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F6X2V8 (MTAP_CIOIN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 22. 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
OrganismCiona intestinalis (Transparent sea squirt) (Ascidia intestinalis) [Reference proteome]
Taxonomic identifier7719 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataTunicataAscidiaceaEnterogonaPhlebobranchiaCionidaeCiona

Protein attributes

Sequence length280 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 – 280280S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_03155
PRO_0000415116

Regions

Region60 – 612Phosphate binding By similarity
Region93 – 942Phosphate binding By similarity
Region220 – 2223Substrate binding By similarity

Sites

Binding site181Phosphate 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
F6X2V8 [UniParc].

Last modified July 27, 2011. Version 1.
Checksum: FDA5FC0E8A8A4B58

FASTA28030,829
        10         20         30         40         50         60 
MMESGDRQNN KIGIIGGSGL ESIELFTVKD KVNCNTPYGK PSSSLINGTL NGIECVLLSR 

        70         80         90        100        110        120 
HGDSHDIMPT DVNYRANLYA LKEAGCSIIL ATTACGSLQE ELKPTDFVVI DQFIDRTTKR 

       130        140        150        160        170        180 
HSTFYDGQNV QMKGVCHIPM RNPFCEKLQN VLLSACNVNN VSCHSKGTMV TIEGPRFSTY 

       190        200        210        220        230        240 
AESNLFRKWG GSLINMTTVP EVVLANELGM LYAALAMVTD YDCWKEDHAS VNVENVMKTM 

       250        260        270        280 
KVNRGNALKV LVSAVEIISK QNLQPDIQLA EKNAKNSVML 

« Hide

Cross-references

Sequence databases

RefSeqXP_002131665.1. XM_002131629.2.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100177521.
KEGGcin:100177521.

Phylogenomic databases

KOK00772.

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_CIOIN
AccessionPrimary (citable) accession number: F6X2V8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: July 27, 2011
Last modified: June 11, 2014
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways