DB code: D00017

CATH domain 3.40.50.720 : Rossmann fold Catalytic domain
3.30.360.10 : Dihydrodipicolinate Reductase; domain 2 Catalytic domain
E.C. 1.1.99.28
CSA 1ofg
M-CSA 1ofg
MACiE

CATH domain Related DB codes (homologues)
3.30.360.10 : Dihydrodipicolinate Reductase; domain 2 T00219 D00003 D00010 D00023 D00027 D00028 D00034 D00476
3.40.50.720 : Rossmann fold S00543 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

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
Q07982 Glucose--fructose oxidoreductase
GFOR
EC 1.1.99.28
YP_162424.1 (Protein)
NC_006526.2 (DNA/RNA sequence)
PF01408 (GFO_IDH_MocA)
PF02894 (GFO_IDH_MocA_C)
[Graphical View]

KEGG enzyme name
glucose-fructose oxidoreductase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q07982 GFO_ZYMMO D-glucose + D-fructose = D-gluconolactone + D- glucitol. Homotetramer. Periplasm. Binds 1 NADP(+) per subunit. The NADP cannot dissociate.

KEGG Pathways
Map code Pathways E.C.

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00005 C00031 C10906 C00198 C00794
E.C.
Compound NADPH D-Glucose D-Fructose D-Gluconolactone D-Sorbitol
Type amide group,amine group,nucleotide carbohydrate carbohydrate carbohydrate carbohydrate
ChEBI 16474
 16474
 		4167
 4167
 		48095
 48095
 		16217
 16217
 		17924
 17924
PubChem 5884
 5884
 		5793
 5793
 		5984
 5984
 		7027
 7027
 		5780
 5780
1ofgA01 Bound:NDP Unbound Unbound Unbound Unbound
1ofgB01 Bound:NDP Unbound Unbound Unbound Unbound
1ofgC01 Bound:NDP Unbound Unbound Unbound Unbound
1ofgD01 Bound:NDP Unbound Unbound Unbound Unbound
1ofgE01 Bound:NDP Unbound Unbound Unbound Unbound
1ofgF01 Bound:NDP Unbound Unbound Unbound Unbound
1evjA01 Analogue:NAD Unbound Unbound Unbound Unbound
1evjB01 Analogue:NAD Unbound Unbound Unbound Unbound
1evjC01 Analogue:NAD Unbound Unbound Unbound Unbound
1evjD01 Analogue:NAD Unbound Unbound Unbound Unbound
1h6aA01 Bound:NDP Unbound Unbound Unbound Unbound
1h6aB01 Bound:NDP Unbound Unbound Unbound Unbound
1h6bA01 Bound:NDP Unbound Unbound Unbound Unbound
1h6bB01 Bound:NDP Unbound Unbound Unbound Unbound
1h6cA01 Bound:NDP Unbound Unbound Unbound Unbound
1h6cB01 Bound:NDP Unbound Unbound Unbound Unbound
1h6dA01 Bound:NDP Unbound Unbound Unbound Unbound
1h6dB01 Bound:NDP Unbound Unbound Unbound Unbound
1h6dC01 Bound:NDP Unbound Unbound Unbound Unbound
1h6dD01 Bound:NDP Unbound Unbound Unbound Unbound
1h6dE01 Bound:NDP Unbound Unbound Unbound Unbound
1h6dF01 Bound:NDP Unbound Unbound Unbound Unbound
1h6dG01 Bound:NDP Unbound Unbound Unbound Unbound
1h6dH01 Bound:NDP Unbound Unbound Unbound Unbound
1h6dI01 Bound:NDP Unbound Unbound Unbound Unbound
1h6dJ01 Bound:NDP Unbound Unbound Unbound Unbound
1h6dK01 Bound:NDP Unbound Unbound Unbound Unbound
1h6dL01 Bound:NDP Unbound Unbound Unbound Unbound
1ofgA02 Unbound Unbound Unbound Unbound Unbound
1ofgB02 Unbound Unbound Unbound Unbound Unbound
1ofgC02 Unbound Unbound Unbound Unbound Unbound
1ofgD02 Unbound Unbound Unbound Unbound Unbound
1ofgE02 Unbound Unbound Unbound Unbound Unbound
1ofgF02 Unbound Unbound Unbound Unbound Unbound
1evjA02 Unbound Unbound Unbound Unbound Unbound
1evjB02 Unbound Unbound Unbound Unbound Unbound
1evjC02 Unbound Unbound Unbound Unbound Unbound
1evjD02 Unbound Unbound Unbound Unbound Unbound
1h6aA02 Unbound Unbound Unbound Unbound Unbound
1h6aB02 Unbound Unbound Unbound Unbound Unbound
1h6bA02 Unbound Analogue:GOL Unbound Unbound Unbound
1h6bB02 Unbound Analogue:GOL Unbound Unbound Unbound
1h6cA02 Unbound Unbound Unbound Unbound Unbound
1h6cB02 Unbound Unbound Unbound Unbound Unbound
1h6dA02 Unbound Analogue:GOL Unbound Unbound Unbound
1h6dB02 Unbound Analogue:GOL Unbound Unbound Unbound
1h6dC02 Unbound Analogue:GOL Unbound Unbound Unbound
1h6dD02 Unbound Analogue:GOL Unbound Unbound Unbound
1h6dE02 Unbound Analogue:GOL Unbound Unbound Unbound
1h6dF02 Unbound Analogue:GOL Unbound Unbound Unbound
1h6dG02 Unbound Analogue:GOL Unbound Unbound Unbound
1h6dH02 Unbound Analogue:GOL Unbound Unbound Unbound
1h6dI02 Unbound Analogue:GOL Unbound Unbound Unbound
1h6dJ02 Unbound Analogue:GOL Unbound Unbound Unbound
1h6dK02 Unbound Analogue:GOL Unbound Unbound Unbound
1h6dL02 Unbound Analogue:GOL Unbound Unbound Unbound

