ACEA_CANGA
ID ACEA_CANGA Reviewed; 553 AA.
AC Q6FPK7;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Isocitrate lyase {ECO:0000250|UniProtKB:P28240};
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:0000250|UniProtKB:P28240}; OrderedLocusNames=CAGL0J03058g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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. 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; CR380956; CAG60786.2; -; Genomic_DNA.
DR RefSeq; XP_447837.2; XM_447837.2.
DR AlphaFoldDB; Q6FPK7; -.
DR SMR; Q6FPK7; -.
DR STRING; 5478.XP_447837.2; -.
DR EnsemblFungi; CAG60786; CAG60786; CAGL0J03058g.
DR GeneID; 2889724; -.
DR KEGG; cgr:CAGL0J03058g; -.
DR CGD; CAL0133590; ICL1.
DR VEuPathDB; FungiDB:CAGL0J03058g; -.
DR eggNOG; KOG1260; Eukaryota.
DR HOGENOM; CLU_019214_2_2_1; -.
DR InParanoid; Q6FPK7; -.
DR OMA; LEKDWAE; -.
DR UniPathway; UPA00703; UER00719.
DR PHI-base; PHI:8917; -.
DR Proteomes; UP000002428; Chromosome J.
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 Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..553
FT /note="Isocitrate lyase"
FT /id="PRO_0000068785"
FT MOTIF 551..553
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 216
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 105..107
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 178
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 217..218
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 436..440
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 470
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
SQ SEQUENCE 553 AA; 62177 MW; D97EB314A3306D9C CRC64;
MPVPNSEANE FQALQARIDA DAKEIEQWWS EPRWNKTKRT YSAREIAIRR GTFPPLTYPS
SVMAKKVYKV LEKHHKEGTV SRTFGALDPV QVSQMAKFLD TIYVSGWQCS STASTSNEPG
PDLADYPMDT VPNKVEHLFK AQQFHDRKQW ENRAKATSQE ELDAMGPAID YMTPIIADAD
AGHGGLTAVF KLTKMFIERG AAGIHMEDQT STNKKCGHMA GRCVIPVQEH INRLVTIRMC
ADIMHSELVI VARTDSEAAT LISSTIDTRD HYFVVGATNP DIEPFAEYMD RAIMAGVSGD
ELQKLEAAWI EKAGLKLFHE AFADEVNKSS VSNKQEIIKK FNDKVGPLTE TSHREAKKLA
KELLGKDIFF DWDLPRVREG LYRYRGGTQC SVMRARAFAP YADLVWMESN YPDFEQAREF
AEGVKAKYPD QWLAYNLSPS FNWPKAMSVD EQATFIERLG QLGYIWQFIT LAGLHTTALA
IHKFSEDFAR EGMKAYAQNV QQIEMDEGVD VLKHQKWSGA EYIDGLLKLA QGGVSATAAM
GQGVTEDQFK SNL
