ID   A0A1I6C3J0_9BACI        Unreviewed;       426 AA.
AC   A0A1I6C3J0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=isocitrate lyase {ECO:0000256|ARBA:ARBA00012909};
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   ORFNames=SAMN04488577_3137 {ECO:0000313|EMBL:SFQ87763.1};
OS   Bacillus sp. cl95.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1761761 {ECO:0000313|EMBL:SFQ87763.1, ECO:0000313|Proteomes:UP000199578};
RN   [1] {ECO:0000313|EMBL:SFQ87763.1, ECO:0000313|Proteomes:UP000199578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL95 {ECO:0000313|EMBL:SFQ87763.1,
RC   ECO:0000313|Proteomes:UP000199578};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOYF01000004; SFQ87763.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6C3J0; -.
DR   STRING; 1761761.SAMN04488577_3137; -.
DR   OrthoDB; 8629576at2; -.
DR   Proteomes; UP000199578; Unassembled WGS sequence.
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; 1.
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:SFQ87763.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR001362-3};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR001362-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199578}.
FT   ACT_SITE        186
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT   BINDING         87..89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         148
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT   BINDING         187..188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         223
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         308..312
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         342
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ   SEQUENCE   426 AA;  46839 MW;  B245ABEA76AF6300 CRC64;
     MNDVRVKQLQ ESWELDSRWN GVKRPYTAEE VIKLRGSVDI EQTLARRGAE KLWKLVNEED
     FVNALGALTG NQAVQQVKAG LKAIYLSGWQ VAADANLSGN MYPDQSLYPA NSVPSVVKRI
     NQALQRADQI THSEGDNTID WFAPIVADAE AGFGGQLNVF ELMKAMIEAG AAGVHFEDQL
     SSEKKCGHLG GKVLLPTQTA VRNLIAARLA ADVMGVPTLV VARTDANAAD LITSDVDPYD
     APFITGERTT EGFFRVNAGL DQAISRGLAY APYADLVWCE TSEPDLEEAR RFAEAIHEKY
     PGKLLAYNCS PSFNWKKKLD DDTIAKFQVE LGKMGYKFQF VTLAGFHALN HSMFELARGY
     KDRGMAAYSE LQQAEFASEV NGYTATRHQR EVGTGYFDQV SMVITGGTSS TTALKGSTEE
     AQFHEK
//