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

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1ofgA01 LYS 129
1ofgB01 LYS 129
1ofgC01 LYS 129
1ofgD01 LYS 129
1ofgE01 LYS 129
1ofgF01 LYS 129
1evjA01 LYS 129
1evjB01 LYS 129
1evjC01 LYS 129
1evjD01 LYS 129
1h6aA01 LYS 181
1h6aB01 LYS 181
1h6bA01 LYS 181
1h6bB01 LYS 181
1h6cA01 LYS 181
1h6cB01 LYS 181
1h6dA01 LYS 181
1h6dB01 LYS 181
1h6dC01 LYS 181
1h6dD01 LYS 181
1h6dE01 LYS 181
1h6dF01 LYS 181
1h6dG01 LYS 181
1h6dH01 LYS 181
1h6dI01 LYS 181
1h6dJ01 LYS 181
1h6dK01 LYS 181
1h6dL01 LYS 181
1ofgA02 TYR 217
1ofgB02 TYR 217
1ofgC02 TYR 217
1ofgD02 TYR 217
1ofgE02 TYR 217
1ofgF02 TYR 217
1evjA02 TYR 217
1evjB02 TYR 217
1evjC02 TYR 217
1evjD02 TYR 217
1h6aA02 TYR 269
1h6aB02 TYR 269
1h6bA02 TYR 269
1h6bB02 TYR 269
1h6cA02 TYR 269
1h6cB02 TYR 269
1h6dA02 TYR 269
1h6dB02 TYR 269
1h6dC02 TYR 269
1h6dD02 TYR 269
1h6dE02 TYR 269
1h6dF02 TYR 269
1h6dG02 TYR 269
1h6dH02 TYR 269
1h6dI02 TYR 269
1h6dJ02 TYR 269
1h6dK02 TYR 269
1h6dL02 TYR 269

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
p.1420-1422
[6]
p.13865-13866

References
[1]
Resource
Comments
Medline ID
PubMed ID 7756998
Journal Protein Sci
Year 1994
Volume 3
Pages 2447-9
Authors Loos H, Ermler U, Sprenger GA, Sahm H
Title Crystallization and preliminary X-ray analysis of glucose-fructose oxidoreductase from Zymomonas mobilis.
Related PDB
Related UniProtKB
[2]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS)
Medline ID 97148336
PubMed ID 8994968
Journal Structure
Year 1996
Volume 4
Pages 1413-28
Authors Kingston RL, Scopes RK, Baker EN
Title The structure of glucose-fructose oxidoreductase from Zymomonas mobilis: an osmoprotective periplasmic enzyme containing non-dissociable NADP.
Related PDB 1ofg
Related UniProtKB Q07982
[3]
Resource
Comments
Medline ID
PubMed ID 9490072
Journal Eur J Biochem
Year 1998
Volume 251
Pages 955-63
Authors Furlinger M, Haltrich D, Kulbe KD, Nidetzky B
Title A multistep process is responsible for product-induced inactivation of glucose-fructose oxidoreductase from Zymomonas mobilis.
Related PDB
Related UniProtKB
[4]
Resource
Comments D00017-15
Medline ID
PubMed ID 11097839
Journal Biochem Biophys Res Commun
Year 2000
Volume 278
Pages 333-7
Authors Asada Y, Aoki S, Ishikura S, Usami N, Hara A
Title Roles of His-79 and Tyr-180 of D-xylose/dihydrodiol dehydrogenase in catalytic function.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 11099381
Journal J Mol Biol
Year 2000
Volume 304
Pages 575-84
Authors Lott JS, Halbig D, Baker HM, Hardman MJ, Sprenger GA, Baker EN
Title Crystal structure of a truncated mutant of glucose-fructose oxidoreductase shows that an N-terminal arm controls tetramer formation.
Related PDB 1evj
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 11705375
Journal Biochemistry
Year 2001
Volume 40
Pages 13857-67
Authors Nurizzo D, Halbig D, Sprenger GA, Baker EN
Title Crystal structures of the precursor form of glucose-fructose oxidoreductase from Zymomonas mobilis and its complexes with bound ligands.
Related PDB 1h6a 1h6b 1h6c 1h6d
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 12423337
Journal Eur J Biochem
Year 2002
Volume 269
Pages 5391-405
Authors Mazitsos CF, Rigden DJ, Tsoungas PG, Clonis YD
Title Galactosyl-mimodye ligands for Pseudomonas fluorescens beta-galactose dehydrogenase.
Related PDB
Related UniProtKB

Comments

Created Updated
2004-07-16 2009-02-26