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Q291H4 (MTAP_DROPS) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:GA18442
OrganismDrosophila pseudoobscura pseudoobscura (Fruit fly) [Reference proteome]
Taxonomic identifier46245 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length289 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 – 289289S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_03155
PRO_0000415120

Regions

Region66 – 672Phosphate binding By similarity
Region99 – 1002Phosphate binding By similarity
Region226 – 2283Substrate binding By similarity

Sites

Binding site241Phosphate By similarity
Binding site2021Substrate; via amide nitrogen By similarity
Binding site2031Phosphate By similarity
Site1841Important for substrate specificity By similarity
Site2391Important for substrate specificity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q291H4 [UniParc].

Last modified April 4, 2006. Version 1.
Checksum: 2109F54933516F64

FASTA28931,844
        10         20         30         40         50         60 
MLHIKCKDTD LDPIPVKIGI IGGSGLDDPD ILENRQEKVI STPYGEPSDA LIQGEIGGVQ 

        70         80         90        100        110        120 
CVLLARHGRK HDIMPSNVNY RANIWALRDV GCTHLIVSTA CGSLREQIKP GNLVMPHDFI 

       130        140        150        160        170        180 
DRTTKRSQTF YDGSATSPRG VCHLPMYPAF SERTRNILIE AAKELEIPAH EKATIVTIEG 

       190        200        210        220        230        240 
PRFSSRSESL MFREWGGDLI NMTTCPEVVL AKEAGLLYGS VAIATDYDCW RMGCEGVNVQ 

       250        260        270        280 
DVLKTFAENV IKVKKILVNA VGRIAKEDWS EDILNAKQCV CNNTMSGAM 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CM000071 Genomic DNA. Translation: EAL25138.1.
RefSeqXP_001360563.1. XM_001360526.2.

3D structure databases

ProteinModelPortalQ291H4.
SMRQ291H4. Positions 16-277.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7237.FBpp0277616.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0279178; FBpp0277616; FBgn0078444.
GeneID4803922.
KEGGdpo:Dpse_GA18442.

Organism-specific databases

FlyBaseFBgn0078444. Dpse\GA18442.

Phylogenomic databases

InParanoidQ291H4.
KOK00772.
OMACEAQLCY.
OrthoDBEOG771270.
PhylomeDBQ291H4.

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_DROPS
AccessionPrimary (citable) accession number: Q291H4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: April 4, 2006
Last modified: July 9, 2014
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase