[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1093/dnares/3.3.137; PubMed=8905232 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "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."; DNA Res. 3:137-155(1996).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; 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.; "Sequence of minutes 4-25 of Escherichia coli."; Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-156. STRAIN=K12 / MG1655 / ATCC 47076; Ingmer H., Cohen S.N.; Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Represents a citryl-ACP lyase (By similarity).
CATALYTIC ACTIVITY: Citrate = acetate + oxaloacetate.
CATALYTIC ACTIVITY: (3S)-citryl-CoA = acetyl-CoA + oxaloacetate.
COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
SUBUNIT: Oligomer with a subunit composition of (alpha,beta, gamma)6 (By similarity).
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the hpcH/hpaI aldolase family. Citrate lyase beta subunit subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U82598; AAB40816.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC73717.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA35252.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U46667; AAC28948.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

F64795; F64795.

RefSeq

AP_001263.1; -.
NP_415149.4; -.

3D structure databases

ModBase

P0A9I1.

Enzyme and pathway databases

BioCyc

EcoCyc:CITRYLY-MON; -.
MetaCyc:CITRYLY-MON; -.

Organism-specific databases

EchoBASE

EB3312; -.

EcoGene

EG13542; citE.

Ontologies

GO:0009346;	Cellular component: citrate lyase complex (inferred from electronic annotation from InterPro).
GO:0008815;	Molecular function: citrate (pro-3S)-lyase activity (inferred from electronic annotation from EC).
GO:0008816;	Molecular function: citryl-CoA lyase activity (inferred from electronic annotation from EC).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006084;	Biological process: acetyl-CoA metabolic process (inferred from electronic annotation from InterPro).
GO:0006725;	Biological process: cellular aromatic compound metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR011206; Citrate_lyase_beta.
IPR006475; Citrate_lyase_beta_bac.
IPR005000; HpcH_HpaI.
IPR015813; Pyrv/PenolPyrv_Kinase_cat.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.60; Pyrv/PenolPyrv_Kinase_cat; 1.

Pfam

PF03328; HpcH_HpaI; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF015582; Cit_lyase_B; 1.

TIGRFAMs

TIGR01588; citE; 1.

Genome annotation databases

GeneID

945406; -.

GenomeReviews

AP009048_GR; JW0608.
U00096_GR; b0616.

KEGG

ecj:JW0608; -.
eco:b0616; -.

Phylogenomic databases

HOGENOM

P0A9I1; -.

OMA

P0A9I1; IELLFAR.

Genome annotation databases

CMR

P0A9I1; b0616.

Other

ProtoNet

P0A9I1.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Lyase; Magnesium; Metal-binding.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 302`	`302`	`Citrate lyase subunit beta.`	`PRO_0000089757`
`METAL`	`139 139`		`Magnesium (By similarity).`
`METAL`	`166 166`		`Magnesium (By similarity).`
`BINDING`	`76 76`		`Substrate (By similarity).`
`BINDING`	`139 139`		`Substrate (By similarity).`
`CONFLICT`	`150 156`		`IAHASER -> SLTLPRL (in Ref. 5; AAC28948).`

Sequence information

Length: 302 AA [This is the length of the unprocessed precursor]

Molecular weight: 33110 Da [This is the MW of the unprocessed precursor]

CRC64: 204E8CCD40A2A52E [This is a checksum on the sequence]

        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

P0A9I1 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools