FAD-binding oxidoreductase [Andreesenia angusta]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| Fpr | COG1018 | Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; |
263-491 | 1.23e-43 | |||||
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; : Pssm-ID: 440641 [Multi-domain] Cd Length: 231 Bit Score: 153.79 E-value: 1.23e-43
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| NapH | COG0348 | Polyferredoxin NapH [Energy production and conversion]; |
3-242 | 1.97e-25 | |||||
Polyferredoxin NapH [Energy production and conversion]; : Pssm-ID: 440117 [Multi-domain] Cd Length: 263 Bit Score: 105.14 E-value: 1.97e-25
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| Name | Accession | Description | Interval | E-value | |||||
| Fpr | COG1018 | Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; |
263-491 | 1.23e-43 | |||||
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; Pssm-ID: 440641 [Multi-domain] Cd Length: 231 Bit Score: 153.79 E-value: 1.23e-43
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| phenol_2-monooxygenase_like | cd06211 | Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ... |
267-491 | 3.35e-37 | |||||
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use molecular oxygen as a substrate in the microbial degredation of phenol. This protein is encoded by a single gene and uses a tightly bound FAD cofactor in the NAD(P)H dependent conversion of phenol and O2 to catechol and H2O. This group is related to the NAD binding ferredoxin reductases. Pssm-ID: 99807 Cd Length: 238 Bit Score: 136.69 E-value: 3.35e-37
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| NapH | COG0348 | Polyferredoxin NapH [Energy production and conversion]; |
3-242 | 1.97e-25 | |||||
Polyferredoxin NapH [Energy production and conversion]; Pssm-ID: 440117 [Multi-domain] Cd Length: 263 Bit Score: 105.14 E-value: 1.97e-25
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| PRK00054 | PRK00054 | dihydroorotate dehydrogenase electron transfer subunit; Reviewed |
268-482 | 2.16e-24 | |||||
dihydroorotate dehydrogenase electron transfer subunit; Reviewed Pssm-ID: 234601 [Multi-domain] Cd Length: 250 Bit Score: 101.87 E-value: 2.16e-24
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| NAD_binding_1 | pfam00175 | Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ... |
374-476 | 2.04e-11 | |||||
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have essentially no similarity. Pssm-ID: 425503 [Multi-domain] Cd Length: 109 Bit Score: 60.74 E-value: 2.04e-11
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| MtMvhB_like | cd10549 | Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
152-237 | 4.35e-10 | |||||
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction. Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 57.41 E-value: 4.35e-10
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| Fer4_7 | pfam12838 | 4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
188-233 | 8.44e-08 | |||||
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters. Pssm-ID: 463724 [Multi-domain] Cd Length: 51 Bit Score: 48.68 E-value: 8.44e-08
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| PRK12769 | PRK12769 | putative oxidoreductase Fe-S binding subunit; Reviewed |
188-252 | 9.91e-08 | |||||
putative oxidoreductase Fe-S binding subunit; Reviewed Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 54.37 E-value: 9.91e-08
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| rnfC | TIGR01945 | electron transport complex, RnfABCDGE type, C subunit; The six subunit complex RnfABCDGE in ... |
187-249 | 1.20e-07 | |||||
electron transport complex, RnfABCDGE type, C subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the C subunit. [Energy metabolism, Electron transport] Pssm-ID: 273888 [Multi-domain] Cd Length: 435 Bit Score: 53.89 E-value: 1.20e-07
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| ferrodoxin_EFR1 | NF038196 | EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ... |
154-246 | 1.10e-04 | |||||
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1). Pssm-ID: 468407 [Multi-domain] Cd Length: 243 Bit Score: 43.69 E-value: 1.10e-04
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| Name | Accession | Description | Interval | E-value | |||||
| Fpr | COG1018 | Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; |
263-491 | 1.23e-43 | |||||
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; Pssm-ID: 440641 [Multi-domain] Cd Length: 231 Bit Score: 153.79 E-value: 1.23e-43
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| Mcr1 | COG0543 | NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ... |
269-491 | 7.23e-43 | |||||
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; Pssm-ID: 440309 [Multi-domain] Cd Length: 247 Bit Score: 152.32 E-value: 7.23e-43
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| phenol_2-monooxygenase_like | cd06211 | Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ... |
267-491 | 3.35e-37 | |||||
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use molecular oxygen as a substrate in the microbial degredation of phenol. This protein is encoded by a single gene and uses a tightly bound FAD cofactor in the NAD(P)H dependent conversion of phenol and O2 to catechol and H2O. This group is related to the NAD binding ferredoxin reductases. Pssm-ID: 99807 Cd Length: 238 Bit Score: 136.69 E-value: 3.35e-37
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| T4MO_e_transfer_like | cd06190 | Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ... |
270-489 | 3.61e-37 | |||||
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates toluene and forms p-cresol as part of a three component toluene-4-monoxygenase system. Electron transfer is from NADH to an NADH:ferredoxin oxidoreductase (TmoF in P. mendocina) to ferredoxin to an iron-containing oxygenase. TmoF is homologous to other mono- and dioxygenase systems within the ferredoxin reductase family. Pssm-ID: 99787 Cd Length: 232 Bit Score: 136.61 E-value: 3.61e-37
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| FNR_like | cd00322 | Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ... |
271-491 | 1.17e-35 | |||||
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in many organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H). Pssm-ID: 99778 [Multi-domain] Cd Length: 223 Bit Score: 132.19 E-value: 1.17e-35
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| O2ase_reductase_like | cd06187 | The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ... |
270-492 | 1.59e-34 | |||||
