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C0NRX4 (MTAP_AJECG) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 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
ORF Names:HCBG_05904
OrganismAjellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432) (Darling's disease fungus) (Histoplasma capsulatum) [Reference proteome]
Taxonomic identifier447093 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesAjellomycetaceaeAjellomyces

Protein attributes

Sequence length313 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 – 313313S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_03155
PRO_0000415123

Regions

Region68 – 692Phosphate binding By similarity
Region101 – 1022Phosphate binding By similarity
Region227 – 2293Substrate binding By similarity

Sites

Binding site201Phosphate By similarity
Binding site2031Substrate; via amide nitrogen By similarity
Binding site2041Phosphate By similarity
Site1851Important for substrate specificity By similarity
Site2401Important for substrate specificity By similarity

Sequences

Sequence LengthMass (Da)Tools
C0NRX4 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: CAE309E63FE7494B

FASTA31334,036
        10         20         30         40         50         60 
MAALRDTYND PVHIAVIGGT GLRELPHFTQ VASLNITTPW GPPSSPITIL HHTCSTSGKV 

        70         80         90        100        110        120 
VPVAFLSRHG LHHEYAPHEV PARANIAALR SIGVRSIVAF SAVGSLQEAI KPRDFVVPDQ 

       130        140        150        160        170        180 
VIDRTKGVRP WTFFEGGAVA HVGFADPFDE QMAKVVRACG HSLEGDGVVL HDRGTLICME 

       190        200        210        220        230        240 
GPQFSTRAES NLYRSWGGSI INMSCIPEAK LAREAEIAYQ MICMSTDYDC WHSEAADVTV 

       250        260        270        280        290        300 
DMVMANMKMN SVNARNFIGA VLDELTKDEH AALVQAKHLE GTCKFGLSTS PGYLSAEALT 

       310 
KLSWLFPGYF SNN 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
GG663370 Genomic DNA. Translation: EEH05640.1.

3D structure databases

ProteinModelPortalC0NRX4.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

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_AJECG
AccessionPrimary (citable) accession number: C0NRX4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: May 5, 2009
Last modified: June 11, 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