S00604
type: Enzyme
rlcp: p8010
cath: Rossmann fold
ec: https://purl.uniprot.org/enzyme/1.1.1.138
uniprot: O93868
uniprot: P0C0Y5
kegg enzyme: Mannitol 2-dehydrogenase (NADP+)
kegg pathway: Fructose and mannose metabolism
kegg substrate: D-mannitol
kegg substrate: NADP+
kegg product: D-fructose
kegg product: NADPH
kegg product: H+
pdb: 1h5qA00
pdb: 1h5qB00
pdb: 1h5qC00
pdb: 1h5qD00
pdb: 1h5qE00
pdb: 1h5qF00
pdb: 1h5qG00
pdb: 1h5qH00
pdb: 1h5qI00
pdb: 1h5qJ00
pdb: 1h5qK00
pdb: 1h5qL00
pdb: 3gdfA00
pdb: 3gdfB00
pdb: 3gdfC00
pdb: 3gdfD00
pdb: 3gdgA00
pdb: 3gdgB00
pdb: 3gdgC00
pdb: 3gdgD00
pdb bound state: Unbound
  compound: D-mannitol
  pdb: 1h5qA00
pdb bound state: Unbound
  compound: D-mannitol
  pdb: 1h5qB00
pdb bound state: Unbound
  compound: D-mannitol
  pdb: 1h5qC00
pdb bound state: Unbound
  compound: D-mannitol
  pdb: 1h5qD00
pdb bound state: Unbound
  compound: D-mannitol
  pdb: 1h5qE00
pdb bound state: Unbound
  compound: D-mannitol
  pdb: 1h5qF00
pdb bound state: Unbound
  compound: D-mannitol
  pdb: 1h5qG00
pdb bound state: Unbound
  compound: D-mannitol
  pdb: 1h5qH00
pdb bound state: Unbound
  compound: D-mannitol
  pdb: 1h5qI00
pdb bound state: Unbound
  compound: D-mannitol
  pdb: 1h5qJ00
pdb bound state: Unbound
  compound: D-mannitol
  pdb: 1h5qK00
pdb bound state: Unbound
  compound: D-mannitol
  pdb: 1h5qL00
pdb bound state: Unbound
  compound: D-mannitol
  pdb: 3gdfA00
pdb bound state: Unbound
  compound: D-mannitol
  pdb: 3gdfB00
pdb bound state: Unbound
  compound: D-mannitol
  pdb: 3gdfC00
pdb bound state: Unbound
  compound: D-mannitol
  pdb: 3gdfD00
pdb bound state: Unbound
  compound: D-mannitol
  pdb: 3gdgA00
pdb bound state: Unbound
  compound: D-mannitol
  pdb: 3gdgB00
pdb bound state: Unbound
  compound: D-mannitol
  pdb: 3gdgC00
pdb bound state: Unbound
  compound: D-mannitol
  pdb: 3gdgD00
pdb bound state: Unbound
  compound: NADP+
  pdb: 3gdfA00
pdb bound state: Unbound
  compound: NADP+
  pdb: 3gdfB00
pdb bound state: Unbound
  compound: NADP+
  pdb: 3gdfC00
pdb bound state: Unbound
  compound: NADP+
  pdb: 3gdfD00
pdb bound state: Unbound
  compound: NADP+
  pdb: 3gdgA00
pdb bound state: Unbound
  compound: NADP+
  pdb: 3gdgB00
pdb bound state: Unbound
  compound: NADP+
  pdb: 3gdgC00
pdb bound state: Unbound
  compound: NADP+
  pdb: 3gdgD00
pdb bound state: Unbound
  compound: D-fructose
  pdb: 1h5qA00
pdb bound state: Unbound
  compound: D-fructose
  pdb: 1h5qB00
pdb bound state: Unbound
  compound: D-fructose
  pdb: 1h5qC00
pdb bound state: Unbound
  compound: D-fructose
  pdb: 1h5qD00
pdb bound state: Unbound
  compound: D-fructose
  pdb: 1h5qE00
pdb bound state: Unbound
  compound: D-fructose
  pdb: 1h5qF00
pdb bound state: Unbound
  compound: D-fructose
  pdb: 1h5qG00
pdb bound state: Unbound
  compound: D-fructose
  pdb: 1h5qH00
pdb bound state: Unbound
  compound: D-fructose
  pdb: 1h5qI00
pdb bound state: Unbound
  compound: D-fructose
  pdb: 1h5qJ00
pdb bound state: Unbound
  compound: D-fructose
  pdb: 1h5qK00
pdb bound state: Unbound
  compound: D-fructose
  pdb: 1h5qL00
pdb bound state: Unbound
  compound: D-fructose
  pdb: 3gdfA00
active site residues resources: Crystal structure of the NADP-dependent mannitol dehydrogenase from Cladosporium herbarum: Implications for oligomerisation and catalysis.
active site residues resources: http://ezcatdb.cbrc.jp/EzCatDB/reference/S00604#4
references: Forms and functions of human SDR enzymes.
references: The crystallographic structure of the mannitol 2-dehydrogenase NADP+ binary complex from Agaricus bisporus.
references: Crystal structure of the NADP-dependent mannitol dehydrogenase from Cladosporium herbarum: Implications for oligomerisation and catalysis.
comment: 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.

