ID G9CP99_RALSL Unreviewed; 210 AA.
AC G9CP99;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Phosphoenolpyruvate synthase {ECO:0000313|EMBL:AEV53319.1};
DE Flags: Fragment;
GN Name=ppsA {ECO:0000313|EMBL:AEV53319.1};
OS Ralstonia solanacearum CMR15.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=859655 {ECO:0000313|EMBL:AEV53319.1};
RN [1] {ECO:0000313|EMBL:AEV53319.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CMR15 {ECO:0000313|EMBL:AEV53319.1};
RA Wicker E.P.P., Lefeuvre P., De Cambiaire J.-C., Lemaire C., Poussier S.,
RA Prior P.;
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEV53319.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CMR15 {ECO:0000313|EMBL:AEV53319.1};
RX PubMed=22094345; DOI=10.1038/ismej.2011.160;
RA Wicker E., Lefeuvre P., de Cambiaire J.C., Lemaire C., Poussier S.,
RA Prior P.;
RT "Contrasting recombination patterns and demographic histories of the plant
RT pathogen Ralstonia solanacearum inferred from MLSA.";
RL ISME J. 6:961-974(2012).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; JF702812; AEV53319.1; -; Genomic_DNA.
DR AlphaFoldDB; G9CP99; -.
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; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
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 InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR43030; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR PANTHER; PTHR43030:SF1; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 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};
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:AEV53319.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 22..93
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEV53319.1"
FT NON_TER 210
FT /evidence="ECO:0000313|EMBL:AEV53319.1"
SQ SEQUENCE 210 AA; 22402 MW; 6D84205A72EF07BC CRC64;
IGQKIGTGPV RVINDPAEME RVQPGDVLVA DMTDPNWEPV MKRAAAIVTN RGGRTCHAAI
IARELGVPAV VGCGDATDLL KDGTLVTVSC AEGDEGRIYD GLLETEITEV RRGEMPSIDV
KIMMNVGNPQ LAFEFAQIPN GGVGLARLEF IINNNIGVHP KAILDYPQVD SDLKKAVESV
ARGHASPRAF YVDKLAEGIA TIAAAFYPKP
//
