ID   A0A317VZZ4_9EURO        Unreviewed;       303 AA.
AC   A0A317VZZ4;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=2,3-Dimethylmalate lyase {ECO:0000313|EMBL:PWY78572.1};
GN   ORFNames=BO94DRAFT_558868 {ECO:0000313|EMBL:PWY78572.1};
OS   Aspergillus sclerotioniger CBS 115572.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1450535 {ECO:0000313|EMBL:PWY78572.1, ECO:0000313|Proteomes:UP000246702};
RN   [1] {ECO:0000313|EMBL:PWY78572.1, ECO:0000313|Proteomes:UP000246702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115572 {ECO:0000313|EMBL:PWY78572.1,
RC   ECO:0000313|Proteomes:UP000246702};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PWY78572.1}.
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DR   EMBL; MSFK01000024; PWY78572.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317VZZ4; -.
DR   STRING; 1450535.A0A317VZZ4; -.
DR   OrthoDB; 554215at2759; -.
DR   Proteomes; UP000246702; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   CDD; cd00377; ICL_PEPM; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR039556; ICL/PEPM.
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; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR42905:SF15; PHOSPHONOMUTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G03820)-RELATED; 1.
DR   Pfam; PF13714; PEP_mutase; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:PWY78572.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000246702}.
SQ   SEQUENCE   303 AA;  32213 MW;  27F1A40FDF995357 CRC64;
     MPMITAATTL RRALEDPKSF VVAPGVYDGL SARIALSVGF DALYMTGAGT AASVHGQADL
     GICTLNDMRA NAEMISNISP STPVIADADT GYGGPIMVAR TTEQYSRSGV AAFHLEDQVQ
     TKRCGHLAGK ILVDKETYVT RIRAAVQARQ RIGSDIVVIA RTDSLQTHGY EESVARLRAA
     RDAGADVGFL EGITSREMAR QVVQDLAPWP LLLNMVEHGA TPSISAAEAK ELGFRIIIFP
     FAALGPACAA MRDAMEKLKK DGIPGLDKEM TPQMLFRVCG LDESMKVDAQ AGGAAFEGGV
     DLQ
//