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Conserved domains on  [gi|1958650256|ref|XP_038948871|]
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NADPH oxidase 4 isoform X1 [Rattus norvegicus]

Protein Classification

ferric reductase family protein( domain architecture ID 10484952)

ferric reductase family protein functions as an oxidoreductase, such as human NADPH oxidase 1, a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes and other tissues

EC:  1.-.-.-
Gene Ontology:  GO:0050661|GO:0016491|GO:0016020

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 311-556 1.68e-34

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: 129.35  E-value: 1.68e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256 311 IISVINHP-SDVMELRMIKE-NFKARPGQ----------------------CPTETKATFGVHFKVV-GDWTERFRDLLL 365
Cdd:cd06186     1 IATVELLPdSDVIRLTIPKPkPFKWKPGQhvylnfpsllsfwqshpftiasSPEDEQDTLSLIIRAKkGFTTRLLRKALK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256 366 PPSSQDSeilpfiqsrnyPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDW-KPYKLRRLYFIWVCRD 444
Cdd:cd06186    81 SPGGGVS-----------LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSsKTSRTRRVKLVWVVRD 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256 445 IQSFQWFADLLyvlhnKFWQENRPDFvNIQLYLSQtdgiqkiigekyhtlnsrlfigrprwkllfdeiakcnrgktvgVF 524
Cdd:cd06186   150 REDLEWFLDEL-----RAAQELEVDG-EIEIYVTR-------------------------------------------VV 180

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958650256 525 CCGPSSISKTLHNLSNRNNsyGTKFEYNKESF 556
Cdd:cd06186   181 VCGPPGLVDDVRNAVAKKG--GTGVEFHEESF 210
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 69-205 2.84e-14

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: 69.22  E-value: 2.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256  69 SLILLPMcrTVLAYLRGSqkVPSRRTRRLLDKSKTLHITCGITICIFSGVHVAAHLVNALNFSVnysEHFLALNAARYQN 148
Cdd:pfam01794   5 ALALLPL--LLLLALRNN--PLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSL---EGILDLLLKRPYN 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958650256 149 edprkllfttvpgLTGVCMVVVLFLMVTASTYAIRVSNYDIFWYTHNLFFVFYMLLL 205
Cdd:pfam01794  78 -------------ILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
 
Name Accession Description Interval E-value
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 311-556 1.68e-34

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: 129.35  E-value: 1.68e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256 311 IISVINHP-SDVMELRMIKE-NFKARPGQ----------------------CPTETKATFGVHFKVV-GDWTERFRDLLL 365
Cdd:cd06186     1 IATVELLPdSDVIRLTIPKPkPFKWKPGQhvylnfpsllsfwqshpftiasSPEDEQDTLSLIIRAKkGFTTRLLRKALK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256 366 PPSSQDSeilpfiqsrnyPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDW-KPYKLRRLYFIWVCRD 444
Cdd:cd06186    81 SPGGGVS-----------LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSsKTSRTRRVKLVWVVRD 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256 445 IQSFQWFADLLyvlhnKFWQENRPDFvNIQLYLSQtdgiqkiigekyhtlnsrlfigrprwkllfdeiakcnrgktvgVF 524
Cdd:cd06186   150 REDLEWFLDEL-----RAAQELEVDG-EIEIYVTR-------------------------------------------VV 180

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958650256 525 CCGPSSISKTLHNLSNRNNsyGTKFEYNKESF 556
Cdd:cd06186   181 VCGPPGLVDDVRNAVAKKG--GTGVEFHEESF 210
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
402-539 5.63e-25

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 100.88  E-value: 5.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256 402 YEVSLCVAGGIGVTPFASILNTLLDDWKPYKLRRLYFIWVCRDIQSFQWFADLLYVLhnkfwQENRPDFVNIQLYLSQTD 481
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKSKKLKTKKIKFYWVVRDLSSLEWFKDVLNEL-----EELKELNIEIHIYLTGEY 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958650256 482 ----------------GIQKIIGEKYHTLNSRLFIGRPRWKLLFDEIAKCNRGKTVGVFCCGPSSISKTLHNLS 539
Cdd:pfam08030  76 eaedasdqsdssirseNFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 69-205 2.84e-14

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: 69.22  E-value: 2.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256  69 SLILLPMcrTVLAYLRGSqkVPSRRTRRLLDKSKTLHITCGITICIFSGVHVAAHLVNALNFSVnysEHFLALNAARYQN 148
Cdd:pfam01794   5 ALALLPL--LLLLALRNN--PLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSL---EGILDLLLKRPYN 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958650256 149 edprkllfttvpgLTGVCMVVVLFLMVTASTYAIRVSNYDIFWYTHNLFFVFYMLLL 205
Cdd:pfam01794  78 -------------ILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 310-482 1.25e-09

