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Q12Z64 (AMPPA_METBU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. 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.-
Alternative name(s):
Nucleoside monophosphate phosphorylase
Short name=NMP phosphorylase
Gene names
Ordered Locus Names:Mbur_0255
OrganismMethanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M) [Complete proteome] [HAMAP]
Taxonomic identifier259564 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanococcoides

Protein attributes

Sequence length506 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 – 506506AMP phosphorylase HAMAP-Rule MF_02132
PRO_0000314720

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
Q12Z64 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: A44D08052CF1DFDA

FASTA50655,123
        10         20         30         40         50         60 
MQLKVQPIDV KVGKYKVILN TIDAKELGVH EGDRVRIKNH VTLTAIVDFT EDMISPGMIG 

        70         80         90        100        110        120 
LYHEVKEALS KEWTETVEVF PAEKPKSTYI IRKTMDGQKL TKEEIDILVK DIVEENLAEI 

       130        140        150        160        170        180 
EIAAFLTATY INDMTDDETE WLTRAMIDSG DKLEFDTHPI MDKHSIGGVP GNKISLLIVP 

       190        200        210        220        230        240 
IVAANGLLIP KTSSRAITGA GGTADLMEIL APVEFDAAEI KRMTEEVGGV LVWGGATNIA 

       250        260        270        280        290        300 
PADDKLIKVE YPLSIDPHCQ MLASIMAKKG AIGADHVVMD IPTGPGTKIK NVQEGRKLAR 

       310        320        330        340        350        360 
DLINLGDRLG MDVDCALTYG ASPVGRTIGP ALEVIEALKV LESFEGPNSL IEKSASLAGM 

       370        380        390        400        410        420 
LLEMGNVAGK DKGYDLAIET LKNGKALTKF KEIIKIQGGN PDVTHKDISV GEFTEDIIAP 

       430        440        450        460        470        480 
NNGYILEMDN KRLVQIARLA GAPNDKGAGI LLHRKQGEPL KEGDPVMTIY AEKKSKLENA 

       490        500 
VKSAKERPPF IVEGMMLERI QSFKEI 

« Hide

References

[1]"Complete sequence of Methanococcoides burtonii DSM 6242."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Kadner K., Aerts A., Dehal P., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Anderson I., Franzmann P., Thomas T., Saunders N., Cavicchioli R., Sowers K., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 6242 / NBRC 107633 / OCM 468 / ACE-M.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000300 Genomic DNA. Translation: ABE51262.1.
RefSeqYP_565012.1. NC_007955.1.

3D structure databases

ProteinModelPortalQ12Z64.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING259564.Mbur_0255.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE51262; ABE51262; Mbur_0255.
GeneID3998750.
KEGGmbu:Mbur_0255.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0213.
HOGENOMHOG000252767.
KOK00758.
OMADVWRRMI.
ProtClustDBPRK04350.

Enzyme and pathway databases

BioCycMBUR259564:GHBZ-266-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.
IPR006657. MoPterin_dinucl-bd_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.
PF01568. Molydop_binding. 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_METBU
AccessionPrimary (citable) accession number: Q12Z64
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 22, 2006
Last modified: February 19, 2014
This is version 57 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