| TCID | Name | Domain | Kingdom/Phylum | Protein(s) |
|---|---|---|---|---|
|
5.A.3.1.1 | Anaerobic, respiratory, membrane-bound nitrate reductase, NarGHI. Two protons are consumed in the cytoplasm while two protons are released in the periplasm, contributing to the pmf (Simon et al., 2008). | Bacteria |
Pseudomonadota | NarGHI of E. coli NarG (α) NarH (β) NarI (γ) |
|
5.A.3.1.2 | Anaerobic, respiratory, membrane-bound nitrate reductase, NarZYV (Blasco et al., 1990) | Bacteria |
Pseudomonadota | NarZYV of E. coli NarZ(α) P19319 NarY(β) P19318 NarV(γ) P19316 |
|
5.A.3.2.1 | Anaerobic, respiratory, membrane-bound formate dehydrogenase, FdnGHI. Two protons are consumed in the cytoplasm while two protons are released in the periplasm, contributing to the pmf (Simon et al., 2008). | Bacteria |
Pseudomonadota | FdnGHI of E. coli FdnG (α) FdnH (β) FdnI (γ) |
|
5.A.3.3.1 | Anaerobic dimethylsulfoxide (DMSO) reductase, (YnfEFGH) (Weiner et al., 1992; Lubitz and Weiner, 2003) | Bacteria |
Pseudomonadota | YnfEFGH of E. coli YnfE(α or A chain) (reductase) (P77374) YnfF (α or A chain) (reductase) (P77783) YnfG (β or B chain) (electron transfer protein) (P0AAJ1) YnfH (γ or C chain) (membrane anchor protein) (P76173) |
|
5.A.3.3.2 | Anaerobic dimethyl sulfoxide (DMSO) reductase, DmsABC (Lubitz and Weiner, 2003) | Bacteria |
Pseudomonadota | DmsABC of E. coli DmsA(α) P18775 DmsB(β) P18776 DmsC(γ) P18777 |
|
5.A.3.3.3 | Anaerobic dimethylsulfoxide (DMSO)/trimethylamine-N-oxide (TMAO) reductase (Müller and DasSarma, 2005) | Archaea |
Euryarchaeota | DmsABCE of Halobacterium sp. strain NRC-1 DmsA (α) (AAG19284) DmsC (β) (AAG19286) DmsB (γ1) (AAG19285) DmsE (γ2 (AAG19283) |
|
5.A.3.4.1 | Anaerobic trimethylamine-N-oxide (TMAO) reductase 1, TorAC (Mejean et al., 1994) | Bacteria |
Pseudomonadota | TorAC of E. coli TorA (α) (precursor 1) (P33225) TorC (cytochrome c-type protein) (P33226) |
|
5.A.3.4.2 | Periplasmic anaerobic trimethylamine-N-oxide reductase 2, TorYZ (also called YecK/BisZ) (Gon et al. 2000). It also reduces biotin sulfoxide and other N- and S-oxides, but less efficiency that TMAO. | Bacteria |
Pseudomonadota | TorYZ of E. coli TorY (cytochrome c-type protein) (P52005) TorZ (α) (P58362) |
|
5.A.3.4.3 | Biotin d-sulfoxide reductase, BisC (requires a small thioredoxin-like protein) (Pierson and Campbell, 1990) | Bacteria |
Pseudomonadota | BisC of E. coli BisC (α) (P20099) |
|
5.A.3.4.4 | Periplasmic anaerobic methionine oxide reductase 2, TorYZ (also called MtsZ/BisC), both with an N-terminal TMS. It supports survival of Haemophilus influenzae in an in vivo model of infection (Dhouib et al. 2016). It is an S- and N-oxide reductase with a stereospecificity for S-sulfoxides. The enzyme converts two physiologically relevant sulfoxides, biotin sulfoxide (BSO) and methionine sulfoxide (MetSO), with the kinetic parameters suggesting that MetSO is the natural substrate of this enzyme (Dhouib et al. 2016). | Bacteria |
Pseudomonadota | TorYZ of Haemophilus influenzae |
|
