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

Q8U0I2 (AMPPA_PYRFU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 80. 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.-
Alternative name(s):
Nucleoside monophosphate phosphorylase
Short name=NMP phosphorylase
Gene names
Ordered Locus Names:PF1607
OrganismPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) [Reference proteome] [HAMAP]
Taxonomic identifier186497 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

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

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

UMP + phosphate = D-ribose 1,5-bisphosphate + uracile. 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_0000059091

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
Q8U0I2 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: DB90216833A12512

FASTA50354,340
        10         20         30         40         50         60 
MRGKIKILDI ETGNLAIFIN PEDAEQWRIH PNDLVKIESG KRYIYGSAFI GNIVEKGEIG 

        70         80         90        100        110        120 
ISKDVLSIHQ FSNGEIVSLS PAGTPESVKY IKKKMRGEKL KKVEIETIVR DIVDRKLRNT 

       130        140        150        160        170        180 
EISAFVSAIE INGLDMEEIA ALTIAMAETG DMLDIERKPI MDIHSIGGVP GNKTNVIVVP 

       190        200        210        220        230        240 
IVAAAGLTIP KTSSRAITSA AGTADVVEVL TNVTLTLEEI KRIVEKIGAC LVWGGALNLA 

       250        260        270        280        290        300 
PADDLMIHVE RRLSLDPRGL MLASIMAKKY AIGSQYILID IPTGKGAKVE SMEEARSLAR 

       310        320        330        340        350        360 
DFIELGKRLG QYVEVAITYG GQPIGYTVGP ALEAKEALET LMTGRGPGSL VEKAIGLAGL 

       370        380        390        400        410        420 
LLEMGGAAPK GKGKIIAREI LEKGKAYQKM REIIEEQGGD PDIKPEDIPI GDKTYTIHAQ 

       430        440        450        460        470        480 
TNGYVTAIDN RGITAIAREA GAPEDKGAGI RLHVKVGDKV KEGDPLFTIH AESESRLDKA 

       490        500 
IVLARRLEPI KIEGMVLQVI ENL 

« Hide

References

[1]"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009950 Genomic DNA. Translation: AAL81731.1.
RefSeqNP_579336.1. NC_003413.1.

3D structure databases

ProteinModelPortalQ8U0I2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING186497.PF1607.

Proteomic databases

PRIDEQ8U0I2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL81731; AAL81731; PF1607.
GeneID1469483.
KEGGpfu:PF1607.

Phylogenomic databases

eggNOGCOG0213.
HOGENOMHOG000252767.
KOK00758.
OMADVWRRMI.
ProtClustDBPRK04350.

Family and domain databases

Gene3D3.40.1030.10. 1 hit.
3.90.1170.30. 1 hit.
HAMAPMF_02132. AMP_phosphorylase.
InterProIPR017713. AMP_phosphorylase.
IPR009010. Asp_de-COase-like_dom.
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.
SSF50692. SSF50692. 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_PYRFU
AccessionPrimary (citable) accession number: Q8U0I2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: June 1, 2002
Last modified: February 19, 2014
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

SIMILARITY comments

Index of protein domains and families