View in Gene3D

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.
« Back to all FunFams

FunFam 10323: Selenate reductase subunit YgfK

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
Glutamate synthase (NADPH). [EC: 1.4.1.13]
2 L-glutamate + NADP(+) = L-glutamine + 2-oxoglutarate + NADPH.
  • The reaction takes place in the opposite direction.
  • The protein is composed of two subunits, alpha and beta.
  • The alpha subunit is composed of two domains, one hydrolyzing L-glutamine to NH(3) and L-glutamate (cf. EC 3.5.1.2), the other combining the produced NH(3) with 2-oxoglutarate to produce a second molecule of L-glutamate (cf. EC 1.4.1.4).
  • The beta subunit transfers electrons to the cosubstrate.
  • The NH(3) is channeled through a 31 A channel in the active protein.
  • In the absence of the beta subunit, coupling between the two domains of the alpha subunit is compromised and some ammonium can be produced.
  • In the intact alpha-beta complex, ammonia production only takes place as part of the overall reaction.
  • Formerly EC 2.6.1.53.
 63 A0A028E720 A0A070SSR0 A0A084A6U8 A0A0A0FIB8 A0A0A8UD16 A0A0D7HA17 A0A0E0U3B4 A0A0E1M5I5 A0A0F6C8K5 A0A0F6FBS4
(53 more...)
Selenate reductase. [EC: 1.97.1.9]
Selenite + H(2)O + acceptor = selenate + reduced acceptor.
  • The periplasmic enzyme from Thauera selenatis is a complex comprising three heterologous subunits (alpha, beta and gamma).
  • Nitrate, nitrite, chlorate and sulfate are not substrates.
  • A number of compounds, including acetate, lactate, pyruvate, and certain sugars, amino acids, fatty acids, di- and tricarboxylic acids, and benzoate can serve as electron donors.
 15 A0A070SSR0 A0A0E1M5I5 A0A0M9J8B3 A0A142V168 A0A1C6Z664 A0A1J0HEX2 D8AK90 D8AXC4 D8C1D8 E1HHE8
(5 more...)
Dihydrouracil dehydrogenase (NAD(+)). [EC: 1.3.1.1]
(1) 5,6-dihydrouracil + NAD(+) = uracil + NADH. (2) 5,6-dihydrothymine + NAD(+) = thymine + NADH.
  • The enzyme was originally discovered in the uracil-fermenting bacterium, Clostridium uracilicum, which utilizes uracil and thymine as nitrogen and carbon sources for growth.
  • Since then the enzyme was found in additional organisms including Alcaligenes eutrophus, Pseudomonas strains and Escherichia coli.
 2 A0A0I2Z2R5 W7PNF5
CATH-Gene3D is a Global Biodata Core Resource Learn more...