arsenate reductase (azurin) large subunit [Aeropyrum pernix]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||||||||
| MopB_Arsenite-Ox | cd02756 | Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
7-854 | 0e+00 | ||||||||||||
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin. Arsenite oxidase is a heterodimeric enzyme containing a large and a small subunit. The large catalytic subunit harbors the molybdopterin cofactor and the [3Fe-4S] cluster; and the small subunit belongs to the structural class of the Rieske proteins. The small subunit is not included in this alignment. Members of MopB_Arsenite-Ox CD belong to the molybdopterin_binding (MopB) superfamily of proteins. : Pssm-ID: 239157 [Multi-domain] Cd Length: 676 Bit Score: 983.51 E-value: 0e+00
|
||||||||||||||||
| MopB_CT_Arsenite-Ox | cd02779 | This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
870-985 | 3.05e-62 | ||||||||||||
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase (Arsenite-Ox) and related proteins. Arsenite oxidase oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin. : Pssm-ID: 239180 [Multi-domain] Cd Length: 115 Bit Score: 206.54 E-value: 3.05e-62
|
||||||||||||||||
| Name | Accession | Description | Interval | E-value | ||||||||||||||
| MopB_Arsenite-Ox | cd02756 | Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
7-854 | 0e+00 | ||||||||||||||
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin. Arsenite oxidase is a heterodimeric enzyme containing a large and a small subunit. The large catalytic subunit harbors the molybdopterin cofactor and the [3Fe-4S] cluster; and the small subunit belongs to the structural class of the Rieske proteins. The small subunit is not included in this alignment. Members of MopB_Arsenite-Ox CD belong to the molybdopterin_binding (MopB) superfamily of proteins. Pssm-ID: 239157 [Multi-domain] Cd Length: 676 Bit Score: 983.51 E-value: 0e+00
|
||||||||||||||||||
| arsenite_ox_L | TIGR02693 | arsenite oxidase, large subunit; This model represents the large subunit of an arsenite ... |
8-985 | 5.82e-180 | ||||||||||||||
arsenite oxidase, large subunit; This model represents the large subunit of an arsenite oxidase complex. The small subunit is a Rieske protein. Homologs to both large and small subunits that score in the gray zone between the set trusted and noise bit score cutoffs for the respective models are found in Aeropyrum pernix K1 and in Sulfolobus tokodaii str. 7. This enzyme acts in energy metabolim by arsenite oxidation, rather than detoxification by reduction of arsenate to arsenite prior to export. [Energy metabolism, Electron transport] Pssm-ID: 274261 [Multi-domain] Cd Length: 806 Bit Score: 543.36 E-value: 5.82e-180
|
||||||||||||||||||
| YjgC | COG3383 | Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
117-987 | 1.27e-71 | ||||||||||||||
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 251.34 E-value: 1.27e-71
|
||||||||||||||||||
| MopB_CT_Arsenite-Ox | cd02779 | This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
870-985 | 3.05e-62 | ||||||||||||||
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase (Arsenite-Ox) and related proteins. Arsenite oxidase oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin. Pssm-ID: 239180 [Multi-domain] Cd Length: 115 Bit Score: 206.54 E-value: 3.05e-62
|
||||||||||||||||||
| Molydop_binding | pfam01568 | Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
872-979 | 4.48e-26 | ||||||||||||||
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - containing oxidoreductases and tungsten formylmethanofuran dehydrogenase subunit d (FwdD) and molybdenum formylmethanofuran dehydrogenase subunit (FmdD); where the domain constitutes almost the entire subunit. The formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and has a molybdopterin dinucleotide cofactor. This domain corresponds to the C-terminal domain IV in dimethyl sulfoxide (DMSO)reductase which interacts with the 2-amino pyrimidone ring of both molybdopterin guanine dinucleotide molecules. Pssm-ID: 426328 [Multi-domain] Cd Length: 110 Bit Score: 103.51 E-value: 4.48e-26
|
||||||||||||||||||
| Rieske_3 | pfam18465 | Rieske 3Fe-4S; This domain is comprised of the iron-sulphur cluster and Rieske subunit found ... |
23-143 | 3.52e-19 | ||||||||||||||
