GenomeNet

Database: UniProt
Entry: A0A0S7WXC3_9BACT
LinkDB: A0A0S7WXC3_9BACT
Original site: A0A0S7WXC3_9BACT 
ID   A0A0S7WXC3_9BACT        Unreviewed;       795 AA.
AC   A0A0S7WXC3;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=AMJ47_03090 {ECO:0000313|EMBL:KPJ54810.1};
OS   Parcubacteria bacterium DG_72.
OC   Bacteria; Candidatus Parcubacteria.
OX   NCBI_TaxID=1703764 {ECO:0000313|EMBL:KPJ54810.1, ECO:0000313|Proteomes:UP000051392};
RN   [1] {ECO:0000313|EMBL:KPJ54810.1, ECO:0000313|Proteomes:UP000051392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG_72 {ECO:0000313|EMBL:KPJ54810.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(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:KPJ54810.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LJND01000005; KPJ54810.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S7WXC3; -.
DR   STRING; 1703764.AMJ47_03090; -.
DR   PATRIC; fig|1703764.3.peg.308; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000051392; 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:KPJ54810.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000854}.
FT   DOMAIN          20..354
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          393..464
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   DOMAIN          486..793
FT                   /note="PEP-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02896"
SQ   SEQUENCE   795 AA;  89506 MW;  BD173C1F16397659 CRC64;
     MLKKLRHILW YREINKDDGE LVGGKNASLG EMHRHLTKQG INLPQGFCLT SRAFWYFLKV
     NKIDRKIKQL FSKFNPKDIK SLQQTGKAVR ELILNSSFPK DLEKKILRAY WKLSKKYPDP
     EKSRRGGTNG ASVAVRSSAT AEDLATASFA GQMETFLNVK GEEDLLEACK KCIASLFTDR
     SIAYREEKGF DHLKIALSVG VQKMVRSDLG SSGVMFTLDT ETGFENVILI NSIWGIGEMV
     VKGKITPDEF YVHKPTLEKG FDSIIVKNLG RKNRKYIYAR KGGLKEVKVK DSDQLKFSLT
     DKDIITLAKW ALRIERLYES HQDIEWAKDG KTKELFIVQS RPETVHTPSE AKKYVEYKVK
     SKKAPILTGI AIGDKIGIGK VRIIPDVSEI ADFKPGEVLV TTMTDPDWVP IMRIASAIVT
     DEGGKTAHAA IVSRELGIPA IVGTKTATKL LKTGQEVTVD CTQGLDGRIF QGKVPFSQKE
     YDLKRVPKLK TKIMMNIGAP DIAFKTSFLP NSGVGLAREE FIIAEKIRVH PLALYHFHKL
     KSKKLKKQIQ EITVEHKDKK EYFVKELAEG IAQIAAAFYP KEVIVRFSDF KTNEYRNLIG
     GDLYEKEENN PMLGFRGSSR YIDESFQPAF QMECKAIKRV REVFGLENVS VMVPFCRTVE
     EGEKVLKLIK KFGLKDLKVY VMCEIPSNVI LADDFLKIFD GMSIGSNDLT QLVLGLDRDN
     ANIAYIGNEM NKAVKDMIAK TIKACKEKNK YCGICGQAPS DIPEFAEFLQ KQGIESMSLN
     PDTVVKTIMN LAKSK
//
DBGET integrated database retrieval system