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons using oxygen as the oxidant. Electron transfer is from NADH via FAD (in the oxygenase reductase) and an [2FE-2S] ferredoxin center (fused to the FAD/NADH domain and/or discrete) to the oxygenase. Dioxygenases add both atoms of oxygen to the substrate, while mono-oxygenases (aka mixed oxygenases) add one atom to the substrate and one atom to water. In dioxygenases, Class I enzymes are 2 component, containing a reductase with Rieske type [2Fe-2S] redox centers and an oxygenase. Class II are 3 component, having discrete flavin and ferredoxin proteins and an oxygenase. Class III have 2 [2Fe-2S] centers, one fused to the flavin domain and the other separate. Pssm-ID: 99784 [Multi-domain] Cd Length: 224 Bit Score: 129.25 E-value: 1.59e-34
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| FNR1 | cd06195 | Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ... |
270-485 | 1.16e-28 | |||||
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH. Pssm-ID: 99792 [Multi-domain] Cd Length: 241 Bit Score: 113.43 E-value: 1.16e-28
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| flavin_oxioreductase | cd06189 | NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ... |
268-489 | 3.02e-27 | |||||
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron transfer from iron complexes or iron proteins. Structurally similar to ferredoxin reductases, but with only 15% sequence identity, flavin reductases reduce FAD, FMN, or riboflavin via NAD(P)H. Flavin is used as a substrate, rather than a tightly bound prosthetic group as in flavoenzymes; weaker binding is due to the absence of a binding site for the AMP moeity of FAD. Pssm-ID: 99786 [Multi-domain] Cd Length: 224 Bit Score: 109.18 E-value: 3.02e-27
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| COG4097 | COG4097 | Predicted ferric reductase [Inorganic ion transport and metabolism]; |
261-491 | 2.64e-26 | |||||
Predicted ferric reductase [Inorganic ion transport and metabolism]; Pssm-ID: 443273 [Multi-domain] Cd Length: 442 Bit Score: 111.14 E-value: 2.64e-26
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| DHOD_e_trans | cd06218 | FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ... |
270-486 | 4.43e-26 | |||||
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster. Pssm-ID: 99814 [Multi-domain] Cd Length: 246 Bit Score: 106.48 E-value: 4.43e-26
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| oxygenase_e_transfer_subunit | cd06213 | The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ... |
266-489 | 7.37e-26 | |||||
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. Electron transfer is from NADH via FAD (in the oxygenase reductase) and an [2FE-2S] ferredoxin center (fused to the FAD/NADH domain and/or discrete) to the oxygenase. Dioxygenases add both atoms of oxygen to the substrate while mono-oxygenases add one atom to the substrate and one atom to water. In dioxygenases, Class I enzymes are 2 component, containing a reductase with Rieske type [2Fe-2S] redox centers and an oxygenase. Class II are 3 component, having discrete flavin and ferredoxin proteins and an oxygenase. Class III have 2 [2Fe-2S] centers, one fused to the flavin domain and the other separate. Pssm-ID: 99809 Cd Length: 227 Bit Score: 105.47 E-value: 7.37e-26
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| NapH | COG0348 | Polyferredoxin NapH [Energy production and conversion]; |
3-242 | 1.97e-25 | |||||
Polyferredoxin NapH [Energy production and conversion]; Pssm-ID: 440117 [Multi-domain] Cd Length: 263 Bit Score: 105.14 E-value: 1.97e-25
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| FNR_iron_sulfur_binding_1 | cd06215 | Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
269-491 | 3.79e-25 | |||||
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal portion of the FAD/NAD binding domain contains most of the NADP(H) binding residues and the N-terminal sub-domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. In this ferredoxin like sub-group, the FAD/NAD sub-domains is typically fused to a C-terminal iron-sulfur binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins which act as electron carriers in photosynthesis and ferredoxins which participate in redox chains from bacteria to mammals. Ferredoxin reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH. Pssm-ID: 99811 [Multi-domain] Cd Length: 231 Bit Score: 103.44 E-value: 3.79e-25
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| sulfite_reductase_like | cd06221 | Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ... |
270-490 | 5.00e-25 | |||||
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural similarity to ferredoxin reductase and sequence similarity to dihydroorotate dehydrogenases. Clostridium pasteurianum inducible dissimilatory type sulfite reductase is linked to ferredoxin and reduces NH2OH and SeO3 at a lesser rate than it's normal substate SO3(2-). Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. Pssm-ID: 99817 [Multi-domain] Cd Length: 253 Bit Score: 103.46 E-value: 5.00e-25
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| PRK00054 | PRK00054 | dihydroorotate dehydrogenase electron transfer subunit; Reviewed |
268-482 | 2.16e-24 | |||||
dihydroorotate dehydrogenase electron transfer subunit; Reviewed Pssm-ID: 234601 [Multi-domain] Cd Length: 250 Bit Score: 101.87 E-value: 2.16e-24
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| BenDO_FAD_NAD | cd06209 | Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ... |
265-491 | 7.22e-24 | |||||
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons using dioxygen as the oxidant. As a Class I bacterial dioxygenases, benzoate dioxygenase like proteins combine an [2Fe-2S] cluster containing N-terminal ferredoxin at the end fused to an FAD/NADP(P) domain. In dioxygenase FAD/NAD(P) binding domain, the reductase transfers 2 electrons from NAD(P)H to the oxygenase which insert into an aromatic substrate, an initial step in microbial aerobic degradation of aromatic rings. Flavin oxidoreductases use flavins as substrates, unlike flavoenzymes which have a flavin prosthetic group. Pssm-ID: 99805 [Multi-domain] Cd Length: 228 Bit Score: 99.59 E-value: 7.22e-24
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| monooxygenase_like | cd06212 | The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ... |
266-491 | 2.05e-23 | |||||
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. These flavoprotein monooxygenases use molecular oxygen as a substrate and require reduced FAD. One atom of oxygen is incorportated into the aromatic compond, while the other is used to form a molecule of water. In contrast dioxygenases add both atoms of oxygen to the substrate. Pssm-ID: 99808 [Multi-domain] Cd Length: 232 Bit Score: 98.56 E-value: 2.05e-23
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| FNR_iron_sulfur_binding_3 | cd06217 | Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
266-491 | 4.76e-23 | |||||
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap between the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH. Pssm-ID: 99813 [Multi-domain] Cd Length: 235 Bit Score: 97.72 E-value: 4.76e-23
