ID A0A1Y2WT11_9PEZI Unreviewed; 547 AA.
AC A0A1Y2WT11;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Isocitrate lyase {ECO:0000256|ARBA:ARBA00017446, ECO:0000256|PIRNR:PIRNR001362};
GN ORFNames=K445DRAFT_321137 {ECO:0000313|EMBL:OTB12401.1};
OS Daldinia sp. EC12.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Daldinia.
OX NCBI_TaxID=1001832 {ECO:0000313|EMBL:OTB12401.1, ECO:0000313|Proteomes:UP000243732};
RN [1] {ECO:0000313|EMBL:OTB12401.1, ECO:0000313|Proteomes:UP000243732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC12 {ECO:0000313|EMBL:OTB12401.1,
RC ECO:0000313|Proteomes:UP000243732};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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 -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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; KZ112955; OTB12401.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2WT11; -.
DR STRING; 1001832.A0A1Y2WT11; -.
DR OrthoDB; 983054at2759; -.
DR Proteomes; UP000243732; 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 Gene3D; 1.10.10.850; -; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 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 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:UP000243732};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT ACT_SITE 215
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 106..108
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT BINDING 216..217
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 433..437
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 467
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ SEQUENCE 547 AA; 61188 MW; 5E3167CFD06E786E CRC64;
MASNNMINPA VDPNIEDDLF LQEVEAVKKW WSDPRWRYTR RPFTAEQIVS KRGHLKIDYP
SNAQSKKLWK ILEGRFKNRD ASYTYGCLEP TMVTQMAKYL DTVYVSGWQS SSTASSSDEP
GPDLADYPYT TVPNKVKHLF MAQLFHDRKQ RQERLSVPKA ERAKLANIDY LRPIVADADT
GHGGLTAVMK LTKLFIEQGA AGIHIEDQAP GTKKCGHMAG KVLVPISEHI NRLVAIRAQA
DIMGTDLVAI ARTDAEAATL ITTSIDPRDH PFILGSTNPQ LQPLNDQMIA AERAGKTGEQ
LQAIEDAWLK QANLRRFDEA VTDAINAAPS LPNKQDLVKK YLEQAKGKSL TEARAIAHKI
TGLDIFFDWD APRTREGFYR LKGGCDCAIN RAIAYAPYCD AIWMESKLPD YKQAEEFAAG
VHAVWPEQKL AYNLSPSFNW KAAMPREEQE TYIRRLAKLG YCWQFITLAG LHTTALISDR
FARAYAEIGM RAYGELVQEP EMEGGVDVVK HQKWSGAAYV DELQKMITGG VSSTAAMGKG
VTEDQFH
//
