UBIG_ECOLI
ID UBIG_ECOLI Reviewed; 240 AA.
AC P17993; P76924;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Ubiquinone biosynthesis O-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00472};
DE AltName: Full=2-octaprenyl-6-hydroxyphenol methylase {ECO:0000255|HAMAP-Rule:MF_00472};
DE EC=2.1.1.222 {ECO:0000255|HAMAP-Rule:MF_00472, ECO:0000269|PubMed:10419476};
DE AltName: Full=3-demethylubiquinone-8 3-O-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00472};
DE EC=2.1.1.64 {ECO:0000255|HAMAP-Rule:MF_00472, ECO:0000269|PubMed:10419476};
GN Name=ubiG {ECO:0000255|HAMAP-Rule:MF_00472}; Synonyms=pufX, yfaB;
GN OrderedLocusNames=b2232, JW2226;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1479344; DOI=10.1099/00221287-138-10-2101;
RA Wu G., Williams H.D., Zamanian M., Gibson F., Poole R.K.;
RT "Isolation and characterization of Escherichia coli mutants affected in
RT aerobic respiration: the cloning and nucleotide sequence of ubiG.
RT Identification of an S-adenosylmethionine-binding motif in protein, RNA,
RT and small-molecule methyltransferases.";
RL J. Gen. Microbiol. 138:2101-2112(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=OV6;
RX PubMed=2834621; DOI=10.1111/j.1365-2958.1987.tb01932.x;
RA Hussain K., Elliott E.J., Salmond G.P.C.;
RT "The parD- mutant of Escherichia coli also carries a gyrAam mutation. The
RT complete sequence of gyrA.";
RL Mol. Microbiol. 1:259-273(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10419476; DOI=10.1074/jbc.274.31.21665;
RA Poon W.W., Barkovich R.J., Hsu A.Y., Frankel A., Lee P.T., Shepherd J.N.,
RA Myles D.C., Clarke C.F.;
RT "Yeast and rat Coq3 and Escherichia coli UbiG polypeptides catalyze both O-
RT methyltransferase steps in coenzyme Q biosynthesis.";
RL J. Biol. Chem. 274:21665-21672(1999).
RN [7]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=30686758; DOI=10.1016/j.chembiol.2018.12.001;
RA Hajj Chehade M., Pelosi L., Fyfe C.D., Loiseau L., Rascalou B.,
RA Brugiere S., Kazemzadeh K., Vo C.D., Ciccone L., Aussel L., Coute Y.,
RA Fontecave M., Barras F., Lombard M., Pierrel F.;
RT "A soluble metabolon synthesizes the isoprenoid lipid ubiquinone.";
RL Cell Chem. Biol. 26:482-492(2019).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS).
RA Zhu Y., Teng M., Li X.;
RT "Crystal structure of UbiG.";
RL Submitted (APR-2013) to the PDB data bank.
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-159 AND 188-240 IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE.
RA Zhu Y., Teng M., Li X.;
RT "Crystal structure of the UbiG/SAH complex.";
RL Submitted (APR-2013) to the PDB data bank.
CC -!- FUNCTION: O-methyltransferase that catalyzes the 2 O-methylation steps
CC in the ubiquinone biosynthetic pathway. {ECO:0000255|HAMAP-
CC Rule:MF_00472, ECO:0000269|PubMed:10419476}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3-demethylubiquinol + S-adenosyl-L-methionine = a ubiquinol
CC + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:44380, Rhea:RHEA-
CC COMP:9566, Rhea:RHEA-COMP:10914, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17976, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:84422; EC=2.1.1.64; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00472, ECO:0000269|PubMed:10419476};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3-(all-trans-polyprenyl)benzene-1,2-diol + S-adenosyl-L-
CC methionine = a 2-methoxy-6-(all-trans-polyprenyl)phenol + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:31411, Rhea:RHEA-COMP:9550,
CC Rhea:RHEA-COMP:9551, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:62729, ChEBI:CHEBI:62731;
CC EC=2.1.1.222; Evidence={ECO:0000255|HAMAP-Rule:MF_00472,
CC ECO:0000269|PubMed:10419476};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00472}.
CC -!- SUBUNIT: Homodimer (Probable). Component of the Ubi complex metabolon,
CC which regroups five ubiquinone biosynthesis proteins (UbiE, UbiF, UbiG,
CC UbiH and UbiI) and two accessory factors (UbiK and the lipid-binding
CC protein UbiJ) (PubMed:30686758). {ECO:0000269|PubMed:30686758,
CC ECO:0000305}.
CC -!- INTERACTION:
CC P17993; P61175: rplV; NbExp=3; IntAct=EBI-559367, EBI-542255;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:30686758}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. UbiG/COQ3
CC family. {ECO:0000255|HAMAP-Rule:MF_00472}.
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DR EMBL; Y00544; CAA68610.1; -; Genomic_DNA.
DR EMBL; M87509; AAA24714.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75292.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16049.1; -; Genomic_DNA.
DR PIR; A47682; A47682.
DR RefSeq; NP_416735.1; NC_000913.3.
DR RefSeq; WP_000990765.1; NZ_SSZK01000030.1.