Rieske 3Fe-4S; This domain is comprised of the iron-sulphur cluster and Rieske subunit found in the large subunit of arsenite oxidase. Arsenite oxidase is a 100 kDa molybdenum- and iron-sulfur-containing protein located on the outer surface of the inner membrane of Gram-negative organizms. The large subunit of arsenite oxidase is similar to other members of the dimethylsulfoxide (DMSO) reductase family of molybdenum enzymes. The large subunit of arsenite oxidase is divided into four domains, with domain I binding the [3Fe-4S] cluster. Domain I, consists of three antiparallel beta sheets and six helices. The [3Fe-4S] cluster is coordinated by the motif Cys21-X2-Cys24-X3-Cys28 near the interface with domains III and IV. A large, flattened funnel-like cavity bounded by domains I, II, and III leads to the molybdenum center pfam00384 located near the center of the molecule. Pssm-ID: 465779 [Multi-domain] Cd Length: 96 Bit Score: 83.17 E-value: 3.52e-19
|
||||||||||||||||||
| PRK14990 | PRK14990 | anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
131-441 | 1.24e-10 | ||||||||||||||
anaerobic dimethyl sulfoxide reductase subunit A; Provisional Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 65.44 E-value: 1.24e-10
|
||||||||||||||||||
| PRK14991 | PRK14991 | tetrathionate reductase subunit TtrA; |
899-946 | 1.23e-06 | ||||||||||||||
tetrathionate reductase subunit TtrA; Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 52.69 E-value: 1.23e-06
|
||||||||||||||||||
| Name | Accession | Description | Interval | E-value | ||||||||||||||
| MopB_Arsenite-Ox | cd02756 | Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
7-854 | 0e+00 | ||||||||||||||
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin. Arsenite oxidase is a heterodimeric enzyme containing a large and a small subunit. The large catalytic subunit harbors the molybdopterin cofactor and the [3Fe-4S] cluster; and the small subunit belongs to the structural class of the Rieske proteins. The small subunit is not included in this alignment. Members of MopB_Arsenite-Ox CD belong to the molybdopterin_binding (MopB) superfamily of proteins. Pssm-ID: 239157 [Multi-domain] Cd Length: 676 Bit Score: 983.51 E-value: 0e+00
|
||||||||||||||||||
| arsenite_ox_L | TIGR02693 | arsenite oxidase, large subunit; This model represents the large subunit of an arsenite ... |
8-985 | 5.82e-180 | ||||||||||||||
arsenite oxidase, large subunit; This model represents the large subunit of an arsenite oxidase complex. The small subunit is a Rieske protein. Homologs to both large and small subunits that score in the gray zone between the set trusted and noise bit score cutoffs for the respective models are found in Aeropyrum pernix K1 and in Sulfolobus tokodaii str. 7. This enzyme acts in energy metabolim by arsenite oxidation, rather than detoxification by reduction of arsenate to arsenite prior to export. [Energy metabolism, Electron transport] Pssm-ID: 274261 [Multi-domain] Cd Length: 806 Bit Score: 543.36 E-value: 5.82e-180
|
||||||||||||||||||
| YjgC | COG3383 | Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
117-987 | 1.27e-71 | ||||||||||||||
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 251.34 E-value: 1.27e-71
|
||||||||||||||||||
| BisC | COG0243 | Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
114-986 | 1.06e-67 | ||||||||||||||
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 240.13 E-value: 1.06e-67
|
||||||||||||||||||
| MopB_CT_Arsenite-Ox | cd02779 | This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
870-985 | 3.05e-62 | ||||||||||||||
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase (Arsenite-Ox) and related proteins. Arsenite oxidase oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin. Pssm-ID: 239180 [Multi-domain] Cd Length: 115 Bit Score: 206.54 E-value: 3.05e-62
|
||||||||||||||||||
| Molybdopterin-Binding | cd00368 | Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
114-694 | 1.44e-43 | ||||||||||||||
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site. Pssm-ID: 238218 [Multi-domain] Cd Length: 374 Bit Score: 162.88 E-value: 1.44e-43
|
||||||||||||||||||
| MopB_Nitrate-R-NapA-like | cd02754 | Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
114-693 | 5.91e-41 | ||||||||||||||
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. Members of the MopB_Nitrate-R-NapA CD belong to the molybdopterin_binding (MopB) superfamily of proteins. Pssm-ID: 239155 [Multi-domain] Cd Length: 565 Bit Score: 159.70 E-value: 5.91e-41
|
||||||||||||||||||
