ACEA_MAGOY
ID ACEA_MAGOY Reviewed; 547 AA.
AC L7HUY5; A4QU17; G4N2R9; Q5EN15; Q8J232;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 30.
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}; ORFNames=OOU_Y34scaffold00745g63;
OS Magnaporthe oryzae (strain Y34) (Rice blast fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=1143189;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Y34;
RA Dong H.T., Peng Y.L., Chen B.S., Li Y.Z., Li D.B.;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y34;
RX PubMed=22876203; DOI=10.1371/journal.pgen.1002869;
RA Xue M., Yang J., Li Z., Hu S., Yao N., Dean R.A., Zhao W., Shen M.,
RA Zhang H., Li C., Liu L., Cao L., Xu X., Xing Y., Hsiang T., Zhang Z.,
RA Xu J.-R., Peng Y.-L.;
RT "Comparative analysis of the genomes of two field isolates of the rice
RT blast fungus Magnaporthe oryzae.";
RL PLoS Genet. 8:E1002869-E1002869(2012).
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; AY849617; AAX07638.1; -; mRNA.
DR EMBL; JH793093; ELQ34788.1; -; Genomic_DNA.
DR AlphaFoldDB; L7HUY5; -.
DR SMR; L7HUY5; -.
DR UniPathway; UPA00703; UER00719.
DR Proteomes; UP000011086; Unassembled WGS sequence.
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 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 2: Evidence at transcript level;
KW Glyoxylate bypass; Glyoxysome; Lyase; Magnesium; Metal-binding; Peroxisome;
KW Tricarboxylic acid cycle.
FT CHAIN 1..547
FT /note="Isocitrate lyase"
FT /id="PRO_0000423539"
FT ACT_SITE 215
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 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 216..217
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 433..437
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 467
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT CONFLICT 227
FT /note="N -> S (in Ref. 1; AAX07638)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="Q -> L (in Ref. 1; AAX07638)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 547 AA; 61028 MW; A31ED3A63BCC38DB CRC64;
MASKNMVNPA VEPSMEDDLF AREVAEVKQW WSDPRWRYTK RPFTAEQIVS KRGNLKIEYP
SNAQSKKLWK ILEGRFQKRD ASYTYGCLEP TMVTQMAKYL DTVYVSGWQS SSTASSSDEP
GPDLADYPYT TVPNKVSHLF MAQLFHDRKQ RHERLSAPKS ERSKLQNIDY LRPIIADADT
GHGGLTAVMK LTKLFIEKGA AGIHIEDQAP GTKKCGHMAG KVLVPINEHI NRLVAIRAQA
DIMGVDLLAI ARTDAEAATL ITTSIDPRDH AFILGCTNPS LQPLADLMNT AEQSGKTGDQ
LQAIEDEWMA KANLKRFDDA VVDVINSSSS IRNPKDVAAK YLQAAKGKSN REARAIASSL
GVPEIFFDWD SPRTREGYFR IKGGCDCAIN RAIAYAPYAD AIWMESKLPD YEQAKEFAEG
VHAVYPEQKL AYNLSPSFNW KTAMPRDEQE TYIRRLAGLG YCWQFITLAG LHTTALISDR
FARAYSEVGM RAYGELVQEP EMELGVDVVK HQKWSGATYV DELQKMVTGG VSSTAAMGKG
VTEDQFH
