P0A9I2 (CITE_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Citrate lyase subunit beta
Short name=Citrase beta chain
EC=4.1.3.6

Alternative name(s):
Citrate (pro-3S)-lyase subunit beta
Citryl-CoA lyase subunit
EC=4.1.3.34

Gene names

Name:	citE
Ordered Locus Names:	c0706

Organism

Escherichia coli O6 [Complete proteome] [HAMAP]

Taxonomic identifier

217992 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	302 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Represents a citryl-ACP lyase By similarity.
Catalytic activity	Citrate = acetate + oxaloacetate. (3S)-citryl-CoA = acetyl-CoA + oxaloacetate.
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Subunit structure	Oligomer with a subunit composition of (alpha,beta, gamma)6 By similarity.
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the HpcH/HpaI aldolase family. Citrate lyase beta subunit subfamily.
Sequence caution	The sequence AAN79181.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	acetyl-CoA metabolic process Inferred from electronic annotation. Source: InterPro cellular aromatic compound metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	citrate lyase complex Inferred from electronic annotation. Source: InterPro
Molecular function	citrate (pro-3S)-lyase activity Inferred from electronic annotation. Source: EC citryl-CoA lyase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 302	302	Citrate lyase subunit beta		PRO_0000089756
Sites
	Metal binding	139	1	Magnesium By similarity
	Metal binding	166	1	Magnesium By similarity
	Binding site	76	1	Substrate By similarity
	Binding site	139	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0A9I2 [UniParc]. Last modified July 19, 2005. Version 1. Checksum: 204E8CCD40A2A52E	FASTA	302	33,110
	10 20 30 40 50 60 MISASLQQRK TRTRRSMLFV PGANAAMVSN SFIYPADALM FDLEDSVALR EKDTARRMVY 70 80 90 100 110 120 HALQHPLYRD IETIVRVNAL DSEWGVNDLE AVVRGGADVV RLPKTDTAQD VLDIEKEILR 130 140 150 160 170 180 IEKACGREPG STGLLAAIES PLGITRAVEI AHASERLIGI ALGAEDYVRN LRTERSPEGT 190 200 210 220 230 240 ELLFARCSIL QAARSAGIQA FDTVYSDANN EAGFLQEAAH IKQLGFDGKS LINPRQIDLL 250 260 270 280 290 300 HNLYAPTQKE VDHARRVVEA AEAAAREGLG VVSLNGKMVD GPVIDRARLV LSRAELSGIR EE

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
EMBL GenBank DDBJ	AE014075 Genomic DNA. Translation: AAN79181.1. Different initiation.
RefSeq	NP_752637.1. NC_004431.1.
3D structure databases
ProteinModelPortal	P0A9I2.
SMR	P0A9I2. Positions 10-245.
ModBase	Search...
Proteomic databases
PRIDE	P0A9I2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000041243; EBESCP00000039592; EBESCG00000040293.
GeneID	1035930.
GenomeReviews	Gene locus c0706 in contig AE014075_GR.
KEGG	ecc:c0706.
PATRIC	18279451. VBIEscCol75197_0669.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000010557.
HOGENOM	HBG676713.
OMA	TDMKTHR.
ProtClustDB	CLSK874112.
Family and domain databases
InterPro	IPR005000. Aldehyde-lyase_domain. IPR011206. Citrate_lyase_beta. IPR006475. Citrate_lyase_beta_bac. IPR015813. Pyrv/PenolPyrv_Kinase. [Graphical view]
Gene3D	G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
KO	K01644.
PANTHER	PTHR11105. PTHR11105. 1 hit.
Pfam	PF03328. HpcH_HpaI. 1 hit. [Graphical view]
PIRSF	PIRSF015582. Cit_lyase_B. 1 hit.
SUPFAM	SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMs	TIGR01588. CitE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

CITE_ECOL6

Accession

Primary (citable) accession number: P0A9I2
Secondary accession number(s): O54335, P77770

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	July 19, 2005
Last modified:	January 25, 2012
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program