ID   ACEA_GOSHI              Reviewed;         576 AA.
AC   P17069;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 117.
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   Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=3635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Deltapine 62; TISSUE=Cotyledon;
RX   PubMed=2194576; DOI=10.1016/0167-4781(90)90045-4;
RA   Turley R.B., Choe S.M., Trelease R.N.;
RT   "Characterization of a cDNA clone encoding the complete amino acid sequence
RT   of cotton isocitrate lyase.";
RL   Biochim. Biophys. Acta 1049:223-226(1990).
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; X52136; CAA36381.1; -; mRNA.
DR   PIR; S10771; WZCNIU.
DR   RefSeq; NP_001314103.1; NM_001327174.1.
DR   AlphaFoldDB; P17069; -.
DR   SMR; P17069; -.
DR   STRING; 3635.P17069; -.
DR   GeneID; 107920350; -.
DR   KEGG; ghi:107920350; -.
DR   BRENDA; 4.1.3.1; 2499.
DR   UniPathway; UPA00703; UER00719.
DR   Proteomes; UP000189702; Genome assembly.
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..576
FT                   /note="Isocitrate lyase"
FT                   /id="PRO_0000068806"
FT   MOTIF           574..576
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   576 AA;  64733 MW;  84D211AA3DCE8700 CRC64;
     MAASFSVPSM IMEEEGRFET EVAEVQAWWN SERFKLTRRP YSARDVVALR GSLKQSYGSN
     EMAKKLWTTL KTHQANGTAS RTFGALDPVQ VTMMAKHLDS IYVSGWQCSS THTTTNEPGP
     DLADYPYDTV PNKVEHLFFA QQYHDRKQRE ARMSMSREER ARTPYVDYLK PIIADGDTGF
     GGTTATVKLC KLFVERGAAG VHIEDQSSVT KKCGHMAGKV LVAVSEHINR LVAARLQFDV
     MGVETVLVAR TDAVAATLIQ TNVDTRDHQF ILGATNPNLR GKSLANMLAE GMAAGKNGPQ
     LQAIEDNWLA IAQLKTFSEC VMDAIKSMNI TEDEKRRRMN EWMNHSSYDK CLSNEQAREI
     AERLGLQNLF WDWDLPRTRE GFYRFRGSVM AAIVRGWAFA PHADLIWMET SSPDMVECTR
     FAEGVKSMHP EIMLAYNLSP SFNWDASGMT DEHMRDFIPR IAKLGFCWQF ITLAGFHADA
     LVTDTFARDF ARRGMLAYVE KIQREERNNG VDTLAHQKWS GANFYDRYLK TVQGGISSTA
     AMGKGVTEEQ FKETWTRPGA GNIGSEGNLV VAKARM