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C6A2A0 (AMPPA_THESM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 39. 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:TSIB_0680
OrganismThermococcus sibiricus (strain MM 739 / DSM 12597) [Complete proteome] [HAMAP]
Taxonomic identifier604354 [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_1000212644

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
C6A2A0 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: 67806AF5CB4333F5

FASTA50354,203
        10         20         30         40         50         60 
MKAKVRILDI ETGRFLAFIS EEDAKNAKLH PGDLVKIETA KRTIYGDVVI SKTINPGEIG 

        70         80         90        100        110        120 
VTKDILRSYT FSEGEVVNLV PSETPESVRY IRRKMNGQKL KKVEIEAIVK DIVNRKLRDI 

       130        140        150        160        170        180 
EISSFVTSLE INGLDMDEIA WLTTAMAETG DMLDIDRKPI MDVHSIGGVP GNKTNILVVP 

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

       250        260        270        280        290        300 
PADDLTIKAE RALSIDPRGL MLASIMSKKY AMGSQYVLID IPTGEGVKVE KVEDARSLAK 

       310        320        330        340        350        360 
DFIELGKRLG QYVETAITYG GQPIGHTVGP ALEAKEALET IIEGKGPGSL VEKATGLAGI 

       370        380        390        400        410        420 
LLEMGGVAPA GMGKKMAKEI LESGKAYEKL KEIIEEQGGD PNIKPEDIPI GDKTYTFVAQ 

       430        440        450        460        470        480 
TSGYITRIDN KAITAIARAA GAPEDKGAGI MLHVKVGEKV KERDPLFTVH AESGTRLDQA 

       490        500 
IIQARRMEPI RIEGMVLQRI GNI 

« Hide

References

[1]"Metabolic versatility and indigenous origin of the archaeon Thermococcus sibiricus, isolated from a siberian oil reservoir, as revealed by genome analysis."
Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V., Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.
Appl. Environ. Microbiol. 75:4580-4588(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MM 739 / DSM 12597.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001463 Genomic DNA. Translation: ACS89745.1.
RefSeqYP_002994094.1. NC_012883.1.

3D structure databases

ProteinModelPortalC6A2A0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING604354.TSIB_0680.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACS89745; ACS89745; TSIB_0680.
GeneID8095668.
KEGGtsi:TSIB_0680.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0213.
HOGENOMHOG000252767.
KOK00758.
OMAFINGVRD.

Enzyme and pathway databases

BioCycTSIB604354:GHMS-701-MONOMER.

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_THESM
AccessionPrimary (citable) accession number: C6A2A0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 1, 2009
Last modified: May 14, 2014
This is version 39 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