ID B6CXR2_PSEAI Unreviewed; 300 AA.
AC B6CXR2;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Phosphoenolpyruvate synthase {ECO:0000256|ARBA:ARBA00021623};
DE Flags: Fragment;
GN Name=ppsA {ECO:0000313|EMBL:ACE07068.1};
OS Pseudomonas aeruginosa.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=287 {ECO:0000313|EMBL:ACE07068.1};
RN [1] {ECO:0000313|EMBL:ACE07068.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ocean-224 {ECO:0000313|EMBL:ACE07068.1};
RX PubMed=18757570; DOI=10.1128/AEM.02322-07;
RA Khan N.H., Ahsan M., Yoshizawa S., Hosoya S., Yokota A., Kogure K.;
RT "Multilocus sequence typing and phylogenetic analyses of Pseudomonas
RT aeruginosa Isolates from the ocean.";
RL Appl. Environ. Microbiol. 74:6194-6205(2008).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837}.
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DR EMBL; EU590736; ACE07068.1; -; Genomic_DNA.
DR AlphaFoldDB; B6CXR2; -.
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; IPR000121; PEP_util_C.
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; PF02896; PEP-utilizers_C; 1.
DR Pfam; PF01326; PPDK_N; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 3: Inferred from homology;
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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..58
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 97..169
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 196..298
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACE07068.1"
FT NON_TER 300
FT /evidence="ECO:0000313|EMBL:ACE07068.1"
SQ SEQUENCE 300 AA; 32646 MW; 60FAA0247C3CFF82 CRC64;
RFALSDAEVT ELAKQAMIIE KHYGRPMDIE WAKDGDDGKL YIVQARPETV KSRASATVME
RYLLKEKGTV LVEGRAIGQR IGAGPVKVIN DVSEMDKVQP GDVLVSDMTD PDWEPVMKRA
SAIVTNRGGR TCHAAIIARE LGIPAVVGCG NATQILQDGQ GVTVSCAEGD TGFIFEGELG
FDVRKNSVDA MPDLPFKIMM NVGNPDRAFD FAQLPNEGVG LARLEFIINR MIGVHPKALL
NFAGLPADIK ESVEKRIAGY PDPVGFYVEK LVEGISTLAA AFWPKKVIVR LSDFKSNENA
//
