ID   M7T2W2_9ARCH            Unreviewed;       290 AA.
AC   M7T2W2;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=PEP phosphonomutase-like enzyme {ECO:0000313|EMBL:EMR73269.1};
DE            EC=4.1.3.32 {ECO:0000313|EMBL:EMR73269.1};
GN   ORFNames=MCGE09_00395 {ECO:0000313|EMBL:EMR73269.1};
OS   Thaumarchaeota archaeon SCGC AB-539-E09.
OC   Archaea; Nitrososphaerota.
OX   NCBI_TaxID=1198115 {ECO:0000313|EMBL:EMR73269.1, ECO:0000313|Proteomes:UP000031483};
RN   [1] {ECO:0000313|EMBL:EMR73269.1, ECO:0000313|Proteomes:UP000031483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCGC AB-539-E09 {ECO:0000313|EMBL:EMR73269.1,
RC   ECO:0000313|Proteomes:UP000031483};
RX   PubMed=23535597; DOI=10.1038/nature12033;
RA   Lloyd K.G., Schreiber L., Petersen D.G., Kjeldsen K.U., Lever M.A.,
RA   Steen A.D., Stepanauskas R., Richter M., Kleindienst S., Lenk S.,
RA   Schramm A., Jorgensen B.B.;
RT   "Predominant archaea in marine sediments degrade detrital proteins.";
RL   Nature 496:215-218(2013).
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:EMR73269.1}.
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DR   EMBL; ALXK01000070; EMR73269.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7T2W2; -.
DR   BioCyc; TARC1198115:G12JZ-394-MONOMER; -.
DR   Proteomes; UP000031483; Unassembled WGS sequence.
DR   GO; GO:0047529; F:2,3-dimethylmalate lyase activity; IEA:UniProtKB-EC.
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:SF5; CARBOXYVINYL-CARBOXYPHOSPHONATE PHOSPHORYLMUTASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 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:0000313|EMBL:EMR73269.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031483}.
SQ   SEQUENCE   290 AA;  31761 MW;  EAF46ACD1F986D06 CRC64;
     MKKTTLLREL IFNPEILVIP VVHDPLCARI AKQAGIKAIF SAGYANSAAY LGKPDVSLMT
     LSEMVDCASR IVDAVNIPVF ADGDTGYGNV TNVIRMVELY EKAGVAGLFI EDQVFPKRCG
     HMEEKQVIPA MEMVAKIQAA VDARKDHDLV IMARTDAIAV HGIDEAIHRA NLYREAGADL
     LFVEAPRSID QMRRICSEVK GPTFANNLPG GKTPFLTSQE LQDIGYAVVA DATSCTYVIA
     HAVRGLFAEL ARTGSSAAFT DRMILFDEFN RLVGLPEIRE NERRYASLSL
//