TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(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









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
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.3.4.4









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
Proteobacteria
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
Proteobacteria
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
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.3.10.2









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
TACK group
Tetrathionate reductase of Pyrobaculum aerophilum
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)