Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A2BIU4 (MTAP_HYPBU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 42. 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:Hbut_0022
OrganismHyperthermus butylicus (strain DSM 5456 / JCM 9403) [Reference proteome] [HAMAP]
Taxonomic identifier415426 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesPyrodictiaceaeHyperthermus

Protein attributes

Sequence length274 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 – 274274S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_01963
PRO_0000415104

Regions

Region62 – 632Phosphate binding By similarity
Region95 – 962Phosphate binding By similarity
Region218 – 2203Substrate binding By similarity

Sites

Binding site201Phosphate By similarity
Binding site1941Substrate; via amide nitrogen By similarity
Binding site1951Phosphate By similarity
Site1751Important for substrate specificity By similarity
Site2291Important for substrate specificity By similarity

Sequences

Sequence LengthMass (Da)Tools
A2BIU4 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: 305ED09C45DDCE01

FASTA27430,784
        10         20         30         40         50         60 
MPDFPPKPSV KADIAIIGGS GLYDPGVLEN AKEYKIYTPY GEPSDYIIVG ELGGKRVAFL 

        70         80         90        100        110        120 
PRHGRGHRIP PHKINYRANI WALKMLGVKW VIAVSAVGSL REDYKPGDIV VPDQFIDMTK 

       130        140        150        160        170        180 
SRVYTFFDEG IVAHVSMADP FCEHLRQEII STARELGYRV HPRGTYICIE GPRFSTRAES 

       190        200        210        220        230        240 
RVWREVFKAD IIGMTLVPEV NLACEAQLCY ATIALVTDYD VWAERPVTAE EVARVMKENT 

       250        260        270 
EKAKKILYKL IPRLPPEPDK ARCSCCSSLE TALL 

« Hide

References

[1]"The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C."
Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M., She Q., Garrett R.A., Klenk H.-P.
Archaea 2:127-135(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 5456 / JCM 9403.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000493 Genomic DNA. Translation: ABM79900.1.
RefSeqYP_001012245.1. NC_008818.1.

3D structure databases

ProteinModelPortalA2BIU4.
SMRA2BIU4. Positions 7-274.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING415426.Hbut_0022.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM79900; ABM79900; Hbut_0022.
GeneID4782054.
KEGGhbu:Hbut_0022.

Phylogenomic databases

eggNOGCOG0005.
HOGENOMHOG000228987.
KOK00772.
OMAMTNHTEA.
ProtClustDBPRK08564.

Enzyme and pathway databases

BioCycHBUT415426:GC56-22-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_HYPBU
AccessionPrimary (citable) accession number: A2BIU4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: February 20, 2007
Last modified: April 16, 2014
This is version 42 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