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Database: UniProt
Entry: A0A1I5LBC4_9RHOB
LinkDB: A0A1I5LBC4_9RHOB
Original site: A0A1I5LBC4_9RHOB 
ID   A0A1I5LBC4_9RHOB        Unreviewed;       245 AA.
AC   A0A1I5LBC4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   08-MAY-2019, entry version 8.
DE   RecName: Full=Ubiquinone biosynthesis O-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00472};
DE   AltName: Full=2-polyprenyl-6-hydroxyphenol methylase {ECO:0000256|HAMAP-Rule:MF_00472};
DE            EC=2.1.1.222 {ECO:0000256|HAMAP-Rule:MF_00472};
DE   AltName: Full=3-demethylubiquinone 3-O-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00472};
DE            EC=2.1.1.64 {ECO:0000256|HAMAP-Rule:MF_00472};
GN   Name=ubiG {ECO:0000256|HAMAP-Rule:MF_00472};
GN   ORFNames=SAMN04488047_101572 {ECO:0000313|EMBL:SFO94674.1};
OS   Tranquillimonas alkanivorans.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Tranquillimonas.
OX   NCBI_TaxID=441119 {ECO:0000313|EMBL:SFO94674.1, ECO:0000313|Proteomes:UP000199356};
RN   [1] {ECO:0000313|EMBL:SFO94674.1, ECO:0000313|Proteomes:UP000199356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19547 {ECO:0000313|EMBL:SFO94674.1,
RC   ECO:0000313|Proteomes:UP000199356};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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_00472, ECO:0000256|SAAS:SAAS00561163}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3-(all-trans-polyprenyl)benzene-1,2-diol + S-adenosyl-
CC         L-methionine = a 2-methoxy-6-(all-trans-polyprenyl)phenol + H(+)
CC         + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:31411, Rhea:RHEA-
CC         COMP:9550, Rhea:RHEA-COMP:9551, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:62729,
CC         ChEBI:CHEBI:62731; EC=2.1.1.222; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00472, ECO:0000256|SAAS:SAAS01122591};
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_00472,
CC         ECO:0000256|SAAS:SAAS01122587};
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00472, ECO:0000256|SAAS:SAAS00063519}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       UbiG/COQ3 family. {ECO:0000256|HAMAP-Rule:MF_00472,
CC       ECO:0000256|SAAS:SAAS01087951}.
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DR   EMBL; FOXA01000001; SFO94674.1; -; Genomic_DNA.
DR   BioCyc; GCF_900115595:BM162_RS02790-MONOMER; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000199356; Unassembled WGS sequence.
DR   GO; GO:0008425; F:2-polyprenyl-6-methoxy-1,4-benzoquinone methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008689; F:3-demethylubiquinone-9 3-O-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.
DR   TIGRFAMs; TIGR01983; UbiG; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000199356};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00472,
KW   ECO:0000256|SAAS:SAAS00448101, ECO:0000313|EMBL:SFO94674.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199356};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00472,
KW   ECO:0000256|SAAS:SAAS00448117};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00472,
KW   ECO:0000256|SAAS:SAAS00448111, ECO:0000313|EMBL:SFO94674.1};
KW   Ubiquinone {ECO:0000313|EMBL:SFO94674.1};
KW   Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_00472,
KW   ECO:0000256|SAAS:SAAS00063552}.
FT   BINDING      38     38       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00472}.
FT   BINDING      69     69       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00472}.
FT   BINDING      90     90       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00472}.
FT   BINDING     133    133       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00472}.
SQ   SEQUENCE   245 AA;  27012 MW;  3C783F955506D546 CRC64;
     MNTTTIDASE VAKFEAMAAE WWDPNGKFKP LHMLNPCRLD YICAQIAAEF GRDLSTGTPF
     DGLRLLDIGC GGGLLAEPMA RLGADVVGAD AAARNIPVAE VHAQQSGLDI DYRHTTAEDM
     AAAGEQFDVV LNMEVVEHVS DPLAYLTACQ QLLKPHGLMI CSTINRNPKS FAMAIVGAEW
     VMRWLPKGTH EWAKFITPDE LYDLIRQSGL DPVDRTGFVF NPVSWSWKLS DRDLSVNYVT
     ASVKR
//
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