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O06401 (MTAP_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:Rv0535
OrganismMycobacterium tuberculosis (strain ATCC 25618 / H37Rv) [Reference proteome] [HAMAP]
Taxonomic identifier83332 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length264 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. Prefers MTA, with 2% activity on adenosine, 0.8% activity on S-adenosyl-L-homocysteine and no activity on other tested nucleosides. HAMAP-Rule MF_01963

Catalytic activity

S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate. Ref.3

Enzyme regulation

Not inhibited by adenosine, potently inhibited by MT-DADMe-immucillin A. Ref.3

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

Homodimer Probable. Ref.3

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=9 µM for S-methyl-5'-thioadenosine Ref.3

KM=260 µM for phosphate

KM=1700 µM for adenosine

pH dependence:

Optimum pH is 7-7.5.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 264264S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_01963
PRO_0000415096

Regions

Region55 – 562Phosphate binding By similarity
Region204 – 2063Substrate binding By similarity

Sites

Binding site141Phosphate By similarity
Binding site1801Substrate; via amide nitrogen By similarity
Binding site1811Phosphate By similarity
Site1621Important for substrate specificity By similarity
Site2171Important for substrate specificity By similarity

Sequences

Sequence LengthMass (Da)Tools
O06401 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 3A850EA1B1873662

FASTA26427,964
        10         20         30         40         50         60 
MHNNGRMLGV IGGSGFYTFF GSDTRTVNSD TPYGQPSAPI TIGTIGVHDV AFLPRHGAHH 

        70         80         90        100        110        120 
QYSAHAVPYR ANMWALRALG VRRVFGPCAV GSLDPELEPG AVVVPDQLVD RTSGRADTYF 

       130        140        150        160        170        180 
DFGGVHAAFA DPYCPTLRAA VTGLPGVVDG GTMVVIQGPR FSTRAESQWF AAAGCNLVNM 

       190        200        210        220        230        240 
TGYPEAVLAR ELELCYAAIA LVTDVDAGVA AGDGVKAADV FAAFGENIEL LKRLVRAAID 

       250        260 
RVADERTCTH CQHHAGVPLP FELP 

« Hide

References

« Hide 'large scale' references
[1]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry."
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M., Kumar P. expand/collapse author list , Chaerkady R., Ramachandran S., Dash D., Pandey A.
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ATCC 25618 / H37Rv.
[3]"Identification of Rv0535 as methylthioadenosine phosphorylase from Mycobacterium tuberculosis."
Buckoreelall K., Sun Y., Hobrath J.V., Wilson L., Parker W.B.
Tuberculosis 92:139-147(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT.
Strain: ATCC 25618 / H37Rv.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL123456 Genomic DNA. Translation: CCP43273.1.
PIRB70546.
RefSeqNP_215049.1. NC_000962.3.
YP_006513868.1. NC_018143.2.

3D structure databases

ProteinModelPortalO06401.
SMRO06401. Positions 2-248.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING83332.Rv0535.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCCP43273; CCP43273; Rv0535.
GeneID887430.
KEGGmtu:Rv0535.
mtv:RVBD_0535.
PATRIC18149684. VBIMycTub87468_0594.

Organism-specific databases

TubercuListRv0535.

Phylogenomic databases

HOGENOMHOG000228987.
KOK00772.
OMACEAQLCY.
OrthoDBEOG6KHFXC.
PhylomeDBO06401.

Enzyme and pathway databases

BioCycMTBRV:RV0535-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_MYCTU
AccessionPrimary (citable) accession number: O06401
Secondary accession number(s): L0T6S7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: July 1, 1997
Last modified: July 9, 2014
This is version 79 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

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names