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Q9V163 (AMPPA_PYRAB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 88. 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
Name:deoA
Ordered Locus Names:PYRAB05650
ORF Names:PAB1982
OrganismPyrococcus abyssi (strain GE5 / Orsay) [Complete proteome] [HAMAP]
Taxonomic identifier272844 [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 = 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 caution

The sequence CAB49487.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 503503AMP phosphorylase HAMAP-Rule MF_02132
PRO_0000059090

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
Q9V163 [UniParc].

Last modified August 29, 2003. Version 2.
Checksum: BDD7A239E1777362

FASTA50354,198
        10         20         30         40         50         60 
MRAKVRILNI RSGHFDVFIN PKDAQEWKLH PNDLVKIESG KRSIYGSVVI GDFVESGEVG 

        70         80         90        100        110        120 
LSLDILDAYQ FSEGELVSIT PSETPESVRY IKKKMRGEKL RKVEIETIVR DIVDRKLRNT 

       130        140        150        160        170        180 
EISALVTAIE VNGLDMDEIA ALTIAMAETG DMLDIDRKPI MDVHSIGGVP GNKTNIIVVP 

       190        200        210        220        230        240 
IVAAAGLTIP KTSSRAITSA AGTADVVEVF TNVTLSLDEI KRIVEKIGAC LVWGGALNLA 

       250        260        270        280        290        300 
PADDLTIHVE RRLSLDPRGL MLASIMSKKY AIGSQYILID IPTGKGAKVE TMEEARSLAK 

       310        320        330        340        350        360 
DFIELGKKLG QYVEVAITYG GQPIGYTVGP ALEAKEALET LMTGKGPGSL VEKALGLAGI 

       370        380        390        400        410        420 
LLEMGGVAPR GMGKKVAREI LESGKAYEKI KEIIEEQGGD PNIKPEDIPI GDKTYTIHAQ 

       430        440        450        460        470        480 
TSGYVTGIDN KAITAIAREA GAPEDKGAGV KLHVKVGEKV KEGDPLFTIH AESESRLDKA 

       490        500 
IILARRLEPI KIEGMVLQVL GNL 

« Hide

References

« Hide 'large scale' references
[1]"An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi."
Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.
Mol. Microbiol. 47:1495-1512(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GE5 / Orsay.
[2]"Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638."
Gao J., Wang J.
Curr. Microbiol. 64:118-129(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: GE5 / Orsay.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ248284 Genomic DNA. Translation: CAB49487.1. Different initiation.
HE613800 Genomic DNA. Translation: CCE69956.1.
PIRH75175.
RefSeqNP_126256.1. NC_000868.1.

3D structure databases

ProteinModelPortalQ9V163.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272844.PAB1982.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB49487; CAB49487; PAB1982.
GeneID1495469.
KEGGpab:PAB1982.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0213.
HOGENOMHOG000252767.
KOK00758.
OMAFINGVRD.

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_PYRAB
AccessionPrimary (citable) accession number: Q9V163
Secondary accession number(s): G8ZJ29
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: August 29, 2003
Last modified: May 14, 2014
This is version 88 of the entry and version 2 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