ID   A0A366S7P4_9HYPO        Unreviewed;       599 AA.
AC   A0A366S7P4;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Isocitrate lyase {ECO:0000256|PIRNR:PIRNR001362};
GN   ORFNames=FIESC28_01790 {ECO:0000313|EMBL:RBR25353.1};
OS   Fusarium coffeatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium incarnatum-equiseti species complex.
OX   NCBI_TaxID=231269 {ECO:0000313|EMBL:RBR25353.1, ECO:0000313|Proteomes:UP000253153};
RN   [1] {ECO:0000313|EMBL:RBR25353.1, ECO:0000313|Proteomes:UP000253153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FIESC_28 {ECO:0000313|EMBL:RBR25353.1,
RC   ECO:0000313|Proteomes:UP000253153};
RA   Gardiner D.M.;
RT   "Fusarium incarnatum-equiseti species complex species 28.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate +
CC         succinate; Xref=Rhea:RHEA:16809, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:57429; EC=4.1.3.30;
CC         Evidence={ECO:0000256|ARBA:ARBA00001050};
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   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC       Isocitrate lyase family. {ECO:0000256|ARBA:ARBA00005704,
CC       ECO:0000256|PIRNR:PIRNR001362}.
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:RBR25353.1}.
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DR   EMBL; QKXC01000039; RBR25353.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A366S7P4; -.
DR   OrthoDB; 983054at2759; -.
DR   Proteomes; UP000253153; Unassembled WGS sequence.
DR   GO; GO:0004451; F:isocitrate lyase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046421; F:methylisocitrate lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   CDD; cd00377; ICL_PEPM; 1.
DR   Gene3D; 1.10.10.850; -; 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; ISOCITRATE LYASE/MALATE SYNTHASE; 1.
DR   PANTHER; PTHR21631:SF13; MITOCHONDRIAL 2-METHYLISOCITRATE LYASE ICL2; 1.
DR   Pfam; PF00463; ICL; 1.
DR   PIRSF; PIRSF001362; Isocit_lyase; 2.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001362};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3}.
FT   ACT_SITE        266
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT   BINDING         157..159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         228
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT   BINDING         267..268
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         303
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         484..488
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         519
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ   SEQUENCE   599 AA;  66582 MW;  BA847A7ABA1F3C11 CRC64;
     MLRRLSPRAS QRLISASLKP RSCAPLLAIR TISSTSVARM SSLSTHATQP ADAFQLLPES
     QKPGEAEDKL YEATVKEIEA WWASPRYKGI KRPYSAEDVA TKRGTQKVQY PSSVMAQKLF
     NLIREREAKG EPIHTMGAID PVQMTQQAPH QEVLYISGWA CSSLLTSTNE VSPDFGDYPY
     NTVPNQVQRL AKAQNMHDRK QWDLRRKMTA DDRTKTPYVD YLRPIIADGD TGHGGLSAVL
     KLAKLFAENG AAAVHFEDQL HGGKKCGHLA GKVLVPIGEH INRLVATRFQ WDVMGCENLV
     IARTDSESGK LLSSAIDVRD HEFILGVADS SIEPLAETIQ AMEAKGAVGA EIDAFEAQWV
     KNTKLVTFDE AAVAHMKKEG VDQAKIDEYL AETENDHDMG ISRRRGLASK YTKEPVYFNW
     DVPRTREGFY HYRAGMQAAT KRALAFGPYA DLLWVETGDP NVEVASKLGR AVREVYPRKG
     LVYNLSPSFN WMAHGFTDET LKSFIWDIAR EGFVLQLISL AGLHSNATIT TELSREFKKD
     GMKAYVDIVQ RREKDLKCDV LTHQKWSGAS YIDGILGAIQ SGSSSSKSMG EGNTEGQFH
//