ID   ACEA_CUCSA              Reviewed;         576 AA.
AC   P49296;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   24-JAN-2024, entry version 111.
DE   RecName: Full=Isocitrate lyase {ECO:0000250|UniProtKB:P28297};
DE            Short=ICL {ECO:0000250|UniProtKB:P28297};
DE            EC=4.1.3.1 {ECO:0000250|UniProtKB:P28297};
DE   AltName: Full=Isocitrase {ECO:0000250|UniProtKB:P28297};
DE   AltName: Full=Isocitratsysase {ECO:0000250|UniProtKB:P28297};
OS   Cucumis sativus (Cucumber).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Masterpiece; TISSUE=Leaf;
RX   PubMed=7894014; DOI=10.1007/bf00019316;
RA   Reynolds S.J., Smith S.M.;
RT   "The isocitrate lyase gene of cucumber: isolation, characterisation and
RT   expression in cotyledons following seed germination.";
RL   Plant Mol. Biol. 27:487-497(1995).
CC   -!- FUNCTION: Involved in storage lipid mobilization during the growth of
CC       higher plant seedling. {ECO:0000250|UniProtKB:P28297}.
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:P28297};
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. {ECO:0000250|UniProtKB:P28297}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P28297}.
CC   -!- SUBCELLULAR LOCATION: Glyoxysome {ECO:0000250|UniProtKB:P28297}.
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC       Isocitrate lyase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z35499; CAA84632.1; -; Genomic_DNA.
DR   PIR; S53505; S53505.
DR   AlphaFoldDB; P49296; -.
DR   SMR; P49296; -.
DR   eggNOG; KOG1260; Eukaryota.
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: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..576
FT                   /note="Isocitrate lyase"
FT                   /id="PRO_0000068804"
FT   MOTIF           574..576
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        213
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         104..106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         175
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         214..215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         437..441
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         472
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
SQ   SEQUENCE   576 AA;  64611 MW;  717D30B83CD81D6C CRC64;
     MAASFSVPSM IMEEEGRFEA EVAEVQAWWN SERFKLTRRP YTAKDVVSLR GSLRQSYASN
     DLAKKLWRTL KTHQANGTAS RTFGALDPVQ VTMMAKHLDT IYVSGWQCSS THTSTNEPGP
     DLADYPYDTV PNKVEHLFFA QQYHDRKQRE ARMSMSREER AKTPYIDYLK PIIADGDTGF
     GGTTATVKLC KLFVERGAAG VHIEDQSSVT KKCGHMAGKV LVAVSEHINR LVAARLQFDV
     MGVETILVAR TDAVAATLIQ TNVDKRDHQF ILGATNPNLR GKSLAGALAE AMAAGKTGAE
     LQALEDQWIS MAQLKTFSEC VTDAIMNTNA TENEKRRKLD EWMNHSSYEK CISNEQGREI
     AEKLGLKNLF WDWDLPRTRE GFYRFKGSVM AAIVRGWAFA PHADLIWMET SSPDLVECTT
     FAKGMKSIHP ETMLAYNLSP SFNWDASGMS DKQMEEFIPR IARLGFCWQF ITLAGFHADA
     LVVDTFARDY ARRGMLAYVE RIQREERNNG VDTLAHQKWS GANYYDRYLK TVQGGISSTA
     AMGKGVTEEQ FKESWTREGA VNLGEEGNVV VAKSRM
//