nitric oxide synthase 3 [Mus musculus]
Protein Classification
NADPH cytochrome P450 oxidoreductase family protein; NADPH--cytochrome P450 reductase( domain architecture ID 10092407)
NADPH cytochrome P450 oxidoreductase family protein may serve as an electron donor in several oxygenase systems, catalyzing the transfer of two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN| NADPH--cytochrome P450 reductase, also called NADPH--hemoprotein reductase, is required for electron transfer from NADP to cytochrome P450 in microsomes
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||
| NOS_oxygenase_euk | cd00795 | Nitric oxide synthase (NOS) eukaryotic oxygenase domain. NOS produces nitric oxide (NO) by ... |
67-479 | 0e+00 | |||||||
Nitric oxide synthase (NOS) eukaryotic oxygenase domain. NOS produces nitric oxide (NO) by catalyzing a five-electron heme-based oxidation of a guanidine nitrogen of L-arginine to L-citrulline via two successive monooxygenation reactions producing N(omega)-hydroxy-L-arginine (NHA) as an intermediate. In mammals, there are three distinct NOS isozymes: neuronal (nNOS or NOS-1), cytokine-inducible (iNOS or NOS-2) and endothelial (eNOS or NOS-3) . Nitric oxide synthases are homodimers. In eukaryotes, each monomer has an N-terminal oxygenase domain, which binds to the substrate L-Arg, zinc, and to the cofactors heme and 5.6.7.8-(6R)-tetrahydrobiopterin (BH4) . Eukaryotic NOS's also have a C-terminal electron supplying reductase region, which is homologous to cytochrome P450 reductase and binds NADH, FAD and FMN. : Pssm-ID: 238410 Cd Length: 412 Bit Score: 865.85 E-value: 0e+00
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| FNR_like super family | cl06868 | Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ... |
761-1163 | 0e+00 | |||||||
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). The actual alignment was detected with superfamily member cd06202: Pssm-ID: 447143 [Multi-domain] Cd Length: 406 Bit Score: 597.39 E-value: 0e+00
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| Flavodoxin_1 | pfam00258 | Flavodoxin; |
521-697 | 1.01e-35 | |||||||
Flavodoxin; : Pssm-ID: 425562 [Multi-domain] Cd Length: 142 Bit Score: 132.49 E-value: 1.01e-35
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| Name | Accession | Description | Interval | E-value | ||||||||||
| NOS_oxygenase_euk | cd00795 | Nitric oxide synthase (NOS) eukaryotic oxygenase domain. NOS produces nitric oxide (NO) by ... |
67-479 | 0e+00 | ||||||||||
Nitric oxide synthase (NOS) eukaryotic oxygenase domain. NOS produces nitric oxide (NO) by catalyzing a five-electron heme-based oxidation of a guanidine nitrogen of L-arginine to L-citrulline via two successive monooxygenation reactions producing N(omega)-hydroxy-L-arginine (NHA) as an intermediate. In mammals, there are three distinct NOS isozymes: neuronal (nNOS or NOS-1), cytokine-inducible (iNOS or NOS-2) and endothelial (eNOS or NOS-3) . Nitric oxide synthases are homodimers. In eukaryotes, each monomer has an N-terminal oxygenase domain, which binds to the substrate L-Arg, zinc, and to the cofactors heme and 5.6.7.8-(6R)-tetrahydrobiopterin (BH4) . Eukaryotic NOS's also have a C-terminal electron supplying reductase region, which is homologous to cytochrome P450 reductase and binds NADH, FAD and FMN. Pssm-ID: 238410 Cd Length: 412 Bit Score: 865.85 E-value: 0e+00
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| NO_synthase | pfam02898 | Nitric oxide synthase, oxygenase domain; |
118-480 | 0e+00 | ||||||||||
Nitric oxide synthase, oxygenase domain; Pssm-ID: 460742 Cd Length: 362 Bit Score: 749.74 E-value: 0e+00
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| Nitric_oxide_synthase | cd06202 | The ferredoxin-reductase (FNR) like C-terminal domain of the nitric oxide synthase (NOS) fuses ... |
761-1163 | 0e+00 | ||||||||||
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: 597.39 E-value: 0e+00
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| COG4362 | COG4362 | Nitric oxide synthase, oxygenase domain [Inorganic ion transport and metabolism]; |
118-477 | 0e+00 | ||||||||||
Nitric oxide synthase, oxygenase domain [Inorganic ion transport and metabolism]; Pssm-ID: 443495 Cd Length: 360 Bit Score: 587.60 E-value: 0e+00
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| CysJ | COG0369 | Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases ... |
