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Database: UniProt
Entry: A0A1G5A2Y2_9BURK
LinkDB: A0A1G5A2Y2_9BURK
Original site: A0A1G5A2Y2_9BURK 
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
//
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