ID A1JRX1_YERE8 Unreviewed; 435 AA.
AC A1JRX1;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=Isocitrate lyase {ECO:0000256|ARBA:ARBA00017446};
DE EC=4.1.3.1 {ECO:0000256|ARBA:ARBA00012909};
DE AltName: Full=Isocitrase {ECO:0000256|ARBA:ARBA00031022};
DE AltName: Full=Isocitratase {ECO:0000256|ARBA:ARBA00031921};
GN Name=aceA {ECO:0000313|EMBL:CAL13899.1};
GN Synonyms=icl {ECO:0000313|EMBL:CAL13899.1};
GN OrderedLocusNames=YE3880 {ECO:0000313|EMBL:CAL13899.1};
OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS 8081).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=393305 {ECO:0000313|EMBL:CAL13899.1, ECO:0000313|Proteomes:UP000000642};
RN [1] {ECO:0000313|EMBL:CAL13899.1, ECO:0000313|Proteomes:UP000000642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13174 / 8081 {ECO:0000313|Proteomes:UP000000642};
RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA Prentice M.B.;
RT "The complete genome sequence and comparative genome analysis of the high
RT pathogenicity Yersinia enterocolitica strain 8081.";
RL PLoS Genet. 2:2039-2051(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-threo-isocitrate = glyoxylate + succinate;
CC Xref=Rhea:RHEA:13245, ChEBI:CHEBI:15562, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:36655; EC=4.1.3.1;
CC Evidence={ECO:0000256|ARBA:ARBA00023531};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR001362-3};
CC Note=Can also use Mn(2+) ion. {ECO:0000256|PIRSR:PIRSR001362-3};
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DR EMBL; AM286415; CAL13899.1; -; Genomic_DNA.
DR RefSeq; WP_005174580.1; NC_008800.1.
DR RefSeq; YP_001008025.1; NC_008800.1.
DR AlphaFoldDB; A1JRX1; -.
DR KEGG; yen:YE3880; -.
DR PATRIC; fig|393305.7.peg.4128; -.
DR eggNOG; COG2224; Bacteria.
DR HOGENOM; CLU_019214_2_0_6; -.
DR OrthoDB; 8629576at2; -.
DR Proteomes; UP000000642; Chromosome.
DR GO; GO:0004451; F:isocitrate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR039556; ICL/PEPM.
DR InterPro; IPR006254; Isocitrate_lyase.
DR InterPro; IPR018523; Isocitrate_lyase_ph_CS.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR NCBIfam; TIGR01346; isocit_lyase; 2.
DR PANTHER; PTHR21631:SF3; BIFUNCTIONAL GLYOXYLATE CYCLE PROTEIN; 1.
DR PANTHER; PTHR21631; ISOCITRATE LYASE/MALATE SYNTHASE; 1.
DR Pfam; PF00463; ICL; 2.
DR PIRSF; PIRSF001362; Isocit_lyase; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE 4: Predicted;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:CAL13899.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3}.
FT ACT_SITE 196
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 92..94
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 158
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT BINDING 197..198
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 318..322
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 352
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ SEQUENCE 435 AA; 47799 MW; 9B8B244A2F87EEDF CRC64;
MTTSRTQQIQ QLEQEWKSPR WEGIIRPYSA EEVIKLRGSV NPECTLAQHG AKRLWELLHG
KSRKDYINCL GALTGGQALQ QAKAGVEAIY LSGWQVAADA NTASSMYPDQ SLYPVDSVPA
VVKRINNSFR RADQIQWSNN IEPDSKGYTD YFLPIVADAE AGFGGVLNAF ELMKAMIEAG
AAGVHFEDQL AAVKKCGHMG GKVLVPTQEA IQKLVAARLA ADVLGVPTLL IARTDADAAD
LLTSDCDPHD SEFITGDRTA EGFFRTHAGI EQAISRGLAY APYADLVWCE TSTPDLALAK
RFADAIHAQF PGKLLAYNCS PSFNWKKNLT DQQIASFQDE LSAMGYKYQF ITLAGIHSMW
FNMFDLAHAY AQGEGMKHYV EKVQQPEFAA VERGYTFASH QQEVGTGYFD KVTNIIQGGE
SSVTALTGST EEQQF
//
