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Conserved domains on  [gi|1958650258|ref|XP_038948872|]
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NADPH oxidase 4 isoform X2 [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 ...
 237-503 1.03e-49

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: 169.41  E-value: 1.03e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 237 IISVINHP-SDVMELRMIKE-NFKARPGQYIILHCPSV-SALENHPFTLTMCPTETKATFGVHFKVV-GDWTERFRDLLL 312
Cdd:cd06186     1 IATVELLPdSDVIRLTIPKPkPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEQDTLSLIIRAKkGFTTRLLRKALK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 313 PPSSQDSeilpfiqsrnyPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDW-KPYKLRRLYFIWVCRD 391
Cdd:cd06186    81 SPGGGVS-----------LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSsKTSRTRRVKLVWVVRD 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 392 IQSFQWFADLLyvlhnKFWQENRPDFvNIQLYLSQtdgiqkiigekyhtlnsrlfigrprwkllfdeiakcnrgktvgVF 471
Cdd:cd06186   150 REDLEWFLDEL-----RAAQELEVDG-EIEIYVTR-------------------------------------------VV 180

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958650258 472 CCGPSSISKTLHNLSNRNNsyGTKFEYNKESF 503
Cdd:cd06186   181 VCGPPGLVDDVRNAVAKKG--GTGVEFHEESF 210
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 17-131 2.30e-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: 69.60  E-value: 2.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258  17 SRRTRRLLDKSKTLHITCGITICIFSGVHVAAHLVNALNFSVnysEHFLALNAARYQNedprkllfttvpgLTGVCMVVV 96
Cdd:pfam01794  23 EWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSL---EGILDLLLKRPYN-------------ILGIIALVL 86

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958650258  97 LFLMVTASTYAIRVSNYDIFWYTHNLFFVFYMLLL 131
Cdd:pfam01794  87 LVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 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 ...
 237-503 1.03e-49

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: 169.41  E-value: 1.03e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 237 IISVINHP-SDVMELRMIKE-NFKARPGQYIILHCPSV-SALENHPFTLTMCPTETKATFGVHFKVV-GDWTERFRDLLL 312
Cdd:cd06186     1 IATVELLPdSDVIRLTIPKPkPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEQDTLSLIIRAKkGFTTRLLRKALK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 313 PPSSQDSeilpfiqsrnyPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDW-KPYKLRRLYFIWVCRD 391
Cdd:cd06186    81 SPGGGVS-----------LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSsKTSRTRRVKLVWVVRD 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 392 IQSFQWFADLLyvlhnKFWQENRPDFvNIQLYLSQtdgiqkiigekyhtlnsrlfigrprwkllfdeiakcnrgktvgVF 471
Cdd:cd06186   150 REDLEWFLDEL-----RAAQELEVDG-EIEIYVTR-------------------------------------------VV 180

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958650258 472 CCGPSSISKTLHNLSNRNNsyGTKFEYNKESF 503
Cdd:cd06186   181 VCGPPGLVDDVRNAVAKKG--GTGVEFHEESF 210
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
349-486 3.55e-25

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 100.88  E-value: 3.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 349 YEVSLCVAGGIGVTPFASILNTLLDDWKPYKLRRLYFIWVCRDIQSFQWFADLLYVLhnkfwQENRPDFVNIQLYLSQTD 428
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKSKKLKTKKIKFYWVVRDLSSLEWFKDVLNEL-----EELKELNIEIHIYLTGEY 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958650258 429 ----------------GIQKIIGEKYHTLNSRLFIGRPRWKLLFDEIAKCNRGKTVGVFCCGPSSISKTLHNLS 486
Cdd:pfam08030  76 eaedasdqsdssirseNFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 88-426 6.65e-18

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 86.82  E-value: 6.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258  88 LTGVCMVVVLFLMVTASTYAIRVSNYDIFWYTHNLFFVFYMLLLLHVSggllkyqtnldthppgcislnrtpsqnmsiad 167
Cdd:PLN02844  238 LAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHHLYIVFLIFFLFHAG-------------------------------- 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 168 yvSEHFHGSLPGGFskledhyqktlvkicleepkfqahfpqtwiwisgplcLYCAERLYRCIRSNKPVTIISVINHPSDV 247
Cdd:PLN02844  286 --DRHFYMVFPGIF-------------------------------------LFGLDKLLRIVQSRPETCILSARLFPCKA 326

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 248 MELRMIKE-NFKARPGQYIILHCPSVSALENHPFTLTMCPTETKATFGVHFKVVGDWTERFRDLLLPPSSQDSEILPFIQ 326
Cdd:PLN02844  327 IELVLPKDpGLKYAPTSVIFMKIPSISRFQWHPFSITSSSNIDDHTMSVIIKCEGGWTNSLYNKIQAELDSETNQMNCIP 406

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 327 SRnypklyIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKP-YKL-RRLYFIWVCRDIQSFQWFADLLYV 404
Cdd:PLN02844  407 VA------IEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILKEIASQSSSrYRFpKRVQLIYVVKKSQDICLLNPISSL 480

                         330       340
                  ....*....|....*....|..
gi 1958650258 405 LHNKFWQENRpdfVNIQLYLSQ 426
Cdd:PLN02844  481 LLNQSSNQLN---LKLKVFVTQ 499
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 236-429 7.77e-16

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 77.21  E-value: 7.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 236 TIISVINHPSDVMELRM--IKENFKARPGQYIILHCPSvsALENHPFTLTMCPTEtKATFGVHFKVVGDWTERFRDLllp 313
Cdd:COG0543     1 KVVSVERLAPDVYLLRLeaPLIALKFKPGQFVMLRVPG--DGLRRPFSIASAPRE-DGTIELHIRVVGKGTRALAEL--- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 314 pssQDSEilpfiqsrnypKLYIDGPFGSPFEeslnYEVS----LCVAGGIGVTPFASILNTLLDdwkpyKLRRLYFIWVC 389
Cdd:COG0543    75 ---KPGD-----------ELDVRGPLGNGFP----LEDSgrpvLLVAGGTGLAPLRSLAEALLA-----RGRRVTLYLGA 131

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1958650258 390 RDiqsfqwfADLLYvLHNKFWQenrpdFVNIQLYLSQTDG 429
Cdd:COG0543   132 RT-------PEDLY-LLDELEA-----LADFRVVVTTDDG 158
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 17-131 2.30e-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: 69.60  E-value: 2.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258  17 SRRTRRLLDKSKTLHITCGITICIFSGVHVAAHLVNALNFSVnysEHFLALNAARYQNedprkllfttvpgLTGVCMVVV 96
Cdd:pfam01794  23 EWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSL---EGILDLLLKRPYN-------------ILGIIALVL 86

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958650258  97 LFLMVTASTYAIRVSNYDIFWYTHNLFFVFYMLLL 131
Cdd:pfam01794  87 LVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 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 ...
 237-503 1.03e-49

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: 169.41  E-value: 1.03e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 237 IISVINHP-SDVMELRMIKE-NFKARPGQYIILHCPSV-SALENHPFTLTMCPTETKATFGVHFKVV-GDWTERFRDLLL 312
Cdd:cd06186     1 IATVELLPdSDVIRLTIPKPkPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEQDTLSLIIRAKkGFTTRLLRKALK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 313 PPSSQDSeilpfiqsrnyPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDW-KPYKLRRLYFIWVCRD 391
Cdd:cd06186    81 SPGGGVS-----------LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSsKTSRTRRVKLVWVVRD 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 392 IQSFQWFADLLyvlhnKFWQENRPDFvNIQLYLSQtdgiqkiigekyhtlnsrlfigrprwkllfdeiakcnrgktvgVF 471
Cdd:cd06186   150 REDLEWFLDEL-----RAAQELEVDG-EIEIYVTR-------------------------------------------VV 180

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958650258 472 CCGPSSISKTLHNLSNRNNsyGTKFEYNKESF 503
Cdd:cd06186   181 VCGPPGLVDDVRNAVAKKG--GTGVEFHEESF 210
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
349-486 3.55e-25

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 100.88  E-value: 3.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 349 YEVSLCVAGGIGVTPFASILNTLLDDWKPYKLRRLYFIWVCRDIQSFQWFADLLYVLhnkfwQENRPDFVNIQLYLSQTD 428
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKSKKLKTKKIKFYWVVRDLSSLEWFKDVLNEL-----EELKELNIEIHIYLTGEY 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958650258 429 ----------------GIQKIIGEKYHTLNSRLFIGRPRWKLLFDEIAKCNRGKTVGVFCCGPSSISKTLHNLS 486
Cdd:pfam08030  76 eaedasdqsdssirseNFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 88-426 6.65e-18

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 86.82  E-value: 6.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258  88 LTGVCMVVVLFLMVTASTYAIRVSNYDIFWYTHNLFFVFYMLLLLHVSggllkyqtnldthppgcislnrtpsqnmsiad 167
Cdd:PLN02844  238 LAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHHLYIVFLIFFLFHAG-------------------------------- 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 168 yvSEHFHGSLPGGFskledhyqktlvkicleepkfqahfpqtwiwisgplcLYCAERLYRCIRSNKPVTIISVINHPSDV 247
Cdd:PLN02844  286 --DRHFYMVFPGIF-------------------------------------LFGLDKLLRIVQSRPETCILSARLFPCKA 326

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 248 MELRMIKE-NFKARPGQYIILHCPSVSALENHPFTLTMCPTETKATFGVHFKVVGDWTERFRDLLLPPSSQDSEILPFIQ 326
Cdd:PLN02844  327 IELVLPKDpGLKYAPTSVIFMKIPSISRFQWHPFSITSSSNIDDHTMSVIIKCEGGWTNSLYNKIQAELDSETNQMNCIP 406

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 327 SRnypklyIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKP-YKL-RRLYFIWVCRDIQSFQWFADLLYV 404
Cdd:PLN02844  407 VA------IEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILKEIASQSSSrYRFpKRVQLIYVVKKSQDICLLNPISSL 480

                         330       340
                  ....*....|....*....|..
gi 1958650258 405 LHNKFWQENRpdfVNIQLYLSQ 426
Cdd:PLN02844  481 LLNQSSNQLN---LKLKVFVTQ 499
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 238-475 2.02e-16

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: 78.26  E-value: 2.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 238 ISVINHPSDVMELRMIKEN-FKARPGQYIILHCPSVSALENHPFTLTMCPTETKaTFGVHFKVV--GDWTERFRDLLLpp 314
Cdd:cd00322     1 VATEDVTDDVRLFRLQLPNgFSFKPGQYVDLHLPGDGRGLRRAYSIASSPDEEG-ELELTVKIVpgGPFSAWLHDLKP-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 315 ssqDSEILpfiqsrnypklyIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKPyklRRLYFIWVCRDiqs 394
Cdd:cd00322    78 ---GDEVE------------VSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPG---GEITLLYGART--- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 395 fqwFADLLYVlhnKFWQENRPDFVNIQLYLSQTDgiqkiigEKYHTLNSRLFIGRPRWKLLFDEIakcnrGKTVGVFCCG 474
Cdd:cd00322   137 ---PADLLFL---DELEELAKEGPNFRLVLALSR-------ESEAKLGPGGRIDREAEILALLPD-----DSGALVYICG 198


                  .
gi 1958650258 475 P 475
Cdd:cd00322   199 P 199
FAD_binding_8 pfam08022
FAD-binding domain;
233-342 3.28e-16

FAD-binding domain;


Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 74.29  E-value: 3.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 233 KPVTIISVINHPSDVMELRMIKEN--FKARPGQYIILHC-PSVSALENHPFTLTMCPTETKATfgVHFKVVGDWTERFRD 309
Cdd:pfam08022   2 FGVPKAKVALLPDNVLKLRVSKPKkpFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLS--LHIKVKGGWTRKLAN 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958650258 310 LLLPpssqdSEILPFIQSRNYPKLYIDGPFGSP 342
Cdd:pfam08022  80 YLSS-----SCPKSPENGKDKPRVLIEGPYGPP 107
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 236-429 7.77e-16

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 77.21  E-value: 7.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 236 TIISVINHPSDVMELRM--IKENFKARPGQYIILHCPSvsALENHPFTLTMCPTEtKATFGVHFKVVGDWTERFRDLllp 313
Cdd:COG0543     1 KVVSVERLAPDVYLLRLeaPLIALKFKPGQFVMLRVPG--DGLRRPFSIASAPRE-DGTIELHIRVVGKGTRALAEL--- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 314 pssQDSEilpfiqsrnypKLYIDGPFGSPFEeslnYEVS----LCVAGGIGVTPFASILNTLLDdwkpyKLRRLYFIWVC 389
Cdd:COG0543    75 ---KPGD-----------ELDVRGPLGNGFP----LEDSgrpvLLVAGGTGLAPLRSLAEALLA-----RGRRVTLYLGA 131

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1958650258 390 RDiqsfqwfADLLYvLHNKFWQenrpdFVNIQLYLSQTDG 429
Cdd:COG0543   132 RT-------PEDLY-LLDELEA-----LADFRVVVTTDDG 158
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 17-131 2.30e-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: 69.60  E-value: 2.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258  17 SRRTRRLLDKSKTLHITCGITICIFSGVHVAAHLVNALNFSVnysEHFLALNAARYQNedprkllfttvpgLTGVCMVVV 96
Cdd:pfam01794  23 EWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSL---EGILDLLLKRPYN-------------ILGIIALVL 86

