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A7EAA1 (MTAP_SCLS1) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 39. 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:SS1G_02233
OrganismSclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum) [Reference proteome]
Taxonomic identifier665079 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaLeotiomycetesHelotialesSclerotiniaceaeSclerotinia

Protein attributes

Sequence length306 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.

Ontologies

Keywords
   Biological processPurine salvage
   Cellular componentCytoplasm
Nucleus
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-methionine salvage from methylthioadenosine

Inferred from electronic annotation. Source: UniProtKB-HAMAP

purine ribonucleoside salvage

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionS-methyl-5-thioadenosine phosphorylase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

phosphorylase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 306306S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_03155
PRO_0000415135

Regions

Region63 – 642Phosphate binding By similarity
Region96 – 972Phosphate binding By similarity
Region222 – 2243Substrate binding By similarity

Sites

Binding site211Phosphate By similarity
Binding site1981Substrate; via amide nitrogen By similarity
Binding site1991Phosphate By similarity
Site1801Important for substrate specificity By similarity
Site2341Important for substrate specificity By similarity

Sequences

Sequence LengthMass (Da)Tools
A7EAA1 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 12F799D117340BF0

FASTA30633,972
        10         20         30         40         50         60 
MVESLPTTFS DSVHIAVIGG TGLQSLEGFI PIATINPLTP WGYPSAPIHI LSHNNTPIAF 

        70         80         90        100        110        120 
LSRHGTHHEL APHEIPNRAN IAALRSMGVR TIIAFSAVGS LREEIKPRDF VVPDQVIDRT 

       130        140        150        160        170        180 
KGVRPFTFFE KGVVGHVGFA DPFDERIAKV VRECGHALEG EGIVLHDKGT IICMEGPAFS 

       190        200        210        220        230        240 
TRAESHMYRS WGGSVINMSA LPEAKLAREA EMVYQMICMA TDYDCWHSTA DVDVEMVMGH 

       250        260        270        280        290        300 
MHANGQNAKR LVGAVLDALN MRWSTIDSIR RRKNKPELAN AQQHQIWRGR TYHFAWSISA 


CYFSSE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH476623 Genomic DNA. Translation: EDN99379.1.
RefSeqXP_001596017.1. XM_001595967.1.

3D structure databases

ProteinModelPortalA7EAA1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING665079.A7EAA1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiEDN99379; EDN99379; SS1G_02233.
GeneID5492464.
KEGGssl:SS1G_02233.

Phylogenomic databases

eggNOGCOG0005.
KOK00772.
OMAHVAFIAR.
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.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view]
PANTHERPTHR11904. PTHR11904. 1 hit.
PfamPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
SUPFAMSSF53167. SSF53167. 1 hit.
TIGRFAMsTIGR01694. MTAP. 1 hit.
PROSITEPS01240. PNP_MTAP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMTAP_SCLS1
AccessionPrimary (citable) accession number: A7EAA1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: September 11, 2007
Last modified: June 11, 2014
This is version 39 of the entry and version 1 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