ID A0A1G5A2Y2_9BURK Unreviewed; 670 AA.
AC A0A1G5A2Y2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
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};
GN ORFNames=SAMN03159363_4182 {ECO:0000313|EMBL:SCX72202.1};
OS Variovorax sp. EL159.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1566270 {ECO:0000313|EMBL:SCX72202.1, ECO:0000313|Proteomes:UP000199507};
RN [1] {ECO:0000313|EMBL:SCX72202.1, ECO:0000313|Proteomes:UP000199507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EL159 {ECO:0000313|EMBL:SCX72202.1,
RC ECO:0000313|Proteomes:UP000199507};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FMUJ01000004; SCX72202.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5A2Y2; -.
DR STRING; 1566270.SAMN03159363_4182; -.
DR Proteomes; UP000199507; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0008986; F:pyruvate, water dikinase activity; IEA:InterPro.
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 InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR006319; PEP_synth.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR PANTHER; PTHR43030; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR PANTHER; PTHR43030:SF1; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR Pfam; PF01326; PPDK_N; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SCX72202.1};
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:SCX72202.1}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..670
FT /note="Phosphoenolpyruvate synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011477415"
FT DOMAIN 367..666
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
SQ SEQUENCE 670 AA; 72876 MW; 5E0C580F791674C5 CRC64;
MKALGRVSVL ALCAMAAAPA PASAQLARKP SYYQQQNQPQ PEGPAAQLVP RPAVPSSLPA
LRSQGDFDTL ARVYDAGTPM QLAHVLFVID RQAKPARMYY IDTPRYQLHV RFLRDTRLTP
NTIKREIDRN YLVPDRRFLF GTLSWQQNIG TFTYEFWEGD RLTAPLLRQA DAQIKASFFG
PVKFKTNSTL HERVAKETGL DYVSQEALIR EQPYMPMNLG TATGRVRIVD EAASANALNA
LLPDDIAVLR QVPIGLPPVA GVLTERPSTA LSHVNLLAKG WGIPNAYVRD AATVLKEHAG
QWVALKVAAS GYQVRRLTPE EIAALPPRAV RTASTGATPG GAKAIKPDLR ETRLLPLASL
RARNSAQCGT KAANLGAMQA AHIPGTSVPD GFCIPFAHYD HFMRSNGLAD RIARMQQQPG
FASDPQLRQK ALAQLRDEIV QWPVDAATAA AWRAAWQAQL GGGGVFVRSS SNSEDLPGFS
GAGLYTTMPN VKTGDALEVA VKKVWASVFN PEAWEARSAA GFGAESVLMG VFVQTAIDST
NAGVMITRDP FDAGHPHVTY ISAKRGIGIR VVEGKRVAEQ VMYSSWSKAI QVLSRSAEET
SLQLDKDGGV KEVPVEAGRN VLTDELVVRL ANVGAAVKRT FNAVDQDIEW ATVGDKIVLL
QARPYVERRR
//