ID I9YVP7_HELPX Unreviewed; 808 AA.
AC I9YVP7;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 45.
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:EJC32985.1};
GN ORFNames=HPHPP15B_0360 {ECO:0000313|EMBL:EJC32985.1};
OS Helicobacter pylori Hp P-15b.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=992108 {ECO:0000313|EMBL:EJC32985.1, ECO:0000313|Proteomes:UP000004543};
RN [1] {ECO:0000313|EMBL:EJC32985.1, ECO:0000313|Proteomes:UP000004543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hp P-15b {ECO:0000313|EMBL:EJC32985.1,
RC ECO:0000313|Proteomes:UP000004543};
RA Blanchard T.G., Czinn S.J., McCracken C., Abolude K., Maroo A.,
RA Santana-Cruz I., Tallon L.J., Ficke F.W.F.;
RT "Genome sequence of Helicobacter pylori Hp P-15b.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJC32985.1}.
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DR EMBL; AKQJ01000002; EJC32985.1; -; Genomic_DNA.
DR RefSeq; WP_001269083.1; NZ_AKQJ01000002.1.
DR AlphaFoldDB; I9YVP7; -.
DR PATRIC; fig|992108.3.peg.346; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000004543; Unassembled WGS sequence.
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 PRINTS; PR01736; PHPHTRNFRASE.
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:EJC32985.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000854}.
FT DOMAIN 16..351
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 395..466
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 488..800
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
SQ SEQUENCE 808 AA; 90836 MW; 35280C71B05DEA5B CRC64;
MRYIKFFKEL NNKNVNLVGG KNASIGEMFQ ELVPIGIKVP DGFAITSEAY WYLLEQGGAK
QKIIELLENV DATEIDVLKI RSKQIRELIF GTPFPSDLRD EIFQAYEILS QQYHMKEADV
AVRSSATAED LPDASFAGQQ DTYLNIKGKT ELIHYIKSCL ASLFTDRAIS YRASRGFDHL
KVALSVGVQK MVRADKGSAG VMFSIDTETG FKDAVFITSA WGLGENVVGG TINPDEFYVF
KPTLEQNKRP IIKRQLGNKT QKMVYAPRGS EHPTRNIKTT KKEWQSFSLS DEDVLILAKY
AIEIEKHYSK EAKQYRPMDI EWAKDGDSGE IFIVQARPET VQSQKSKEEN QVFEKFKFKN
PNEKKEIILQ GRAIGSKIGS GKVRIINDLE HMNSFKEGEI LVTDNTDPDW EPCMKKASAV
ITNRGGRTCH AAIVAREIGV PAIVGVSGAT DSLYTGMEIT VSCAEGEEGY VYAGIYEHEI
ERVELSNMQE TQTKIYINIG NPEKAFSFSQ LPNHGVGLAR MEMIILNQIK AHPLALVDLH
HKKSVKEKNE IENLMAGYAN PKDFFVKKIA EGIGMISAAF YPKPVIVRTS DFKSNEYMRM
LGGSSYEPNE ENPMLGYRGA SRYYSESYNE AFSWECEALA LVREEMGLTN MKVMIPFLRT
IEEGKKVLEI LRKNNLESGK NGLEIYIMCE LPVNVILADD FLSLFDGFSI GSNDLTQLTL
GVDRDSELVS HVFDERNEAM LKMFKKAIEA CKRHNKYCGI CGQAPSDYPE VTEFLVKEGI
TSISLNPDSV IPTWNAVAKL EKELKDHA
//
