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InterPro: IPR000683 Oxidoreductase, N-terminal

Protein matchesHelp
UniProtKB
Matches:
8078 proteins
AccessionHelp IPR000683 Oxidoreductase_N
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR008354 Glucose-fructose oxidoreductase, bacterial
IPR010091 Thiazolinyl imide reductase
IPR016040 NAD(P)-binding domain
IPR017094 Biliverdin reductase A
GO Term annotationHelp
Function GO:0016491 oxidoreductase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This group of enzymes utilise NADP or NAD, and is known as the GFO/IDH/MOCA family in UniProtKB/Swiss-Prot. GFO is a glucose--fructose oxidoreductase, which converts D-glucose and D-fructose into D-gluconolactone and D-glucitol in the sorbitol-gluconate pathway. MOCA is a rhizopine catabolism protein which may catalyse the NADH-dependent dehydrogenase reaction involved in rhizopine catabolism. Other proteins belonging to this family include Gal80, a negative regulator for the expression of lactose and galactose metabolic genes; and several hypothetical proteins from yeast, Escherichia coli and Bacillus subtilis.

The oxidoreductase, N-terminal domain is almost always associated with the oxidoreductase, C-terminal domain (see IPR004104).

Structural linksHelp
SCOP: c.2.1.3
CATH: 3.40.50.720
Database linksHelp
PANDIT: PF01408
Blocks: IPB000683
Pfam Clan: CL0063.21

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR000683 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P04387 Galactose/lactose metabolism regulatory protein GAL80

P53004 Biliverdin reductase A

P74041 Uncharacterized oxidoreductase sll0816

Q3UHD2 Glucose-fructose oxidoreductase domain-containing protein 1

Q9SZ83 Uncharacterized oxidoreductase At4g09670

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR000683 Oxidoreductase, N-terminal
IPR015249 Biliverdin reductase, catalytic
IPR017094 Biliverdin reductase A
IPR016040 NAD(P)-binding domain
IPR004104 Oxidoreductase, C-terminal
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp

Additional ReadingHelp
Levin EJ, Kondrashov DA, Wesenberg GE, Phillips GN Jr.
Ensemble refinement of protein crystal structures: validation and application.
Structure 15 2007 1040-52 [PubMed: 17850744]
http://dx.doi.org/10.1016/j.str.2007.06.019
Nurizzo D, Halbig D, Sprenger GA, Baker EN.
Crystal structures of the precursor form of glucose-fructose oxidoreductase from Zymomonas mobilis and its complexes with bound ligands.
Biochemistry 40 2001 13857-67 [PubMed: 11705375]
http://dx.doi.org/10.1021/bi011355d
Kingston RL, Scopes RK, Baker EN.
The structure of glucose-fructose oxidoreductase from Zymomonas mobilis: an osmoprotective periplasmic enzyme containing non-dissociable NADP.
Structure 4 1996 1413-28 [PubMed: 8994968]
http://dx.doi.org/10.1016/S0969-2126(96)00149-9
Thoden JB, Ryan LA, Reece RJ, Holden HM.
The interaction between an acidic transcriptional activator and its inhibitor. The molecular basis of Gal4p recognition by Gal80p.
J. Biol. Chem. 283 2008 30266-72 [PubMed: 18701455]
http://dx.doi.org/10.1074/jbc.M805200200
Thoden JB, Sellick CA, Reece RJ, Holden HM.
Understanding a transcriptional paradigm at the molecular level. The structure of yeast Gal80p.
J. Biol. Chem. 282 2007 1534-8 [PubMed: 17121853]
http://dx.doi.org/10.1074/jbc.C600285200
Whitby FG, Phillips JD, Hill CP, McCoubrey W, Maines MD.
Crystal structure of a biliverdin IXalpha reductase enzyme-cofactor complex.
J. Mol. Biol. 319 2002 1199-210 [PubMed: 12079357]
http://dx.doi.org/10.1016/S0022-2836(02)00383-2
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InterPro 23.1