EzCatDB: S00605
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DB codeS00605
RLCP classification9.1050.440000.8010 : Hydride transfer
9.5010.536200.8010 : Hydride transfer
CATH domainDomain 13.40.50.720 : Rossmann foldCatalytic domain
E.C.1.1.1.14

CATH domainRelated DB codes (homologues)
3.40.50.720 : Rossmann foldS00543,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

Enzyme Name
UniProtKBKEGG

Q59787Q92N06
Protein nameSorbitol dehydrogenase
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
SynonymsEC 1.1.1.14
L-iditol 2-dehydrogenase
Polyol dehydrogenase
Probable sorbitol dehydrogenase (L-iditol 2-dehydrogenase)
EC 1.1.1.14
RefSeq
NP_386547.1 (Protein)
NC_003047.1 (DNA/RNA sequence)
PfamPF00106 (adh_short)
[Graphical view]
PF00106 (adh_short)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00051Fructose and mannose metabolism

UniProtKB:Accession NumberQ59787Q92N06
Entry nameDHSO_RHOSHQ92N06_RHIME
ActivityL-iditol + NAD(+) = L-sorbose + NADH.
SubunitHomodimer.
Subcellular location

Cofactor


Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC01507C00003C00247C00004C00080
CompoundL-iditolNAD+L-sorboseNADHH+
Typecarbohydrateamide group,amine group,nucleotidecarbohydrateamide group,amine group,nucleotideothers
ChEBI18202
15846
48649
16908
15378
PubChem5460044
453
5893
439192
439153
1038
             
1k2wA00UnboundUnboundUnboundUnbound 
1k2wB00UnboundUnboundUnboundUnbound 
4e6pA00UnboundUnboundUnboundUnbound 
4e6pB00UnboundUnboundUnboundUnbound 
4e6pC00UnboundUnboundUnboundUnbound 
4e6pD00UnboundUnboundUnboundUnbound 

Active-site residues
resource
literature [3], [5]
pdbCatalytic residues
         
1k2wA00SER 139;TYR 152;LYS 156
1k2wB00SER 139;TYR 152;LYS 156
4e6pA00SER 140;TYR 153;LYS 157
4e6pB00SER 140;TYR 153;LYS 157
4e6pC00SER 140;TYR 153;LYS 157
4e6pD00SER 140;TYR 153;LYS 157

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]Fig.11, p.7727-77282
[3]Fig.5, p.25682
[4]p.250
[5]p.377

references
[1]
PubMed ID8672472
JournalBiochemistry
Year1996
Volume35
Pages7715-30
AuthorsTanaka N, Nonaka T, Tanabe T, Yoshimoto T, Tsuru D, Mitsui Y
TitleCrystal structures of the binary and ternary complexes of 7 alpha-hydroxysteroid dehydrogenase from Escherichia coli.
[2]
PubMed ID11306087
JournalChem Biol Interact
Year2001
Volume130-132
Pages699-705
AuthorsOppermann UC, Filling C, Jornvall H
TitleForms and functions of human SDR enzymes.
[3]
PubMed ID11976334
JournalJ Biol Chem
Year2002
Volume277
Pages25677-84
AuthorsFilling C, Berndt KD, Benach J, Knapp S, Prozorovski T, Nordling E, Ladenstein R, Jornvall H, Oppermann U
TitleCritical residues for structure and catalysis in short-chain dehydrogenases/reductases.
[4]
PubMed ID12604210
JournalChem Biol Interact
Year2003
Volume143-144
Pages247-53
AuthorsOppermann U, Filling C, Hult M, Shafqat N, Wu X, Lindh M, Shafqat J, Nordling E, Kallberg Y, Persson B, Jornvall H
TitleShort-chain dehydrogenases/reductases (SDR): the 2002 update.
[5]
CommentsX-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
PubMed ID15805591
JournalActa Crystallogr D Biol Crystallogr
Year2005
Volume61
Pages374-9
AuthorsPhilippsen A, Schirmer T, Stein MA, Giffhorn F, Stetefeld J
TitleStructure of zinc-independent sorbitol dehydrogenase from Rhodobacter sphaeroides at 2.4 A resolution.
Related PDB1k2w
Related UniProtKBQ59787

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.

createdupdated
2012-07-302012-08-28


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
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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