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Q57962 (PPSA_METJA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable phosphoenolpyruvate synthase

Short name=PEP synthase
EC=2.7.9.2
Alternative name(s):
Pyruvate, water dikinase

Cleaved into the following chain:

  1. Mja pep intein
    Alternative name(s):
    Mja pepA intein
Gene names
Name:ppsA
Ordered Locus Names:MJ0542
OrganismMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP]
Taxonomic identifier243232 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus

Protein attributes

Sequence length1188 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate By similarity.

Catalytic activity

ATP + pyruvate + H2O = AMP + phosphoenolpyruvate + phosphate.

Cofactor

Magnesium By similarity.

Pathway

Carbohydrate biosynthesis; gluconeogenesis.

Domain

The N-terminal domain contains the ATP/Pi binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site By similarity.

Post-translational modification

This protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation Potential.

Miscellaneous

The reaction takes place in three steps, mediated by a phosphocarrier histidine residue located on the surface of the central domain. The two first partial reactions are catalyzed at an active site located on the N-terminal domain, and the third partial reaction is catalyzed at an active site located on the C-terminal domain. For catalytic turnover, the central domain swivels from the concave surface of the N-terminal domain to that of the C-terminal domain By similarity.

Sequence similarities

Belongs to the PEP-utilizing enzyme family.

Contains 1 DOD-type homing endonuclease domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 410410Probable phosphoenolpyruvate synthase, 1st part Potential
PRO_0000023556
Chain411 – 822412Mja pep intein Potential
PRO_0000023557
Chain823 – 1188366Probable phosphoenolpyruvate synthase, 2nd part Potential
PRO_0000023558

Regions

Domain536 – 670135DOD-type homing endonuclease

Sites

Active site8241Tele-phosphohistidine intermediate By similarity
Active site11331Proton donor By similarity
Metal binding10611Magnesium By similarity
Metal binding10861Magnesium By similarity
Binding site9171Substrate By similarity
Binding site9641Substrate By similarity
Binding site10611Substrate By similarity
Binding site10831Substrate; via carbonyl oxygen By similarity
Binding site10841Substrate; via amide nitrogen By similarity
Binding site10851Substrate By similarity
Binding site10861Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q57962 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 5547E2E2A8C46AEC

FASTA1,188134,012
        10         20         30         40         50         60 
MLIIQNTKGD SMKFIAWLDE LSNKDVDIAG GKGASLGEMW NAGLPVPPAF VVTADAYRHF 

        70         80         90        100        110        120 
IKETGLMDKI REILSGLDVN DTDALTNASK KIRKLIEEAE MPEDLRLAII EAYNKLCEMC 

       130        140        150        160        170        180 
GEDEVTVAVR SSATAEDLPE ASFAGQQDTY LNIKGAENVV KYVQKCFSSL FTPRAIFYRE 

       190        200        210        220        230        240 
QQGFDHFKVA LAAVVQKLVN AEKAGVMFTV NPISENYDEL VIEAAWGLGE GVVSGSVSPD 

       250        260        270        280        290        300 
TYIVNKKTLE IVDKHIARKE TMFVKDEKGE TKVVEVPDDM KEKQVLSDDE IKELAKIGLN 

       310        320        330        340        350        360 
IEKHYGKPMD VEWAYEKGKF YMLQARPITT LKKGKKEKKA KEEDIEAKIL LKGIGASPGI 

       370        380        390        400        410        420 
ATGVVKIIHD VSEIDKVKEG DILVTEMTTP DMVPAMKKAA AIVTDEGGLT CIEGDAKILT 

       430        440        450        460        470        480 
DRGFLKMKEV YKLVKNGEKL KVLGLNAETL KTEWKEIIDA QKREARRYEI GVYRKNKNTK 

       490        500        510        520        530        540 
DTIKITPDHK FPVFVNGELS KVQLCDIIDN NLSVLSIDYI PMIEEKYESL AEVMYLGGAV 

       550        560        570        580        590        600 
LSDGHIVRRN GKPIRVRFTQ KDTEEKKDFI EKVKGDVKLI GGNFIEISNR NNVIEYQTSR 

