PPSA_METTH
ID PPSA_METTH Reviewed; 684 AA.
AC O27190;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Probable phosphoenolpyruvate synthase;
DE Short=PEP synthase;
DE EC=2.7.9.2;
DE AltName: Full=Pyruvate, water dikinase;
GN Name=ppsA; OrderedLocusNames=MTH_1118;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
CC -!- FUNCTION: Catalyzes the phosphorylation of pyruvate to
CC phosphoenolpyruvate. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC -!- DOMAIN: The N-terminal domain contains the ATP/Pi binding site, the
CC central domain the pyrophosphate/phosphate carrier histidine, and the
CC C-terminal domain the pyruvate binding site. {ECO:0000250}.
CC -!- MISCELLANEOUS: The reaction takes place in three steps, mediated by a
CC phosphocarrier histidine residue located on the surface of the central
CC domain. The two first partial reactions are catalyzed at an active site
CC located on the N-terminal domain, and the third partial reaction is
CC catalyzed at an active site located on the C-terminal domain. For
CC catalytic turnover, the central domain swivels from the concave surface
CC of the N-terminal domain to that of the C-terminal domain (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. {ECO:0000305}.
CC -!- CAUTION: Lacks some of the catalytic-important sites due to premature
CC sequence termination compared to the close ortholog in M.jannaschii.
CC The missing 250 amino acids or so may be retrieved through a serie of
CC sequence corrections. {ECO:0000305}.
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DR EMBL; AE000666; AAB85607.1; -; Genomic_DNA.
DR PIR; G69015; G69015.
DR AlphaFoldDB; O27190; -.
DR SMR; O27190; -.
DR STRING; 187420.MTH_1118; -.
DR PRIDE; O27190; -.
DR EnsemblBacteria; AAB85607; AAB85607; MTH_1118.
DR KEGG; mth:MTH_1118; -.
DR PATRIC; fig|187420.15.peg.1094; -.
DR HOGENOM; CLU_007308_6_2_2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000005223; 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; 3.20.20.60; -; 1.
DR Gene3D; 3.30.1490.20; -; 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; 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 PANTHER; PTHR43030; PTHR43030; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR Pfam; PF01326; PPDK_N; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR SUPFAM; SSF52009; SSF52009; 1.
DR TIGRFAMs; TIGR01418; PEP_synth; 1.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..684
FT /note="Probable phosphoenolpyruvate synthase"
FT /id="PRO_0000147042"
FT ACT_SITE 424
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 517
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 564
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 661
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 661
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 684 AA; 75619 MW; 44A76335F01798F0 CRC64;
MTGARNWLNK PLIFFKFNNH HTASPGDKMV KYVAFFEELG KDDVGIAGGK GANLGELTQA
GIPVPPGFVV TAATYDKFMT DTGLQPVVME MLENLDVNDT KELQRVSAEI KDIITSTEVP
EDIQTLIIES YNALCQRIGK DDVYVAIRSS ATAEDLPEAS FAGQQDTFLN IRGAEDVLDY
VRRCWASLFE ARAIFYREEN NFDHSKVYIA VVVQEMVDAE KAGVMFTVHP STGEDRILIE
GSWGLGEAVV SGSVTPDTYW VDKGTGKLLE FTVGEKNIMF TREDGRTVKK EVPPELRNKR
VLSDGEIAAL AEMGRRIQDH YGSPQDTEWA IMDGDVYMLQ SRPITTLGEA TEETEVKSRE
ILVKGLGASP GLASGRVKII REIHELDKIQ IGDILVTVMT TPDMVPAMKR ASGIITDEGG
VTCHAAIVSR ELGIPCVVGT GNATEVLKEN QVVSIDGNRG LVYEGSVIEG EKKEAEAETV
TVESPLLTVT EVKVNVSMPE AARKAAATGA DGVGLLRTEH MMLTTGVHPR KFIEEGREDE
LVNTLAENIL KVADEFYPRP VWYRTLDAPT DEFKTLEGGE NEPYEHNPML GWRGIRRELD
EPEILRAEFR AIKKLHEQGY TNIGIMIPLV QHPDELRKAK MIAEEAGLKP HRDVEFGIMV
ETPAAALIIE DFIEEGIDFV RLEP