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| PRK07609 | PRK07609 | CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated |
229-489 | 3.07e-22 | |||||
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated Pssm-ID: 181058 [Multi-domain] Cd Length: 339 Bit Score: 97.63 E-value: 3.07e-22
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| cyt_b5_reduct_like | cd06183 | Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ... |
269-490 | 3.56e-21 | |||||
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as an electron donor. Like ferredoxin reductases, these proteins have an N-terminal FAD binding subdomain and a C-terminal NADH binding subdomain, separated by a cleft, which accepts FAD. The NADH-binding moiety interacts with part of the FAD and resembles a Rossmann fold. However, NAD is bound differently than in canonical Rossmann fold proteins. Nitrate reductases, flavoproteins similar to pyridine nucleotide cytochrome reductases, catalyze the reduction of nitrate to nitrite. The enzyme can be divided into three functional fragments that bind the cofactors molybdopterin, heme-iron, and FAD/NADH. Pssm-ID: 99780 [Multi-domain] Cd Length: 234 Bit Score: 92.24 E-value: 3.56e-21
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| NADH_quinone_reductase | cd06188 | Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ... |
257-489 | 9.80e-21 | |||||
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) provides a means of storing redox reaction energy via the transmembrane translocation of Na2+ ions. The C-terminal domain resembles ferredoxin:NADP+ oxidoreductase, and has NADH and FAD binding sites. (Na+-NQR) is distinct from H+-translocating NADH:quinone oxidoreductases and noncoupled NADH:quinone oxidoreductases. The NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain of this group typically contains an iron-sulfur cluster binding domain. Pssm-ID: 99785 [Multi-domain] Cd Length: 283 Bit Score: 91.98 E-value: 9.80e-21
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| flavohem_like_fad_nad_binding | cd06184 | FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ... |
294-492 | 3.43e-20 | |||||
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain containing a B-type heme fused with a ferredoxin reductase-like FAD/NAD-binding domain. Flavohemoglobins detoxify nitric oxide (NO) via an NO dioxygenase reaction. The hemoglobin domain adopts a globin fold with an embedded heme molecule. Flavohemoglobins also have a C-terminal reductase domain with bindiing sites for FAD and NAD(P)H. This domain catalyzes the conversion of NO + O2 + NAD(P)H to NO3- + NAD(P)+. Instead of the oxygen transport function of hemoglobins, flavohemoglobins seem to act in NO dioxygenation and NO signalling. Pssm-ID: 99781 Cd Length: 247 Bit Score: 89.54 E-value: 3.43e-20
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| FNR_iron_sulfur_binding_2 | cd06216 | Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
268-486 | 7.72e-20 | |||||
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH. Pssm-ID: 99812 [Multi-domain] Cd Length: 243 Bit Score: 88.44 E-value: 7.72e-20
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| PA_degradation_oxidoreductase_like | cd06214 | NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ... |
294-491 | 9.79e-20 | |||||
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation oxidoreductase. PA oxidoreductases of E. coli hydroxylate PA-CoA in the second step of PA degradation. Members of this group typically fuse a ferredoxin reductase-like domain with an iron-sulfur binding cluster domain. Ferredoxins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal portion may contain a flavin prosthetic group, as in flavoenzymes, or use flavin as a substrate. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria and participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH. Pssm-ID: 99810 [Multi-domain] Cd Length: 241 Bit Score: 88.37 E-value: 9.79e-20
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| FNR_like_3 | cd06198 | NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ... |
294-491 | 4.38e-19 | |||||
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) domain, which varies in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH. Pssm-ID: 99795 [Multi-domain] Cd Length: 216 Bit Score: 85.77 E-value: 4.38e-19
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| FNR_iron_sulfur_binding | cd06191 | Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
268-491 | 5.96e-18 | |||||
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with a C-terminal iron-sulfur binding cluster domain. FNR was intially identified as a chloroplast reductase activity catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methnae assimilation in a variety of organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H). Pssm-ID: 99788 [Multi-domain] Cd Length: 231 Bit Score: 82.96 E-value: 5.96e-18
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| DHOD_e_trans_like | cd06192 | FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ... |
270-491 | 9.25e-17 | |||||
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as NAD binding. NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH. Pssm-ID: 99789 [Multi-domain] Cd Length: 243 Bit Score: 79.68 E-value: 9.25e-17
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| DHOD_e_trans_like2 | cd06220 | FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ... |
268-486 | 2.74e-16 | |||||
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster. Pssm-ID: 99816 [Multi-domain] Cd Length: 233 Bit Score: 78.06 E-value: 2.74e-16
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| FNR_N-term_Iron_sulfur_binding | cd06194 | Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
270-489 | 1.31e-15 | |||||
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an N-terminal Iron-Sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH. Pssm-ID: 99791 [Multi-domain] Cd Length: 222 Bit Score: 75.77 E-value: 1.31e-15
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| DHOD_e_trans_like1 | cd06219 | FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ... |
268-483 | 7.18e-15 | |||||
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as NAD binding. NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group, as in flavoenzymes, or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD, forming FADH2 via a semiquinone intermediate, and then transfers a hydride ion to convert NADP+ to NADPH. Pssm-ID: 99815 [Multi-domain] Cd Length: 248 Bit Score: 74.15 E-value: 7.18e-15
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| FNR_like_1 | cd06196 | Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ... |
283-491 | 1.04e-13 | |||||
