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P0AG03 (UBIX_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-octaprenyl-4-hydroxybenzoate carboxy-lyase partner protein

EC=4.1.1.-
Alternative name(s):
Polyprenyl p-hydroxybenzoate decarboxylase
Gene names
Name:ubiX
Synonyms:dedF
Ordered Locus Names:b2311, JW2308
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length189 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Acts in concert with UbiD to perform the decarboxylation of 4-hydroxy-3-octaprenyl-benzoate, a step in the biosynthesis of coenzyme Q. Nevertheless, it is not clear how UbiX and UbiD act together and if UbiX has itself a decarboxylase activity. UbiX may function to deliver the substrate to its UbiD partner, which performs the decarboxylation step. Ref.6 Ref.7

Cofactor

Binds 1 FMN per subunit By similarity.

Pathway

Cofactor biosynthesis; ubiquinone biosynthesis.

Induction

During aerobic growth, expression depends on the carbon source, with the highest expression on succinate, a median expression on glycerol, and the lowest on glucose. During anaerobic growth, glucose does not inhibit expression. Ref.5

Disruption phenotype

Cells lacking this gene produce very low levels of coenzyme Q8 during logarithmic growth, grow slowly on succinate as the sole carbon source, accumulate 4-hydroxy-3-octaprenyl-benzoate, and have reduced UbiG O-methyltransferase activity. In contrast, they synthesize near normal levels of Q8 in the stationary phase. Ref.7

Sequence similarities

Belongs to the polyprenyl p-hydroxybenzoate / phenylacrylic acid decarboxylases family.

Ontologies

Keywords
   Biological processUbiquinone biosynthesis
   LigandFlavoprotein
FMN
   Molecular functionDecarboxylase
Lyase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processubiquinone biosynthetic process

Inferred from genetic interaction Ref.6. Source: EcoCyc

   Molecular_function3-octaprenyl-4-hydroxybenzoate carboxy-lyase activity

Inferred from genetic interaction Ref.6. Source: EcoCyc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1891893-octaprenyl-4-hydroxybenzoate carboxy-lyase partner protein
PRO_0000134950

Regions

Nucleotide binding10 – 123FMN By similarity
Nucleotide binding88 – 914FMN By similarity

Sites

Binding site371FMN By similarity
Binding site1231FMN By similarity

Experimental info

Sequence conflict621T → S in AAA23970. Ref.1
Sequence conflict139 – 14810AEIGAVIMPP → GRNRCGDYAS in AAA23970. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P0AG03 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 057255DB020BF5B4

FASTA18920,695
        10         20         30         40         50         60 
MKRLIVGISG ASGAIYGVRL LQVLRDVTDI ETHLVMSQAA RQTLSLETDF SLREVQALAD 

        70         80         90        100        110        120 
VTHDARDIAA SISSGSFQTL GMVILPCSIK TLSGIVHSYT DGLLTRAADV VLKERRPLVL 

       130        140        150        160        170        180 
CVRETPLHLG HLRLMTQAAE IGAVIMPPVP AFYHRPQSLD DVINQTVNRV LDQFAITLPE 


DLFARWQGA 

« Hide

References

« Hide 'large scale' references
[1]"The hisT-purF region of the Escherichia coli K-12 chromosome. Identification of additional genes of the hisT and purF operons."
Nonet M.L., Marvel C.C., Tolan D.R.
J. Biol. Chem. 262:12209-12217(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"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. expand/collapse author list , 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.
[3]"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 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"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.
[5]"Regulation of the isofunctional genes ubiD and ubiX of the ubiquinone biosynthetic pathway of Escherichia coli."
Zhang H., Javor G.T.
FEMS Microbiol. Lett. 223:67-72(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[6]"Genetic evidence for an interaction of the UbiG O-methyltransferase with UbiX in Escherichia coli coenzyme Q biosynthesis."
Gulmezian M., Zhang H., Javor G.T., Clarke C.F.
J. Bacteriol. 188:6435-6439(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"The role of UbiX in Escherichia coli coenzyme Q biosynthesis."
Gulmezian M., Hyman K.R., Marbois B.N., Clarke C.F., Javor G.T.
Arch. Biochem. Biophys. 467:144-153(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M68935 Genomic DNA. Translation: AAA23970.1.
U00096 Genomic DNA. Translation: AAC75371.1.
AP009048 Genomic DNA. Translation: BAA16157.1.
PIRXMECFD. E65003.
RefSeqNP_416814.1. NC_000913.3.
YP_490553.1. NC_007779.1.

3D structure databases

ProteinModelPortalP0AG03.
SMRP0AG03. Positions 3-188.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-47873N.
IntActP0AG03. 6 interactions.
MINTMINT-1239757.
STRING511145.b2311.

Proteomic databases

PaxDbP0AG03.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75371; AAC75371; b2311.
BAA16157; BAA16157; BAA16157.
GeneID12931532.
949033.
KEGGecj:Y75_p2277.
eco:b2311.
PATRIC32119993. VBIEscCol129921_2406.

Organism-specific databases

EchoBASEEB1037.
EcoGeneEG11044. ubiX.

Phylogenomic databases

eggNOGCOG0163.
HOGENOMHOG000225437.
KOK03186.
OMAIHIENML.
OrthoDBEOG6C8MXR.
PhylomeDBP0AG03.
ProtClustDBPRK06029.

Enzyme and pathway databases

BioCycEcoCyc:UBIX-MONOMER.
ECOL316407:JW2308-MONOMER.
MetaCyc:UBIX-MONOMER.
UniPathwayUPA00232.

Gene expression databases

GenevestigatorP0AG03.

Family and domain databases

Gene3D3.40.50.1950. 1 hit.
InterProIPR003382. Flavoprotein.
IPR004507. UbiX_Pad1.
[Graphical view]
PfamPF02441. Flavoprotein. 1 hit.
[Graphical view]
SUPFAMSSF52507. SSF52507. 1 hit.
TIGRFAMsTIGR00421. ubiX_pad. 1 hit.
ProtoNetSearch...

Other

PROP0AG03.

Entry information

Entry nameUBIX_ECOLI
AccessionPrimary (citable) accession number: P0AG03
Secondary accession number(s): P09550, P77715
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: April 16, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene