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A1RWC3 (AMPPA_THEPD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:Tpen_0093
OrganismThermofilum pendens (strain Hrk 5) [Reference proteome] [HAMAP]
Taxonomic identifier368408 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermofilaceaeThermofilum

Protein attributes

Sequence length511 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 ABL77503.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 511511AMP phosphorylase HAMAP-Rule MF_02132
PRO_0000314732

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 site2621AMP By similarity
Binding site2861AMP By similarity

Sequences

Sequence LengthMass (Da)Tools
A1RWC3 [UniParc].

Last modified January 15, 2008. Version 2.
Checksum: C655AF7EA9714244

FASTA51155,569
        10         20         30         40         50         60 
MKLKTRILPF ESAHYTVVLD QSVAKKLDVR PSDRVLVRFN GKTVVAIANI AKEFSHEHVG 

        70         80         90        100        110        120 
VYVNIAKALG ISDGDEVEVE ATSPPASLQA IRKKLQGLSL ESDEIYQVVK DIVDGKLSEL 

       130        140        150        160        170        180 
ELAAFVTAVH FQGMTPSEIY SFTLSMVETG QRLRLKRKPI LDKHSLGGVP GDKTSLLVVP 

       190        200        210        220        230        240 
IIASLGFTIP KTSSRAITSA AGTADRMEVL APVNLSIDEI ERIVEKTNAC LVWGGALNLA 

       250        260        270        280        290        300 
PADDIIIRVE YPLGIDPFYI PSILAKKLAV GSTHVVLDVP TGRGTKVKTL EEAKRISQSF 

       310        320        330        340        350        360 
FEIARMFGMN LQAVATYAEE PIGHAIGPAL EAREALIALR ELRPGDLVDK AASLAGTLLE 

       370        380        390        400        410        420 
MVGVENGYET AMEALRTGKA EKKLREIIEA QGGDPDVTPE EIPLGDKTYT LYSEEDGFVY 

       430        440        450        460        470        480 
YIDNSLLANI GKIAGAPIDK GAGVYIHVKL GEKVRKGDPL LTVYSSSSAK LQAVERILED 

       490        500        510 
SKPVLVGRTA GRRMLLERIQ YQPPRQLVLE R 

« Hide

References

[1]"Genome sequence of Thermofilum pendens reveals an exceptional loss of biosynthetic pathways without genome reduction."
Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E., Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M., Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B. expand/collapse author list , Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.
J. Bacteriol. 190:2957-2965(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hrk 5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000505 Genomic DNA. Translation: ABL77503.1. Different initiation.
RefSeqYP_919506.1. NC_008698.1.

3D structure databases

ProteinModelPortalA1RWC3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING368408.Tpen_0093.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL77503; ABL77503; Tpen_0093.
GeneID4601385.
KEGGtpe:Tpen_0093.

Phylogenomic databases

eggNOGCOG0213.
HOGENOMHOG000252767.
KOK00758.

Enzyme and pathway databases

BioCycTPEN368408:GHSG-95-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_THEPD
AccessionPrimary (citable) accession number: A1RWC3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: May 14, 2014
This is version 53 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