511-1159 | 2.65e-151 | ||||||||||
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases [Nucleotide transport and metabolism, Inorganic ion transport and metabolism]; Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases is part of the Pathway/BioSystem: Cysteine biosynthesis Pssm-ID: 440138 [Multi-domain] Cd Length: 561 Bit Score: 465.78 E-value: 2.65e-151
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| FAD_binding_1 | pfam00667 | FAD binding domain; This domain is found in sulfite reductase, NADPH cytochrome P450 reductase, ... |
751-978 | 7.22e-92 | ||||||||||
FAD binding domain; This domain is found in sulfite reductase, NADPH cytochrome P450 reductase, Nitric oxide synthase and methionine synthase reductase. Pssm-ID: 395540 [Multi-domain] Cd Length: 219 Bit Score: 294.25 E-value: 7.22e-92
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| PRK06214 | PRK06214 | sulfite reductase subunit alpha; |
759-1159 | 1.03e-64 | ||||||||||
sulfite reductase subunit alpha; Pssm-ID: 235745 [Multi-domain] Cd Length: 530 Bit Score: 229.19 E-value: 1.03e-64
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| Flavodoxin_1 | pfam00258 | Flavodoxin; |
521-697 | 1.01e-35 | ||||||||||
Flavodoxin; Pssm-ID: 425562 [Multi-domain] Cd Length: 142 Bit Score: 132.49 E-value: 1.01e-35
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| PRK09004 | PRK09004 | FMN-binding protein MioC; Provisional |
518-678 | 5.41e-06 | ||||||||||
FMN-binding protein MioC; Provisional Pssm-ID: 181608 [Multi-domain] Cd Length: 146 Bit Score: 47.52 E-value: 5.41e-06
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| FldA | COG0716 | Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ... |
519-589 | 1.94e-03 | ||||||||||
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: Heme biosynthesis Pssm-ID: 440480 [Multi-domain] Cd Length: 135 Bit Score: 39.89 E-value: 1.94e-03
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| Name | Accession | Description | Interval | E-value | ||||||||||
| NOS_oxygenase_euk | cd00795 | Nitric oxide synthase (NOS) eukaryotic oxygenase domain. NOS produces nitric oxide (NO) by ... |
67-479 | 0e+00 | ||||||||||
Nitric oxide synthase (NOS) eukaryotic oxygenase domain. NOS produces nitric oxide (NO) by catalyzing a five-electron heme-based oxidation of a guanidine nitrogen of L-arginine to L-citrulline via two successive monooxygenation reactions producing N(omega)-hydroxy-L-arginine (NHA) as an intermediate. In mammals, there are three distinct NOS isozymes: neuronal (nNOS or NOS-1), cytokine-inducible (iNOS or NOS-2) and endothelial (eNOS or NOS-3) . Nitric oxide synthases are homodimers. In eukaryotes, each monomer has an N-terminal oxygenase domain, which binds to the substrate L-Arg, zinc, and to the cofactors heme and 5.6.7.8-(6R)-tetrahydrobiopterin (BH4) . Eukaryotic NOS's also have a C-terminal electron supplying reductase region, which is homologous to cytochrome P450 reductase and binds NADH, FAD and FMN. Pssm-ID: 238410 Cd Length: 412 Bit Score: 865.85 E-value: 0e+00
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| NO_synthase | pfam02898 | Nitric oxide synthase, oxygenase domain; |
118-480 | 0e+00 | ||||||||||
Nitric oxide synthase, oxygenase domain; Pssm-ID: 460742 Cd Length: 362 Bit Score: 749.74 E-value: 0e+00
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| NOS_oxygenase | cd00575 | Nitric oxide synthase (NOS) produces nitric oxide (NO) by catalyzing a five-electron ... |
121-476 | 0e+00 | ||||||||||
Nitric oxide synthase (NOS) produces nitric oxide (NO) by catalyzing a five-electron heme-based oxidation of a guanidine nitrogen of L-arginine to L-citrulline via two successive monooxygenation reactions producing N(omega)-hydroxy-L-arginine (NHA) as an intermediate. In mammals, there are three distinct NOS isozymes: neuronal (nNOS or NOS-1), cytokine-inducible (iNOS or NOS-2) and endothelial (eNOS or NOS-3) . Nitric oxide synthases are homodimers. In eukaryotes, each monomer has an N-terminal oxygenase domain which binds to the substrate L-Arg, zinc, and to the cofactors heme and 5.6.7.8-(6R)-tetrahydrobiopterin (BH4) . Eukaryotic NOSs also have a C-terminal electron supplying reductase region, which is homologous to cytochrome P450 reductase and binds NADH, FAD and FMN. While prokaryotes can produce NO as a byproduct of denitrification, using a completely different set of enzymes than NOS, a few prokaryotes also have a NOS which consists solely of the NOS oxygenase domain. Prokaryotic NOS binds to the substrate L-Arg, zinc, and to the cofactors heme and tetrahydrofolate. Pssm-ID: 238321 Cd Length: 356 Bit Score: 735.62 E-value: 0e+00
