ID A0A0C3LFG0_9AGAM Unreviewed; 537 AA.
AC A0A0C3LFG0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Isocitrate lyase {ECO:0000256|ARBA:ARBA00017446, ECO:0000256|PIRNR:PIRNR001362};
GN ORFNames=M407DRAFT_245908 {ECO:0000313|EMBL:KIO20187.1};
OS Tulasnella calospora MUT 4182.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Tulasnellaceae; Tulasnella.
OX NCBI_TaxID=1051891 {ECO:0000313|EMBL:KIO20187.1, ECO:0000313|Proteomes:UP000054248};
RN [1] {ECO:0000313|EMBL:KIO20187.1, ECO:0000313|Proteomes:UP000054248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUT 4182 {ECO:0000313|EMBL:KIO20187.1,
RC ECO:0000313|Proteomes:UP000054248};
RG DOE Joint Genome Institute;
RA Kuo A., Girlanda M., Perotto S., Kohler A., Nagy L.G., Floudas D.,
RA Copeland A., Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K.,
RA Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C., Sun H.,
RA Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
RA Nordberg H.P., Cantor M.N., Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUT 4182 {ECO:0000313|Proteomes:UP000054248};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:0000256|ARBA:ARBA00023531};
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 -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC isocitrate: step 1/2. {ECO:0000256|ARBA:ARBA00004793}.
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; KN823183; KIO20187.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3LFG0; -.
DR STRING; 1051891.A0A0C3LFG0; -.
DR HOGENOM; CLU_019214_2_2_1; -.
DR OrthoDB; 983054at2759; -.
DR Proteomes; UP000054248; 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:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
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:SF3; BIFUNCTIONAL GLYOXYLATE CYCLE PROTEIN; 1.
DR PANTHER; PTHR21631; ISOCITRATE LYASE/MALATE SYNTHASE; 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 Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435};
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:UP000054248};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT ACT_SITE 204
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 95..97
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 166
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT BINDING 205..206
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 418..422
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 453
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ SEQUENCE 537 AA; 59843 MW; E6D6188B4F500D46 CRC64;
MAVDESKTFE QQVAEVEQWW KHPRFAQVTR TYTAAQVVAK RGTIDIKYPS DIQAKKLWAL
LENHAKNGTP SHTYGALDPV QVTQMAKYLE TVYVSGWQSS STASSTNEPG PDLADYPYNT
VPNKVEHLFQ AQLFHDRKQR EARSHLSPAQ LRSTPRIDYL RPIVADADTG HGGLTAVMKL
TKLFVEKGAA GIHIEDQAPG TKKCGHMAGK VLVPISEHIN RLVAIRLQYD IMGVSNLVVA
RTDSEAATLI TSNIDERDHP FILGCTNPSL PPLVEVMRKA ENQGVAGDAL QAIEDKWVTA
AGLKLYSHAI AEKLPKNKAG PFIDEVYRSS HAVTEKIAVE KYGLKRSDLP YWNWDVPRTR
EGYYRYQGGT KCAINRCIAF APYCDLLWME TKSPIYAQAK EFADGVHKER PGKWLAYNLS
PSFNWDAAGL GEKDMKEFVW KLGKLGFVWQ FITLGGLHSN GYISDLFAQN FAKDGMLAYV
SLIQRREREL GTDVLTHQKW SGAEYADRLL MTVTGGVSST AAMGKGVTET QFGSRSK
//
