NO-inducible flavohemoprotein [Vibrio breoganii]
Protein Classification
NO-inducible flavohemoprotein( domain architecture ID 11486532)
NO-inducible flavohemoprotein such as nitric oxide dioxygenase, which catalyzes the conversion of NO, O2, and NAD(P)H to NO3-, NAD(P)+, and H+, and is involved NO detoxification and NO signaling
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| PRK13289 | PRK13289 | NO-inducible flavohemoprotein; |
1-394 | 0e+00 | ||||||
NO-inducible flavohemoprotein; : Pssm-ID: 237337 [Multi-domain] Cd Length: 399 Bit Score: 715.04 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | ||||||
| PRK13289 | PRK13289 | NO-inducible flavohemoprotein; |
1-394 | 0e+00 | ||||||
NO-inducible flavohemoprotein; Pssm-ID: 237337 [Multi-domain] Cd Length: 399 Bit Score: 715.04 E-value: 0e+00
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| flavohem_like_fad_nad_binding | cd06184 | FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ... |
147-391 | 1.67e-132 | ||||||
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: 379.59 E-value: 1.67e-132
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| Fpr | COG1018 | Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; |
150-386 | 2.28e-80 | ||||||
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; Pssm-ID: 440641 [Multi-domain] Cd Length: 231 Bit Score: 246.24 E-value: 2.28e-80
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| Globin | pfam00042 | Globin; |
26-129 | 4.64e-16 | ||||||
Globin; Pssm-ID: 459646 [Multi-domain] Cd Length: 117 Bit Score: 73.86 E-value: 4.64e-16
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| Name | Accession | Description | Interval | E-value | ||||||
| PRK13289 | PRK13289 | NO-inducible flavohemoprotein; |
1-394 | 0e+00 | ||||||
NO-inducible flavohemoprotein; Pssm-ID: 237337 [Multi-domain] Cd Length: 399 Bit Score: 715.04 E-value: 0e+00
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| flavohem_like_fad_nad_binding | cd06184 | FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ... |
147-391 | 1.67e-132 | ||||||
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: 379.59 E-value: 1.67e-132
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| HmpEc-globin-like | cd14776 | Globin domain of Escherichia coli flavohemoglobin (Hmp) and related proteins; Flavohemoglobins ... |
2-139 | 1.12e-80 | ||||||
Globin domain of Escherichia coli flavohemoglobin (Hmp) and related proteins; Flavohemoglobins (flavoHbs) function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. This subfamily includes Vibrio fischeri Hmp and E.coli Hmp. NO scavenging by flavoHb affects the swarming behavior of Escherichia coli, and protects against NO during initiation of the squid-Vibrio symbiosis. E.coli Hmp can catalyze the reduction of several alkylhydroperoxide substrates into their corresponding alcohols using NADH as an electron donor, and it has been suggested that it participates in the repair of the lipid membrane oxidative damage generated during oxidative/nitrosative stress. Pssm-ID: 271309 Cd Length: 138 Bit Score: 243.91 E-value: 1.12e-80
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| Fpr | COG1018 | Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; |
150-386 | 2.28e-80 | ||||||
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; Pssm-ID: 440641 [Multi-domain] Cd Length: 231 Bit Score: 246.24 E-value: 2.28e-80
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| FHb-globin | cd08922 | Globin domain of flavohemoglobins (flavoHbs); FlavoHbs function primarily as nitric oxide ... |
2-139 | 1.53e-71 | ||||||
Globin domain of flavohemoglobins (flavoHbs); FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. NO scavenging by flavoHb attenuates the expression of the nitrosative stress response, affects the swarming behavior of Escherichia coli, and maintains squid-Vibrio fischeri and Medicago truncatula-Sinorhizobium meliloti symbioses. FlavoHb expression affects Aspergillus nidulans sexual development and mycotoxin production, and Dictyostelium discoideum development. This family also includes some single-domain goblins (SDgbs). Pssm-ID: 381260 Cd Length: 140 Bit Score: 220.53 E-value: 1.53e-71
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| Hmp | COG1017 | Hemoglobin-like flavoprotein [Energy production and conversion]; |
2-137 | 2.71e-62 | ||||||
Hemoglobin-like flavoprotein [Energy production and conversion]; Pssm-ID: 440640 [Multi-domain] Cd Length: 135 Bit Score: 196.53 E-value: 2.71e-62
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| FHP_Ae-globin-like | cd14779 | Globin domain of Alcaligenes eutrophus flavohemoglobin (FHP) and related proteins; ... |
2-139 | 7.96e-59 | ||||||
