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Database: UniProt
Entry: E2GMN9_9GAMM
LinkDB: E2GMN9_9GAMM
Original site: E2GMN9_9GAMM 
ID   E2GMN9_9GAMM            Unreviewed;       164 AA.
AC   E2GMN9;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Phosphoenolpyruvate synthase {ECO:0000256|ARBA:ARBA00021623};
DE   Flags: Fragment;
GN   Name=ppsA {ECO:0000313|EMBL:ADK66989.1};
OS   Stenotrophomonas humi.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=405444 {ECO:0000313|EMBL:ADK66989.1};
RN   [1] {ECO:0000313|EMBL:ADK66989.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 18929 {ECO:0000313|EMBL:ADK66989.1};
RX   PubMed=21247714; DOI=10.1016/j.syapm.2010.11.011;
RA   Vasileuskaya-Schulz Z., Kaiser S., Maier T., Kostrzewa M., Jonas D.;
RT   "Delineation of Stenotrophomonas spp. by multi-locus sequence analysis and
RT   MALDI-TOF mass spectrometry.";
RL   Syst. Appl. Microbiol. 34:35-39(2011).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; HM370260; ADK66989.1; -; Genomic_DNA.
DR   AlphaFoldDB; E2GMN9; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 3.50.30.10; 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   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; 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:ADK66989.1};
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:ADK66989.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          3..65
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          103..164
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADK66989.1"
FT   NON_TER         164
FT                   /evidence="ECO:0000313|EMBL:ADK66989.1"
SQ   SEQUENCE   164 AA;  17639 MW;  1DAF26CE5F2EFB98 CRC64;
     VEIRNTFSIS DEDVQELSKQ ALVIEKHYGR PMDIEWAKDG VSGKLFIVQA RPETVKSRAK
     ATQMERYALQ GKGEVIAEGR AVGAKIGAGT ARVVKSLEDM ARVQPGDVLI ADMTDPDWEP
     VMKRASAIVT NRGGRTCHAA IIARELGVPA VVGSGNATQL IKDG
//
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