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Database: UniProt
Entry: K7Y446_HELPX
LinkDB: K7Y446_HELPX
Original site: K7Y446_HELPX 
ID   K7Y446_HELPX            Unreviewed;       812 AA.
AC   K7Y446;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
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   ORFNames=HPAKL117_00585 {ECO:0000313|EMBL:AFX90534.1};
OS   Helicobacter pylori Aklavik117.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1055531 {ECO:0000313|EMBL:AFX90534.1, ECO:0000313|Proteomes:UP000010079};
RN   [1] {ECO:0000313|EMBL:AFX90534.1, ECO:0000313|Proteomes:UP000010079}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Aklavik117 {ECO:0000313|EMBL:AFX90534.1};
RX   PubMed=25883278;
RA   Kersulyte D., Bertoli M.T., Tamma S., Keelan M., Munday R., Geary J.,
RA   Veldhuyzen van Zanten S., Goodman K.J., Berg D.E.;
RT   "Complete Genome Sequences of Two Helicobacter pylori Strains from a
RT   Canadian Arctic Aboriginal Community.";
RL   Genome Announc. 3:0-0(2015).
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; CP003483; AFX90534.1; -; Genomic_DNA.
DR   RefSeq; WP_015085371.1; NC_019560.1.
DR   AlphaFoldDB; K7Y446; -.
DR   KEGG; hpya:HPAKL117_00585; -.
DR   PATRIC; fig|1055531.3.peg.122; -.
DR   HOGENOM; CLU_007308_6_2_7; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000010079; 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   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:AFX90534.1};
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   812 AA;  91206 MW;  4560FD916C23576F CRC64;
     MRYIKFFKEL NNKNVNLVGG KNASIGEMFQ ELVPIGIKVP DGFAITSEAY WYLLEQGGAK
     QKIIELLENV DATEIDVLKI RSKQIRELIF GTPFPSDLRD EIFQAYEILS QQYNMKEADV
     AVRSSATAED LPDASFAGQQ DTYLNIKGKT ELIHYIKSCL ASLFTDRAIS YRASRGFDHL
     KVALSVGVQK MVRADKGSAG VMFSIDTETG FKDAVFITSA WGLGENVVGG TINPDEFYVF
     KPTLEQNKRP IIKRQLGNKT QKMVYAPRGS EHPTRNIKTT KKEWQSFSLS DEDVLILAKY
     AIEIEKHYSK EAKQYRPMDI EWAKDGDSGE IFIVQARPET VQSQKTKEES QVFEKFKFKN
     PNEKKEIILQ GRAIGSKIGS GKVRIINDLE HMNSFKEGEI LVTDNTDPDW EPCMKKASAV
     ITNRGGRTCH AAIVAREIGV PAIVGVSGAT DSLYTGMEIT VSCAEGEEGY VYAGIYEHEI
     ERVELSNMQE TQTKIYINIG NPEKAFGFSQ LPNHGVGLAR MEMIILNQIK AHPLALVDLH
     HKKSVKEKNE IENLMAGYAN PKDFFVRKIA EGIGMISAAF YPKPVIVRTS DFKSNEYMRM
     LGGSSYEPNE ENPMLGYRGA SRYYSESYNE AFSWECEALA LVREEMGLTN MKVMIPFLRT
     IEEGKKVLEI LRKNNLESGK NGLEIYIMCE LPVNVILADD FLSLFDGFSI GSNDLTQLTL
     GVDRDSELVS HVFDERNEAM LKMFKKAIEA CKRHNKYCGI CGQAPSDYPE VTEFLVKEGI
     TSISLNPDSV IPTWNAVAKL EKELKDHGLT AH
//
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