Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q59ST1 (MTAP_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 61. 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
Name:MEU1
ORF Names:CaO19.14200, CaO19.6938
OrganismCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) [Reference proteome]
Taxonomic identifier237561 [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
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 – 344344S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_03155
PRO_0000415124

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
Q59ST1 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: 28EA961C08D0C36F

FASTA34437,618
        10         20         30         40         50         60 
MVKLVLKGNN LSKLIKMSVH REKIDLAKLP HHYDGPVTLA VIGGTGLYDL PNLHPVARLT 

        70         80         90        100        110        120 
ISTPWGFPSG SITISKTDSG FPVAFLARHG AHHDLLPSDV PSRANIAALK RLGVKAIIAF 

       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

References

[1]"The diploid genome sequence of Candida albicans."
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S.
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314 / ATCC MYA-2876.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AACQ01000148 Genomic DNA. Translation: EAK93531.1.
AACQ01000147 Genomic DNA. Translation: EAK93568.1.
RefSeqXP_712702.1. XM_707609.1.
XP_712739.1. XM_707646.1.

3D structure databases

ProteinModelPortalQ59ST1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5476.CAL0000248.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3645635.
3645671.
KEGGcal:CaO19.14200.
cal:CaO19.6938.

Organism-specific databases

CGDCAL0000248. orf19.6938.

Phylogenomic databases

eggNOGCOG0005.
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.
TIGRFAMsTIGR01694. MTAP. 1 hit.
PROSITEPS01240. PNP_MTAP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMTAP_CANAL
AccessionPrimary (citable) accession number: Q59ST1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: April 26, 2005
Last modified: April 16, 2014
This is version 61 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

Candida albicans

Candida albicans: entries and gene names