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D5GFR0 (MTAP_TUBMM) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 25. 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:GSTUM_00007013001
OrganismTuber melanosporum (strain Mel28) (Perigord black truffle) [Reference proteome]
Taxonomic identifier656061 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaPezizomycetesPezizalesTuberaceaeTuber

Protein attributes

Sequence length309 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 caution

The sequence CAZ83353.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

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-UniPathway

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-EC

phosphorylase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 309309S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_03155
PRO_0000415136

Regions

Region64 – 652Phosphate binding By similarity
Region97 – 982Phosphate binding By similarity
Region225 – 2273Substrate binding By similarity

Sites

Binding site191Phosphate By similarity
Binding site2011Substrate; via amide nitrogen By similarity
Binding site2021Phosphate By similarity
Site1831Important for substrate specificity By similarity
Site2381Important for substrate specificity By similarity

Sequences

Sequence LengthMass (Da)Tools
D5GFR0 [UniParc].

Last modified January 25, 2012. Version 2.
Checksum: 0D3FA92C97BF9093

FASTA30933,148
        10         20         30         40         50         60 
MPLPDTFSES VRIAVIGGTG ISALEAEGFT AVASLDIQTP YGAPGSPLTI LKTPQNTPIA 

        70         80         90        100        110        120 
FLSRHGLHHE LTPTEIPNRA NIAALRSIGV RSIIAFSAVG SLQEHIRPRD FVVPSQIIDR 

       130        140        150        160        170        180 
TKGLRASTFF EGGLVGHVGF ADPFDSELSK VVFDIGSDGV LNGEGVKMHK DALLICMEGP 

       190        200        210        220        230        240 
QFSTRAESNL YRSWGGDVIN MSALPEAKLA KEAEIAYVMV CMSTDYDCWK TNEAAVTVET 

       250        260        270        280        290        300 
VMGNMHANGA NAKHLAAAIL KELAKEEHQD LVGAKHLEGL SKWACCTAPA GRKAEVVKKI 


EFMLPGYFS 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FN430220 Genomic DNA. Translation: CAZ83353.1. Different initiation.
UniGeneTme.3343.

3D structure databases

ProteinModelPortalD5GFR0.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCAZ83353; CAZ83353; GSTUM_00007013001.

Phylogenomic databases

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_TUBMM
AccessionPrimary (citable) accession number: D5GFR0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: January 25, 2012
Last modified: April 16, 2014
This is version 25 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