ID A0A0J0YQ27_9NEIS Unreviewed; 796 AA.
AC A0A0J0YQ27;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=PL75_09145 {ECO:0000313|EMBL:KLT72237.1};
OS Neisseria arctica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=1470200 {ECO:0000313|EMBL:KLT72237.1, ECO:0000313|Proteomes:UP000036027};
RN [1] {ECO:0000313|EMBL:KLT72237.1, ECO:0000313|Proteomes:UP000036027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH1503 {ECO:0000313|EMBL:KLT72237.1,
RC ECO:0000313|Proteomes:UP000036027};
RA Hansen C.M., Hueffer K., Choi S.C.;
RT "Genome of a novel goose pathogen.";
RL Submitted (NOV-2014) 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:KLT72237.1}.
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DR EMBL; JTDO01000016; KLT72237.1; -; Genomic_DNA.
DR RefSeq; WP_047761631.1; NZ_JTDO01000016.1.
DR AlphaFoldDB; A0A0J0YQ27; -.
DR STRING; 1470200.PL75_09145; -.
DR PATRIC; fig|1470200.3.peg.799; -.
DR OrthoDB; 9765468at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000036027; 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 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:KLT72237.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000036027};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000854}.
FT DOMAIN 18..352
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 387..458
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 482..788
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
SQ SEQUENCE 796 AA; 87024 MW; 69B60DCFC8BAB1A4 CRC64;
MSANYVIWFE NLRMTDVESV GGKNASLGEM ISQLTEKGVR VPGGFATTAD AYRAFLAHNG
LNERISAALA TLDVEDVAEL ARVGKQIREW ILETPFPEQL DADIQTAWEK MVAEAGTDQI
SVAVRSSATA EDLPDASFAG QQETFLNING LENVKEAMKH VFASLYNDRA ISYRVHKGFA
HDVVALSAGV QRMVRSDSGA AGVMFSIDTE SGFDQVVFVT SSYGLGETVV QGAVNPDEFY
VHKPTLQAGK PAILRKTLGS KLIKMTFTDQ AQAGKSVQVV DVPENERKQF SISDEEITEL
AKYAVIIEQH YGRPMDIEWG RDGVDGKLYI LQARPETVKS QETGGRSLRR YRIDQKSTVL
CEGRAIGQKV GQGVVRLVKD ASEMETVKPG DVLVTDMTDP DWEPVMKRAA AIVTNRGGRT
CHAAIIAREL GIPAVVGCGN ATEVLSEGQE VTVSCAEGDT GLIYEGLLNV EVNDVALDNM
PKSPVKIMMN VGNPELAFSF ASLPSEGIGL ARMEFIINRQ IGIHPKALLE FDKQDEDLKA
EISERIAGYA SPVSFFVDKI AEGVSTLAAS VYPRKVIVRM SDFKSNEYAG LIGGNLYEPH
EENPMLGFRG AARYVSEDFK DCFALECQAL KRVRDDMGLT NVEIMIPFVR TLSEAEQVVK
ALKENGLERG KNGLRLIMMC EVPSNALLAE QFLQYFDGFS IGSNDMTQLT LGLDRDSGGP
IASTFDERNA AVKVMLHLAI SACRKHNKYV GICGQGPSDH PDFAKWLVEE GIDTVSLNPD
TVIETWLYLA KEVAAK
//