DR PDB; 4KDC; X-ray; 2.09 A; A=1-240.
DR PDB; 4KDR; X-ray; 2.00 A; A=1-159, A=188-240.
DR PDB; 5DPM; X-ray; 2.10 A; A=1-240.
DR PDBsum; 4KDC; -.
DR PDBsum; 4KDR; -.
DR PDBsum; 5DPM; -.
DR AlphaFoldDB; P17993; -.
DR SMR; P17993; -.
DR BioGRID; 4262129; 12.
DR BioGRID; 850953; 7.
DR DIP; DIP-11070N; -.
DR IntAct; P17993; 19.
DR STRING; 511145.b2232; -.
DR jPOST; P17993; -.
DR PaxDb; P17993; -.
DR PRIDE; P17993; -.
DR EnsemblBacteria; AAC75292; AAC75292; b2232.
DR EnsemblBacteria; BAA16049; BAA16049; BAA16049.
DR GeneID; 946607; -.
DR KEGG; ecj:JW2226; -.
DR KEGG; eco:b2232; -.
DR PATRIC; fig|1411691.4.peg.3; -.
DR EchoBASE; EB1133; -.
DR eggNOG; COG2227; Bacteria.
DR HOGENOM; CLU_042432_5_0_6; -.
DR InParanoid; P17993; -.
DR OMA; RGTHDWE; -.
DR PhylomeDB; P17993; -.
DR BioCyc; EcoCyc:DHHB-METHYLTRANSFER-MON; -.
DR BioCyc; MetaCyc:DHHB-METHYLTRANSFER-MON; -.
DR BRENDA; 2.1.1.114; 2026.
DR BRENDA; 2.1.1.222; 2026.
DR UniPathway; UPA00232; -.
DR PRO; PR:P17993; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0110142; C:ubiquinone biosynthesis complex; IDA:EcoCyc.
DR GO; GO:0043431; F:2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone methyltransferase activity; IDA:EcoCyc.
DR GO; GO:0102208; F:2-polyprenyl-6-hydroxyphenol methylase activity; IEA:RHEA.
DR GO; GO:0008425; F:2-polyprenyl-6-methoxy-1,4-benzoquinone methyltransferase activity; IEA:InterPro.
DR GO; GO:0099119; F:3-demethylubiquinol-8 3-O-methyltransferase activity; IDA:EcoCyc.
DR GO; GO:0008689; F:3-demethylubiquinone-9 3-O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004395; F:hexaprenyldihydroxybenzoate methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:1901611; F:phosphatidylglycerol binding; IDA:EcoCyc.
DR GO; GO:0042538; P:hyperosmotic salinity response; IMP:EcoCyc.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IMP:EcoCyc.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00472; UbiG; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR010233; UbiG_MeTrfase.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR01983; UbiG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Ubiquinone biosynthesis.
FT CHAIN 1..240
FT /note="Ubiquinone biosynthesis O-methyltransferase"
FT /id="PRO_0000193379"
FT BINDING 44
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00472,
FT ECO:0000269|Ref.9"
FT BINDING 64
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00472,
FT ECO:0000269|Ref.9"
FT BINDING 85
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00472,
FT ECO:0000269|Ref.9"
FT BINDING 129
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00472,
FT ECO:0000269|Ref.9"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:4KDR"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:4KDR"
FT HELIX 35..52
FT /evidence="ECO:0007829|PDB:4KDR"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:4KDR"
FT HELIX 69..76
FT /evidence="ECO:0007829|PDB:4KDR"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:4KDR"
FT HELIX 88..101
FT /evidence="ECO:0007829|PDB:4KDR"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:4KDR"
FT HELIX 112..118
FT /evidence="ECO:0007829|PDB:4KDR"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:4KDR"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:4KDR"
FT HELIX 138..148
FT /evidence="ECO:0007829|PDB:4KDR"
FT STRAND 149..159
FT /evidence="ECO:0007829|PDB:4KDR"
FT HELIX 167..172
FT /evidence="ECO:0007829|PDB:4KDC"
FT HELIX 174..179
FT /evidence="ECO:0007829|PDB:4KDC"
FT HELIX 194..201
FT /evidence="ECO:0007829|PDB:4KDR"
FT STRAND 204..217
FT /evidence="ECO:0007829|PDB:4KDR"
FT TURN 218..221
FT /evidence="ECO:0007829|PDB:4KDR"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:4KDR"
FT STRAND 233..239
FT /evidence="ECO:0007829|PDB:4KDR"
SQ SEQUENCE 240 AA; 26555 MW; D4EB4707A06F5613 CRC64;
MNAEKSPVNH NVDHEEIAKF EAVASRWWDL EGEFKPLHRI NPLRLGYIAE RAGGLFGKKV
LDVGCGGGIL AESMAREGAT VTGLDMGFEP LQVAKLHALE SGIQVDYVQE TVEEHAAKHA
GQYDVVTCME MLEHVPDPQS VVRACAQLVK PGGDVFFSTL NRNGKSWLMA VVGAEYILRM
VPKGTHDVKK FIKPAELLGW VDQTSLKERH ITGLHYNPIT NTFKLGPGVD VNYMLHTQNK
