Protein Family Models

This domain is Psb31, an extrinsic protein found in photosystem II (PSII) present in Chaetoceros gracilis. Photosystem II (PSII) is a multisubunit, membrane protein complex located in the thylakoid membranes of oxygenic photosynthetic organisms from cyanobacteria to higher plants. The four helices in the N-terminal domain are arranged in an up-down-up-down fold and are similar in structure to PsbQ protein in Spinach, despite low sequence homology [1]. [1]. 23988112. Crystal structure of Psb31, a novel extrinsic protein of. photosystem II from a marine centric diatom and implications for. its binding and function.. Nagao R, Suga M, Niikura A, Okumura A, Koua FH, Suzuki T, Tomo. T, Enami I, Shen JR;. Biochemistry. 2013;52:6646-6652. (from Pfam)

Date:

2024-08-14

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:

2024-08-14

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)

Date:

2024-08-14

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:

2024-08-14