ID   A0A319ETK4_9EURO        Unreviewed;       312 AA.
AC   A0A319ETK4;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Phosphoenolpyruvate/pyruvate domain-containing protein {ECO:0000313|EMBL:PYH94482.1};
GN   ORFNames=BO71DRAFT_398843 {ECO:0000313|EMBL:PYH94482.1};
OS   Aspergillus ellipticus CBS 707.79.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448320 {ECO:0000313|EMBL:PYH94482.1, ECO:0000313|Proteomes:UP000247810};
RN   [1] {ECO:0000313|EMBL:PYH94482.1, ECO:0000313|Proteomes:UP000247810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 707.79 {ECO:0000313|EMBL:PYH94482.1,
RC   ECO:0000313|Proteomes:UP000247810};
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 (FEB-2018) 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};
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DR   EMBL; KZ825870; PYH94482.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319ETK4; -.
DR   STRING; 1448320.A0A319ETK4; -.
DR   Proteomes; UP000247810; 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:SF2; PHOSPHOENOLPYRUVATE CARBOXYLASE FAMILY PROTEIN; 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};
KW   Pyruvate {ECO:0000313|EMBL:PYH94482.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247810}.
SQ   SEQUENCE   312 AA;  33587 MW;  F29F7BDABB7F6664 CRC64;
     MTTTPPPLTA ASRLRTHLAT PNHTLFCPGI YDGLTARIAL NEQFPALYMT GAGTAATRLG
     APDLGLATLN DMVENARMIA SLDRTVPLIA DADTGYGGPL MVARTVQAYM TAGVAGMHLE
     DQVVTKRCGH LSGKELVSEE EYLARIRAAV LAREEVRSAW PGADIVLIAR TDSLQSLGYE
     AAVQRLKRAV EVGADVAFLE GMTSLEECRR VCVDLAPTPV LLNMVAGGVT PEVGLDEARE
     LGFKIVIFPA VCLGPVVEEA TRALRRLKAE RRNEVSEFQK RTGVKGFFEV VRLGDFLEFD
     QRAGGSAFEN GV
//