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Database: UniProt
Entry: A0A0D6ZCB5_9BACI
LinkDB: A0A0D6ZCB5_9BACI
Original site: A0A0D6ZCB5_9BACI 
ID   A0A0D6ZCB5_9BACI        Unreviewed;       427 AA.
AC   A0A0D6ZCB5;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-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=UB32_04160 {ECO:0000313|EMBL:KIY23192.1};
OS   Mesobacillus subterraneus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX   NCBI_TaxID=285983 {ECO:0000313|EMBL:KIY23192.1, ECO:0000313|Proteomes:UP000032512};
RN   [1] {ECO:0000313|EMBL:KIY23192.1, ECO:0000313|Proteomes:UP000032512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MITOT1 {ECO:0000313|EMBL:KIY23192.1,
RC   ECO:0000313|Proteomes:UP000032512};
RA   Peet K.C., Thompson J.R.;
RT   "Draft genome sequences of the supercritical CO2 tolerant bacteria Bacillus
RT   subterraneus MITOT1 and Bacillus cereus MIT0214.";
RL   Submitted (JAN-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:KIY23192.1}.
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DR   EMBL; JXIQ01000023; KIY23192.1; -; Genomic_DNA.
DR   RefSeq; WP_044391455.1; NZ_JXIQ01000023.1.
DR   AlphaFoldDB; A0A0D6ZCB5; -.
DR   PATRIC; fig|285983.3.peg.3209; -.
DR   OrthoDB; 8629576at2; -.
DR   Proteomes; UP000032512; 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:KIY23192.1};
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:UP000032512}.
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   427 AA;  46959 MW;  9185A15945E7BED0 CRC64;
     MTQDRVKQLQ ESWELDNRWA AVERTYTAED VIKLRGSIDM EYTLARRGAE KLWKLLNEED
     FVNALGALTG NQAVQQVKAG LKAIYLSGWQ VAADANLSGN MYPDQSLYPA NSVPAVVKRI
     NQALQRADQI TYGEGEDSID WFAPIIADAE AGFGGQLNVF ELMKGMIEAG AAGVHFEDQL
     SSEKKCGHLG GKVLLPTQTA VRNLIAARLA ADVMGTPTLI VARTDANAAD LITSDVDPTD
     APFITGERTP EGFFRTKAGL DQAIARGLAY APYADLVWCE TSEPDLEEAR RFAEAIQEKF
     PGKLLAYNCS PSFNWKKKLD EETIAKFQIE LGKMGYKFQF VTLAGFHALN HSMFELARGY
     KERGMAAYSE LQQAEFASEQ YGYTATRHQR EVGTGYFDDV SMVISGGTSS TTALKGSTEE
     AQFTASR
//
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