ID   ACEA_YARLI              Reviewed;         540 AA.
AC   P41555; Q6CBN9;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 3.
DT   04-NOV-2026, entry version 141.
DE   RecName: Full=Isocitrate lyase {ECO:0000303|PubMed:8246896};
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:8246896};
GN   OrderedLocusNames=YALI0C16885g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Dipodascomycetes;
OC   Dipodascales; Dipodascales incertae sedis; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC   STRAIN=B204-12C;
RX   PubMed=8246896; DOI=10.1007/bf00284696;
RA   Barth G., Scheuber T.;
RT   "Cloning of the isocitrate lyase gene (ICL1) from Yarrowia lipolytica and
RT   characterization of the deduced protein.";
RL   Mol. Gen. Genet. 241:422-430(1993).
RN   [2]
RP   SEQUENCE REVISION.
RA   Juretzek T.;
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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. Also acts 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   -!- DISRUPTION PHENOTYPE: Inhibits the utilization of acetate, ethanol, and
CC       fatty acids, but also reduces the growth rate on glucose.
CC       {ECO:0000269|PubMed:8246896}.
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC       Isocitrate lyase family. {ECO:0000305}.
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DR   EMBL; X72848; CAA51362.1; -; Genomic_DNA.
DR   EMBL; CR382129; CAG82243.1; -; Genomic_DNA.
DR   AlphaFoldDB; P41555; -.
DR   SMR; P41555; -.
DR   FunCoup; P41555; 185.
DR   STRING; 284591.P41555; -.
DR   EnsemblFungi; CAG82243; CAG82243; YALI0_C16885g.
DR   VEuPathDB; FungiDB:YALI0_C16885g; -.
DR   HOGENOM; CLU_019214_2_2_1; -.
DR   InParanoid; P41555; -.
DR   OMA; AACVHFE; -.
DR   OrthoDB; 73716at4891; -.
DR   UniPathway; UPA00703; UER00719.
DR   Proteomes; UP000001300; Chromosome C.
DR   GO; GO:0009514; C:glyoxysome; ISS:UniProtKB.
DR   GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR   GO; GO:0004451; F:isocitrate lyase activity; ISS:UniProtKB.
DR   GO; GO:0046421; F:methylisocitrate lyase activity; ISS:UniProtKB.
DR   GO; GO:0006097; P:glyoxylate cycle; IBA:GO_Central.
DR   FunFam; 1.10.10.850:FF:000001; Isocitrate lyase; 1.
DR   Gene3D; 1.10.10.850; -; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
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   3: Inferred from homology;
KW   Glyoxylate bypass; Glyoxysome; Lyase; Magnesium; Metal-binding; Peroxisome;
KW   Reference proteome.
FT   CHAIN           1..540
FT                   /note="Isocitrate lyase"
FT                   /id="PRO_0000068798"
FT   MOTIF           538..540
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        203
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         93..95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         165
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         204..205
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         240
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         423..427
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         457
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   CONFLICT        73..74
FT                   /note="GA -> AS (in Ref. 1; CAA51362)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        97
FT                   /note="S -> C (in Ref. 1; CAA51362)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        107
FT                   /note="P -> S (in Ref. 1; CAA51362)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        112..113
FT                   /note="AD -> GG (in Ref. 1; CAA51362)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        134
FT                   /note="D -> E (in Ref. 1; CAA51362)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        149..155
FT                   /note="RSKLPAP -> PIQAPRAR (in Ref. 1; CAA51362)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        167
FT                   /note="D -> E (in Ref. 1; CAA51362)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        232..234
FT                   /note="GSD -> ALN (in Ref. 1; CAA51362)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        281..288
FT                   /note="LEGKQGAA -> ARGQAGAP (in Ref. 1; CAA51362)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        315
FT                   /note="A -> D (in Ref. 1; CAA51362)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        340..345
FT                   /note="ALEARA -> DIEDRY (in Ref. 1; CAA51362)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        383..384
FT                   /note="IA -> YS (in Ref. 1; CAA51362)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        471..472
FT                   /note="FA -> SC (in Ref. 1; CAA51362)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   540 AA;  60049 MW;  340B608321946098 CRC64;
     MSEQQRFNNE VEEIKKWWSS PRWKHTKRVY SPEDIASRRG TIKVPQASSQ QADKLFKLLQ
     EHEKNHTASF TYGALDPVQV TQMAKYLDSI YVSGWQSSST ASTSNEPSPD LADYPMDTVP
     NKVEHLWFAQ LFHDRKQNEE RLSLPESERS KLPAPVDYLR PIIADADTGH GGLTAVVKLT
     KMFIERGAAG IHIEDQAPGT KKCGHMAGKV LVPIQEHINR LIAIRASADI FGSDLLAIAR
     TDSEAATLIT SSIDYRDHYF IAGATNKDAG HLVDVMVAAE LEGKQGAALQ AVEDEWNRKA
     GVKLFHEAFA DEVNAGSYSN KAELIAEFNK KVTPLSNTPA LEARALAARL LGKDIYFNWE
     AARVREGYYR YQGGTQCAVN RGIAYAPYAD LIWMESKLPD YAQAKEFAEG VKNAVPHQWL
     AYNLSPSFNW TTAMSPEDQE TYISRLAKLG YVWQFITLAG LHTNALISDK FAKAYSERGM
     KAYGGEIQQP EIDQGCEVVK HQKWSGAEYI DGILRMVTGG ITSTAAMGAG VTEDQFKSKL
//