(data stored in ACNUC7421 zone)

SWISSPROT: UBIG_RUEPO

ID   UBIG_RUEPO              Reviewed;         248 AA.
AC   Q5LWM6;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 86.
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=SPO0067;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C.,
RA   Brinkac L.M., Lewis M., Johri S., Weaver B., Pai G., Eisen J.A.,
RA   Rahe E., Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., DeBoy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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; CP000031; AAV93398.1; -; Genomic_DNA.
DR   RefSeq; WP_011045840.1; NC_003911.12.
DR   SMR; Q5LWM6; -.
DR   STRING; 246200.SPO0067; -.
DR   EnsemblBacteria; AAV93398; AAV93398; SPO0067.
DR   KEGG; sil:SPO0067; -.
DR   eggNOG; ENOG4108HWB; Bacteria.
DR   eggNOG; COG2227; LUCA.
DR   HOGENOM; HOG000278064; -.
DR   KO; K00568; -.
DR   OMA; GTHDYAK; -.
DR   OrthoDB; 1515497at2; -.
DR   BioCyc; RPOM246200:G1G48-68-MONOMER; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000001023; 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; Q5LWM6.
DR   SWISS-2DPAGE; Q5LWM6.
KW   Complete proteome; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase; Ubiquinone biosynthesis.
FT   CHAIN         1    248       Ubiquinone biosynthesis O-
FT                                methyltransferase.
FT                                /FTId=PRO_0000241739.
FT   BINDING      40     40       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_00472}.
FT   BINDING      71     71       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00472}.
FT   BINDING      92     92       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_00472}.
FT   BINDING     135    135       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00472}.
SQ   SEQUENCE   248 AA;  27614 MW;  76BF892F26E2C70A CRC64;
     MQAHPNTVDP SEIAKFEAMA AEWWDPHGKF KPLHMLNPCR LDYITRQIAG EFDRDLGTER
     PFAGLRLLDI GCGGGLLSEP MARLGAEVVG ADAAEGNLPV ARIHAEQSGL EIDYRHTTAE
     ALAEAGEQFD VVLNMEVVEH VADPLSYLRA THDLLKPGGL QICSTINRNP KSYAMAILGA
     EVVMRWLPRG THDWSKFITP DELFDLLRQA GLEPVDRKGF VFNPISWQWS ISDRDLSVNY
     VTASLRPR
//

If you have problems or comments...

PBIL Back to PBIL home page