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

Q0U796 (MTAP_PHANO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 48. 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
Short name=MTAPase
Gene names
ORF Names:SNOG_12368
OrganismPhaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Septoria nodorum) [Reference proteome]
Taxonomic identifier321614 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaePhaeosphaeriaceaeParastagonospora

Protein attributes

Sequence length344 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_03155

Catalytic activity

S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate. HAMAP-Rule MF_03155

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_03155

Subunit structure

Homotrimer By similarity. HAMAP-Rule MF_03155

Subcellular location

Cytoplasm By similarity. Nucleus By similarity HAMAP-Rule MF_03155.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 344344S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_03155
PRO_0000415132

Regions

Region99 – 1002Phosphate binding By similarity
Region132 – 1332Phosphate binding By similarity
Region258 – 2603Substrate binding By similarity

Sites

Binding site511Phosphate By similarity
Binding site2341Substrate; via amide nitrogen By similarity
Binding site2351Phosphate By similarity
Site2161Important for substrate specificity By similarity
Site2721Important for substrate specificity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0U796 [UniParc].

Last modified February 5, 2008. Version 2.
Checksum: 2BA85D8DF4E3577A

FASTA34438,059
        10         20         30         40         50         60 
MLQRARLWPP IFTSRCAPFP FSRSISIPYR RMAGVPSTYD APVHIAVIGG TGISSLPGFE 

        70         80         90        100        110        120 
LAATLDVDTP WGKPSSPISI LQHNSPTTGK PVPVAFLSRH GLHHEHAPHE VKNQANIAAL 

       130        140        150        160        170        180 
RHIGVRTIIA FSAVGSLQEE VRPRDFVVPD QIIDRTKGIR PFTFFEKGMV GHVGFGDPFD 

       190        200        210        220        230        240 
KSLAEIVRKC GHSLEGEGVR LHDKGLLICM EGPQFSTRAE SNLYRTWGGS VINMSALPEA 

       250        260        270        280        290        300 
KLAREAEISY QMICMATDYD CWRGDGSEDV NVEMVMAHMK ANAENARRFV GAVLNELTKE 

       310        320        330        340 
EHGELVLAKH IEGQMRFAGA MTKKEGRGQD AEKKLQWLFP GYFD 

« Hide

References

[1]"Dothideomycete-plant interactions illuminated by genome sequencing and EST analysis of the wheat pathogen Stagonospora nodorum."
Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L., Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E., Torriani S.F.F., McDonald B.A., Oliver R.P.
Plant Cell 19:3347-3368(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SN15 / ATCC MYA-4574 / FGSC 10173.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH445346 Genomic DNA. Translation: EAT80181.2.
RefSeqXP_001802590.1. XM_001802538.1.

3D structure databases

ProteinModelPortalQ0U796.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSNOT_12368; SNOT_12368; SNOG_12368.
GeneID5979499.
KEGGpno:SNOG_12368.

Phylogenomic databases

KOK00772.
OrthoDBEOG77DJGM.

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.
[Graphical view]
PANTHERPTHR11904. PTHR11904. 1 hit.
PfamPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
SUPFAMSSF53167. SSF53167. 1 hit.
TIGRFAMsTIGR01694. MTAP. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMTAP_PHANO
AccessionPrimary (citable) accession number: Q0U796
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: February 5, 2008
Last modified: June 11, 2014
This is version 48 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways