ID   ACEA_CUCMA              Reviewed;         576 AA.
AC   P93110;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 106.
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   Cucurbita maxima (Pumpkin) (Winter squash).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Cucurbiteae; Cucurbita.
OX   NCBI_TaxID=3661;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Cotyledon;
RX   PubMed=8979395; DOI=10.1093/oxfordjournals.pcp.a029043;
RA   Mano S., Hayashi M., Kondo M., Nishimura M.;
RT   "cDNA cloning and expression of a gene for isocitrate lyase in pumpkin
RT   cotyledons.";
RL   Plant Cell Physiol. 37:941-948(1996).
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}.
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DR   EMBL; D78256; BAA11320.1; -; mRNA.
DR   AlphaFoldDB; P93110; -.
DR   SMR; P93110; -.
DR   PRIDE; P93110; -.
DR   OrthoDB; 905115at2759; -.
DR   UniPathway; UPA00703; UER00719.
DR   Proteomes; UP000504608; Unplaced.
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; 3.20.20.60; -; 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   PANTHER; PTHR21631; PTHR21631; 1.
DR   Pfam; PF00463; ICL; 1.
DR   PIRSF; PIRSF001362; Isocit_lyase; 1.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   TIGRFAMs; TIGR01346; isocit_lyase; 1.
DR   PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE   2: Evidence at transcript level;
KW   Glyoxylate bypass; Glyoxysome; Lyase; Magnesium; Metal-binding; Peroxisome;
KW   Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN           1..576
FT                   /note="Isocitrate lyase"
FT                   /id="PRO_0000068803"
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;  64359 MW;  269D93D4F13B5990 CRC64;
     MATSFSVPSM IMEEEGRFEA EVAEVQAWWN SERFKLTRRP YTAKDVVSLR GSLRQSYASN
     DLAKKLWRTL KTHQANSTAS RTFGALDPVQ VTMMAKHLDS IYVSGWQCSS THTSTNEPGP
     DLADYPYDTV PNKVEHLFFA QQYHDRKQRE ARMSMSREER AKTPYVDYLK PIIADGDTGF
     GGTTATVKLC KLFVERGAAG VHIEDQSSVT KKCGHMAGKV LVAVSEHINR LVAARLQFDV
     MGVETVLVAR TDAVAATLIQ TNVDSRDHQF ILGATNPNLR GKSLAGVLAE AMAAGKTGAE
     LQALEDQWIS MAQLKTFSEC VTDAIMNSNG TESEKRRKLD EWMNHSSYEK CISNEQGREI
     AEKLGLKNLF WDWDLPRTRE GFYRFKGSVM AAIVRGWAFA PHADLIWMET SSPDLVECTT
     FAKGVKSVHP EIMLAYNLSP SFNWDASGMS DKQMEEFIPT IARLGFCWQF ITLAGFHADA
     LVIDTFARDY ARRGMLAYVE RIQREERNNG VDTLAHQKWS GANYYDRYLK TVQGGISSTA
     AMGKGVTEEQ FKESWTRAGA GNLGEEGSVV VAKSRM