PPSA_METJA
ID PPSA_METJA Reviewed; 1188 AA.
AC Q57962;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Probable phosphoenolpyruvate synthase;
DE Short=PEP synthase;
DE EC=2.7.9.2;
DE AltName: Full=Pyruvate, water dikinase;
DE Contains:
DE RecName: Full=Mja pep intein;
DE AltName: Full=Mja pepA intein;
GN Name=ppsA; OrderedLocusNames=MJ0542;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(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 -!- PTM: This protein undergoes a protein self splicing that involves a
CC post-translational excision of the intervening region (intein) followed
CC by peptide ligation. {ECO:0000305}.
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; L77117; AAB98534.1; -; Genomic_DNA.
DR PIR; F64367; F64367.
DR AlphaFoldDB; Q57962; -.
DR SMR; Q57962; -.
DR STRING; 243232.MJ_0542; -.
DR EnsemblBacteria; AAB98534; AAB98534; MJ_0542.
DR KEGG; mja:MJ_0542; -.
DR eggNOG; arCOG01111; Archaea.
DR HOGENOM; CLU_007308_6_1_2; -.
DR InParanoid; Q57962; -.
DR OMA; RRFVQMY; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
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:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR Gene3D; 3.10.28.10; -; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR Gene3D; 3.30.1490.20; -; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR006319; PEP_synth.
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; 2.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR Pfam; PF01326; PPDK_N; 1.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF51294; SSF51294; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR SUPFAM; SSF52009; SSF52009; 1.
DR SUPFAM; SSF55608; SSF55608; 1.
DR TIGRFAMs; TIGR01443; intein_Cterm; 1.
DR TIGRFAMs; TIGR01445; intein_Nterm; 1.
DR PROSITE; PS50818; INTEIN_C_TER; 1.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
DR PROSITE; PS00742; PEP_ENZYMES_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Autocatalytic cleavage; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Protein splicing; Reference proteome;
KW Transferase.
FT CHAIN 1..410
FT /note="Probable phosphoenolpyruvate synthase, 1st part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000023556"
FT CHAIN 411..822
FT /note="Mja pep intein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000023557"
FT CHAIN 823..1188
FT /note="Probable phosphoenolpyruvate synthase, 2nd part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000023558"
FT DOMAIN 536..670
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
FT ACT_SITE 824
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 1133
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 917
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 964
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1061
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1061
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1083
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1084
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1085
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1086
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1086
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1188 AA; 134012 MW; 5547E2E2A8C46AEC CRC64;
MLIIQNTKGD SMKFIAWLDE LSNKDVDIAG GKGASLGEMW NAGLPVPPAF VVTADAYRHF
IKETGLMDKI REILSGLDVN DTDALTNASK KIRKLIEEAE MPEDLRLAII EAYNKLCEMC
GEDEVTVAVR SSATAEDLPE ASFAGQQDTY LNIKGAENVV KYVQKCFSSL FTPRAIFYRE
QQGFDHFKVA LAAVVQKLVN AEKAGVMFTV NPISENYDEL VIEAAWGLGE GVVSGSVSPD
TYIVNKKTLE IVDKHIARKE TMFVKDEKGE TKVVEVPDDM KEKQVLSDDE IKELAKIGLN
IEKHYGKPMD VEWAYEKGKF YMLQARPITT LKKGKKEKKA KEEDIEAKIL LKGIGASPGI
ATGVVKIIHD VSEIDKVKEG DILVTEMTTP DMVPAMKKAA AIVTDEGGLT CIEGDAKILT
DRGFLKMKEV YKLVKNGEKL KVLGLNAETL KTEWKEIIDA QKREARRYEI GVYRKNKNTK
DTIKITPDHK FPVFVNGELS KVQLCDIIDN NLSVLSIDYI PMIEEKYESL AEVMYLGGAV
LSDGHIVRRN GKPIRVRFTQ KDTEEKKDFI EKVKGDVKLI GGNFIEISNR NNVIEYQTSR
KIPSEILGFI EVNINTIPLY ATKDEIADLI AGFVDGDGCL SGKRRVEIYQ NSSHIKKIEG
LIVGLYRLGI IPRLRYKRSS TATIYFNNNL ETILQRTRRI KLDKLKEFKK PVEDKKLIDI
SQILPELKEF DYKGYLYKTY KEKLFIGINK LEEYLSKIDK DGIERIKQKI KLLKESDIYS
IRIKKVGEDY GEVYNITVKA ENEFNHNYVV WTKHYTPIVV FNCHAAIVSR ELGTPCVVGT
KKATKVLKDG MIVTVDGEKG IVYEGEIKKV EEKEKKQEVV VQQAPIITAT EVKVNVSMPE
VAERAAATGA DGVGLLRAEH MILGLGKHPR KILEEEGEEA LIEALMEGIR KVADAFYPRP
VTYRTLDAPT DEFRGLEGGE NEPIEHNPML GWRGIRRDLD EVDILKCELK AIKRLREEGY
KNIEIMIPLV THPDEVRRVK EIMREVGLEP CKDIPFGIMV ETPAAALIIE DFIKEGINFV
SLGTNDLTQY TIAIDRNNEL VSKYYKEDHP AVLKLVEHVI KTCKKHGIKT SICGQAGSRP
HIVEKLVEWG IDSVSANIDA VETIRRVVAR TEQKVILNYI RKSYVERE
