ACEA_ASHGO
ID ACEA_ASHGO Reviewed; 560 AA.
AC O94198;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 126.
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=ADL066C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=10037140; DOI=10.1016/s0014-5793(99)00017-4;
RA Maeting I., Schmidt G., Sahm H., Revuelta J.L., Stierhof Y.D.,
RA Stahmann K.-P.;
RT "Isocitrate lyase of Ashbya gossypii -- transcriptional regulation and
RT peroxisomal localization.";
RL FEBS Lett. 444:15-21(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AJ010727; CAB37065.1; -; Genomic_DNA.
DR EMBL; AE016817; AAS51854.1; -; Genomic_DNA.
DR RefSeq; NP_984030.1; NM_209383.1.
DR AlphaFoldDB; O94198; -.
DR SMR; O94198; -.
DR STRING; 33169.AAS51854; -.
DR EnsemblFungi; AAS51854; AAS51854; AGOS_ADL066C.
DR GeneID; 4620172; -.
DR KEGG; ago:AGOS_ADL066C; -.
DR eggNOG; KOG1260; Eukaryota.
DR HOGENOM; CLU_019214_2_2_1; -.
DR InParanoid; O94198; -.
DR OMA; LEKDWAE; -.
DR UniPathway; UPA00703; UER00719.
DR Proteomes; UP000000591; Chromosome IV.
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 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..560
FT /note="Isocitrate lyase"
FT /id="PRO_0000068782"
FT MOTIF 558..560
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 217
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 106..108
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 218..219
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 439..443
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 473
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
SQ SEQUENCE 560 AA; 62585 MW; 6E9FCA3A608438AD CRC64;
MSPSVRDARN DLASLQQQAA AEAEDIRRWW SQPRWAGTKR VYTAEDIVKR RGTFPVVEYP
SSVMADKLVE TLARHSRNGT VSQTFGVLDP VQMTQMVKYL DTIYVSGWQC SATASTSNEP
GPDLADYPMD TVPNKVEHLF MAQLFHDRKQ REARLSCTTQ RELDQLGPEI DYLRPIVADA
DTGHGGLTAV FKLTKMFIER GAAGIHMEDQ SSSNKKCGHM AGRCVIPVQE HISRLVTVRM
CADVMHSNLV LVARTDSEAA TLLSSNIDAR DHYYIVGASN PEVTVPLIEV LDAAQQAGAS
GDRLAQLEED WCKKAKLRLF HEAFADQVNA SPSIKDKAGV IAKFNSQIGP QTGASIREMR
KLGRELLGQD VYFDWDLPRA REGLYRYKGG TQCAIMRARA FAPYADLVWF ESNFPDFQQA
KEFAQGVREK FPNKWMAYNL SPSFNWPKAM PPKEQENYIQ RLGEIGYVWQ FITLAGLHTN
ALAIDNFSRE FSRFGMRAYA QGIQQREMDE GVDVLKHQKW AGAEYVDSIL KLAQGGVSST
ASMGKGVTEE QFGSSNGAKL
