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Entry: A0A2B7WZ40_9EURO
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ID   A0A2B7WZ40_9EURO        Unreviewed;       388 AA.
AC   A0A2B7WZ40;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   05-JUN-2019, entry version 10.
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};
GN   ORFNames=GX51_05013 {ECO:0000313|EMBL:PGH01833.1};
OS   Blastomyces parvus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=2060905 {ECO:0000313|EMBL:PGH01833.1, ECO:0000313|Proteomes:UP000224080};
RN   [1] {ECO:0000313|EMBL:PGH01833.1, ECO:0000313|Proteomes:UP000224080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH130 {ECO:0000313|EMBL:PGH01833.1,
RC   ECO:0000313|Proteomes:UP000224080};
RA   Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT   "Comparative genomics in systemic dimorphic fungi from
RT   Ajellomycetaceae.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: O-methyltransferase that catalyzes the 2 O-methylation
CC       steps 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-
CC         adenosyl-L-methionine = 3-methoxy,4-hydroxy-5-all-trans-
CC         polyprenylbenzoate + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:44452, Rhea:RHEA-COMP:10930, Rhea:RHEA-
CC         COMP:10931, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:64694, ChEBI:CHEBI:84443;
CC         EC=2.1.1.114; Evidence={ECO:0000256|HAMAP-Rule:MF_03190};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3-demethylubiquinol + S-adenosyl-L-methionine = a
CC         ubiquinol + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:44380, Rhea:RHEA-COMP:9566, Rhea:RHEA-COMP:10914,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17976, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:84422; EC=2.1.1.64;
CC         Evidence={ECO:0000256|HAMAP-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, composed
CC       of at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9.
CC       {ECO:0000256|HAMAP-Rule:MF_03190}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|HAMAP-Rule:MF_03190}; Peripheral membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_03190}; Matrix side {ECO:0000256|HAMAP-
CC       Rule:MF_03190}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. UbiG/COQ3 family.
CC       {ECO:0000256|HAMAP-Rule:MF_03190}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:PGH01833.1}.
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DR   EMBL; PDNC01000067; PGH01833.1; -; Genomic_DNA.
DR   OrthoDB; 1542938at2759; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000224080; 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:1990886; F:3,4-dihydroxy-5-polyprenylbenzoic acid O-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008689; F:3-demethylubiquinone-9 3-O-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004395; F:hexaprenyldihydroxybenzoate methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00472; UbiG; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR010233; UbiG_MeTrfase.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000224080};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_03190};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_03190,
KW   ECO:0000313|EMBL:PGH01833.1};
KW   Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03190};
KW   Mitochondrion inner membrane {ECO:0000256|HAMAP-Rule:MF_03190};
KW   Reference proteome {ECO:0000313|Proteomes:UP000224080};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03190};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03190,
KW   ECO:0000313|EMBL:PGH01833.1};
KW   Ubiquinone {ECO:0000313|EMBL:PGH01833.1};
KW   Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_03190}.
FT   REGION       27     47       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A2B7WZ40}.
FT   REGION       90    119       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A2B7WZ40}.
FT   REGION      136    166       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A2B7WZ40}.
FT   REGION      224    251       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A2B7WZ40}.
FT   COMPBIAS     33     47       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A2B7WZ40}.
FT   COMPBIAS     90    118       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A2B7WZ40}.
FT   COMPBIAS    149    166       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A2B7WZ40}.
FT   COMPBIAS    231    251       Pro-rich. {ECO:0000256|MobiDB-lite:
FT                                A0A2B7WZ40}.
FT   BINDING      76     76       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_03190}.
FT   BINDING     126    126       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03190}.
FT   BINDING     185    185       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_03190}.
FT   BINDING     260    260       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03190}.
SQ   SEQUENCE   388 AA;  41459 MW;  150E9E494F0C87E2 CRC64;
     MALNPLRPSA AAARNITLLL RHAPRRTTTQ LDRVRQHSSS ASSVSSDEIT HFSSLASSWW
     DPLGPSRILH LMNPLRHEFI ASCIAESNPR SAASSSSSSS NPHNKGDENT NTNTATPPGL
     RYLDIGCGGG IFAESLARTI PPSPSPNPNA SHQSTTTSTS TSTGTCATAS NLSPVTQASS
     ILAIDPSPVM IKIATAHARA DPLVYSHLQS GAFKYQNTSL EALLQNRPPS SPPSSSSPPP
     PSSPSAPPPP PQPFDIITLF EVLEHVNPQT SSPRSFLKQC LRLLQPGGWL VGSTIARTVP
     SYIVNQVIAE APWPIGVVPR GTHEWGKFVN DGELRGWVGE GLREIDGVGD GAVRWKCVGA
     MYFPGLGWKM IPGTEKLGNY FWAVQRGF
//
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