The 3'-phosphoadenosine 5'-phosphosulfate (PAPS) reductase called also PAPS sulfotransferase catalyses the reduction of activated sulfate into sulfite; The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP); Belongs to the PAPS reductase family; Localized in the cytoplasm; High confidence in function and specificity.

Oxidoreductase that contains in its C-terminal, a flavodoxin-like domain with a flavin mononucleotide (FMN)-binding site and a NAD-binding domain. In its N-terminal part there are four transmembrane segemnts; Belongs to the Flavoprotein pyridine nucleotide cytochrome reductase family; Localized in the cytoplasmic membrane; Specificity unclear.

O-succinylhomoserine sulfhydrylase; Catalyzes the formation of L-homocysteine from O-succinyl-L- homoserine (OSHS) and hydrogen sulfide.

Sulfide:quinone oxidoreductase; Enzyme that uses electrons from H2S to reduce quinones with the use of NADP. S0 is oxidized to sulfite and water. This process confers resistance to heavy metals such as cadmium and cisplatin; Binds 1 FAD noncovalently as cofactors; Belongs to the Pyridine nucleotide- disulphide oxidoreductase family; Localized in the cytoplasm; High confidence in function and specificity.

Oxidoreductase that uses the FAD and NADH as coenzyme; Belongs to the pyridine nucleotide-disulphide oxidoreductase superfamily; Localized in the cytoplasm; Specificity unclear.

Sulfite reductase catalyses the six-electron reduction reactions of sulfite to sulfide; Contains a Fe(4)S(4) cluster coupled to a siroheme through a cysteine bridge; Would contains a C-terminal HEPN domain of unknown function; Belongs to the nitrite and sulfite reductase 4Fe-4S domain family; Localized in the cytoplasm; High confidence in function and specificity.

Sulfate adenylyltransferase subunit 1; May be the GTPase, regulating ATP sulfurylase activity. Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. CysN/NodQ subfamily.

The transcriptional regulators with the Rrf2-type HTH domain control a variety of operons that encode iron-sulfur-containing proteins as well as other proteins involved in electron transport. Other rrf2-type HTH proteins are repressors of genes involved in nitrite or iron metabolism. The C-terminal part of the rrf2-type HTH domain contains 3 conserved cysteine residues that may bind an Fe-S cluster. Contains a DNA-binding, winged helix-turn-helix (wHTH) domain. Localized in the cytoplasm; Family membership.

Uroporphyrin-III C-methyltransferase; This enzyme catalyzes two sequential methylation reactions, forming precorrin-1 and precorrin-2 by methylations at C-2 and C-7 of uroporphyrinogen III respectively; It is the first enzyme specific to the cobalamin (vitamin B12) pathway and precorrin-2 is a common intermediate in the biosynthesis of corrinoids such as vitamin B12, siroheme and coenzyme F430; Belongs to the precorrin methyltransferase family; Localized in the cytoplasm; High confidence in function and specificity.