ID A0A0G0R2Z8_9BACT Unreviewed; 482 AA.
AC A0A0G0R2Z8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Phosphoenolpyruvate synthase/pyruvate phosphate dikinase {ECO:0000313|EMBL:KKR44106.1};
GN ORFNames=UT79_C0002G0146 {ECO:0000313|EMBL:KKR44106.1};
OS Candidatus Moranbacteria bacterium GW2011_GWC2_40_12.
OC Bacteria; Candidatus Moranbacteria.
OX NCBI_TaxID=1618699 {ECO:0000313|EMBL:KKR44106.1, ECO:0000313|Proteomes:UP000034716};
RN [1] {ECO:0000313|EMBL:KKR44106.1, ECO:0000313|Proteomes:UP000034716}
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:KKR44106.1}.
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DR EMBL; LBYD01000002; KKR44106.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0R2Z8; -.
DR PATRIC; fig|1618699.3.peg.640; -.
DR Proteomes; UP000034716; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KKR44106.1};
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:KKR44106.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 404..474
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT COILED 234..261
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 482 AA; 56115 MW; 84DBEC6527E2AA0A CRC64;
MKKIFEQYVS RKYGVLTSEL FIRGFSKPKK VEKIFFISSL FIPSGVILDR WFYSKDFKKL
GERLLEKDSK EKNYLDKFFS NTYKLGEDLI KKSADIKKID LTDLSLEELV YIFDEFTDYY
ETFSVTLAGF CLQIPLEEKL RELLKRRIDI GEDLAILSSP YKKNIINKEQ EALLKIAVAF
RKGKISVQLV SGLPKKYRVR IKRHIKKFGW MTRGGLDDAW TEEDVFVRLK ESVKEDCAKK
LVTLEKNRRN LKQKSEEILR QIKADKFARR LIKNAKELVY FRTFRTDYLN LAMFNIRPLL
AEIGKRKGYA FREIAQFRLN EISSIRSVRK SELTKRLKNY IIFSKSPNKI IFSSNQEEIE
KYKNKYFEED NIGNHEVKGN VAFRGKVRGR VVIIRDKSDF RKSRKGCILV AAMTTPDFIG
AMEKAAAFIT DEGGITCHAA IIAREMKKPC IIGTKIATKV LRDGDLVEVD ADKGVVRIIK
RK
//
