P0C0Y5 · NMTDH_DAVTA
- ProteinNADP-dependent mannitol dehydrogenase
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids267 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Interconverts D-mannitol and D-fructose. Not active with fructose 6-phosphate or NADH.
Catalytic activity
- D-mannitol + NADP+ = D-fructose + H+ + NADPHThis reaction proceeds in the forward and the backward directions.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
1.17 μM | D-fructose | 7.5 | ||||
0.23 μM | D-mannitol | 7.5 | ||||
53 μM | NADPH | 7.5 | ||||
67 μM | NADP+ | 7.5 |
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 108 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 141 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 160 | Proton donor | ||||
Sequence: S | ||||||
Active site | 175 | Proton acceptor | ||||
Sequence: Y | ||||||
Binding site | 175 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Active site | 179 | Lowers pKa of active site Tyr | ||||
Sequence: K | ||||||
Binding site | 179 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 207 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 209 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | mannitol 2-dehydrogenase (NADP+) activity | |
Molecular Function | NADP binding | |
Molecular Function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor | |
Molecular Function | protein homodimerization activity | |
Biological Process | mannitol metabolic process | |
Biological Process | protein homotetramerization |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameNADP-dependent mannitol dehydrogenase
- EC number
- Short namesMtDH
- Alternative names
- Allergen nameCla h 8
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Dothideomycetes > Dothideomycetidae > Cladosporiales > Cladosporiaceae > Cladosporium
Accessions
- Primary accessionP0C0Y5
- Secondary accessions
Phenotypes & Variants
Allergenic properties
Causes an allergic reaction in human. Binds to IgE in 57% of 21 C.herbarum-allergic patients tested.
Keywords
- Disease
Protein family/group databases
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000054728 | 2-267 | NADP-dependent mannitol dehydrogenase | |||
Sequence: PGQQATKHESLLDQLSLKGKVVVVTGASGPKGMGIEAARGCAEMGAAVAITYASRAQGAEENVKELEKTYGIKAKAYKCQVDSYESCEKLVKDVVADFGQIDAFIANAGATADSGILDGSVEAWNHVVQVDLNGTFHCAKAVGHHFKERGTGSLVITASMSGHIANFPQEQTSYNVAKAGCIHMARSLANEWRDFARVNSISPGYIDTGLSDFVPKETQQLWHSMIPMGRDGLAKELKGAYVYFASDASTYTTGADLLIDGGYTTR |
Interaction
Subunit
Exists as monomer, dimer and tetramer.
Structure
Sequence
- Sequence statusComplete
- Length267
- Mass (Da)28,464
- Last updated2006-01-24 v1
- Checksum4CF5EA012D71D446
Keywords
- Technical term