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A2BJU0 (AMPPA_HYPBU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 52. 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:Hbut_0381
OrganismHyperthermus butylicus (strain DSM 5456 / JCM 9403) [Reference proteome] [HAMAP]
Taxonomic identifier415426 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesPyrodictiaceaeHyperthermus

Protein attributes

Sequence length502 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 – 502502AMP phosphorylase HAMAP-Rule MF_02132
PRO_0000314719

Regions

Nucleotide binding195 – 2006AMP By similarity

Sites

Active site2571Proton donor By similarity
Binding site1681AMP; via amide nitrogen By similarity
Binding site2041AMP; via amide nitrogen By similarity
Binding site2651AMP By similarity
Binding site2891AMP By similarity

Sequences

Sequence LengthMass (Da)Tools
A2BJU0 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: 124DF85BC940F955

FASTA50253,499
        10         20         30         40         50         60 
MPVKGLKVEA ASIDPGHDAV ILNPRDAEHL GVVAGLRASV VCRGRGVGAV VIVDPRVPER 

        70         80         90        100        110        120 
VAQLTKGLVE RLGDCDTVDV HPIDVPPSFD AFKKRLSGAR LSAAEYKMLI ADIVAGYYDD 

       130        140        150        160        170        180 
AQIASFLVSQ LYSKLADEEL EHLIRAMVET GEVVKFGEPV YDVHSIGGVP GNSKVALLVV 

       190        200        210        220        230        240 
PIVASRGLLI PKTSSRAITS PAGTADTMEV LAKVAFKPQE LHDMALRARG LIVWGGALNL 

       250        260        270        280        290        300 
APADDIFVRV ERRIGVDPPT QMVASILAKK LAMSVSRLVI DLPTGRGAKV QDESEAELLA 

       310        320        330        340        350        360 
SMFLAQAGRL NIAMRVAITF GGEPIGFSVG PALEAREALQ TLMKGDGASS LVEKACSLAG 

       370        380        390        400        410        420 
LVFELGGVVP RGRGYSLACE ILRSGAAYRK FREIIEVQEG DPDIKPEDIK LAPKQFTLEA 

       430        440        450        460        470        480 
PRDGIVTMID NRAISLAARA AGAPEDKGAG IQLHVKTGYR VRKGDPLLTI YASSDTRLHE 

       490        500 
AVRLLDEYNA VLIEGVVVKV LP 

« Hide

References

[1]"The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C."
Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M., She Q., Garrett R.A., Klenk H.-P.
Archaea 2:127-135(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 5456 / JCM 9403.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000493 Genomic DNA. Translation: ABM80251.1.
RefSeqYP_001012596.1. NC_008818.1.

3D structure databases

ProteinModelPortalA2BJU0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING415426.Hbut_0381.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM80251; ABM80251; Hbut_0381.
GeneID4782885.
KEGGhbu:Hbut_0381.

Phylogenomic databases

eggNOGCOG0213.
HOGENOMHOG000252767.
KOK00758.
OMADVWRRMI.
ProtClustDBCLSK2399321.

Enzyme and pathway databases

BioCycHBUT415426:GC56-381-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]
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_HYPBU
AccessionPrimary (citable) accession number: A2BJU0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 20, 2007
Last modified: February 19, 2014
This is version 52 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