DB code: S00604

RLCP classification 9.1050.440000.8010 : Hydride transfer
9.5010.536200.8010 : Hydride transfer
CATH domain 3.40.50.720 : Rossmann fold Catalytic domain
E.C. 1.1.1.138
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.40.50.720 : Rossmann fold S00543 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

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
O93868 NADP-dependent mannitol dehydrogenase
MtDH
EC 1.1.1.138
Mannitol 2-dehydrogenase [NADP+]
PF00106 (adh_short)
[Graphical View]
P0C0Y5 Probable NADP-dependent mannitol dehydrogenase (MtDH) (EC 1.1.1.138) (Mannitol 2-dehydrogenase [NADP+])AltName: Allergen=Cla h 8;
None PF00106 (adh_short)
[Graphical View]

KEGG enzyme name
Mannitol 2-dehydrogenase (NADP+)
Mannitol 2-dehydrogenase (NADP+)

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
O93868 MTDH_AGABI D-mannitol + NADP(+) = D-fructose + NADPH. Homotetramer.
P0C0Y5 MTDH_DAVTA D-mannitol + NADP(+) = D-fructose + NADPH.

KEGG Pathways
Map code Pathways E.C.
MAP00051 Fructose and mannose metabolism

Compound table
Substrates Products Intermediates
KEGG-id C00392 C00006 C00095 C00005 C00080
E.C.
Compound D-mannitol NADP+ D-fructose NADPH H+
Type carbohydrate amide group,amine group,nucleotide carbohydrate amide group,amine group,nucleotide others
ChEBI 16899
 16899
 		18009
 18009
 		37721
 37721
 		16474
 16474
 		15378
 15378
PubChem 6251
 6251
 		5886
 5886
 		439163
 439163
 		5884
 5884
 		1038
 1038
1h5qA00 Unbound Bound:NAP Unbound Unbound
1h5qB00 Unbound Bound:NAP Unbound Unbound
1h5qC00 Unbound Bound:NAP Unbound Unbound
1h5qD00 Unbound Bound:NAP Unbound Unbound
1h5qE00 Unbound Bound:NAP Unbound Unbound
1h5qF00 Unbound Bound:NAP Unbound Unbound
1h5qG00 Unbound Bound:NAP Unbound Unbound
1h5qH00 Unbound Bound:NAP Unbound Unbound
1h5qI00 Unbound Bound:NAP Unbound Unbound
1h5qJ00 Unbound Bound:NAP Unbound Unbound
1h5qK00 Unbound Bound:NAP Unbound Unbound
1h5qL00 Unbound Bound:NAP Unbound Unbound
3gdfA00 Unbound Unbound Unbound Unbound
3gdfB00 Unbound Unbound Unbound Unbound
3gdfC00 Unbound Unbound Unbound Unbound
3gdfD00 Unbound Unbound Unbound Unbound
3gdgA00 Unbound Unbound Unbound Unbound
3gdgB00 Unbound Unbound Unbound Unbound
3gdgC00 Unbound Unbound Unbound Unbound
3gdgD00 Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature[2],[3]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1h5qA00 SER 149;TYR 169;LYS 173
1h5qB00 SER 149;TYR 169;LYS 173
1h5qC00 SER 149;TYR 169;LYS 173
1h5qD00 SER 149;TYR 169;LYS 173
1h5qE00 SER 149;TYR 169;LYS 173
1h5qF00 SER 149;TYR 169;LYS 173
1h5qG00 SER 149;TYR 169;LYS 173
1h5qH00 SER 149;TYR 169;LYS 173
1h5qI00 SER 149;TYR 169;LYS 173
1h5qJ00 SER 149;TYR 169;LYS 173
1h5qK00 SER 149;TYR 169;LYS 173
1h5qL00 SER 149;TYR 169;LYS 173
3gdfA00 SER 149;TYR 169;LYS 173
3gdfB00 SER 160;TYR 175;Lys 179
3gdfC00 SER 160;TYR 175;Lys 179
3gdfD00 SER 160;TYR 175;Lys 179
3gdgA00 SER 160;TYR 175;Lys 179
3gdgB00 SER 160;TYR 175;Lys 179
3gdgC00 SER 160;TYR 175;Lys 179
3gdgD00 SER 160;TYR 175;Lys 179

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
Fig.4, p.27558
[3]
Fig.6, p.990-992

References
[1]
Resource
Comments
Medline ID
PubMed ID 11306087
Journal Chem Biol Interact
Year 2001
Volume 130-132
Pages 699-705
Authors Oppermann UC, Filling C, Jornvall H
Title Forms and functions of human SDR enzymes.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 11335726
Journal J Biol Chem
Year 2001
Volume 276
Pages 27555-61
Authors Horer S, Stoop J, Mooibroek H, Baumann U, Sassoon J
Title The crystallographic structure of the mannitol 2-dehydrogenase NADP+ binary complex from Agaricus bisporus.
Related PDB 1h5q
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 20420880
Journal Biochimie
Year 2010
Volume 92
Pages 985-93
Authors Nuss D, Goettig P, Magler I, Denk U, Breitenbach M, Schneider PB, Brandstetter H, Simon-Nobbe B
Title Crystal structure of the NADP-dependent mannitol dehydrogenase from Cladosporium herbarum: Implications for oligomerisation and catalysis.
Related PDB 3gdf 3gdg
Related UniProtKB

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.

Created Updated
2012-09-12 2012-09-28