5.A.3.5.1 | Thiosulfate reductase, PhsABC (Heinzinger et al., 1995) (Clark and Barrett 1987). Menaquinone is the sole electron donor. The endoergonic reduction reaction is driven by the pmf by a reverse loop mechanism (Stoffels et al. 2012). The enzyme can catalyze oxidation of sulfide to sulfite and sulfite to thiosulfate in an exergonic reaction that is pmf-independent (Stoffels et al. 2012). Because the endoergonic reaction is dependent on the pmf, there may be a proton channels in the complex, (possibly subunit C) that allows proton flux into the cell, coupled to the reduction reaction. | Bacteria |
Pseudomonadota | PhsABC of Salmonella typhimurium PhsA (α) (molybdopterin subunit; 758 aas and 1 - 3 TMSs) (P37600) PhsB (β) (cytochrome b reductase; 192 aas) (P0A1I1) PhsC (γ) (cytochrome b subunit; 254 aas and 5 TMSs in a 1 + 2 + 2 TMS arrangement) (P37602) |
|
5.A.3.5.2 | Polysulfide reductase, PsrABC | Bacteria |
Campylobacterota | PsrABC of Wolinella succinogenes PsrA (α or chain A) (P31075) PsrB (β or chain B) (P31076) PsrC (γ or chain C) (P31077) |
|
5.A.3.5.3 | Nitrite reductase complex, NrfABCD with subunits: NrfA, 478 aas and 1 N-terminal TMS, P0ABK9; NrfB or YjcI, 188 aas and 1 N-terminal TMS, P0ABL1; NrfC or YjcJ, 223 aas and 1 N-terminal TMS, P0AAK7; NrfD or YjcK, 318 aas and 8 TMSs, P32709. | Bacteria |
Pseudomonadota | NrfABCD of E. coli |
|
5.A.3.6.1 | Arsenite oxidase, AoxAB | Bacteria |
Pseudomonadota | AoxAB of Alcaligenes faecalis AoxB (α) (AOI) (Q7SIF4) AoxA (β) (AOII) (Q7SIF3) |
|
5.A.3.7.1 | Pyrogallol hydroxytransferase, AthL/BthL | Bacteria |
Thermodesulfobacteriota | AthL/BthL of Pelobacter acidigallici AthL (α) (P80563) BthL (β) (P80564) |
|
5.A.3.8.1 | Selenate reductase, SerABC | Bacteria |
Pseudomonadota | SerABC of Thauera selenatis SerA (α) (Q9S1H0) SerB (β) (Q9S1G9 SerC (γ) (Q9S1G7) |
|
5.A.3.8.2 | Chlorate reductase, ClrABC | Bacteria |
Pseudomonadota | ClrABC of Ideonella dechloratans ClrA (α) (P60068) ClrB (β) (P60069) ClrC (γ) (P60000) |
|
5.A.3.9.1 | Anaerobic ethylbenzene dehydrogenase, EbdABC (Johnson et al., 2001) | Bacteria |
Pseudomonadota | EbdABC in Azoarcus sp EB1 EbdA (α or A-chain) (AAK76387) EbdB (β or B-chain) (AAK76388 EbdC (γ or C-chain) (AAK76389) |
|
5.A.3.10.1 | Tetrathionate reductase, TtrABC | Bacteria |
Pseudomonadota | TtrABC of Bordetella bronchiseptica TtrA (α) (NP_887789) TtrB (β) (NP_887791) TtrC (γ) (NP_887790) |
|
5.A.3.10.2 | Tetrathionate reductase, subunit A of 1173 aas and up to 4 TMSs, 2 TMSs N-terminal and 2 TMSs in the middle of the protein. | Archaea |
Thermoproteota | Tetrathionate reductase of Pyrobaculum aerophilum |
|
5.A.3.11.1 | Phenylacetyl-CoA:acceptor oxidoreductase (Rhee and Fuchs, 1999) | Bacteria |
Pseudomonadota | PadB2C2D of Azoarcus sp. EbN1 PadB2 (α) CAI09327 PadC2 (β) CAI09328 PadD (γ) CAI09186 |
|
5.A.3.11.2 | The cytoplasmic sulfur/tetrathionate/polysulfide oxidoreductase, SreABC (Guiral et al., 2005) [While SreA and B most resemble 5.A.3.11.1, SreC most resembles 5.A.3.3.2.] | Bacteria |
Aquificota | SreABC of Aquifex aeolicus SreA (α) (AAC07243) SreB (β) (AAC07244) SreC (γ) (AAC07245) |