ID   A0A078B7E7_STYLE        Unreviewed;       518 AA.
AC   A0A078B7E7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Isocitrate lyase {ECO:0000256|ARBA:ARBA00012909, ECO:0000256|PIRNR:PIRNR001362};
GN   Name=Contig7484.g7995 {ECO:0000313|EMBL:CDW90410.1};
GN   ORFNames=STYLEM_19553 {ECO:0000313|EMBL:CDW90410.1};
OS   Stylonychia lemnae (Ciliate).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX   NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW90410.1, ECO:0000313|Proteomes:UP000039865};
RN   [1] {ECO:0000313|EMBL:CDW90410.1, ECO:0000313|Proteomes:UP000039865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=130c {ECO:0000313|EMBL:CDW90410.1,
RC   ECO:0000313|Proteomes:UP000039865};
RA   Swart Estienne;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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   -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC       isocitrate: step 1/2. {ECO:0000256|ARBA:ARBA00004793}.
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC       Isocitrate lyase family. {ECO:0000256|PIRNR:PIRNR001362}.
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DR   EMBL; CCKQ01018442; CDW90410.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A078B7E7; -.
DR   EnsemblProtists; CDW90410; CDW90410; STYLEM_19553.
DR   InParanoid; A0A078B7E7; -.
DR   OMA; YVSGWQV; -.
DR   OrthoDB; 983054at2759; -.
DR   Proteomes; UP000039865; 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:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
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; 2.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE   3: Inferred from homology;
KW   Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000039865};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   REGION          491..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        491..509
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        202
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT   BINDING         92..94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         164
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT   BINDING         203..204
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         239
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         390..394
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         425
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ   SEQUENCE   518 AA;  59111 MW;  279DD090DA998B53 CRC64;
     MTQKSNTFLD FIQIRWWANE RWRFIKRNYK SADVAALRSS IDLVTPSHYL SRKLYWLLRS
     KFDERDCSKT YGALDTVQVT NMCKYLSSIY VSGWQCSSTH VPAGHEPGPD FADYPMSTVP
     DKVMQLVKAQ LFHDRRQNEE RSTMTQQQRE QHKKVDYLVP IIADADAGFG GITSVMKLVK
     MFIEAGAGGI HIEDQKPGVK KCGHLGGKVL VSTREHVTRL QAARLQADVM GCDLVICART
     DALSAAFIDN NIDPADHPFI LGCVDPNNQQ KLLTFPQAGR ISICQNFRQE ERDRILKLWD
     QHAIHMSLEQ AMDMAKKHKF EFYFDWEGCR TQEGYYRVEG SVAFCVKRGI IFADYADLLW
     METPTPDLQV AKEFADGIHS QKPHALLSYN LSPSFNWDAQ QMSEEDLENF IPNLASMGYC
     WQFITLAGFH MDALISEVFS SNFQKTGMLG FVEYIQRKEK SENVDQLLHQ KWSGANLKDR
     EVNLASNNQI STLSNQMGGG TTEDQFYKNG QNKGHGHH
//