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A1RXU2 (MTAP_THEPD) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 43. 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:Tpen_0618
OrganismThermofilum pendens (strain Hrk 5) [Reference proteome] [HAMAP]
Taxonomic identifier368408 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermofilaceaeThermofilum

Protein attributes

Sequence length262 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 – 262262S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_01963
PRO_0000415110

Regions

Region54 – 552Phosphate binding By similarity
Region87 – 882Phosphate binding By similarity
Region209 – 2113Substrate binding By similarity

Sites

Binding site121Phosphate By similarity
Binding site1851Substrate; via amide nitrogen By similarity
Binding site1861Phosphate By similarity
Site1671Important for substrate specificity By similarity
Site2201Important for substrate specificity By similarity

Sequences

Sequence LengthMass (Da)Tools
A1RXU2 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 0805BD30C4FB86E6

FASTA26229,467
        10         20         30         40         50         60 
MEKVKIGIIG GSGLYSPDFL TNPKEEKIYT PYGPPSSHVV IGEIAGRKVA FIPRHGKRHE 

        70         80         90        100        110        120 
IPPHKVNYRA NIYALKELGV ERLISVSAVG SLREDYKPGD FVCTDQFIDM TKGRVYTFYD 

       130        140        150        160        170        180 
GPVVAHVSMA DPFCPELREL CIRSARKLGI TMHEKGTYIC IEGPRFSTRA ESRLWRQFGA 

       190        200        210        220        230        240 
DIIGMTLVPE VNLAREARMC FLNIAMVTDY DVWAEKPVTA HEVARVMAEN TEKVKRLLAD 

       250        260 
LIPSIPEERK CQCARALDEA LI 

« Hide

References

[1]"Genome sequence of Thermofilum pendens reveals an exceptional loss of biosynthetic pathways without genome reduction."
Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E., Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M., Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B. expand/collapse author list , Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.
J. Bacteriol. 190:2957-2965(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hrk 5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000505 Genomic DNA. Translation: ABL78022.1.
RefSeqYP_920025.1. NC_008698.1.

3D structure databases

ProteinModelPortalA1RXU2.
SMRA1RXU2. Positions 2-262.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING368408.Tpen_0618.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL78022; ABL78022; Tpen_0618.
GeneID4601324.
KEGGtpe:Tpen_0618.

Phylogenomic databases

eggNOGCOG0005.
HOGENOMHOG000228987.
KOK00772.
OMAMTNHTEA.
ProtClustDBPRK08564.

Enzyme and pathway databases

BioCycTPEN368408:GHSG-657-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_THEPD
AccessionPrimary (citable) accession number: A1RXU2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: February 6, 2007
Last modified: April 16, 2014
This is version 43 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