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| Nitric_oxide_synthase | cd06202 | The ferredoxin-reductase (FNR) like C-terminal domain of the nitric oxide synthase (NOS) fuses ... |
761-1163 | 0e+00 | ||||||||||
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: 597.39 E-value: 0e+00
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| COG4362 | COG4362 | Nitric oxide synthase, oxygenase domain [Inorganic ion transport and metabolism]; |
118-477 | 0e+00 | ||||||||||
Nitric oxide synthase, oxygenase domain [Inorganic ion transport and metabolism]; Pssm-ID: 443495 Cd Length: 360 Bit Score: 587.60 E-value: 0e+00
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| NOS_oxygenase_prok | cd00794 | Nitric oxide synthase (NOS) prokaryotic oxygenase domain. NOS produces nitric oxide (NO) by ... |
122-476 | 1.46e-152 | ||||||||||
Nitric oxide synthase (NOS) prokaryotic oxygenase domain. NOS produces nitric oxide (NO) by catalyzing a five-electron heme-based oxidation of a guanidine nitrogen of L-arginine to L-citrulline via two successive monooxygenation reactions producing N(omega)-hydroxy-L-arginine (NHA) as an intermediate. Nitric oxide synthases are homodimers. Most prokaryotes produce NO as a byproduct of denitrification, using a completely different set of enzymes than NOS. However, a few prokaryotes also have a NOS, consisting solely of the NOS oxygenase domain. Prokaryotic NOS binds to the substrate L-Arg, zinc, and to the cofactors heme and tetrahydrofolate. Pssm-ID: 238409 Cd Length: 353 Bit Score: 461.13 E-value: 1.46e-152
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| CysJ | COG0369 | Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases ... |
511-1159 | 2.65e-151 | ||||||||||
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases [Nucleotide transport and metabolism, Inorganic ion transport and metabolism]; Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases is part of the Pathway/BioSystem: Cysteine biosynthesis Pssm-ID: 440138 [Multi-domain] Cd Length: 561 Bit Score: 465.78 E-value: 2.65e-151
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| FAD_binding_1 | pfam00667 | FAD binding domain; This domain is found in sulfite reductase, NADPH cytochrome P450 reductase, ... |
751-978 | 7.22e-92 | ||||||||||
FAD binding domain; This domain is found in sulfite reductase, NADPH cytochrome P450 reductase, Nitric oxide synthase and methionine synthase reductase. Pssm-ID: 395540 [Multi-domain] Cd Length: 219 Bit Score: 294.25 E-value: 7.22e-92
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| CYPOR | cd06204 | NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ... |
758-1158 | 4.58e-91 | ||||||||||
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: 99801 [Multi-domain] Cd Length: 416 Bit Score: 299.56 E-value: 4.58e-91
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| SiR | cd06199 | Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ... |
761-1159 | 5.10e-82 | ||||||||||
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. Pssm-ID: 99796 [Multi-domain] Cd Length: 360 Bit Score: 272.56 E-value: 5.10e-82
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| CyPoR_like | cd06207 | NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ... |
765-1154 | 1.90e-80 | ||||||||||
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: 269.14 E-value: 1.90e-80
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| CYPOR_like | cd06182 | NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ... |
934-1159 | 5.57e-78 | ||||||||||
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: 257.65 E-value: 5.57e-78
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| bifunctional_CYPOR | cd06206 | These bifunctional proteins fuse N-terminal cytochrome p450 with a cytochrome p450 reductase ... |
761-1159 | 7.84e-76 | ||||||||||
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: 256.03 E-value: 7.84e-76
