Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B6YWT7 (AMPPA_THEON) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
AMP phosphorylase

Short name=AMPpase
EC=2.4.2.57
Alternative name(s):
Nucleoside monophosphate phosphorylase
Short name=NMP phosphorylase
Gene names
Ordered Locus Names:TON_1062
OrganismThermococcus onnurineus (strain NA1) [Complete proteome] [HAMAP]
Taxonomic identifier523850 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus

Protein attributes

Sequence length503 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO By similarity. HAMAP-Rule MF_02132

Catalytic activity

AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate. HAMAP-Rule MF_02132

CMP + phosphate = cytosine + alpha-D-ribose 1,5-bisphosphate. HAMAP-Rule MF_02132

UMP + phosphate = uracil + alpha-D-ribose 1,5-bisphosphate. HAMAP-Rule MF_02132

Sequence similarities

Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 503503AMP phosphorylase HAMAP-Rule MF_02132
PRO_1000132354

Regions

Nucleotide binding194 – 1996AMP By similarity

Sites

Active site2561Proton donor By similarity
Binding site1681AMP; via amide nitrogen By similarity
Binding site2031AMP; via amide nitrogen By similarity
Binding site2641AMP By similarity
Binding site2881AMP By similarity

Sequences

Sequence LengthMass (Da)Tools
B6YWT7 [UniParc].

Last modified January 20, 2009. Version 1.
Checksum: EDB7364EEF6ACA68

FASTA50353,952
        10         20         30         40         50         60 
MKAKVRILDM YSGRYSVFIN EKEAKKAKLH PDDLVKLETG KKTVYGSVTI SNLVKEGEIG 

        70         80         90        100        110        120 
ISKDVLQLHN FSEGEVVTVL PSGAPESVRY IKKKMNGEKL RKVEIETIVK DIVDRKLRDI 

       130        140        150        160        170        180 
EISSFVTALE INGLDMDEIA ALTIAMAETG DMLDIDRKPI MDVHSIGGVP GNKTNILVVP 

       190        200        210        220        230        240 
IVAAAGLTIP KTSSRAITSA AGTADVVEVF AEVSFSLDEI KRIVEKIGAC MVWGGALNLA 

       250        260        270        280        290        300 
PADDITIKAE RALSIDPVGL MLASIMSKKY AMGSQYVLID IPTGKGVKVE TVDEARALAR 

       310        320        330        340        350        360 
DFIELGKRLG QYVEVAITYG GQPIGHTVGP ALEAREALQA LMSGTGPGSL IEKATGLAGI 

       370        380        390        400        410        420 
LLEMGGVAPS GMGKKMAREI LESGKAYQKM REIIEEQGGN PDIKPEEIPI GDKTYTFTAP 

       430        440        450        460        470        480 
TSGYITAIDN KAITGIARAA GAPEDKGAGI ELYVKVGEKV KEGDPLFTIY AESEARLDQA 

       490        500 
IVFARRAEPI RIEGMVLQRI GNI 

« Hide

References

[1]"The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophic and carboxydotrophic metabolism."
Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H., Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J., Colwell R.R., Kim S.-J., Lee J.-H.
J. Bacteriol. 190:7491-7499(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NA1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000855 Genomic DNA. Translation: ACJ16550.1.
RefSeqYP_002307447.1. NC_011529.1.

3D structure databases

ProteinModelPortalB6YWT7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING523850.TON_1062.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACJ16550; ACJ16550; TON_1062.
GeneID7018084.
KEGGton:TON_1062.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0213.
HOGENOMHOG000252767.
KOK00758.
OMAFINGVRD.

Enzyme and pathway databases

BioCycTONN523850:GC7X-1094-MONOMER.

Family and domain databases

Gene3D3.40.1030.10. 1 hit.
3.90.1170.30. 1 hit.
HAMAPMF_02132. AMP_phosphorylase.
InterProIPR017713. AMP_phosphorylase.
IPR000312. Glycosyl_Trfase_fam3.
IPR017459. Glycosyl_Trfase_fam3_N_dom.
IPR013102. PYNP_C.
IPR000053. Pyrmidine_PPase.
IPR017872. Pyrmidine_PPase_CS.
IPR013466. Thymidine/AMP_Pase.
[Graphical view]
PANTHERPTHR10515. PTHR10515. 1 hit.
PfamPF02885. Glycos_trans_3N. 1 hit.
PF00591. Glycos_transf_3. 1 hit.
PF07831. PYNP_C. 1 hit.
[Graphical view]
PIRSFPIRSF000478. TP_PyNP. 1 hit.
SMARTSM00941. PYNP_C. 1 hit.
[Graphical view]
SUPFAMSSF47648. SSF47648. 1 hit.
SSF52418. SSF52418. 1 hit.
SSF54680. SSF54680. 1 hit.
TIGRFAMsTIGR03327. AMP_phos. 1 hit.
TIGR02645. ARCH_P_rylase. 1 hit.
PROSITEPS00647. THYMID_PHOSPHORYLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMPPA_THEON
AccessionPrimary (citable) accession number: B6YWT7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: January 20, 2009
Last modified: May 14, 2014
This is version 41 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