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Q5KPU2 (MTAP_CRYNJ) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 68. 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
Ordered Locus Names:CNA01530
OrganismCryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) (Filobasidiella neoformans) [Reference proteome]
Taxonomic identifier214684 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaTremellomycetesTremellalesTremellaceaeFilobasidiellaFilobasidiella/Cryptococcus neoformans species complex

Protein attributes

Sequence length303 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 – 303303S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_03155
PRO_0000415127

Regions

Region58 – 592Phosphate binding By similarity
Region91 – 922Phosphate binding By similarity
Region220 – 2223Substrate binding By similarity

Sites

Binding site151Phosphate 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
Q5KPU2 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 852840F01808DC68

FASTA30333,121
        10         20         30         40         50         60 
MENNEKVLVG CIGGSGLYHL DNLTFVKTVH IETPWGKPSS PINISSLPSG ALVAFISRHG 

        70         80         90        100        110        120 
SHHSITPSEV PCRANIAALK HIGCEAIIAF SAVGSLREEI APGHFIIPDQ IIDRTKGIRE 

       130        140        150        160        170        180 
DTFFRGEGLV VHSMFGEPFS QKLNAFVAPR VEKILKETGD VVLHTGKTVV CMEGPAFSTR 

       190        200        210        220        230        240 
AESLMYRQWG GDIINMSVIP EAKLAREAEL DYTLICTSTD FDAWRTGYDP VTVEEVVKVL 

       250        260        270        280        290        300 
HTNAGNSRAV AAGILQDVHD VVVEGKTLTD IKGSMKFACV TRKDIQPEAS RKKLSYILPY 


FSD 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017341 Genomic DNA. Translation: AAW40807.1.
RefSeqXP_566626.1. XM_566626.1.

3D structure databases

ProteinModelPortalQ5KPU2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING214684.CNA01530.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiAAW40807; AAW40807; CNA01530.
GeneID3253655.
KEGGcne:CNA01530.

Phylogenomic databases

HOGENOMHOG000228986.
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_CRYNJ
AccessionPrimary (citable) accession number: Q5KPU2
Secondary accession number(s): Q560U2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: February 15, 2005
Last modified: April 16, 2014
This is version 68 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