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C4YQD9 (MTAP_CANAW) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 28. 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
Name:MEU1
ORF Names:CAWG_02696
OrganismCandida albicans (strain WO-1) (Yeast) [Complete proteome]
Taxonomic identifier294748 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length344 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
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 – 344344S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_03155
PRO_0000415125

Regions

Region88 – 892Phosphate binding By similarity
Region121 – 1222Phosphate binding By similarity
Region262 – 2643Substrate binding By similarity

Sites

Binding site451Phosphate By similarity
Binding site2381Substrate; via amide nitrogen By similarity
Binding site2391Phosphate By similarity
Site2201Important for substrate specificity By similarity
Site2751Important for substrate specificity By similarity

Sequences

Sequence LengthMass (Da)Tools
C4YQD9 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: F46085046FB08F8B

FASTA34437,552
        10         20         30         40         50         60 
MAKLVLKGNN LSKLIKMSVH REKIDLAKLP HHYDGPVTLA VIGGTGLYDL PNLHPVARLT 

        70         80         90        100        110        120 
ISTSWGFPSG SITISKTDSG FPVAFLARHG AHHDLLPSDV PSRANIAALK KLGVKAIIAF 

       130        140        150        160        170        180 
SAVGSLQQEI KPRDFVLPTQ IIDRTKGIRP STFFEKGFVA HAMFGEPFDL KLNKLISDAI 

       190        200        210        220        230        240 
PSKGFLEGFD TDGTPVLHTK ENTNNGEDLT IICMEGPQFS TRAESRLYRS WGGSVINMSV 

       250        260        270        280        290        300 
LPEAKLAREA EIAYQMICMS TDYDSWNESE EPVTVETVVG NLKANSANAC KLAAKLIDEF 

       310        320        330        340 
AAKGGEIGKD LQGSMKYAVS TSPHGVKKEL LEKMHFLFPG YWEV 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CM000310 Genomic DNA. Translation: EEQ44428.1.

3D structure databases

ProteinModelPortalC4YQD9.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOGENOMHOG000228986.
OMAGCADVLK.
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_CANAW
AccessionPrimary (citable) accession number: C4YQD9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: July 28, 2009
Last modified: April 16, 2014
This is version 28 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