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Database: UniProt
Entry: A0A0N1L8D2_9SPHN
LinkDB: A0A0N1L8D2_9SPHN
Original site: A0A0N1L8D2_9SPHN 
ID   A0A0N1L8D2_9SPHN        Unreviewed;       245 AA.
AC   A0A0N1L8D2;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   08-MAY-2019, entry version 20.
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=IP79_11195 {ECO:0000313|EMBL:KPF63103.1};
OS   Porphyrobacter sp. AAP60.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Porphyrobacter.
OX   NCBI_TaxID=1523423 {ECO:0000313|EMBL:KPF63103.1, ECO:0000313|Proteomes:UP000037996};
RN   [1] {ECO:0000313|EMBL:KPF63103.1, ECO:0000313|Proteomes:UP000037996}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP60 {ECO:0000313|EMBL:KPF63103.1,
RC   ECO:0000313|Proteomes:UP000037996};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome
RT   Sequencing.";
RL   Submitted (AUG-2015) 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}.
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:KPF63103.1}.
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DR   EMBL; LJHV01000011; KPF63103.1; -; Genomic_DNA.
DR   RefSeq; WP_054119387.1; NZ_LJHV01000011.1.
DR   EnsemblBacteria; KPF63103; KPF63103; IP79_11195.
DR   PATRIC; fig|1523423.3.peg.389; -.
DR   OrthoDB; 1515497at2; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000037996; 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:UP000037996};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00472,
KW   ECO:0000256|SAAS:SAAS00448101, ECO:0000313|EMBL:KPF63103.1};
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:KPF63103.1};
KW   Ubiquinone {ECO:0000313|EMBL:KPF63103.1};
KW   Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_00472,
KW   ECO:0000256|SAAS:SAAS00063552}.
FT   BINDING      43     43       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00472}.
FT   BINDING      74     74       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00472}.
FT   BINDING      95     95       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00472}.
FT   BINDING     136    136       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00472}.
SQ   SEQUENCE   245 AA;  25658 MW;  7A88DAAAFB978376 CRC64;
     MGNANIPNVT IRPEEADFFA KLARDWWNPK GPMASLHQVN PVRMAFIREA IDAHWTGAGA
     SAKPLAGKSA LDIGCGAGLV CEPLARLGAS VTGVDAAAEN VAAAAAHAEG VGLDIRYMAG
     EVAGLDIGTF DLVTTVEVIE HVADKPAFLR DVAARLAPDG LLVMSTPNRT AASRVLLVGA
     AEAVGYVPKG THHWEDFITP DELEALLGDA GLAVTAKRGI AWRPGKGLHL SDDMALNYIL
     SARRV
//
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