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CATH Superfamily 3.30.413.10

Sulfite Reductase Hemoprotein, domain 1

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:

"
Sulfite Reductase Hemoprotein, domain 1
".

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 4974: Sulfite reductase beta subunit

There are 6 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
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.
 2388 A0A010Q8C5 A0A014NMB8 A0A017I961 A0A022PMB9 A0A022T0S5 A0A023E3A4 A0A023NQ29 A0A023RH07 A0A023V202 A0A023VU52
(2378 more...)
Assimilatory sulfite reductase (ferredoxin). [EC: 1.8.7.1]
Hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H(2)O = sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H(+).
  • The enzyme participates in sulfate assimilation.
  • While it is usually found in cyanobacteria, plants and algae, it has also been reported in bacteria (cf. EC 1.8.1.2).
  • Formerly EC 1.8.99.1.
 152 A0A068MW51 A0A073CEC8 A0A086CGQ5 A0A089P3V0 A0A089PDR2 A0A0A1W167 A0A0A1ZHP0 A0A0A1ZV40 A0A0A2A630 A0A0A2A964
(142 more...)
Deleted entry. [EC: 1.8.99.1]
    		2 F9XKI4 M9T6Y7
    Ferredoxin--nitrite reductase. [EC: 1.7.7.1]
    NH(3) + 2 H(2)O + 6 oxidized ferredoxin = nitrite + 6 reduced ferredoxin + 7 H(+).
      		 1 A3LW26
      Nitrite reductase (NO-forming). [EC: 1.7.2.1]
      Nitric oxide + H(2)O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H(+).
      • The reaction is catalyzed by two types of enzymes, found in the perimplasm of denitrifying bacteria.
      • One type comprises proteins containing multiple copper centers, the other a heme protein, cytochrome cd1.
      • Acceptors include c-type cytochromes such as cytochrome c-550 or cytochrome c-551 from Paracoccus denitrificans or Pseudomonas aeruginosa, and small blue copper proteins such as azurin and pseudoazurin.
      • Cytochrome cd1 also has oxidase and hydroxylamine reductase activities.
      • May also catalyze the reaction of EC 1.7.99.1 since this is a well- known activity of cytochrome cd1.
      • Formerly EC 1.6.6.5, EC 1.7.99.3 and EC 1.9.3.2.
      		 1 Q17UY6
      Phosphoadenylyl-sulfate reductase (thioredoxin). [EC: 1.8.4.8]
      Adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin.
      • Specific for PAPS.
      • The enzyme from Escherichia coli will use thioredoxins from other species.
      • Formerly EC 1.8.99.4.
      		 1 A0A090P9B2
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