PPSA_STAMF
ID PPSA_STAMF Reviewed; 834 AA.
AC P46893; A3DKU4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=Smar_0141;
OS Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / F1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Staphylothermus.
OX NCBI_TaxID=399550;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 296-320;
RP 528-546; 625-636; 638-647; 657-661; 682-694; 698-720 AND 742-752.
RX PubMed=7805870; DOI=10.1016/0014-5793(94)01304-7;
RA Cicicopol C., Peters J., Kellermann J., Baumeister W.;
RT "Primary structure of a multimeric protein, homologous to the PEP-utilizing
RT enzyme family and isolated from a hyperthermophilic archaebacterium.";
RL FEBS Lett. 356:345-350(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43588 / DSM 3639 / JCM 9404 / F1;
RX PubMed=19341479; DOI=10.1186/1471-2164-10-145;
RA Anderson I.J., Dharmarajan L., Rodriguez J., Hooper S., Porat I.,
RA Ulrich L.E., Elkins J.G., Mavromatis K., Sun H., Land M., Lapidus A.,
RA Lucas S., Barry K., Huber H., Zhulin I.B., Whitman W.B., Mukhopadhyay B.,
RA Woese C., Bristow J., Kyrpides N.;
RT "The complete genome sequence of Staphylothermus marinus reveals
RT differences in sulfur metabolism among heterotrophic Crenarchaeota.";
RL BMC Genomics 10:145-145(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43588 / DSM 3639 / JCM 9404 / F1;
RX PubMed=21304655; DOI=10.4056/sigs.30527;
RA Anderson I.J., Sun H., Lapidus A., Copeland A., Glavina Del Rio T.,
RA Tice H., Dalin E., Lucas S., Barry K., Land M., Richardson P., Huber H.,
RA Kyrpides N.C.;
RT "Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986
RT type strain F1.";
RL Stand. Genomic Sci. 1:183-188(2009).
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 -!- SUBUNIT: Homooligomer. Forms a large complex of about 2000 kDa.
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 -!- PTM: The N-terminus is blocked.
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}.
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DR EMBL; S74619; AAB32888.1; -; Genomic_DNA.
DR EMBL; CP000575; ABN69254.1; -; Genomic_DNA.
DR PIR; S51006; S51006.
DR RefSeq; WP_011838445.1; NC_009033.1.
DR AlphaFoldDB; P46893; -.
DR SMR; P46893; -.
DR STRING; 399550.Smar_0141; -.
DR EnsemblBacteria; ABN69254; ABN69254; Smar_0141.
DR GeneID; 4907183; -.
DR KEGG; smr:Smar_0141; -.
DR eggNOG; arCOG01111; Archaea.
DR HOGENOM; CLU_007308_6_2_2; -.
DR OMA; LETWFFL; -.
DR OrthoDB; 3139at2157; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000000254; 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; 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 PANTHER; PTHR43030; PTHR43030; 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; SSF51621; SSF51621; 1.
DR SUPFAM; SSF52009; SSF52009; 1.
DR TIGRFAMs; TIGR01418; PEP_synth; 1.
DR PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..834
FT /note="Probable phosphoenolpyruvate synthase"
FT /id="PRO_0000147038"
FT ACT_SITE 447
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 772
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 550
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 598
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 699
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 699
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 720
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 721
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 722
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 723
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 723
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 834 AA; 93736 MW; 4F6C80446D4D327C CRC64;
MSNVPKEKRF IVWLDEVTKD DVVLVGGKNA NLGEMIRAGI PVPPGFAVTA YAYKYFIEKT
GLKDKIYPLL NSIDVNDKKV LDETTAKIRQ WIMDTPMPPE VEEEIRKYYR ELAKKIGMEP
EKLRVAVRSS ATAEDMPEAS FAGQQDTYLN VYGEDNVVYY VKRCWASLFT SRAVFYRVAQ
GIPHEKSLMS VTVQKMVNSR TAGVMFTLHP VTGDEKVVVI EASWGLGESV VGGKVTPDEW
VVDKQTLQIV DQKIHHKTLA IVFDPKKGKN VEIRWDENKQ AWVSEEGPVD IEMVKHFHPD
KPALKEEEVK RLAELALLIE KHYGRHMDIE WAVDYDIPFP DNVFIVQARL ETVWSVRKEK
EKAEKKAEIK GKNIVKLSEA KVLVRGLPAS PGIGAGVAKV IFDPHSKEAQ EFKEGEVLVT
KMTDPDWVPL MKKAVAIVTD EGGMTSHAAI VSRELGIPAI VGTGNATQVI KSGIEVTVDG
SRGVVYEGIV EDLVKPKEEV KAEVAGVGIS PEQLLPLYPV TATKIYMNLG EPDAIEKYKD
LPFDGIGLMR IEFIITDWVQ YHPLYLIEQG KESLFIDKLA EGIAKVAQAI YPRPVVVRFS
DFKTNEYRGL KGGEKYEPEE RNPMIGWRGV SRYIHPKYEP AFRLEVRAIK KVREEMGLTN
VWVMFPFVRT TWELERALKI MEEEGLKRGK DFKVWAMAEV PSIVLLADKF AEYVDGFSIG
SNDLTQLILG ADRDSNILAE MGYFDERDPA VLAGIKMIIE KAHSKGATVS ICGQAPSVYP
EIVEFLVEAG IDSISVNPDA VIATRRLVAS IERKIMLKRL NKIMDKLNKL ELGF
