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Database: UniProt
Entry: A0A1U7VIP9_NICSY
LinkDB: A0A1U7VIP9_NICSY
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ID   A0A1U7VIP9_NICSY        Unreviewed;       322 AA.
AC   A0A1U7VIP9;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, 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=LOC104217617 {ECO:0000313|RefSeq:XP_009766213.1};
GN   Synonyms=COQ3 {ECO:0000256|HAMAP-Rule:MF_03190};
OS   Nicotiana sylvestris (Wood tobacco) (South American tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4096 {ECO:0000313|Proteomes:UP000189701, ECO:0000313|RefSeq:XP_009766213.1};
RN   [1] {ECO:0000313|Proteomes:UP000189701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23773524; DOI=10.1186/gb-2013-14-6-r60;
RA   Sierro N., Battey J.N., Ouadi S., Bovet L., Goepfert S., Bakaher N.,
RA   Peitsch M.C., Ivanov N.V.;
RT   "Reference genomes and transcriptomes of Nicotiana sylvestris and Nicotiana
RT   tomentosiformis.";
RL   Genome Biol. 14:R60.1-R60.17(2013).
RN   [2] {ECO:0000313|RefSeq:XP_009766213.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_009766213.1};
RG   RefSeq;
RL   Submitted (NOV-2023) 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   RefSeq; XP_009766213.1; XM_009767911.1.
DR   AlphaFoldDB; A0A1U7VIP9; -.
DR   SMR; A0A1U7VIP9; -.
DR   STRING; 4096.A0A1U7VIP9; -.
DR   GeneID; 104217617; -.
DR   KEGG; nsy:104217617; -.
DR   eggNOG; KOG1270; Eukaryota.
DR   OrthoDB; 1459at2759; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000189701; Unplaced.
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:UP000189701};
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          48..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..67
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         106
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03190"
FT   BINDING         137
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03190"
FT   BINDING         158
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03190"
FT   BINDING         203
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03190"
SQ   SEQUENCE   322 AA;  35745 MW;  3A4F0DADA2788970 CRC64;
     MASKLVHNRL RSLCRISQLS NARFNNKLRD PNSNFPSLHN QVKWRSYSEV SQPTPINPPP
     PPSPNPSTTS TSSLNEFELA KFSAISETWW DAEGPFKPLH MMNPTRLAFI RSSLCRHFRK
     DPNCTRPFEG LKFVDVGCGG GILTEPLARM GATIMGVDAV DKNIKIARLH ADLDPKASSI
     EYRCTTAENL VEEQRQFDAV ISLEVIEHVA DPAGFCKSLS ALTIPGGATV ISTINRSMRA
     YATTIVAAEY LLHWLPKGTH QWSSFVTPEE LVLILQRASI TVQEMAGFVY NPLTGRWFLS
     DDISVNYIAL GTKPANSDET LD
//
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