P17993 (UBIG_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-demethylubiquinone-9 3-methyltransferase
EC=2.1.1.64

Alternative name(s):
2-polyprenyl-6-hydroxyphenyl methylase
EC=2.1.1.222
3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase
Short name=DHHB methyltransferase

Gene names

Name:	ubiG
Synonyms:	pufX, yfaB
Ordered Locus Names:	b2232, JW2226

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	240 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Non-specific O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway. Ref.6
Catalytic activity	S-adenosyl-L-methionine + 3-demethylubiquinone-n = S-adenosyl-L-homocysteine + ubiquinone-n. Ref.6 S-adenosyl-L-methionine + 3-(all-trans-polyprenyl)benzene-1,2-diol = S-adenosyl-L-homocysteine + 2-methoxy-6-(all-trans-polyprenyl)phenol. Ref.6
Pathway	Cofactor biosynthesis; ubiquinone biosynthesis. HAMAP-Rule MF_00472
Subunit structure	Homodimer Probable.
Sequence similarities	Belongs to the methyltransferase superfamily. UbiG/COQ3 family.

Ontologies

Keywords
Biological process	Ubiquinone biosynthesis
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ubiquinone biosynthetic process Inferred from mutant phenotype PubMed 8703953. Source: EcoCyc
Molecular_function	2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone methyltransferase activity Inferred from direct assay Ref.6. Source: EcoCyc 2-polyprenyl-6-methoxy-1,4-benzoquinone methyltransferase activity Inferred from electronic annotation. Source: InterPro 3-demethylubiquinone-9 3-O-methyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
rplV	P61175	1	EBI-559367,EBI-542255

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 240	240	3-demethylubiquinone-9 3-methyltransferase HAMAP-Rule MF_00472		PRO_0000193379

Sequences

	Sequence		Length	Mass (Da)
	P17993 [UniParc]. Last modified November 1, 1990. Version 1. Checksum: D4EB4707A06F5613	FASTA	240	26,555
	10 20 30 40 50 60 MNAEKSPVNH NVDHEEIAKF EAVASRWWDL EGEFKPLHRI NPLRLGYIAE RAGGLFGKKV 70 80 90 100 110 120 LDVGCGGGIL AESMAREGAT VTGLDMGFEP LQVAKLHALE SGIQVDYVQE TVEEHAAKHA 130 140 150 160 170 180 GQYDVVTCME MLEHVPDPQS VVRACAQLVK PGGDVFFSTL NRNGKSWLMA VVGAEYILRM 190 200 210 220 230 240 VPKGTHDVKK FIKPAELLGW VDQTSLKERH ITGLHYNPIT NTFKLGPGVD VNYMLHTQNK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of Escherichia coli mutants affected in aerobic respiration: the cloning and nucleotide sequence of ubiG. Identification of an S-adenosylmethionine-binding motif in protein, RNA, and small-molecule methyltransferases." Wu G., Williams H.D., Zamanian M., Gibson F., Poole R.K. J. Gen. Microbiol. 138:2101-2112(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"The parD- mutant of Escherichia coli also carries a gyrAam mutation. The complete sequence of gyrA." Hussain K., Elliott E.J., Salmond G.P.C. Mol. Microbiol. 1:259-273(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: OV6.
[3]	"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T. DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Yeast and rat Coq3 and Escherichia coli UbiG polypeptides catalyze both O-methyltransferase steps in coenzyme Q biosynthesis." Poon W.W., Barkovich R.J., Hsu A.Y., Frankel A., Lee P.T., Shepherd J.N., Myles D.C., Clarke C.F. J. Biol. Chem. 274:21665-21672(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y00544 Genomic DNA. Translation: CAA68610.1. M87509 Genomic DNA. Translation: AAA24714.1. U00096 Genomic DNA. Translation: AAC75292.1. AP009048 Genomic DNA. Translation: BAA16049.1.
PIR	A47682.
RefSeq	NP_416735.1. NC_000913.2. YP_490471.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P17993.
SMR	P17993. Positions 9-214.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-11070N.
IntAct	P17993. 12 interactions.
MINT	MINT-1254635.
STRING	511145.b2232.
Proteomic databases
PaxDb	P17993.
PRIDE	P17993.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC75292; AAC75292; b2232. BAA16049; BAA16049; BAA16049.
GeneID	12933135. 946607.
KEGG	ecj:Y75_p2194. eco:b2232.
PATRIC	32119823. VBIEscCol129921_2321.
Organism-specific databases
EchoBASE	EB1133.
EcoGene	EG11143. ubiG.
Phylogenomic databases
eggNOG	COG2227.
HOGENOM	HOG000278065.
KO	K00568.
OMA	QETVESH.
ProtClustDB	PRK05134.
Enzyme and pathway databases
BioCyc	EcoCyc:DHHB-METHYLTRANSFER-MONOMER. ECOL316407:JW2226-MONOMER. MetaCyc:DHHB-METHYLTRANSFER-MONOMER.
UniPathway	UPA00232.
Gene expression databases
Genevestigator	P17993.
Family and domain databases
HAMAP	MF_00472. UbiG.
InterPro	IPR010233. UbiG_MeTrfase. [Graphical view]
PANTHER	PTHR23134. PTHR23134. 1 hit.
TIGRFAMs	TIGR01983. UbiG. 1 hit.
ProtoNet	Search...

Entry information

Entry name

UBIG_ECOLI

Accession

Primary (citable) accession number: P17993
Secondary accession number(s): P76924

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	May 1, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program