EzCatDB: D00017

DB codeD00017
CATH domainDomain 13.40.50.720Catalytic domain
Domain 23.30.360.10Catalytic domain
E.C.1.1.99.28
CSA1ofg

CATH domainRelated DB codes (homologues)
3.30.360.10T00219,D00003,D00010,D00023,D00027,D00028,D00034,D00476
3.40.50.720S00543,S00551,S00552,S00553,S00602,S00604,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,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
Swiss-protKEGG

Q07982
Protein nameGlucose--fructose oxidoreductaseglucose-fructose oxidoreductase
SynonymsGFOR
EC 1.1.99.28


Swiss-prot:Accession NumberQ07982
Entry nameGFO_ZYMMO
ActivityD-glucose + D-fructose = D-gluconolactone + D- glucitol.
SubunitHomotetramer.
Subcellular locationPeriplasm.
CofactorBinds 1 NADP(+) per subunit. The NADP cannot dissociate.


CofactorsSubstratesProducts
KEGG-idC00005C00031C10906C00198C00794
CompoundNADPHD-GlucoseD-FructoseD-GluconolactoneD-Sorbitol
Typeamide group,amine group,nucleotidecarbohydratecarbohydratecarbohydratecarbohydrate
1ofgA01Bound:NDPUnboundUnboundUnboundUnbound
1ofgB01Bound:NDPUnboundUnboundUnboundUnbound
1ofgC01Bound:NDPUnboundUnboundUnboundUnbound
1ofgD01Bound:NDPUnboundUnboundUnboundUnbound
1ofgE01Bound:NDPUnboundUnboundUnboundUnbound
1ofgF01Bound:NDPUnboundUnboundUnboundUnbound
1evjA01Analogue:NADUnboundUnboundUnboundUnbound
1evjB01Analogue:NADUnboundUnboundUnboundUnbound
1evjC01Analogue:NADUnboundUnboundUnboundUnbound
1evjD01Analogue:NADUnboundUnboundUnboundUnbound
1h6aA01Bound:NDPUnboundUnboundUnboundUnbound
1h6aB01Bound:NDPUnboundUnboundUnboundUnbound
1h6bA01Bound:NDPUnboundUnboundUnboundUnbound
1h6bB01Bound:NDPUnboundUnboundUnboundUnbound
1h6cA01Bound:NDPUnboundUnboundUnboundUnbound
1h6cB01Bound:NDPUnboundUnboundUnboundUnbound
1h6dA01Bound:NDPUnboundUnboundUnboundUnbound
1h6dB01Bound:NDPUnboundUnboundUnboundUnbound
1h6dC01Bound:NDPUnboundUnboundUnboundUnbound
1h6dD01Bound:NDPUnboundUnboundUnboundUnbound
1h6dE01Bound:NDPUnboundUnboundUnboundUnbound
1h6dF01Bound:NDPUnboundUnboundUnboundUnbound
1h6dG01Bound:NDPUnboundUnboundUnboundUnbound
1h6dH01Bound:NDPUnboundUnboundUnboundUnbound
1h6dI01Bound:NDPUnboundUnboundUnboundUnbound
1h6dJ01Bound:NDPUnboundUnboundUnboundUnbound
1h6dK01Bound:NDPUnboundUnboundUnboundUnbound
1h6dL01Bound:NDPUnboundUnboundUnboundUnbound
1ofgA02UnboundUnboundUnboundUnboundUnbound
1ofgB02UnboundUnboundUnboundUnboundUnbound
1ofgC02UnboundUnboundUnboundUnboundUnbound
1ofgD02UnboundUnboundUnboundUnboundUnbound
1ofgE02UnboundUnboundUnboundUnboundUnbound
1ofgF02UnboundUnboundUnboundUnboundUnbound
1evjA02UnboundUnboundUnboundUnboundUnbound
1evjB02UnboundUnboundUnboundUnboundUnbound
1evjC02UnboundUnboundUnboundUnboundUnbound
1evjD02UnboundUnboundUnboundUnboundUnbound
1h6aA02UnboundUnboundUnboundUnboundUnbound
1h6aB02UnboundUnboundUnboundUnboundUnbound
1h6bA02UnboundAnalogue:GOLUnboundUnboundUnbound
1h6bB02UnboundAnalogue:GOLUnboundUnboundUnbound
1h6cA02UnboundUnboundUnboundUnboundUnbound
1h6cB02UnboundUnboundUnboundUnboundUnbound
1h6dA02UnboundAnalogue:GOLUnboundUnboundUnbound
1h6dB02UnboundAnalogue:GOLUnboundUnboundUnbound
1h6dC02UnboundAnalogue:GOLUnboundUnboundUnbound
1h6dD02UnboundAnalogue:GOLUnboundUnboundUnbound
1h6dE02UnboundAnalogue:GOLUnboundUnboundUnbound
1h6dF02UnboundAnalogue:GOLUnboundUnboundUnbound
1h6dG02UnboundAnalogue:GOLUnboundUnboundUnbound
1h6dH02UnboundAnalogue:GOLUnboundUnboundUnbound
1h6dI02UnboundAnalogue:GOLUnboundUnboundUnbound
1h6dJ02UnboundAnalogue:GOLUnboundUnboundUnbound
1h6dK02UnboundAnalogue:GOLUnboundUnboundUnbound
1h6dL02UnboundAnalogue:GOLUnboundUnboundUnbound