| MopB_Formate-Dh-H | cd02753 | Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
117-694 | 6.47e-39 | ||||||||||||||
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. Members of the MopB_Formate-Dh-H CD belong to the molybdopterin_binding (MopB) superfamily of proteins. Pssm-ID: 239154 [Multi-domain] Cd Length: 512 Bit Score: 152.37 E-value: 6.47e-39
|
||||||||||||||||||
| Molydop_binding | pfam01568 | Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
872-979 | 4.48e-26 | ||||||||||||||
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - containing oxidoreductases and tungsten formylmethanofuran dehydrogenase subunit d (FwdD) and molybdenum formylmethanofuran dehydrogenase subunit (FmdD); where the domain constitutes almost the entire subunit. The formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and has a molybdopterin dinucleotide cofactor. This domain corresponds to the C-terminal domain IV in dimethyl sulfoxide (DMSO)reductase which interacts with the 2-amino pyrimidone ring of both molybdopterin guanine dinucleotide molecules. Pssm-ID: 426328 [Multi-domain] Cd Length: 110 Bit Score: 103.51 E-value: 4.48e-26
|
||||||||||||||||||
| MopB_3 | cd02766 | The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
117-694 | 7.76e-25 | ||||||||||||||
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins Pssm-ID: 239167 [Multi-domain] Cd Length: 501 Bit Score: 109.65 E-value: 7.76e-25
|
||||||||||||||||||
| MopB_CT_Fdh-Nap-like | cd00508 | This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
870-984 | 2.78e-20 | ||||||||||||||
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and other related proteins. Formate dehydrogenase H is a component of the anaerobic formate hydrogen lyase complex and catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. Formate dehydrogenase N (alpha subunit) is the major electron donor to the bacterial nitrate respiratory chain and nitrate reductases, Nap and Nas, catalyze the reduction of nitrate to nitrite. This CD (MopB_CT_Fdh-Nap-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs. Pssm-ID: 238282 [Multi-domain] Cd Length: 120 Bit Score: 87.18 E-value: 2.78e-20
|
||||||||||||||||||
| MopB_CT | cd02775 | Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
879-976 | 2.45e-19 | ||||||||||||||
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site. This hierarchy is of the conserved MopB_CT domain present in many, but not all, MopB homologs. Pssm-ID: 239176 [Multi-domain] Cd Length: 101 Bit Score: 83.91 E-value: 2.45e-19
|
||||||||||||||||||
| Rieske_3 | pfam18465 | Rieske 3Fe-4S; This domain is comprised of the iron-sulphur cluster and Rieske subunit found ... |
23-143 | 3.52e-19 | ||||||||||||||
Rieske 3Fe-4S; This domain is comprised of the iron-sulphur cluster and Rieske subunit found in the large subunit of arsenite oxidase. Arsenite oxidase is a 100 kDa molybdenum- and iron-sulfur-containing protein located on the outer surface of the inner membrane of Gram-negative organizms. The large subunit of arsenite oxidase is similar to other members of the dimethylsulfoxide (DMSO) reductase family of molybdenum enzymes. The large subunit of arsenite oxidase is divided into four domains, with domain I binding the [3Fe-4S] cluster. Domain I, consists of three antiparallel beta sheets and six helices. The [3Fe-4S] cluster is coordinated by the motif Cys21-X2-Cys24-X3-Cys28 near the interface with domains III and IV. A large, flattened funnel-like cavity bounded by domains I, II, and III leads to the molybdenum center pfam00384 located near the center of the molecule. Pssm-ID: 465779 [Multi-domain] Cd Length: 96 Bit Score: 83.17 E-value: 3.52e-19
|
||||||||||||||||||
| MopB_Acetylene-hydratase | cd02759 | The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
118-431 | 2.76e-18 | ||||||||||||||
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins. Pssm-ID: 239160 [Multi-domain] Cd Length: 477 Bit Score: 89.29 E-value: 2.76e-18
|
||||||||||||||||||
| MopB_1 | cd02762 | The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
151-688 | 1.84e-15 | ||||||||||||||
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins. Pssm-ID: 239163 [Multi-domain] Cd Length: 539 Bit Score: 80.52 E-value: 1.84e-15
|
||||||||||||||||||
| MopB_DMSOR-like | cd02751 | The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
130-445 | 2.89e-15 | ||||||||||||||
