ID G8NA21_9DEIN Unreviewed; 796 AA.
AC G8NA21;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=Phosphoenolpyruvate synthase {ECO:0000256|ARBA:ARBA00021623, ECO:0000256|PIRNR:PIRNR000854};
DE Short=PEP synthase {ECO:0000256|PIRNR:PIRNR000854};
DE EC=2.7.9.2 {ECO:0000256|ARBA:ARBA00011996, ECO:0000256|PIRNR:PIRNR000854};
DE AltName: Full=Pyruvate, water dikinase {ECO:0000256|ARBA:ARBA00033470, ECO:0000256|PIRNR:PIRNR000854};
GN ORFNames=TCCBUS3UF1_5440 {ECO:0000313|EMBL:AEV15592.1};
OS Thermus sp. CCB_US3_UF1.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=1111069 {ECO:0000313|EMBL:AEV15592.1, ECO:0000313|Proteomes:UP000005635};
RN [1] {ECO:0000313|EMBL:AEV15592.1, ECO:0000313|Proteomes:UP000005635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCB_US3_UF1 {ECO:0000313|EMBL:AEV15592.1,
RC ECO:0000313|Proteomes:UP000005635};
RA Teh B.S., Abdul Rahman A.Y., Saito J.A., Hou S., Alam M.;
RT "Complete genome sequence of thermophilic Thermus sp. CCB_US3_UF1.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of pyruvate to
CC phosphoenolpyruvate. {ECO:0000256|ARBA:ARBA00002988,
CC ECO:0000256|PIRNR:PIRNR000854}.
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 ECO:0000256|PIRNR:PIRNR000854};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR000854};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742, ECO:0000256|PIRNR:PIRNR000854}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837, ECO:0000256|PIRNR:PIRNR000854}.
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DR EMBL; CP003126; AEV15592.1; -; Genomic_DNA.
DR RefSeq; WP_014514952.1; NC_017278.1.
DR AlphaFoldDB; G8NA21; -.
DR STRING; 1111069.TCCBUS3UF1_5440; -.
DR KEGG; thc:TCCBUS3UF1_5440; -.
DR PATRIC; fig|1111069.3.peg.524; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG1080; Bacteria.
DR HOGENOM; CLU_007308_6_2_0; -.
DR OrthoDB; 9765468at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000005635; 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 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; IPR023151; PEP_util_CS.
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 PIRSF; PIRSF000854; PEP_synthase; 1.
DR PRINTS; PR01736; PHPHTRNFRASE.
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; PS00742; PEP_ENZYMES_2; 1.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000854};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000854};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR000854};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000854};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000854}; Pyruvate {ECO:0000313|EMBL:AEV15592.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000854}.
FT DOMAIN 16..344
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 386..457
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 479..790
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
SQ SEQUENCE 796 AA; 88149 MW; 307CE82B8AFD1BB3 CRC64;
MRWVRFFHEV GLEDVPLVGG KNASLGEMIR ELSPLGVRVP GGFATTSEAY WYFLERNGLK
EAIAQTLKEG DLEDPKTLQR ASRQLRNLIL RGAYPPDLEE EIRLAYRRLS QEAGEEALPV
AVRSSATAED LPTASFAGQQ ESYLYVQGEE DLLLHVKQAM ASLFTARAIS YRAHMGFDHL
KVALSVGVQR MVRADTAASG VIFTLDPDTG HPGFVYLTAI WGLGENIVQG RVGPDGYYVH
KETLKAGYKA LVYKRLGSKE LTLAFDPKEG RLKNRPTPPY LRNQFALQDE EALLLADWSL
KIEAHYTEKR GAPTPMDIEW AKDGVTGELF ILQARPETVH SQKRPVLRIH RLLARGEVLA
EGLAVGEAIA AGRARILRDP KEMDRFQEGE VLVTETTNPD WEPIMKRAAA IVTERGGRTS
HAAIVARELG VPAVVGAVGA TRLIPDGEKV TVSCAEGETG RVYRGELPFA VEEIRPEALP
RTRTRIMVNV GTPDEALRAS LLPTDGVGLL RMEFVFASHV RVHPLALTRF PSLPKEVQRQ
VEEVTEAYAD KRAYFVDTLA QGIGLIAAAF YPRPVLLRFS DFKTNEYARL LGGHLFEPKE
ENPMLGWRGA SRYYHPEYKE GFLLEVAAVK KVREEMGLKN LMVMVPFCRT PEEGQRVLEV
MAEGGLRRGE GGLEVYVMAE IPSNILEAEA FCELFDGFSI GSNDLTQLAL GLDRDSERVA
SLFDERRPTV KALCALLIEK AHARGKKVGI CGQAPSDYPE FAAFLVERGI DSISLNPDAL
LRTVAKVAEL EAVLGR
//