       610        620        630        640        650        660 
KIPSEILGFI EVNINTIPLY ATKDEIADLI AGFVDGDGCL SGKRRVEIYQ NSSHIKKIEG 

       670        680        690        700        710        720 
LIVGLYRLGI IPRLRYKRSS TATIYFNNNL ETILQRTRRI KLDKLKEFKK PVEDKKLIDI 

       730        740        750        760        770        780 
SQILPELKEF DYKGYLYKTY KEKLFIGINK LEEYLSKIDK DGIERIKQKI KLLKESDIYS 

       790        800        810        820        830        840 
IRIKKVGEDY GEVYNITVKA ENEFNHNYVV WTKHYTPIVV FNCHAAIVSR ELGTPCVVGT 

       850        860        870        880        890        900 
KKATKVLKDG MIVTVDGEKG IVYEGEIKKV EEKEKKQEVV VQQAPIITAT EVKVNVSMPE 

       910        920        930        940        950        960 
VAERAAATGA DGVGLLRAEH MILGLGKHPR KILEEEGEEA LIEALMEGIR KVADAFYPRP 

       970        980        990       1000       1010       1020 
VTYRTLDAPT DEFRGLEGGE NEPIEHNPML GWRGIRRDLD EVDILKCELK AIKRLREEGY 

      1030       1040       1050       1060       1070       1080 
KNIEIMIPLV THPDEVRRVK EIMREVGLEP CKDIPFGIMV ETPAAALIIE DFIKEGINFV 

      1090       1100       1110       1120       1130       1140 
SLGTNDLTQY TIAIDRNNEL VSKYYKEDHP AVLKLVEHVI KTCKKHGIKT SICGQAGSRP 

      1150       1160       1170       1180 
HIVEKLVEWG IDSVSANIDA VETIRRVVAR TEQKVILNYI RKSYVERE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L77117 Genomic DNA. Translation: AAB98534.1.
PIRF64367.
RefSeqNP_247521.1. NC_000909.1.

3D structure databases

ProteinModelPortalQ57962.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243232.MJ0542.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB98534; AAB98534; MJ_0542.
GeneID1451407.
KEGGmja:MJ_0542.

Phylogenomic databases

eggNOGCOG0574.
KOK01007.
OMAINTIPLY.
ProtClustDBCLSK2749892.

Enzyme and pathway databases

UniPathwayUPA00138.

Family and domain databases

Gene3D3.10.28.10. 1 hit.
3.20.20.60. 1 hit.
3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.50.30.10. 2 hits.
InterProIPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR003587. Hint_dom_N.
IPR027434. Homing_endonucl.
IPR004042. Intein_endonuc.
IPR006141. Intein_splice_site.
IPR008279. PEP-util_enz_mobile_dom.
IPR000121. PEP_util_C.
IPR023151. PEP_util_CS.
IPR006318. PEP_util_enz.
IPR002192. PPDK_PEP-bd.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PfamPF00391. PEP-utilizers. 2 hits.
PF02896. PEP-utilizers_C. 1 hit.
PF01326. PPDK_N. 1 hit.
[Graphical view]
PRINTSPR01736. PHPHTRNFRASE.
SMARTSM00306. HintN. 1 hit.
[Graphical view]
SUPFAMSSF51621. SSF51621. 1 hit.
SSF52009. SSF52009. 1 hit.
SSF55608. SSF55608. 1 hit.
TIGRFAMsTIGR01443. intein_Cterm. 1 hit.
TIGR01445. intein_Nterm. 1 hit.
PROSITEPS50818. INTEIN_C_TER. 1 hit.
PS50819. INTEIN_ENDONUCLEASE. 1 hit.
PS50817. INTEIN_N_TER. 1 hit.
PS00742. PEP_ENZYMES_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePPSA_METJA
AccessionPrimary (citable) accession number: Q57962
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Methanococcus jannaschii

Methanococcus jannaschii: entries and gene names

Intein-containing proteins

List of intein-containing protein entries