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

Q2RXH9 (MTAP_RHORT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 54. 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:Rru_A0361
OrganismRhodospirillum rubrum (strain ATCC 11170 / NCIB 8255) [Reference proteome] [HAMAP]
Taxonomic identifier269796 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeRhodospirillum

Protein attributes

Sequence length294 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 – 294294S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_01963
PRO_0000415099

Regions

Region58 – 592Phosphate binding By similarity
Region91 – 922Phosphate binding By similarity
Region213 – 2153Substrate binding By similarity

Sites

Binding site161Phosphate By similarity
Binding site1891Substrate; via amide nitrogen By similarity
Binding site1901Phosphate By similarity
Site1711Important for substrate specificity By similarity
Site2261Important for substrate specificity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2RXH9 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 58481196C7CCFB4B

FASTA29432,078
        10         20         30         40         50         60 
MSEAYRQPVL GVIGGSGVYD IDGLEGARWQ TVESPFGDVS DQILRGTLDG LEMAFLPRHG 

        70         80         90        100        110        120 
RGHVLAPSDV NYRANIDALK RAGVTEILSV SAVGSLAEDL PPGTFVIADQ FIDRTFAREK 

       130        140        150        160        170        180 
SFFGKGLVAH VSMAHPVSAW LGDRVEEVLA DLAIPHRRGG TYLCMEGPQF STLAESNLYR 

       190        200        210        220        230        240 
QWGCHVIGMT NMPEAKLARE AEIAYCTVAM VTDFDCWHPD HDHVSVEAVV RVLLQNADKA 

       250        260        270        280        290 
RSLVKAMPAK LKDRPYPLPD GSHRSLDNAI ITHPDRRNPG MARKLSAVAG RVLG 

« Hide

References

[1]"Complete sequence of the chromosome of Rhodospirillum rubrum ATCC 11170."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G., Reslewic S., Zhou S., Schwartz D.C.
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000230 Genomic DNA. Translation: ABC21166.1.
RefSeqYP_425453.1. NC_007643.1.

3D structure databases

ProteinModelPortalQ2RXH9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269796.Rru_A0361.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC21166; ABC21166; Rru_A0361.
GeneID3834648.
KEGGrru:Rru_A0361.
PATRIC23324297. VBIRhoRub82919_0417.

Phylogenomic databases

eggNOGCOG0005.
HOGENOMHOG000228986.
KOK00772.
OMAISTTACG.
OrthoDBEOG6KHFXC.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-17874.
RRUB269796:GCN1-373-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_RHORT
AccessionPrimary (citable) accession number: Q2RXH9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: January 24, 2006
Last modified: May 14, 2014
This is version 54 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