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P0DJF9 (MTAP_SYNYG) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 16. 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:SYNGTS_1998
OrganismSynechocystis sp. (strain PCC 6803 / GT-S) [Complete proteome] [HAMAP]
Taxonomic identifier1111707 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis

Protein attributes

Sequence length326 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 – 326326S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_01963
PRO_0000416437

Regions

Region86 – 872Phosphate binding By similarity
Region119 – 1202Phosphate binding By similarity
Region244 – 2463Substrate binding By similarity

Sites

Binding site441Phosphate By similarity
Binding site2201Substrate; via amide nitrogen By similarity
Binding site2211Phosphate By similarity
Site2021Important for substrate specificity By similarity
Site2571Important for substrate specificity By similarity

Sequences

Sequence LengthMass (Da)Tools
P0DJF9 [UniParc].

Last modified March 21, 2012. Version 1.
Checksum: 06F7D98E67A7BCD8

FASTA32635,319
        10         20         30         40         50         60 
MGMIISMAMT AVTIWTKTKP GRVSCFIRKN STMVNAPIGI IGGSGLYQME ALKNVEEVTL 

        70         80         90        100        110        120 
DTPFGAPSDS FIVGELAGVR VAFLARHGRG HHLLPSEIPF RANIHGMKQL GVKYLISASA 

       130        140        150        160        170        180 
VGSLQAEAKP LDMVVPDQFI DRTRQRISTF FGEGIVAHIG FGNPICPQLA QCLSTAIAGL 

       190        200        210        220        230        240 
ELEGVTLHDR GTYVSMEGPA FSTIAESNLY RSWGGTVIGM TNLPEAKLAR EAEIAYATLA 

       250        260        270        280        290        300 
LVTDYDCWHP DHDHVTVEMV IGNLQKNAVN AQQVILETVK QLAANPFESI AHRALQYAVL 

       310        320 
TPPDKFPAAT YEKLSLLLGK YYPPAP 

« Hide

References

[1]"Genomic structure of the cyanobacterium Synechocystis sp. PCC 6803 strain GT-S."
Tajima N., Sato S., Maruyama F., Kaneko T., Sasaki N.V., Kurokawa K., Ohta H., Kanesaki Y., Yoshikawa H., Tabata S., Ikeuchi M., Sato N.
DNA Res. 18:393-399(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 6803 / GT-S.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP012205 Genomic DNA. Translation: BAK50746.1.
RefSeqNP_441892.1. NC_000911.1.
YP_005651951.1. NC_017277.1.
YP_007451772.1. NC_020286.1.

3D structure databases

ProteinModelPortalP0DJF9.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAK50746; BAK50746; SYNGTS_1998.
GeneID952850.
KEGGsyn:sll0135.
syy:SYNGTS_1998.
syz:MYO_120170.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK00772.

Enzyme and pathway databases

BioCycSSP1148:GJOT-2026-MONOMER.
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_SYNYG
AccessionPrimary (citable) accession number: P0DJF9
Secondary accession number(s): P74469
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2012
Last sequence update: March 21, 2012
Last modified: July 9, 2014
This is version 16 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