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Q4PH43 (MTAP_USTMA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 52. 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:UM00570, UM10466
OrganismUstilago maydis (strain 521 / FGSC 9021) (Corn smut fungus) [Reference proteome]
Taxonomic identifier237631 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaUstilaginomycotinaUstilaginomycetesUstilaginalesUstilaginaceaeUstilago

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.

Sequence caution

The sequence EAK81219.1 differs from that shown. Reason: Erroneous gene model prediction.

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_0000415137

Regions

Region94 – 952Phosphate binding By similarity
Region127 – 1282Phosphate binding By similarity
Region258 – 2603Substrate binding By similarity

Sites

Binding site511Phosphate By similarity
Binding site2341Substrate; via amide nitrogen By similarity
Binding site2351Phosphate By similarity
Site2161Important for substrate specificity By similarity
Site2711Important for substrate specificity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4PH43 [UniParc].

Last modified January 25, 2012. Version 2.
Checksum: 079237753E5CB5F3

FASTA34437,446
        10         20         30         40         50         60 
MLPRVSFVTT SLQQPNVSRC ISVRTLHRRM SVPTVTSWTG APILLGVIGG SGLYKLDSIT 

        70         80         90        100        110        120 
PVAEISISTP WGSASSPITI AKTSAGNHVA FLARHGRDHA ILPSNVPNLA NIAALKHLGV 

       130        140        150        160        170        180 
KAIVAFSAVG SLREEIAPKD FVIPSQIIDR TKGVRRASFF GFGDEESVVA HAGFGDPFCE 

       190        200        210        220        230        240 
TLRPIVYSTV QATLASHPIK VHTDKTVVCM EGPQFSTRAE SLMYRTWGGD IINMSVLPEA 

       250        260        270        280        290        300 
KLAREAEIAY VLIATATDYD AWRPSTAAVN VAEVMESLKA NVEASNLVTT KVLDRVWLEI 

       310        320        330        340 
DTDEKPAVKN IKDSTKFSIM TKSQVIPDKA KQNLRFLHPW FARD 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AACP01000013 Genomic DNA. Translation: EAK81219.1. Sequence problems.
RefSeqXP_756717.1. XM_751624.1.

3D structure databases

ProteinModelPortalQ4PH43.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5270.UM00570.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiUM00570T0; UM00570P0; UM00570.
GeneID3628633.
KEGGuma:UM00570.1.

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

Entry information

Entry nameMTAP_USTMA
AccessionPrimary (citable) accession number: Q4PH43
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: January 25, 2012
Last modified: February 19, 2014
This is version 52 of the entry and version 2 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