ID A0A0B6WZI9_9BACT Unreviewed; 643 AA.
AC A0A0B6WZI9;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=PYK22_01730 {ECO:0000313|EMBL:CDM65724.1};
OS Pyrinomonas methylaliphatogenes.
OC Bacteria; Acidobacteriota; Blastocatellia; Blastocatellales;
OC Pyrinomonadaceae; Pyrinomonas.
OX NCBI_TaxID=454194 {ECO:0000313|EMBL:CDM65724.1, ECO:0000313|Proteomes:UP000031518};
RN [1] {ECO:0000313|EMBL:CDM65724.1, ECO:0000313|Proteomes:UP000031518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K22 {ECO:0000313|EMBL:CDM65724.1,
RC ECO:0000313|Proteomes:UP000031518};
RA Stott M.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDM65724.1, ECO:0000313|Proteomes:UP000031518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K22 {ECO:0000313|EMBL:CDM65724.1,
RC ECO:0000313|Proteomes:UP000031518};
RA Lee K.C.Y., Power J.F., Dunfield P.F., Morgan X.C., Huttenhower C.,
RA Stott M.B.;
RT "Complete genome sequence of Pyrinomonas methylaliphatogenes type strain
RT K22T.";
RL Submitted (JAN-2015) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CBXV010000006; CDM65724.1; -; Genomic_DNA.
DR RefSeq; WP_041976227.1; NZ_CBXV010000006.1.
DR AlphaFoldDB; A0A0B6WZI9; -.
DR STRING; 454194.PYK22_01730; -.
DR OrthoDB; 180730at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000031518; 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 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:CDM65724.1};
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:CDM65724.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031518};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 340..635
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
SQ SEQUENCE 643 AA; 72869 MW; 43FFCDB87849969A CRC64;
MDSVRKASVA LIGLALLLSR GGGCAVLGAQ NGAQVEPRSL PAIRSRAEFD ALARVYTDAN
VPLPHVLFVI DRQDGDRIYY INSKRYRFHR DFVNGTYLSL ERGQEFFDNN YLKPNRRFIL
GTIAYQAPVG KWTFEFWEGD RITADLISLT AEKLRQTFFA PIAFKPNSTH QEREAARVGG
LEIVLPSEIL REQEYQPLNV ARGIGRIHII KRLDEHTDIH FNEIVVLDEV PLHLPPVAGI
ITSQPSTPLS HINLLAKSWG VPNAYIKNAT EVLKEYDGWW VTFETKPDSY AIKRADLKQL
DEYQKRLKAR LDIMTPRYDL SVRRLASLSE QRARDVVAYG AKSANLGEVM RARLAGVIVP
RGFTIPFFYY DQFVRENGLD EAIYELLNDQ RFVHDPAYRR EQLAALREKF QRGRMNDRLR
AMVLARFHRE FRGRGVFVRS STNSEDLPNF NGAGLYTTVP NVRTDGQLIE AIKTVWGSVW
NFEAYEARER AGIDHTKVFM AVLIQEGINA DSAGVMITTD PFNEENHDAV YISAKRGLGI
KVVEGQKIAE QVIYRPASDT VQVLTRSAED SLLTFDERGG VKEVPITGDR AVLTDEMARR
LARVGLALKK VFGGRDQDVE WVYMRGQLYI VQSRPYIAGR GGS
//
