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Database: UniProt
Entry: A0A2N5G4Q1_9BACI
LinkDB: A0A2N5G4Q1_9BACI
Original site: A0A2N5G4Q1_9BACI 
ID   A0A2N5G4Q1_9BACI        Unreviewed;       426 AA.
AC   A0A2N5G4Q1;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=CU633_19850 {ECO:0000313|EMBL:PLR75685.1};
OS   Bacillus sp. V3-13.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2053728 {ECO:0000313|EMBL:PLR75685.1, ECO:0000313|Proteomes:UP000234805};
RN   [1] {ECO:0000313|EMBL:PLR75685.1, ECO:0000313|Proteomes:UP000234805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V3-13 {ECO:0000313|EMBL:PLR75685.1,
RC   ECO:0000313|Proteomes:UP000234805};
RA   Seuylemezian A., Cooper K., Vaishampayan P.;
RT   "Comparitive Functional Genomics of Dry Heat Resistant strains isolated
RT   from the Viking Spacecraft.";
RL   Submitted (NOV-2017) 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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PLR75685.1}.
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DR   EMBL; PGUZ01000069; PLR75685.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N5G4Q1; -.
DR   OrthoDB; 8629576at2; -.
DR   Proteomes; UP000234805; 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; 1.
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:PLR75685.1};
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:UP000234805}.
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;  46844 MW;  14055310EFEB493F CRC64;
     MTDERVQELQ ESWELDPRWR GVTRPYSAED VIKLRGSIDI EHTLARRGAE KLWNLINQED
     FVNALGALTG NQAVQQVKAG LKAIYLSGWQ VAADANLSGH MYPDQSLYPA NSVPNVVKRI
     NQALQRADQI HHSEGDNSID WFAPIVADAE AGFGGQLNVF ELMKGMIEAG AAGVHFEDQL
     SSEKKCGHLG GKVLLPTQTA IRNLIAARLA ADVMGVPTVL VARTDANAAD LITSDVDPYD
     APFITGERTP EGFFRVEAGL EQAIARGLAY APYADLIWCE TSEPNIEEAR QFAEAIHAKY
     PGKLLAYNCS PSFNWKKKLD DQTIAQFQIE LGKMGYKFQF VTLAGFHALN HSMFELARGY
     KERGMAAYSE LQEAEFASEE HGYTATRHQR EVGTGYFDQV SMVITGGTSS TTALKGSTEE
     AQFTAS
//
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