ID   ACEA_TALMA              Reviewed;         540 AA.
AC   Q96WZ5;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   13-SEP-2023, entry version 83.
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};
OS   Talaromyces marneffei (Penicillium marneffei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=37727;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PM30;
RA   Haycocks N.G., McGinnis M.R., Cooper C.R. Jr.;
RT   "Nucleotide sequence of the isocitrate lyase gene from the pathogenic
RT   fungus, Penicillium marneffei.";
RL   Submitted (APR-2001) 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; AF373018; AAK54240.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q96WZ5; -.
DR   SMR; Q96WZ5; -.
DR   VEuPathDB; FungiDB:PMAA_080470; -.
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   Gene3D; 1.10.10.850; -; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
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..540
FT                   /note="Isocitrate lyase"
FT                   /id="PRO_0000068795"
FT   ACT_SITE        208
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         99..101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         170
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         209..210
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         245
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         425..429
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         459
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
SQ   SEQUENCE   540 AA;  60493 MW;  3544DC375A692E1B CRC64;
     MASTNFDLED QKYLEDVNAV KQWWTDSRWR YTKRPFTAEQ IVAKRGTLKI EYPSNTQAKK
     LWKILEERFN DKTVSYTYGC LEPTMLTQMI KYLDTIYVSG WQSSSTASST DEPSPDLADY
     PMNTVPNKVN QLFMAQLFHD RKQREERITT PREKRSSVQN YDYLRPIIAD ADTGHGGLTA
     VMKLTKLFVE RGAAGIHIED QAPGTKKCGH MAGKVLVPIS EHINRLVAIR AQADIMGTDL
     LAIARTDSEA ATLITSTIDY RDHAYLLGST NPSLQPLNDL MVAAEQSGKS GEQLQAIEDS
     WIAQAGIKKF DDAVIDTINQ GSFANKKELI NRYLTAAKGK SNSEARAIAK GITGMDIYWN
     WDAPRTRGGF YRYQGGTQCA VNRAVAYAPF ADLIWMESKL PDYKQAKEFA DGVHAVWPEQ
     KLAYNLSPSF NWKAAMSKEE QLTYIKRLGK LGYCWQFITL AGLHSTALIS DQFASAYAKQ
     GMRAYGELIQ EPEMERKVDI VTHQKWSGAN LIDHSLAMVT GGISSTAAMG KGVTEDQFKS
//