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which varies in orientation with respect to the NAD(P) binding domain. The N-terminal region may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH. Pssm-ID: 99793 [Multi-domain] Cd Length: 218 Bit Score: 70.35 E-value: 1.04e-13
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| CYPOR_like_FNR | cd06208 | These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ... |
308-491 | 2.20e-13 | |||||
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but lack the FAD-binding region connecting sub-domain. Ferredoxin-NADP+ reductase (FNR) is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins, such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap between the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2, which then transfers two electrons and a proton to NADP+ to form NADPH. CYPOR serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases, sulfite reducatase, and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. CYPOR has a C-terminal FNR-like FAD and NAD binding module, an FMN-binding domain, and an additional connecting domain (inserted within the FAD binding region) that orients the FNR and FMN -binding domains. The C-terminal domain contains most of the NADP(H) binding residues, and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule, which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH. Pssm-ID: 99804 [Multi-domain] Cd Length: 286 Bit Score: 70.43 E-value: 2.20e-13
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| PRK08345 | PRK08345 | cytochrome-c3 hydrogenase subunit gamma; Provisional |
267-490 | 3.53e-13 | |||||
cytochrome-c3 hydrogenase subunit gamma; Provisional Pssm-ID: 236247 [Multi-domain] Cd Length: 289 Bit Score: 69.84 E-value: 3.53e-13
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| NOX_Duox_like_FAD_NADP | cd06186 | NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ... |
286-491 | 7.71e-13 | |||||
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as superoxide and hydrogen peroxide. ROS were originally identified as bactericidal agents in phagocytes, but are now also implicated in cell signaling and metabolism. NOX has a 6-alpha helix heme-binding transmembrane domain fused to a flavoprotein with the nucleotide binding domain located in the cytoplasm. Duox enzymes link a peroxidase domain to the NOX domain via a single transmembrane and EF-hand Ca2+ binding sites. The flavoprotein module has a ferredoxin like FAD/NADPH binding domain. In classical phagocytic NOX2, electron transfer occurs from NADPH to FAD to the heme of cytb to oxygen leading to superoxide formation. Pssm-ID: 99783 [Multi-domain] Cd Length: 210 Bit Score: 67.33 E-value: 7.71e-13
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| MMO_FAD_NAD_binding | cd06210 | Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ... |
267-491 | 8.78e-12 | |||||
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent hydroxylation of methane to methanol. This multicomponent enzyme mediates electron transfer via a hydroxylase (MMOH), a coupling protein, and a reductase which is comprised of an N-terminal [2Fe-2S] ferredoxin domain, an FAD binding subdomain, and an NADH binding subdomain. Oxygenases oxidize hydrocarbons using dioxygen as the oxidant. Dioxygenases add both atom of oxygen to the substrate, while mono-oxygenases add one atom to the substrate and one atom to water. Pssm-ID: 99806 Cd Length: 236 Bit Score: 65.06 E-value: 8.78e-12
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| PRK12778 | PRK12778 | bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
269-483 | 8.80e-12 | |||||
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase; Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 67.46 E-value: 8.80e-12
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| NAD_binding_1 | pfam00175 | Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ... |
374-476 | 2.04e-11 | |||||
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have essentially no similarity. Pssm-ID: 425503 [Multi-domain] Cd Length: 109 Bit Score: 60.74 E-value: 2.04e-11
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| PLN02252 | PLN02252 | nitrate reductase [NADPH] |
246-490 | 2.37e-11 | |||||
nitrate reductase [NADPH] Pssm-ID: 215141 [Multi-domain] Cd Length: 888 Bit Score: 66.24 E-value: 2.37e-11
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| PRK06222 | PRK06222 | sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein; |
269-462 | 9.50e-11 | |||||
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein; Pssm-ID: 235747 [Multi-domain] Cd Length: 281 Bit Score: 62.51 E-value: 9.50e-11
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| PRK10684 | PRK10684 | HCP oxidoreductase, NADH-dependent; Provisional |
295-491 | 1.72e-10 | |||||
HCP oxidoreductase, NADH-dependent; Provisional Pssm-ID: 236735 [Multi-domain] Cd Length: 332 Bit Score: 62.42 E-value: 1.72e-10
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| MtMvhB_like | cd10549 | Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
152-237 | 4.35e-10 | |||||
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction. Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 57.41 E-value: 4.35e-10
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| NapF | COG1145 | Ferredoxin [Energy production and conversion]; |
26-240 | 4.87e-10 | |||||
Ferredoxin [Energy production and conversion]; Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 59.74 E-value: 4.87e-10
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| DsrA | COG2221 | Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
184-238 | 1.10e-09 | |||||
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism]; Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 54.67 E-value: 1.10e-09
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| IorA | COG4231 | TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
173-242 | 1.38e-09 | |||||
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion]; Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 54.28 E-value: 1.38e-09
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| COG2768 | COG2768 | Uncharacterized Fe-S cluster protein [Function unknown]; |
184-240 | 1.64e-09 | |||||
Uncharacterized Fe-S cluster protein [Function unknown]; Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 54.35 E-value: 1.64e-09
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| NuoI | COG1143 | Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
185-244 | 5.15e-09 | |||||
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase Pssm-ID: 440758 [Multi-domain] Cd Length: 66 Bit Score: 52.44 E-value: 5.15e-09
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| RnfC | COG4656 | Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit [Energy production and ... |
187-255 | 1.02e-08 | |||||
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase Pssm-ID: 443694 [Multi-domain] Cd Length: 451 Bit Score: 57.46 E-value: 1.02e-08
