(data stored in ACNUC7421 zone)

SWISSPROT: UBIG_RHOPS

ID   UBIG_RHOPS              Reviewed;         253 AA.
AC   Q13EZ9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 82.
DE   RecName: Full=Ubiquinone biosynthesis O-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00472};
DE   AltName: Full=2-polyprenyl-6-hydroxyphenol methylase {ECO:0000255|HAMAP-Rule:MF_00472};
DE            EC=2.1.1.222 {ECO:0000255|HAMAP-Rule:MF_00472};
DE   AltName: Full=3-demethylubiquinone 3-O-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00472};
DE            EC=2.1.1.64 {ECO:0000255|HAMAP-Rule:MF_00472};
GN   Name=ubiG {ECO:0000255|HAMAP-Rule:MF_00472};
GN   OrderedLocusNames=RPD_0100;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: O-methyltransferase that catalyzes the 2 O-methylation
CC       steps in the ubiquinone biosynthetic pathway. {ECO:0000255|HAMAP-
CC       Rule:MF_00472}.
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:0000255|HAMAP-Rule:MF_00472};
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:0000255|HAMAP-
CC         Rule:MF_00472};
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00472}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       UbiG/COQ3 family. {ECO:0000255|HAMAP-Rule:MF_00472}.
DR   EMBL; CP000283; ABE37340.1; -; Genomic_DNA.
DR   RefSeq; WP_011500533.1; NC_007958.1.
DR   SMR; Q13EZ9; -.
DR   STRING; 316057.RPD_0100; -.
DR   EnsemblBacteria; ABE37340; ABE37340; RPD_0100.
DR   KEGG; rpd:RPD_0100; -.
DR   eggNOG; ENOG4108HWB; Bacteria.
DR   eggNOG; COG2227; LUCA.
DR   HOGENOM; HOG000278064; -.
DR   KO; K00568; -.
DR   OMA; GTHDYAK; -.
DR   OrthoDB; 1515497at2; -.
DR   BioCyc; RPAL316057:RPD_RS00500-MONOMER; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000001818; Chromosome.
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;
DR   PRODOM; Q13EZ9.
DR   SWISS-2DPAGE; Q13EZ9.
KW   Complete proteome; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase; Ubiquinone biosynthesis.
FT   CHAIN         1    253       Ubiquinone biosynthesis O-
FT                                methyltransferase.
FT                                /FTId=PRO_1000013913.
FT   BINDING      47     47       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_00472}.
FT   BINDING      78     78       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00472}.
FT   BINDING      99     99       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_00472}.
FT   BINDING     141    141       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00472}.
SQ   SEQUENCE   253 AA;  28015 MW;  89A964384B4AAE1F CRC64;
     MALQSESTGP VSPSVDPAEI AKFSRLSAEW WDPTGKMAPL HRINPLRISF IRDAACRKFE
     RNAKSLSCLS GLRMLDIGCG AGLLCEPFTR LGAQVIGIDP SATNIAAAKL HADKSHLAID
     YRCTTVEEID PRERFDIVMA MEVIEHVNDV PAFLGRCAAL MKPTGIMLVA TLNRNWKSFA
     LAIVGAEYVM RWLPRGTHQW DKFVTPDELE QHLQGLGLVV TEQSGLVFNP LADRWRLSPD
     MDVNYMVVAE TAP
//

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