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Q8U4Q8 (MTAP_PYRFU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 65. 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
Short name=PfMTAP
Gene names
Name:mtnP
Ordered Locus Names:PF0016
OrganismPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) [Reference proteome] [HAMAP]
Taxonomic identifier186497 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length257 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. Ref.2 Ref.3 Ref.4

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. Ref.2

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=147 µM for S-methyl-5'-thioadenosine Ref.2

KM=109 µM for adenosine

KM=963 µM for inosine

KM=916 µM for guanosine

pH dependence:

Optimum pH is 7.4. Active from pH 5 to 10.

Temperature dependence:

Optimum temperature is 125 degrees Celsius. Thermostable up to 137 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 257257S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_01963
PRO_0000415107

Regions

Region50 – 512Phosphate binding By similarity
Region204 – 2063Substrate binding By similarity

Sites

Binding site101Phosphate By similarity
Binding site1801Substrate; via amide nitrogen By similarity
Binding site1811Phosphate By similarity
Site1631Important for substrate specificity By similarity
Site2151Important for substrate specificity By similarity

Amino acid modifications

Disulfide bond130 ↔ 195 Ref.3
Disulfide bond246 ↔ 248 Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q8U4Q8 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: A1B8194889A30AB8

FASTA25729,220
        10         20         30         40         50         60 
MPKIGIIGGS GVYGIFEPKE TVKVHTPYGR PSAPVEIGEI EGVEVAFIPR HGKYHEFPPH 

        70         80         90        100        110        120 
EVPYRANIWA LHELGVERVI AVNAVGSLKE EYKPGDIVII DQFIDFTKKR EYTFYNGPRV 

       130        140        150        160        170        180 
AHISMADPFC PELRRIFIET AKELNLPVHE KGTYICIEGP RFSTRAESRM FRQFADVIGM 

       190        200        210        220        230        240 
TLVPEVNLAR ELGMCYVNIS TVTDYDVWAE KPVDAQEVLR VMKENEEKVQ KLLKRAIPKI 

       250 
PEERKCGCAD VLKTMFV 

« Hide

References

« Hide 'large scale' references
[1]"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[2]"Purification and characterization of 5'-methylthioadenosine phosphorylase from the hyperthermophilic archaeon Pyrococcus furiosus: substrate specificity and primary structure analysis."
Cacciapuoti G., Bertoldo C., Brio A., Zappia V., Porcelli M.
Extremophiles 7:159-168(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-27, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
[3]"Methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus. Mechanism of the reaction and assignment of disulfide bonds."
Cacciapuoti G., Moretti M.A., Forte S., Brio A., Camardella L., Zappia V., Porcelli M.
Eur. J. Biochem. 271:4834-4844(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISULFIDE BONDS.
[4]"Unraveling the structural and functional differences between purine nucleoside phosphorylase and 5'-deoxy-5'-methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus."
Cacciapuoti G., Marabotti A., Fuccio F., Porcelli M.
Biochim. Biophys. Acta 1814:1358-1366(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009950 Genomic DNA. Translation: AAL80140.1.
RefSeqNP_577745.1. NC_003413.1.

3D structure databases

ProteinModelPortalQ8U4Q8.
SMRQ8U4Q8. Positions 4-243.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING186497.PF0016.

Proteomic databases

PRIDEQ8U4Q8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL80140; AAL80140; PF0016.
GeneID1467844.
KEGGpfu:PF0016.

Phylogenomic databases

eggNOGCOG0005.
HOGENOMHOG000228987.
KOK00772.
OMAGCADVLK.
ProtClustDBPRK08564.

Enzyme and pathway databases

SABIO-RKQ8U4Q8.
UniPathwayUPA00904; UER00873.

Family and domain databases

Gene3D3.40.50.1580. 1 hit.
HAMAPMF_01963. MTAP.
InterProIPR010044. MTAP.
IPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view]
PANTHERPTHR11904. PTHR11904. 1 hit.
PfamPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
SUPFAMSSF53167. SSF53167. 1 hit.
TIGRFAMsTIGR01694. MTAP. 1 hit.
PROSITEPS01240. PNP_MTAP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMTAP_PYRFU
AccessionPrimary (citable) accession number: Q8U4Q8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: June 1, 2002
Last modified: April 16, 2014
This is version 65 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