ID G0ZF08_9ENTR Unreviewed; 165 AA.
AC G0ZF08;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Phosphoenolpyruvate synthase {ECO:0000256|ARBA:ARBA00021623};
DE Flags: Fragment;
GN Name=ppsA {ECO:0000313|EMBL:AEL99377.1};
OS Cronobacter condimenti 1330.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=1073999 {ECO:0000313|EMBL:AEL99377.1};
RN [1] {ECO:0000313|EMBL:AEL99377.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=1330 {ECO:0000313|EMBL:AEL99377.1};
RX PubMed=22661070; DOI=10.1099/ijs.0.032292-0;
RA Joseph S., Cetinkaya E., Drahovska H., Levican A., Figueras M.J.,
RA Forsythe S.J.;
RT "Cronobacter condimenti sp. nov., isolated from spiced meat, and
RT Cronobacter universalis sp. nov., a species designation for Cronobacter sp.
RT genomospecies 1, recovered from a leg infection, water and food
RT ingredients.";
RL Int. J. Syst. Evol. Microbiol. 62:1277-1283(2012).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; JF268312; AEL99377.1; -; Genomic_DNA.
DR AlphaFoldDB; G0ZF08; -.
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; 3.50.30.10; 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; SSF56059; Glutathione synthetase ATP-binding domain-like; 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:AEL99377.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..73
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 112..165
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEL99377.1"
FT NON_TER 165
FT /evidence="ECO:0000313|EMBL:AEL99377.1"
SQ SEQUENCE 165 AA; 18223 MW; 98E9A5255E851A91 CRC64;
HGKQVRIEDV PQADRDLFCI TPEEVQELAK QAVQIEKHYG RPMDIEWAKD GHTGKLFIVQ
ARPETVRSRG QVMERYMLHS QGNVVAEGRA IGHRIGAGTV KVIHDISEMN RIQPGDVLVT
DMTDPDWEPI MKKAAAIVTN RGGRTCHAAI IARELGIPAV VGCGD
//
