NADH-cytochrome b5 reductase-like isoform X12 [Mus musculus]
Protein Classification
Oxidored-like and cyt_b5_reduct_like domain-containing protein( domain architecture ID 10298874)
Oxidored-like and cyt_b5_reduct_like domain-containing protein
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| cyt_b5_reduct_like | cd06183 | Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ... |
123-321 | 8.67e-49 | ||||
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: 162.74 E-value: 8.67e-49
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| Oxidored-like super family | cl10765 | Oxidoreductase-like protein, N-terminal; Members of this family are found in the N terminal ... |
53-92 | 1.82e-09 | ||||
Oxidoreductase-like protein, N-terminal; Members of this family are found in the N terminal region of various oxidoreductase like proteins. Their exact function is, as yet, unknown. The actual alignment was detected with superfamily member pfam09791: Pssm-ID: 462904 Cd Length: 45 Bit Score: 52.57 E-value: 1.82e-09
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| Name | Accession | Description | Interval | E-value | |||||
| cyt_b5_reduct_like | cd06183 | Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ... |
123-321 | 8.67e-49 | |||||
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: 162.74 E-value: 8.67e-49
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| PLN02252 | PLN02252 | nitrate reductase [NADPH] |
96-321 | 3.11e-20 | |||||
nitrate reductase [NADPH] Pssm-ID: 215141 [Multi-domain] Cd Length: 888 Bit Score: 91.28 E-value: 3.11e-20
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| Fpr | COG1018 | Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; |
116-319 | 8.65e-20 | |||||
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; Pssm-ID: 440641 [Multi-domain] Cd Length: 231 Bit Score: 86.38 E-value: 8.65e-20
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| FAD_binding_6 | pfam00970 | Oxidoreductase FAD-binding domain; |
127-186 | 1.91e-15 | |||||
Oxidoreductase FAD-binding domain; Pssm-ID: 425968 [Multi-domain] Cd Length: 99 Bit Score: 70.69 E-value: 1.91e-15
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| Oxidored-like | pfam09791 | Oxidoreductase-like protein, N-terminal; Members of this family are found in the N terminal ... |
53-92 | 1.82e-09 | |||||
Oxidoreductase-like protein, N-terminal; Members of this family are found in the N terminal region of various oxidoreductase like proteins. Their exact function is, as yet, unknown. Pssm-ID: 462904 Cd Length: 45 Bit Score: 52.57 E-value: 1.82e-09
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| Name | Accession | Description | Interval | E-value | |||||
| cyt_b5_reduct_like | cd06183 | Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ... |
123-321 | 8.67e-49 | |||||
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: 162.74 E-value: 8.67e-49
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| PLN02252 | PLN02252 | nitrate reductase [NADPH] |
96-321 | 3.11e-20 | |||||
nitrate reductase [NADPH] Pssm-ID: 215141 [Multi-domain] Cd Length: 888 Bit Score: 91.28 E-value: 3.11e-20
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| Fpr | COG1018 | Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; |
116-319 | 8.65e-20 | |||||
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; Pssm-ID: 440641 [Multi-domain] Cd Length: 231 Bit Score: 86.38 E-value: 8.65e-20
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| FNR_like | cd00322 | Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ... |
127-319 | 3.20e-19 | |||||
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: 84.42 E-value: 3.20e-19
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| FNR_iron_sulfur_binding_3 | cd06217 | Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
130-316 | 1.33e-17 | |||||
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: 80.39 E-value: 1.33e-17
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| PTZ00319 | PTZ00319 | NADH-cytochrome B5 reductase; Provisional |
113-321 | 6.37e-16 | |||||
NADH-cytochrome B5 reductase; Provisional Pssm-ID: 173521 [Multi-domain] Cd Length: 300 Bit Score: 76.79 E-value: 6.37e-16
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| FAD_binding_6 | pfam00970 | Oxidoreductase FAD-binding domain; |
127-186 | 1.91e-15 | |||||
Oxidoreductase FAD-binding domain; Pssm-ID: 425968 [Multi-domain] Cd Length: 99 Bit Score: 70.69 E-value: 1.91e-15
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| Mcr1 | COG0543 | NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ... |
123-316 | 5.68e-13 | |||||
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; Pssm-ID: 440309 [Multi-domain] Cd Length: 247 Bit Score: 67.58 E-value: 5.68e-13
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| PA_degradation_oxidoreductase_like | cd06214 | NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ... |
118-316 | 6.75e-13 | |||||
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: 67.18 E-value: 6.75e-13
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| PTZ00274 | PTZ00274 | cytochrome b5 reductase; Provisional |
129-296 | 3.84e-11 | |||||
cytochrome b5 reductase; Provisional Pssm-ID: 140300 Cd Length: 325 Bit Score: 63.01 E-value: 3.84e-11
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| NAD_binding_1 | pfam00175 | Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ... |
192-306 | 9.26e-11 | |||||
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have essentially no similarity. Pssm-ID: 425503 [Multi-domain] Cd Length: 109 Bit Score: 58.04 E-value: 9.26e-11
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| Oxidored-like | pfam09791 | Oxidoreductase-like protein, N-terminal; Members of this family are found in the N terminal ... |
53-92 | 1.82e-09 | |||||
Oxidoreductase-like protein, N-terminal; Members of this family are found in the N terminal region of various oxidoreductase like proteins. Their exact function is, as yet, unknown. Pssm-ID: 462904 Cd Length: 45 Bit Score: 52.57 E-value: 1.82e-09
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| FNR_iron_sulfur_binding_2 | cd06216 | Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
129-313 | 1.15e-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: 54.92 E-value: 1.15e-08
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| FNR_iron_sulfur_binding_1 | cd06215 | Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
130-319 | 1.40e-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 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: 54.52 E-value: 1.40e-08
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| FNR_iron_sulfur_binding | cd06191 | Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
130-318 | 6.87e-08 | |||||
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: 52.53 E-value: 6.87e-08
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| FNR1 | cd06195 | Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ... |
190-317 | 9.98e-07 | |||||
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: 49.10 E-value: 9.98e-07
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| FNR_like_1 | cd06196 | Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ... |
123-317 | 1.37e-05 | |||||
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: 45.31 E-value: 1.37e-05
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| BenDO_FAD_NAD | cd06209 | Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ... |
123-224 | 4.71e-05 | |||||
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: 43.74 E-value: 4.71e-05
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| O2ase_reductase_like | cd06187 | The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ... |
127-316 | 1.87e-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: 42.19 E-value: 1.87e-04
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| sulfite_reductase_like | cd06221 | Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ... |
189-320 | 2.85e-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: 41.82 E-value: 2.85e-04
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| flavin_oxioreductase | cd06189 | NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ... |
122-319 | 2.43e-03 | |||||
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: 38.68 E-value: 2.43e-03
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| PRK05713 | PRK05713 | iron-sulfur-binding ferredoxin reductase; |
190-313 | 2.87e-03 | |||||
iron-sulfur-binding ferredoxin reductase; Pssm-ID: 235575 [Multi-domain] Cd Length: 312 Bit Score: 38.94 E-value: 2.87e-03
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