DB code: S00605

RLCP classification 9.5010.536200.8010 : Hydride transfer
9.1050.440000.8010 : Hydride transfer
CATH domain 3.40.50.720 : Rossmann fold Catalytic domain
E.C. 1.1.1.14
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.40.50.720 : Rossmann fold S00543 S00551 S00552 S00553 S00602 S00604 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 RefSeq
Q59787 Sorbitol dehydrogenase
EC 1.1.1.14
L-iditol 2-dehydrogenase
Polyol dehydrogenase
PF00106 (adh_short)
[Graphical View]
Q92N06
Probable sorbitol dehydrogenase (L-iditol 2-dehydrogenase)
EC 1.1.1.14
PF00106 (adh_short)
[Graphical View]
NP_386547.1 (Protein)
NC_003047.1 (DNA/RNA sequence)

KEGG enzyme name
L-iditol 2-dehydrogenase
Polyol dehydrogenase
Sorbitol dehydrogenase
L-iditol:NAD+ 5-oxidoreductase
L-iditol (sorbitol) dehydrogenase
Glucitol dehydrogenase
L-iditol:NAD+ oxidoreductase
NAD+-dependent sorbitol dehydrogenase
NAD+-dependent sorbitol dehydrogenase
NAD+-sorbitol dehydrogenase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q92N06 Q92N06_RHIME
Q59787 DHSO_RHOSH L-iditol + NAD(+) = L-sorbose + NADH. Homodimer.

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

Compound table
Substrates Products Intermediates
KEGG-id C01507 C00003 C00247 C00004 C00080
E.C.
Compound L-iditol NAD+ L-sorbose NADH H+
Type carbohydrate amide group,amine group,nucleotide carbohydrate amide group,amine group,nucleotide others
ChEBI 18202
15846
48649
16908
15378
PubChem 453
5460044
5893
439192
439153
1038
1k2wA00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1k2wB00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
4e6pA00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
4e6pB00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
4e6pC00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
4e6pD00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [3], [5]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1k2wA00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 139;TYR 152;LYS 156
1k2wB00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 139;TYR 152;LYS 156
4e6pA00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 140;TYR 153;LYS 157
4e6pB00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 140;TYR 153;LYS 157
4e6pC00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 140;TYR 153;LYS 157
4e6pD00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 140;TYR 153;LYS 157

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[1]
Fig.11, p.7727-7728 2
[3]
Fig.5, p.25682
[4]
p.250
[5]
p.377

References
[1]
Resource
Comments
Medline ID
PubMed ID 8672472
Journal Biochemistry
Year 1996
Volume 35
Pages 7715-30
Authors Tanaka N, Nonaka T, Tanabe T, Yoshimoto T, Tsuru D, Mitsui Y
Title Crystal structures of the binary and ternary complexes of 7 alpha-hydroxysteroid dehydrogenase from Escherichia coli.
Related PDB
Related UniProtKB
[2]
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
[3]
Resource
Comments
Medline ID
PubMed ID 11976334
Journal J Biol Chem
Year 2002
Volume 277
Pages 25677-84
Authors Filling C, Berndt KD, Benach J, Knapp S, Prozorovski T, Nordling E, Ladenstein R, Jornvall H, Oppermann U
Title Critical residues for structure and catalysis in short-chain dehydrogenases/reductases.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 12604210
Journal Chem Biol Interact
Year 2003
Volume 143-144
Pages 247-53
Authors Oppermann U, Filling C, Hult M, Shafqat N, Wu X, Lindh M, Shafqat J, Nordling E, Kallberg Y, Persson B, Jornvall H
Title Short-chain dehydrogenases/reductases (SDR): the 2002 update.
Related PDB
Related UniProtKB
[5]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
Medline ID
PubMed ID 15805591
Journal Acta Crystallogr D Biol Crystallogr
Year 2005
Volume 61
Pages 374-9
Authors Philippsen A, Schirmer T, Stein MA, Giffhorn F, Stetefeld J
Title Structure of zinc-independent sorbitol dehydrogenase from Rhodobacter sphaeroides at 2.4 A resolution.
Related PDB 1k2w
Related UniProtKB Q59787

Comments
This enzyme belongs to short-chain dehydrogenases/reductases (SDR)(see [2], [4]) (S00320, S00327, S00328, S00330, S00332, S00602 and S00610 in EzCatDB).
Since the active site of this enzyme is similar to those homologous enzymes, the catalytic mechanism can be similar to those mechanisms.

Created Updated
2012-07-30 2012-08-28