ID   ACEA_CYBJA              Reviewed;         550 AA.
AC   Q9HFN2;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   13-SEP-2023, entry version 79.
DE   RecName: Full=Isocitrate lyase {ECO:0000250|UniProtKB:P28240};
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:0000250|UniProtKB:P28240};
GN   Synonyms=ICL {ECO:0000303|Ref.1};
OS   Cyberlindnera jadinii (Torula yeast) (Pichia jadinii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX   NCBI_TaxID=4903;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 9256 / CBS 841 / DSM 70167 / JCM 2311 / NBRC 0626 / NRRL
RC   Y-1084 / VKM Y-768;
RA   Menendez J.D.D.J., Rivero D., Valdes I.;
RT   "The ICL gene from Camdida utilis.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
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; AJ404885; CAC08487.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9HFN2; -.
DR   SMR; Q9HFN2; -.
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_0000068796"
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;  62394 MW;  495D6179D8D1629C CRC64;
     MPYTPIDIKA EQEAFEREVA AVEQWWKEPR WRKTTRIYTA KDIVQKRGTL QIHYPSSDQA
     KKLYKLLEEH DRNKTASFTF GALDPIHVTQ MAKYLDTVYI SGWQSSSTAS TSNEPSPDLA
     DYPYDTVPNK CEHLWFAQLF HDRKQHEERF RMTPEERAKT PYTDFLRPII ADADTGHGGI
     TAIIKLTKLF IERGAAGIHI EDQAPGTKKC GHMAGKVLVP IQEHINRLVA IRTAADIFGS
     DLLCVARTDS EAATLLTSTI DHRDHYFIIG STNKDLQPLS EVMFQAEQRG LLKVMLAAVE
     EDWTKKAGLK LFHEAVIDEI NSGYYPNKQA LIAEFTTKVH PLSNTSNKEA RALAKKLTGK
     DIFFDWEAPR VREGYYRYQG GTQCAVNRAR AYAPYADIIW MESKLPDYAQ AKEFADGVKA
     QWPEQWLSYN LSPSFNWNKA MSVLYQETYI QKLAKLGYVW QFITLAGLHT TALAVDNFAR
     DYAKIGMRAY GQQIQAPEIE NGVEVVKHQK WSGAEYIDNL LKLVTGGVTS TAAMGKGVTE
     DQFKDDKSKL
//