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Q8Q0P9 (AMPPA_METMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 83. 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:MM_0087
OrganismMethanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia) [Complete proteome] [HAMAP]
Taxonomic identifier192952 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

Protein attributes

Sequence length507 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 – 507507AMP phosphorylase HAMAP-Rule MF_02132
PRO_0000059089

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
Q8Q0P9 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 439264B574089495

FASTA50754,899
        10         20         30         40         50         60 
MMQLKLEHYN IKIGQHKVLL NIVDAKELGV NPGDRVRIRG HQSLSAIVDT TDDMVPPGTL 

        70         80         90        100        110        120 
GVFTEVYEHF EDWDKPVEVV PSFRSKSAAV IKKMLDKKPV VQDEIKMLVS DIVDENLSDV 

       130        140        150        160        170        180 
ELSAFITASY IHGMTDDEVE WLTRAMIDTG DTIEFDTHPI MDKHSIGGVP GNKISLLIVP 

       190        200        210        220        230        240 
IVAANGLLIP KTSSRAITGA GGTADLMEVL SPVEFSSQEV KEITEKVGGA LVWGGATNIA 

       250        260        270        280        290        300 
PADDKLIKIE YPLSIDPYYQ MLASIMAKKG AIGADNVVMD IPVGPGTKVP TVQEGQKLAR 

       310        320        330        340        350        360 
DLINLGHRLG MNVECAITYG SSPIGRRVGP SLEVKEAMKV LESMEGPNSL IEKSAALAGI 

       370        380        390        400        410        420 
LLEMGGAAPR DQGKELALET LRSGKALEKM KQIIEAQGGD PNIKSDDIQT GQYTADIFAS 

       430        440        450        460        470        480 
TDGYVMEFDN KWIIEIARLA GAPNDKGAGV AIHKKRGEQV KKGDPILTIY AEKEIKLDNA 

       490        500 
LATAQRTNPI IVEGMLLRRI PGTYGFQ 

« Hide

References

[1]"The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea."
Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R. expand/collapse author list , Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008384 Genomic DNA. Translation: AAM29783.1.
RefSeqNP_632111.1. NC_003901.1.

3D structure databases

ProteinModelPortalQ8Q0P9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING192952.MM_0087.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM29783; AAM29783; MM_0087.
GeneID1478429.
KEGGmma:MM_0087.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0213.
HOGENOMHOG000252767.
KOK00758.
OMAFINGVRD.

Enzyme and pathway databases

BioCycMMAZ192952:GCK2-87-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_METMA
AccessionPrimary (citable) accession number: Q8Q0P9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: October 1, 2002
Last modified: May 14, 2014
This is version 83 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