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Protein

Citrate lyase subunit beta

Gene

citE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Represents a citryl-ACP lyase.By similarity

Catalytic activityi

Citrate = acetate + oxaloacetate.
(3S)-citryl-CoA = acetyl-CoA + oxaloacetate.

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei76 – 761SubstrateBy similarity
Metal bindingi139 – 1391MagnesiumBy similarity
Binding sitei139 – 1391SubstrateBy similarity
Metal bindingi166 – 1661MagnesiumBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:CITRYLY-MONOMER.
ECOL316407:JW0608-MONOMER.
MetaCyc:CITRYLY-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Citrate lyase subunit beta (EC:4.1.3.6)
Short name:
Citrase beta chain
Alternative name(s):
Citrate (pro-3S)-lyase subunit beta
Citryl-CoA lyase subunit (EC:4.1.3.34)
Gene namesi
Name:citE
Synonyms:ybdW
Ordered Locus Names:b0616, JW0608
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13542. citE.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 302302Citrate lyase subunit betaPRO_0000089757Add
BLAST

Proteomic databases

PaxDbiP0A9I1.
PRIDEiP0A9I1.

Expressioni

Inductioni

Repressed by H-NS. Part of the citCDEFXG operon.1 Publication

Interactioni

Subunit structurei

Oligomer with a subunit composition of (alpha,beta, gamma)6.By similarity

Protein-protein interaction databases

BioGridi4261999. 12 interactions.
DIPiDIP-9285N.
IntActiP0A9I1. 9 interactions.
MINTiMINT-1283346.
STRINGi511145.b0616.

Structurei

3D structure databases

ProteinModelPortaliP0A9I1.
SMRiP0A9I1. Positions 6-298.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CI0. Bacteria.
COG2301. LUCA.
HOGENOMiHOG000242282.
InParanoidiP0A9I1.
KOiK01644.
OMAiMALNKMS.
OrthoDBiEOG6DVJVX.
PhylomeDBiP0A9I1.

Family and domain databases

Gene3Di3.20.20.60. 1 hit.
InterProiIPR005000. Aldolase/citrate-lyase_domain.
IPR011206. Citrate_lyase_beta/mcl1/mcl2.
IPR006475. Citrate_lyase_beta_bac.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PANTHERiPTHR32308. PTHR32308. 1 hit.
PfamiPF03328. HpcH_HpaI. 1 hit.
[Graphical view]
PIRSFiPIRSF015582. Cit_lyase_B. 1 hit.
SUPFAMiSSF51621. SSF51621. 1 hit.
TIGRFAMsiTIGR01588. citE. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A9I1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MISASLQQRK TRTRRSMLFV PGANAAMVSN SFIYPADALM FDLEDSVALR
60 70 80 90 100
EKDTARRMVY HALQHPLYRD IETIVRVNAL DSEWGVNDLE AVVRGGADVV
110 120 130 140 150
RLPKTDTAQD VLDIEKEILR IEKACGREPG STGLLAAIES PLGITRAVEI
160 170 180 190 200
AHASERLIGI ALGAEDYVRN LRTERSPEGT ELLFARCSIL QAARSAGIQA
210 220 230 240 250
FDTVYSDANN EAGFLQEAAH IKQLGFDGKS LINPRQIDLL HNLYAPTQKE
260 270 280 290 300
VDHARRVVEA AEAAAREGLG VVSLNGKMVD GPVIDRARLV LSRAELSGIR

EE
Length:302
Mass (Da):33,110
Last modified:July 19, 2005 - v1
Checksum:i204E8CCD40A2A52E
GO

Sequence cautioni

The sequence AAB40816.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti150 – 1567IAHASER → SLTLPRL in AAC28948 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiF64795.
RefSeqiNP_415149.4. NC_000913.3.
WP_000622357.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73717; AAC73717; b0616.
BAA35252; BAA35252; BAA35252.
GeneIDi945406.
KEGGiecj:JW0608.
eco:b0616.
PATRICi32116412. VBIEscCol129921_0646.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiF64795.
RefSeqiNP_415149.4. NC_000913.3.
WP_000622357.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0A9I1.
SMRiP0A9I1. Positions 6-298.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261999. 12 interactions.
DIPiDIP-9285N.
IntActiP0A9I1. 9 interactions.
MINTiMINT-1283346.
STRINGi511145.b0616.

Proteomic databases

PaxDbiP0A9I1.
PRIDEiP0A9I1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73717; AAC73717; b0616.
BAA35252; BAA35252; BAA35252.
GeneIDi945406.
KEGGiecj:JW0608.
eco:b0616.
PATRICi32116412. VBIEscCol129921_0646.

Organism-specific databases

EchoBASEiEB3312.
EcoGeneiEG13542. citE.

Phylogenomic databases

eggNOGiENOG4105CI0. Bacteria.
COG2301. LUCA.
HOGENOMiHOG000242282.
InParanoidiP0A9I1.
KOiK01644.
OMAiMALNKMS.
OrthoDBiEOG6DVJVX.
PhylomeDBiP0A9I1.

Enzyme and pathway databases

BioCyciEcoCyc:CITRYLY-MONOMER.
ECOL316407:JW0608-MONOMER.
MetaCyc:CITRYLY-MONOMER.

Miscellaneous databases

PROiP0A9I1.

Family and domain databases

Gene3Di3.20.20.60. 1 hit.
InterProiIPR005000. Aldolase/citrate-lyase_domain.
IPR011206. Citrate_lyase_beta/mcl1/mcl2.
IPR006475. Citrate_lyase_beta_bac.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PANTHERiPTHR32308. PTHR32308. 1 hit.
PfamiPF03328. HpcH_HpaI. 1 hit.
[Graphical view]
PIRSFiPIRSF015582. Cit_lyase_B. 1 hit.
SUPFAMiSSF51621. SSF51621. 1 hit.
TIGRFAMsiTIGR01588. citE. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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. 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. 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.
  6. "Involvement of the leucine response transcription factor LeuO in regulation of the genes for sulfa drug efflux."
    Shimada T., Yamamoto K., Ishihama A.
    J. Bacteriol. 191:4562-4571(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: OPERON STRUCTURE, INDUCTION.
    Strain: K12 / BW25113.

Entry informationi

Entry nameiCITE_ECOLI
AccessioniPrimary (citable) accession number: P0A9I1
Secondary accession number(s): O54335, P77770
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: January 20, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.