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Q5JEQ6 (MTAP_THEKO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 59. 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:TK1895
OrganismThermococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) [Reference proteome] [HAMAP]
Taxonomic identifier69014 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus

Protein attributes

Sequence length257 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 – 257257S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_01963
PRO_0000415108

Regions

Region50 – 512Phosphate binding By similarity
Region83 – 842Phosphate 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

Sequences

Sequence LengthMass (Da)Tools
Q5JEQ6 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: F2655D33A7EADFF5

FASTA25729,076
        10         20         30         40         50         60 
MPRIGIIGGS GVYGVFEPKE TVKVHTPYGR PSAPVEIGEI EGVEVAFIPR HGKHHEFPPH 

        70         80         90        100        110        120 
EVPYRANIWA LKELGVERVI GITAVGSLRE EYKPGDIVIT DQFIDFTKKR DYTFYNGPRV 

       130        140        150        160        170        180 
AHVSMADPFC PEMRKIFYET AKELGFPVHE KGTYVCIEGP RFSTRAESFM FRQFAHIIGM 

       190        200        210        220        230        240 
TLVPEVNLAR ELGMCYVNIA TVTDYDVWAD KPVDAQEVLK VMAENNYKVQ ELLKKGIPKI 

       250 
PEERHCGCAD VLKTMFV 

« Hide

References

[1]"Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes."
Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.
Genome Res. 15:352-363(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-918 / JCM 12380 / KOD1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006878 Genomic DNA. Translation: BAD86084.1.
RefSeqYP_184308.1. NC_006624.1.

3D structure databases

ProteinModelPortalQ5JEQ6.
SMRQ5JEQ6. Positions 4-257.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ5JEQ6. 1 interaction.
MINTMINT-8377197.
STRING69014.TK1895.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD86084; BAD86084; TK1895.
GeneID3235538.
KEGGtko:TK1895.

Phylogenomic databases

eggNOGCOG0005.
HOGENOMHOG000228987.
KOK00772.
OMADYTFYNG.

Enzyme and pathway databases

BioCycTKOD69014:GH72-1932-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...

Entry information

Entry nameMTAP_THEKO
AccessionPrimary (citable) accession number: Q5JEQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: February 15, 2005
Last modified: May 14, 2014
This is version 59 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