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InterPro: IPR004104 Oxidoreductase, C-terminal

Protein matchesHelp
UniProtKB
Matches:
5260 proteins
AccessionHelp IPR004104 OxRdtase_C
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR008354 Glucose-fructose oxidoreductase, bacterial
GO Term annotationHelp
Process GO:0008152 metabolic process
GO:0055114 oxidation reduction
Function GO:0016491 oxidoreductase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Enzymes containing this domain utilise NADP or NAD, and are 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, C-terminal domain is almost always associated with the oxidoreductase, N-terminal domain (see IPR000683).

Structural linksHelp
SCOP: d.81.1.5
CATH: 3.30.360.10
Database linksHelp
Enzyme: EC:1
PANDIT: PF02894
Pfam Clan: CL0218.8

Taxonomic coverageHelp

Example proteinsHelp
P74041 Uncharacterized oxidoreductase sll0816

Q04869 Uncharacterized protein YMR315W

Q3B7J2 Glucose-fructose oxidoreductase domain-containing protein 2

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
IPR016040 NAD(P)-binding domain
IPR004104 Oxidoreductase, C-terminal
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp

Additional ReadingHelp
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
Lott JS, Halbig D, Baker HM, Hardman MJ, Sprenger GA, Baker EN.
Crystal structure of a truncated mutant of glucose-fructose oxidoreductase shows that an N-terminal arm controls tetramer formation.
J. Mol. Biol. 304 2000 575-84 [PubMed: 11099381]
http://dx.doi.org/10.1006/jmbi.2000.4245
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InterPro 23.1