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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.

MDR family oxidoreductase

MDR (medium chain dehydrogenase/reductase) family oxidoreductase similar to acrylyl-CoA reductase AcuI, which catalyzes the NADPH-dependent reduction of acrylyl-CoA to propanoyl-CoA

Date:
2023-03-01
Family Accession:
10169682
Method:
Sparcle
8.

acryloyl-CoA reductase

This model represents a subfamily of PF00107 as defined by Pfam, a superfamily in which some members are zinc-binding medium-chain alcohol dehydrogenases while others are quinone oxidoreductases with no bound zinc. This subfamily includes proteins studied crystallographically for insight into function: YhdH from Escherichia coli and YhfP from Bacillus subtilis. Members bind NADPH or NAD, but not zinc.

GO Terms:
Biological Process:
metabolic process (GO:0008152)
Molecular Function:
oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor (GO:0016655)
Date:
2021-04-27
Family Accession:
TIGR02823.1
Method:
HMM
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