ID Q8Z8I9_SALTI Unreviewed; 302 AA.
AC Q8Z8I9;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 24-JAN-2024, entry version 122.
DE SubName: Full=Citrate lyase beta chain {ECO:0000313|EMBL:CAD05099.1};
DE EC=4.1.3.6 {ECO:0000313|EMBL:CAD05099.1};
GN Name=citE {ECO:0000313|EMBL:CAD05099.1};
GN OrderedLocusNames=STY0671 {ECO:0000313|EMBL:CAD05099.1};
OS Salmonella typhi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370 {ECO:0000313|EMBL:CAD05099.1, ECO:0000313|Proteomes:UP000000541};
RN [1] {ECO:0000313|EMBL:CAD05099.1, ECO:0000313|Proteomes:UP000000541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18 {ECO:0000313|EMBL:CAD05099.1,
RC ECO:0000313|Proteomes:UP000000541};
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.,
RA Rutherford K., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; AL513382; CAD05099.1; -; Genomic_DNA.
DR RefSeq; NP_455199.1; NC_003198.1.
DR RefSeq; WP_000622336.1; NZ_QXGZ01000014.1.
DR AlphaFoldDB; Q8Z8I9; -.
DR STRING; 220341.gene:17584680; -.
DR KEGG; sty:STY0671; -.
DR PATRIC; fig|220341.7.peg.672; -.
DR eggNOG; COG2301; Bacteria.
DR HOGENOM; CLU_044864_0_0_6; -.
DR OMA; AWLFCPA; -.
DR Proteomes; UP000000541; Chromosome.
DR GO; GO:0008815; F:citrate (pro-3S)-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR InterPro; IPR011206; Citrate_lyase_beta/mcl1/mcl2.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR32308:SF10; CITRATE LYASE SUBUNIT BETA; 1.
DR PANTHER; PTHR32308; LYASE BETA SUBUNIT, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G13030)-RELATED; 1.
DR Pfam; PF03328; HpcH_HpaI; 1.
DR PIRSF; PIRSF015582; Cit_lyase_B; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:CAD05099.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2}.
FT DOMAIN 15..234
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 76
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 166
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 302 AA; 33038 MW; E37E0F513C8C5489 CRC64;
MISASLQQRK TRTRRSMLFV PGANAAMVNN SFIYPADALM FDLEDSVALR EKHAARRLVY
HALQHPLYRD VETIVRVNAL DSEWGVNDLE AVVRGGADVV RLPKTDTAQD VIDIENEILR
IENACGREPG STGLLAAVES PLGITRAVEI AHASERLIGI ALGAEDYVRN LRTERSPEGT
ELLFARCAIL QAARSAGIQA FDTVYSDANN EAGFLQEAAH IKQLGFDGKS LINPRQIELL
HNLYAPTRKE VAHARLVVEA AEAAAREGLG VVSLNGKMVD SPVIERARLV LSRAELSGIR
EE
//