ACEA1_SOYBN
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 03-AUG-2022, entry version 113.
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.GLYMA06G45950.1; -.
DR PRIDE; P45456; -.
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; 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..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
