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A6VIW6 (AMPPA_METM7) 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:MmarC7_1329
OrganismMethanococcus maripaludis (strain C7 / ATCC BAA-1331) [Complete proteome] [HAMAP]
Taxonomic identifier426368 [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_0000314724

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
A6VIW6 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 6820393DF490FF6F

FASTA50554,585
        10         20         30         40         50         60 
MLFLNAKFID LDLGESAVIV NEEDLKGTSY YPQDRVLIES HAGSVIGNIY STKTMVQKGE 

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

       130        140        150        160        170        180 
NIELSAFVSS TYINGMNMDE ISEMTKRIAE TGDMISWEKS LVVDIHSIGG VPGNKYALLS 

       190        200        210        220        230        240 
IPILAAAGIT VPKTSSRAIT SPAGTADVME VLTNVELKEE EIKRIVKTTN GCLAWGGGVN 

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

       310        320        330        340        350        360 
ARKFIELGEM LNIKVECVLT YGGQPLGRAI GPALEAKEAI ESLQDPKNAP KSLIEKSLSL 

       370        380        390        400        410        420 
AGILLELGGA AQIGEGQNLA WEILESGKAL EKFNQIIVEQ GGTPKKPEEI ELGEYVEEIL 

       430        440        450        460        470        480 
APIDGYITDI SNTAITNVVK EAGAPRDKKA GILLNSKIGN KVTQGDVLYT IYSGSEERLI 

       490        500 
SAVNLARRVY PVKVEGMLIE RISKF 

« Hide

References

[1]"Complete sequence of Methanococcus maripaludis C7."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., 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: C7 / ATCC BAA-1331.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000745 Genomic DNA. Translation: ABR66392.1.
RefSeqYP_001330543.1. NC_009637.1.

3D structure databases

ProteinModelPortalA6VIW6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING426368.MmarC7_1329.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR66392; ABR66392; MmarC7_1329.
GeneID5329203.
KEGGmmz:MmarC7_1329.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0213.
HOGENOMHOG000252767.
KOK00758.
OMAFINGVRD.

Enzyme and pathway databases

BioCycMMAR426368:GHHL-1369-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_METM7
AccessionPrimary (citable) accession number: A6VIW6
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