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:

"
HUPs
".

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 88968: Probable phosphoadenosine phosphosulfate reductase

There are 11 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
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.
13610 A0A009ET45 A0A009ET45 A0A009H948 A0A009H948 A0A009HH60 A0A009HH60 A0A009HUQ1 A0A009HUQ1 A0A009I3E7 A0A009I3E7
(13600 more...)
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.
11436 A0A009FTL0 A0A009FTL0 A0A009GZ45 A0A009GZ45 A0A009HHU4 A0A009HHU4 A0A009IAQ8 A0A009IAQ8 A0A009IV93 A0A009IV93
(11426 more...)
Adenylyl-sulfate reductase (thioredoxin). [EC: 1.8.4.10]
AMP + sulfite + thioredoxin disulfide = 5'-adenylyl sulfate + thioredoxin.
  • Uses adenylyl sulfate, not phosphoadenylyl sulfate, distinguishing this enzyme from EC 1.8.4.8.
  • Uses thioredoxin as electron donor, not glutathione or other donors, distinguishing it from EC 1.8.4.9 and EC 1.8.99.2.
586 A0A009GZ45 A0A009GZ45 A0A009IV93 A0A009IV93 A0A009JMK3 A0A009JMK3 A0A009SF29 A0A009SF29 A0A022T0S9 A0A022T0S9
(576 more...)
Adenylyl-sulfate reductase (glutathione). [EC: 1.8.4.9]
AMP + sulfite + glutathione disulfide = adenylyl sulfate + 2 glutathione.
  • Differs from EC 1.8.99.2, in using glutathione as the reductant.
  • Glutathione can be replaced by gamma-glutamylcysteine or dithiothreitol, but not by thioredoxin, glutaredoxin or mercaptoethanol.
  • The enzyme from Arabidopsis thaliana contains a glutaredoxin-like domain.
  • Also found in other photosynthetic eukaryotes, e.g., the Madagascar periwinkle, Catharanthus roseus and the hollow green seaweed, Enteromorpha intestinalis.
78 A0A0A7Q1B3 A0A0A7Q1B3 A0A0B2RLU1 A0A0B2RLU1 A0A0B2RTN8 A0A0B2RTN8 A0A0B2S9D3 A0A0B2S9D3 A0A0U2X312 A0A0U2X312
(68 more...)
Adenylyl-sulfate reductase. [EC: 1.8.99.2]
AMP + sulfite + acceptor = adenylyl sulfate + reduced acceptor.
  • Methyl viologen can act as acceptor.
32 A0A098FNW4 A0A098FNW4 A0A0I9SJD7 A0A0I9SJD7 A0A1D5UXB2 A0A1D5UXB2 A0A1G3D399 A0A1G3D399 A0A1L6KKK6 A0A1L6KKK6
(22 more...)
H(+)-transporting two-sector ATPase. [EC: 3.6.3.14]
ATP + H(2)O + H(+)(In) = ADP + phosphate + H(+)(Out).
  • A multisubunit non-phosphorylated ATPase that is involved in the transport of ions.
  • Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)).
  • The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases.
  • All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits.
  • Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis.
  • This movement is driven by the H(+) electrochemical potential gradient.
  • The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP.
  • Formerly EC 3.6.1.34.
4 A0A077XYH6 A0A077XYH6 F0IEZ8 F0IEZ8
Adenylyl-sulfate kinase. [EC: 2.7.1.25]
ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl 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.
4 A7HAV0 A7HAV0 Q01NE3 Q01NE3
Transferred entry: 1.8.4.8. [EC: 1.8.99.4]
    2 Q82W42 Q82W42
    Ferredoxin--nitrite reductase. [EC: 1.7.7.1]
    NH(3) + 2 H(2)O + 6 oxidized ferredoxin = nitrite + 6 reduced ferredoxin + 7 H(+).
      2 A0A1J0LIU1 A0A1J0LIU1
      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.
      2 A0A1N5KMF7 A0A1N5KMF7
      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.
      2 A0A090P9B2 A0A090P9B2