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| methionine_synthase_red | cd06203 | Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for ... |
777-1158 | 5.90e-71 | ||||||||||
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: 243.00 E-value: 5.90e-71
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| PRK06214 | PRK06214 | sulfite reductase subunit alpha; |
759-1159 | 1.03e-64 | ||||||||||
sulfite reductase subunit alpha; Pssm-ID: 235745 [Multi-domain] Cd Length: 530 Bit Score: 229.19 E-value: 1.03e-64
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| cysJ | PRK10953 | NADPH-dependent assimilatory sulfite reductase flavoprotein subunit; |
520-1159 | 2.24e-54 | ||||||||||
NADPH-dependent assimilatory sulfite reductase flavoprotein subunit; Pssm-ID: 182862 [Multi-domain] Cd Length: 600 Bit Score: 200.72 E-value: 2.24e-54
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| Flavodoxin_1 | pfam00258 | Flavodoxin; |
521-697 | 1.01e-35 | ||||||||||
Flavodoxin; Pssm-ID: 425562 [Multi-domain] Cd Length: 142 Bit Score: 132.49 E-value: 1.01e-35
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| FNR_like | cd00322 | Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ... |
926-1134 | 9.06e-31 | ||||||||||
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: 121.40 E-value: 9.06e-31
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| SiR_like2 | cd06201 | Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ... |
936-1159 | 1.06e-30 | ||||||||||
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: 123.21 E-value: 1.06e-30
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| SiR_like1 | cd06200 | Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ... |
934-1159 | 1.18e-26 | ||||||||||
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: 110.06 E-value: 1.18e-26
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| CYPOR_like_FNR | cd06208 | These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ... |
936-1155 | 2.01e-25 | ||||||||||
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: 107.79 E-value: 2.01e-25
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| NAD_binding_1 | pfam00175 | Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ... |
1010-1122 | 3.01e-18 | ||||||||||
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: 81.54 E-value: 3.01e-18
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| Fpr | COG1018 | Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; |
935-1134 | 5.53e-17 | ||||||||||
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; Pssm-ID: 440641 [Multi-domain] Cd Length: 231 Bit Score: 81.37 E-value: 5.53e-17
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| FNR1 | cd06195 | Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ... |
937-1118 | 2.38e-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: 65.28 E-value: 2.38e-11
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| Mcr1 | COG0543 | NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ... |
934-1134 | 2.00e-10 | ||||||||||
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; Pssm-ID: 440309 [Multi-domain] Cd Length: 247 Bit Score: 62.57 E-value: 2.00e-10
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| PLN03116 | PLN03116 | ferredoxin--NADP+ reductase; Provisional |
969-1140 | 6.14e-10 | ||||||||||
ferredoxin--NADP+ reductase; Provisional Pssm-ID: 215586 [Multi-domain] Cd Length: 307 Bit Score: 62.04 E-value: 6.14e-10
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| PLN03115 | PLN03115 | ferredoxin--NADP(+) reductase; Provisional |
937-1134 | 7.57e-10 | ||||||||||
ferredoxin--NADP(+) reductase; Provisional Pssm-ID: 215585 [Multi-domain] Cd Length: 367 Bit Score: 62.33 E-value: 7.57e-10
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| FNR_iron_sulfur_binding_2 | cd06216 | Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
937-1134 | 1.95e-08 | ||||||||||
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: 56.46 E-value: 1.95e-08
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| flavohem_like_fad_nad_binding | cd06184 | FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ... |
916-1122 | 7.79e-07 | ||||||||||
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: 51.79 E-value: 7.79e-07
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| BenDO_FAD_NAD | cd06209 | Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ... |
911-1094 | 3.19e-06 | ||||||||||
