ID A0A0L1J0Z8_ASPNO Unreviewed; 303 AA.
AC A0A0L1J0Z8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Putative carboxyphosphonoenolpyruvate phosphonomutase {ECO:0000313|EMBL:KNG85461.1};
GN ORFNames=ANOM_005846 {ECO:0000313|EMBL:KNG85461.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG85461.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG85461.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG85461.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) 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:KNG85461.1}.
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DR EMBL; JNOM01000156; KNG85461.1; -; Genomic_DNA.
DR RefSeq; XP_015406384.1; XM_015551103.1.
DR AlphaFoldDB; A0A0L1J0Z8; -.
DR STRING; 1509407.A0A0L1J0Z8; -.
DR GeneID; 26807650; -.
DR OrthoDB; 554215at2759; -.
DR Proteomes; UP000037505; 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:KNG85461.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037505}.
SQ SEQUENCE 303 AA; 32064 MW; 1FAE4D39B80237D4 CRC64;
MPMVTAATGL RRTLEDPNSF VVAPGVYDGL SARIALSVGF DALYMTGAGT AASVHGQADL
GICTLNDMRA NAEMLSNLSP TTPVIADADT GYGGPIMVAR TTEQYSRSGV AAFHIEDQVQ
TKRCGHLGGK ILVDTDTYVT RIRAAVQARK RIGSDIVVIA RTDSLQTHGY EESVARLRAA
RDAGADVGFL EGITSKEMAR QVVKELAPWP MLLNMVEHGA TPSISAAEAK EMGFRIIIFP
FAGLGPACAA MREAMEKLKV DGIPGLSKEM TPQMLFRVCG LDESVKVDAE AGGAAFEGGV
DLK
//