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| COG1149 | COG1149 | MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
184-240 | 2.02e-08 | |||||
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only]; Pssm-ID: 440763 [Multi-domain] Cd Length: 68 Bit Score: 50.88 E-value: 2.02e-08
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| PDR_like | cd06185 | Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ... |
313-492 | 3.01e-08 | |||||
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron transfer from NADH to FMN to an iron sulfur cluster. PDR has an an N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding domain and a C-terminal iron-sulfur [2Fe-2S] cluster domain. Although structurally homologous to FNR, PDR binds FMN rather than FAD in it's FNR-like domain. Electron transfer between pyrimidines and iron-sulfur clusters (Rieske center [2Fe-2S]) or heme groups is mediated by flavins in respiration, photosynthesis, and oxygenase systems. Type I dioxygenase systems, including the hydroxylate phthalate system, have 2 components, a monomeric reductase consisting of a flavin and a 2Fe-2S center and a multimeric oxygenase. In contrast to other Rieske dioxygenases the ferredoxin like domain is C-, not N-terminal. Pssm-ID: 99782 [Multi-domain] Cd Length: 211 Bit Score: 54.03 E-value: 3.01e-08
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| FNR_like_2 | cd06197 | FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) ... |
278-419 | 3.36e-08 | |||||
FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and have a variety of physiological functions in a variety of organisms including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which varies in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one-electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and two electron carriers. FNR has a strong preference for NADP(H) vs NAD(H). Pssm-ID: 99794 Cd Length: 220 Bit Score: 53.93 E-value: 3.36e-08
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| Fer4_7 | pfam12838 | 4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
188-233 | 8.44e-08 | |||||
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters. Pssm-ID: 463724 [Multi-domain] Cd Length: 51 Bit Score: 48.68 E-value: 8.44e-08
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| MtMvhB_like | cd10549 | Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
182-241 | 9.51e-08 | |||||
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction. Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 50.86 E-value: 9.51e-08
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| Nar1 | COG4624 | Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
151-257 | 9.64e-08 | |||||
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 54.26 E-value: 9.64e-08
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| MtMvhB_like | cd10549 | Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
169-246 | 9.79e-08 | |||||
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction. Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 50.86 E-value: 9.79e-08
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| PRK12769 | PRK12769 | putative oxidoreductase Fe-S binding subunit; Reviewed |
188-252 | 9.91e-08 | |||||
putative oxidoreductase Fe-S binding subunit; Reviewed Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 54.37 E-value: 9.91e-08
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| rnfC | TIGR01945 | electron transport complex, RnfABCDGE type, C subunit; The six subunit complex RnfABCDGE in ... |
187-249 | 1.20e-07 | |||||
electron transport complex, RnfABCDGE type, C subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the C subunit. [Energy metabolism, Electron transport] Pssm-ID: 273888 [Multi-domain] Cd Length: 435 Bit Score: 53.89 E-value: 1.20e-07
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| Fer4_10 | pfam13237 | 4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
184-230 | 1.32e-07 | |||||
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich. Pssm-ID: 404174 [Multi-domain] Cd Length: 56 Bit Score: 48.40 E-value: 1.32e-07
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| PreA | COG1146 | NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
184-242 | 2.07e-07 | |||||
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism]; Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 48.17 E-value: 2.07e-07
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| PRK10926 | PRK10926 | ferredoxin-NADP reductase; Provisional |
360-480 | 5.27e-07 | |||||
ferredoxin-NADP reductase; Provisional Pssm-ID: 182844 Cd Length: 248 Bit Score: 50.85 E-value: 5.27e-07
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| Fer4_9 | pfam13187 | 4Fe-4S dicluster domain; |
187-234 | 9.12e-07 | |||||
4Fe-4S dicluster domain; Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 45.62 E-value: 9.12e-07
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| CYPOR_like | cd06182 | NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ... |
295-487 | 1.61e-06 | |||||
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. CYPOR has a C-terminal ferredoxin reducatase (FNR)- like FAD and NAD binding module, an FMN-binding domain, and an additional conecting domain (inserted within the FAD binding region) that orients the FNR and FMN binding domains. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria and participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2, which then transfers two electrons and a proton to NADP+ to form NADPH. Pssm-ID: 99779 [Multi-domain] Cd Length: 267 Bit Score: 49.64 E-value: 1.61e-06
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| PorD | COG1144 | Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ... |
184-241 | 1.92e-06 | |||||
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation Pssm-ID: 440759 [Multi-domain] Cd Length: 84 Bit Score: 45.81 E-value: 1.92e-06
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| PTZ00319 | PTZ00319 | NADH-cytochrome B5 reductase; Provisional |
264-489 | 2.50e-06 | |||||
NADH-cytochrome B5 reductase; Provisional Pssm-ID: 173521 [Multi-domain] Cd Length: 300 Bit Score: 49.06 E-value: 2.50e-06
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| Fer4_5 | pfam12801 | 4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ... |
36-82 | 5.66e-06 | |||||
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Pssm-ID: 432796 [Multi-domain] Cd Length: 48 Bit Score: 43.32 E-value: 5.66e-06
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| DMSOR_beta_like | cd16373 | uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
149-247 | 8.53e-06 | |||||
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system. Pssm-ID: 319895 [Multi-domain] Cd Length: 154 Bit Score: 45.71 E-value: 8.53e-06
