ACEA_CANTR
ID ACEA_CANTR Reviewed; 550 AA.
AC P20014;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Isocitrate lyase {ECO:0000303|PubMed:2361956};
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:2361956};
OS Candida tropicalis (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5482;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2361956; DOI=10.1093/oxfordjournals.jbchem.a123036;
RA Atomi H., Ueda M., Hikida M., Hishida T., Teranishi Y., Tanaka A.;
RT "Peroxisomal isocitrate lyase of the n-alkane-assimilating yeast Candida
RT tropicalis: gene analysis and characterization.";
RL J. Biochem. 107:262-266(1990).
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; D00703; BAA00611.1; -; Genomic_DNA.
DR PIR; JX0105; WZCKI.
DR AlphaFoldDB; P20014; -.
DR SMR; P20014; -.
DR PRIDE; P20014; -.
DR VEuPathDB; FungiDB:CTMYA2_028160; -.
DR VEuPathDB; FungiDB:CTRG_04702; -.
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: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_0000068786"
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; 61577 MW; BA86F18169B5AC0C CRC64;
MAYTKIDINQ EEADFQKEVA EIKKWWSEPR WRKTKRIYSA EDIAKKRGTL KIAYPSSQQS
DKLFKLLEKH DAEKSVSFTF GALDPIHVAQ MAKYLDSIYV SGWQCSSTAS TSNEPSPDLA
DYPMDTVPNK VEHLWFAQLF HDRKQREERL NMTKEERANT PYIDFLRPII ADADTGHGGI
TAIIKLTKLF IERGAAGIHI EDQAPGTKKC GHMAGKVLVP VQEHINRLVA IRASADIFGS
NLLAVARTDS EAATLITSTI DHRDHYFIIG ATNPESGDLA ALMAEAEAKG IYGDELARIE
TEWTKKAGLK LFHEAVIDEI KAGNYSNKEA LIKKFTDKVN PLSHTSHKEA KKLAKELTGK
DIYFNWDVAR AREGYYRYQG GTQCAVMRGR AFAPYADLIW MESALPDYNQ AKEFADGVKA
AVPDQWLAYN LSPSFNWNKA MPADEQETYI KRLGQLGYVW QFITLAGLHT TALAVDDFAN
QYSQIGMRAY GQTVQQPEIE KGVEVVKHQK WSGANYIDGL LRMVSGGVTS TAAMGAGVTE
DQFKETKAKV
