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Q9YAQ8 (MTAP_AERPE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:APE_1885
OrganismAeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1) [Complete proteome] [HAMAP]
Taxonomic identifier272557 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeAeropyrum

Protein attributes

Sequence length275 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 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 – 275275S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_01963
PRO_0000415102

Regions

Region62 – 632Phosphate binding By similarity
Region95 – 962Phosphate binding By similarity
Region219 – 2213Substrate binding By similarity

Sites

Binding site201Phosphate By similarity
Binding site1951Substrate; via amide nitrogen By similarity
Binding site1961Phosphate By similarity
Site1761Important for substrate specificity By similarity
Site2301Important for substrate specificity By similarity

Amino acid modifications

Disulfide bond143 ↔ 210 HAMAP-Rule MF_01963
Disulfide bond205 ↔ 266 HAMAP-Rule MF_01963
Disulfide bond264 ↔ 267 HAMAP-Rule MF_01963

Secondary structure

................................................. 275
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9YAQ8 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 86CC11C1FB2DB091

FASTA27530,737
        10         20         30         40         50         60 
MFEITRPPGV RAHVGVIGGS GLYDPGIVEN PVEVKVSTPY GNPSDFIVVG DVAGVKVAFL 

        70         80         90        100        110        120 
PRHGRGHRIP PHAINYRANI WALKALGVKW VISVSAVGSL REDYRPGDFV VPDQFIDMTK 

       130        140        150        160        170        180 
NRRHYTFYDG PVTVHVSMAD PFCEDLRQRL IDSGRRLGYT VHERGTYVCI EGPRFSTRAE 

       190        200        210        220        230        240 
SRVWKDVFKA DIIGMTLVPE INLACEAQLC YATLAMVTDY DVWADRPVTA EEVERVMISN 

       250        260        270 
VERARRMLYD VIPKLAGEPE LERCSCCRAL DTAAI 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1."
Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S. expand/collapse author list , Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.
DNA Res. 6:83-101(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1.
[2]"Crystal structure of 5'-deoxy-5'-methylthioadenosine from Aeropyrum pernix (R32 form)."
Tsunoda M., Murakami Y., Nakamura K.T.
Submitted (NOV-2004) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) IN COMPLEX WITH PHOSPHATE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000002 Genomic DNA. Translation: BAA80890.1.
PIRE72575.
RefSeqNP_148238.1. NC_000854.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WTAX-ray1.78A1-275[»]
ProteinModelPortalQ9YAQ8.
SMRQ9YAQ8. Positions 3-275.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272557.APE_1885.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA80890; BAA80890; APE_1885.
GeneID1446318.
KEGGape:APE_1885.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0005.
HOGENOMHOG000228987.
KOK00772.
OMACEAQLCY.

Enzyme and pathway databases

BioCycAPER272557:GJD6-1277-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

EvolutionaryTraceQ9YAQ8.

Entry information

Entry nameMTAP_AERPE
AccessionPrimary (citable) accession number: Q9YAQ8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: November 1, 1999
Last modified: May 14, 2014
This is version 78 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