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Q3J5E8 (MTAP_RHOS4) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 52. 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:RHOS4_04180
ORF Names:RSP_1837
OrganismRhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158) [Reference proteome] [HAMAP]
Taxonomic identifier272943 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Protein attributes

Sequence length290 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 – 290290S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_01963
PRO_0000415098

Regions

Region53 – 542Phosphate binding By similarity
Region86 – 872Phosphate binding By similarity
Region208 – 2103Substrate binding By similarity

Sites

Binding site111Phosphate By similarity
Binding site1841Substrate; via amide nitrogen By similarity
Binding site1851Phosphate By similarity
Site1661Important for substrate specificity By similarity
Site2211Important for substrate specificity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3J5E8 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 35B46FAB615584CF

FASTA29030,950
        10         20         30         40         50         60 
MKTMIGVIGG SGVYEIDGLE DAVWTKVETP WGDPSDEILT GRLDGVPMAF LPRHGRGHVH 

        70         80         90        100        110        120 
SPTTVPYRAN IDALKRLGVT DLVSVSACGS FREEMAPGDF VIVDQFIDRS FARAKSFFGS 

       130        140        150        160        170        180 
GCVAHVSLAH PTCGRLSALC AEAARATGVT VHEGGTYLCM EGPQFSTLAE SLLYKSWGCH 

       190        200        210        220        230        240 
VIGMTNMPEA KLAREAEICY ASVAMVTDYD SWHPHHGEVD ITAIIATLGT NADHARGLVA 

       250        260        270        280        290 
GLPARLGTER DLCPHGCDRA LDHALMTAPA KRDPELLAKL DAVAGRVLKG 

« Hide

References

[1]"Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C., Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000143 Genomic DNA. Translation: ABA77986.1.
RefSeqYP_351887.1. NC_007493.2.

3D structure databases

ProteinModelPortalQ3J5E8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272943.RSP_1837.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA77986; ABA77986; RSP_1837.
GeneID3719104.
KEGGrsp:RSP_1837.
PATRIC23150648. VBIRhoSph57909_0724.

Phylogenomic databases

eggNOGCOG0005.
HOGENOMHOG000228986.
KOK00772.
OMAISTTACG.
OrthoDBEOG6KHFXC.
PhylomeDBQ3J5E8.

Enzyme and pathway databases

BioCycRSPH272943:GJAS-431-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_RHOS4
AccessionPrimary (citable) accession number: Q3J5E8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: November 8, 2005
Last modified: July 9, 2014
This is version 52 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