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Q8DJE4 (MTAP_THEEB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 55. 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
Gene names
Name:mtnP
Ordered Locus Names:tlr1281
OrganismThermosynechococcus elongatus (strain BP-1) [Reference proteome] [HAMAP]
Taxonomic identifier197221 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus

Protein attributes

Sequence length289 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_01963

Catalytic activity

S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate. HAMAP-Rule MF_01963

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_01963

Subunit structure

Homohexamer. Dimer of a homotrimer By similarity. HAMAP-Rule MF_01963

Sequence similarities

Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 289289S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_01963
PRO_0000415101

Regions

Region53 – 542Phosphate binding By similarity
Region86 – 872Phosphate binding By similarity
Region211 – 2133Substrate binding By similarity

Sites

Binding site111Phosphate By similarity
Binding site1871Substrate; via amide nitrogen By similarity
Binding site1881Phosphate By similarity
Site1691Important for substrate specificity By similarity
Site2241Important for substrate specificity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8DJE4 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: E78D1687C7C49704

FASTA28931,354
        10         20         30         40         50         60 
MTAKIGIIGG SGLYKMEALT DVEEVRLTTP FGDPSDAFIC GKIGGVPVVF LARHGRHHHL 

        70         80         90        100        110        120 
LPTEIPFRAN IYGFKSLGVE YLLSASAVGS LQEAVKPLDI VVPDQFIDRT RNRISTFFGD 

       130        140        150        160        170        180 
GIVAHIGFAD PVCPALAGVL ADAIADLNLP DVTLHRQGTY VCMEGPAFST LAESNLYRSW 

       190        200        210        220        230        240 
GGTVIGMTNL PEAKLAREAE IAYATLALVT DYDCWHPEHD SVTVEMIMGN LQRNVKNAQA 

       250        260        270        280 
IICETVKRVH AHPPVSKAHR ALKNAILTPL DQVPAATKEK LHLLLAKYL 

« Hide

References

[1]"Complete genome structure of the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1."
Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takeuchi C., Yamada M., Tabata S.
DNA Res. 9:123-130(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BP-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000039 Genomic DNA. Translation: BAC08833.1.
RefSeqNP_682071.1. NC_004113.1.

3D structure databases

ProteinModelPortalQ8DJE4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING197221.tlr1281.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC08833; BAC08833; BAC08833.
GeneID1011666.
KEGGtel:tlr1281.
PATRIC23927900. VBITheElo119873_1348.

Phylogenomic databases

eggNOGCOG0005.
HOGENOMHOG000228986.
KOK00772.
OMACEAQLCY.
OrthoDBEOG6KHFXC.

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.
[Graphical view]
PANTHERPTHR11904. PTHR11904. 1 hit.
PfamPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
SUPFAMSSF53167. SSF53167. 1 hit.
TIGRFAMsTIGR01694. MTAP. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMTAP_THEEB
AccessionPrimary (citable) accession number: Q8DJE4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: March 1, 2003
Last modified: May 14, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways