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

C7YLQ3 (MTAP_NECH7) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 31. 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:NECHADRAFT_67177
OrganismNectria haematococca (strain 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI) (Fusarium solani subsp. pisi) [Reference proteome]
Taxonomic identifier660122 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaemitosporic NectriaceaeFusariumFusarium solani species complex

Protein attributes

Sequence length307 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 307307S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_03155
PRO_0000415129

Regions

Region62 – 632Phosphate binding By similarity
Region95 – 962Phosphate binding By similarity
Region221 – 2233Substrate binding By similarity

Sites

Binding site201Phosphate By similarity
Binding site1971Substrate; via amide nitrogen By similarity
Binding site1981Phosphate By similarity
Site1791Important for substrate specificity By similarity
Site2331Important for substrate specificity By similarity

Sequences

Sequence LengthMass (Da)Tools
C7YLQ3 [UniParc].

Last modified October 13, 2009. Version 1.
Checksum: 9323A88A26A7E0A0

FASTA30733,543
        10         20         30         40         50         60 
MGDLPTTFDK PVHIAVIGGT GLGQLEGFEP IAALNPITPW GAPASPIQIL SHKGVNVAFL 

        70         80         90        100        110        120 
ARHGIHHQFA PHEVPNRANI AALRHIGVRC VIAFSAVGSL QEEIKPMDFV VPDQVIDRTK 

       130        140        150        160        170        180 
GVRPFTFFEG GVVGHVGFAD PFDAGLAKVV KTCAEHMEGD GVVLHEKGTV IVMEGPQFST 

       190        200        210        220        230        240 
RAESHMYRSW GGSVINMSTL PEAKLAREAE MAYQVIAMAT DYDCWHSFED VNVEMVGKYM 

       250        260        270        280        290        300 
KANSKNAKRL VGAVLDRLAD LDNSDLVLAK HWQGASQGAV KFMTKPEGRD PEAMKRVEYL 


FPGFWEE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
GG698897 Genomic DNA. Translation: EEU47310.1.
RefSeqXP_003053023.1. XM_003052977.1.

3D structure databases

ProteinModelPortalC7YLQ3.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiNechaT67177; NechaP67177; NechaG67177.
GeneID9663789.
KEGGnhe:NECHADRAFT_67177.

Phylogenomic databases

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

Entry information

Entry nameMTAP_NECH7
AccessionPrimary (citable) accession number: C7YLQ3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: October 13, 2009
Last modified: February 19, 2014
This is version 31 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