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958650258  97 LFLMVTASTYAIRVSNYDIFWYTHNLFFVFYMLLL 131
Cdd:pfam01794  87 LVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
200-391 3.94e-13

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 71.08  E-value: 3.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 200 PKFQAHFPQTWIWIS---GPLCLYCAERLYRCIRSNK-PVTIISVINHPSDVMELRM---IKENFKARPGQYIIL--HCP 270
Cdd:COG4097   178 GPFYWSPPAGVLWAAlaaAGLAAAVYSRLGRPLRSRRhPYRVESVEPEAGDVVELTLrpeGGRWLGHRAGQFAFLrfDGS 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 271 SVSaLENHPFTLTMCPTET-KATFGVhfKVVGDWTERFRDLllPPSSqdseilpfiqsrnypKLYIDGPFGS-PFEESLN 348
Cdd:COG4097   258 PFW-EEAHPFSISSAPGGDgRLRFTI--KALGDFTRRLGRL--KPGT---------------RVYVEGPYGRfTFDRRDT 317

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958650258 349 YEVSLCVAGGIGVTPFASILNTLldDWKPYKLRRLYFIWVCRD 391
Cdd:COG4097   318 APRQVWIAGGIGITPFLALLRAL--AARPGDQRPVDLFYCVRD 358
PLN02631 PLN02631
ferric-chelate reductase
 205-404 1.13e-10

ferric-chelate reductase


Pssm-ID: 178238 [Multi-domain]  Cd Length: 699  Bit Score: 63.91  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 205 HFPQTWIWISGP-LCLYCAERLYRCIRSNKPVTIISVINHPSDVMELRMIK-ENFKARPGQYIILHCPSVSALENHPFTL 282
Cdd:PLN02631  279 HVGDSWFCMILPnIFLFFIDRYLRFLQSTKRSRLVSARILPSDNLELTFSKtPGLHYTPTSILFLHVPSISKLQWHPFTI 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 283 TMCPTETKATFGVHFKVVGDWTERFRDLLlpPSSQDSeilpfiqsrnyPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVT 362
Cdd:PLN02631  359 TSSSNLEKDTLSVVIRRQGSWTQKLYTHL--SSSIDS-----------LEVSTEGPYGPNSFDVSRHNSLILVSGGSGIT 425

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958650258 363 PFASILNTLLDDWKPYKLRRLYFIWVCrdiqSFQWFADLLYV 404
Cdd:PLN02631  426 PFISVIRELIFQSQNPSTKLPDVLLVC----SFKHYHDLAFL 463
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 243-484 3.02e-10

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: 59.96  E-value: 3.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 243 HPSDVMELRMIKENFKARPGQYIILHCPSVSALENHPFTLTMCPTETK-ATFGVhfKVVGDWTERFRDLLLPPSsqdsei 321
Cdd:cd06198     7 RPTTTLTLEPRGPALGHRAGQFAFLRFDASGWEEPHPFTISSAPDPDGrLRFTI--KALGDYTRRLAERLKPGT------ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 322 lpfiqsrnypKLYIDGPFGSpFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKPyklRRLYFIWVCRDIQSFqWFADL 401
Cdd:cd06198    79 ----------RVTVEGPYGR-FTFDDRRARQIWIAGGIGITPFLALLEALAARGDA---RPVTLFYCVRDPEDA-VFLDE 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 402 LyvlhnkfWQENRPDFVNIQLYLSQTDGiqkiigekyhtlnsRLFIGRPRWKLLFDeiakcnrGKTVGVFCCGPSSISKT 481
Cdd:cd06198   144 L-------RALAAAAGVVLHVIDSPSDG--------------RLTLEQLVRALVPD-------LADADVWFCGPPGMADA 195


                  ...
gi 1958650258 482 LHN 484
Cdd:cd06198   196 LEK 198
PLN02292 PLN02292
ferric-chelate reductase
 99-372 5.56e-10

ferric-chelate reductase


Pssm-ID: 215165 [Multi-domain]  Cd Length: 702  Bit Score: 61.81  E-value: 5.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258  99 LMVTASTY-AIRVSNYDIFWYTHNLFFVFYMLLLLHVSggllkyqtnldthppgcISlnrtpsqnmsiadyvseHFHGSL 177
Cdd:PLN02292  261 LVMWATTYpKIRRRFFEVFFYTHYLYIVFMLFFVFHVG-----------------IS-----------------FALISF 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 178 PGGFskledhyqktlvkicleepkfqahfpqtwiwisgplcLYCAERLYRCIRSNKPVTIISVINHPSDVMELRMIKEN- 256
Cdd:PLN02292  307 PGFY-------------------------------------IFLVDRFLRFLQSRNNVKLVSARVLPCDTVELNFSKNPm 349

