EzCatDB: S00604
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DB codeS00604
RLCP classification9.1050.440000.8010 : Hydride transfer
9.5010.536200.8010 : Hydride transfer
CATH domainDomain 13.40.50.720 : Rossmann foldCatalytic domain
E.C.1.1.1.138

CATH domainRelated DB codes (homologues)
3.40.50.720 : Rossmann foldS00543,S00551,S00552,S00553,S00602,S00605,S00608,S00610,S00625,S00319,S00328,S00329,S00330,S00331,S00332,D00456,D00457,D00458,S00324,S00320,S00325,S00326,S00327,D00459,S00335,S00336,S00334,T00219,S00339,D00513,D00001,D00002,D00003,D00005,D00007,D00008,D00010,D00012,D00017,D00018,D00023,D00027,D00028,D00031,D00032,D00033,D00034,D00035,D00037,D00048,D00071,D00476,D00481,D00482,D00490,D00492,D00494,D00545,D00601,D00603,D00604,D00605,D00615,D00845,D00857,D00858,M00161,M00171,M00210,T00002,T00010,T00011,T00015,T00227,T00247,T00408,T00414,D00827,D00262,D00274,D00275,M00035,T00109

Enzyme Name
UniProtKBKEGG

O93868P0C0Y5
Protein nameNADP-dependent mannitol dehydrogenaseProbable NADP-dependent mannitol dehydrogenase (MtDH) (EC 1.1.1.138) (Mannitol 2-dehydrogenase [NADP+])AltName: Allergen=Cla h 8;Mannitol 2-dehydrogenase (NADP+)
Mannitol 2-dehydrogenase (NADP+)
SynonymsMtDH
EC 1.1.1.138
Mannitol 2-dehydrogenase [NADP+]
None
PfamPF00106 (adh_short)
[Graphical view]
PF00106 (adh_short)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00051Fructose and mannose metabolism

UniProtKB:Accession NumberO93868P0C0Y5
Entry nameMTDH_AGABIMTDH_DAVTA
ActivityD-mannitol + NADP(+) = D-fructose + NADPH.D-mannitol + NADP(+) = D-fructose + NADPH.
SubunitHomotetramer.
Subcellular location

Cofactor


Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00392C00006C00095C00005C00080
CompoundD-mannitolNADP+D-fructoseNADPHH+
Typecarbohydrateamide group,amine group,nucleotidecarbohydrateamide group,amine group,nucleotideothers
ChEBI16899
18009
37721
16474
15378
PubChem6251
5886
439163
5884
1038
             
1h5qA00UnboundBound:NAPUnboundUnbound 
1h5qB00UnboundBound:NAPUnboundUnbound 
1h5qC00UnboundBound:NAPUnboundUnbound 
1h5qD00UnboundBound:NAPUnboundUnbound 
1h5qE00UnboundBound:NAPUnboundUnbound 
1h5qF00UnboundBound:NAPUnboundUnbound 
1h5qG00UnboundBound:NAPUnboundUnbound 
1h5qH00UnboundBound:NAPUnboundUnbound 
1h5qI00UnboundBound:NAPUnboundUnbound 
1h5qJ00UnboundBound:NAPUnboundUnbound 
1h5qK00UnboundBound:NAPUnboundUnbound 
1h5qL00UnboundBound:NAPUnboundUnbound 
3gdfA00UnboundUnboundUnboundUnbound 
3gdfB00UnboundUnboundUnboundUnbound 
3gdfC00UnboundUnboundUnboundUnbound 
3gdfD00UnboundUnboundUnboundUnbound 
3gdgA00UnboundUnboundUnboundUnbound 
3gdgB00UnboundUnboundUnboundUnbound 
3gdgC00UnboundUnboundUnboundUnbound 
3gdgD00UnboundUnboundUnboundUnbound 

Active-site residues
resource
literature[2],[3]
pdbCatalytic residues
         
1h5qA00SER 149;TYR 169;LYS 173
1h5qB00SER 149;TYR 169;LYS 173
1h5qC00SER 149;TYR 169;LYS 173
1h5qD00SER 149;TYR 169;LYS 173
1h5qE00SER 149;TYR 169;LYS 173
1h5qF00SER 149;TYR 169;LYS 173
1h5qG00SER 149;TYR 169;LYS 173
1h5qH00SER 149;TYR 169;LYS 173
1h5qI00SER 149;TYR 169;LYS 173
1h5qJ00SER 149;TYR 169;LYS 173
1h5qK00SER 149;TYR 169;LYS 173
1h5qL00SER 149;TYR 169;LYS 173
3gdfA00SER 149;TYR 169;LYS 173
3gdfB00SER 160;TYR 175;Lys 179
3gdfC00SER 160;TYR 175;Lys 179
3gdfD00SER 160;TYR 175;Lys 179
3gdgA00SER 160;TYR 175;Lys 179
3gdgB00SER 160;TYR 175;Lys 179
3gdgC00SER 160;TYR 175;Lys 179
3gdgD00SER 160;TYR 175;Lys 179

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]Fig.4, p.27558
[3]Fig.6, p.990-992

references
[1]
PubMed ID11306087
JournalChem Biol Interact
Year2001
Volume130-132
Pages699-705
AuthorsOppermann UC, Filling C, Jornvall H
TitleForms and functions of human SDR enzymes.
[2]
PubMed ID11335726
JournalJ Biol Chem
Year2001
Volume276
Pages27555-61
AuthorsHorer S, Stoop J, Mooibroek H, Baumann U, Sassoon J
TitleThe crystallographic structure of the mannitol 2-dehydrogenase NADP+ binary complex from Agaricus bisporus.
Related PDB1h5q
[3]
PubMed ID20420880
JournalBiochimie
Year2010
Volume92
Pages985-93
AuthorsNuss D, Goettig P, Magler I, Denk U, Breitenbach M, Schneider PB, Brandstetter H, Simon-Nobbe B
TitleCrystal structure of the NADP-dependent mannitol dehydrogenase from Cladosporium herbarum: Implications for oligomerisation and catalysis.
Related PDB3gdf,3gdg

comments
This enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily.
Since the active site is the same as those of the homologous enzymes (S00320, S00327, S00328, S00330, S00332, S00602, S00605, S00608 and S00610 in EzCatDB), this enzyme must catalyzes the same reaction as those homologues.

createdupdated
2012-09-122012-09-28


Copyright: Nozomi Nagano, JST & CBRC-AIST
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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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