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: 12

1.

Trans-2-enoyl-CoA reductase catalytic region

This family of trans-2-enoyl-CoA reductases, EC:1.3.1.44, carries the the catalytic sites of the enzyme, characterised by the conserved sequence motifs: YNThhhFxK, and YShAPxR. In Euglena where the enzyme has been characterised it catalyses the reduction of enoyl-CoA to acyl-CoA in an unusual fatty acid pathway in mitochondria. the whole path performs a malonyl-CoA independent synthesis of fatty acids leading to accumulation of wax esters, which serve as the sink for electrons stemming from glycolytic ATP synthesis and pyruvate oxidation. [1]. 15569691. Mitochondrial trans-2-enoyl-CoA reductase of wax ester fermentation from Euglena gracilis defines a new family of enzymes involved in lipid synthesis. Hoffmeister M, Piotrowski M, Nowitzki U, Martin W;. J Biol Chem. 2005;280:4329-4338. (from Pfam)

Date:
2024-10-16
Family Accession:
NF023662.5
Method:
HMM
2.

NAD(P)H binding domain of trans-2-enoyl-CoA reductase

This family carries the region of the enzyme trans-2-enoyl-CoA reductase, EC:1.3.1.44, which binds NAD(P)H. The activity of the enzyme was characterised in Euglena where an unusual fatty acid synthesis path-way in the mitochondria performs a malonyl-CoA independent synthesis of fatty acids leading to accumulation of wax esters, which serve as the sink for electrons stemming from glycolytic ATP synthesis and pyruvate oxidation. The full enzyme catalyses the reduction of enoyl-CoA to acyl-CoA. The binding site is conserved as GA/CSpGYG, where p is any polar residue [1]. [1]. 15569691. Mitochondrial trans-2-enoyl-CoA reductase of wax ester fermentation from Euglena gracilis defines a new family of enzymes involved in lipid synthesis. Hoffmeister M, Piotrowski M, Nowitzki U, Martin W;. J Biol Chem. 2005;280:4329-4338. (from Pfam)

GO Terms:
Molecular Function:
oxidoreductase activity (GO:0016491)
Date:
2024-10-16
Family Accession:
NF023663.5
Method:
HMM
3.

Enoyl reductase FAD binding domain

This family carries the region of the enzyme trans-2-enoyl-CoA reductase, at the very C-terminus, that binds to FAD. The activity was characterised in Euglena where an unusual fatty acid synthesis path-way in mitochondria performs a malonyl-CoA independent synthesis of fatty acids leading to accumulation of wax esters, which serve as the sink for electrons stemming from glycolytic ATP synthesis and pyruvate oxidation. The full enzyme catalyses the reduction of enoyl-CoA to acyl-CoA. The conserved region is seen as the motif FGFxxxxxDY [1]. [1]. 15569691. Mitochondrial trans-2-enoyl-CoA reductase of wax ester fermentation from Euglena gracilis defines a new family of enzymes involved in lipid synthesis. Hoffmeister M, Piotrowski M, Nowitzki U, Martin W;. J Biol Chem. 2005;280:4329-4338. (from Pfam)

Date:
2024-10-16
Family Accession:
NF018724.5
Method:
HMM
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.

enoyl-ACP reductase FabV

Gene:
fabV
GO Terms:
Molecular Function:
enoyl-[acyl-carrier-protein] reductase (NADH) activity (GO:0004318)
Biological Process:
fatty acid biosynthetic process (GO:0006633)
Date:
2023-10-21
Family Accession:
NF043048.1
Method:
HMM
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.

trans-2-enoyl-CoA reductase family protein

trans-2-enoyl-CoA reductase (TER) family protein such as enoyl-[acyl-carrier-protein] reductase FabV and trans-2-enoyl-CoA reductase, which are both involved in fatty acid synthesis

Date:
2018-05-16
Family Accession:
11486784
Method:
Sparcle
12.

enoyl-[acyl-carrier-protein] reductase FabV

FabV is one of several classes of enoyl-[acyl-carrier-protein] reductase that are only very distantly related to each other. Other classes include FabI (as in E. coli K-12), FabK, and FabL.

Gene:
fabV
Date:
2020-10-26
Family Accession:
NF010177.0
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