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CATH Superfamily 1.10.1060.10

Alpha-helical ferredoxin

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Alpha-helical ferredoxin
".

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 10341: Heterodisulfide reductase subunit C

There are 3 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
Glycerol-3-phosphate dehydrogenase. [EC: 1.1.5.3]
sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol.
  • An essential membrane enzyme, functioning at the central junction of glycolysis, respiration and phospholipid biosynthesis.
  • In bacteria, the enzyme is localized to the cytoplasmic membrane, while in eukaryotes it is tightly bound to the outer surface of the inner mitochondrial membrane.
  • In eukaryotes, this enzyme, together with the cytosolic enzyme EC 1.1.1.8 forms the glycerol-3-phosphate shuttle by which NADH produced in the cytosol, primarily from glycolysis, can be reoxidized to NAD(+) by the mitochondrial electron-transport chain.
  • This shuttle plays a critical role in transferring reducing equivalents from cytosolic NADH into the mitochondrial matrix.
  • Insect flight muscle uses only CoQ(10) as the physiological quinone whereas hamster and rat mitochondria use mainly CoQ(9).
  • The enzyme is activated by calcium.
  • Formerly EC 1.1.2.1 and EC 1.1.99.5.
 376 A0A017IGU3 A0A023Z0W1 A0A024KX15 A0A025CEG8 A0A026RGU3 A0A026UKR0 A0A027U775 A0A028AQW1 A0A028E6F4 A0A029HTQ3
(366 more...)
Transferred entry: 1.1.5.3. [EC: 1.1.99.5]
    		111 A0A026RGU3 A0A026UKR0 A0A027U775 A0A028AQW1 A0A028E6F4 A0A029HTQ3 A0A029IPH4 A0A064TMK2 A0A066RG69 A0A070CQI4
    (101 more...)
    CoB--CoM heterodisulfide reductase. [EC: 1.8.98.1]
    Coenzyme B + coenzyme M + methanophenazine = N-(7-((2-sulfoethyl)dithio)heptanoyl)-O(3)-phospho-L-threonine + dihydromethanophenazine.
    • Found in methanogenic archaea, particularly Methanosarcina species, and regenerates coenzyme M and coenzyme B after the action of EC 2.8.4.1.
    • Highly specific for both coenzyme M and coenzyme B.
    • Reacts with various phenazine derivatives, including 2-hydroxyphenazine and 2-bromophenazine.
    • Formerly EC 1.12.99.2.
    		 31 A0A089ZUU9 A0A090I1I9 A0A0E3KUN9 A0A0E3KZM2 A0A0E3LKJ2 A0A0E3LTH2 A0A0E3PUR2 A0A0E3QZ19 A0A0E3R4W3 A0A0E3RRF3
    (21 more...)
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