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Database: UniProt
Entry: Q6D011_PECAS
LinkDB: Q6D011_PECAS
Original site: Q6D011_PECAS 
ID   Q6D011_PECAS            Unreviewed;       435 AA.
AC   Q6D011;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   27-MAR-2024, entry version 110.
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:CAG76887.1};
GN   Synonyms=icl {ECO:0000313|EMBL:CAG76887.1};
GN   OrderedLocusNames=ECA3990 {ECO:0000313|EMBL:CAG76887.1};
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491 {ECO:0000313|EMBL:CAG76887.1, ECO:0000313|Proteomes:UP000007966};
RN   [1] {ECO:0000313|EMBL:CAG76887.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SCRI1043 {ECO:0000313|EMBL:CAG76887.1};
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M., Hyman L.J., Holeva M.C.,
RA   Thomson N.R., Bentley S.D., Churcher C., Mungall K., Atkin R., Bason N.,
RA   Brooks K., Chillingworth T., Clark K., Doggett J., Fraser A., Hance Z.,
RA   Hauser H., Jagels K., Moule S., Norbertczak H., Ormond D., Price C.,
RA   Quail M.A., Sanders M., Walker D., Whitehead S., Salmond G.P.C.,
RA   Birch P.R.J., Barrell B.G., Parkhill J., Toth I.K.;
RT   "The genome sequence of the enterobacterial phytopathogen Erwinia
RT   carotovora subsp. atroseptica SCRI1043 and functional genomic
RT   identification of novel virulence factors.";
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
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; BX950851; CAG76887.1; -; Genomic_DNA.
DR   RefSeq; WP_011095484.1; NC_004547.2.
DR   AlphaFoldDB; Q6D011; -.
DR   STRING; 218491.ECA3990; -.
DR   GeneID; 57210650; -.
DR   KEGG; eca:ECA3990; -.
DR   PATRIC; fig|218491.5.peg.4053; -.
DR   eggNOG; COG2224; Bacteria.
DR   HOGENOM; CLU_019214_2_0_6; -.
DR   OrthoDB; 8629576at2; -.
DR   Proteomes; UP000007966; 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:CAG76887.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007966}.
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;  47956 MW;  EB0B9A93C0E43E72 CRC64;
     MTTSRTQQVQ HIEKEWKTAR WEGITRPYSA EDVINLRGSV NPECTLAQLG AARLWSLLHG
     EARKGYVNCL GALTGGQALQ QAKAGIEAIY LSGWQVAADA NLASSMYPDQ SLYPANSVPA
     VIERINNTFR RADQIQWANH IEPGDKRHTD YFLPIVADAE AGFGGVLNAF ELMKSMIEAG
     AAAVHFEDQL ASAKKCGHMG GKVLVPTQEA VQKLVAARLA ADVMGVPTLV VARTDADAAD
     LMTSDCDEYD RDFITGERTV EGFYRTRAGI EQAISRGLAY APYADLVWCE TSTPDLSLAR
     RFAEAIHAKF PGKLLAYNCS PSFNWKKNLD DSTIARFQDE LSAMGYKYQF ITLAGIHSMW
     FNMFDLAHAY AQGEGMRHYV EKVQQPEFEA IKDGYTFSSH QQEVGTGYFD KVTNIIQGGQ
     SSVTALTGST EEQQF
//
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