ID   ACEA_SOLLC              Reviewed;         575 AA.
AC   P49297;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 123.
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   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. UC82B; TISSUE=Leaf;
RX   PubMed=7630969; DOI=10.1104/pp.108.3.1339;
RA   Janssen B.-J.;
RT   "A cDNA clone for isocitrate lyase from tomato.";
RL   Plant Physiol. 108:1339-1339(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; U18678; AAA82738.1; -; mRNA.
DR   PIR; T06353; T06353.
DR   AlphaFoldDB; P49297; -.
DR   SMR; P49297; -.
DR   STRING; 4081.Solyc07g052480.2.1; -.
DR   PaxDb; P49297; -.
DR   PRIDE; P49297; -.
DR   eggNOG; KOG1260; Eukaryota.
DR   UniPathway; UPA00703; UER00719.
DR   Proteomes; UP000004994; Unplaced.
DR   GO; GO:0009514; C:glyoxysome; IBA:GO_Central.
DR   GO; GO:0004451; F:isocitrate lyase activity; IBA:GO_Central.
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..575
FT                   /note="Isocitrate lyase"
FT                   /id="PRO_0000068808"
FT   MOTIF           573..575
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   575 AA;  64720 MW;  F398FA96C7110B4E CRC64;
     MAASYSVPSM IMEEERRFEA EVAEVQAWWN TERFRLTKRA YSARDVVALR GTMRQSYASN
     ELAQKLWRTL KTHQANGTAS RTFGALDPVQ VTMMAKHLDT IYVSGWQCSS THTSTNEPGP
     DLADYPYDTV PNKVEHLFFA QQYHDRKQRE ARMSMCREER ARTPFIDYLK PIIADGDTGF
     GGATATVKLC KLFVERGAAG VHIEDQSSVT KKCGHMAGKV LVAVSEHINR LVAARLQFDV
     MGTETVLVAR TDAVAATLIQ TNVDTRDHQF ILGASNPNLK GKGLATHLSE AMAAGKTGPE
     LQAIEDNWLG MAELKTFSQC VTDAIKKMNL AEYEKQRKLN EWMNHSSYEK CLSHEQAREV
     AERLGLPNLF WDWDLPRTRE GFYRFQGSVE AAIVRGWAFA EYCDLVWMET SSPDMVECTK
     FSQGVKTLRP ELMLAYNLSP SFNWDASGMN DNQMMDFIPR IAKLGYCWQF ITLAGFHADA
     LIVDTFAKDF ARRGMLAYVE KIQREERSNG VDTLAHQKWS GANYYDRVLR TVQGGITSTA
     AMGKGVTEEQ FEEKWTRTGA TNLGDGSVVI AKARM