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
//