferase, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03190};
DE AltName: Full=3-demethylubiquinol 3-O-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03190};
DE EC=2.1.1.64 {ECO:0000256|HAMAP-Rule:MF_03190};
DE AltName: Full=Polyprenyldihydroxybenzoate methyltransferase {ECO:0000256|HAMAP-Rule:MF_03190};
DE EC=2.1.1.114 {ECO:0000256|HAMAP-Rule:MF_03190};
GN Name=COQ3 {ECO:0000256|HAMAP-Rule:MF_03190};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM06G03540.2};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM06G03540.2}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM06G03540.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- FUNCTION: O-methyltransferase that catalyzes the 2 O-methylation steps
CC in the ubiquinone biosynthetic pathway. {ECO:0000256|HAMAP-
CC Rule:MF_03190}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,4-dihydroxy-5-all-trans-polyprenylbenzoate + S-adenosyl-L-
CC methionine = 3-methoxy,4-hydroxy-5-all-trans-polyprenylbenzoate +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:44452, Rhea:RHEA-
CC COMP:10930, Rhea:RHEA-COMP:10931, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:64694,
CC ChEBI:CHEBI:84443; EC=2.1.1.114; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03190};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3-demethylubiquinol + S-adenosyl-L-methionine = a ubiquinol
CC + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:44380, Rhea:RHEA-
CC COMP:9566, Rhea:RHEA-COMP:10914, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17976, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:84422; EC=2.1.1.64; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03190};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_03190}.
CC -!- SUBUNIT: Component of a multi-subunit COQ enzyme complex.
CC {ECO:0000256|HAMAP-Rule:MF_03190}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_03190}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_03190}; Matrix side {ECO:0000256|HAMAP-Rule:MF_03190}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. UbiG/COQ3 family. {ECO:0000256|HAMAP-Rule:MF_03190}.
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DR AlphaFoldDB; A0A0E0A556; -.
DR EnsemblPlants; OGLUM06G03540.2; OGLUM06G03540.2; OGLUM06G03540.
DR Gramene; OGLUM06G03540.2; OGLUM06G03540.2; OGLUM06G03540.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000026961; Unassembled WGS sequence.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0008425; F:2-polyprenyl-6-methoxy-1,4-benzoquinone methyltransferase activity; IEA:InterPro.
DR GO; GO:0061542; F:3-demethylubiquinol-n 3-O-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004395; F:hexaprenyldihydroxybenzoate methyltransferase 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_00472; UbiG; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR010233; UbiG_MeTrfase.
DR NCBIfam; TIGR01983; UbiG; 1.
DR PANTHER; PTHR43464; METHYLTRANSFERASE; 1.
DR PANTHER; PTHR43464:SF19; UBIQUINONE BIOSYNTHESIS O-METHYLTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF13489; Methyltransf_23; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|HAMAP-Rule:MF_03190};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_03190}; Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03190};
KW Mitochondrion inner membrane {ECO:0000256|HAMAP-Rule:MF_03190};
KW Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_03190};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03190};
KW Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688, ECO:0000256|HAMAP-
KW Rule:MF_03190}.
FT REGION 46..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..65
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 107
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03190"
FT BINDING 138
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03190"
FT BINDING 159
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03190"
FT BINDING 204
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03190"
SQ SEQUENCE 316 AA; 33902 MW; FBE4F83EDADFF9FD CRC64;
MLRRVAPSLR RAILTTSAHG RAGAQLTEPG LSPPHALLPQ WRLCSSAAST NSPPPPPPPP
QGTPRPAGGS TVSSLNPAEV AKFAAIAETW WDSEGPFKPL HLMNPTRLSF IRSTLCRHFR
RDPNSCKPLE GLKVIDVGCG GGILSEPLAR MGATVTGIDA VDKNIKIARV HAASDPSTAS
IEYFCTTAED LVKEHKQFDA VISLEVIEHV ANPSGFCESL SALTVPNGAT VISTINRSMR
AYATAIVAAE YILNWLPKGT HQWSKLVTPE ELVLILERAS ISVQEMAGFM YNPLRGEWSL
SDDLTGACSS VMGKPH
//