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. Members of the MopB_DMSOR-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins. Pssm-ID: 239152 [Multi-domain] Cd Length: 609 Bit Score: 80.35 E-value: 2.89e-15
|
||||||||||||||||||
| MopB_CT_Nitrate-R-NapA-like | cd02791 | Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
870-985 | 2.26e-14 | ||||||||||||||
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. This CD (MopB_CT_Nitrate-R-Nap) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs Pssm-ID: 239192 [Multi-domain] Cd Length: 122 Bit Score: 70.68 E-value: 2.26e-14
|
||||||||||||||||||
| MopB_Formate-Dh-Na-like | cd02752 | Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
111-486 | 2.38e-14 | ||||||||||||||
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. Members of the MopB_Formate-Dh-Na-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins. Pssm-ID: 239153 [Multi-domain] Cd Length: 649 Bit Score: 77.44 E-value: 2.38e-14
|
||||||||||||||||||
| MopB_CT_Formate-Dh-Na-like | cd02792 | Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
868-984 | 1.05e-13 | ||||||||||||||
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. This CD (MopB_CT_Formate-Dh-Na-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs. Pssm-ID: 239193 [Multi-domain] Cd Length: 122 Bit Score: 68.40 E-value: 1.05e-13
|
||||||||||||||||||
| MopB_DmsA-EC | cd02770 | This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
131-434 | 5.03e-13 | ||||||||||||||
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins. Pssm-ID: 239171 [Multi-domain] Cd Length: 617 Bit Score: 73.13 E-value: 5.03e-13
|
||||||||||||||||||
| Molybdopterin | pfam00384 | Molybdopterin oxidoreductase; |
151-362 | 5.14e-13 | ||||||||||||||
Molybdopterin oxidoreductase; Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 71.66 E-value: 5.14e-13
|
||||||||||||||||||
| MopB_CT_Formate-Dh_H | cd02790 | Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
870-984 | 1.44e-12 | ||||||||||||||
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. This CD (MopB_CT_Formate-Dh_H) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs. Pssm-ID: 239191 [Multi-domain] Cd Length: 116 Bit Score: 65.34 E-value: 1.44e-12
|
||||||||||||||||||
| PRK14990 | PRK14990 | anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
131-441 | 1.24e-10 | ||||||||||||||
anaerobic dimethyl sulfoxide reductase subunit A; Provisional Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 65.44 E-value: 1.24e-10
|
||||||||||||||||||
| MopB_Thiosulfate-R-like | cd02755 | The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
118-428 | 1.09e-09 | ||||||||||||||
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Members of the MopB_Thiosulfate-R-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins. Pssm-ID: 239156 [Multi-domain] Cd Length: 454 Bit Score: 61.93 E-value: 1.09e-09
|
||||||||||||||||||
| MopB_CT_DMSOR-like | cd02777 | The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
894-946 | 1.14e-09 | ||||||||||||||
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs. Pssm-ID: 239178 [Multi-domain] Cd Length: 127 Bit Score: 57.21 E-value: 1.14e-09
|
||||||||||||||||||
| MopB_DMSOR-BSOR-TMAOR | cd02769 | The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
148-433 | 3.92e-09 | ||||||||||||||
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins. Pssm-ID: 239170 [Multi-domain] Cd Length: 609 Bit Score: 60.35 E-value: 3.92e-09
|
||||||||||||||||||
| MopB_CT_Tetrathionate_Arsenate-R | cd02780 | This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
891-946 | 4.51e-08 | ||||||||||||||
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate reductase, subunit A, (TtrA); respiratory arsenate As(V) reductase, catalytic subunit (ArrA); and other related proteins. Pssm-ID: 239181 [Multi-domain] Cd Length: 143 Bit Score: 53.07 E-value: 4.51e-08
|
||||||||||||||||||
| MopB_4 | cd02765 | The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
131-378 | 6.00e-08 | ||||||||||||||
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins Pssm-ID: 239166 [Multi-domain] Cd Length: 567 Bit Score: 56.72 E-value: 6.00e-08
|
||||||||||||||||||
| MopB_CT_DMSOR-BSOR-TMAOR | cd02793 | The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
904-946 | 1.37e-07 | ||||||||||||||
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO.This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs. Pssm-ID: 239194 [Multi-domain] Cd Length: 129 Bit Score: 51.48 E-value: 1.37e-07
