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Links from Protein

Items: 8

1.

alcohol dehydrogenase catalytic domain-containing protein

This is the catalytic domain of alcohol dehydrogenases. Many of them contain an inserted zinc binding domain. This domain has a GroES-like structure [1-2]. [1]. 8804825. Structural classification of proteins: new superfamilies. Murzin AG;. Curr Opin Struct Biol 1996;6:386-394. [2]. 10556240. Conserved structural features and sequence patterns in the GroES fold family. Taneja B, Mande SC;. Protein Eng 1999;12:815-818. (from Pfam)

Date:
2024-10-16
Family Accession:
NF019845.5
Method:
HMM
2.

zinc-binding dehydrogenase

Date:
2024-08-14
Family Accession:
NF012335.5
Method:
HMM
3.
new record, indexing in progress
Family Accession:
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.

zinc-binding alcohol dehydrogenase family protein

zinc-binding alcohol dehydrogenase family protein such as quinone oxidoreductase (QOR), which catalyzes the conversion of a quinone and NAD(P)H to a hydroquinone and NAD(P)+

Date:
2017-11-06
Family Accession:
10169592
Method:
Sparcle
8.

zinc-binding alcohol dehydrogenase family protein

Members of this model form a distinct subset of the larger family of oxidoreductases that includes zinc-binding alcohol dehydrogenases and NADPH:quinone reductases (PF00107). While some current members of this family carry designations as putative alginate lyase, it seems no sequence with a direct characterization as such is detected by this model.

GO Terms:
Molecular Function:
alcohol dehydrogenase (NAD+) activity (GO:0004022)
Molecular Function:
zinc ion binding (GO:0008270)
Date:
2024-10-21
Family Accession:
TIGR02817.1
Method:
HMM
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