U.S. flag

An official website of the United States government

Format
Items per page
Sort by

Send to:

Choose Destination

Links from Protein

Items: 14

1.

SDR family oxidoreductase

This domain is found in Enoyl-(Acyl carrier protein) reductases. (from Pfam)

Date:
2024-08-14
Family Accession:
NF024950.5
Method:
HMM
2.

KR domain-containing protein

This enzymatic domain is part of bacterial polyketide synthases and catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group [1]. [1]. 23790488. Structural and stereochemical analysis of a modular polyketide synthase ketoreductase domain required for the generation of a cis-alkene. Bonnett SA, Whicher JR, Papireddy K, Florova G, Smith JL, Reynolds KA;. Chem Biol. 2013;20:772-783. (from Pfam)

Date:
2024-10-16
Family Accession:
NF020243.5
Method:
HMM
3.

NAD-dependent epimerase/dehydratase family protein

This family of proteins utilise NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions. [1]. 9174344. Structural analysis of UDP-sugar binding to UDP-galactose 4-epimerase from Escherichia coli. Thoden JB, Hegeman AD, Wesenberg G, Chapeau MC, Frey PA, Holden HM;. Biochemistry 1997;36:6294-6304. (from Pfam)

GO Terms:
Molecular Function:
catalytic activity (GO:0003824)
Date:
2024-10-16
Family Accession:
NF013530.5
Method:
HMM
4.

SDR family NAD(P)-dependent oxidoreductase

This family contains a wide variety of dehydrogenases. [1]. 9735295. The refined crystal structure of Drosophila lebanonensis alcohol dehydrogenase at 1.9 A resolution. Benach J, Atrian S, Gonzalez-Duarte R, Ladenstein R;. J Mol Biol 1998;282:383-399. [2]. 10387002. Structure of tropinone reductase-II complexed with NADP+ and pseudotropine at 1.9 A resolution: implication for stereospecific substrate binding and catalysis. Yamashita A, Kato H, Wakatsuki S, Tomizaki T, Nakatsu T, Nakajima K, Hashimoto T, Yamada Y, Oda J;. Biochemistry 1999;38:7630-7637. (from Pfam)

Date:
2024-10-16
Family Accession:
NF012334.5
Method:
HMM
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.
new record, indexing in progress
Family Accession:
8.
new record, indexing in progress
Family Accession:
9.
new record, indexing in progress
Family Accession:
10.
new record, indexing in progress
Family Accession:
11.
new record, indexing in progress
Family Accession:
12.
new record, indexing in progress
Family Accession:
13.

glucose 1-dehydrogenase

GO Terms:
Molecular Function:
oxidoreductase activity (GO:0016491)
Date:
2021-07-21
Family Accession:
NF005559.1
Method:
HMM
14.

acetoin reductase

One member of this family, as characterized in Klebsiella terrigena, is described as able to interconvert acetoin + NADH with meso-2,3-butanediol + NAD(+). It is also called capable of irreversible reduction of diacetyl with NADH to acetoin. Blomqvist, et al. decline to specify either EC 1.1.1.4 which is (R,R)-butanediol dehydrogenase, or EC 1.1.1.5, which is acetoin dehydrogenase without a specified stereochemistry, for this enzyme. This enzyme is a homotetramer in the family of short chain dehydrogenases (PF00106). Another member of this family, from Corynebacterium glutamicum, is called L-2,3-butanediol dehydrogenase (PMID:11577733).

GO Terms:
Molecular Function:
acetoin dehydrogenase (NAD+) activity (GO:0019152)
Biological Process:
acetoin catabolic process (GO:0045150)
Date:
2021-10-04
Family Accession:
TIGR02415.1
Method:
HMM
Format
Items per page
Sort by

Send to:

Choose Destination

Supplemental Content

Find related data

Recent activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...
Support Center