Integral membrane Acyl-coA desaturase superfamily

Families in this clan are integral membrane di-iron-containing enzymes that share the same fold consisting of four transmembrane helices (TM1-TM4) that anchor them to the endoplasmic reticulum (ER) membrane, capped by a cytosolic domain containing a unique 9-10 histidine-coordinating dimetal (di-iron) catalytic centre. This fold is found in fatty acid hydroxylases and fatty acid desaturases, which hydroxylate or desaturate lipid-based substrates in a NADH and oxygen-dependent reaction [1,2,3]. The structure of mouse stearoyl-CoA desaturase (SDC) revealed that TM2 and TM4 are longer than TM1 and TM3 and protrude into the cytosolic domain, providing three of the nine histidine residues that coordinate the two metal ions, while the other histidine residues are provided by the soluble domain in this enzyme [4].

This clan contains 3 families and the total number of domains in the clan is 51009. The clan was built by S;0000-0002-0520-0736 Chuguransky.

Literature references

1. Zhu G, Koszelak-Rosenblum M, Connelly SM, Dumont ME, Malkowski MG;, J Biol Chem. 2015;290:29820-29833.: The Crystal Structure of an Integral Membrane Fatty Acid alpha-Hydroxylase. PUBMED:26515067 EPMC:26515067
2. Wang H, Klein MG, Zou H, Lane W, Snell G, Levin I, Li K, Sang BC;, Nat Struct Mol Biol. 2015;22:581-585.: Crystal structure of human stearoyl-coenzyme A desaturase in complex with substrate. PUBMED:26098317 EPMC:26098317
3. Bai Y, McCoy JG, Levin EJ, Sobrado P, Rajashankar KR, Fox BG, Zhou M;, Nature. 2015;524:252-256.: X-ray structure of a mammalian stearoyl-CoA desaturase. PUBMED:26098370 EPMC:26098370
4. Shen J, Wu G, Tsai AL, Zhou M;, J Mol Biol. 2020;432:5152-5161.: Structure and Mechanism of a Unique Diiron Center in Mammalian Stearoyl-CoA Desaturase. PUBMED:32470559 EPMC:32470559

Members

This clan contains the following 3 member families:

Below is a listing of the unique domain organisations or architectures from this clan. More...

The table below shows the number of occurrences of each domain throughout the sequence database. More...

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This diagram shows the relationships between members of this clan. More...

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD group, to allow us to map Pfam domains onto UniProt three-dimensional structures. The table below shows the mapping between the Pfam families in this clan, the corresponding UniProt entries, and the region of the three-dimensional structures that are available for that sequence.