ID M4YMR2_THEXX Unreviewed; 431 AA.
AC M4YMR2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=phosphoenolpyruvate mutase {ECO:0000256|ARBA:ARBA00024063};
DE EC=5.4.2.9 {ECO:0000256|ARBA:ARBA00024063};
GN ORFNames=TALC_00083 {ECO:0000313|EMBL:AGI47098.1};
OS Thermoplasmatales archaeon (strain BRNA1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales.
OX NCBI_TaxID=1054217 {ECO:0000313|EMBL:AGI47098.1, ECO:0000313|Proteomes:UP000012076};
RN [1] {ECO:0000313|EMBL:AGI47098.1, ECO:0000313|Proteomes:UP000012076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRNA1 {ECO:0000313|EMBL:AGI47098.1,
RC ECO:0000313|Proteomes:UP000012076};
RA Denman S.E., Evans P., Bragg L., Padmanahba J., McKenzie M., Edwards D.,
RA Krzycki J., McSweeney C., Morrison M.;
RT "Thermoplasmatales-like gut symbionts are pyrrolysine dependent-
RT methanogens.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. PEP
CC mutase family. {ECO:0000256|ARBA:ARBA00038455}.
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DR EMBL; CP002916; AGI47098.1; -; Genomic_DNA.
DR AlphaFoldDB; M4YMR2; -.
DR STRING; 1054217.TALC_00083; -.
DR KEGG; tar:TALC_00083; -.
DR PATRIC; fig|1054217.5.peg.81; -.
DR eggNOG; arCOG00581; Archaea.
DR eggNOG; arCOG01222; Archaea.
DR HOGENOM; CLU_027389_0_1_2; -.
DR Proteomes; UP000012076; Chromosome.
DR GO; GO:0050188; F:phosphoenolpyruvate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR039556; ICL/PEPM.
DR InterPro; IPR012698; PEnolPyrv_PMutase_core.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR NCBIfam; TIGR02320; PEP_mutase; 1.
DR PANTHER; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR PANTHER; PTHR42905:SF7; PHOSPHOENOLPYRUVATE PHOSPHOMUTASE-RELATED; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR Pfam; PF13714; PEP_mutase; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AGI47098.1};
KW Pyruvate {ECO:0000313|EMBL:AGI47098.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000012076};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 11..103
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
SQ SEQUENCE 431 AA; 48655 MW; 1FDEAF14102C4B3B CRC64;
MAIVYTCFST DIVHEGHLNI IKNAQKYGDV YVGVLSDKAT IRYNKFPTVS FEDRFKMIEA
IPGVTRVLVQ DDVMYDGIVK QIRPDYIIHG DNWKTGAMKA IRDNAEKLIA PYGGKIIDVP
YTFSESVRRE DARIKEKLAM PEYRRKRLKQ LLALRPIVKA MEVHSGLTGL IVEKTCVEHN
GEIDQFDAMW LSSLCDSTAK GKPDIEVVDM TSRFRTIDDV MEVTTKPIIF DGDTGGLPEH
FVYIVRSLER MGVSAVIIED KTGLKKNSLF GTEVKQTQDS IENFCEKIKA GKRVQLTDDF
MIIARIESLI LEQGMDDALA RARAYVAAGA DGIMIHSRKN DPAEILEFCD LFRKENKDTP
IVVVPTSFNS ITESELAEHG VNIVIYANQL TRSAFPAMEQ TAKDILRYHR AQEVDSRLLP
IKDIISLIDE L
//
