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A0QR54 (MTAP_MYCS2) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 56. 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
Synonyms:pnp
Ordered Locus Names:MSMEG_0990, MSMEI_0963
OrganismMycobacterium smegmatis (strain ATCC 700084 / mc(2)155) [Reference proteome] [HAMAP]
Taxonomic identifier246196 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length259 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. 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.

Biophysicochemical properties

Kinetic parameters:

KM=1.6 µM for S-methyl-5'-thioadenosine Ref.4

KM=310 µM for adenosine

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 259259S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_01963
PRO_0000415095

Regions

Region50 – 512Phosphate binding By similarity
Region199 – 2013Substrate binding By similarity

Sites

Binding site91Phosphate By similarity
Binding site1751Substrate; via amide nitrogen By similarity
Binding site1761Phosphate By similarity
Site1571Important for substrate specificity By similarity
Site2121Important for substrate specificity By similarity

Sequences

Sequence LengthMass (Da)Tools
A0QR54 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 8D379609536F84FF

FASTA25927,723
        10         20         30         40         50         60 
MMLGVIGGSG FYTFFGSDAR AVSVETPYGP PSAPITVGTV GDHEVAFLPR HGVKHEFSPH 

        70         80         90        100        110        120 
TVPYRANLWA LRSLGVRRVF APCAVGSLTP DLGPGSIVVP DQLVDRTSGR DDTYFDSGGI 

       130        140        150        160        170        180 
HVAFADPYCP TLRAAATGLP GVVDGGTMVV IQGPRFSTRA ESRWFASQGF TLVNMTGYPE 

       190        200        210        220        230        240 
AVLARELEMC YAAVALVTDL DAGIEVGSGV RAVDVFAEFE RNMPPFKKLV FEALEAVEVE 

       250 
RTCTHCLTHS GVQLPFELP 

« Hide

References

« Hide 'large scale' references
[1]Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[2]"Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[3]"Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[4]"Identification and characterization of two adenosine phosphorylase activities in Mycobacterium smegmatis."
Buckoreelall K., Wilson L., Parker W.B.
J. Bacteriol. 193:5668-5674(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
Strain: ATCC 700084 / mc(2)155.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000480 Genomic DNA. Translation: ABK70512.1.
CP001663 Genomic DNA. Translation: AFP37443.1.
RefSeqYP_006565738.1. NC_018289.1.
YP_885392.1. NC_008596.1.

3D structure databases

ProteinModelPortalA0QR54.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING246196.MSMEG_0990.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK70512; ABK70512; MSMEG_0990.
AFP37443; AFP37443; MSMEI_0963.
GeneID4532080.
KEGGmsg:MSMEI_0963.
msm:MSMEG_0990.
PATRIC18074434. VBIMycSme59918_0978.

Phylogenomic databases

eggNOGCOG0005.
HOGENOMHOG000228987.
KOK00772.
OMAHEFSAHT.
OrthoDBEOG6KHFXC.

Enzyme and pathway databases

BioCycMSME246196:GJ4Y-990-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_MYCS2
AccessionPrimary (citable) accession number: A0QR54
Secondary accession number(s): I7FF12
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: January 9, 2007
Last modified: July 9, 2014
This is version 56 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