ID A0A0G0W196_9BACT Unreviewed; 840 AA.
AC A0A0G0W196;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=UU61_C0030G0004 {ECO:0000313|EMBL:KKS06800.1};
OS Parcubacteria group bacterium GW2011_GWB1_41_4.
OC Bacteria.
OX NCBI_TaxID=1618867 {ECO:0000313|EMBL:KKS06800.1, ECO:0000313|Proteomes:UP000034734};
RN [1] {ECO:0000313|EMBL:KKS06800.1, ECO:0000313|Proteomes:UP000034734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(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}.
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:KKS06800.1}.
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DR EMBL; LCBH01000030; KKS06800.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0W196; -.
DR PATRIC; fig|1618867.3.peg.390; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000034734; 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:KKS06800.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000854}.
FT DOMAIN 26..367
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 409..478
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 502..834
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
SQ SEQUENCE 840 AA; 93214 MW; D06B9BBE9E2C17B7 CRC64;
MGKRQSRENK NLWVFWFKEL TIKDVPLVGG KNAALGEMYQ ELTPLGVKIP NGYAVSAEAF
RYFVKFNNLG DRISRALKGL DTHDVSDLAK RGKIVRSLIL SGYFPEDLKI QIFSYYHQLS
KQYKTNNVDV AVRSSATAED LPGASFAGQQ ETYLNIRGEK VLLEATKKCF ASLFTDRAIS
YRVDKGFDQM SVALSVGVQK MVRSDKAVSG VAFTIDTETG FSNAVVIDSV YGLGEMIVQG
KVDPDEFIVF KPSLANGKYP IINKKLADKN VKMIYSSTAL GTSASAGINK KPVKIVPVPE
SQRKSFSLTD KEVISLAQDC IKVEKHFSKK HGKYMPMDLE WAKDGLTNEL FVVQARPETI
HAGKKETVFE EYSLISRPQK SLISGIPIGK EIVSGKVRVI KSVKDIHTFK PGEVLVTEIT
DPDWEPIMKI ASAIVTDKGG RTSHAAIVSR ELGVQCIVGS GDATRVLKTG QTVTVDCSSD
EAGRVYSGVL KFKIQKHSLK NLPKIKTKIS LNIGSPDEAF RYHSLPVTGV GLGRLEFIIA
SKIQIHPNVL IDYEKIKSGK KKFFGHDRAE INSILKKIEA LTVGYKDKKQ YYVDKLAEGI
AMIASAFWPY EVIIRFSDFK TNEYNTLIGG PLYEPKEENP MIGWRGSSRY YDPKFSEAFG
LECRAMKKVR ETMGLVNVVP MIVFCRTVEE AKKVLAEMAK HGLKRGSRPV RQAQGKQLQP
LKVYMMCEIP SNVILIDDFL KLFDGFSIGS NDLAQLTLGL DRDSGIIAHI ANENNQAVKD
LIKIVIQKCN QKKKYIGICG QAPSDYPEFA IFLKKLGIGA MSLNADSVIK TLIALGKTNN
//
