View in Gene3D

CATH Superfamily 3.40.50.720

NAD(P)-binding Rossmann-like Domain

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:

"
NAD(P)-binding Rossmann-like 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.
« Back to all FunFams

FunFam 289792: Sulphate adenylate transferase subunit 1

There are 4 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
Sirohydrochlorin ferrochelatase. [EC: 4.99.1.4]
Siroheme + 2 H(+) = sirohydrochlorin + Fe(2+).
  • This enzyme catalyzes the third of three steps leading to the formation of siroheme from uroporphyrinogen III.
  • The first step involves the donation of two S-adenosyl-L-methionine- derived methyl groups to carbons 2 and 7 of uroporphyrinogen III to form precorrin-2 (EC 2.1.1.107) and the second step involves an NAD(+)-dependent dehydrogenation to form sirohydrochlorin from precorrin-2 (EC 1.3.1.76).
  • In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p.
  • In some bacteria, steps 1-3 are catalyzed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirB being responsible for the above reaction.
 44 A0A0A7MGW3 A0A0C1M981 A0A0E0TRS6 A0A0G4C196 A0A0H5QD07 A0A0Y5CTG2 A0A0Y5SYG3 A0A0Y6FGA8 A0A0Y6RVA0 A0A112FAN2
(34 more...)
Uroporphyrinogen-III C-methyltransferase. [EC: 2.1.1.107]
(1) S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L- homocysteine + precorrin-1. (2) S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2.
  • This enzyme catalyzes two sequential methylation reactions, the first forming precorrin-1 and the second leading to the formation of precorrin-2.
  • It is the first of three steps leading to the formation of siroheme from uroporphyrinogen III.
  • The second step involves an NAD(+)-dependent dehydrogenation to form sirohydrochlorin from precorrin-2 (EC 1.3.1.76) and the third step involves the chelation of Fe(2+) to sirohydrochlorin to form siroheme (EC 4.99.1.4).
  • In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p.
  • In some bacteria, steps 1-3 are catalyzed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirA being responsible for the above reaction.
  • Also involved in the biosynthesis of cobalamin.
 43 A0A0A7MGW3 A0A0C1M981 A0A0E0TRS6 A0A0G4C196 A0A0H5QD07 A0A0Y5CTG2 A0A0Y5SYG3 A0A0Y6FGA8 A0A0Y6RVA0 A0A112FAN2
(33 more...)
Precorrin-2 dehydrogenase. [EC: 1.3.1.76]
Precorrin-2 + NAD(+) = sirohydrochlorin + NADH.
  • Catalyzes the second of three steps leading to the formation of siroheme from uroporphyrinogen III.
  • The first step involves the donation of two S-adenosyl-L-methionine- derived methyl groups to carbons 2 and 7 of uroporphyrinogen III to form precorrin-2 (EC 2.1.1.107) and the third step involves the chelation of ferrous iron to sirohydrochlorin to form siroheme (EC 4.99.1.4).
  • In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p.
  • In some bacteria, steps 1-3 are catalyzed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirC being responsible for the above reaction.
 43 A0A0A7MGW3 A0A0C1M981 A0A0E0TRS6 A0A0G4C196 A0A0H5QD07 A0A0Y5CTG2 A0A0Y5SYG3 A0A0Y6FGA8 A0A0Y6RVA0 A0A112FAN2
(33 more...)
Sulfate adenylyltransferase. [EC: 2.7.7.4]
ATP + sulfate = diphosphate + adenylyl sulfate.
  • The human phosphoadenosine-phosphosulfate synthase (PAPS) system is a bifunctional enzyme: ATP sulfurylase, which catalyzes the formation of adenosine 5'-phosphosulfate (APS) from ATP and inorganic sulfate and the second step is catalyzed by the APS kinase portion of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase, which involves the formation of PAPS from enzyme bound APS and ATP.
  • This is in contrast to what is found in bacteria, yeasts, fungi and plants, where the formation of PAPS is carried out by two individual polypeptides, EC 2.7.7.4 and EC 2.7.1.25.
 5 A0A0M3H0H0 A0A1D3E8J2 A0A1D3H2K7 A0A1D3I8I6 B4RLJ4
CATH-Gene3D is a Global Biodata Core Resource Learn more...