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CATH Superfamily 3.40.50.1980

Nitrogenase molybdenum iron protein 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:

"
Nitrogenase molybdenum iron protein 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 29180: Chlorophyllide reductase subunit Z

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
Chlorophyllide a reductase. [EC: 1.3.7.15]
(1) 3-deacetyl-3-vinylbacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate = chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H(2)O + 2 H(+). (2) Bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate = 3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H(2)O + 2 H(+). (3) 3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate = 3-devinyl-3- (1-hydroxyethyl)chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H(2)O + 2 H(+).
  • The enzyme, together with EC 1.1.1.396 and EC 4.2.1.165, is involved in the conversion of chlorophyllide a to bacteriochlorophyllide a.
  • These enzymes can act in multiple orders, resulting in the formation of different intermediates, but the final product of the cumulative action of the three enzymes is always bacteriochlorophyllide a.
  • This enzyme catalyzes a trans-reduction of the B-ring; the product has the (7R,8R)-configuration.
  • In addition, the enzyme has a latent activity of EC 1.3.7.13.
  • Formerly EC 1.3.99.35.
 4 P26277 Q3J1A0 Q9JPB9 Q9KWI8
Ferredoxin:protochlorophyllide reductase (ATP-dependent). [EC: 1.3.7.7]
Protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H(2)O = chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate.
  • Occurs in photosynthetic bacteria, cyanobacteria, green algae and gymnosperms.
  • The enzyme catalyzes trans-reduction of the D-ring of protochlorophyllide; the product has the (7S,8S)-configuration.
  • Unlike EC 1.3.1.33 light is not required.
  • The enzyme contains a [4Fe-4S] cluster, and structurally resembles the Fe protein/MoFe protein complex of EC 1.18.6.1, which catalyzes an ATP-driven reduction.
 3 A0A0B8ZCT1 A0A0D1EGD6 A0A177HCT1
Protochlorophyllide reductase. [EC: 1.3.1.33]
Chlorophyllide a + NADP(+) = protochlorophyllide + NADPH.
  • Catalyzes a light-dependent trans-reduction of the D-ring of protochlorophyllide; the product has the (7S,8S)-configuration.
 3 A0A0D6B8I8 A8LQ12 Q58PR4