Globin domain of Alcaligenes eutrophus flavohemoglobin (FHP) and related proteins; Flavohemoglobins (flavoHbs) function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. NO scavenging by flavoHb maintains Medicago truncatula-Sinorhizobium meliloti symbiosis. Alcaligenes eutrophus FHP contains a phospholipid-binding site. Pssm-ID: 381287 Cd Length: 140 Bit Score: 187.65 E-value: 7.96e-59
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| Yhb1-globin-like | cd14777 | Globin domain of Saccharomyces cerevisiae flavohemoglobin (Yhb1p) and related domains; ... |
2-139 | 5.02e-57 | ||||||
Globin domain of Saccharomyces cerevisiae flavohemoglobin (Yhb1p) and related domains; FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. S. cerevisiae Yhb1p has been shown to protect against nitrosative stress and to control ferric reductase activity; it may participate in regulating the activity of plasma membrane ferric reductase(s). Also included in this subfamily is Dictyostelium discoideum FlavoHb, the expression of which affects D. discoideum development. Pssm-ID: 381285 Cd Length: 140 Bit Score: 183.31 E-value: 5.02e-57
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| FHb-globin_3 | cd14783 | Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function ... |
2-139 | 6.39e-57 | ||||||
Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. Pssm-ID: 271316 Cd Length: 140 Bit Score: 183.05 E-value: 6.39e-57
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| VtHb-like_SDgb | cd14778 | Vitreoscilla stercoraria hemoglobin and related proteins; single-domain globins; VtHb is ... |
2-139 | 1.17e-47 | ||||||
Vitreoscilla stercoraria hemoglobin and related proteins; single-domain globins; VtHb is homodimeric, and may both transport oxygen to terminal respiratory oxidases, and provide resistance to nitrosative stress. It has medium oxygen affinity and displays cooperative ligand-binding properties. VHb has biotechnological application, its expression in heterologous hosts (bacteria and plants) has improved growth and productivity under microaerobic conditions. Another member of this subfamily Campylobacter jejuni hemoglobin (Cgb) is monomeric, and plays a role in detoxifying NO. Along with a truncated globin Ctb, it is up-regulated by the transcription factor NssR in response to nitrosative stress. Pssm-ID: 381286 [Multi-domain] Cd Length: 140 Bit Score: 159.13 E-value: 1.17e-47
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| FHb-globin_1 | cd14781 | Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function ... |
2-139 | 2.44e-47 | ||||||
Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. This subfamily may contain some single-domain goblins (SDgbs). Pssm-ID: 381289 Cd Length: 139 Bit Score: 158.02 E-value: 2.44e-47
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| FNR_like | cd00322 | Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ... |
158-386 | 7.14e-46 | ||||||
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: 157.22 E-value: 7.14e-46
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| HmpPa-globin-like | cd14780 | Globin domain of Pseudomonas aeruginosa flavohemoglobin (HmpPa) and related proteins; ... |
2-139 | 9.09e-46 | ||||||
Globin domain of Pseudomonas aeruginosa flavohemoglobin (HmpPa) and related proteins; Flavohemoglobins (flavoHbs) function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. The physiological role of HmpPa is thought to be detoxification of NO under aerobic conditions. Pssm-ID: 381288 Cd Length: 140 Bit Score: 154.15 E-value: 9.09e-46
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| FNR_iron_sulfur_binding_1 | cd06215 | Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
169-388 | 1.35e-44 | ||||||
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: 153.90 E-value: 1.35e-44
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| FNR_iron_sulfur_binding_2 | cd06216 | Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
149-388 | 1.57e-42 | ||||||
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: 148.91 E-value: 1.57e-42
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| PA_degradation_oxidoreductase_like | cd06214 | NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ... |
154-389 | 4.25e-40 | ||||||
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: 142.68 E-value: 4.25e-40
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| FHb_fungal-globin | cd19754 | Globin domain of fungal flavohemoglobin; FlavoHbs function primarily as nitric oxide ... |
2-139 | 5.39e-39 | ||||||
