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 08-NOV-2023, entry version 121. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PaxDb; 3635-P17069; -. DR GeneID; 107920350; -. DR KEGG; ghi:107920350; -. DR OrthoDB; 983054at2759; -. 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; 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..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 //