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Reviewed, UniProtKB/Swiss-Prot O29548 (PPSA_ARCFU)

Last modified November 3, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Probable phosphoenolpyruvate synthase
      Short name=PEP synthase
    EC=2.7.9.2
Alternative name(s):
    Pyruvate, water dikinase
Gene names
Name: ppsA
Ordered Locus Names: AF_0710
OrganismArchaeoglobus fulgidus [Complete proteome] [HAMAP]
Taxonomic identifier2234 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus

Protein attributes

Sequence length753 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 753753Probable phosphoenolpyruvate synthase
PRO_0000147041

Sites

Active site3981Tele-phosphohistidine intermediate By similarity
Active site7031Proton donor By similarity
Metal binding6311Magnesium By similarity
Metal binding6561Magnesium By similarity
Binding site4881Substrate By similarity
Binding site5351Substrate By similarity
Binding site6311Substrate By similarity
Binding site6531Substrate; via carbonyl oxygen By similarity
Binding site6541Substrate; via amide nitrogen By similarity
Binding site6551Substrate By similarity
Binding site6561Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
O29548-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 3D087F950321A83B

FASTA75383,868
        10         20         30         40         50         60 
MPVLWLADVD KNDIPLVGGK GANLGELLRA EIPVPDGFVV DARTFREFIQ KTGIAEKIYS 

        70         80         90        100        110        120 
LLRELDVEDT EKLDAVSREI REIIEKTEMP EDIEREIREA YRKLCEEEGK EVYVAVRSSA 

       130        140        150        160        170        180 
TAEDLPDASF AGQQETYLNV VGEDEVVEKV KKCWGSLFTP RAIYYRVQKG FRHEDVSIAV 

       190        200        210        220        230        240 
VVQKMVNSEK SGVMFTSHPV SGEKKCIIEA VFGLGEAIVS GLVTPDTYVY DRVKRKIEEV 

       250        260        270        280        290        300 
KIGEKKFMLT RKDGKTVKVE LPPEKANERV LSDEEIEKLV TLGELIEDHY GKPQDVEWAI 

       310        320        330        340        350        360 
EGGKIYIVQS RPITTIRKEK KEAEEEVSEE AEGKILLKGL GASPGIASGK VKVIFSEKEI 

       370        380        390        400        410        420 
SKVEEGDILV TTMTTPDMVP AMKRAAAIVT DEGGMTCHAA IVSRELGVPA VVGTKVATKV 

       430        440        450        460        470        480 
LKDGMVVTVD GEKGIVYEGR IEKKEEPKPV VASAPIITAT EVKVNISIPD VAERVARETN 

       490        500        510        520        530        540 
ADGVGLFRIE HMVLGLEKHP MKFIRDGEID RYIDLLYQEM KKVVKAFYPK PVWIRTIDAP 

       550        560        570        580        590        600 
TDEFRAMEGG EDEPIEANPM LGFRGIRRDL AEEEHFRAEM RAIKKLVDEG YTNVGVMLPL 

       610        620        630        640        650        660 
ITSPEEVKRA KEIAISEGLP LDKIEFGVMV ETPAAALILE DIIKEGIDFV SLGTNDLTQY 

       670        680        690        700        710        720 
TLAVDRNNEN VAYLYNETHP AVLKLIERTI KVCKEHGVKS SICGQAGSYP HVVEKLVEFG 

       730        740        750 
IDSVSANPDA VQRIREVVAR AEKRIILEKL RKI 

« Hide

Cross-references

Sequence databases

AE000782 Genomic DNA. Translation: AAB90532.1.
PIRF69338.
RefSeqNP_069544.1.

3D structure databases

HSSPHSSP built from PDB template 1H6Z based on UniProtKB O76283.
ModBaseSearch...

Genome annotation databases

GeneID1483928.
GenomeReviewsGene locus AF_0710 in contig AE000782_GR.
KEGGafu:AF0710.
NMPDRfig|224325.1.peg.703.
TIGRAF_0710.

Phylogenomic databases

HOGENOMO29548.
OMARAEHMIL.

Enzyme and pathway databases

BioCycAFUL224325:AF_0710-MON.
BRENDA2.7.9.2. 7576.

Family and domain databases

InterProIPR013815. ATP_grasp_subdomain_1.
IPR008279. PEP_mobile.
IPR018274. PEP_mobile_CS.
IPR006318. PEP_P_trans.
IPR006319. PEP_synth.
IPR000121. PEP_utilizers.
IPR002192. PPDK_PEP_bd.
IPR015813. Pyrv/PenolPyrv_Kinase_cat.
[Graphical view]
Gene3DG3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 1 hit.
G3DSA:3.50.30.10. PEP_mobile. 1 hit.
G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
PfamPF00391. PEP-utilizers. 1 hit.
PF02896. PEP-utilizers_C. 1 hit.
PF01326. PPDK_N. 1 hit.
[Graphical view]
PRINTSPR01736. PHPHTRNFRASE.
ProDomPD000940. PEP_utilizers. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01418. PEP_synth. 1 hit.
PROSITEPS00742. PEP_ENZYMES_2. 1 hit.
PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePPSA_ARCFU
AccessionPrimary (citable) accession number: O29548
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: November 3, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents