ID A0A2V1CEU8_9HELO Unreviewed; 304 AA.
AC A0A2V1CEU8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Phosphoenolpyruvate/pyruvate domain-containing protein {ECO:0000313|EMBL:PVH84227.1};
GN ORFNames=DL98DRAFT_546899 {ECO:0000313|EMBL:PVH84227.1};
OS Cadophora sp. DSE1049.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiales incertae sedis; Cadophora.
OX NCBI_TaxID=1485229 {ECO:0000313|EMBL:PVH84227.1, ECO:0000313|Proteomes:UP000244409};
RN [1] {ECO:0000313|EMBL:PVH84227.1, ECO:0000313|Proteomes:UP000244409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE1049 {ECO:0000313|EMBL:PVH84227.1,
RC ECO:0000313|Proteomes:UP000244409};
RX PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT "Comparative genomics provides insights into the lifestyle and reveals
RT functional heterogeneity of dark septate endophytic fungi.";
RL Sci. Rep. 8:6321-6321(2018).
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; KZ804124; PVH84227.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1CEU8; -.
DR STRING; 1485229.A0A2V1CEU8; -.
DR Proteomes; UP000244409; 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:PVH84227.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000244409}.
SQ SEQUENCE 304 AA; 32534 MW; A93B62BA3E516BA7 CRC64;
MSNAPLTGAK RLRELLADRH KIVVCPGVYD GITARLSRAA GFEALYMTGA GTSMSKLGWA
DLGMATLNDM QSNASMIASL DPSCPVIADA DTGYGGPVMV ARTVAQYSRG GVAALHIEDQ
VQEKRCGHLL GKQIVDREMF YTRLRAAVKA RNDLQSDMLI IARTDARQSF GFDEAAERLK
EAVKIGVDAV FLEALQSKDE ARRICETMGD VPVLLNMVPG GTTPDITVDE AKNLGFRIIT
FPGLSLTPVM LGVQAELEHL KTNGFVSPEN AGHGVKGLFN MCGLQECIDI DKAAGGKAYA
DVGK
//