ID C3MSQ8_SULIM Unreviewed; 312 AA.
AC C3MSQ8;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=pyruvate, water dikinase {ECO:0000256|ARBA:ARBA00011996};
DE EC=2.7.9.2 {ECO:0000256|ARBA:ARBA00011996};
DE AltName: Full=Pyruvate, water dikinase {ECO:0000256|ARBA:ARBA00033470};
GN OrderedLocusNames=M1425_2477 {ECO:0000313|EMBL:ACP39201.1};
OS Sulfolobus islandicus (strain M.14.25 / Kamchatka #1).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=427317 {ECO:0000313|EMBL:ACP39201.1, ECO:0000313|Proteomes:UP000001350};
RN [1] {ECO:0000313|EMBL:ACP39201.1, ECO:0000313|Proteomes:UP000001350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M.14.25 / Kamchatka #1 {ECO:0000313|Proteomes:UP000001350};
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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; CP001400; ACP39201.1; -; Genomic_DNA.
DR RefSeq; WP_012712408.1; NC_012588.1.
DR AlphaFoldDB; C3MSQ8; -.
DR GeneID; 84062729; -.
DR KEGG; sia:M1425_2477; -.
DR HOGENOM; CLU_007308_6_0_2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001350; Chromosome.
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:ACP39201.1};
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:ACP39201.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACP39201.1}.
FT DOMAIN 16..307
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
SQ SEQUENCE 312 AA; 35251 MW; 67B9E6CD76A4CD3C CRC64;
MNYTYLLEEV SLSMVSIVGR KSAYLGELYK MGFNVPKGFI VSSRGVNEAI KDLDDEIRGI
LSSVNLNDTT DLEKKSEMIK NMIIMSKLPE EMEKEIYERF SQLGSKYVAV RATATSPLSG
ASFAGEYETD LFVTKENLIP SIKRVIASYF NPRAIAYRIL THNEAGMAIF VQTMINPVSA
GTAFSIHPIT EEPDYVFIES SFGLGESVTR GMVTPDQYIV SKATRSLVSK RISEKVMKLT
YDFEDRKIKS VELSKEEASA ESLSDNDAIR IANMVIAVEN IFKRNINIEW AMEDKKVYLL
EVRGIRRLYP EF
//
