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Database: UniProt
Entry: A0A3A2ZRW3_9EURO
LinkDB: A0A3A2ZRW3_9EURO
Original site: A0A3A2ZRW3_9EURO 
ID   A0A3A2ZRW3_9EURO        Unreviewed;       337 AA.
AC   A0A3A2ZRW3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Carboxyphosphonoenolpyruvate phosphonomutase {ECO:0000313|EMBL:RJE25063.1};
GN   ORFNames=PHISCL_02598 {ECO:0000313|EMBL:RJE25063.1};
OS   Aspergillus sclerotialis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Polypaecilum.
OX   NCBI_TaxID=2070753 {ECO:0000313|EMBL:RJE25063.1, ECO:0000313|Proteomes:UP000266188};
RN   [1] {ECO:0000313|Proteomes:UP000266188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 366.77 {ECO:0000313|Proteomes:UP000266188};
RA   Tafer H., Lopandic K.;
RL   Submitted (FEB-2017) 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:RJE25063.1}.
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DR   EMBL; MVGC01000059; RJE25063.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A2ZRW3; -.
DR   STRING; 2070753.A0A3A2ZRW3; -.
DR   Proteomes; UP000266188; 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:RJE25063.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266188}.
SQ   SEQUENCE   337 AA;  36289 MW;  C93572E81AB42017 CRC64;
     MKVEESSLKT DVVTTITVEK NGVYEVNGVK HEPSVSVQML TGASKLRRQL LESKDLIVCP
     GVYDGLSARI AIQLGFKALY MTGAGTTASR LGMADLGLAQ LHDMRTNAEM IASLDPFGPP
     LIADMDTGYG GPLMVAKSVQ QYIQAGVAGF HIEDQVQNKR CGHLAGKKVV SLDEYLIRIR
     AAKRTKDRLH SDIVLIARTD ALQQHGYDEC IRRLKAAQDL GADVGLLEGF TSKEQARQAV
     QDLAPWPLLL NMVENGAGPV ITTQEAQEMG FRIMIFSFAS LAPAYLGIKA ALERLKTHGI
     VGTPEGVGPK KLFEVCGLME SVYIDTTAGG SGFVNGV
//
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