ID   A0A0G1P6Y3_9BACT        Unreviewed;       488 AA.
AC   A0A0G1P6Y3;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Phosphoenolpyruvate synthase/pyruvate phosphate dikinase {ECO:0000313|EMBL:KKT92119.1};
GN   ORFNames=UW91_C0026G0003 {ECO:0000313|EMBL:KKT92119.1};
OS   Parcubacteria group bacterium GW2011_GWF2_45_11.
OC   Bacteria.
OX   NCBI_TaxID=1618973 {ECO:0000313|EMBL:KKT92119.1, ECO:0000313|Proteomes:UP000034898};
RN   [1] {ECO:0000313|EMBL:KKT92119.1, ECO:0000313|Proteomes:UP000034898}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:KKT92119.1}.
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DR   EMBL; LCKE01000026; KKT92119.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1P6Y3; -.
DR   PATRIC; fig|1618973.3.peg.690; -.
DR   Proteomes; UP000034898; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008986; F:pyruvate, water dikinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR   Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR   InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR   InterPro; IPR006319; PEP_synth.
DR   InterPro; IPR036637; Phosphohistidine_dom_sf.
DR   PANTHER; PTHR43030; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR   PANTHER; PTHR43030:SF1; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KKT92119.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Pyruvate {ECO:0000313|EMBL:KKT92119.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          399..471
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
SQ   SEQUENCE   488 AA;  56426 MW;  4910D540122FC34A CRC64;
     MMWQKYITRR LAVQVAQAWN FGWDTAMRKV YGISLRNTLV FRDSQKTEYY VNQDEYARHV
     KGLSGLLNCE AFLRTFHHEA KAELEKILFK LRAKLRLKFV QLSNEEFLQV YQNDILPAVA
     QFYARMGTVF NLGLPLSEMI TAKLRKKITD PTEFNQRLLV LFSPLEPNDA VNERLSLLTI
     ASQKPKLKKS EFEKRVRNHT KNYRHIPMFD FDHQPYTEAS FIKELRKIEY PSNELADLRL
     MFKNRRLKFN QVVRSLKPDK KFKLLLEFLK ENIFLRDYRD MIRQKLNLEL RKFYVEAGKR
     LGLSLAQVAT LTNEEIIKSL GENKKFSPAE AKRREQAFLL IQKSSAVEIY SGQKAVARFK
     KECKPYQPKV LEKIRGSLAA PGRARGPVKI VRTNQDLNKI KDGDIMVTGM TRQDFVPALR
     RVSALVTDEG GMICHAAIIA REFKIPCVVG AKIATLALSD GDLVDVDADR GIIRKVTKHK
     GPLRSKKS
//