ID J0KG50_9BURK Unreviewed; 600 AA.
AC J0KG50;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Phosphoenolpyruvate synthase {ECO:0000256|ARBA:ARBA00021623};
DE EC=2.7.9.2 {ECO:0000256|ARBA:ARBA00011996};
DE AltName: Full=Pyruvate, water dikinase {ECO:0000256|ARBA:ARBA00033470};
DE Flags: Fragment;
GN ORFNames=PMI14_02733 {ECO:0000313|EMBL:EJE52635.1};
OS Acidovorax sp. CF316.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1144317 {ECO:0000313|EMBL:EJE52635.1, ECO:0000313|Proteomes:UP000004811};
RN [1] {ECO:0000313|EMBL:EJE52635.1, ECO:0000313|Proteomes:UP000004811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF316 {ECO:0000313|EMBL:EJE52635.1,
RC ECO:0000313|Proteomes:UP000004811};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
CC -!- FUNCTION: Catalyzes the phosphorylation of pyruvate to
CC phosphoenolpyruvate. {ECO:0000256|ARBA:ARBA00002988}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837}.
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:EJE52635.1}.
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DR EMBL; AKJX01000111; EJE52635.1; -; Genomic_DNA.
DR RefSeq; WP_007854710.1; NZ_AKJX01000111.1.
DR AlphaFoldDB; J0KG50; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000004811; 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; 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 SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyruvate {ECO:0000313|EMBL:EJE52635.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004811};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 23..353
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 390..462
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 485..591
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT NON_TER 600
FT /evidence="ECO:0000313|EMBL:EJE52635.1"
SQ SEQUENCE 600 AA; 64740 MW; 9D7830A143815008 CRC64;
MSALFSPTAL VVPFENLRMT DVESVGGKNA SLGEMISQLP EGVRVPTGFA TTAHAFREFL
AHDGLADKIS AKLASLDTED VRALAKVGAE IRALVEAQPF PADLQKAIGE AFATLSEGNP
QASFAVRSSA TAEDLPDASF AGQQETFLNV VGIDDVLHKM KEVFASLYND RAISYRVHKG
FAHDVVALSA GVQRMVRSDL GAAGVMFTID TESGFEEVVF ITSSYGLGET VVQGAVNPDE
FYVHKPTLKA GKKAVIRRNL GSKLVQMVFS SAEEKAASGK LVKTTDVPTE QRNRYSLSDA
DVQQLAHYAL VIEQHYGRPM DIEWGKDGTD GLLYILQARP ETVKSQSKGQ AEMRYKLKGQ
GTVLAEGRAI GQKIGTGPVR LVHNISEMDK VQPGDVLVTD MTDPNWEPVM KRASAIVTNR
GGRTCHAAII ARELGIPAVV GCGDATELLK DGTLVTVSCS EGDTGRIYDG LLETEITEVQ
RGEMPSIQTK IMMNVGNPQL AFDFCQLPNE GVGLARLEFI INNNIGVHPK AILDYPQIDA
DLKKAVESVA RGHASPRAFY VDKVAEGVAT IAAAFYPKPV IVRLSDFKSN EYRKLIGGSR
//
