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A6URW3 (AMPPA_METVS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 47. 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:Mevan_1338
OrganismMethanococcus vannielii (strain SB / ATCC 35089 / DSM 1224) [Complete proteome] [HAMAP]
Taxonomic identifier406327 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus

Protein attributes

Sequence length505 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 – 505505AMP phosphorylase HAMAP-Rule MF_02132
PRO_0000314725

Regions

Nucleotide binding196 – 2016AMP By similarity

Sites

Active site2581Proton donor By similarity
Binding site1701AMP; via amide nitrogen By similarity
Binding site2051AMP; via amide nitrogen By similarity
Binding site2661AMP By similarity
Binding site2901AMP By similarity

Sequences

Sequence LengthMass (Da)Tools
A6URW3 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 4D915C86528E1F02

FASTA50554,620
        10         20         30         40         50         60 
MLFLNAKFID LDLGANAVIV NEEDLKGTSY YPQDRVLIES HSGSVLGILY STKTMVQKGE 

        70         80         90        100        110        120 
VGIPVRKMKG ISLKEGEEVN LRHAEKPESI QFIKKKMDGQ VLSPNEIRTI IDEIVSKKLS 

       130        140        150        160        170        180 
NIELAAFVTS TYVNGMNMEE IVEMTKRMAE TGDMISWEKS LVVDIHSIGG VPGNKYALLS 

       190        200        210        220        230        240 
IPILAAAGIT IPKTSSRAIT SPAGTADVME VLTNVELDEE ELKRVVKATN GCLVWGGGVN 

       250        260        270        280        290        300 
LAPADDIIIN VERPVSIDPQ PQLLASVMAK KVATGIKYAV IDIPVGKGVK IKNEAEGAKL 

       310        320        330        340        350        360 
ARKFIELGEL LNIRVECVLT YGGQPLGRAI GPALEAKEAL EALTDPKSAP KSLIEKAISL 

       370        380        390        400        410        420 
AGILLELGGS AQIGDGQKLA WEILESGRAL EKFNQIIVEQ GGTPKKPEEI ELGKYVEEVR 

       430        440        450        460        470        480 
SPIDGYIVGI NNTSITNVVK EAGAPRDKKA GLLLNAKIGN KVKRGDILYT IYSGSEERLN 

       490        500 
SAVNLARRVY PVNVEGMMIE RISKF 

« Hide

References

[1]"Complete sequence of Methanococcus vannielii SB."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I. expand/collapse author list , Sieprawska-Lupa M., Whitman W.B., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SB / ATCC 35089 / DSM 1224.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000742 Genomic DNA. Translation: ABR55235.1.
RefSeqYP_001323847.1. NC_009634.1.

3D structure databases

ProteinModelPortalA6URW3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING406327.Mevan_1338.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR55235; ABR55235; Mevan_1338.
GeneID5325128.
KEGGmvn:Mevan_1338.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0213.
HOGENOMHOG000252767.
KOK00758.
OMAESVPGFH.

Enzyme and pathway databases

BioCycMVAN406327:GI04-1382-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_METVS
AccessionPrimary (citable) accession number: A6URW3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 21, 2007
Last modified: May 14, 2014
This is version 47 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