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Q97W94 (MTAP_SULSO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 68. 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
Short name=MTAPII
Gene names
Name:mtnP
Ordered Locus Names:SSO2343
OrganismSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) [Reference proteome] [HAMAP]
Taxonomic identifier273057 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length270 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

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=0.7 mM for S-methyl-5'-thioadenosine Ref.2

KM=270 µM for adenosine

Temperature dependence:

Optimum temperature is 120 degrees Celsius. Highly thermostable.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 270270S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_01963
PRO_0000415109

Regions

Region58 – 592Phosphate binding By similarity
Region91 – 922Phosphate binding By similarity
Region214 – 2163Substrate binding By similarity

Sites

Binding site161Phosphate By similarity
Binding site1901Substrate; via amide nitrogen By similarity
Binding site1911Phosphate By similarity
Site1711Important for substrate specificity By similarity
Site2251Important for substrate specificity By similarity

Amino acid modifications

Disulfide bond138 ↔ 205 Ref.3
Disulfide bond200 ↔ 262 Ref.3
Disulfide bond259 ↔ 261 Ref.3

Experimental info

Mutagenesis2591C → S: Reduces thermostability of the enzyme; when associated with S-261. Ref.2
Mutagenesis2611C → S: Reduces thermostability of the enzyme; when associated with S-259. Ref.2
Mutagenesis2621C → S: Reduces thermostability of the enzyme. Ref.2

Secondary structure

.............................................. 270
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q97W94 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 682A166698935A88

FASTA27030,141
        10         20         30         40         50         60 
MIEQNEKASI GIIGGSGLYD PGIFSESKEI KVYTPYGQPS DFITIGKIGN KSVAFLPRHG 

        70         80         90        100        110        120 
RGHRIPPHKI NYRANIWALK ELGVRWVISV SAVGSLRMDY KLGDFVIPDQ FIDMTKNREY 

       130        140        150        160        170        180 
SFFDGPVVAH VSMADPFCNS LRKLAIETAK ELNIKTHESG TYICIEGPRF STRAESRTWR 

       190        200        210        220        230        240 
EVYKADIIGM TLVPEVNLAC EAQMCYATIA MVTDYDVFAE IPVTAEEVTR VMAENTEKAK 

       250        260        270 
KLLYALIQKL PEKPEEGSCS CCNSLKTALV 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome of the crenarchaeon Sulfolobus solfataricus P2."
She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G., Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X. expand/collapse author list , Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T., Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.
Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
[2]"A novel hyperthermostable 5'-deoxy-5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus."
Cacciapuoti G., Forte S., Moretti M.A., Brio A., Zappia V., Porcelli M.
FEBS J. 272:1886-1899(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-259; CYS-261 AND CYS-262, SUBUNIT.
[3]"The crystal structure of 5'-deoxy-5'-methylthioadenosine phosphorylase II from Sulfolobus solfataricus, a thermophilic enzyme stabilized by intramolecular disulfide bonds."
Zhang Y., Porcelli M., Cacciapuoti G., Ealick S.E.
J. Mol. Biol. 357:252-262(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH SUBSTRATES, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006641 Genomic DNA. Translation: AAK42494.1.
PIRG90404.
RefSeqNP_343704.1. NC_002754.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2A8YX-ray1.45A/B/C/D/E/F/G/H/I/J/K/L1-270[»]
3T94X-ray1.45A/B/C/D/E/F1-270[»]
ProteinModelPortalQ97W94.
SMRQ97W94. Positions 1-270.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273057.SSO2343.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK42494; AAK42494; SSO2343.
GeneID1453821.
KEGGsso:SSO2343.

Phylogenomic databases

eggNOGCOG0005.
HOGENOMHOG000228986.
KOK00772.
OMACEAQLCY.

Enzyme and pathway databases

BioCycSSOL273057:GCH2-2180-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.
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...

Other

EvolutionaryTraceQ97W94.

Entry information

Entry nameMTAP_SULSO
AccessionPrimary (citable) accession number: Q97W94
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: October 1, 2001
Last modified: May 14, 2014
This is version 68 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways