GenomeNet

Database: UniProt
Entry: A0A0D3B307_BRAOL
LinkDB: A0A0D3B307_BRAOL
Original site: A0A0D3B307_BRAOL 
ID   A0A0D3B307_BRAOL        Unreviewed;       286 AA.
AC   A0A0D3B307;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   08-NOV-2023, entry version 40.
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   Synonyms=106335176 {ECO:0000313|EnsemblPlants:Bo3g019370.1};
OS   Brassica oleracea var. oleracea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo3g019370.1, ECO:0000313|Proteomes:UP000032141};
RN   [1] {ECO:0000313|EnsemblPlants:Bo3g019370.1, ECO:0000313|Proteomes:UP000032141}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX   PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA   Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA   Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA   Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA   Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA   Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA   Chalhoub B., Sharpe A.G.;
RT   "Transcriptome and methylome profiling reveals relics of genome dominance
RT   in the mesopolyploid Brassica oleracea.";
RL   Genome Biol. 15:R77-R77(2014).
RN   [2] {ECO:0000313|EnsemblPlants:Bo3g019370.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
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.
CC       {ECO:0000256|HAMAP-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   ---------------------------------------------------------------------------
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   RefSeq; XP_013629074.1; XM_013773620.1.
DR   RefSeq; XP_013629076.1; XM_013773622.1.
DR   AlphaFoldDB; A0A0D3B307; -.
DR   STRING; 109376.A0A0D3B307; -.
DR   EnsemblPlants; Bo3g019370.1; Bo3g019370.1; Bo3g019370.
DR   GeneID; 106335176; -.
DR   Gramene; Bo3g019370.1; Bo3g019370.1; Bo3g019370.
DR   KEGG; boe:106335176; -.
DR   eggNOG; KOG1540; Eukaryota.
DR   HOGENOM; CLU_037990_0_1_1; -.
DR   OMA; GHEETHF; -.
DR   OrthoDB; 5487921at2759; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000032141; Chromosome C3.
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:UP000032141};
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         92
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03191"
FT   BINDING         128
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03191"
FT   BINDING         158..159
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03191"
SQ   SEQUENCE   286 AA;  32082 MW;  3CD8A5AAC0F5788D CRC64;
     MALRLLSRRT LGSRILSYRA SLHSHATSFG FQQVKEEEKS KLVGNVFTNV ASSYDIMNDV
     MSAGLHRLWK ERLVGKLSPF AGMKHLDVAG GTGDVAFRIF DAVNSVKRRA LRKVDEASLE
     ETQIYVCDIN PNMLNVGKQR AADRGLRDNK SLVWVEGDAE ALSFDDNSMD GYTIAFGIRN
     VTHIEKALAE AYRVLKRGGR FLCLELSHVD IPVFKELYDL YSFQVIPNLG ELIAGDRDSY
     QYLVESVRRF PPQERFAKMI GDAGFEKVEY ENLVGGVVAI HSAIKL
//
DBGET integrated database retrieval system