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Q9HL98 (MTAP_THEAC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 60. 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
Ordered Locus Names:Ta0332
OrganismThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) [Reference proteome] [HAMAP]
Taxonomic identifier273075 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma

Protein attributes

Sequence length261 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 – 261261S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_01963
PRO_0000415111

Regions

Region54 – 552Phosphate binding By similarity
Region208 – 2103Substrate binding By similarity

Sites

Binding site141Phosphate By similarity
Binding site1841Substrate; via amide nitrogen By similarity
Binding site1851Phosphate By similarity
Site1671Important for substrate specificity By similarity
Site2191Important for substrate specificity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9HL98 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 693551EEA388EE42

FASTA26129,364
        10         20         30         40         50         60 
MTVNMAYIGI IGGSGLYDLM PESTKKVIET PFGNPSDAVE IGEVNGVEVA FLPRHGKKHT 

        70         80         90        100        110        120 
IPPHKVNYRA NIWALHELGV ERIIGLNAVG SLREDYKPGE IVIPDQYIDF TKRRDLTFYD 

       130        140        150        160        170        180 
GPQVYHISEA DPFCPEMNSI LYDTARNLKI PVHNSGTYIT IEGPRFSTRA ESKMFRQFAD 

       190        200        210        220        230        240 
IIGMTLVPEV SLAGELALCY SVIASITDYD VWSTKPVDAR EVMNIMKQND HKVRDILFNA 

       250        260 
LPLIKKERKC SCSLRLDNAK M 

« Hide

References

[1]"The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum."
Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.
Nature 407:508-513(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL445064 Genomic DNA. Translation: CAC11476.1.
RefSeqNP_393811.1. NC_002578.1.

3D structure databases

ProteinModelPortalQ9HL98.
SMRQ9HL98. Positions 6-259.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273075.Ta0332.

Proteomic databases

PRIDEQ9HL98.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC11476; CAC11476; CAC11476.
GeneID1455951.
KEGGtac:Ta0332.

Phylogenomic databases

eggNOGCOG0005.
HOGENOMHOG000228987.
KOK00772.
OMACEAQLCY.

Enzyme and pathway databases

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_THEAC
AccessionPrimary (citable) accession number: Q9HL98
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: March 1, 2001
Last modified: May 14, 2014
This is version 60 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