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A8P7Y3 (MTAP_COPC7) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 37. 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:CC1G_06667
OrganismCoprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003) (Inky cap fungus) (Hormographiella aspergillata) [Reference proteome]
Taxonomic identifier240176 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesPsathyrellaceaeCoprinopsis

Protein attributes

Sequence length324 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 – 324324S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_03155
PRO_0000415126

Regions

Region57 – 582Phosphate binding By similarity
Region90 – 912Phosphate binding By similarity
Region220 – 2223Substrate binding By similarity

Sites

Binding site141Phosphate By similarity
Binding site1961Substrate; via amide nitrogen By similarity
Binding site1971Phosphate By similarity
Site1781Important for substrate specificity By similarity
Site2331Important for substrate specificity By similarity

Sequences

Sequence LengthMass (Da)Tools
A8P7Y3 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: E040B635EF883BE6

FASTA32435,186
        10         20         30         40         50         60 
MSEENVLIGV IGGSGLYQLD NLTVVKTVNP ETPWGFPSSP ITIAALPSGT KVAFLARHGI 

        70         80         90        100        110        120 
GHVIPPSSVP STANIAALKS LGVSAILSFS AVGSLREEIS PGSFALPSQI IDRTKGIRDS 

       130        140        150        160        170        180 
SFFNGTSIVA HAMFGDPFSN KLIRWLEPRV RKALEKEGKG KLLFTDKTIV CMEGPQFSTR 

       190        200        210        220        230        240 
AESVMYRQWG GDLINMSVLP EAKLAREAEL SYALIAMATD YDSWRPHSDA VTAHDVVQTL 

       250        260        270        280        290        300 
HDNGASAKLV LSTILDDLHT TINTHHRALT NGNSQDLEAI REEEALLQER GSMKFSIMPA 

       310        320 
SPQQKAEDRK KLAFILPEHF KDAA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AACS02000005 Genomic DNA. Translation: EAU82357.1.
RefSeqXP_001839454.1. XM_001839402.2.

3D structure databases

ProteinModelPortalA8P7Y3.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6016068.
KEGGcci:CC1G_06667.

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

Entry information

Entry nameMTAP_COPC7
AccessionPrimary (citable) accession number: A8P7Y3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: January 15, 2008
Last modified: June 11, 2014
This is version 37 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