PPSA_DEIRA
ID PPSA_DEIRA Reviewed; 780 AA.
AC O83026;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 128.
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=DR_1727;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 259-780.
RA Narumi I., Islam S., Cherdchu K., Kikuchi M., Watanabe H., Kitayama S.,
RA Yamamoto K.;
RT "IS8301: the second insertion sequence element from Deinococcus
RT radiodurans.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
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; AE000513; AAF11283.1; -; Genomic_DNA.
DR EMBL; AB016803; BAA32387.1; -; Genomic_DNA.
DR PIR; D75361; D75361.
DR PIR; T44369; T44369.
DR RefSeq; NP_295450.1; NC_001263.1.
DR RefSeq; WP_010888362.1; NZ_CP015081.1.
DR AlphaFoldDB; O83026; -.
DR SMR; O83026; -.
DR STRING; 243230.DR_1727; -.
DR EnsemblBacteria; AAF11283; AAF11283; DR_1727.
DR KEGG; dra:DR_1727; -.
DR PATRIC; fig|243230.17.peg.1936; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG1080; Bacteria.
DR HOGENOM; CLU_007308_6_2_0; -.
DR InParanoid; O83026; -.
DR OMA; LETWFFL; -.
DR OrthoDB; 997616at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000002524; Chromosome I.
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..780
FT /note="Phosphoenolpyruvate synthase"
FT /id="PRO_0000147033"
FT ACT_SITE 409
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 499
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 566
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 668
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 668
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 689
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 690
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 691
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 692
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 692
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 780 AA; 84895 MW; AD555076324ADA47 CRC64;
MDMIRPFGTL RMTDVEIVGG KNASIGEMIQ GLAQADVRVP GGFATTADAF RLFLRENQIE
EKINAKLQAL DVNDVNALVA AGKEIRGWVE EARLPAALED AIRQAYGEMG DDPDVAVRSS
ATAEDLPEAS FAGQQETFLN VRGIEEVLNH VKLVFASLYN DRAISYRVHH NFEHSEVALS
AGVQRMVRTD LGVSGVAFTL DTESGFRDAV FVTSSYGLGE MVVQGAVNPD EFFVYKPALE
QGKKAVLRRT RGSKQKKMIY AEAGGVKTVD VDEAEQRAFS LSDDDLTELA RQCVTIEKHY
GRPMDIEWGK DGRDVQIYIL QARPETVQSR AGRTLERFEL TGKGDVLVEG RAVGSRIGAG
VVRVVKSLDQ MDSVQDGDIL VADMTDPDWE PVMKRASAIV TNRGGRTCHA AIIARELGIP
AVVGTGNATR ELHNGDEVTV SCAEGDTGYV YAGRLDFHVN RVELDAMPEV GMKIMMNVAS
PDRAFSFAAL PNEGVGLARV EFIISNVIGI HPRALLDYPD VPADVKAQIE EKTAGYASPR
DFFREKLAEG VASIAAAFAP KPVIVRLSDF KSNEYHHLIG GPAYEPTEEN PMIGFRGASR
YRSADFAEAF ALECQAMKQV RDDMGLTNVQ LMIPFVRTVA EGQRILEILA ANGLTQREND
LKVIMMCEVP SNALLADQFL DLFDGFSIGS NDLTQLTLAL DRDSGLVADM FDEQNEAVLA
LMGMAIKAAK AKGKYVGICG QGPSDHPALA QWLMDQGIDS VSLNPDSVLS TWLHLAGEQA
