ID   A0A2T3AB43_9PEZI        Unreviewed;       362 AA.
AC   A0A2T3AB43;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Putative carboxyphosphonoenolpyruvate phosphonomutase {ECO:0000313|EMBL:PSR90318.1};
GN   ORFNames=BD289DRAFT_431163 {ECO:0000313|EMBL:PSR90318.1};
OS   Coniella lustricola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Schizoparmaceae; Coniella.
OX   NCBI_TaxID=2025994 {ECO:0000313|EMBL:PSR90318.1, ECO:0000313|Proteomes:UP000241462};
RN   [1] {ECO:0000313|EMBL:PSR90318.1, ECO:0000313|Proteomes:UP000241462}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B22-T-1 {ECO:0000313|EMBL:PSR90318.1,
RC   ECO:0000313|Proteomes:UP000241462};
RA   Raudabaugh D.B., Iturriaga T., Carver A., Mondo S., Pangilinan J.,
RA   Lipzen A., He G., Amirebrahimi M., Grigoriev I.V., Miller A.N.;
RT   "Coniella lustricola, a new species from submerged detritus.";
RL   Mycol. Prog. 17:191-203(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; KZ678421; PSR90318.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T3AB43; -.
DR   STRING; 2025994.A0A2T3AB43; -.
DR   InParanoid; A0A2T3AB43; -.
DR   Proteomes; UP000241462; 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:PSR90318.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000241462}.
SQ   SEQUENCE   362 AA;  39292 MW;  B0290F7766897562 CRC64;
     MASQTTELAP RVFNTSPSFK QSVLVQHIPQ APLTPEELVV DKTNDTKFLT MTPTTYSPGK
     PLSGATKLRR MIFETKNLIV CPGVYDGLSA RTALELGFQA LYMTGAGTTA SRLGQPDLAI
     AQLYEMRENA DMIAGLDPYG PPLIADMDTG YGGPLMVART VEQYIRSGVA GAHLEDQVLM
     KRCGHLGGKK VVPREEYLQR IRAAHQARMR LQSDFVLIAR TDALQSLGYD ECIARLRAAR
     DIGADVGLLE GFKSKEQAAQ AVQDLAPWPL LYNSVENGAS PAITVEEARQ MGFRIMIFSF
     ATLAPAYTAI RDALIRLKTV GGVGTPKEIT PVRLFEVCGL KHSMSVDIAA GGKAFDDDVS
     KV
//