ID Q9FQD2_IPOBA Unreviewed; 575 AA.
AC Q9FQD2;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 24-JAN-2024, entry version 84.
DE RecName: Full=Isocitrate lyase {ECO:0000256|ARBA:ARBA00012909, ECO:0000256|PIRNR:PIRNR001362};
GN Name=ICL {ECO:0000313|EMBL:AAG44479.1};
OS Ipomoea batatas (Sweet potato) (Convolvulus batatas).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
OX NCBI_TaxID=4120 {ECO:0000313|EMBL:AAG44479.1};
RN [1] {ECO:0000313|EMBL:AAG44479.1}
RP NUCLEOTIDE SEQUENCE.
RA Chen H.-J., Hou W.-C., Lin Y.-H.;
RT "Isolation of an isocitrate lyase cDNA clone from senescent leaves of sweet
RT potato (Ipomoea batatas cv. Tainong 57).";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in storage lipid mobilization during the growth of
CC higher plant seedling. {ECO:0000256|ARBA:ARBA00003575}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR001362-3};
CC Note=Can also use Mn(2+) ion. {ECO:0000256|PIRSR:PIRSR001362-3};
CC -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC isocitrate: step 1/2. {ECO:0000256|ARBA:ARBA00004793}.
CC -!- SUBCELLULAR LOCATION: Glyoxysome {ECO:0000256|ARBA:ARBA00004130}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Isocitrate lyase family. {ECO:0000256|PIRNR:PIRNR001362}.
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DR EMBL; AF243525; AAG44479.1; -; mRNA.
DR AlphaFoldDB; Q9FQD2; -.
DR UniPathway; UPA00703; UER00719.
DR GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0004451; F:isocitrate lyase activity; IEA:InterPro.
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; 2.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE 2: Evidence at transcript level;
KW Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435};
KW Glyoxysome {ECO:0000256|ARBA:ARBA00022453};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001362};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT ACT_SITE 213
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 104..106
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 175
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT BINDING 214..215
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 437..441
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 472
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ SEQUENCE 575 AA; 64429 MW; 23DF26719E038662 CRC64;
MASPFTAPSM IMEEERRFEA EVGEVQAWWN SERFKLTRRP YTARGVVALR GHLRQGYGSN
EMAKKLWRTL KNHQANGTAS RTFGALDPVQ VTMMAKHLDT IYVSGWQCSS THTTSNEPGP
DLADYPYDTV PNKCQHLFFA QQYHDRKQRE ARMNMSREER ARTPFIDYLK PIIADGDTGF
GGTTATVKLC KLFVERGAAG VHIEDQSSVT KKCGHMAGKV LVAVSEHINR LVAARLQFDI
MGTETVLVAR TDAVAATLIQ TNVDTRDHQF ILGVTNPNLK GKGLATILSE AMAAGKTGLE
LQAIEDNWIA MAELKTFSET VVDAINRLNI GEPEKQRRLN EWMKHSSYEK CLSNFQAREI
AENLGLNNLF WDWDLPRTRE GFYRFKGSVM AAIVRGWAFA PHSDLIWMET SSPDLVECTK
FAQGVKSVHP EMMLAYNLSP SFNWDASGMN DNQMMDFIPG IAKLGYCWQF ITLAGFHGNA
LIIDTFAKDF ASRGMLAYVE KIQREERNNG VDTLAHQKWS GANYYDRVLR TVQGGITSTA
AMGKGVTEEQ FQESWTRPGT TNMGDGGVVI AKARM
//
