ID   ACEA2_SOYBN             Reviewed;         557 AA.
AC   P45457;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   04-NOV-2026, entry version 127.
DE   RecName: Full=Isocitrate lyase 2 {ECO:0000250|UniProtKB:P28297};
DE            Short=ICL 2 {ECO:0000250|UniProtKB:P28297};
DE            EC=4.1.3.1 {ECO:0000250|UniProtKB:P28297};
DE   AltName: Full=Isocitrase 2 {ECO:0000250|UniProtKB:P28297};
DE   AltName: Full=Isocitratsysase 2 {ECO:0000250|UniProtKB:P28297};
DE   Flags: Fragment;
GN   Name=ICL2;
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Maple Arrow; TISSUE=Cotyledon;
RA   Guex N., Henry H., Widmer F.;
RL   Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
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; L02330; AAA33977.1; -; mRNA.
DR   PIR; T07632; T07632.
DR   AlphaFoldDB; P45457; -.
DR   SMR; P45457; -.
DR   FunCoup; P45457; 471.
DR   STRING; 3847.P45457; -.
DR   PaxDb; 3847-P45457; -.
DR   eggNOG; KOG1260; Eukaryota.
DR   InParanoid; P45457; -.
DR   OMA; AACVHFE; -.
DR   UniPathway; UPA00703; UER00719.
DR   Proteomes; UP000008827; Unplaced.
DR   GO; GO:0009514; C:glyoxysome; ISS:UniProtKB.
DR   GO; GO:0004451; F:isocitrate lyase activity; ISS:UniProtKB.
DR   GO; GO:0006097; P:glyoxylate cycle; IBA:GO_Central.
DR   CDD; cd00377; ICL_PEPM; 1.
DR   FunFam; 1.10.10.850:FF:000001; Isocitrate lyase; 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   2: Evidence at transcript level;
KW   Glyoxylate bypass; Glyoxysome; Lyase; Magnesium; Metal-binding; Peroxisome;
KW   Reference proteome.
FT   CHAIN           <1..557
FT                   /note="Isocitrate lyase 2"
FT                   /id="PRO_0000068812"
FT   MOTIF           555..557
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        195
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         86..88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         157
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         196..197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         232
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         419..423
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         454
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   NON_TER         1
SQ   SEQUENCE   557 AA;  62840 MW;  486D5CE420B7AD95 CRC64;
     EAEVAEVQAW WNSERFRLTK RPYTARDVVS LRGNLRQTYA SNEMAKKLWC LLKNHQANGT
     ASRTFGALDP VQVTQMAKHL DTIYVSGWQC SATHTTSNEP GPDLADYPYD TVPNKVEHLF
     FAQQYHDRKQ REERMRMSRE ERARTPYVDY LRPIIADGDT GFGGTTATVK LCKLFVERGA
     AGIHIEDQSS VTKKCGHMAG KVLVAISEHI NRLVAARLQF DVMGVETVLV ARTDAEAANL
     IQSNIDTRDH QFILGVTNPN LKGKSLATLM QQGMAAGKSG AELQALEDEW LSKAQLKTLS
     EAVVEAIERQ NIGEEEKRRK LNEWMHHSSY ERCLSNEEGR EIAEKLGVRN LFWDWDLPRT
     REGFYRFKGS VIASVVRGWA FSPHADVIWM ETASPNVIEC TQFSEGVRSK HPQMMLGYNL
     SPSFNWDASG MSDEQMRDFI PKIAKLGYVW QFITVGGLHS NALITSTFAR DFANRGMLAY
     VERIQREERN NGVDTLAHQK WAGANYYDRY LKTVQGGVAS TAAMGKGVTE EQFKESWTRP
     GAVEIDRGSI VVAKARM
//