Globin domain of fungal flavohemoglobin; FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. NO scavenging by flavoHb attenuates the expression of the nitrosative stress response, affects the swarming behavior of Escherichia coli, and maintains squid-Vibrio fischeri and Medicago truncatula-Sinorhizobium meliloti symbioses. FlavoHb expression affects Aspergillus nidulans sexual development and mycotoxin production, and Dictyostelium discoideum development. Pssm-ID: 381294 Cd Length: 141 Bit Score: 136.31 E-value: 5.39e-39
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| PDR_like | cd06185 | Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ... |
158-389 | 6.06e-39 | ||||||
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: 138.38 E-value: 6.06e-39
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| FNR_iron_sulfur_binding_3 | cd06217 | Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
149-388 | 5.67e-33 | ||||||
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: 123.53 E-value: 5.67e-33
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| FHb-globin_2 | cd14782 | Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function ... |
9-139 | 1.47e-31 | ||||||
Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. Pssm-ID: 381290 Cd Length: 143 Bit Score: 116.73 E-value: 1.47e-31
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| FNR_iron_sulfur_binding | cd06191 | Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
156-388 | 6.41e-29 | ||||||
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: 112.62 E-value: 6.41e-29
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| O2ase_reductase_like | cd06187 | The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ... |
157-388 | 8.00e-26 | ||||||
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: 103.83 E-value: 8.00e-26
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| COG4097 | COG4097 | Predicted ferric reductase [Inorganic ion transport and metabolism]; |
149-388 | 2.99e-25 | ||||||
Predicted ferric reductase [Inorganic ion transport and metabolism]; Pssm-ID: 443273 [Multi-domain] Cd Length: 442 Bit Score: 106.52 E-value: 2.99e-25
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| Mcr1 | COG0543 | NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ... |
156-383 | 9.64e-24 | ||||||
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; Pssm-ID: 440309 [Multi-domain] Cd Length: 247 Bit Score: 98.78 E-value: 9.64e-24
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| phenol_2-monooxygenase_like | cd06211 | Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ... |
152-388 | 2.16e-22 | ||||||
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: 94.70 E-value: 2.16e-22
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| BenDO_FAD_NAD | cd06209 | Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ... |
158-388 | 3.50e-22 | ||||||
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: 93.81 E-value: 3.50e-22
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| flavin_oxioreductase | cd06189 | NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ... |
182-383 | 5.92e-22 | ||||||
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: 93.00 E-value: 5.92e-22
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| FNR_like_3 | cd06198 | NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ... |
163-388 | 9.22e-22 | ||||||
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: 92.32 E-value: 9.22e-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 ... |
155-382 | 1.07e-18 | ||||||
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: 84.16 E-value: 1.07e-18
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| NADH_quinone_reductase | cd06188 | Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ... |
154-388 | 1.09e-17 | ||||||
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: 82.35 E-value: 1.09e-17
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| NqrF | COG2871 | Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ... |
154-390 | 1.95e-17 | ||||||
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and conversion]; Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF is part of the Pathway/BioSystem: Na+-translocating NADH dehydrogenase Pssm-ID: 442118 [Multi-domain] Cd Length: 396 Bit Score: 82.99 E-value: 1.95e-17
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| Mb-like_oxidoreductase | cd19753 | Globin domain of uncharacterized oxidoreductases containing a FAD/NADH binding domain; This ... |
10-128 | 3.49e-17 | ||||||
Globin domain of uncharacterized oxidoreductases containing a FAD/NADH binding domain; This subfamily is composed of uncharacterized proteins containing an N-terminal myoglobin-like (M family globin) domain and a C-terminal oxygenase reductase FAD/NADH binding domain belonging to the ferredoxin reductase (FNR) family and is usually part of multi-component bacterial oxygenases which oxidize hydrocarbons using oxygen as the oxidant. The domain architecture of this subfamily is similar to flavohemoglobins, which function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. NO scavenging by flavoHb attenuates the expression of the nitrosative stress response, affects the swarming behavior of Escherichia coli, and maintains squid-Vibrio fischeri and Medicago truncatula-Sinorhizobium meliloti symbioses. Pssm-ID: 381293 [Multi-domain] Cd Length: 121 Bit Score: 76.90 E-value: 3.49e-17
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| oxygenase_e_transfer_subunit | cd06213 | The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ... |
183-388 | 1.74e-16 | ||||||
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: 77.74 E-value: 1.74e-16
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| HGbI-like | cd12131 | Hell's gate globin I (HGbI) from Methylacidophilum infernorum and related proteins; HGbI is a ... |
6-132 | 1.75e-16 | ||||||
Hell's gate globin I (HGbI) from Methylacidophilum infernorum and related proteins; HGbI is a single-domain heme-containing protein isolated from Methylacidiphilum infernorum, an aerobic acidophilic and thermophilic methanotroph. M. infernorum grows optimally at pH 2.0 and 60C and its home is New Zealand's Hell's Gate geothermal park. The physiological role of HGbI has yet to be determined. It has an extremely strong resistance to auto-oxidation, and has fast oxygen-binding/slow release characteristics. Its CO on-rate is comparable to the O2 on-rate, and it is able to bind acetate with high affinity in the ferric state. The coordination of the heme iron changes in the ferrous form from pentacoordinate at low pH to predominantly hexacoordinate at high pH; in the ferric form, it is predominantly hexacoordinate at all pH. Pssm-ID: 381269 [Multi-domain] Cd Length: 128 Bit Score: 75.28 E-value: 1.75e-16
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| monooxygenase_like | cd06212 | The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ... |
175-388 | 4.10e-16 | ||||||
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: 76.99 E-value: 4.10e-16
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| Globin | pfam00042 | Globin; |
26-129 | 4.64e-16 | ||||||
Globin; Pssm-ID: 459646 [Multi-domain] Cd Length: 117 Bit Score: 73.86 E-value: 4.64e-16
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| NAD_binding_1 | pfam00175 | Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ... |
264-371 | 1.08e-15 | ||||||
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: 72.29 E-value: 1.08e-15
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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 ... |
182-373 | 5.70e-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: 73.46 E-value: 5.70e-15
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| Mb-like | cd01040 | myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ... |
10-131 | 2.68e-14 | ||||||
myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) and single-domain globins: FHbs, Ngbs/neuroglobins, Cygb/cytoglobins, GbE/avian eye specific globin E, GbX/globin X, amphibian GbY/globin Y, Mb/myoglobin, HbA/hemoglobin-alpha, HbB/hemoglobin-beta, SDgbs/single-domain globins related to FHbs, and Adgb/androglobin. The M family exhibits the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments (named A through H). In Adgbs, the globin domain is split into two: helices C-H are followed by helices A-B and the two parts are separated by the IQ motif. Although rearranged, the globin domain of most Adgbs contains a number of conserved residues which play critical roles in heme-coordination and gas ligand binding. Adgbs have been omitted from this A-H helix cd. Pssm-ID: 381254 Cd Length: 133 Bit Score: 69.41 E-value: 2.68e-14
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| antC | PRK11872 | anthranilate 1,2-dioxygenase electron transfer component AntC; |
182-389 | 4.94e-14 | ||||||
anthranilate 1,2-dioxygenase electron transfer component AntC; Pssm-ID: 183350 [Multi-domain] Cd Length: 340 Bit Score: 72.47 E-value: 4.94e-14
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| T4MO_e_transfer_like | cd06190 | Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ... |
181-389 | 3.60e-13 | ||||||
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: 68.43 E-value: 3.60e-13
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| MMO_FAD_NAD_binding | cd06210 | Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ... |
173-388 | 8.43e-13 | ||||||
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: 67.37 E-value: 8.43e-13
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| FNR_like_1 | cd06196 | Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ... |
