ACEA_CANAX
ID ACEA_CANAX Reviewed; 550 AA.
AC Q9P8Q7;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Isocitrate lyase {ECO:0000303|PubMed:12702281};
DE Short=ICL {ECO:0000305};
DE Short=Isocitrase {ECO:0000305};
DE Short=Isocitratase {ECO:0000305};
DE EC=4.1.3.1 {ECO:0000250|UniProtKB:P28240};
DE AltName: Full=Methylisocitrate lyase {ECO:0000250|UniProtKB:P28240};
DE Short=MICA {ECO:0000305};
DE EC=4.1.3.30 {ECO:0000250|UniProtKB:P28240};
DE AltName: Full=Threo-D(S)-isocitrate glyoxylate-lyase {ECO:0000305};
GN Name=ICL1 {ECO:0000303|PubMed:12702281};
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12702281; DOI=10.1111/j.1567-1364.2002.tb00100.x;
RA Eschrich D., Koetter P., Entian K.-D.;
RT "Gluconeogenesis in Candida albicans.";
RL FEMS Yeast Res. 2:315-325(2002).
CC -!- FUNCTION: Catalyzes the formation of succinate and glyoxylate from
CC isocitrate, a key step of the glyoxylate cycle, which operates as an
CC anaplerotic route for replenishing the tricarboxylic acid cycle.
CC Required for growth on ethanol or acetate, but dispensable when
CC fermentable carbon sources are available. Acts also on 2-
CC methylisocitrate. {ECO:0000250|UniProtKB:P28240}.
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:P28240};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate +
CC succinate; Xref=Rhea:RHEA:16809, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:57429; EC=4.1.3.30;
CC Evidence={ECO:0000250|UniProtKB:P28240};
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:P28240}.
CC -!- SUBCELLULAR LOCATION: Glyoxysome {ECO:0000250|UniProtKB:P28299}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Isocitrate lyase family. {ECO:0000305}.
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DR EMBL; AF222905; AAF34690.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9P8Q7; -.
DR SMR; Q9P8Q7; -.
DR BindingDB; Q9P8Q7; -.
DR ChEMBL; CHEMBL5359; -.
DR PRIDE; Q9P8Q7; -.
DR VEuPathDB; FungiDB:C1_04500W_A; -.
DR VEuPathDB; FungiDB:CAWG_00944; -.
DR BRENDA; 4.1.3.1; 1096.
DR UniPathway; UPA00703; UER00719.
DR PHI-base; PHI:6192; -.
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:0046421; F:methylisocitrate lyase activity; IEA:UniProtKB-EC.
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 3: Inferred from homology;
KW Glyoxylate bypass; Glyoxysome; Lyase; Magnesium; Metal-binding; Peroxisome;
KW Tricarboxylic acid cycle.
FT CHAIN 1..550
FT /note="Isocitrate lyase"
FT /id="PRO_0000068784"
FT MOTIF 548..550
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 210
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 101..103
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 211..212
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 430..434
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 464
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
SQ SEQUENCE 550 AA; 61395 MW; FFBDB59FB60BE337 CRC64;
MPYTPIDIQK EEADFQKEVA EIKKWWSEPR WRKTKRIYSA EDIAKKRGTL KINHPSSQQA
DKLFKLLETH DADKTVSFTF GALDPIHVAQ MAKYLDSIYV SGWQCSSTAS TSNEPSPDLA
DYPMDTVPNK VEHLWFAQLF HDRKQREERL TLSKEERAKT PYIDFLRPII ADADTGHGGI
TAIIKLTKMF IERGAAGIHI EDQAPGTKKC GHMAGKVLVP VQEHINRLVA IRASADIFGS
NLLAVARTDS EAATLITSTI DHRDHYFIIG ATNPEAGDLA ALMAEAESKG IYGNELAAIE
SEWTKKAGLK LFHEAVIDEI KNGNYSNKDA LIKKFTDKVN PLSHTSHKEA KKLAKELTGK
DIYFNWDVAR AREGYYRYQG GTQCAVMRGR AFAPYADLIW MESALPDYAQ AKEFADGVKA
AVPDQWLAYN LSPSFNWNKA MPADEQETYI KRLGKLGYVW QFITLAGLHT TALAVDDFSN
QYSQIGMKAY GQTVQQPEIE KGVEVVKHQK WSGATYIDGL LKMVSGGVTS TAAMGQGVTE
DQFKESKAKA
