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A0RVQ7 (MTAP_CENSY) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
S-methyl-5'-thioadenosine phosphorylase

EC=2.4.2.28
Alternative name(s):
5'-methylthioadenosine phosphorylase
Short name=MTA phosphorylase
Short name=MTAP
Gene names
Name:mtnP
Ordered Locus Names:CENSYa_0791
OrganismCenarchaeum symbiosum (strain A) [Reference proteome] [HAMAP]
Taxonomic identifier414004 [NCBI]
Taxonomic lineageArchaeaThaumarchaeotaCenarchaealesCenarchaeaceaeCenarchaeum

Protein attributes

Sequence length240 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates By similarity. HAMAP-Rule MF_01963

Catalytic activity

S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate. HAMAP-Rule MF_01963

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (phosphorylase route): step 1/1. HAMAP-Rule MF_01963

Subunit structure

Homohexamer. Dimer of a homotrimer By similarity. HAMAP-Rule MF_01963

Sequence similarities

Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 240240S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_01963
PRO_0000415103

Regions

Region36 – 372Phosphate binding By similarity
Region69 – 702Phosphate binding By similarity
Region187 – 1893Substrate binding By similarity

Sites

Binding site1631Substrate; via amide nitrogen By similarity
Binding site1641Phosphate By similarity
Site1451Important for substrate specificity By similarity
Site1981Important for substrate specificity By similarity

Sequences

Sequence LengthMass (Da)Tools
A0RVQ7 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: E9CEEEFD720F522A

FASTA24025,982
        10         20         30         40         50         60 
MLDNAEELSM DTPYGAPSDT ITLGGIGGRR LAFIPRHGKK HNIAPHKINY RANIWALQKL 

        70         80         90        100        110        120 
GVSRVVAPSA VGSLREELAP GRFVVPSQFL DFTRTREGSF SEDGRVIHIS VAEPFCPELR 

       130        140        150        160        170        180 
TVLLDAAGDA HDGGTYACIE GPRFSTRAES ALFRAAGADI IGMTMVPECQ LSREAQMCYA 

       190        200        210        220        230        240 
SVSTVTDYDA WAEKAVTAKE VLATLADNVE RTKALLAKLI PTIPRDRKCT CADALAEAEF 

« Hide

References

[1]"Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum symbiosum."
Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y., Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.
Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DP000238 Genomic DNA. Translation: ABK77424.1.
RefSeqYP_875728.1. NC_014820.1.

3D structure databases

ProteinModelPortalA0RVQ7.
SMRA0RVQ7. Positions 2-238.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK77424; ABK77424; CENSYa_0791.
GeneID6370971.
KEGGcsy:CENSYa_0791.

Phylogenomic databases

HOGENOMHOG000228987.
KOK00772.
OMAESRWYSK.

Enzyme and pathway databases

UniPathwayUPA00904; UER00873.

Family and domain databases

Gene3D3.40.50.1580. 1 hit.
HAMAPMF_01963. MTAP.
InterProIPR010044. MTAP.
IPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view]
PANTHERPTHR11904. PTHR11904. 1 hit.
PfamPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
TIGRFAMsTIGR01694. MTAP. 1 hit.
PROSITEPS01240. PNP_MTAP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMTAP_CENSY
AccessionPrimary (citable) accession number: A0RVQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: January 9, 2007
Last modified: February 19, 2014
This is version 40 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

PATHWAY comments

Index of metabolic and biosynthesis pathways