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
//