Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A2SPI9 (AMPPA_METLZ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 50. 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:Mlab_0067
OrganismMethanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z) [Complete proteome] [HAMAP]
Taxonomic identifier410358 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesMethanocorpusculaceaeMethanocorpusculum

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_0000314726

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
A2SPI9 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: D3756779BAE97100

FASTA50553,294
        10         20         30         40         50         60 
MNLILDMIDI STPVILLNDT DARQIGVLEG DRVTITRIKT KHTIAAPVSI TKTLTSQGTA 

        70         80         90        100        110        120 
TISLGTNENL AAEKGDEIEI RAAPRPASIA FIRKKMDGGK FTREETATII SDMSSNVLSP 

       130        140        150        160        170        180 
SEITAYITAA YINGLDMDEV EFLTREMVAS GEQITFSKKP VVDKHSIGGV PGNKITLLVV 

       190        200        210        220        230        240 
PVIAASGLLI PKTSSRAITG AGGTADLMEA LAPVAFSAAE IKTMTEKAGG VIVWGGATNI 

       250        260        270        280        290        300 
APADDMIVTY EYPLKIDARG QMLASIMAKK MAVGSDTCVI DIPIGPGTKI PDEAEGRVLA 

       310        320        330        340        350        360 
NELITLGNRL GIRVECAVTF GGSPIGRNIG VNLEVSEALS LLEGKRGANS LVQKSVAIAG 

       370        380        390        400        410        420 
IALEMTGKTG ADSGAEAAYD IIKKGKALKK MLDIIEIQGG DPKVKSTDFP VGEHTFVVPA 

       430        440        450        460        470        480 
ASDGYVVSVK NQALISIARA AGSPVDHGAG LHLHKKPGEY VKRGEPLLTI YAERGWRLTR 

       490        500 
AIEEARTSYP VLVEGMLLER ISSNR 

« Hide

References

[1]"Complete genome sequence of Methanocorpusculum labreanum type strain Z."
Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A., Copeland A., Glavina Del Rio T., Tice H., Dalin E., Barry K., Pitluck S., Hauser L., Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.
Stand. Genomic Sci. 1:197-203(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43576 / DSM 4855 / Z.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000559 Genomic DNA. Translation: ABN06245.1.
RefSeqYP_001029512.1. NC_008942.1.

3D structure databases

ProteinModelPortalA2SPI9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING410358.Mlab_0067.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN06245; ABN06245; Mlab_0067.
GeneID4795851.
KEGGmla:Mlab_0067.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0213.
HOGENOMHOG000252767.
KOK00758.
OMAESVPGFH.
ProtClustDBPRK04350.

Enzyme and pathway databases

BioCycMLAB410358:GH7C-67-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_METLZ
AccessionPrimary (citable) accession number: A2SPI9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 6, 2007
Last modified: February 19, 2014
This is version 50 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