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O57830 (PPSA_PYRHO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:PH0092
OrganismPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]
Taxonomic identifier70601 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length821 AA.
Sequence statusComplete.
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 – 821821Probable phosphoenolpyruvate synthase
PRO_0000147045

Regions

Compositional bias812 – 8187Poly-Glu

Sites

Active site4441Tele-phosphohistidine intermediate By similarity
Active site7591Proton donor By similarity
Metal binding6871Magnesium By similarity
Metal binding7121Magnesium By similarity
Binding site5431Substrate By similarity
Binding site5901Substrate By similarity
Binding site6871Substrate By similarity
Binding site7091Substrate; via carbonyl oxygen By similarity
Binding site7101Substrate; via amide nitrogen By similarity
Binding site7111Substrate By similarity
Binding site7121Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
O57830 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: A93816D865F8A0BF

FASTA82190,812
        10         20         30         40         50         60 
MDKMAYKFIK WFEELRKDDV PLVGGKGANL GEMTNAGIPV PPGFCVTAEA YKYFVENVKV 

        70         80         90        100        110        120 
SKEDVKKILG EKANKGTIAE VLASAPDEPR TLQEWIMDII NRTNVDDSKQ LQENTAIIRE 

       130        140        150        160        170        180 
LIESLEMPNE IADEIKQAYK ELSQRFGKDE IYVAVRSSAT AEDLPEASFA GQQETYLDVL 

       190        200        210        220        230        240 
GADDVIDKVK KCWASLWTAR ATFYRAKQGF DHSKVYLSAV VQKMVNSEKS GVMFTANPVT 

       250        260        270        280        290        300 
NNRNEIMINA SWGLGEAVVS GAVTPDEYIV EKGTWKIKEK VIAKKEVMVI RNPETGKGTV 

       310        320        330        340        350        360 
QVKVAEYLGP EWVEKQVLTD EQIIEVAKMG QKIEEHYGWP QDIEWAYDKD DGKLYIVQSR 

       370        380        390        400        410        420 
PITTLKETTT EEVEEVEEAE VILKGLGASP GIGAGRVVVI FDASEIDKVK EGDVLVTTMT 

       430        440        450        460        470        480 
NPDMVPAMKR ASAIITDEGG RTSHAAIVSR ELGIPAVVGT KEATKKLKTG DYVTVDGTRG 

       490        500        510        520        530        540 
LVYKGIVKSL VEKKKKEEAA AAPGAAVAAA PLVTGTLVKV NVSMPEVAER AAATGADGVG 

       550        560        570        580        590        600 
LLRAEHMILS IGQHPVKFIK EGKEDELVER LAEGIEKVAA AFYPRPVWYR TLDAPTNEFR 

       610        620        630        640        650        660 
EMPGGEDEPE ERNPMLGWRG IRRGLDQPEL LRAEFKAIKK VVEKGYNNIG VMLPLVSHPE 

       670        680        690        700        710        720 
QIRKAKEIAR EVGLEPHKDV AWGIMIEVPA AAIIIEDLIK EGIDFVSFGT NDLTQYTLAI 

       730        740        750        760        770        780 
DRDNERVAKL YDETHPAVLK LIKHVIKVCK KYGVETSICG QAGSDPKMAR ILVRLGIDSI 

       790        800        810        820 
SANPDAVQLI RQVVAQEERK LMLEAARKKL LEEEEEEEDL F

« Hide

References

[1]"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3."
Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. expand/collapse author list , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.
DNA Res. 5:55-76(1998) [PubMed: 9679194] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000001 Genomic DNA. Translation: BAA29161.1.
PIRB71229.
RefSeqNP_142107.1. NC_000961.1.

3D structure databases

ProteinModelPortalO57830.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBPYRT00000001105; EBPYRP00000001105; EBPYRG00000001105.
GeneID1443992.
GenomeReviewsGene locus PH0092 in contig BA000001_GR.
KEGGpho:PH0092.
NMPDRfig|70601.1.peg.92.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000022475.
HOGENOMHBG284863.
OMALLRAEHM.
PhylomeDBO57830.
ProtClustDBPRK06464.

Enzyme and pathway databases

BioCycPHOR70601:PH0092-MONOMER.

Family and domain databases

InterProIPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR008279. PEP-util_enz_mobile_dom.
IPR006319. PEP_synth.
IPR018274. PEP_util_AS.
IPR000121. PEP_util_C.
IPR023151. PEP_util_CS.
IPR006318. PEP_util_enz.
IPR002192. PPDK_PEP-bd.
IPR015813. Pyrv/PenolPyrv_Kinase.
[Graphical view]
Gene3DG3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 2 hits.
G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit.
G3DSA:3.50.30.10. PEP_mobile. 1 hit.
G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
KOK01007.
PfamPF00391. PEP-utilizers. 1 hit.
PF02896. PEP-utilizers_C. 1 hit.
PF01326. PPDK_N. 1 hit.
[Graphical view]
PRINTSPR01736. PHPHTRNFRASE.
SUPFAMSSF52009. PEP_mobile. 1 hit.
SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
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_PYRHO
AccessionPrimary (citable) accession number: O57830
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: December 14, 2011
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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