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| PRK13289 | PRK13289 | NO-inducible flavohemoprotein; |
293-491 | 1.08e-05 | |||||
NO-inducible flavohemoprotein; Pssm-ID: 237337 [Multi-domain] Cd Length: 399 Bit Score: 47.49 E-value: 1.08e-05
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| napH | PRK09477 | quinol dehydrogenase membrane component; Provisional |
148-236 | 1.08e-05 | |||||
quinol dehydrogenase membrane component; Provisional Pssm-ID: 236535 [Multi-domain] Cd Length: 271 Bit Score: 47.20 E-value: 1.08e-05
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| DMSOR_beta_like | cd16369 | uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
194-241 | 1.14e-05 | |||||
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system. Pssm-ID: 319891 [Multi-domain] Cd Length: 172 Bit Score: 45.84 E-value: 1.14e-05
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| FDH-N | cd10558 | The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ... |
185-241 | 2.78e-05 | |||||
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS subunit of formate dehydrogenase-N (FDH-N), a member of the DMSO reductase family. FDH-N is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. Thus, FDH-N is a major component of nitrate respiration of Escherichia coli. This integral membrane enzyme forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. Pssm-ID: 319880 [Multi-domain] Cd Length: 208 Bit Score: 45.07 E-value: 2.78e-05
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| Fer4_8 | pfam13183 | 4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
187-233 | 2.81e-05 | |||||
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters. Pssm-ID: 433017 [Multi-domain] Cd Length: 64 Bit Score: 41.91 E-value: 2.81e-05
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| NapF_like | cd10564 | NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ... |
186-247 | 3.44e-05 | |||||
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system. Pssm-ID: 319886 [Multi-domain] Cd Length: 139 Bit Score: 43.77 E-value: 3.44e-05
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| PLN02844 | PLN02844 | oxidoreductase/ferric-chelate reductase |
288-414 | 3.63e-05 | |||||
oxidoreductase/ferric-chelate reductase Pssm-ID: 215453 [Multi-domain] Cd Length: 722 Bit Score: 46.38 E-value: 3.63e-05
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| PRK05035 | PRK05035 | electron transport complex protein RnfC; Provisional |
187-255 | 4.18e-05 | |||||
electron transport complex protein RnfC; Provisional Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.09 E-value: 4.18e-05
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| HycB | COG1142 | Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion]; |
188-246 | 5.53e-05 | |||||
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion]; Pssm-ID: 440757 [Multi-domain] Cd Length: 138 Bit Score: 43.11 E-value: 5.53e-05
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| PRK12809 | PRK12809 | putative oxidoreductase Fe-S binding subunit; Reviewed |
183-276 | 5.69e-05 | |||||
putative oxidoreductase Fe-S binding subunit; Reviewed Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 45.79 E-value: 5.69e-05
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| FDH_beta_like | cd16366 | beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ... |
185-239 | 6.66e-05 | |||||
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family contains beta FeS subunits of several dehydrogenases in the DMSO reductase superfamily, including formate dehydrogenase N (FDH-N), tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N is a major component of nitrate respiration of Escherichia coli; it catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate to a cytochrome. W-FDH contains a tungsten instead of molybdenum at the catalytic center and seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate. Pssm-ID: 319888 [Multi-domain] Cd Length: 156 Bit Score: 43.16 E-value: 6.66e-05
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| PRK09898 | PRK09898 | ferredoxin-like protein; |
186-241 | 7.52e-05 | |||||
ferredoxin-like protein; Pssm-ID: 182135 [Multi-domain] Cd Length: 208 Bit Score: 44.06 E-value: 7.52e-05
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| PRK08348 | PRK08348 | NADH-plastoquinone oxidoreductase subunit; Provisional |
184-251 | 7.61e-05 | |||||
NADH-plastoquinone oxidoreductase subunit; Provisional Pssm-ID: 181399 [Multi-domain] Cd Length: 120 Bit Score: 42.13 E-value: 7.61e-05
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| PRK09898 | PRK09898 | ferredoxin-like protein; |
153-249 | 7.66e-05 | |||||
ferredoxin-like protein; Pssm-ID: 182135 [Multi-domain] Cd Length: 208 Bit Score: 43.67 E-value: 7.66e-05
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| SIMIBI_bact_arch | cd03110 | bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ... |
184-240 | 8.03e-05 | |||||
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown. Pssm-ID: 349764 [Multi-domain] Cd Length: 246 Bit Score: 44.30 E-value: 8.03e-05
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| FDH_b_like | cd10562 | uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ... |
185-243 | 9.19e-05 | |||||
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes the beta-subunit of formate dehydrogenases that are as yet uncharacterized. Members of the DMSO reductase family include formate dehydrogenase N and O (FDH-N, FDH-O) and tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N, a major component of nitrate respiration of Escherichia coli, is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. It forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. W-FDH contains a tungsten instead of molybdenum at the catalytic center. This enzyme seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It is a heterodimer of a large and a small subunit; the large subunit harbors the W site and one [4Fe-4S] center and the small subunit, containing three [4Fe-4S] clusters, functions to transfer electrons. Pssm-ID: 319884 [Multi-domain] Cd Length: 161 Bit Score: 43.06 E-value: 9.19e-05
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| ferrodoxin_EFR1 | NF038196 | EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ... |
154-246 | 1.10e-04 | |||||
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1). Pssm-ID: 468407 [Multi-domain] Cd Length: 243 Bit Score: 43.69 E-value: 1.10e-04
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| PRK07118 | PRK07118 | Fe-S cluster domain-containing protein; |
135-254 | 1.65e-04 | |||||
Fe-S cluster domain-containing protein; Pssm-ID: 235941 [Multi-domain] Cd Length: 280 Bit Score: 43.38 E-value: 1.65e-04
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| PFLE_PFLC | TIGR02494 | glycyl-radical enzyme activating protein; This subset of the radical-SAM family (pfam04055) ... |
184-244 | 1.77e-04 | |||||