Rossmann fold
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.720
catalytic domain: index.html

Fructose and mannose metabolism
type: KeggPathway
references: KEGG:MAP00051

D-mannitol
type: KeggSubstrate
references: KEGG:C00392
compound type: carbohydrate
references: CHEBI:16899
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

NADP+
type: KeggSubstrate
references: KEGG:C00006
compound type: amide group
compound type: amine group
compound type: nucleotide
references: CHEBI:18009
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

D-fructose
type: KeggProduct
references: KEGG:C00095
compound type: carbohydrate
references: CHEBI:37721
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

NADPH
type: KeggProduct
references: KEGG:C00005
compound type: amide group
compound type: amine group
compound type: nucleotide
references: CHEBI:16474
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

H+
type: KeggProduct
references: KEGG:C00080
compound type: others
references: CHEBI:15378
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

1h5qA00
type: Pdb
references: 1h5q
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h5q
catalytic residue: SER 149;TYR 169;LYS 173

1h5qB00
type: Pdb
references: 1h5q
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h5q
catalytic residue: SER 149;TYR 169;LYS 173

1h5qC00
type: Pdb
references: 1h5q
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h5q
catalytic residue: SER 149;TYR 169;LYS 173

1h5qD00
type: Pdb
references: 1h5q
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h5q
catalytic residue: SER 149;TYR 169;LYS 173

1h5qE00
type: Pdb
references: 1h5q
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h5q
catalytic residue: SER 149;TYR 169;LYS 173

1h5qF00
type: Pdb
references: 1h5q
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h5q
catalytic residue: SER 149;TYR 169;LYS 173

1h5qG00
type: Pdb
references: 1h5q
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h5q
catalytic residue: SER 149;TYR 169;LYS 173

1h5qH00
type: Pdb
references: 1h5q
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h5q
catalytic residue: SER 149;TYR 169;LYS 173

1h5qI00
type: Pdb
references: 1h5q
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h5q
catalytic residue: SER 149;TYR 169;LYS 173

1h5qJ00
type: Pdb
references: 1h5q
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h5q
catalytic residue: SER 149;TYR 169;LYS 173

1h5qK00
type: Pdb
references: 1h5q
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h5q
catalytic residue: SER 149;TYR 169;LYS 173

1h5qL00
type: Pdb
references: 1h5q
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h5q
catalytic residue: SER 149;TYR 169;LYS 173

3gdfA00
type: Pdb
references: 3gdf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3gdf
catalytic residue: SER 149;TYR 169;LYS 173

3gdfB00
type: Pdb
references: 3gdf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3gdf
catalytic residue: SER 160;TYR 175;Lys 179

3gdfC00
type: Pdb
references: 3gdf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3gdf
catalytic residue: SER 160;TYR 175;Lys 179

3gdfD00
type: Pdb
references: 3gdf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3gdf
catalytic residue: SER 160;TYR 175;Lys 179

3gdgA00
type: Pdb
references: 3gdg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3gdg
catalytic residue: SER 160;TYR 175;Lys 179

3gdgB00
type: Pdb
references: 3gdg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3gdg
catalytic residue: SER 160;TYR 175;Lys 179

3gdgC00
type: Pdb
references: 3gdg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3gdg
catalytic residue: SER 160;TYR 175;Lys 179

3gdgD00
type: Pdb
references: 3gdg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3gdg
catalytic residue: SER 160;TYR 175;Lys 179

Forms and functions of human SDR enzymes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11306087
journal: Chem Biol Interact
volume: 130-132
pages: 699-705
published year: 2001
authors:
  item: Oppermann UC
  item: Filling C
  item: Jornvall H

The crystallographic structure of the mannitol 2-dehydrogenase NADP+ binary complex from Agaricus bisporus.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11335726
journal: J Biol Chem
volume: 276
pages: 27555-61
published year: 2001
authors:
  item: Horer S
  item: Stoop J
  item: Mooibroek H
  item: Baumann U
  item: Sassoon J
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Crystal structure of the NADP-dependent mannitol dehydrogenase from Cladosporium herbarum: Implications for oligomerisation and catalysis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/20420880
journal: Biochimie
volume: 92
pages: 985-93
published year: 2010
authors:
  item: Nuss D
  item: Goettig P
  item: Magler I
  item: Denk U
  item: Breitenbach M
  item: Schneider PB
  item: Brandstetter H
  item: Simon-Nobbe B
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

ReferenceForCatalyticMechanism
reference index: 2
reference section: Fig.4, p.27558

ReferenceForCatalyticMechanism
reference index: 3
reference section: Fig.6, p.990-992