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Database: UniProt
Entry: F0XKB8_GROCL
LinkDB: F0XKB8_GROCL
Original site: F0XKB8_GROCL 
ID   F0XKB8_GROCL            Unreviewed;       608 AA.
AC   F0XKB8;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Isocitrate lyase {ECO:0000256|PIRNR:PIRNR001362};
GN   ORFNames=CMQ_5021 {ECO:0000313|EMBL:EFX01950.1};
OS   Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS   (Graphiocladiella clavigera).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Leptographium.
OX   NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN   [1] {ECO:0000313|EMBL:EFX01950.1, ECO:0000313|Proteomes:UP000007796}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX   PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA   DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA   Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA   Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA   Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT   "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT   symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
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:0000256|ARBA:ARBA00001050};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001362-3};
CC       Note=Can also use Mn(2+) ion. {ECO:0000256|PIRSR:PIRSR001362-3};
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC       Isocitrate lyase family. {ECO:0000256|ARBA:ARBA00005704,
CC       ECO:0000256|PIRNR:PIRNR001362}.
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DR   EMBL; GL629787; EFX01950.1; -; Genomic_DNA.
DR   RefSeq; XP_014171432.1; XM_014315957.1.
DR   AlphaFoldDB; F0XKB8; -.
DR   STRING; 655863.F0XKB8; -.
DR   GeneID; 25978298; -.
DR   eggNOG; KOG1260; Eukaryota.
DR   HOGENOM; CLU_019214_2_2_1; -.
DR   InParanoid; F0XKB8; -.
DR   OrthoDB; 983054at2759; -.
DR   Proteomes; UP000007796; Unassembled WGS sequence.
DR   GO; GO:0004451; F:isocitrate lyase activity; IEA:InterPro.
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:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   CDD; cd00377; ICL_PEPM; 1.
DR   Gene3D; 1.10.10.850; -; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 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   NCBIfam; TIGR01346; isocit_lyase; 1.
DR   PANTHER; PTHR21631; ISOCITRATE LYASE/MALATE SYNTHASE; 1.
DR   PANTHER; PTHR21631:SF13; MITOCHONDRIAL 2-METHYLISOCITRATE LYASE ICL2; 1.
DR   Pfam; PF00463; ICL; 1.
DR   PIRSF; PIRSF001362; Isocit_lyase; 2.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001362};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007796}.
FT   ACT_SITE        273
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT   BINDING         164..166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         235
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT   BINDING         274..275
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         310
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         493..497
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         528
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ   SEQUENCE   608 AA;  66477 MW;  7283957976D34637 CRC64;
     MLRRPVLFAA ARRTTSSLVP RNPKTFNFVA ARLLSTTMAR RGASLPVVQP PLTSTHAADA
     FQLLPEAEKA GAAEDLLYEQ QIKDVEAWWA TPRYAGIRRP YSAADVVSKR GSQMQTYPSS
     AMARKLWNLV REREAKGEPI HTLGAIDPVQ MTQQAPHQEV LYISGWACSS TLTTTNEVSP
     DFGDYPYNTV PNQVQRMAKA QSMHDRKQWD ARRKLTAAER AKTPYTDYLR PIVADGDTGH
     GGLSAVLKLA KLFAENGAAA VHFEDQLHGG KKCGHLAGKV LVPMGEHINR LVAARFQWDV
     MGTENLVIAR TDSESGRLIS SAIDVRDHEF VLGVADPSVQ PLAETLQAME ARGASSEEID
     IFEAEWVKKS TLVTFDEAAV AHLRAEGVAE ADVASYEAAV AANRDMGISE HRALANSRAP
     AGRPVYFSWD VPRTREGFYH YRAGMAAATK RALAFGPYAD LLWVETGDPS VEVARDLGRQ
     VRAAYPGKGL VYNLSPSFNW MAHGFSEETL RSFVWDIARE GFVLQLVSLA GLHTTATATC
     ALARSFRSDG MLAYVNLVQR PEKELGCDVL THQKWSGASY MDGIMGAIQS GSSGSKSMGE
     GGTESQFE
//
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