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Database: UniProt
Entry: A0A246WUT6_9BURK
LinkDB: A0A246WUT6_9BURK
Original site: A0A246WUT6_9BURK 
ID   A0A246WUT6_9BURK        Unreviewed;       805 AA.
AC   A0A246WUT6;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=CEJ42_01570 {ECO:0000313|EMBL:OWY30792.1};
OS   Herbaspirillum robiniae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herbaspirillum.
OX   NCBI_TaxID=2014887 {ECO:0000313|EMBL:OWY30792.1, ECO:0000313|Proteomes:UP000197596};
RN   [1] {ECO:0000313|EMBL:OWY30792.1, ECO:0000313|Proteomes:UP000197596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HZ10 {ECO:0000313|EMBL:OWY30792.1,
RC   ECO:0000313|Proteomes:UP000197596};
RA   Fan M., Lin Y.;
RT   "Herbaspirillum phytohormonus sp. nov., isolated from the root nodule of
RT   Robinia pseudoacacia in lead-zinc mine.";
RL   Submitted (JUN-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:OWY30792.1}.
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DR   EMBL; NJGU01000001; OWY30792.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A246WUT6; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000197596; 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:OWY30792.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000854}.
FT   DOMAIN          25..364
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          398..469
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   DOMAIN          495..803
FT                   /note="PEP-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02896"
SQ   SEQUENCE   805 AA;  87526 MW;  5F339F4102C7EE74 CRC64;
     MSNAVNTQGA VYVASFETLR MTDVESVGGK NASLGEMISQ LAGAGVRVPG GFATTAQAFR
     DFLEHSADGG QTLAARIAAR LEGLDIDDVR SLAAAGAEIR QWIVDTPFQP RLDQEIRSFY
     DKLVADSTSE MSFAVRSSAT AEDLPDASFA GQQETFLNVV GIDNVLEAMK HVFASLYNDR
     AISYRVHKGF THAEVALSAG VQRMVRSDLG AAGVMFTIDT ESGFKDVVFI TSSYGLGETV
     VQGAVNPDEY YVHKPMLELG KQPVIRRNLG SKLIKMEFTG EAKAGRSVKT VDVPVELRNR
     YSLTDAEVVE LAKYATIIEK HYQRPMDIEW GKDGRDGKLY ILQARPETVK SQQKATDAQQ
     RFKLKSSGTV LATGRAIGQK IGAGPVRVIN DPAEMERVQP GDVLVADMTD PNWEPVMKRA
     SAIVTNRGGR TCHAAIIARE LGVPAVVGCG DATDVLKDGT LVTVSCAEGD EGKIYDGLLE
     TEVTEVARGE LPEIPLKVMM NVGNPQLAFD FQSIPNGGVG LARLEFIINN NIGVHPKAIL
     EYPNIDNDLK KAVESVARGH ASPKAFYVDK LAEGIATIAA AFWPKPVIVR LSDFKSNEYK
     KLIGGSRYEP DEENPMLGFR GAARYLADDF AEAFQMECQA MKRVREDMGL TNVEVMVPFV
     RTLGQAEKVI GLLGKYGLKR GENGLRVIMM CEVPSNAILA EQFLEHFDGF SIGSNDLTQL
     TLGLDRDSGM ELLAADFDER DPALQALLSK VISTCLAKGK YVGICGQGPS DHPDFAEWLM
     AQGIESISLN PDTVIDTWQH LAKKK
//
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