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Database: UniProt
Entry: A0A0P6W3I0_9BACI
LinkDB: A0A0P6W3I0_9BACI
Original site: A0A0P6W3I0_9BACI 
ID   A0A0P6W3I0_9BACI        Unreviewed;       426 AA.
AC   A0A0P6W3I0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=AM506_06090 {ECO:0000313|EMBL:KPL60677.1};
OS   Rossellomorea vietnamensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX   NCBI_TaxID=218284 {ECO:0000313|EMBL:KPL60677.1, ECO:0000313|Proteomes:UP000050398};
RN   [1] {ECO:0000313|EMBL:KPL60677.1, ECO:0000313|Proteomes:UP000050398}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCD-SED5 {ECO:0000313|EMBL:KPL60677.1,
RC   ECO:0000313|Proteomes:UP000050398};
RA   Lee R.D., Jospin G., Lang J.M., Coil D.A., Eisen J.A.;
RT   "Draft Genome Sequence of Bacillus vietnamensis UCD-SED5.";
RL   Submitted (AUG-2015) 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:KPL60677.1}.
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DR   EMBL; LIXZ01000003; KPL60677.1; -; Genomic_DNA.
DR   RefSeq; WP_060671592.1; NZ_LIXZ01000003.1.
DR   AlphaFoldDB; A0A0P6W3I0; -.
DR   PATRIC; fig|218284.4.peg.2341; -.
DR   eggNOG; COG2224; Bacteria.
DR   OrthoDB; 8629576at2; -.
DR   Proteomes; UP000050398; 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:KPL60677.1};
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:UP000050398}.
FT   ACT_SITE        189
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT   BINDING         90..92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         151
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT   BINDING         190..191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         226
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         311..315
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         345
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ   SEQUENCE   426 AA;  46905 MW;  D49E6F178333D90D CRC64;
     MVKANNERVT ALQENWEMDQ RWKGITRPYS AEDVIRLRGS IDIEHTLARH GSEKLWNLLH
     EEDYINALGA LTGNQAVQQV RAGLKAIYLS GWQVAADANL SGHMYPDQSL YPANSVPSVV
     KRINQALQRA DQVHYVEGDE SIDWFVPIVA DAEAGFGGQL NVFELMKGMI EAGASAVHFE
     DQLSSEKKCG HLGGKVLLPT QTSVKNLISA RLAADVMGVP TLIVARTDAN AADLITSDVD
     PYDAQFITGE RTPEGFFRTN AGLDQAIARG LAYAPYADLV WCETSEPSLE EARRFAEAIH
     AEHPGKLLAY NCSPSFNWKK KLDDETIAKF QVELGKMGYK FQFVTLAGFH ALNHSMFELA
     RGYKDRGMAA YSQLQEAEFA SEKHGYSATR HQREVGTGYF DEVSMVISGG TSSTTALKGS
     TEAAQF
//
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