ID U5YKV1_9BACT Unreviewed; 135 AA.
AC U5YKV1;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=PEP mutase {ECO:0000313|EMBL:AGZ93265.1};
DE Flags: Fragment;
GN Name=pepM {ECO:0000313|EMBL:AGZ93265.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:AGZ93265.1};
RN [1] {ECO:0000313|EMBL:AGZ93265.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24297932; DOI=10.1073/pnas.1315107110;
RA Yu X., Doroghazi J.R., Janga S.C., Zhang J.K., Circello B., Griffin B.M.,
RA Labeda D.P., Metcalf W.W.;
RT "Diversity and abundance of phosphonate biosynthetic genes in nature.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20759-20764(2013).
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. PEP
CC mutase family. {ECO:0000256|ARBA:ARBA00038455}.
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DR EMBL; KF387133; AGZ93265.1; -; Genomic_DNA.
DR AlphaFoldDB; U5YKV1; -.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR039556; ICL/PEPM.
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:SF7; PHOSPHOENOLPYRUVATE PHOSPHOMUTASE-RELATED; 1.
DR Pfam; PF13714; PEP_mutase; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 3: Inferred from homology;
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AGZ93265.1"
FT NON_TER 135
FT /evidence="ECO:0000313|EMBL:AGZ93265.1"
SQ SEQUENCE 135 AA; 14941 MW; 538CDCDEBCB0BEFC CRC64;
AGVCVEDKLF PKTNSFIGDH QPLADREEFC GRIRAGKDSQ TDDDFSIVAR IEALIAGQGM
DEALRRAEAY HAAGADAILI HSKRSTASEI LSFMEHWGQR CPVVIVPTMY YATPTQAFRE
VGVSTVIWAN HMMRA
//