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Literature summary extracted from

  • Workun, G.J.; Moquin, K.; Rothery, R.A.; Weiner, J.H.
    Evolutionary persistence of the molybdopyranopterin-containing sulfite oxidase protein fold (2008), Microbiol. Mol. Biol. Rev., 72, 228-48.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.8.3.1
-
 Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
1.8.3.1 A208D SUOX deficiency Homo sapiens
1.8.3.1 G473D SUOX deficiency Homo sapiens
1.8.3.1 additional information SUOX deficiency is typically inherited as a recessive autosomal trait for which there is no known therapy and typically results in death in infancy Homo sapiens
1.8.3.1 R138Q the side chain nitrogen of the Gln appears to be within the coordination sphere of the Mo Gallus gallus
1.8.3.1 R160Q mutation increases the Km for sulfite and decreases the kcat, resulting in a 1000fold decrease in catalytic efficiency. Reveals an increase in coordination number for the Mo, from 5 to 6 Homo sapiens
1.8.3.1 S370Y SUOX deficiency Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.8.3.1 additional information is inactivated in the dark via a process in which a Ser residue (Ser543) in the hinge region connecting the Mo-PPT dimerization domain with the heme b5 domain is phosphorylated, followed by binding of the NIA inhibitor protein Spinacia oleracea

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.8.2.1 periplasm
-
 Starkeya novella
-
-
1.8.3.1 cytoplasm
-
 Deinococcus radiodurans 5737
-
1.8.3.1 periplasm
-
 Thermus thermophilus
-
-
1.8.3.1 periplasm
-
 Escherichia coli
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.8.2.1 Mo Mo-PPT binding catalytic subunit (SorA) comprised of an SUOX fold and a dimerization domain Starkeya novella
1.8.3.1 Mo
-
 Homo sapiens
1.8.3.1 Mo
-
 Spinacia oleracea
1.8.3.1 Mo
-
 Chlorella vulgaris
1.8.3.1 Mo
-
 Gallus gallus
1.8.3.1 Mo the organism is comprised of only the Mo-PPT binding SUOX fold itself Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.8.2.1 Starkeya novella
-
-
-
1.8.3.1 Arabidopsis thaliana Q9S850
-
-
1.8.3.1 Bacillus licheniformis
-
-
-
1.8.3.1 Bacillus sp. (in: Bacteria)
-
-
-
1.8.3.1 Bacillus sp. (in: Bacteria) NRRL B-14911
-
-
-
1.8.3.1 Chlorella vulgaris
-
-
-
1.8.3.1 Deinococcus radiodurans
-
-
-
1.8.3.1 Erythrobacter litoralis
-
-
-
1.8.3.1 Escherichia coli
-
-
-
1.8.3.1 Gallus gallus P07850
-
-
1.8.3.1 Homo sapiens
-
-
-
1.8.3.1 Maribacter sp. HTCC2170
-
-
-
1.8.3.1 Ogataea angusta
-
-
-
1.8.3.1 Paenarthrobacter aurescens
-
-
-
1.8.3.1 Rhizorhabdus wittichii RW1 A5V4U9
-
-
1.8.3.1 Roseovarius nubinhibens
-
-
-
1.8.3.1 Rubrobacter xylanophilus
-
-
-
1.8.3.1 Saccharopolyspora erythraea
-
-
-
1.8.3.1 Spinacia oleracea
-
-
-
1.8.3.1 Streptomyces ambofaciens
-
-
-
1.8.3.1 Thermus thermophilus
-
-
-
1.8.3.1 Zea mays
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.8.3.1 liver
-
 Gallus gallus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.2.1 sulfite + H2O + acceptor
-
 Starkeya novella sulfate + reduced acceptor + 2 H+
-
 ?
1.8.3.1 additional information R138, R190, and R450 contribute to a positively charged binding pocket, which stabilizes substrate/product binding Gallus gallus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.8.2.1 heterodimer
-
 Starkeya novella
1.8.3.1 pentamer crystallography Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
1.8.2.1 SorAB
-
 Starkeya novella
1.8.2.1 sulfite dehydrogenase
-
 Starkeya novella
1.8.3.1 NIA
-
 Spinacia oleracea
1.8.3.1 NIA
-
 Zea mays
1.8.3.1 NIA
-
 Ogataea angusta
1.8.3.1 NIA
-
 Chlorella vulgaris
1.8.3.1 sulfite oxidase
-
 Thermus thermophilus
1.8.3.1 sulfite oxidase
-
 Escherichia coli
1.8.3.1 sulfite oxidase
-
 Homo sapiens
1.8.3.1 sulfite oxidase
-
 Spinacia oleracea
1.8.3.1 sulfite oxidase
-
 Zea mays
1.8.3.1 sulfite oxidase
-
 Ogataea angusta
1.8.3.1 sulfite oxidase
-
 Bacillus sp. (in: Bacteria)
1.8.3.1 sulfite oxidase
-
 Bacillus licheniformis
1.8.3.1 sulfite oxidase
-
 Chlorella vulgaris
1.8.3.1 sulfite oxidase
-
 Saccharopolyspora erythraea
1.8.3.1 sulfite oxidase
-
 Paenarthrobacter aurescens
1.8.3.1 sulfite oxidase
-
 Deinococcus radiodurans
1.8.3.1 sulfite oxidase
-
 Arabidopsis thaliana
1.8.3.1 sulfite oxidase
-
 Streptomyces ambofaciens
1.8.3.1 sulfite oxidase
-
 Erythrobacter litoralis
1.8.3.1 sulfite oxidase
-
 Rubrobacter xylanophilus
1.8.3.1 sulfite oxidase
-
 Rhizorhabdus wittichii RW1
1.8.3.1 sulfite oxidase
-
 Maribacter sp. HTCC2170
1.8.3.1 sulfite oxidase
-
 Roseovarius nubinhibens
1.8.3.1 sulfite oxidase
-
 Gallus gallus
1.8.3.1 SUOX
-
 Thermus thermophilus
1.8.3.1 SUOX
-
 Escherichia coli
1.8.3.1 SUOX
-
 Homo sapiens
1.8.3.1 SUOX
-
 Spinacia oleracea
1.8.3.1 SUOX
-
 Zea mays
1.8.3.1 SUOX
-
 Ogataea angusta
1.8.3.1 SUOX
-
 Bacillus sp. (in: Bacteria)
1.8.3.1 SUOX
-
 Bacillus licheniformis
1.8.3.1 SUOX
-
 Chlorella vulgaris
1.8.3.1 SUOX
-
 Saccharopolyspora erythraea
1.8.3.1 SUOX
-
 Paenarthrobacter aurescens
1.8.3.1 SUOX
-
 Deinococcus radiodurans
1.8.3.1 SUOX
-
 Arabidopsis thaliana
1.8.3.1 SUOX
-
 Streptomyces ambofaciens
1.8.3.1 SUOX
-
 Erythrobacter litoralis
1.8.3.1 SUOX
-
 Rubrobacter xylanophilus
1.8.3.1 SUOX
-
 Rhizorhabdus wittichii RW1
1.8.3.1 SUOX
-
 Maribacter sp. HTCC2170
1.8.3.1 SUOX
-
 Roseovarius nubinhibens
1.8.3.1 SUOX
-
 Gallus gallus
1.8.3.1 YedY
-
 Escherichia coli