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Q8ZTB2 (MTAP_PYRAE) 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:PAE3338
OrganismPyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827) [Reference proteome] [HAMAP]
Taxonomic identifier178306 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum

Protein attributes

Sequence length279 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 – 279279S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_01963
PRO_0000415106

Regions

Region70 – 712Phosphate binding By similarity
Region103 – 1042Phosphate binding By similarity
Region226 – 2283Substrate binding By similarity

Sites

Binding site281Phosphate By similarity
Binding site2021Substrate; via amide nitrogen By similarity
Binding site2031Phosphate By similarity
Site1831Important for substrate specificity By similarity
Site2381Important for substrate specificity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8ZTB2 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 86D368E1B1CDB7C0

FASTA27931,014
        10         20         30         40         50         60 
MVKLTNPPKS PKELGFDEFP SIGIIGGSGL YDPGIFENAV EVQIHTPYGL PSDNVIVGRV 

        70         80         90        100        110        120 
AGRVVAFLPR HGRGHKYPPH KIPYRANIYS LYMLGVRSIV AVSAVGSLRP DYAPGDFVVP 

       130        140        150        160        170        180 
DQFVDMTKGR EYTFYDGPRT CHIQIGLEPF TQEIRQILIE TAKKYNRTHD GGCYVCIEGP 

       190        200        210        220        230        240 
RFSTKAESRI WREVFGCDII GMTLVPEINL ARELGMCYGL IALVTDYDIW VPHQPVTAEA 

       250        260        270 
VEKMMTEKLG IIKKVIAEAV PKLPAELPKC SETLKYACV 

« Hide

References

[1]"Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum."
Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I., Miller J.H.
Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009441 Genomic DNA. Translation: AAL64851.1.
RefSeqNP_560669.1. NC_003364.1.

3D structure databases

ProteinModelPortalQ8ZTB2.
SMRQ8ZTB2. Positions 22-271.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING178306.PAE3338.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL64851; AAL64851; PAE3338.
GeneID1464041.
KEGGpai:PAE3338.

Phylogenomic databases

eggNOGCOG0005.
HOGENOMHOG000228987.
KOK00772.
OMADYTFYNG.

Enzyme and pathway databases

BioCycPAER178306:GCEO-2448-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_PYRAE
AccessionPrimary (citable) accession number: Q8ZTB2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: March 1, 2002
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