|
||||||||||||||||||
| MopB_CT_Thiosulfate-R-like | cd02778 | The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
890-950 | 1.62e-07 | ||||||||||||||
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Also included in this CD is the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), which has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. The MopB_CT_Thiosulfate-R-like CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs. Pssm-ID: 239179 [Multi-domain] Cd Length: 123 Bit Score: 51.12 E-value: 1.62e-07
|
||||||||||||||||||
| MopB_Nitrate-R-NarG-like | cd02750 | Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
109-466 | 4.57e-07 | ||||||||||||||
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. Members of the MopB_Nitrate-R-NarG-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins. Pssm-ID: 239151 [Multi-domain] Cd Length: 461 Bit Score: 53.48 E-value: 4.57e-07
|
||||||||||||||||||
| PRK14991 | PRK14991 | tetrathionate reductase subunit TtrA; |
899-946 | 1.23e-06 | ||||||||||||||
tetrathionate reductase subunit TtrA; Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 52.69 E-value: 1.23e-06
|
||||||||||||||||||
| MopB_CT_3 | cd02786 | The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
904-963 | 4.11e-06 | ||||||||||||||
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs. Pssm-ID: 239187 [Multi-domain] Cd Length: 116 Bit Score: 46.89 E-value: 4.11e-06
|
||||||||||||||||||
| MopB_CT_DmsA-EC | cd02794 | The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
902-946 | 6.66e-06 | ||||||||||||||
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs. Pssm-ID: 239195 [Multi-domain] Cd Length: 121 Bit Score: 46.13 E-value: 6.66e-06
|
||||||||||||||||||
| MopB_NADH-Q-OR-NuoG2 | cd02768 | MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
151-311 | 2.88e-05 | ||||||||||||||
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone oxidoreductase (NADH-Q-OR)/respiratory complex I/NADH dehydrogenase-1 (NDH-1). The NADH-Q-OR is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The atomic structure of complex I is not known and the mechanisms of electron transfer and proton pumping are not established. The nad11 gene codes for the largest (75-kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Escherichia coli, this subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The nad11 gene is nuclear-encoded in animals, plants, and fungi, but is still encoded in the mitochondrial genome of some protists. The Nad11/NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain family belongs to the molybdopterin_binding (MopB) superfamily of proteins. Bacterial type II NADH-quinone oxidoreductases and NQR-type sodium-motive NADH-quinone oxidoreductases are not homologs of this domain family. Pssm-ID: 239169 [Multi-domain] Cd Length: 386 Bit Score: 47.66 E-value: 2.88e-05
|
||||||||||||||||||
| MopB_CT_Nitrate-R-NarG-like | cd02776 | Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
904-948 | 5.54e-05 | ||||||||||||||
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. This CD (MopB_CT_Nitrate-R-NarG-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs. Pssm-ID: 239177 [Multi-domain] Cd Length: 141 Bit Score: 44.29 E-value: 5.54e-05
|
||||||||||||||||||
| MopB_CT_4 | cd02785 | The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
871-946 | 7.77e-05 | ||||||||||||||
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs. Pssm-ID: 239186 [Multi-domain] Cd Length: 124 Bit Score: 43.12 E-value: 7.77e-05
|
||||||||||||||||||
| MopB_CT_ydeP | cd02787 | The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial ... |
903-982 | 9.81e-05 | ||||||||||||||
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs. Pssm-ID: 239188 [Multi-domain] Cd Length: 112 Bit Score: 42.65 E-value: 9.81e-05
|
||||||||||||||||||
| MopB_CT_Acetylene-hydratase | cd02781 | The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
893-947 | 1.13e-04 | ||||||||||||||
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs. Pssm-ID: 239182 [Multi-domain] Cd Length: 130 Bit Score: 43.07 E-value: 1.13e-04
|
||||||||||||||||||
| MopB_Res-Cmplx1_Nad11 | cd02773 | MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
150-182 | 1.42e-04 | ||||||||||||||
