ID   CITE_ECOL6              Reviewed;         302 AA.
AC   P0A9I2; O54335; P77770;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Citrate lyase subunit beta;
DE            Short=Citrase beta chain;
DE            EC=4.1.3.6;
DE   AltName: Full=Citrate (pro-3S)-lyase subunit beta;
DE   AltName: Full=Citryl-CoA lyase subunit;
DE            EC=4.1.3.34;
GN   Name=citE; OrderedLocusNames=c0706;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Represents a citryl-ACP lyase. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=citrate = acetate + oxaloacetate; Xref=Rhea:RHEA:10760,
CC         ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:30089; EC=4.1.3.6;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3S)-citryl-CoA = acetyl-CoA + oxaloacetate;
CC         Xref=Rhea:RHEA:20812, ChEBI:CHEBI:16452, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:57321; EC=4.1.3.34;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Oligomer with a subunit composition of (alpha,beta,gamma)6.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family. Citrate lyase
CC       beta subunit subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN79181.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN79181.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000622357.1; NC_004431.1.
DR   AlphaFoldDB; P0A9I2; -.
DR   SMR; P0A9I2; -.
DR   STRING; 199310.c0706; -.
DR   EnsemblBacteria; AAN79181; AAN79181; c0706.
DR   GeneID; 67416340; -.
DR   KEGG; ecc:c0706; -.
DR   eggNOG; COG2301; Bacteria.
DR   HOGENOM; CLU_044864_0_0_6; -.
DR   OMA; AWLFCPA; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0009346; C:ATP-independent citrate lyase complex; IEA:InterPro.
DR   GO; GO:0008815; F:citrate (pro-3S)-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008816; F:citryl-CoA lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.60; -; 1.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR   InterPro; IPR011206; Citrate_lyase_beta/mcl1/mcl2.
DR   InterPro; IPR006475; Citrate_lyase_beta_bac.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   Pfam; PF03328; HpcH_HpaI; 1.
DR   PIRSF; PIRSF015582; Cit_lyase_B; 1.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   TIGRFAMs; TIGR01588; citE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..302
FT                   /note="Citrate lyase subunit beta"
FT                   /id="PRO_0000089756"
FT   BINDING         76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         139
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   302 AA;  33110 MW;  204E8CCD40A2A52E CRC64;
     MISASLQQRK TRTRRSMLFV PGANAAMVSN SFIYPADALM FDLEDSVALR EKDTARRMVY
     HALQHPLYRD IETIVRVNAL DSEWGVNDLE AVVRGGADVV RLPKTDTAQD VLDIEKEILR
     IEKACGREPG STGLLAAIES PLGITRAVEI AHASERLIGI ALGAEDYVRN LRTERSPEGT
     ELLFARCSIL QAARSAGIQA FDTVYSDANN EAGFLQEAAH IKQLGFDGKS LINPRQIDLL
     HNLYAPTQKE VDHARRVVEA AEAAAREGLG VVSLNGKMVD GPVIDRARLV LSRAELSGIR
     EE