ID I0ERX5_HELCM Unreviewed; 806 AA.
AC I0ERX5;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 56.
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 OrderedLocusNames=HCD_03390 {ECO:0000313|EMBL:AFI05694.1};
OS Helicobacter cetorum (strain ATCC BAA-540 / MIT 99-5656).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1163745 {ECO:0000313|EMBL:AFI05694.1, ECO:0000313|Proteomes:UP000005013};
RN [1] {ECO:0000313|Proteomes:UP000005013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-540 / MIT 99-5656 {ECO:0000313|Proteomes:UP000005013};
RA Kersulyte D., Berg D.E.;
RT "Complete genome sequence of Helicobacter cetorum strain MIT 99-5656.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFI05694.1, ECO:0000313|Proteomes:UP000005013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-540 / MIT 99-5656 {ECO:0000313|Proteomes:UP000005013};
RX PubMed=24358262;
RA Kersulyte D., Rossi M., Berg D.E.;
RT "Sequence Divergence and Conservation in Genomes ofHelicobacter cetorum
RT Strains from a Dolphin and a Whale.";
RL PLoS ONE 8:E83177-E83177(2013).
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; CP003481; AFI05694.1; -; Genomic_DNA.
DR RefSeq; WP_014659203.1; NC_017735.1.
DR AlphaFoldDB; I0ERX5; -.
DR STRING; 1163745.HCD_03390; -.
DR KEGG; hcm:HCD_03390; -.
DR PATRIC; fig|1163745.3.peg.722; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG1080; Bacteria.
DR HOGENOM; CLU_007308_6_2_7; -.
DR OrthoDB; 9765468at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000005013; 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:AFI05694.1};
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 485..800
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
SQ SEQUENCE 806 AA; 90716 MW; 7E938BEA3D424664 CRC64;
MRYIKFFKEL NNKDVNLVGG KNASIGEMFQ ELVPIGIKVP DGFAITSEAY WYLLEQGGVK
QKIIELLENV DATEIDVLKV RSKKIRELIF GTPFPTDLRD EIFQAYEILS QQYDMKEADV
AVRSSATAED LPDASFAGQQ DTYLNIKGKT ELVHYIKSCI ASLFTDRAIS YRASRGFDHL
KVALSVGVQK MVRADKSSAG VMFSIDTETG FKDAVFITSA WGLGENVVGG MVNPDEFYVF
KPTLEQNKRP IIKRQLGNKF QKMVYAPRGS EHPTKNIETT QKELQSFSLS DEDVLILAKY
AIEIEKHYTK EAGTYRPMDI EWAKDGNSGE IFIVQARPET VQSQKNKNNN QVFEKFKFKN
PNEKKEIILQ GRAIGNKIGS GKVRIINDLE HMNSFKEGEI LVTDNTDPDW EPCMKKASAV
ITNRGGRTCH AAIVAREIGV PAIVGASGAT DRLYTGMEIT VSCAEGEEGY VYAGIYEHEI
ERVELSCLEE TKTKIYVNIG NPEKAFGFSQ LPNHGVGLAR MEMIILNQIK AHPLALVDLH
HKKPVKEKNE IENLMAGYAN PKDFFVKKIA EGIGMISAAF YPKPVIVRTS DFKSNEYMRM
LGGSSYEPHE ENPMLGYRGA SRYYSERYNE AFSWECEALA LVREEMGLTN MKIMIPFLRT
IEEGKKVLEI LRKNNLESGK NGLEIYIMCE LPINVILADD FLSLFDGFSI GSNDLTQLTL
GVDRDSELVS HVFDERNPAM LEMFKRAIEA CKRHHKYCGI CGQAPSDYPE VAEFLVKESI
TSISLNPDSV ISTWNAIAKL EKELKR
//
