ACEA_MAGO7
ID ACEA_MAGO7 Reviewed; 547 AA.
AC P0CT06; A4QU17; G4N2R9; Q5EN15; Q8J232;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Isocitrate lyase {ECO:0000303|PubMed:12622815};
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:12622815}; ORFNames=MGG_04895;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, AND FUNCTION.
RC STRAIN=Guyane 11;
RX PubMed=12622815; DOI=10.1046/j.1365-2958.2003.03412.x;
RA Wang Z.Y., Thornton C.R., Kershaw M.J., Debao L., Talbot N.J.;
RT "The glyoxylate cycle is required for temporal regulation of virulence by
RT the plant pathogenic fungus Magnaporthe grisea.";
RL Mol. Microbiol. 47:1601-1612(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
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 (By similarity). plays an important role in plant
CC pathogenicity. {ECO:0000250|UniProtKB:P28240,
CC ECO:0000269|PubMed:12622815}.
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: Leads to reduced virulence and a delay in the
CC expression of rice blast symptoms. {ECO:0000269|PubMed:12622815}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Isocitrate lyase family. {ECO:0000305}.
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DR EMBL; AF540383; AAN28719.1; -; Genomic_DNA.
DR EMBL; CM001233; EHA52574.1; -; Genomic_DNA.
DR RefSeq; XP_003712381.1; XM_003712333.1.
DR PDB; 5E9F; X-ray; 2.80 A; A/B/C/D=1-547.
DR PDB; 5E9G; X-ray; 2.10 A; A/B/C/D=1-547.
DR PDBsum; 5E9F; -.
DR PDBsum; 5E9G; -.
DR AlphaFoldDB; P0CT06; -.
DR SMR; P0CT06; -.
DR STRING; 318829.MGG_04895T0; -.
DR BindingDB; P0CT06; -.
DR ChEMBL; CHEMBL1075264; -.
DR PRIDE; P0CT06; -.
DR EnsemblFungi; MGG_04895T0; MGG_04895T0; MGG_04895.
DR GeneID; 2675603; -.
DR KEGG; mgr:MGG_04895; -.
DR VEuPathDB; FungiDB:MGG_04895; -.
DR eggNOG; KOG1260; Eukaryota.
DR HOGENOM; CLU_019214_2_2_1; -.
DR OMA; LEKDWAE; -.
DR OrthoDB; 905115at2759; -.
DR BRENDA; 4.1.3.1; 5238.
DR UniPathway; UPA00703; UER00719.
DR PHI-base; PHI:305; -.
DR PRO; PR:P0CT06; -.
DR Proteomes; UP000009058; Chromosome 3.
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 1: Evidence at protein level;
KW 3D-structure; Glyoxylate bypass; Glyoxysome; Lyase; Magnesium;
KW Metal-binding; Peroxisome; Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..547
FT /note="Isocitrate lyase"
FT /id="PRO_0000068793"
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 TURN 13..15
FT /evidence="ECO:0007829|PDB:5E9G"
FT HELIX 16..31
FT /evidence="ECO:0007829|PDB:5E9G"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:5E9G"
FT HELIX 45..49
FT /evidence="ECO:0007829|PDB:5E9G"
FT HELIX 60..78
FT /evidence="ECO:0007829|PDB:5E9G"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:5E9G"
FT HELIX 90..96
FT /evidence="ECO:0007829|PDB:5E9G"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:5E9G"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:5E9G"
FT HELIX 107..113
FT /evidence="ECO:0007829|PDB:5E9G"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:5E9G"
FT HELIX 131..156
FT /evidence="ECO:0007829|PDB:5E9G"
FT HELIX 159..164
FT /evidence="ECO:0007829|PDB:5E9G"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:5E9G"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:5E9G"
FT HELIX 185..198
FT /evidence="ECO:0007829|PDB:5E9G"
FT STRAND 201..208
FT /evidence="ECO:0007829|PDB:5E9G"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:5E9G"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:5E9G"
FT HELIX 226..243
FT /evidence="ECO:0007829|PDB:5E9G"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:5E9G"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:5E9G"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:5E9G"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:5E9G"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:5E9G"
FT HELIX 284..292
FT /evidence="ECO:0007829|PDB:5E9G"
FT HELIX 299..312
FT /evidence="ECO:0007829|PDB:5E9G"
FT HELIX 317..325
FT /evidence="ECO:0007829|PDB:5E9G"
FT HELIX 334..345
FT /evidence="ECO:0007829|PDB:5E9G"
FT HELIX 350..359
FT /evidence="ECO:0007829|PDB:5E9G"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:5E9G"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:5E9G"
FT HELIX 385..395
FT /evidence="ECO:0007829|PDB:5E9G"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:5E9G"
FT STRAND 400..404
FT /evidence="ECO:0007829|PDB:5E9G"
FT HELIX 411..422
FT /evidence="ECO:0007829|PDB:5E9G"
FT STRAND 430..433
FT /evidence="ECO:0007829|PDB:5E9G"
FT HELIX 440..443
FT /evidence="ECO:0007829|PDB:5E9G"
FT HELIX 446..458
FT /evidence="ECO:0007829|PDB:5E9G"
FT STRAND 461..466
FT /evidence="ECO:0007829|PDB:5E9G"
FT HELIX 469..488
FT /evidence="ECO:0007829|PDB:5E9G"
FT HELIX 490..496
FT /evidence="ECO:0007829|PDB:5E9G"
FT HELIX 498..504
FT /evidence="ECO:0007829|PDB:5E9G"
FT HELIX 507..509
FT /evidence="ECO:0007829|PDB:5E9G"
FT HELIX 511..514
FT /evidence="ECO:0007829|PDB:5E9G"
FT HELIX 517..526
FT /evidence="ECO:0007829|PDB:5E9G"
SQ SEQUENCE 547 AA; 61001 MW; 0BF3F9921E04D1D0 CRC64;
MASKNMVNPA VEPSMEDDLF AREVAEVKQW WSDPRWRYTK RPFTAEQIVS KRGNLKIEYP
SNAQSKKLWK ILEGRFQKRD ASYTYGCLEP TMVTQMAKYL DTVYVSGWQS SSTASSSDEP
GPDLADYPYT TVPNKVSHLF MAQLFHDRKQ RHERLSAPKS ERSKLQNIDY LRPIIADADT
GHGGLTAVMK LTKLFIEKGA AGIHIEDQAP GTKKCGHMAG KVLVPISEHI 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