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 257 FKARPGQYIILHCPSVSALENHPFTLTMCPTETKATFGVHFKVVGDWTERFRDLLlppSSQDSeilpfiqsRNYPKLYID 336
Cdd:PLN02292  350 LMYSPTSIMFVNIPSISKLQWHPFTITSSSKLEPEKLSVMIKSQGKWSTKLYHML---SSSDQ--------IDRLAVSVE 418

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1958650258 337 GPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLL 372
Cdd:PLN02292  419 GPYGPASTDFLRHESLVMVSGGSGITPFISIIRDLI 454
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 235-367 6.95e-07

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 50.64  E-value: 6.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 235 VTIISVINHPSDVMELRM-IKENFKARPGQYIILHCPSVSALENHPFTLTMCPTEtKATFGVhfKVVGDWTERFRDLllp 313
Cdd:PRK00054    7 MKIVENKEIAPNIYTLVLdGEKVFDMKPGQFVMVWVPGVEPLLERPISISDIDKN-EITILY--RKVGEGTKKLSKL--- 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958650258 314 pSSQDSeilpfiqsrnypkLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASI 367
Cdd:PRK00054   81 -KEGDE-------------LDIRGPLGNGFDLEEIGGKVLLVGGGIGVAPLYEL 120
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
234-402 2.16e-06

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 48.63  E-value: 2.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 234 PVTIISVINHPSDVMELRM----IKENFKARPGQYIILHCPSVSALENHPFTLTMCPTETKATFGV------------HF 297
Cdd:COG1018     5 PLRVVEVRRETPDVVSFTLeppdGAPLPRFRPGQFVTLRLPIDGKPLRRAYSLSSAPGDGRLEITVkrvpggggsnwlHD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 298 KV-VGDwterfrdlllppssqdseilpfiqsrnypKLYIDGPFGS---PFEESLNYevsLCVAGGIGVTPFASILNTLLd 373
Cdd:COG1018    85 HLkVGD-----------------------------TLEVSGPRGDfvlDPEPARPL---LLIAGGIGITPFLSMLRTLL- 131

                         170       180
                  ....*....|....*....|....*....
gi 1958650258 374 DWKPYklRRLYFIWVCRDIQSFQwFADLL 402
Cdd:COG1018   132 ARGPF--RPVTLVYGARSPADLA-FRDEL 157
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 235-377 1.10e-05

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: 46.86  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 235 VTIISVINHPSDVMELRMiKENFKARPGQYIILHCPSVSALenhPFTLTMCPTEtkatFGVHFKVVGDWTERFRDLllpp 314
Cdd:cd06220     1 VTIKEVIDETPTVKTFVF-DWDFDFKPGQFVMVWVPGVDEI---PMSLSYIDGP----NSITVKKVGEATSALHDL---- 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958650258 315 ssqdseilpfiqsRNYPKLYIDGPFGSPFEesLNYEVSLCVAGGIGVTPfasiLNTLLDDWKP 377
Cdd:cd06220    69 -------------KEGDKLGIRGPYGNGFE--LVGGKVLLIGGGIGIAP----LAPLAERLKK 112
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 332-475 2.98e-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: 45.25  E-value: 2.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 332 KLYIDGPFGS-PFEESLNYEVSLCVAGGIGVTPFASILNTLLDDwkPYKLRRLYFIWVCR---DIqsfqWFADLLyvlhn 407
Cdd:cd06183    86 TVEIRGPFGKfEYKPNGKVKHIGMIAGGTGITPMLQLIRAILKD--PEDKTKISLLYANRteeDI----LLREEL----- 154

