ID   ACEA1_SOYBN             Reviewed;         558 AA.
AC   P45456;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   24-JAN-2024, entry version 119.
DE   RecName: Full=Isocitrate lyase 1 {ECO:0000250|UniProtKB:P28297};
DE            Short=ICL 1 {ECO:0000250|UniProtKB:P28297};
DE            EC=4.1.3.1 {ECO:0000250|UniProtKB:P28297};
DE   AltName: Full=Isocitrase 1 {ECO:0000250|UniProtKB:P28297};
DE   AltName: Full=Isocitratsysase 1 {ECO:0000250|UniProtKB:P28297};
DE   Flags: Fragment;
GN   Name=ICL1;
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.
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; L02329; AAA33976.1; -; mRNA.
DR   PIR; T07631; T07631.
DR   AlphaFoldDB; P45456; -.
DR   SMR; P45456; -.
DR   STRING; 3847.P45456; -.
DR   PaxDb; 3847-GLYMA06G45950-1; -.
DR   eggNOG; KOG1260; Eukaryota.
DR   InParanoid; P45456; -.
DR   UniPathway; UPA00703; UER00719.
DR   Proteomes; UP000008827; 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; 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; Tricarboxylic acid cycle.
FT   CHAIN           <1..558
FT                   /note="Isocitrate lyase 1"
FT                   /id="PRO_0000068811"
FT   MOTIF           556..558
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         420..424
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         455
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   NON_TER         1
SQ   SEQUENCE   558 AA;  62845 MW;  99B5CA5EA24F5DDB CRC64;
     EAEVAEVQAW WNSERFRLTK RPYTARDVVS LRGNLRQTYA SNEMAKKLWR LLKNHQANGT
     ASRTFGALDP VQVTQMAKHL DTIYVSGWQC SATHTTSNEP GPDLADYPYD TVPNKVEHLF
     FAQQYHDRKQ KEERMRMSRE ERARTPYVDY LRPIIADGDT GFGGTTATVK LCKLFVERGA
     AGIHIEDQSS VTKKCGHMAG KVLVAISEHI NRLVAARLQF DVMGVETVLV ARTDAEAANL
     IQSNIDTRDH QFILGVTNPN LKGKSLATLM QQGMAAGKNG AELQALEDEW LSKAQLKTLS
     EAVVEAIERQ NNIGEEEKRR KLNEWMHHSS YERCLSNEEG REIAEKLGVR NLFWDWDLPR
     TREGFYRFKG SVTASVVRGC AFSPHADVIW METASPNVVE CTEFSEGVRS KHPQMMLGYN
     LSPSFNWDAS GMSDEQMKDF IPKIAKLGYV WQFITVGGLH SNALITSTFA RDFANRGMLA
     YVERIQREER NNGVDTLAHQ KWAGANYYDR YLKTVQGGVA STAAMGKGVT EEQFKESWTR
     SGAVNIDRGS IVVAKARM
//