ID A0A0G1IBK1_9BACT Unreviewed; 517 AA.
AC A0A0G1IBK1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Phosphoenolpyruvate synthase/pyruvate phosphate dikinase {ECO:0000313|EMBL:KKT56168.1};
GN ORFNames=UW45_C0002G0043 {ECO:0000313|EMBL:KKT56168.1};
OS Parcubacteria group bacterium GW2011_GWC2_44_22.
OC Bacteria.
OX NCBI_TaxID=1618930 {ECO:0000313|EMBL:KKT56168.1, ECO:0000313|Proteomes:UP000034136};
RN [1] {ECO:0000313|EMBL:KKT56168.1, ECO:0000313|Proteomes:UP000034136}
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:KKT56168.1}.
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DR EMBL; LCII01000002; KKT56168.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1IBK1; -.
DR Proteomes; UP000034136; 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; IPR018274; PEP_util_AS.
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.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KKT56168.1};
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:KKT56168.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 436..507
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 517 AA; 59893 MW; 9CF71885D53D0B5C CRC64;
MTESERLKII TSHECKEEEA RVALLFLDLY KTCHLEGIKM YRKQLFSFNI FSLTDNYCRE
WTSITETKEL WGWVLRQFRR RKSFAITINN VLSEIILATD KFLNKLRLEV PVLSNRELNQ
IFLELFLLGN RQYGLTILSE GSDILAEKDY LRHLKAVPPI NQAGAIRLLT TPGDLTAIER
ERLGLWRLAQ EAGQNQLIKK ILLARDWPAL RQNHFFTKLE SHAQVFCWVQ NGFESATNLD
WRYFVMQLRE ILDTKTELEI QKTIKRLADK SSLIKKKQRQ LISKYQLSLE TQSFFSLISW
LAILQDKRKE QVQKAIAALD FIWVEIERRL KVPRAQLYKY LVPEITALLL RGRRVKITEL
KARRQIICFS YLKNGQIKTD YVVGHEAIAI NNHFLEKRKF AITDKKLRGF VASVGRNQKK
VSGKVRLVFN PARDTFRTGE ILVTGMTRPE FVPLMKRALA IITNEGGVTS HAAIVARELG
IPCIIGTRHA TEVLKSGDKI ELDLREGTVR LNLSIAK
//
