ID A0A2A2GU16_9HELI Unreviewed; 809 AA.
AC A0A2A2GU16;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=B9T66_00215 {ECO:0000313|EMBL:PAV00857.1};
OS Helicobacter sp. TUL.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1848928 {ECO:0000313|EMBL:PAV00857.1, ECO:0000313|Proteomes:UP000218502};
RN [1] {ECO:0000313|EMBL:PAV00857.1, ECO:0000313|Proteomes:UP000218502}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUL {ECO:0000313|EMBL:PAV00857.1,
RC ECO:0000313|Proteomes:UP000218502};
RA Van Der Mee-Marquet N., Benejat L., Diene S.M., Gaia N., Cherkaoui A.,
RA Lemaignen A., Ducournau A., Lacomme S., Gontier E., Bernard L., Megraud F.,
RA Goudeau A., Lehours P., Francois P.;
RT "Helicobacter caesarodunum: a novel human pathogen identified in a
RT bloodstream infection.";
RL Submitted (APR-2017) 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:PAV00857.1}.
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DR EMBL; NESU01000001; PAV00857.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2GU16; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000218502; 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; 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; 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:PAV00857.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000218502};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000854}.
FT DOMAIN 16..352
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 396..467
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 491..803
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
SQ SEQUENCE 809 AA; 90655 MW; A0A6D09C204E3760 CRC64;
MKYIKFFKEL NNKDVPIVGG KNASIGEMFQ ELVSEGIKVP NGFAITSDAY WYLLDSGGIR
HTIEELLKGV DVTEIDVLKT RSKKIRELIF GTPFPDDLRE EIFQAYKILS EEYGMKETDV
AVRSSATAED LPDASFAGQQ DTYLSVRGKS ELIHYIKSCF ASLFTDRAVS YRASRGFDHF
KVALSVGVQK MVRADKGSAG VMFSIDTETG FKDAVFITAA WGLGENVVGG TVNPDEFYVF
KPTLKDGKRP IIKRQLGHKH QKMVYAPRGS EHPTKNIKTT QKELKTFAIT DEDILTLARY
AIRIEEHYTK EAGEYRPMDM EWAKDGESGE IFIVQARPET VQSQKFKNQT GNRLEEFTFT
NPSESREVII TGRAIGNKIG AGKVRIINDL EHMNTFKEGE ILVTDNTDPD WEPVMKKAAA
VITNRGGRTC HAAIVAREIG VPAIVGAVGA TDRLYTGMEI TVSCAEGEEG YVYAGICDYE
VKSVELDNLG ETKTKIYMNV GNPEKAFGFA KLPNSGVGLA RMELIVLNQI KAHPLALLDI
QNGKDKDIKE RAEIEKLMAG YESPKDFFVK KIAEGIGMIC SAFYPNPVIV RTSDFKSNEY
RGMVAGTYYE PQEENPMLGY RGASRYYSDL YRVAFEWECE ALAMVRDEMG LNNMKVMIPF
LRTPEEGKKV LEIMRRNGLE SGRNGLEIYV MCELPVNVIL ADEFLSMFDG YSIGSNDLTQ
LTLGVDRDGQ LVTHIFDERN PAMFEMFRQA IAACKRHNKY CGICGQAPSD YPEVTEFLVK
EGISSISLNP DSVVKTWRFV AELEKKLNK
//
