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A0B6C9 (AMPPA_METTP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 56. 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:Mthe_0462
OrganismMethanosaeta thermophila (strain DSM 6194 / PT) (Methanothrix thermophila (strain DSM 6194 / PT)) [Complete proteome] [HAMAP]
Taxonomic identifier349307 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosaetaceaeMethanosaeta

Protein attributes

Sequence length512 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 – 512512AMP phosphorylase HAMAP-Rule MF_02132
PRO_0000314729

Regions

Nucleotide binding192 – 1976AMP By similarity

Sites

Active site2541Proton donor By similarity
Binding site1661AMP; via amide nitrogen By similarity
Binding site2011AMP; via amide nitrogen By similarity
Binding site2621AMP By similarity
Binding site2861AMP By similarity

Sequences

Sequence LengthMass (Da)Tools
A0B6C9 [UniParc].

Last modified November 28, 2006. Version 1.
Checksum: 0C521FACEB78335E

FASTA51255,406
        10         20         30         40         50         60 
MFEVVPFDIE IGQYKVMLNI ADARAMGLNP GDRVRVRTRG ASLTAILDVT GQMIGQGQVG 

        70         80         90        100        110        120 
IFTEAFRDLK EAKSVEISPA PRPASISYIK MLMDRQKLSE DQIRSIVRDI VYNNLSEIEL 

       130        140        150        160        170        180 
SAYITASYIH NLDPQETEWL TRAMIETGER IYFDKHPVVD KHSIGGVPGN KVSMLVVPIV 

       190        200        210        220        230        240 
AASGLLIPKT SSRAITGAGG TADLMEVLAP VEFTADEIKE ITETVGGVIA WGGATNIAPA 

       250        260        270        280        290        300 
DDRLIKAEYA LAIDPYSQML ASIMAKKGAV GADAVVVDMP TGPGTKLETP EKARVLAKDL 

       310        320        330        340        350        360 
TDLGERLGIR VECAMTFGGS PVGRTVGPAL EVREALKMLE TGEGPNSLRE KSLALAGILL 

       370        380        390        400        410        420 
EMGGVAARGE GYRAAEEILV SGKAHRKLME IVEAQGGDPK IRSEDIQIGE HQKQILSPTN 

       430        440        450        460        470        480 
GYVVAFYNKR IIEIARAAGA PGDKRAGVII HKKMGEIVKK GEPLLTICSS TDWELECAVK 

       490        500        510 
MCSMRDALEQ PPIVVEGMLL ERYPTERYPR TI 

« Hide

References

[1]"Complete sequence of Methanosaeta thermophila PT."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Smith K.S., Ingram-Smith C., Richardson P.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 6194 / PT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000477 Genomic DNA. Translation: ABK14253.1.
RefSeqYP_842893.1. NC_008553.1.

3D structure databases

ProteinModelPortalA0B6C9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349307.Mthe_0462.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK14253; ABK14253; Mthe_0462.
GeneID4462619.
KEGGmtp:Mthe_0462.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0213.
HOGENOMHOG000252767.
KOK00758.
OMACLIWGGH.

Enzyme and pathway databases

BioCycMMET349307:GHKI-470-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.
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.
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_METTP
AccessionPrimary (citable) accession number: A0B6C9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 28, 2006
Last modified: May 14, 2014
This is version 56 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