182-386 | 1.81e-12 | ||||||
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: 66.11 E-value: 1.81e-12
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| sulfite_reductase_like | cd06221 | Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ... |
157-382 | 6.09e-12 | ||||||
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: 65.32 E-value: 6.09e-12
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| PRK10684 | PRK10684 | HCP oxidoreductase, NADH-dependent; Provisional |
183-390 | 1.06e-11 | ||||||
HCP oxidoreductase, NADH-dependent; Provisional Pssm-ID: 236735 [Multi-domain] Cd Length: 332 Bit Score: 65.50 E-value: 1.06e-11
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| FNR1 | cd06195 | Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ... |
170-381 | 4.97e-11 | ||||||
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: 62.20 E-value: 4.97e-11
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| PRK07609 | PRK07609 | CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated |
182-300 | 6.89e-11 | ||||||
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated Pssm-ID: 181058 [Multi-domain] Cd Length: 339 Bit Score: 62.97 E-value: 6.89e-11
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| SiR_like2 | cd06201 | Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ... |
172-278 | 5.88e-10 | ||||||
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: 59.65 E-value: 5.88e-10
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| FNR_like_2 | cd06197 | FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) ... |
163-369 | 1.31e-09 | ||||||
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: 57.79 E-value: 1.31e-09
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| PRK00054 | PRK00054 | dihydroorotate dehydrogenase electron transfer subunit; Reviewed |
156-311 | 7.60e-09 | ||||||
dihydroorotate dehydrogenase electron transfer subunit; Reviewed Pssm-ID: 234601 [Multi-domain] Cd Length: 250 Bit Score: 56.03 E-value: 7.60e-09
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| PRK08345 | PRK08345 | cytochrome-c3 hydrogenase subunit gamma; Provisional |
183-383 | 2.41e-08 | ||||||
cytochrome-c3 hydrogenase subunit gamma; Provisional Pssm-ID: 236247 [Multi-domain] Cd Length: 289 Bit Score: 54.81 E-value: 2.41e-08
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| CYPOR_like_FNR | cd06208 | These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ... |
186-361 | 1.79e-07 | ||||||
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: 52.32 E-value: 1.79e-07
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| DHOD_e_trans_like2 | cd06220 | FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ... |
155-377 | 2.48e-07 | ||||||
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: 51.09 E-value: 2.48e-07
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| CYPOR_like | cd06182 | NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ... |
178-302 | 1.39e-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: 49.26 E-value: 1.39e-06
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| SiR_like1 | cd06200 | Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ... |
204-302 | 5.92e-06 | ||||||
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: 99797 Cd Length: 245 Bit Score: 47.27 E-value: 5.92e-06
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| bifunctional_CYPOR | cd06206 | These bifunctional proteins fuse N-terminal cytochrome p450 with a cytochrome p450 reductase ... |
204-287 | 9.54e-06 | ||||||
These bifunctional proteins fuse N-terminal cytochrome p450 with a cytochrome p450 reductase (CYPOR). NADPH cytochrome p450 reductase 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: 99802 [Multi-domain] Cd Length: 384 Bit Score: 47.25 E-value: 9.54e-06
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| YjbI | COG2346 | Truncated hemoglobin YjbI [Inorganic ion transport and metabolism]; |
23-134 | 5.39e-05 | ||||||
Truncated hemoglobin YjbI [Inorganic ion transport and metabolism]; Pssm-ID: 441915 Cd Length: 120 Bit Score: 42.16 E-value: 5.39e-05
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| FAD_binding_6 | pfam00970 | Oxidoreductase FAD-binding domain; |
154-253 | 5.49e-05 | ||||||
Oxidoreductase FAD-binding domain; Pssm-ID: 425968 [Multi-domain] Cd Length: 99 Bit Score: 41.80 E-value: 5.49e-05
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| fre | PRK08051 | FMN reductase; Validated |
182-286 | 2.02e-04 | ||||||
FMN reductase; Validated Pssm-ID: 236142 [Multi-domain] Cd Length: 232 Bit Score: 42.53 E-value: 2.02e-04
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| PLN02844 | PLN02844 | oxidoreductase/ferric-chelate reductase |
