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Database: UniProt
Entry: A0A317WXV2_9EURO
LinkDB: A0A317WXV2_9EURO
Original site: A0A317WXV2_9EURO 
ID   A0A317WXV2_9EURO        Unreviewed;       236 AA.
AC   A0A317WXV2;
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:PWY91179.1};
GN   ORFNames=BO70DRAFT_358610 {ECO:0000313|EMBL:PWY91179.1};
OS   Aspergillus heteromorphus CBS 117.55.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY91179.1, ECO:0000313|Proteomes:UP000247233};
RN   [1] {ECO:0000313|EMBL:PWY91179.1, ECO:0000313|Proteomes:UP000247233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY91179.1,
RC   ECO:0000313|Proteomes:UP000247233};
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:PWY91179.1}.
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DR   EMBL; MSFL01000002; PWY91179.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317WXV2; -.
DR   STRING; 1448321.A0A317WXV2; -.
DR   VEuPathDB; FungiDB:BO70DRAFT_358610; -.
DR   OrthoDB; 554215at2759; -.
DR   Proteomes; UP000247233; 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};
KW   Pyruvate {ECO:0000313|EMBL:PWY91179.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247233}.
SQ   SEQUENCE   236 AA;  25381 MW;  238B7574B23C05A1 CRC64;
     MRANAEMISN ISPSTPVIAD ADTGYGGPIM VARTTEQYSR SGVAAFHLED QVQTKRCGHL
     SGKILVDKDT YVTRIRAAVQ ARQRIGSDIV VIARTDSLQT HGYEESVARL RAARDAGADV
     GFLEGITSRE MARQVVQDLA PWPLLLNMVE HGATPSISAA EAKEMGFRII IFPFAALGPA
     CAAMREAMEK LKVDGIPGLD KEMTPQMLFR ECGLDESMKV DAQAGGAAFD GGVDLK
//
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