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Q6M0E4 (AMPPA_METMP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. 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:MMP0327
OrganismMethanococcus maripaludis (strain S2 / LL) [Complete proteome] [HAMAP]
Taxonomic identifier267377 [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 = 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 – 505505AMP phosphorylase HAMAP-Rule MF_02132
PRO_0000314722

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
Q6M0E4 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 466AEE8D187F9B8C

FASTA50554,597
        10         20         30         40         50         60 
MLFLNAKFID LDLGENAVIV NEDDLKGTSY YPQDRVLIES HAGSVIGNIY STKTMVQKGE 

        70         80         90        100        110        120 
VGMLVSELAE ISISEGEEVK LRHAEKPESI PFIKKKMDGQ VLNPHEIRTI IDEIVSKKLS 

       130        140        150        160        170        180 
NIELSAFVSS TYINGMNMDE IGEMTKRIAE TGDMISWEKN LVVDIHSIGG VPGNKYALLS 

       190        200        210        220        230        240 
IPILAAAGIT IPKTSSRAIT SPAGTADVME VLTNVELKED EIKRIVKTTN GCLVWGGGVN 

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

       310        320        330        340        350        360 
ARKFIELGEL LNIKVECVLT YGGQPLGRAI GPALEAKEAI EALQDPKNAP KSLIEKALSL 

       370        380        390        400        410        420 
AGILLELGGA AQIGEGQNLA WEILESGRAL EKFNQIIIEQ GGTPKKPEEI ELGDYIEEII 

       430        440        450        460        470        480 
APIDGYVTDI NNTGITNVVK EAGAPRDKKA GLLLNSKIGN KVKKGDVLYT IYSGSEERLV 

       490        500 
SAVNLARRVY PVKVEGMLIE RISKF 

« Hide

References

[1]"Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis."
Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J., Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M., Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A., Moore B.C. expand/collapse author list , Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D., Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W., Olson M.V., Leigh J.A.
J. Bacteriol. 186:6956-6969(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: S2 / LL.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX950229 Genomic DNA. Translation: CAF29883.1.
RefSeqNP_987447.1. NC_005791.1.

3D structure databases

ProteinModelPortalQ6M0E4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING267377.MMP0327.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAF29883; CAF29883; MMP0327.
GeneID2761854.
KEGGmmp:MMP0327.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0213.
HOGENOMHOG000252767.
KOK00758.
OMADVWRRMI.
ProtClustDBPRK04350.

Enzyme and pathway databases

BioCycMMAR267377:GJ77-349-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_METMP
AccessionPrimary (citable) accession number: Q6M0E4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 5, 2004
Last modified: February 19, 2014
This is version 71 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