156-281 | 2.40e-04 | ||||||
oxidoreductase/ferric-chelate reductase Pssm-ID: 215453 [Multi-domain] Cd Length: 722 Bit Score: 43.30 E-value: 2.40e-04
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| PLN03115 | PLN03115 | ferredoxin--NADP(+) reductase; Provisional |
177-278 | 1.11e-03 | ||||||
ferredoxin--NADP(+) reductase; Provisional Pssm-ID: 215585 [Multi-domain] Cd Length: 367 Bit Score: 40.76 E-value: 1.11e-03
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| PTZ00319 | PTZ00319 | NADH-cytochrome B5 reductase; Provisional |
227-383 | 1.13e-03 | ||||||
NADH-cytochrome B5 reductase; Provisional Pssm-ID: 173521 [Multi-domain] Cd Length: 300 Bit Score: 40.59 E-value: 1.13e-03
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| Ngb | cd08920 | Neuroglobins; The Ngb described in this subfamily is a hexacoordinated heme globin chiefly ... |
29-127 | 1.18e-03 | ||||||
Neuroglobins; The Ngb described in this subfamily is a hexacoordinated heme globin chiefly expressed in neurons of the brain and retina. In the human brain, it is highly expressed in the hypothalamus, amygdala, and in the pontine tegmental nuclei. It affords protection of brain neurons from ischemia and hypoxia. In rats, it plays a role in the neuroprotection of limb ischemic preconditioning (LIP). It plays roles as: a sensor of oxygen levels; a store or reservoir for oxygen; a facilitator for oxygen transport; a regulator of ROS; and a scavenger of nitric oxide. It also functions in the protection against apoptosis and in sleep regulation. This subgroup contains Ngb from mammalian and non-mammalian vertebrates, including fish, amphibians and reptiles; the functionally pentacoordinated acoelomorph Symsagittifera roscoffensis Ngb does not belong to this subgroup. Pssm-ID: 271272 Cd Length: 148 Bit Score: 39.05 E-value: 1.18e-03
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| CyPoR_like | cd06207 | NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ... |
204-287 | 1.89e-03 | ||||||
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: 99803 [Multi-domain] Cd Length: 382 Bit Score: 39.95 E-value: 1.89e-03
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| PLN02292 | PLN02292 | ferric-chelate reductase |
191-281 | 3.47e-03 | ||||||
ferric-chelate reductase Pssm-ID: 215165 [Multi-domain] Cd Length: 702 Bit Score: 39.46 E-value: 3.47e-03
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| globin_sensor | cd01068 | Globin sensor domain of globin-coupled-sensors (GCSs), protoglobins (Pgbs), and sensor ... |
2-119 | 5.89e-03 | ||||||
Globin sensor domain of globin-coupled-sensors (GCSs), protoglobins (Pgbs), and sensor single-domain globins (SSDgbs); S family; This family includes sensor domains which binds porphyrins, and other non-heme cofactors. GCSs have an N-terminal sensor domain coupled to a functional domain. For heme-bound oxygen sensing/binding globin domains, O2 binds to/dissociates from the heme iron complex inducing a structural change in the sensor domain, which is then transduced to the functional domain, switching on (or off) the function of the latter. Functional domains include DGC/GGDEF, EAL, histidine kinase, MCP, PAS, and GAF domains. Characterized members include Bacillus subtilis heme-based aerotaxis transducer (HemAT-Bs) which has a sensor domain coupled to an MCP domain. HemAT-Bs mediates an aerophilic response, and may control the movement direction of bacteria and archaea. Its MCP domain interacts with the CheA histidine kinase, a component of the CheA/CheY signal transduction system that regulates the rotational direction of flagellar motors. Another GCS having the sensor domain coupled to an MCP domain is Caulobacter crescentus McpB. McpB is encoded by a gene which lies adjacent to the major chemotaxis operon. Like McpA (encoded on this operon), McpB has three potential methylation sites, a C-terminal CheBR docking motif, and a motif needed for proteolysis via a ClpX-dependent pathway during the swarmer-to-stalked cell transition. Also included is Geobacter sulfurreducens GCS, a GCS of unknown function, in which the sensor domain is coupled to a transmembrane signal-transduction domain. Pgbs are single-domain globins of unknown function. Methanosarcina acetivorans Pgbs is dimeric and has an N-terminal extension, which together with other Pgb-specific loops, buries the heme within the protein; small ligand molecules gain access to the heme via two orthogonal apolar tunnels. Pgbs and other single-domain globins can function as sensors, when coupled to an appropriate regulator domain. Pssm-ID: 381256 [Multi-domain] Cd Length: 146 Bit Score: 36.79 E-value: 5.89e-03
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