ID   A0A0H4P415_9BACI        Unreviewed;       429 AA.
AC   A0A0H4P415;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
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=BSM4216_3411 {ECO:0000313|EMBL:AKP48589.1};
OS   Bacillus smithii.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1479 {ECO:0000313|EMBL:AKP48589.1, ECO:0000313|Proteomes:UP000036353};
RN   [1] {ECO:0000313|EMBL:AKP48589.1, ECO:0000313|Proteomes:UP000036353}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4216 {ECO:0000313|EMBL:AKP48589.1,
RC   ECO:0000313|Proteomes:UP000036353};
RA   Bosma E.F., Koehorst J.J., van Hijum S.A.F.T., Renckens B., Vriesendorp B.,
RA   van de Weijer A.H.P., Schaap P.J., de Vos W.M., van der Oost J.,
RA   van Kranenburg R.;
RT   "Complete genome sequence of thermophilic Bacillus smithii type strain DSM
RT   4216T.";
RL   Submitted (JUL-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};
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DR   EMBL; CP012024; AKP48589.1; -; Genomic_DNA.
DR   RefSeq; WP_003354103.1; NZ_JAQEZK010000015.1.
DR   AlphaFoldDB; A0A0H4P415; -.
DR   STRING; 1479.BSM4216_3411; -.
DR   KEGG; bsm:BSM4216_3411; -.
DR   eggNOG; COG2224; Bacteria.
DR   OrthoDB; 8629576at2; -.
DR   Proteomes; UP000036353; 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; 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:AKP48589.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR001362-3};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR001362-3}.
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   429 AA;  47738 MW;  A8CDC207DA32603E CRC64;
     MTDPRVQKLK ESWENDERWK GITRPYTAEE VIKLRGSIDI EYTLARRGAE KLWKLLHTED
     YINALGALTG NQAVQQVKAG LKAIYLSGWQ VAADANLAGQ MYPDQSLYPA NSVPHVVKRI
     NQALQRADQI HHLEGDDSID WFAPIVADAE AGFGGQLNVF ELMKAMIEAG AAGVHFEDQL
     SSEKKCGHLG GKVLLPTQTA VRNLIAARLA ADVMGVPTIL VGRTDAQAAD LITSDIDPYD
     APFITGERTE EGFYRTKKGI EQAIARGLAY APYADLIWCE TSEPNVEEAR QFAEAIHEKF
     PGKLLAYNCS PSFNWKAKLD DKTILNFQKE LAKMGYKFQF VTLAGFHTLN YSMFELARGY
     KERGMAAYSE LQQKEFASEK YGYTATRHQR EVGTGYFDEV SMVVTGGNAS TVALKGSTEV
     EQFQTQPQR
//