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A3CSY4 (AMPPA_METMJ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 49. 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:Memar_0551
OrganismMethanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1) [Complete proteome] [HAMAP]
Taxonomic identifier368407 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesMethanomicrobiaceaeMethanoculleus

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 = 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 – 507507AMP phosphorylase HAMAP-Rule MF_02132
PRO_0000314727

Regions

Nucleotide binding195 – 2006AMP By similarity

Sites

Active site2571Proton donor By similarity
Binding site1691AMP; via amide nitrogen By similarity
Binding site2041AMP; via amide nitrogen By similarity
Binding site2651AMP By similarity
Binding site2891AMP By similarity

Sequences

Sequence LengthMass (Da)Tools
A3CSY4 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: E68D40285499FDFC

FASTA50754,481
        10         20         30         40         50         60 
MKLTVKLLDI ENRGVLLHCT DARSMRVRDG DRVQIVDEAT GKTAQAHVDT TGSLIEPGVI 

        70         80         90        100        110        120 
GVYRPVNATL AVDEGTPVEV RGAERPASLE HIKKKMDGGR FTKDDTVDIV RDIVDDVLSP 

       130        140        150        160        170        180 
GEITAYVTAS YINGLDMDEV EYLTRATVET GERLHFTRHP IVDKHSIGGV PGNKITLLIA 

       190        200        210        220        230        240 
PIIAASGLLI PKTSSRAITG AGGTADLMEV LAPVSFPALE VQQMTEKVGG AIVWGGATNI 

       250        260        270        280        290        300 
APADDKIITY EYPLRIDARG QMIASVMAKK FAVGADLVVI DIPVGRNTKI ATAQEGRKLA 

       310        320        330        340        350        360 
REFIDLGERL GMRVECALSY GESLVGHTIG PNLEVREALA VLEGATEPNS LIQKSLSLAG 

       370        380        390        400        410        420 
IALEMAGKAG PGQGARAAAD ILRSGKALEK MRQIIEIQGG DPNVKAEDIV PGECRFDVNA 

       430        440        450        460        470        480 
PQDGYVIELN NSALVTLARL AGSPYDHGAG LLVHAKKGTR VRKGDPIFTI YADREWRLER 

       490        500 
AIEVGRTLMP VLVEGMVLER IPHERWV 

« Hide

References

[1]"Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1."
Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A., Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C., Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L., Land M. expand/collapse author list , Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.
Stand. Genomic Sci. 1:189-196(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35101 / DSM 1498 / JR1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000562 Genomic DNA. Translation: ABN56484.1.
RefSeqYP_001046466.1. NC_009051.1.

3D structure databases

ProteinModelPortalA3CSY4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING368407.Memar_0551.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN56484; ABN56484; Memar_0551.
GeneID4846965.
KEGGmem:Memar_0551.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0213.
HOGENOMHOG000252767.
KOK00758.
OMACHSEGFE.
ProtClustDBPRK04350.

Enzyme and pathway databases

BioCycMMAR368407:GH7L-563-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_METMJ
AccessionPrimary (citable) accession number: A3CSY4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 20, 2007
Last modified: February 19, 2014
This is version 49 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