glycyl-radical enzyme activating protein; This subset of the radical-SAM family (pfam04055) includes a number of probable activating proteins acting on different enzymes all requiring an amino-acid-centered radical. The closest relatives to this family are the pyruvate-formate lyase activating enzyme (PflA, 1.97.1.4, TIGR02493) and the anaerobic ribonucleotide reductase activating enzyme (TIGR02491). Included within this subfamily are activators of hydroxyphenyl acetate decarboxylase (HdpA), benzylsuccinate synthase (BssD), gycerol dehydratase (DhaB2) as well as enzymes annotated in E. coli as activators of different isozymes of pyruvate-formate lyase (PFLC and PFLE) however, these appear to lack characterization and may activate enzymes with distinctive functions. Most of the sequence-level variability between these forms is concentrated within an N-terminal domain which follows a conserved group of three cysteines and contains a variable pattern of 0 to 8 additional cysteines. Pssm-ID: 274163 [Multi-domain] Cd Length: 295 Bit Score: 43.48 E-value: 1.77e-04
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| DMSOR_beta_like | cd16372 | uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
153-237 | 2.26e-04 | |||||
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system. Pssm-ID: 319894 [Multi-domain] Cd Length: 125 Bit Score: 41.17 E-value: 2.26e-04
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| HdrA | COG1148 | Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
169-237 | 2.74e-04 | |||||
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 43.31 E-value: 2.74e-04
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| HybA | COG0437 | Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ... |
185-244 | 3.60e-04 | |||||
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion]; Pssm-ID: 440206 [Multi-domain] Cd Length: 184 Bit Score: 41.47 E-value: 3.60e-04
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| SiR_like2 | cd06201 | Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ... |
366-480 | 5.00e-04 | |||||
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta subunits to catalyze the NADPH dependent reduction of sulfite to sulfide. Beta subunits have an Fe4S4 cluster and a siroheme, while the alpha subunits (cysJ gene) are of the cytochrome p450 (CyPor) family having FAD and FMN as prosthetic groups and utilizing NADPH. Cypor (including cyt -450 reductase, nitric oxide synthase, and methionine synthase reductase) are ferredoxin reductase (FNR)-like proteins with an additional N-terminal FMN domain and a connecting sub-domain inserted within the flavin binding portion of the FNR-like domain. The connecting domain orients the N-terminal FMN domain with the C-terminal FNR domain. NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH. Pssm-ID: 99798 [Multi-domain] Cd Length: 289 Bit Score: 41.93 E-value: 5.00e-04
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| Fer4_17 | pfam13534 | 4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
187-233 | 6.15e-04 | |||||
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich. Pssm-ID: 433287 [Multi-domain] Cd Length: 61 Bit Score: 38.21 E-value: 6.15e-04
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| Fer4_17 | pfam13534 | 4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
154-203 | 6.65e-04 | |||||
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich. Pssm-ID: 433287 [Multi-domain] Cd Length: 61 Bit Score: 37.83 E-value: 6.65e-04
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| PRK12775 | PRK12775 | putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
296-483 | 6.80e-04 | |||||
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 42.24 E-value: 6.80e-04
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| HdrC | COG1150 | Heterodisulfide reductase, subunit C [Energy production and conversion]; |
187-233 | 6.94e-04 | |||||
Heterodisulfide reductase, subunit C [Energy production and conversion]; Pssm-ID: 440764 [Multi-domain] Cd Length: 79 Bit Score: 38.34 E-value: 6.94e-04
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| Nitric_oxide_synthase | cd06202 | The ferredoxin-reductase (FNR) like C-terminal domain of the nitric oxide synthase (NOS) fuses ... |
373-487 | 9.48e-04 | |||||
The ferredoxin-reductase (FNR) like C-terminal domain of the nitric oxide synthase (NOS) fuses with a heme-containing N-terminal oxidase domain. The reductase portion is similar in structure to NADPH dependent cytochrome-450 reductase (CYPOR), having an inserted connecting sub-domain within the FAD binding portion of FNR. NOS differs from CYPOR in a requirement for the cofactor tetrahydrobiopterin and unlike most CYPOR is dimeric. Nitric oxide synthase produces nitric oxide in the conversion of L-arginine to L-citruline. NOS has been implicated in a variety of processes including cytotoxicity, anti-inflamation, neurotransmission, and vascular smooth muscle relaxation. Pssm-ID: 99799 [Multi-domain] Cd Length: 406 Bit Score: 41.55 E-value: 9.48e-04
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| methionine_synthase_red | cd06203 | Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for ... |
372-475 | 1.05e-03 | |||||
Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for the regeneration of methionine from homocysteine, as well as the coversion of methyltetrahydrofolate to tetrahydrofolate. In MSR, electrons are transferred from NADPH to FAD to FMN to cob(II)alamin. MSR resembles proteins of the cytochrome p450 family including nitric oxide synthase, the alpha subunit of sulfite reductase, but contains an extended hinge region. NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. CYPORs resemble ferredoxin reductase (FNR) but have a connecting subdomain inserted within the flavin binding region, which helps orient the FMN binding doamin with the FNR module. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH. Pssm-ID: 99800 [Multi-domain] Cd Length: 398 Bit Score: 41.54 E-value: 1.05e-03
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| PreA | COG1146 | NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
153-199 | 1.16e-03 | |||||
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism]; Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 37.38 E-value: 1.16e-03
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| FDH-O_like | cd10560 | beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ... |
186-239 | 1.27e-03 | |||||
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes beta subunit of formate dehydrogenase family O (FDH-O), which is highly homologous to formate dehydrogenase N (FDH-N), a member of the DMSO reductase family. In E. coli three formate dehydrogenases are synthesized that are capable of oxidizing formate; Fdh-H, couples formate disproportionation to hydrogen and CO2, and is part of the cytoplasmically oriented formate hydrogenlyase complex, while FDH-N and FDH-O indicate their respective induction after growth with nitrate and oxygen. Little is known about FDH-O, although it shows formate oxidase activity during aerobic growth and is also synthesized during nitrate respiration, similar to FDH-N. Pssm-ID: 319882 [Multi-domain] Cd Length: 225 Bit Score: 40.45 E-value: 1.27e-03
