P0A9I1 (CITE_ECOLI) 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
Synonyms:	ybdW
Ordered Locus Names:	b0616, JW0608

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [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.
Sequence similarities	Belongs to the HpcH/HpaI aldolase family. Citrate lyase beta subunit subfamily.
Sequence caution	The sequence AAB40816.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Lyase
Technical term	Complete proteome Reference 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_0000089757
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
Experimental info
	Sequence conflict	150 – 156	7	IAHASER → SLTLPRL in AAC28948. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P0A9I1 [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

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	Ingmer H., Cohen S.N. Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-156. Strain: K12 / MG1655 / ATCC 47076.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U82598 Genomic DNA. Translation: AAB40816.1. Different initiation. U00096 Genomic DNA. Translation: AAC73717.2. AP009048 Genomic DNA. Translation: BAA35252.1. U46667 Genomic DNA. Translation: AAC28948.1.
PIR	F64795.
RefSeq	NP_415149.4. NC_000913.2.
3D structure databases
ProteinModelPortal	P0A9I1.
SMR	P0A9I1. Positions 10-245.
ModBase	Search...
Protein-protein interaction databases
IntAct	P0A9I1. 1 interaction.
MINT	MINT-1283346.
Proteomic databases
PRIDE	P0A9I1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000005021; EBESCP00000005021; EBESCG00000004097. EBESCT00000014845; EBESCP00000014136; EBESCG00000013905.
GeneID	945406.
GenomeReviews	Gene locus JW0608 in contig AP009048_GR. Gene locus b0616 in contig U00096_GR.
KEGG	ecj:JW0608. eco:b0616.
PATRIC	32116412. VBIEscCol129921_0646.
Organism-specific databases
EchoBASE	EB3312.
EcoGene	EG13542. citE.
Phylogenomic databases
eggNOG	COG2301.
GeneTree	EBGT00050000010557.
HOGENOM	HBG676713.
OMA	TDMKTHR.
PhylomeDB	P0A9I1.
ProtClustDB	CLSK874112.
Enzyme and pathway databases
BioCyc	EcoCyc:CITRYLY-MONOMER. MetaCyc:CITRYLY-MONOMER.
Gene expression databases
Genevestigator	P0A9I1.
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_ECOLI

Accession

Primary (citable) accession number: P0A9I1
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 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program