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 58.72  E-value: 1.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256 310 TIISVINHPSDVMELRM--IKENFKARPGQ-------------------CPTEtKATFGVHFKVVGDWTERFRDLllpps 368
Cdd:COG0543     1 KVVSVERLAPDVYLLRLeaPLIALKFKPGQfvmlrvpgdglrrpfsiasAPRE-DGTIELHIRVVGKGTRALAEL----- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256 369 sQDSEilpfiqsrnypKLYIDGPFGSPFEeslnYEVS----LCVAGGIGVTPFASILNTLLDdwkpyKLRRLYFIWVCRD 444
Cdd:COG0543    75 -KPGD-----------ELDVRGPLGNGFP----LEDSgrpvLLVAGGTGLAPLRSLAEALLA-----RGRRVTLYLGART 133

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958650256 445 iqsfqwfADLLYvLHNKFWQenrpdFVNIQLYLSQTDG 482
Cdd:COG0543   134 -------PEDLY-LLDELEA-----LADFRVVVTTDDG 158
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 162-479 1.87e-08

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 57.16  E-value: 1.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256 162 LTGVCMVVVLFLMVTASTYAIRVSNYDIFWYTHNLFFVFYMLLLLHVSggllkyqtnldthppgcislnrtpsqnmsiad 241
Cdd:PLN02844  238 LAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHHLYIVFLIFFLFHAG-------------------------------- 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256 242 yvSEHFHGSLPGGFskledhyqktlvkicleepkfqahfpqtwiwisgplcLYCAERLYRCIRSNKPVTIISVINHPSDV 321
Cdd:PLN02844  286 --DRHFYMVFPGIF-------------------------------------LFGLDKLLRIVQSRPETCILSARLFPCKA 326

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256 322 MELRMIKE-------------------NFKARPGQCPTET---KATFGVHFKVVGDWTERFRDLLLPPSSQDSEILPFIQ 379
Cdd:PLN02844  327 IELVLPKDpglkyaptsvifmkipsisRFQWHPFSITSSSnidDHTMSVIIKCEGGWTNSLYNKIQAELDSETNQMNCIP 406

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256 380 SRnypklyIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKP-YKL-RRLYFIWVCRDIQSFQWFADLLYV 457
Cdd:PLN02844  407 VA------IEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILKEIASQSSSrYRFpKRVQLIYVVKKSQDICLLNPISSL 480

                         330       340
                  ....*....|....*....|..
gi 1958650256 458 LHNKFWQENRpdfVNIQLYLSQ 479
Cdd:PLN02844  481 LLNQSSNQLN---LKLKVFVTQ 499
 
Name Accession Description Interval E-value
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 311-556 1.68e-34

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: 129.35  E-value: 1.68e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256 311 IISVINHP-SDVMELRMIKE-NFKARPGQ----------------------CPTETKATFGVHFKVV-GDWTERFRDLLL 365
Cdd:cd06186     1 IATVELLPdSDVIRLTIPKPkPFKWKPGQhvylnfpsllsfwqshpftiasSPEDEQDTLSLIIRAKkGFTTRLLRKALK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256 366 PPSSQDSeilpfiqsrnyPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDW-KPYKLRRLYFIWVCRD 444
Cdd:cd06186    81 SPGGGVS-----------LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSsKTSRTRRVKLVWVVRD 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256 445 IQSFQWFADLLyvlhnKFWQENRPDFvNIQLYLSQtdgiqkiigekyhtlnsrlfigrprwkllfdeiakcnrgktvgVF 524
Cdd:cd06186   150 REDLEWFLDEL-----RAAQELEVDG-EIEIYVTR-------------------------------------------VV 180

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958650256 525 CCGPSSISKTLHNLSNRNNsyGTKFEYNKESF 556
Cdd:cd06186   181 VCGPPGLVDDVRNAVAKKG--GTGVEFHEESF 210
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
402-539 5.63e-25

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 100.88  E-value: 5.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256 402 YEVSLCVAGGIGVTPFASILNTLLDDWKPYKLRRLYFIWVCRDIQSFQWFADLLYVLhnkfwQENRPDFVNIQLYLSQTD 481
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKSKKLKTKKIKFYWVVRDLSSLEWFKDVLNEL-----EELKELNIEIHIYLTGEY 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958650256 482 ----------------GIQKIIGEKYHTLNSRLFIGRPRWKLLFDEIAKCNRGKTVGVFCCGPSSISKTLHNLS 539
Cdd:pfam08030  76 eaedasdqsdssirseNFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 69-205 2.84e-14

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: 69.22  E-value: 2.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256  69 SLILLPMcrTVLAYLRGSqkVPSRRTRRLLDKSKTLHITCGITICIFSGVHVAAHLVNALNFSVnysEHFLALNAARYQN 148
Cdd:pfam01794   5 ALALLPL--LLLLALRNN--PLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSL---EGILDLLLKRPYN 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958650256 149 edprkllfttvpgLTGVCMVVVLFLMVTASTYAIRVSNYDIFWYTHNLFFVFYMLLL 205
Cdd:pfam01794  78 -------------ILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 310-482 1.25e-09

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 58.72  E-value: 1.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256 310 TIISVINHPSDVMELRM--IKENFKARPGQ-------------------CPTEtKATFGVHFKVVGDWTERFRDLllpps 368
Cdd:COG0543     1 KVVSVERLAPDVYLLRLeaPLIALKFKPGQfvmlrvpgdglrrpfsiasAPRE-DGTIELHIRVVGKGTRALAEL----- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256 369 sQDSEilpfiqsrnypKLYIDGPFGSPFEeslnYEVS----LCVAGGIGVTPFASILNTLLDdwkpyKLRRLYFIWVCRD 444
Cdd:COG0543    75 -KPGD-----------ELDVRGPLGNGFP----LEDSgrpvLLVAGGTGLAPLRSLAEALLA-----RGRRVTLYLGART 133

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958650256 445 iqsfqwfADLLYvLHNKFWQenrpdFVNIQLYLSQTDG 482
Cdd:COG0543   134 -------PEDLY-LLDELEA-----LADFRVVVTTDDG 158
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 388-528 2.52e-09

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: 57.46  E-value: 2.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256 388 IDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKPyklRRLYFIWVCRDiqsfqwFADLLYVlhnKFWQENR 467
Cdd:cd00322    83 VSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPG---GEITLLYGART------PADLLFL---DELEELA 150

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958650256 468 PDFVNIQLYLSQTDgiqkiigEKYHTLNSRLFIGRPRWKLLFDEIakcnrGKTVGVFCCGP 528
Cdd:cd00322   151 KEGPNFRLVLALSR-------ESEAKLGPGGRIDREAEILALLPD-----DSGALVYICGP 199
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 162-479 1.87e-08

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 57.16  E-value: 1.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256 162 LTGVCMVVVLFLMVTASTYAIRVSNYDIFWYTHNLFFVFYMLLLLHVSggllkyqtnldthppgcislnrtpsqnmsiad 241
Cdd:PLN02844  238 LAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHHLYIVFLIFFLFHAG-------------------------------- 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256 242 yvSEHFHGSLPGGFskledhyqktlvkicleepkfqahfpqtwiwisgplcLYCAERLYRCIRSNKPVTIISVINHPSDV 321
Cdd:PLN02844  286 --DRHFYMVFPGIF-------------------------------------LFGLDKLLRIVQSRPETCILSARLFPCKA 326

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256 322 MELRMIKE-------------------NFKARPGQCPTET---KATFGVHFKVVGDWTERFRDLLLPPSSQDSEILPFIQ 379
Cdd:PLN02844  327 IELVLPKDpglkyaptsvifmkipsisRFQWHPFSITSSSnidDHTMSVIIKCEGGWTNSLYNKIQAELDSETNQMNCIP 406

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256 380 SRnypklyIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKP-YKL-RRLYFIWVCRDIQSFQWFADLLYV 457
Cdd:PLN02844  407 VA------IEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILKEIASQSSSrYRFpKRVQLIYVVKKSQDICLLNPISSL 480

                         330       340
                  ....*....|....*....|..
gi 1958650256 458 LHNKFWQENRpdfVNIQLYLSQ 479
Cdd:PLN02844  481 LLNQSSNQLN---LKLKVFVTQ 499
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
274-444 5.18e-07

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 52.20  E-value: 5.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256 274 PKFQAHFPQTWIWIS---GPLCLYCAERLYRCIRSNK-PVTIISVINHPSDVMELRM---IKENFKARPGQ--------- 337
Cdd:COG4097   178 GPFYWSPPAGVLWAAlaaAGLAAAVYSRLGRPLRSRRhPYRVESVEPEAGDVVELTLrpeGGRWLGHRAGQfaflrfdgs 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256 338 -------------CPTET-KATFGVhfKVVGDWTERFRDLllPPSSqdseilpfiqsrnypKLYIDGPFGS-PFEESLNY 402
Cdd:COG4097   258 pfweeahpfsissAPGGDgRLRFTI--KALGDFTRRLGRL--KPGT---------------RVYVEGPYGRfTFDRRDTA 318

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958650256 403 EVSLCVAGGIGVTPFASILNTLldDWKPYKLRRLYFIWVCRD 444
Cdd:COG4097   319 PRQVWIAGGIGITPFLALLRAL--AARPGDQRPVDLFYCVRD 358
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 385-528 2.75e-05

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: 45.64  E-value: 2.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256 385 KLYIDGPFGS-PFEESLNYEVSLCVAGGIGVTPFASILNTLLDDwkPYKLRRLYFIWVCR---DIqsfqWFADLLyvlhn 460
Cdd:cd06183    86 TVEIRGPFGKfEYKPNGKVKHIGMIAGGTGITPMLQLIRAILKD--PEDKTKISLLYANRteeDI----LLREEL----- 154

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958650256 461 KFWQENRPDFVNIQLYLSQTDGIQKIigekyhtlnsrlFIGRPRWKLLFDEIAKCNRGKTVgVFCCGP 528
Cdd:cd06183   155 DELAKKHPDRFKVHYVLSRPPEGWKG------------GVGFITKEMIKEHLPPPPSEDTL-VLVCGP 209
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 385-537 7.56e-05

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: 44.17  E-value: 7.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256 385 KLYIDGPFGSpFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKPyklRRLYFIWVCRDIQSFqWFADLLyvlhnkfWQ 464
Cdd:cd06198    79 RVTVEGPYGR-FTFDDRRARQIWIAGGIGITPFLALLEALAARGDA---RPVTLFYCVRDPEDA-VFLDEL-------RA 146

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958650256 465 ENRPDFVNIQLYLSQTDGiqkiigekyhtlnsRLFIGRPRWKLLFDeiakcnrGKTVGVFCCGPSSISKTLHN 537
Cdd:cd06198   147 LAAAAGVVLHVIDSPSDG--------------RLTLEQLVRALVPD-------LADADVWFCGPPGMADALEK 198
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
386-455 1.06e-04

Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 44.01  E-value: 1.06e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958650256 386 LYIDGPFGS---PFEESLNYevsLCVAGGIGVTPFASILNTLLdDWKPYklRRLYFIWVCRDIQSFQwFADLL 455
Cdd:COG1018    92 LEVSGPRGDfvlDPEPARPL---LLIAGGIGITPFLSMLRTLL-ARGPF--RPVTLVYGARSPADLA-FRDEL 157
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 385-528 4.21e-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: 42.21  E-value: 4.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650256 385 KLYIDGPFGSPF--EESLNYEVsLCVAGGIGVTPFASILNTLLDDWKPYKlrRLYFIWVCRDIQsfqwfaDLLYVLHNKF 462
Cdd:cd06221    80 TVGLRGPFGNGFpvEEMKGKDL-LLVAGGLGLAPLRSLINYILDNREDYG--KVTLLYGARTPE------DLLFKEELKE 150

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958650256 463 WQENrpdfVNIQLYLSQTDGiqkIIGEKYHTlnsrlfiGRPrwKLLFDEIAkCNRGKTVgVFCCGP 528
Cdd:cd06221   151 WAKR----SDVEVILTVDRA---EEGWTGNV-------GLV--TDLLPELT-LDPDNTV-AIVCGP 198
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 408-460 6.37e-04

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: 41.77  E-value: 6.37e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958650256 408 VAGGIGVTPFASILNTLLDDWKPyklRRLYFIWVCRDIQS--F-QWFADLLYVLHN 460
Cdd:cd06184   119 ISAGVGITPMLSMLEALAAEGPG---RPVTFIHAARNSAVhaFrDELEELAARLPN 171
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 385-430 4.17e-03

FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster.


Pssm-ID: 99816 [Multi-domain]  Cd Length: 233  Bit Score: 39.15  E-value: 4.17e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1958650256 385 KLYIDGPFGSPFEesLNYEVSLCVAGGIGVTPfasiLNTLLDDWKP 430
Cdd:cd06220    73 KLGIRGPYGNGFE--LVGGKVLLIGGGIGIAP----LAPLAERLKK 112
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 385-458 4.29e-03

Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates toluene and forms p-cresol as part of a three component toluene-4-monoxygenase system. Electron transfer is from NADH to an NADH:ferredoxin oxidoreductase (TmoF in P. mendocina) to ferredoxin to an iron-containing oxygenase. TmoF is homologous to other mono- and dioxygenase systems within the ferredoxin reductase family.


Pssm-ID: 99787  Cd Length: 232  Bit Score: 39.16  E-value: 4.29e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958650256 385 KLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKPYKlRRLYFIWVCRDIQSFqWFADLLYVL 458
Cdd:cd06190    80 ELELDGPYGLAYLRPDEDRDIVCIAGGSGLAPMLSILRGAARSPYLSD-RPVDLFYGGRTPSDL-CALDELSAL 151
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 408-482 5.02e-03

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: 36.85  E-value: 5.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958650256 408 VAGGIGVTPFASILNTLLDDWKPykLRRLYFIWVCRDiqsfqwFADLLYVLHNKFWQENRPDFVNIQLYLSQTDG 482
Cdd:pfam00175   2 IAGGTGIAPVRSMLRAILEDPKD--PTQVVLVFGNRN------EDDILYREELDELAEKHPGRLTVVYVVSRPEA 68
 
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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