ACEA_YARLI
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 03-AUG-2022, entry version 128.
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}; OrderedLocusNames=YALI0C16885g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; 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. 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 -!- 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X72848; CAA51362.1; -; Genomic_DNA.
DR EMBL; CR382129; CAG82243.1; -; Genomic_DNA.
DR RefSeq; XP_501923.1; XM_501923.1.
DR AlphaFoldDB; P41555; -.
DR SMR; P41555; -.
DR STRING; 4952.CAG82243; -.
DR EnsemblFungi; CAG82243; CAG82243; YALI0_C16885g.
DR GeneID; 2909302; -.
DR KEGG; yli:YALI0C16885g; -.
DR VEuPathDB; FungiDB:YALI0_C16885g; -.
DR HOGENOM; CLU_019214_2_2_1; -.
DR InParanoid; P41555; -.
DR OMA; LEKDWAE; -.
DR UniPathway; UPA00703; UER00719.
DR Proteomes; UP000001300; Chromosome C.
DR GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0004451; F:isocitrate lyase activity; IBA:GO_Central.
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 Gene3D; 3.20.20.60; -; 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 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..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
