The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Cytochrome b5-like heme/steroid binding domain
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 2: Cytochrome b5 type B

There are 2 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Dihydroceramide fatty acyl 2-hydroxylase. [EC: 1.14.18.7]
A dihydroceramide + 2 ferrocytochrome b5 + O(2) + 2 H(+) = a (2'R)- 2'-hydroxydihydroceramide + 2 ferricytochrome b5 + H(2)O.
  • The enzyme, characterized from plants, catalyzes the hydroxylation of carbon 2 of long- or very-long-chain fatty acids attached to sphinganine during de novo ceramide synthesis.
  • The enzyme requires an external cytochrome b5 as the electron donor.
  • The newly introduced 2-hydroxyl group has R-configuration.
  • Cf. EC 1.14.18.6.
81 A0A0L8VJ82 A0A0L8VJ82 A0A0L8VJ82 A0A0L8VJ82 A0A0L8VJ82 A0A0L8VJ82 A0A0L8VJ82 A0A0L8VJ82 A0A0L8VJ82 A6ZMY7
(71 more...)
4-hydroxysphinganine ceramide fatty acyl 2-hydroxylase. [EC: 1.14.18.6]
A phytoceramide + 2 ferrocytochrome b5 + O(2) + 2 H(+) = a (2'R)- 2'-hydroxyphytoceramide + 2 ferricytochrome b5 + H(2)O.
  • The enzyme, characterized from yeast and mammals, catalyzes the hydroxylation of carbon 2 of long- or very-long-chain fatty acids attached to (4R)-4-hydroxysphinganine during de novo ceramide synthesis.
  • The enzymes from yeast and from mammals contain an N-terminal cytochrome b5 domain that acts as the direct electron donor to the desaturase active site.
  • The newly introduced 2-hydroxyl group has R-configuration.
  • Cf. EC 1.14.18.7.
81 A0A0L8VJ82 A0A0L8VJ82 A0A0L8VJ82 A0A0L8VJ82 A0A0L8VJ82 A0A0L8VJ82 A0A0L8VJ82 A0A0L8VJ82 A0A0L8VJ82 A6ZMY7
(71 more...)