PPSA_PYRAB
ID PPSA_PYRAB Reviewed; 819 AA.
AC Q9V2H7; G8ZFT2;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
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=PYRAB00970; ORFNames=PAB0057;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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}.
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DR EMBL; AJ248283; CAB49021.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE69473.1; -; Genomic_DNA.
DR PIR; F75196; F75196.
DR RefSeq; WP_010867221.1; NC_000868.1.
DR AlphaFoldDB; Q9V2H7; -.
DR SMR; Q9V2H7; -.
DR STRING; 272844.PAB0057; -.
DR EnsemblBacteria; CAB49021; CAB49021; PAB0057.
DR GeneID; 1494984; -.
DR KEGG; pab:PAB0057; -.
DR PATRIC; fig|272844.11.peg.110; -.
DR eggNOG; arCOG01111; Archaea.
DR HOGENOM; CLU_007308_6_2_2; -.
DR OMA; RRFVQMY; -.
DR OrthoDB; 3139at2157; -.
DR PhylomeDB; Q9V2H7; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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 3: Inferred from homology;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..819
FT /note="Probable phosphoenolpyruvate synthase"
FT /id="PRO_0000147043"
FT ACT_SITE 441
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 756
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 540
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 587
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 684
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 684
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 706
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 707
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 708
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 709
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 709
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 819 AA; 90653 MW; E09486ABB527C6EA CRC64;
MAYRFIKWFE ELRKEDVPLV GGKGANLGEM TNAGIPVPPG FCVTAEAYKY FVENVKISKE
DVKRILGEKA NKGTIAEVLA QAPDEPRPLQ EWIMDIINRT NVDDSKQLQE NTAVIRELIK
SLDMPAEIAD EIKQAYKELS QRFGKDEIYV AVRSSATAED LPEASFAGQQ ETYLDVLGAD
DVIDKVKRCW ASLWTARATF YRAKQGFDHS KVYLSAVVQK MVNSEKSGVM FTANPVTNNR
NEIMINASWG LGEAVVSGAV TPDEYIVEKG TWKIKEKVIA KKEVMVIRNP ETGKGTVTVK
VAEYLGPEWV EKQVLTDEQI IEVAKMGQKI EEHYGWPQDI EWAYDKDDGK LYIVQSRPVT
TLKETTTEEV EEVEEAEVIL KGLGASPGIG AGRVVVIFDA SEIDKVKEGD VLVTTMTNPD
MVPAMKRAAA IITDEGGRTS HAAIVSRELG IPAVVGTKEA TKKLKTGDYV TVDGTRGLVY
KGIVKSLVEK KKKEEAAAAP GAAVAAAPLV TGTLVKVNVS MPEVAERAAA TGADGVGLLR
AEHMILSIGQ HPVKFIKEGK EEELVEKLAE GIEKVAAAFY PRPVWYRTLD APTNEFREMP
GGEDEPEERN PMLGWRGIRR GLDQPELLRA EFKAIKKVVE KGYNNIGVML PLVSHPEQIR
KAKEIARSVG LEPHKDVAWG IMIEVPAAAI IIEDLIKEGI DFVSFGTNDL TQYTLAIDRD
NERVAKLYDE THPAVLKLIK HVIKVCKRYG VETSICGQAG SDPKMARILV RLGIDSISAN
PDAVQLIRQV VAQEERKLML EAARKRLFEE EEEEEEFLF