Active-site residues
resource
literature [2]
pdbCatalytic residues
1ofgA01LYS 129
1ofgB01LYS 129
1ofgC01LYS 129
1ofgD01LYS 129
1ofgE01LYS 129
1ofgF01LYS 129
1evjA01LYS 129
1evjB01LYS 129
1evjC01LYS 129
1evjD01LYS 129
1h6aA01LYS 181
1h6aB01LYS 181
1h6bA01LYS 181
1h6bB01LYS 181
1h6cA01LYS 181
1h6cB01LYS 181
1h6dA01LYS 181
1h6dB01LYS 181
1h6dC01LYS 181
1h6dD01LYS 181
1h6dE01LYS 181
1h6dF01LYS 181
1h6dG01LYS 181
1h6dH01LYS 181
1h6dI01LYS 181
1h6dJ01LYS 181
1h6dK01LYS 181
1h6dL01LYS 181
1ofgA02TYR 217
1ofgB02TYR 217
1ofgC02TYR 217
1ofgD02TYR 217
1ofgE02TYR 217
1ofgF02TYR 217
1evjA02TYR 217
1evjB02TYR 217
1evjC02TYR 217
1evjD02TYR 217
1h6aA02TYR 269
1h6aB02TYR 269
1h6bA02TYR 269
1h6bB02TYR 269
1h6cA02TYR 269
1h6cB02TYR 269
1h6dA02TYR 269
1h6dB02TYR 269
1h6dC02TYR 269
1h6dD02TYR 269
1h6dE02TYR 269
1h6dF02TYR 269
1h6dG02TYR 269
1h6dH02TYR 269
1h6dI02TYR 269
1h6dJ02TYR 269
1h6dK02TYR 269
1h6dL02TYR 269

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]p.1420-1422
[6]p.13865-13866

references
[1]
PubMed ID7756998
JournalProtein Sci
Year1994
Volume3
Pages2447-9
AuthorsLoos H, Ermler U, Sprenger GA, Sahm H
TitleCrystallization and preliminary X-ray analysis of glucose-fructose oxidoreductase from Zymomonas mobilis.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS)
Medline ID97148336
PubMed ID8994968
JournalStructure
Year1996
Volume4
Pages1413-28
AuthorsKingston RL, Scopes RK, Baker EN
TitleThe structure of glucose-fructose oxidoreductase from Zymomonas mobilis: an osmoprotective periplasmic enzyme containing non-dissociable NADP.
Related PDB1ofg
Related Swiss-protQ07982
[3]
PubMed ID9490072
JournalEur J Biochem
Year1998
Volume251
Pages955-63
AuthorsFurlinger M, Haltrich D, Kulbe KD, Nidetzky B
TitleA multistep process is responsible for product-induced inactivation of glucose-fructose oxidoreductase from Zymomonas mobilis.
[4]
CommentsD00017-15
PubMed ID11097839
JournalBiochem Biophys Res Commun
Year2000
Volume278
Pages333-7
AuthorsAsada Y, Aoki S, Ishikura S, Usami N, Hara A
TitleRoles of His-79 and Tyr-180 of D-xylose/dihydrodiol dehydrogenase in catalytic function.
[5]
PubMed ID11099381
JournalJ Mol Biol
Year2000
Volume304
Pages575-84
AuthorsLott JS, Halbig D, Baker HM, Hardman MJ, Sprenger GA, Baker EN
TitleCrystal structure of a truncated mutant of glucose-fructose oxidoreductase shows that an N-terminal arm controls tetramer formation.
Related PDB1evj
[6]
PubMed ID11705375
JournalBiochemistry
Year2001
Volume40
Pages13857-67
AuthorsNurizzo D, Halbig D, Sprenger GA, Baker EN
TitleCrystal structures of the precursor form of glucose-fructose oxidoreductase from Zymomonas mobilis and its complexes with bound ligands.
Related PDB1h6a,1h6b,1h6c,1h6d
[7]
PubMed ID12423337
JournalEur J Biochem
Year2002
Volume269
Pages5391-405
AuthorsMazitsos CF, Rigden DJ, Tsoungas PG, Clonis YD
TitleGalactosyl-mimodye ligands for Pseudomonas fluorescens beta-galactose dehydrogenase.


createdupdated
2004-07-162009-02-26


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 2010)
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)

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