ID G2WWY9_VERDV Unreviewed; 600 AA.
AC G2WWY9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Isocitrate lyase {ECO:0000256|PIRNR:PIRNR001362};
GN ORFNames=VDAG_02768 {ECO:0000313|EMBL:EGY21244.1};
OS Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY21244.1, ECO:0000313|Proteomes:UP000001611};
RN [1] {ECO:0000313|Proteomes:UP000001611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VdLs.17 / ATCC MYA-4575 / FGSC 10137
RC {ECO:0000313|Proteomes:UP000001611};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(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; DS572698; EGY21244.1; -; Genomic_DNA.
DR RefSeq; XP_009651716.1; XM_009653421.1.
DR AlphaFoldDB; G2WWY9; -.
DR STRING; 498257.G2WWY9; -.
DR EnsemblFungi; EGY21244; EGY21244; VDAG_02768.
DR GeneID; 20704231; -.
DR KEGG; vda:VDAG_02768; -.
DR eggNOG; KOG1260; Eukaryota.
DR HOGENOM; CLU_019214_2_2_1; -.
DR InParanoid; G2WWY9; -.
DR OMA; WFVYNLS; -.
DR OrthoDB; 983054at2759; -.
DR Proteomes; UP000001611; Chromosome 3.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:EnsemblFungi.
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:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IEA:EnsemblFungi.
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:UP000001611}.
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 267
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 158..160
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT BINDING 268..269
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 304
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 485..489
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 520
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ SEQUENCE 600 AA; 66003 MW; 69DA676B7EECBB0F CRC64;
MMRRIATKSP RRVPLPKPRT TPISAPSLAA RCLSTTPKMA KTPANPFSDV PADAFQLLSE
ANKAGEAEDA LYESQIKEVE AWWRSPRYEG IKRPYSAADV VSKRGTQQQT YASSLMARKL
FNLIKERGAE GKPLHTMGAI DPVQMTQQAP HQEVLYISGW ACSSLLTSTN EVSPDFGDYP
YNTVPNQVQR LAKAQSMHDR KQWDARRKLT PEQRAKAPYT DYLRPIIADG DTGHGGLSAV
LKLAKLFAEN GAAAVHFEDQ LHGGKKCGHL AGKVLVPVGE HINRLNAARF QWDVMGTENL
VIARTDSESG KLISSAIDVR DHEFILGVAD PSIEPLAETL QAMEARGAVG SEIDAFEANW
VKSTKLVSFD EAAVAHMKSE GVAQEHIDWY LETVRANRDL GVAHRRKLAS QHTSTPVYFS
WDVPRTREGY YHYRAGMDAA TKRALAFGPY ADLLWVETGD PNVEVATTLA RAVRAQMPGK
GLVYNLSPSF NWMAHGFTDA TLKSFIWDIA REGFVLQLIS LAGLHSNATI TNELARDFKS
DGMLAYVNLV QRREKEGGCD VLTHQKWSGA SYIDGILGAI QSGSSSSKSM GEGNTEGQFN
//
