CITE_ECOLI
ID CITE_ECOLI Reviewed; 302 AA.
AC P0A9I1; O54335; P77770;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
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; Synonyms=ybdW; OrderedLocusNames=b0616, JW0608;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-156.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Ingmer H., Cohen S.N.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP OPERON STRUCTURE, AND INDUCTION.
RC STRAIN=K12 / BW25113;
RX PubMed=19429622; DOI=10.1128/jb.00108-09;
RA Shimada T., Yamamoto K., Ishihama A.;
RT "Involvement of the leucine response transcription factor LeuO in
RT regulation of the genes for sulfa drug efflux.";
RL J. Bacteriol. 191:4562-4571(2009).
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.
CC -!- INDUCTION: Repressed by H-NS. Part of the citCDEFXG operon.
CC {ECO:0000269|PubMed:19429622}.
CC -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family. Citrate lyase
CC beta subunit subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB40816.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U82598; AAB40816.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73717.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA35252.1; -; Genomic_DNA.
DR EMBL; U46667; AAC28948.1; -; Genomic_DNA.
DR PIR; F64795; F64795.
DR RefSeq; NP_415149.4; NC_000913.3.
DR RefSeq; WP_000622357.1; NZ_STEB01000031.1.
DR AlphaFoldDB; P0A9I1; -.
DR SMR; P0A9I1; -.
DR BioGRID; 4261999; 12.
DR BioGRID; 849780; 6.
DR ComplexPortal; CPX-4781; Citrate lyase complex.
DR DIP; DIP-9285N; -.
DR IntAct; P0A9I1; 9.
DR STRING; 511145.b0616; -.
DR PaxDb; P0A9I1; -.
DR PRIDE; P0A9I1; -.
DR EnsemblBacteria; AAC73717; AAC73717; b0616.
DR EnsemblBacteria; BAA35252; BAA35252; BAA35252.
DR GeneID; 67416340; -.
DR GeneID; 945406; -.
DR KEGG; ecj:JW0608; -.
DR KEGG; eco:b0616; -.
DR PATRIC; fig|1411691.4.peg.1652; -.
DR EchoBASE; EB3312; -.
DR eggNOG; COG2301; Bacteria.
DR HOGENOM; CLU_044864_0_0_6; -.
DR InParanoid; P0A9I1; -.
DR OMA; AWLFCPA; -.
DR PhylomeDB; P0A9I1; -.
DR BioCyc; EcoCyc:CITRYLY-MON; -.
DR BioCyc; MetaCyc:CITRYLY-MON; -.
DR PRO; PR:P0A9I1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009346; C:ATP-independent citrate lyase complex; IPI:ComplexPortal.
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:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; IDA:ComplexPortal.
DR GO; GO:0006101; P:citrate metabolic process; IDA:ComplexPortal.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cytoplasm; Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..302
FT /note="Citrate lyase subunit beta"
FT /id="PRO_0000089757"
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"
FT CONFLICT 150..156
FT /note="IAHASER -> SLTLPRL (in Ref. 5; AAC28948)"
FT /evidence="ECO:0000305"
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