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: 49.51 E-value: 3.19e-06
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| PRK09004 | PRK09004 | FMN-binding protein MioC; Provisional |
518-678 | 5.41e-06 | ||||||||||
FMN-binding protein MioC; Provisional Pssm-ID: 181608 [Multi-domain] Cd Length: 146 Bit Score: 47.52 E-value: 5.41e-06
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| PRK08105 | PRK08105 | flavodoxin; Provisional |
565-679 | 9.89e-06 | ||||||||||
flavodoxin; Provisional Pssm-ID: 181230 [Multi-domain] Cd Length: 149 Bit Score: 46.80 E-value: 9.89e-06
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| COG4097 | COG4097 | Predicted ferric reductase [Inorganic ion transport and metabolism]; |
939-1128 | 1.15e-05 | ||||||||||
Predicted ferric reductase [Inorganic ion transport and metabolism]; Pssm-ID: 443273 [Multi-domain] Cd Length: 442 Bit Score: 49.12 E-value: 1.15e-05
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| PRK06703 | PRK06703 | flavodoxin; Provisional |
518-676 | 1.83e-05 | ||||||||||
flavodoxin; Provisional Pssm-ID: 235854 [Multi-domain] Cd Length: 151 Bit Score: 45.91 E-value: 1.83e-05
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| DHOD_e_trans | cd06218 | FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ... |
978-1134 | 2.58e-05 | ||||||||||
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: 47.16 E-value: 2.58e-05
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| NADH_quinone_reductase | cd06188 | Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ... |
937-1059 | 3.69e-05 | ||||||||||
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: 46.91 E-value: 3.69e-05
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| FNR_iron_sulfur_binding_3 | cd06217 | Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
937-1123 | 5.47e-05 | ||||||||||
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: 46.11 E-value: 5.47e-05
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| FNR_like_3 | cd06198 | NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ... |
939-1128 | 2.37e-04 | ||||||||||
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: 43.78 E-value: 2.37e-04
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| cyt_b5_reduct_like | cd06183 | Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ... |
937-1118 | 3.48e-04 | ||||||||||
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: 43.71 E-value: 3.48e-04
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| O2ase_reductase_like | cd06187 | The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ... |
935-1048 | 5.05e-04 | ||||||||||
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: 42.97 E-value: 5.05e-04
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| sulfite_reductase_like | cd06221 | Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ... |
940-1080 | 6.85e-04 | ||||||||||
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: 42.98 E-value: 6.85e-04
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| flavin_oxioreductase | cd06189 | NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ... |
935-1066 | 9.25e-04 | ||||||||||
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: 42.15 E-value: 9.25e-04
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| phenol_2-monooxygenase_like | cd06211 | Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ... |
935-1066 | 1.38e-03 | ||||||||||
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: 41.93 E-value: 1.38e-03
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| FldA | COG0716 | Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ... |
519-589 | 1.94e-03 | ||||||||||
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: Heme biosynthesis Pssm-ID: 440480 [Multi-domain] Cd Length: 135 Bit Score: 39.89 E-value: 1.94e-03
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| FNR_iron_sulfur_binding_1 | cd06215 | Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
934-1066 | 2.77e-03 | ||||||||||
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: 40.65 E-value: 2.77e-03
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| FNR_iron_sulfur_binding | cd06191 | Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
937-1081 | 5.08e-03 | ||||||||||
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: 39.82 E-value: 5.08e-03
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