| 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 |
Proteobacteria | 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 |
Proteobacteria | 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 |
Proteobacteria | 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 |
Proteobacteria | 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 |
Proteobacteria | 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 |
Proteobacteria | TorAC of E. coli TorA (α) (precursor 1) (P33225) TorC (cytochrome c-type protein) (P33226) |
|
*5.A.3.4.2 | Anaerobic trimethylamine-N-oxide reductase 2, TorYZ | Bacteria |
Proteobacteria | 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 |
Proteobacteria | BisC of E. coli BisC (α) (P20099) |
|
*5.A.3.5.1 | Thiosulfate reductase, PhsABC (Heinzinger et al., 1995). Menaquinone is the sole electron donor. The endoergonic reduction reaction is driven by the pmf by a reverse loop mechanism. The enzyme can catalyze oxidation of sulfide to sulfite and sulfite to thiosulfate in an exergonic reaction that is pmf-independent (Stoffels et al., 2011). | Bacteria |
Proteobacteria | PhsABC of Salmonella typhimurium PhsA (α) (molybdopterin subunit) (P37600) PhsB (β) (reductase) (P0A1I1) PhsC (γ) (cytochrome b subunit) (P37602) |
|
*5.A.3.5.2 | Polysulfide reductase, PsrABC | Bacteria |
Proteobacteria | PsrABC of Wolinella succinogenes PsrA (α or chain A) (P31075) PsrB (β or chain B) (P31076) PsrC (γ or chain C) (P31077) |
|
*5.A.3.6.1 | Arsenite oxidase, AoxAB | Bacteria |
Proteobacteria | AoxAB of Alcaligenes faecalis AoxB (α) (AOI) (Q7SIF4) AoxA (β) (AOII) (Q7SIF3) |
|
*5.A.3.7.1 | Pyrogallol hydroxytransferase, AthL/BthL | Bacteria |
Proteobacteria | AthL/BthL of Pelobacter acidigallici AthL (α) (P80563) BthL (β) (P80564) |
|
*5.A.3.8.1 | Selenate reductase, SerABC | Bacteria |
Proteobacteria | SerABC of Thauera selenatis SerA (α) (Q9S1H0) SerB (β) (Q9S1G9 SerC (γ) (Q9S1G7) |
|
*5.A.3.8.2 | Chlorate reductase, ClrABC | Bacteria |
Proteobacteria | 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 |
Proteobacteria | 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 |
Proteobacteria | TtrABC of Bordetella bronchiseptica TtrA (α) (NP_887789) TtrB (β) (NP_887791) TtrC (γ) (NP_887790) |
|
*5.A.3.11.1 | Phenylacetyl-CoA:acceptor oxidoreductase (Rhee and Fuchs, 1999) | Bacteria |
Proteobacteria | 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 |
Aquificae | SreABC of Aquifex aeolicus SreA (α) (AAC07243) SreB (β) (AAC07244) SreC (γ) (AAC07245) |