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| PLN00071 | PLN00071 | photosystem I subunit VII; Provisional |
186-236 | 1.56e-03 | |||||
photosystem I subunit VII; Provisional Pssm-ID: 177700 [Multi-domain] Cd Length: 81 Bit Score: 37.62 E-value: 1.56e-03
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| DMSOR_beta_like | cd16373 | uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
187-241 | 1.68e-03 | |||||
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system. Pssm-ID: 319895 [Multi-domain] Cd Length: 154 Bit Score: 39.16 E-value: 1.68e-03
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| Fer4_6 | pfam12837 | 4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ... |
184-202 | 1.73e-03 | |||||
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Pssm-ID: 432822 [Multi-domain] Cd Length: 24 Bit Score: 35.67 E-value: 1.73e-03
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| HycB_like | cd10554 | HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ... |
187-255 | 2.00e-03 | |||||
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation. Pssm-ID: 319876 [Multi-domain] Cd Length: 149 Bit Score: 38.78 E-value: 2.00e-03
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| vorD | PRK09623 | 3-methyl-2-oxobutanoate dehydrogenase subunit delta; |
182-241 | 2.33e-03 | |||||
3-methyl-2-oxobutanoate dehydrogenase subunit delta; Pssm-ID: 170016 [Multi-domain] Cd Length: 105 Bit Score: 37.62 E-value: 2.33e-03
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| DMSOR_beta_like | cd16370 | uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
184-238 | 2.54e-03 | |||||
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system. Pssm-ID: 319892 [Multi-domain] Cd Length: 131 Bit Score: 38.02 E-value: 2.54e-03
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| DMSOR_beta-like | cd04410 | Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ... |
150-234 | 2.56e-03 | |||||
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system. Pssm-ID: 319870 [Multi-domain] Cd Length: 136 Bit Score: 38.14 E-value: 2.56e-03
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| napF | TIGR00402 | ferredoxin-type protein NapF; The gene codes for a ferredoxin-type cytosolic protein, NapF, of ... |
188-235 | 2.71e-03 | |||||
ferredoxin-type protein NapF; The gene codes for a ferredoxin-type cytosolic protein, NapF, of the periplasmic nitrate reductase system, as in Escherichia coli. NapF interacts with the catalytic subunit, NapA, and may be an accessory protein for NapA maturation. [Energy metabolism, Electron transport] Pssm-ID: 273060 [Multi-domain] Cd Length: 101 Bit Score: 37.23 E-value: 2.71e-03
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| RDH | TIGR02486 | reductive dehalogenase; This model represents a family of corrin and 8-iron Fe-S ... |
188-230 | 2.83e-03 | |||||
reductive dehalogenase; This model represents a family of corrin and 8-iron Fe-S cluster-containing reductive dehalogenases found primarily in halorespiring microorganisms such as dehalococcoides ethenogenes which contains as many as 17 enzymes of this type with varying substrate ranges. One example of a characterized species is the tetrachloroethene reductive dehalogenase (1.97.1.8) which also acts on trichloroethene converting it to dichloroethene. Pssm-ID: 274158 Cd Length: 314 Bit Score: 39.73 E-value: 2.83e-03
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| Fer4_9 | pfam13187 | 4Fe-4S dicluster domain; |
151-202 | 2.90e-03 | |||||
4Fe-4S dicluster domain; Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 35.99 E-value: 2.90e-03
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| NAD_binding_6 | pfam08030 | Ferric reductase NAD binding domain; |
372-414 | 3.04e-03 | |||||
Ferric reductase NAD binding domain; Pssm-ID: 429792 [Multi-domain] Cd Length: 149 Bit Score: 38.09 E-value: 3.04e-03
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| Fer4_8 | pfam13183 | 4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
151-202 | 3.37e-03 | |||||
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters. Pssm-ID: 433017 [Multi-domain] Cd Length: 64 Bit Score: 36.13 E-value: 3.37e-03
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| oorD | PRK09626 | 2-oxoglutarate-acceptor oxidoreductase subunit OorD; Reviewed |
215-249 | 3.44e-03 | |||||
2-oxoglutarate-acceptor oxidoreductase subunit OorD; Reviewed Pssm-ID: 236597 [Multi-domain] Cd Length: 103 Bit Score: 37.01 E-value: 3.44e-03
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| Fer4_6 | pfam12837 | 4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ... |
213-234 | 4.44e-03 | |||||
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Pssm-ID: 432822 [Multi-domain] Cd Length: 24 Bit Score: 34.51 E-value: 4.44e-03
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| FDH-N | cd10558 | The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ... |
184-254 | 4.45e-03 | |||||
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS subunit of formate dehydrogenase-N (FDH-N), a member of the DMSO reductase family. FDH-N is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. Thus, FDH-N is a major component of nitrate respiration of Escherichia coli. This integral membrane enzyme forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. Pssm-ID: 319880 [Multi-domain] Cd Length: 208 Bit Score: 38.52 E-value: 4.45e-03
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| Nar1 | COG4624 | Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
176-243 | 5.22e-03 | |||||
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 39.24 E-value: 5.22e-03
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| CooF_like | cd10563 | CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ... |
188-243 | 9.29e-03 | |||||
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the iron-sulfur subunit of carbon monoxide dehydrogenase (CODH), found in anaerobic bacteria and archaea. Carbon monoxide dehydrogenase is a key enzyme for carbon monoxide (CO) metabolism, where CooF is the proposed mediator of electron transfer between CODH and the CO-induced hydrogenase, catalyzing the reaction that uses CO as a single carbon and energy source, and producing only H2 and CO2. The ion-sulfur subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons in the protein complex during reaction. Pssm-ID: 319885 [Multi-domain] Cd Length: 140 Bit Score: 36.46 E-value: 9.29e-03
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