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958650258 408 KFWQENRPDFVNIQLYLSQTDGIQKIigekyhtlnsrlFIGRPRWKLLFDEIAKCNRGKTVgVFCCGP 475
Cdd:cd06183   155 DELAKKHPDRFKVHYVLSRPPEGWKG------------GVGFITKEMIKEHLPPPPSEDTL-VLVCGP 209
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 255-475 2.76e-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: 42.59  E-value: 2.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 255 ENFKARPGQYIILHCPSVSALenhPFTLTMCPTEtKATFGVHFKVVGDWTERFRDLllPPSSqdseilpfiqsrnypKLY 334
Cdd:cd06221    24 ELFTFKPGQFVMLSLPGVGEA---PISISSDPTR-RGPLELTIRRVGRVTEALHEL--KPGD---------------TVG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 335 IDGPFGSPF--EESLNYEVsLCVAGGIGVTPFASILNTLLDDWKPYKlrRLYFIWVCRDIQsfqwfaDLLYVLHNKFWQE 412
Cdd:cd06221    83 LRGPFGNGFpvEEMKGKDL-LLVAGGLGLAPLRSLINYILDNREDYG--KVTLLYGARTPE------DLLFKEELKEWAK 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958650258 413 NrpdfVNIQLYLSQTDGiqkIIGEKYHTlnsrlfiGRPrwKLLFDEIAkCNRGKTVgVFCCGP 475
Cdd:cd06221   154 R----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 ...
 355-407 5.59e-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: 5.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958650258 355 VAGGIGVTPFASILNTLLDDWKPyklRRLYFIWVCRDIQS--F-QWFADLLYVLHN 407
Cdd:cd06184   119 ISAGVGITPMLSMLEALAAEGPG---RPVTFIHAARNSAVhaFrDELEELAARLPN 171
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 235-417 1.05e-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: 40.61  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 235 VTIISVINHpsDVMELR-MIKENFKARPGQYIILHCPSVSALenhPFTLTMCPTETkATFGVHFKVVGDWteRFRDlllp 313
Cdd:cd06189     3 VESIEPLND--DVYRVRlKPPAPLDFLAGQYLDLLLDDGDKR---PFSIASAPHED-GEIELHIRAVPGG--SFSD---- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 314 pssqdsEILPFIQSRNypKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDwkpyKLRR-LYFIWVCRDI 392
Cdd:cd06189    71 ------YVFEELKENG--LVRIEGPLGDFFLREDSDRPLILIAGGTGFAPIKSILEHLLAQ----GSKRpIHLYWGARTE 138

                         170       180
                  ....*....|....*....|....*
gi 1958650258 393 qsfqwfADLLYVLHNKFWQENRPDF 417
Cdd:cd06189   139 ------EDLYLDELLEAWAEAHPNF 157
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
 237-364 1.96e-03

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: 39.84  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 237 IISVINHPSDVMELRMIKEN--FKARPGQYIILHCPSVSA-LENHPFTLTMCpTETKATFGVHFKVVGDWTERFRDLllp 313
Cdd:cd06218     1 VLSNREIADDIYRLVLEAPEiaAAAKPGQFVMLRVPDGSDpLLRRPISIHDV-DPEEGTITLLYKVVGKGTRLLSEL--- 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958650258 314 pSSQDS-EILpfiqsrnypklyidGPFGSPFEESLNYEVSLCVAGGIGVTPF 364
Cdd:cd06218    77 -KAGDElDVL--------------GPLGNGFDLPDDDGKVLLVGGGIGIAPL 113
DHOD_e_trans_like1 cd06219
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 258-368 3.37e-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 NAD binding. 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 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, and then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99815 [Multi-domain]  Cd Length: 248  Bit Score: 39.10  E-value: 3.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650258 258 KARPGQYIIlhcpsVSALENH---PFTLTMCPTEtKATFGVHFKVVGDWTERFRDLllppsSQDSEIlpfiqsrnypkLY 334
Cdd:cd06219    26 KAKPGQFVI-----VRADEKGeriPLTIADWDPE-KGTITIVVQVVGKSTRELATL-----EEGDKI-----------HD 83

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958650258 335 IDGPFGSPFeESLNYEVSLCVAGGIGVTPFASIL 368
Cdd:cd06219    84 VVGPLGKPS-EIENYGTVVFVGGGVGIAPIYPIA 116
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 332-405 3.77e-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: 3.77e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958650258 332 KLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKPYKlRRLYFIWVCRDIQSFqWFADLLYVL 405
Cdd:cd06190    80 ELELDGPYGLAYLRPDEDRDIVCIAGGSGLAPMLSILRGAARSPYLSD-RPVDLFYGGRTPSDL-CALDELSAL 151
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 355-429 4.50e-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: 4.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958650258 355 VAGGIGVTPFASILNTLLDDWKPykLRRLYFIWVCRDiqsfqwFADLLYVLHNKFWQENRPDFVNIQLYLSQTDG 429
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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