ID   ACEA_DENCR              Reviewed;         574 AA.
AC   Q9SE26;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 98.
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};
GN   Name=ICL;
OS   Dendrobium crumenatum (Tropical pigeon orchid).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC   Epidendroideae; Malaxideae; Dendrobiinae; Dendrobium.
OX   NCBI_TaxID=51096;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Vellupillai M., Goh C.-J., Swarup S.;
RT   "Sequence analysis of DcrIcl, an isocitrate lyase gene from the tropical
RT   orchid, Dendrobium crumenatum.";
RL   (er) Plant Gene Register PGR99-178(1999).
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   -!- DEVELOPMENTAL STAGE: Expressed maximally during postgerminative growth.
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC       Isocitrate lyase family. {ECO:0000305}.
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DR   EMBL; AF193815; AAF04598.1; -; mRNA.
DR   AlphaFoldDB; Q9SE26; -.
DR   SMR; Q9SE26; -.
DR   PRIDE; Q9SE26; -.
DR   UniPathway; UPA00703; UER00719.
DR   GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004451; F:isocitrate lyase activity; IEA:UniProtKB-EC.
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   Tricarboxylic acid cycle.
FT   CHAIN           1..574
FT                   /note="Isocitrate lyase"
FT                   /id="PRO_0000068805"
FT   REGION          549..574
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           572..574
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        212
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         103..105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         174
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         213..214
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         436..440
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         471
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
SQ   SEQUENCE   574 AA;  63993 MW;  0B568ADE3248DE2E CRC64;
     MASSSVPPMI TEEEARFEAE VSAVESWWRT DRFRLTRRPY SARDVVSLRG TLHHSYASDQ
     MAKKLWRTLK SHQSAGTASR TFGALDPVQV TMMAKHLDTI YVSGWQCSST HTATNEPGPD
     LADYPYNTVP NKVEHLFFAQ LYHDRKQHEA RVSMTREQRA KTPYVDYLRP IIADGDTGFG
     GATATVKLCK LFVERGAAGV HIEDQSSVTK KCGHMAGKVL VAVSEHINRL VAARLQFDVM
     GVETVLVART DAVAATLIQS NVDLRDHQFI LGATNPDFKR RSLAAVLSAA MAAGKTGAVL
     QAIEDDWLSR AGLMTFSDAV INGINRQNLP EYEKQRRLNE WAAATEYSKC VSNEQGREIA
     ERLGAGEIFW DWDIARTREG FYRFRGSVEA AVVRGRAFAP HADLIWMETS SPDLVECGKF
     AQGMKASHPE IMLAYNLSPS FNWDAAGMTD EEMRDFIPRI AKMGFCWQFI TLGGFHADAL
     VTDTFAREFA KQGMLAYVER IQREERNNGV DTLAHQKWSG ANYYDRYLKT VQGGISSTAA
     MGKGVTEEQF KEESRTGTRG LDRGGITVNA KSRL