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E3XFR6 (MTAP_ANODA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 19. 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:AND_22863
OrganismAnopheles darlingi (Mosquito) [Reference proteome]
Taxonomic identifier43151 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeAnophelinaeAnopheles

Protein attributes

Sequence length281 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-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 – 281281S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_03155
PRO_0000415118

Regions

Region57 – 582Phosphate binding By similarity
Region90 – 912Phosphate binding By similarity
Region217 – 2193Substrate binding By similarity

Sites

Binding site151Phosphate By similarity
Binding site1931Substrate; via amide nitrogen By similarity
Binding site1941Phosphate By similarity
Site1751Important for substrate specificity By similarity
Site2301Important for substrate specificity By similarity

Sequences

Sequence LengthMass (Da)Tools
E3XFR6 [UniParc].

Last modified February 8, 2011. Version 1.
Checksum: 25C4B713B9CF05E5

FASTA28130,799
        10         20         30         40         50         60 
MWIIFSSQIG IIGGSGLDDS QIIENRTERV VNTHFGIPSD VLIEGKIAGV ECVLLARHGR 

        70         80         90        100        110        120 
NHSIMPTNVN YRANIWALKT LGCTHVLVST ATGSLRDEIH PGDIVIPDNF IDRTTKRVQT 

       130        140        150        160        170        180 
FYDGNELLVG VCHIPMEPAF CSRTRDVLIE TARELGTAGV HNSGTVVTIE GPRFSSKAES 

       190        200        210        220        230        240 
NLFRQWGAHL VNMTLVSEVV LAKEAGLCYA AIAMATDYDC WRETGEDVNV ADVLATFKKN 

       250        260        270        280 
VTKVTELIIN AIPKIAALDW TETIEELAKT VNTSIMLPHS N 

« Hide

References

[1]"Combination of measures distinguishes pre-miRNAs from other stem-loops in the genome of the newly sequenced Anopheles darlingi."
Mendes N.D., Freitas A.T., Vasconcelos A.T., Sagot M.F.
BMC Genomics 11:529-529(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
ADMH01003944 Genomic DNA. Translation: EFR19223.1.

3D structure databases

ProteinModelPortalE3XFR6.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_ANODA
AccessionPrimary (citable) accession number: E3XFR6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: February 8, 2011
Last modified: April 16, 2014
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways