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Conserved domains on  [gi|2462525668|ref|XP_054224983|]
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NADPH oxidase 4 isoform X1 [Homo sapiens]

Protein Classification

ferredoxin reductase family protein( domain architecture ID 10485033)

ferredoxin reductase family protein may transfer electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH; contains a ferric reductase-like transmembrane domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 91-227 2.91e-13

Ferric reductase like transmembrane component; This family includes a common region in the transmembrane proteins mammalian cytochrome B-245 heavy chain (gp91-phox), ferric reductase transmembrane component in yeast and respiratory burst oxidase from mouse-ear cress. This may be a family of flavocytochromes capable of moving electrons across the plasma membrane. The Frp1 protein from S. pombe is a ferric reductase component and is required for cell surface ferric reductase activity, mutants in frp1 are deficient in ferric iron uptake. Cytochrome B-245 heavy chain is a FAD-dependent dehydrogenase it is also has electron transferase activity which reduces molecular oxygen to superoxide anion, a precursor in the production of microbicidal oxidants. Mutations in the sequence of cytochrome B-245 heavy chain (gp91-phox) lead to the X-linked chronic granulomatous disease. The bacteriocidal ability of phagocytic cells is reduced and is characterized by the absence of a functional plasma membrane associated NADPH oxidase. The chronic granulomatous disease gene codes for the beta chain of cytochrome B-245 and cytochrome B-245 is missing from patients with the disease.


:

Pssm-ID: 426438 [Multi-domain]  Cd Length: 121  Bit Score: 66.14  E-value: 2.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525668  91 SLILLPMcrTLLAYLRGSqkVPSRRTRRLLDKSRTFHITCGVTICIFSGVHVAAHLVNALNFSVnysEDFVELNAARYRD 170
Cdd:pfam01794   5 ALALLPL--LLLLALRNN--PLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSL---EGILDLLLKRPYN 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462525668 171 edprkllfttvpgLTGVCMVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLT 227
Cdd:pfam01794  78 -------------ILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
FNR_like super family cl06868
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 333-400 1.81e-12

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 cd06186:

Pssm-ID: 447143 [Multi-domain]  Cd Length: 210  Bit Score: 66.17  E-value: 1.81e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462525668 333 IISVISHP-SDVMEIRMVKE-NFKARPGQYITLHCPSV-SALENHPFTLTMCPTETKATFGVHLKIV-GDWT 400
Cdd:cd06186     1 IATVELLPdSDVIRLTIPKPkPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEQDTLSLIIRAKkGFTT 72
 
Name Accession Description Interval E-value
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 91-227 2.91e-13

Ferric reductase like transmembrane component; This family includes a common region in the transmembrane proteins mammalian cytochrome B-245 heavy chain (gp91-phox), ferric reductase transmembrane component in yeast and respiratory burst oxidase from mouse-ear cress. This may be a family of flavocytochromes capable of moving electrons across the plasma membrane. The Frp1 protein from S. pombe is a ferric reductase component and is required for cell surface ferric reductase activity, mutants in frp1 are deficient in ferric iron uptake. Cytochrome B-245 heavy chain is a FAD-dependent dehydrogenase it is also has electron transferase activity which reduces molecular oxygen to superoxide anion, a precursor in the production of microbicidal oxidants. Mutations in the sequence of cytochrome B-245 heavy chain (gp91-phox) lead to the X-linked chronic granulomatous disease. The bacteriocidal ability of phagocytic cells is reduced and is characterized by the absence of a functional plasma membrane associated NADPH oxidase. The chronic granulomatous disease gene codes for the beta chain of cytochrome B-245 and cytochrome B-245 is missing from patients with the disease.


Pssm-ID: 426438 [Multi-domain]  Cd Length: 121  Bit Score: 66.14  E-value: 2.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525668  91 SLILLPMcrTLLAYLRGSqkVPSRRTRRLLDKSRTFHITCGVTICIFSGVHVAAHLVNALNFSVnysEDFVELNAARYRD 170
Cdd:pfam01794   5 ALALLPL--LLLLALRNN--PLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSL---EGILDLLLKRPYN 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462525668 171 edprkllfttvpgLTGVCMVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLT 227
Cdd:pfam01794  78 -------------ILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 333-400 1.81e-12

NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as superoxide and hydrogen peroxide. ROS were originally identified as bactericidal agents in phagocytes, but are now also implicated in cell signaling and metabolism. NOX has a 6-alpha helix heme-binding transmembrane domain fused to a flavoprotein with the nucleotide binding domain located in the cytoplasm. Duox enzymes link a peroxidase domain to the NOX domain via a single transmembrane and EF-hand Ca2+ binding sites. The flavoprotein module has a ferredoxin like FAD/NADPH binding domain. In classical phagocytic NOX2, electron transfer occurs from NADPH to FAD to the heme of cytb to oxygen leading to superoxide formation.


Pssm-ID: 99783 [Multi-domain]  Cd Length: 210  Bit Score: 66.17  E-value: 1.81e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462525668 333 IISVISHP-SDVMEIRMVKE-NFKARPGQYITLHCPSV-SALENHPFTLTMCPTETKATFGVHLKIV-GDWT 400
Cdd:cd06186     1 IATVELLPdSDVIRLTIPKPkPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEQDTLSLIIRAKkGFTT 72
FAD_binding_8 pfam08022
FAD-binding domain;
329-400 3.30e-10

FAD-binding domain;


Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 56.96  E-value: 3.30e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462525668 329 KPVTIISVISHPSDVMEIRMVKEN--FKARPGQYITLHC-PSVSALENHPFTLTMCPTETKATfgVHLKIVGDWT 400
Cdd:pfam08022   2 FGVPKAKVALLPDNVLKLRVSKPKkpFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLS--LHIKVKGGWT 74
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 91-400 6.69e-06

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 48.30  E-value: 6.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525668  91 SLILLPMCRTL-LAYLRGSQKVPSRRtrrlldksrtFHITCGVTICIFSGVHVAAHLvnalnfsvnysedFVELNAARYR 169
Cdd:PLN02844  168 ALLLLPVLRGLaLFRLLGIQFEASVR----------YHVWLGTSMIFFATVHGASTL-------------FIWGISHHIQ 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525668 170 DEdPRKLLFTTVPGLTGVCMVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLTLHVSggllkyqtnldthppgci 249
Cdd:PLN02844  225 DE-IWKWQKTGRIYLAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHHLYIVFLIFFLFHAG------------------ 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525668 250 slnrtssqnislpeyfSEHFHEPFPEGFskpaeftqhkfvkicmeeprfqanfpqtwlwisgplcLYCAERLYRYIRSNK 329
Cdd:PLN02844  286 ----------------DRHFYMVFPGIF-------------------------------------LFGLDKLLRIVQSRP 312

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462525668 330 PVTIISVISHPSDVMEIRMVKE-NFKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHLKIVGDWT 400
Cdd:PLN02844  313 ETCILSARLFPCKAIELVLPKDpGLKYAPTSVIFMKIPSISRFQWHPFSITSSSNIDDHTMSVIIKCEGGWT 384
PLN02631 PLN02631
ferric-chelate reductase
 315-400 7.77e-06

ferric-chelate reductase


Pssm-ID: 178238 [Multi-domain]  Cd Length: 699  Bit Score: 48.11  E-value: 7.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525668 315 LYCAERLYRYIRSNKPVTIISVISHPSDVMEIRMVK-ENFKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHL 393
Cdd:PLN02631  294 LFFIDRYLRFLQSTKRSRLVSARILPSDNLELTFSKtPGLHYTPTSILFLHVPSISKLQWHPFTITSSSNLEKDTLSVVI 373


                  ....*..
gi 2462525668 394 KIVGDWT 400
Cdd:PLN02631  374 RRQGSWT 380
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 332-400 2.02e-04

NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 42.54  E-value: 2.02e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462525668 332 TIISVISHPSDV--MEIRMVKENFKARPGQYITLHCPsvSALENHPFTLTMCPTEtKATFGVHLKIVGDWT 400
Cdd:COG0543     1 KVVSVERLAPDVylLRLEAPLIALKFKPGQFVMLRVP--GDGLRRPFSIASAPRE-DGTIELHIRVVGKGT 68
 
Name Accession Description Interval E-value
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 91-227 2.91e-13

Ferric reductase like transmembrane component; This family includes a common region in the transmembrane proteins mammalian cytochrome B-245 heavy chain (gp91-phox), ferric reductase transmembrane component in yeast and respiratory burst oxidase from mouse-ear cress. This may be a family of flavocytochromes capable of moving electrons across the plasma membrane. The Frp1 protein from S. pombe is a ferric reductase component and is required for cell surface ferric reductase activity, mutants in frp1 are deficient in ferric iron uptake. Cytochrome B-245 heavy chain is a FAD-dependent dehydrogenase it is also has electron transferase activity which reduces molecular oxygen to superoxide anion, a precursor in the production of microbicidal oxidants. Mutations in the sequence of cytochrome B-245 heavy chain (gp91-phox) lead to the X-linked chronic granulomatous disease. The bacteriocidal ability of phagocytic cells is reduced and is characterized by the absence of a functional plasma membrane associated NADPH oxidase. The chronic granulomatous disease gene codes for the beta chain of cytochrome B-245 and cytochrome B-245 is missing from patients with the disease.


Pssm-ID: 426438 [Multi-domain]  Cd Length: 121  Bit Score: 66.14  E-value: 2.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525668  91 SLILLPMcrTLLAYLRGSqkVPSRRTRRLLDKSRTFHITCGVTICIFSGVHVAAHLVNALNFSVnysEDFVELNAARYRD 170
Cdd:pfam01794   5 ALALLPL--LLLLALRNN--PLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSL---EGILDLLLKRPYN 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462525668 171 edprkllfttvpgLTGVCMVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLT 227
Cdd:pfam01794  78 -------------ILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 333-400 1.81e-12

NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as superoxide and hydrogen peroxide. ROS were originally identified as bactericidal agents in phagocytes, but are now also implicated in cell signaling and metabolism. NOX has a 6-alpha helix heme-binding transmembrane domain fused to a flavoprotein with the nucleotide binding domain located in the cytoplasm. Duox enzymes link a peroxidase domain to the NOX domain via a single transmembrane and EF-hand Ca2+ binding sites. The flavoprotein module has a ferredoxin like FAD/NADPH binding domain. In classical phagocytic NOX2, electron transfer occurs from NADPH to FAD to the heme of cytb to oxygen leading to superoxide formation.


Pssm-ID: 99783 [Multi-domain]  Cd Length: 210  Bit Score: 66.17  E-value: 1.81e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462525668 333 IISVISHP-SDVMEIRMVKE-NFKARPGQYITLHCPSV-SALENHPFTLTMCPTETKATFGVHLKIV-GDWT 400
Cdd:cd06186     1 IATVELLPdSDVIRLTIPKPkPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEQDTLSLIIRAKkGFTT 72
FAD_binding_8 pfam08022
FAD-binding domain;
329-400 3.30e-10

FAD-binding domain;


Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 56.96  E-value: 3.30e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462525668 329 KPVTIISVISHPSDVMEIRMVKEN--FKARPGQYITLHC-PSVSALENHPFTLTMCPTETKATfgVHLKIVGDWT 400
Cdd:pfam08022   2 FGVPKAKVALLPDNVLKLRVSKPKkpFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLS--LHIKVKGGWT 74
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 91-400 6.69e-06

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 48.30  E-value: 6.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525668  91 SLILLPMCRTL-LAYLRGSQKVPSRRtrrlldksrtFHITCGVTICIFSGVHVAAHLvnalnfsvnysedFVELNAARYR 169
Cdd:PLN02844  168 ALLLLPVLRGLaLFRLLGIQFEASVR----------YHVWLGTSMIFFATVHGASTL-------------FIWGISHHIQ 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525668 170 DEdPRKLLFTTVPGLTGVCMVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLTLHVSggllkyqtnldthppgci 249
Cdd:PLN02844  225 DE-IWKWQKTGRIYLAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHHLYIVFLIFFLFHAG------------------ 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525668 250 slnrtssqnislpeyfSEHFHEPFPEGFskpaeftqhkfvkicmeeprfqanfpqtwlwisgplcLYCAERLYRYIRSNK 329
Cdd:PLN02844  286 ----------------DRHFYMVFPGIF-------------------------------------LFGLDKLLRIVQSRP 312

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462525668 330 PVTIISVISHPSDVMEIRMVKE-NFKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHLKIVGDWT 400
Cdd:PLN02844  313 ETCILSARLFPCKAIELVLPKDpGLKYAPTSVIFMKIPSISRFQWHPFSITSSSNIDDHTMSVIIKCEGGWT 384
PLN02631 PLN02631
ferric-chelate reductase
 315-400 7.77e-06

ferric-chelate reductase


Pssm-ID: 178238 [Multi-domain]  Cd Length: 699  Bit Score: 48.11  E-value: 7.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525668 315 LYCAERLYRYIRSNKPVTIISVISHPSDVMEIRMVK-ENFKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHL 393
Cdd:PLN02631  294 LFFIDRYLRFLQSTKRSRLVSARILPSDNLELTFSKtPGLHYTPTSILFLHVPSISKLQWHPFTITSSSNLEKDTLSVVI 373


                  ....*..
gi 2462525668 394 KIVGDWT 400
Cdd:PLN02631  374 RRQGSWT 380
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 332-400 2.02e-04

NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 42.54  E-value: 2.02e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462525668 332 TIISVISHPSDV--MEIRMVKENFKARPGQYITLHCPsvSALENHPFTLTMCPTEtKATFGVHLKIVGDWT 400
Cdd:COG0543     1 KVVSVERLAPDVylLRLEAPLIALKFKPGQFVMLRVP--GDGLRRPFSIASAPRE-DGTIELHIRVVGKGT 68
PLN02292 PLN02292
ferric-chelate reductase
 195-400 3.01e-03

ferric-chelate reductase


Pssm-ID: 215165 [Multi-domain]  Cd Length: 702  Bit Score: 39.85  E-value: 3.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525668 195 LMITASTY-AIRVSNYDIFWYTHNLFFVFYMLLTLHVSggllkyqtnldthppgcislnrTSSQNISLPEYFsehfhepf 273
Cdd:PLN02292  261 LVMWATTYpKIRRRFFEVFFYTHYLYIVFMLFFVFHVG----------------------ISFALISFPGFY-------- 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525668 274 pegfskpaeftqhkfvkicmeeprfqanfpqtwlwisgplcLYCAERLYRYIRSNKPVTIISVISHPSDVMEIRMVKEN- 352
Cdd:PLN02292  311 -----------------------------------------IFLVDRFLRFLQSRNNVKLVSARVLPCDTVELNFSKNPm 349

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2462525668 353 FKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHLKIVGDWT 400
Cdd:PLN02292  350 LMYSPTSIMFVNIPSISKLQWHPFTITSSSKLEPEKLSVMIKSQGKWS 397
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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