PPSA_SYNY3
ID PPSA_SYNY3 Reviewed; 818 AA.
AC Q55905;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Phosphoenolpyruvate synthase;
DE Short=PEP synthase;
DE EC=2.7.9.2;
DE AltName: Full=Pyruvate, water dikinase;
GN Name=ppsA; OrderedLocusNames=slr0301;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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; BA000022; BAA10668.1; -; Genomic_DNA.
DR PIR; S76976; S76976.
DR AlphaFoldDB; Q55905; -.
DR SMR; Q55905; -.
DR STRING; 1148.1001788; -.
DR PaxDb; Q55905; -.
DR PRIDE; Q55905; -.
DR EnsemblBacteria; BAA10668; BAA10668; BAA10668.
DR KEGG; syn:slr0301; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG1080; Bacteria.
DR InParanoid; Q55905; -.
DR OMA; RRFVQMY; -.
DR PhylomeDB; Q55905; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001425; 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 Reference proteome; Transferase.
FT CHAIN 1..818
FT /note="Phosphoenolpyruvate synthase"
FT /id="PRO_0000147039"
FT ACT_SITE 442
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 774
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 532
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 601
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 703
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 703
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 724
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 725
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 726
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 727
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 727
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 818 AA; 89929 MW; E6A93834607733F5 CRC64;
MVSSVVEKTS VAHKETALIL WFEEVGTHDV GLVGGKNSSL GEMIQQLTNK GVNVPSGFAT
TAYAYRYFIQ EAGLEQKLRD LFTDLDVNDM ANLQERGHLA RQLILDTPFP QNLQTAIAEA
YGAMCERYGQ KMGRTGVDVA VRSSATAEDL PEASFAGQQE TYLNVHSLSC VLESCHKCFA
SLFTDRAISY RHHNGFDHFA VALSVGVQKM VRSDLATSGV MFSIDTETGF KNAALITAAY
GLGENVVQGA VNPDEYFVFK PTLKEGFKPI LEKRLGSKAI KMVYDVGGSK LTKNVEVAEP
EREKYCINDE EILQLARWAC IIEDHYSGVR GVYTPMDIEW AKDGQTGELF IVQARPETVQ
SQKSANVIKT YELKDHSQVL ATGRSVGAAI GQGKAQVIRN VSQINQFRPG EVLITNRTDP
DWEPIMKQAS AIVTNQGGKT CHAAIIAREM GIPAIVGCGD ATDTIKTGED VTICCSEGDE
GSVYSGILNY EVHETELSNL PRTKTQILMN VGNPEQAFGF ASYPADGVGL ARLEFIIANH
IKAHPLALMK FDELEDPLAK AEIAELTKLY AGDRPRFFVD KLAHGIAMIA AAFYPKPVVV
RMSDFKSNEY ANLLGGRQFE PKEENPMIGW RGASRYYDPN YREAYALECQ ALKRVRDEMG
LTNVIPMIPF CRTPDEGRKV IAEMAKHGLK QGKNGLEIYV MCELPSNVIL ADEFSEVFDG
FSIGSNDLTQ LTLGLDRDSS LVAHLFDERN LGVKRMVKMA IETAKANGRK IGICGQAPSD
YPEFAEFLVE LGIDSISLNP DSVLKTVLRI AEVEKALG
