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Q89VT5 (MTAP_BRADU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:blr0960
OrganismBradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110) [Reference proteome] [HAMAP]
Taxonomic identifier224911 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

Protein attributes

Sequence length291 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 – 291291S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_01963
PRO_0000415090

Regions

Region54 – 552Phosphate binding By similarity
Region87 – 882Phosphate binding By similarity
Region209 – 2113Substrate binding By similarity

Sites

Binding site121Phosphate By similarity
Binding site1851Substrate; via amide nitrogen By similarity
Binding site1861Phosphate By similarity
Site1671Important for substrate specificity By similarity
Site2221Important for substrate specificity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q89VT5 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 4C5769311BFC605E

FASTA29131,461
        10         20         30         40         50         60 
MTQAVLGIIG GSGIYDLPGL EGAHEEVIKS PWGEPSAPLR RGTIAGLPIV FLPRHDKGHR 

        70         80         90        100        110        120 
LSPSDINYRA NIDVLKRAGV TDLISLSACG SFKEEMPPGT FVLVDQFVDR THKRESSFFG 

       130        140        150        160        170        180 
RGCVAHVSMA HPVSPRLRIH LAAAAEAEGI AIARGGTYVC MEGPQFSTYA ESMTYKTSGY 

       190        200        210        220        230        240 
SVIGMTNMPE AKLAREAEIC YATVAMVTDF DCWHPDHDAV TVQDIIRVLT SNADKAKALV 

       250        260        270        280        290 
ARLAKDFPRE HEPCPIGSDR ALDTALITAP EARDPELLKK LDAVAGRVLR G 

« Hide

References

[1]"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110."
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.
DNA Res. 9:189-197(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000040 Genomic DNA. Translation: BAC46225.1.
RefSeqNP_767600.1. NC_004463.1.

3D structure databases

ProteinModelPortalQ89VT5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224911.blr0960.

Proteomic databases

PRIDEQ89VT5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC46225; BAC46225; BAC46225.
GeneID1048928.
KEGGbja:blr0960.
PATRIC21185422. VBIBraJap65052_0982.

Phylogenomic databases

HOGENOMHOG000228986.
KOK00772.
OrthoDBEOG6KHFXC.
PhylomeDBQ89VT5.

Enzyme and pathway databases

BioCycBJAP224911:GJEJ-969-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_BRADU
AccessionPrimary (citable) accession number: Q89VT5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 64 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