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Database: UniProt
Entry: E1SB65_PANVC
LinkDB: E1SB65_PANVC
Original site: E1SB65_PANVC 
ID   E1SB65_PANVC            Unreviewed;       793 AA.
AC   E1SB65;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 71.
DE   RecName: Full=Phosphoenolpyruvate synthase {ECO:0000256|ARBA:ARBA00021623, ECO:0000256|PIRNR:PIRNR000854};
DE            Short=PEP synthase {ECO:0000256|PIRNR:PIRNR000854};
DE            EC=2.7.9.2 {ECO:0000256|ARBA:ARBA00011996, ECO:0000256|PIRNR:PIRNR000854};
DE   AltName: Full=Pyruvate, water dikinase {ECO:0000256|ARBA:ARBA00033470, ECO:0000256|PIRNR:PIRNR000854};
GN   Name=ppsA {ECO:0000313|EMBL:ADO09343.1};
GN   OrderedLocusNames=Pvag_1150 {ECO:0000313|EMBL:ADO09343.1};
OS   Pantoea vagans (strain C9-1) (Pantoea agglomerans (strain C9-1)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=712898 {ECO:0000313|EMBL:ADO09343.1, ECO:0000313|Proteomes:UP000006631};
RN   [1] {ECO:0000313|EMBL:ADO09343.1, ECO:0000313|Proteomes:UP000006631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C9-1 {ECO:0000313|EMBL:ADO09343.1,
RC   ECO:0000313|Proteomes:UP000006631};
RX   PubMed=20952567; DOI=10.1128/JB.01122-10;
RA   Smits T.H., Rezzonico F., Kamber T., Goesmann A., Ishimaru C.A.,
RA   Stockwell V.O., Frey J.E., Duffy B.;
RT   "The genome sequence of the biocontrol agent Pantoea vagans strain C9-1.";
RL   J. Bacteriol. 192:6486-6487(2010).
CC   -!- FUNCTION: Catalyzes the phosphorylation of pyruvate to
CC       phosphoenolpyruvate. {ECO:0000256|ARBA:ARBA00002988,
CC       ECO:0000256|PIRNR:PIRNR000854}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate +
CC         phosphoenolpyruvate; Xref=Rhea:RHEA:11364, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58702, ChEBI:CHEBI:456215; EC=2.7.9.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001518,
CC         ECO:0000256|PIRNR:PIRNR000854};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|PIRNR:PIRNR000854};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|ARBA:ARBA00004742, ECO:0000256|PIRNR:PIRNR000854}.
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007837, ECO:0000256|PIRNR:PIRNR000854}.
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DR   EMBL; CP002206; ADO09343.1; -; Genomic_DNA.
DR   RefSeq; WP_013357692.1; NC_014562.1.
DR   AlphaFoldDB; E1SB65; -.
DR   KEGG; pva:Pvag_1150; -.
DR   eggNOG; COG0574; Bacteria.
DR   eggNOG; COG1080; Bacteria.
DR   HOGENOM; CLU_007308_6_2_6; -.
DR   OMA; LETWFFL; -.
DR   OrthoDB; 9765468at2; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000006631; Chromosome.
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:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
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; IPR013815; ATP_grasp_subdomain_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; IPR023151; PEP_util_CS.
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   NCBIfam; TIGR01418; PEP_synth; 1.
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   PIRSF; PIRSF000854; PEP_synthase; 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; PS00742; PEP_ENZYMES_2; 1.
DR   PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000854};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000854};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR000854};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR000854};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR000854}; Pyruvate {ECO:0000313|EMBL:ADO09343.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000854}.
FT   DOMAIN          21..347
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          385..456
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   DOMAIN          483..789
FT                   /note="PEP-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02896"
SQ   SEQUENCE   793 AA;  87258 MW;  21BFC8669D57A514 CRC64;
     MSTQEQPLVL WYNQLGMHDV DRVGGKNASL GEMITNLSSL GVSVPNGFAT TSYAFNLFLD
     QSGLNQRIYA LLDETDIDDV DALAKAGKQI RQWVVETPFL PELESAILDA YQQLSADDAA
     ASFAVRSSAT AEDMPDASFA GQQETFLNVQ GIDAVMVAVK HVFASLFNDR AISYRVHQGY
     DHRGVALSAG IQRMVRSDLA SSGVMFTIDT ESGFDQVVFI TAALGLGEMV VQGAVNPDEF
     YVHKPTLAAD RPSIVRRNMG SKKVRMVYAD SQAHGEQVRI EDVPEAERDR FCLNDEEVQA
     LAKQAVLIEQ HYQRPMDIEW AKDGHTGKLF IVQARPETVR SNGQVMERYT LQGQGSVVVE
     GRAIGHRIGA GVVKVIHDIS EMNRIEKGDV LVTDMTDPDW EPIMKKASAI VTNRGGRTCH
     AAIIARELGI PAVVGCGDAT DRLREGHQVT VSCAEGDTGY VYDQLLDFDV TSSQVDSLPE
     LPLKIMMNVG NPDRAFDFAC LPNEGVGLAR LEFIINRMIG VHPKALLEFE QQTPALQQQI
     RKMMKGFDNP VEFYIARLTE GIATLGAAFA PKRVIVRLSD FKTNEYANLV GGERYEPEEE
     NPMLGFRGAG RYVADNFRDC FALECEAVKR VRNEMGLTNV EIMVPFVRTV DQAQAVVEEL
     ARQGLKRGEN GLKIIMMCEI PSNALLAEQF LQHFDGFSIG SNDMTQLTLG LDRDSGVVSA
     LFDERNEAVK ALLSMAIRAA KQQGKYVGIC GQGPSDHQDF AAWLMEEGID SLSLNPDTVV
     ETWVSLAQLN KTA
//
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