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Database: UniProt
Entry: A0A3Q9QW94_9BACI
LinkDB: A0A3Q9QW94_9BACI
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ID   A0A3Q9QW94_9BACI        Unreviewed;       427 AA.
AC   A0A3Q9QW94;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=CHR53_02540 {ECO:0000313|EMBL:AZU60234.1};
OS   Neobacillus mesonae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX   NCBI_TaxID=1193713 {ECO:0000313|EMBL:AZU60234.1, ECO:0000313|Proteomes:UP000282892};
RN   [1] {ECO:0000313|EMBL:AZU60234.1, ECO:0000313|Proteomes:UP000282892}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H20-5 {ECO:0000313|EMBL:AZU60234.1,
RC   ECO:0000313|Proteomes:UP000282892};
RA   Kim S.Y., Song H., Sang M.K., Weon H.-Y., Song J.;
RT   "The complete genome sequence of Bacillus mesonae strain H20-5, an
RT   efficient strain improving plant abiotic stress resistance.";
RL   Submitted (JUL-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};
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DR   EMBL; CP022572; AZU60234.1; -; Genomic_DNA.
DR   RefSeq; WP_066390965.1; NZ_KV440949.1.
DR   AlphaFoldDB; A0A3Q9QW94; -.
DR   STRING; 1193713.GCA_001636315_03031; -.
DR   KEGG; nmk:CHR53_02540; -.
DR   OrthoDB; 8629576at2; -.
DR   Proteomes; UP000282892; 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; 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:AZU60234.1};
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:UP000282892}.
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;  46735 MW;  8B47D5C518F38566 CRC64;
     MTNSRAAQLQ ESWEMDARWK GIARPYTAED VIKLRGSIDI EHTLARKGAE KLWKLINEED
     YINALGALTG NQAVQQVKAG LKAIYLSGWQ VAADANLSGH MYPDQSLYPA NSVPSVVKRI
     NQALQRADQI SHSEGDNSID WFAPIVADAE AGFGGQLNCF ELMKGMIEAG AAGVHFEDQL
     SSEKKCGHLG GKVLLPTQTA VRNLIAARLA ADVMGVPTVL VARTDANAAD LITSDIDMND
     APFITGERTP EGFYRTNAGL DQAIARGLAY APYADLIWCE TSEPNIEEAR RFAEAIHEQF
     PGKLLAYNCS PSFNWKAKLD EETIAKFQQE LGKMGYKFQF VTLAGFHALN HSMFELARGY
     KDNGMAAYSK LQQAEFASEQ HGYTATRHQR EVGTGYFDQV SMVITGGTSS TTALKGSTEE
     EQFTGAK
//
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