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CATH Superfamily 3.40.50.360

Flavodoxin 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: waiting to be named.

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 16321: Short-chain flavodoxin YkuP

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
Nitrogenase (flavodoxin). [EC: 1.19.6.1]
4 reduced flavodoxin + N(2) + 16 ATP + 16 H(2)O = 4 oxidized flavodoxin + H(2) + 2 NH(3) + 16 ADP + 16 phosphate.
  • Composed of two components, dinitrogen reductase and dinitrogenase, that can be separated but are both required for nitrogenase activity.
  • Dinitrogen reductase is a [4Fe-4S] protein, which, at the expense of ATP, transfers electrons from a dedicated flavodoxin to dinitrogenase.
  • Dinitrogenase is a protein complex that contains either a molybdenum- iron cofactor, a vanadium-iron cofactor, or an iron-iron cofactor, that reduces dinitrogen in three succesive two-electron reductions from nitrogen to diimine to hydrazine to two molecules of ammonia.
  • The reduction is initiated by formation of hydrogen.
  • The enzyme can also reduce acetylene to ethylene (but only very slowly to ethane), azide to nitrogen and ammonia, and cyanide to methane and ammonia.
  • In the absence of a suitable substrate, hydrogen is slowly formed.
  • Some enzymes utilize ferredoxin rather than flavodoxin as the electron donor (see EC 1.18.6.1).
  • Formerly EC 1.19.2.1.
 212 A0A023P2B5 A0A023P2B5 A0A061BM22 A0A061BM22 A0A089XGR9 A0A089XGR9 A0A0A3VYT8 A0A0A3VYT8 A0A0B5X571 A0A0B5X571
(202 more...)
Assimilatory sulfite reductase (NADPH). [EC: 1.8.1.2]
H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3 NADPH.
  • The enzyme, which catalyzes the six-electron reduction of sulfite to sulfide, is involved in sulfate assimilation in bacteria and yeast.
  • Different from EC 1.8.99.5, which is involved in prokaryotic sulfur- based energy metabolism.
  • Formerly EC 1.8.99.1.
 100 A0A059MW55 A0A059MW55 A0A0E9DYR3 A0A0E9DYR3 A0A0H1UK25 A0A0H1UK25 A0A0M1ZEF2 A0A0M1ZEF2 A0A0M2AA39 A0A0M2AA39
(90 more...)
Propionyl-CoA carboxylase. [EC: 6.4.1.3]
ATP + propanoyl-CoA + HCO(3)(-) = ADP + phosphate + (S)-methylmalonyl- CoA.
  • Also carboxylates butanoyl-CoA and catalyzes transcarboxylation.
 6 A0A081RML2 A0A081RML2 A0A087RPL0 A0A087RPL0 A0A087RT02 A0A087RT02
Cob(II)yrinic acid a,c-diamide reductase. [EC: 1.16.8.1]
2 cob(I)yrinic acid a,c-diamide + FMN + 2 H(+) = 2 cob(II)yrinic acid a,c-diamide + FMNH(2).
  • This enzyme also catalyzes the reduction of cob(II)yric acid, cob(II)inamide, cob(II)inamide phosphate, GDP-cob(II)inamide and cob(II)alamin although cob(II)yrinic acid a,c-diamide is thought to be the physiological substrate.
  • Also uses FAD and NADH but not NADPH.
 2 A0A0A8HTT8 A0A0A8HTT8
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