ID   ACEA_CANTR              Reviewed;         550 AA.
AC   P20014;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   13-SEP-2023, entry version 109.
DE   RecName: Full=Isocitrate lyase {ECO:0000303|PubMed:2361956};
DE            Short=ICL {ECO:0000305};
DE            Short=Isocitrase {ECO:0000305};
DE            Short=Isocitratase {ECO:0000305};
DE            EC=4.1.3.1 {ECO:0000250|UniProtKB:P28240};
DE   AltName: Full=Methylisocitrate lyase {ECO:0000250|UniProtKB:P28240};
DE            Short=MICA {ECO:0000305};
DE            EC=4.1.3.30 {ECO:0000250|UniProtKB:P28240};
DE   AltName: Full=Threo-D(S)-isocitrate glyoxylate-lyase {ECO:0000305};
GN   Name=ICL1 {ECO:0000303|PubMed:2361956};
OS   Candida tropicalis (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2361956; DOI=10.1093/oxfordjournals.jbchem.a123036;
RA   Atomi H., Ueda M., Hikida M., Hishida T., Teranishi Y., Tanaka A.;
RT   "Peroxisomal isocitrate lyase of the n-alkane-assimilating yeast Candida
RT   tropicalis: gene analysis and characterization.";
RL   J. Biochem. 107:262-266(1990).
CC   -!- FUNCTION: Catalyzes the formation of succinate and glyoxylate from
CC       isocitrate, a key step of the glyoxylate cycle, which operates as an
CC       anaplerotic route for replenishing the tricarboxylic acid cycle.
CC       Required for growth on ethanol or acetate, but dispensable when
CC       fermentable carbon sources are available. Acts also on 2-
CC       methylisocitrate. {ECO:0000250|UniProtKB:P28240}.
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:0000250|UniProtKB:P28240};
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:0000250|UniProtKB:P28240};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P9WKK7};
CC   -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC       isocitrate: step 1/2.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P28240}.
CC   -!- SUBCELLULAR LOCATION: Glyoxysome {ECO:0000250|UniProtKB:P28299}.
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC       Isocitrate lyase family. {ECO:0000305}.
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DR   EMBL; D00703; BAA00611.1; -; Genomic_DNA.
DR   PIR; JX0105; WZCKI.
DR   AlphaFoldDB; P20014; -.
DR   SMR; P20014; -.
DR   VEuPathDB; FungiDB:CTMYA2_028160; -.
DR   VEuPathDB; FungiDB:CTRG_04702; -.
DR   UniPathway; UPA00703; UER00719.
DR   GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
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:0046421; F:methylisocitrate lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
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: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   3: Inferred from homology;
KW   Glyoxylate bypass; Glyoxysome; Lyase; Magnesium; Metal-binding; Peroxisome;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..550
FT                   /note="Isocitrate lyase"
FT                   /id="PRO_0000068786"
FT   MOTIF           548..550
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        210
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         101..103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         172
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         211..212
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         247
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         430..434
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         464
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
SQ   SEQUENCE   550 AA;  61577 MW;  BA86F18169B5AC0C CRC64;
     MAYTKIDINQ EEADFQKEVA EIKKWWSEPR WRKTKRIYSA EDIAKKRGTL KIAYPSSQQS
     DKLFKLLEKH DAEKSVSFTF GALDPIHVAQ MAKYLDSIYV SGWQCSSTAS TSNEPSPDLA
     DYPMDTVPNK VEHLWFAQLF HDRKQREERL NMTKEERANT PYIDFLRPII ADADTGHGGI
     TAIIKLTKLF IERGAAGIHI EDQAPGTKKC GHMAGKVLVP VQEHINRLVA IRASADIFGS
     NLLAVARTDS EAATLITSTI DHRDHYFIIG ATNPESGDLA ALMAEAEAKG IYGDELARIE
     TEWTKKAGLK LFHEAVIDEI KAGNYSNKEA LIKKFTDKVN PLSHTSHKEA KKLAKELTGK
     DIYFNWDVAR AREGYYRYQG GTQCAVMRGR AFAPYADLIW MESALPDYNQ AKEFADGVKA
     AVPDQWLAYN LSPSFNWNKA MPADEQETYI KRLGQLGYVW QFITLAGLHT TALAVDDFAN
     QYSQIGMRAY GQTVQQPEIE KGVEVVKHQK WSGANYIDGL LRMVSGGVTS TAAMGAGVTE
     DQFKETKAKV
//