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Q3IP82 (AMPPA_NATPD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 62. 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:NP_3958A
OrganismNatronomonas pharaonis (strain ATCC 35678 / DSM 2160) (Halobacterium pharaonis) [Complete proteome] [HAMAP]
Taxonomic identifier348780 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeNatronomonas

Protein attributes

Sequence length500 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 – 500500AMP phosphorylase HAMAP-Rule MF_02132
PRO_0000314731

Regions

Nucleotide binding192 – 1976AMP By similarity

Sites

Active site2541Proton donor By similarity
Binding site1661AMP; via amide nitrogen By similarity
Binding site2011AMP; via amide nitrogen By similarity
Binding site2621AMP By similarity
Binding site2861AMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3IP82 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 7E1341E905A7E241

FASTA50052,699
        10         20         30         40         50         60 
MELTVEPIDI GTERPVVLLN CADAETLGVH SLDRVEIDWD GTTEVGIVKV TDELVAAGRI 

        70         80         90        100        110        120 
GASHGFPEIT DGTVVAVTPA GQPESVESIR RKLDGRELDS DELGAIVADI EADRLSDLEL 

       130        140        150        160        170        180 
SAYVCASHAN GLSLEETKQL TERMAEVGKQ LSWEQPVVAD KHSIGGVAGN RVTPVVVAIV 

       190        200        210        220        230        240 
AAAGLTIPKT SSRAVTSPAG TADTMEVFCP VEFSREEIRD IVTETGGCLV WGGAVDLSPV 

       250        260        270        280        290        300 
DDKVIRAQRP LSLDPPGQVI ASVLSKKQSA GSSHIVVDIP YGAGAKVTSL SEARDLADDF 

       310        320        330        340        350        360 
RRVGDHLGLT IECALTRGSD PIGHGIGPVL EARDVLAVLE GEGPEPLRIK SLRLADIIFD 

       370        380        390        400        410        420 
MAREAGMPVD DRSAADILDS GAALSKFRDI VAVQGGDPDV SRDDLQPGDR TETVTADTDG 

       430        440        450        460        470        480 
LVVDVDNQAV SQLARRAGAP NDHGAGVVIH RRTGDKAVAG DVLYTIHAES SDRLEAAREY 

       490        500 
AAGDEIVRVG GRDEALVERR 

« Hide

References

[1]"Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis."
Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J., Oesterhelt D.
Genome Res. 15:1336-1343(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35678 / DSM 2160.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR936257 Genomic DNA. Translation: CAI50070.1.
RefSeqYP_327621.1. NC_007426.1.

3D structure databases

ProteinModelPortalQ3IP82.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING348780.NP3958A.

Proteomic databases

PRIDEQ3IP82.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI50070; CAI50070; NP_3958A.
GeneID3702662.
KEGGnph:NP3958A.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0213.
HOGENOMHOG000252767.
KOK00758.
OMAFINGVRD.

Enzyme and pathway databases

BioCycNPHA348780:GJX0-2009-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_NATPD
AccessionPrimary (citable) accession number: Q3IP82
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 8, 2005
Last modified: May 14, 2014
This is version 62 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