ACEA2_SOYBN
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 03-AUG-2022, entry version 114.
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 STRING; 3847.GLYMA12G10780.1; -.
DR PRIDE; P45457; -.
DR eggNOG; KOG1260; Eukaryota.
DR InParanoid; P45457; -.
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; 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..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
