Reviewed, UniProtKB/Swiss-Prot Q8FB35 (UBIC_ECOL6)

Names and origin

Protein names

Recommended name:
    Chorismate--pyruvate lyase
      Short name=CL
      Short name=CPL
    EC=4.1.3.40

Gene names

Name:	ubiC
Ordered Locus Names:	c5009

Organism

Escherichia coli O6 [Complete proteome] [HAMAP]

Taxonomic identifier

217992 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	165 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway By similarity.
Catalytic activity	Chorismate = 4-hydroxybenzoate + pyruvate. HAMAP MF_01632
Pathway	Cofactor biosynthesis; ubiquinone biosynthesis. HAMAP MF_01632
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the ubiC family.

Ontologies

Keywords
Biological process	Ubiquinone biosynthesis
Cellular component	Cytoplasm
Ligand	Pyruvate
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	pyruvate biosynthetic process Inferred from electronic annotation. Source: HAMAP ubiquinone biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	chorismate lyase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 165	165	Chorismate--pyruvate lyase HAMAP MF_01632		PRO_0000240547
Sites
	Binding site	35	1	Substrate; via amide nitrogen By similarity
	Binding site	77	1	Substrate By similarity
	Binding site	115	1	Substrate; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8FB35-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 7705434B48859FB6	FASTA	165	18,808
	10 20 30 40 50 60 MSHPALTQLR ALRYFTEIPA LEPQLLDWLL LEDSMTKRFE QQGKTVSVTM IREGFVEQNE 70 80 90 100 110 120 IPEELPLLPK ESRYWLREIL LCADGEPWLA GRTVVPVSTL SGPELALQKL GKTPLGRYLF 130 140 150 160 TSSTLTRDFI EIGRDAGLWG RRSRLRLSGK PLLLTELFLP ASPLY

References

[1]

"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014075 Genomic DNA. Translation: AAN83435.1.
RefSeq	NP_756861.1.
3D structure databases
HSSP	HSSP built from PDB template 1FW9 based on UniProtKB P26602.
SMR	Q8FB35. Positions 2-165.
ModBase	Search...
Genome annotation databases
GeneID	1039545.
GenomeReviews	Gene locus c5009 in contig AE014075_GR.
KEGG	ecc:c5009.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8FB35.
OMA	WGRRSRF.
Enzyme and pathway databases
BRENDA	4.1.3.40. 292881.
Family and domain databases
HAMAP	MF_01632. [Tree]
InterPro	IPR007440. Chorismate--pyruvate_lyase. [Graphical view]
Pfam	PF04345. Chor_lyase. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

UBIC_ECOL6

Accession

Primary (citable) accession number: Q8FB35

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 27, 2006
Last sequence update:	March 1, 2003
Last modified:	November 3, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)