Q2RXI0 · MTNA_RHORT
- ProteinMethylthioribose-1-phosphate isomerase
- GenemtnA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids390 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P) (PubMed:23042035, PubMed:31950558).
Also catalyzes the interconversion of 5-deoxyribose 1-phosphate and 5-deoxyribulose 1-phosphate (PubMed:23042035, PubMed:31950558).
Part of a bifunctional DHAP-shunt salvage pathway for SAM by-products (PubMed:31950558).
Also catalyzes the interconversion of 5-deoxyribose 1-phosphate and 5-deoxyribulose 1-phosphate (PubMed:23042035, PubMed:31950558).
Part of a bifunctional DHAP-shunt salvage pathway for SAM by-products (PubMed:31950558).
Catalytic activity
- S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphateThis reaction proceeds in the forward direction.
- 5-deoxy-alpha-D-ribose 1-phosphate = 5-deoxy-D-ribulose 1-phosphateThis reaction proceeds in the forward direction.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
134 μM | methylthioribose-1-phosphate | |||||
171 μM | deoxyribose-1-phosphate |
kcat is 0.1 sec-1 with methylthioribose-1-phosphate as substrate. kcat is 0.18 sec-1 with deoxyribose-1-phosphate as substrate (PubMed:23042035).
kcat is 0.03 sec-1 with ribose-1-phosphate as substrate (PubMed:31950558).
kcat is 0.03 sec-1 with ribose-1-phosphate as substrate (PubMed:31950558).
Pathway
Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 1/6.
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 53-55 | substrate | ||||
Sequence: RGA | ||||||
Binding site | 90 | substrate | ||||
Sequence: R | ||||||
Site | 168 | Transition state stabilizer | ||||
Sequence: C | ||||||
Binding site | 207 | substrate | ||||
Sequence: Q | ||||||
Active site | 248 | Proton donor | ||||
Sequence: D | ||||||
Binding site | 258-259 | substrate | ||||
Sequence: NK |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | S-methyl-5-thioribose-1-phosphate isomerase activity | |
Biological Process | L-methionine salvage from methylthioadenosine | |
Biological Process | L-methionine salvage from S-adenosylmethionine |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMethylthioribose-1-phosphate isomerase
- EC number
- Short namesM1Pi ; MTR-1-P isomerase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rhodospirillales > Rhodospirillaceae > Rhodospirillum
Accessions
- Primary accessionQ2RXI0
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000445437 | 1-390 | Methylthioribose-1-phosphate isomerase | |||
Sequence: MNVKGTPTRTIWPAREGGAVWIIDQTRLPHEFVTQRLNDLGAVAHAIRAMLVRGAPLIGATAAYGVALGMAEDPSDEGLTRACQTLLATRPTAVNLRWAIEAMAESLAAVPPDQRAQAAWAKAGAICDEDVALNEAIGDHGLGIIKDLARTKGVEKGGEGPINILTHCNAGWLATVDWGTALAPLYKAHDAGLPIHVWVDETRPRNQGASLTAWELNSHGVPHTVIADNTGGHLMQHGLVDMVIVGTDRTTATGDVCNKIGTYLKALAAFDNAVPFYVALPGPTIDWTVNDGLREIPIEQRDAAEVTRVWGRTAAGALEWVTITPTGSPAANYAFDVTPARLITGLITERGVCAASAAGLAGLYPERAPAPVPAGSAAGKGAAATADGAL |
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length390
- Mass (Da)40,656
- Last updated2006-01-24 v1
- ChecksumFAC7D0B6F8B90750
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000230 EMBL· GenBank· DDBJ | ABC21165.1 EMBL· GenBank· DDBJ | Genomic DNA |