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone oxidoreductase/respiratory complex I/NADH dehydrogenase-1(NDH-1) of eukaryotes and the Nqo3/G subunit of alphaproteobacteria NDH-1. The NADH-quinone oxidoreductase is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The nad11 gene codes for the largest (75 kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Paracoccus denitrificans, this subunit is encoded by the nqo3 gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The Nad11/Nqo3 subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins. Pssm-ID: 239174 [Multi-domain] Cd Length: 375 Bit Score: 45.33 E-value: 1.42e-04
|
||||||||||||||||||
| PRK15488 | PRK15488 | thiosulfate reductase PhsA; Provisional |
859-950 | 1.57e-04 | ||||||||||||||
thiosulfate reductase PhsA; Provisional Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 45.81 E-value: 1.57e-04
|
||||||||||||||||||
| MopB_CT_FmdC-FwdD | cd02789 | The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran ... |
902-976 | 2.66e-04 | ||||||||||||||
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran dehydrogenase (FmdC) and subunit D of tungsten formylmethanofuran dehydrogenase (FwdD), and other related proteins. Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and some eubacteria. Members of this CD belong to the molybdopterin_binding superfamily of proteins. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs. Pssm-ID: 239190 [Multi-domain] Cd Length: 106 Bit Score: 41.26 E-value: 2.66e-04
|
||||||||||||||||||
| MopB_NDH-1_NuoG2-N7 | cd02771 | MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of ... |
600-712 | 2.76e-04 | ||||||||||||||
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1) found in various bacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Unique to this group, compared to the other prokaryotic and eukaryotic groups in this domain protein family (NADH-Q-OR-NuoG2), is an N-terminal [4Fe-4S] cluster (N7/N1c) present in the second domain. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins. Pssm-ID: 239172 [Multi-domain] Cd Length: 472 Bit Score: 44.69 E-value: 2.76e-04
|
||||||||||||||||||
| NuoG | COG1034 | NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
613-693 | 8.66e-04 | ||||||||||||||
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase Pssm-ID: 440657 [Multi-domain] Cd Length: 453 Bit Score: 42.90 E-value: 8.66e-04
|
||||||||||||||||||
| MopB_CT_1 | cd02782 | The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
904-984 | 1.10e-03 | ||||||||||||||
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs. Pssm-ID: 239183 [Multi-domain] Cd Length: 129 Bit Score: 40.07 E-value: 1.10e-03
|
||||||||||||||||||
| MopB_NDH-1_NuoG2-N7 | cd02771 | MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of ... |
146-285 | 1.77e-03 | ||||||||||||||
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1) found in various bacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Unique to this group, compared to the other prokaryotic and eukaryotic groups in this domain protein family (NADH-Q-OR-NuoG2), is an N-terminal [4Fe-4S] cluster (N7/N1c) present in the second domain. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins. Pssm-ID: 239172 [Multi-domain] Cd Length: 472 Bit Score: 41.99 E-value: 1.77e-03
|
||||||||||||||||||
| MopB_Arsenate-R | cd02757 | This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
263-431 | 2.70e-03 | ||||||||||||||
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other related proteins. These members belong to the molybdopterin_binding (MopB) superfamily of proteins. Pssm-ID: 239158 [Multi-domain] Cd Length: 523 Bit Score: 41.66 E-value: 2.70e-03
|
||||||||||||||||||
| PRK15102 | PRK15102 | trimethylamine-N-oxide reductase TorA; |
898-946 | 3.00e-03 | ||||||||||||||
trimethylamine-N-oxide reductase TorA; Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 41.58 E-value: 3.00e-03
|
||||||||||||||||||
| MopB_NDH-1_NuoG2 | cd02772 | MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
149-187 | 4.14e-03 | ||||||||||||||
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1), found in beta- and gammaproteobacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins. Pssm-ID: 239173 [Multi-domain] Cd Length: 414 Bit Score: 40.80 E-value: 4.14e-03
|
||||||||||||||||||
| PRK13532 | PRK13532 | nitrate reductase catalytic subunit NapA; |
627-701 | 6.22e-03 | ||||||||||||||
nitrate reductase catalytic subunit NapA; Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 40.65 E-value: 6.22e-03
|
||||||||||||||||||
| Blast search parameters | ||||
|
