ID   G8HMX4_RALSL            Unreviewed;       330 AA.
AC   G8HMX4;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Phosphoenolpyruvate synthase {ECO:0000256|ARBA:ARBA00021623};
DE   Flags: Fragment;
GN   Name=ppsA {ECO:0000313|EMBL:AET79887.1};
OS   Ralstonia solanacearum (Pseudomonas solanacearum).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=305 {ECO:0000313|EMBL:AET79887.1};
RN   [1] {ECO:0000313|EMBL:AET79887.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CRs-Avl {ECO:0000313|EMBL:AET79887.1};
RA   Kumar A., Prameela T.P.II., Bhai S.R.;
RT   "Multilocus sequence typing of Ralstonia solanacaearum causing bacterial
RT   wilt of ginger in India.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; JN609198; AET79887.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8HMX4; -.
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:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
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; IPR002192; PPDK_AMP/ATP-bd.
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   Pfam; PF01326; PPDK_N; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 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:AET79887.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          2..131
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          172..243
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AET79887.1"
FT   NON_TER         330
FT                   /evidence="ECO:0000313|EMBL:AET79887.1"
SQ   SEQUENCE   330 AA;  35903 MW;  F24C38A20234B509 CRC64;
     QDVVFITSSY GLGETVVQGA VNPDEFYVFK PTLAAGKYPI IRRSIGSKLI KMEFTQAGEE
     GRVKTVDVPG ELRNRYSLVD EDVVELAKYA VIIEKHYGRP MDIEWGKDGK DGKIYILQAR
     PETVKSQSVG KVEQRFRLKG SAPVLTTGRA IGQKIGTGPV RVINDPAEME RVQPGDVLVA
     DMTDPNWEPV MKRASAIVTN RGGRTCHAAI IARELGVPAV VGCGDATDLL KDGTLVTVSC
     AEGDEGKIYD GLLETEITEV RRGEMPPIDV KIMMNVGNPQ LAFEFAQIPN GGVGLARLEF
     IINNNIGVHP KAILDYPQVD SDLKKAVESV
//