ID M4YP10_THEXX Unreviewed; 780 AA.
AC M4YP10;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Phosphoenolpyruvate synthase {ECO:0000256|PIRNR:PIRNR000854};
DE Short=PEP synthase {ECO:0000256|PIRNR:PIRNR000854};
DE EC=2.7.9.2 {ECO:0000256|PIRNR:PIRNR000854};
DE AltName: Full=Pyruvate, water dikinase {ECO:0000256|PIRNR:PIRNR000854};
GN ORFNames=TALC_01169 {ECO:0000313|EMBL:AGI48157.1};
OS Thermoplasmatales archaeon (strain BRNA1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales.
OX NCBI_TaxID=1054217 {ECO:0000313|EMBL:AGI48157.1, ECO:0000313|Proteomes:UP000012076};
RN [1] {ECO:0000313|EMBL:AGI48157.1, ECO:0000313|Proteomes:UP000012076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRNA1 {ECO:0000313|EMBL:AGI48157.1,
RC ECO:0000313|Proteomes:UP000012076};
RA Denman S.E., Evans P., Bragg L., Padmanahba J., McKenzie M., Edwards D.,
RA Krzycki J., McSweeney C., Morrison M.;
RT "Thermoplasmatales-like gut symbionts are pyrrolysine dependent-
RT methanogens.";
RL Submitted (JUL-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}.
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; CP002916; AGI48157.1; -; Genomic_DNA.
DR AlphaFoldDB; M4YP10; -.
DR STRING; 1054217.TALC_01169; -.
DR KEGG; tar:TALC_01169; -.
DR PATRIC; fig|1054217.5.peg.1112; -.
DR eggNOG; arCOG01111; Archaea.
DR HOGENOM; CLU_007308_6_2_2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000012076; 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 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:AGI48157.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000012076};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000854}.
FT DOMAIN 22..333
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 370..441
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 466..763
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
SQ SEQUENCE 780 AA; 85479 MW; 0C0F680938B3A973 CRC64;
MDETTTTKRI IDVNELRVTD VPIVGGKGAN LGELTSSGFP VPHAFVLTTV SYDEFVNANK
LMPKIMKEIK GIDPNSDDSL VAASEKIRAI FDKSKIPAAL KKDIEDNYKI LCGSSKQKTF
VAVRSSATAE DLPDASFAGQ QETYLNVASL TELYEKIIMC WSSLFTARAI SYREKQGYSH
EEVKLAVVVQ RMVNSEFSGI MFTVNPNNGA KNIIVEGGYG LGEAIVGGEI TPDTYTIDKV
KMDITDRRFS TQKWKYARGP KGGLVKVDIP EDLQKAQKID DAHVREIAEI GRQVEIHYEK
PMDMEWCIEE GNVYLVQARP ITTLNKIKEA NTSEGPIDGG DVVLTGLGAS PGMASGRVCI
YDEGMSLDVI KDGDVLVTKM TMPDMVPAMS RSVAIVTDEG GMTCHAAIIS RELGTPCVVG
TGEATSALKN GDIVTVDGST GTVYRGEIKG KAAEQAAPAA ATAVFAEQVP ITGTKVMVNM
SMPNKAEEIA QLPCDGVGLL RSEFLFTNYI GEHPCAVIAD GRSQELIDKL ADGVGKVARA
FYPRPVTLRT SDFKTNEYRD MKGGANYEPN EDNPMIGWRG CSRYVSENYR EAFMCELKAI
KKVRDEMGMK NVNIMLPFVR TIDEVKEITA MMESVGLKRG LDLKLYFMAE VPVNIFMAEE
FCKYCDWFSI GSNDLTQLTM GCDRDSDILG KMGYFDERNP GVKAAIKHLI KVAHKYGNHV
SICGQAPSVY PDFCEFLVET GIDCISLNPD TFVKTKKIIA SAEQRVLLNA ARRNAGCCDD
//
