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Conserved domains on  [gi|16758288|ref|NP_445976|]
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NADPH oxidase 4 [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 ...
 311-577 2.79e-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: 169.79  E-value: 2.79e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288 311 IISVINHP-SDVMELRMIKE-NFKARPGQYIILHCPSV-SALENHPFTLTMCPTETKATFGVHFKVV-GDWTERFRDLLL 386
Cdd:cd06186   1 IATVELLPdSDVIRLTIPKPkPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEQDTLSLIIRAKkGFTTRLLRKALK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288 387 PPSSQDSeilpfiqsrnyPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDW-KPYKLRRLYFIWVCRD 465
Cdd:cd06186  81 SPGGGVS-----------LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSsKTSRTRRVKLVWVVRD 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288 466 IQSFQWFADLLyvlhnKFWQENRPDFvNIQLYLSQtdgiqkiigekyhtlnsrlfigrprwkllfdeiakcnrgktvgVF 545
Cdd:cd06186 150 REDLEWFLDEL-----RAAQELEVDG-EIEIYVTR-------------------------------------------VV 180

                       250       260       270
                ....*....|....*....|....*....|..
gi 16758288 546 CCGPSSISKTLHNLSNRNNsyGTKFEYNKESF 577
Cdd:cd06186 181 VCGPPGLVDDVRNAVAKKG--GTGVEFHEESF 210
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 69-205 3.74e-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: 3.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288    69 SLILLPMcrTVLAYLRGSqkVPSRRTRRLLDKSKTLHITCGITICIFSGVHVAAHLVNALNFSVnysEHFLALNAARYQN 148
Cdd:pfam01794   5 ALALLPL--LLLLALRNN--PLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSL---EGILDLLLKRPYN 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 16758288   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 ...
 311-577 2.79e-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: 169.79  E-value: 2.79e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288 311 IISVINHP-SDVMELRMIKE-NFKARPGQYIILHCPSV-SALENHPFTLTMCPTETKATFGVHFKVV-GDWTERFRDLLL 386
Cdd:cd06186   1 IATVELLPdSDVIRLTIPKPkPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEQDTLSLIIRAKkGFTTRLLRKALK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288 387 PPSSQDSeilpfiqsrnyPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDW-KPYKLRRLYFIWVCRD 465
Cdd:cd06186  81 SPGGGVS-----------LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSsKTSRTRRVKLVWVVRD 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288 466 IQSFQWFADLLyvlhnKFWQENRPDFvNIQLYLSQtdgiqkiigekyhtlnsrlfigrprwkllfdeiakcnrgktvgVF 545
Cdd:cd06186 150 REDLEWFLDEL-----RAAQELEVDG-EIEIYVTR-------------------------------------------VV 180

                       250       260       270
                ....*....|....*....|....*....|..
gi 16758288 546 CCGPSSISKTLHNLSNRNNsyGTKFEYNKESF 577
Cdd:cd06186 181 VCGPPGLVDDVRNAVAKKG--GTGVEFHEESF 210
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
423-560 6.14e-25

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 100.88  E-value: 6.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288   423 YEVSLCVAGGIGVTPFASILNTLLDDWKPYKLRRLYFIWVCRDIQSFQWFADLLYVLhnkfwQENRPDFVNIQLYLSQTD 502
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKSKKLKTKKIKFYWVVRDLSSLEWFKDVLNEL-----EELKELNIEIHIYLTGEY 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16758288   503 ----------------GIQKIIGEKYHTLNSRLFIGRPRWKLLFDEIAKCNRGKTVGVFCCGPSSISKTLHNLS 560
Cdd:pfam08030  76 eaedasdqsdssirseNFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 162-500 2.06e-17

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 86.05  E-value: 2.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288  162 LTGVCMVVVLFLMVTASTYAIRVSNYDIFWYTHNLFFVFYMLLLLHVSggllkyqtnldthppgcislnrtpsqnmsiad 241
Cdd:PLN02844 238 LAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHHLYIVFLIFFLFHAG-------------------------------- 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288  242 yvSEHFHGSLPGGFskledhyqktlvkicleepkfqahfpqtwiwisgplcLYCAERLYRCIRSNKPVTIISVINHPSDV 321
Cdd:PLN02844 286 --DRHFYMVFPGIF-------------------------------------LFGLDKLLRIVQSRPETCILSARLFPCKA 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288  322 MELRMIKE-NFKARPGQYIILHCPSVSALENHPFTLTMCPTETKATFGVHFKVVGDWTERFRDLLLPPSSQDSEILPFIQ 400
Cdd:PLN02844 327 IELVLPKDpGLKYAPTSVIFMKIPSISRFQWHPFSITSSSNIDDHTMSVIIKCEGGWTNSLYNKIQAELDSETNQMNCIP 406

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288  401 SRnypklyIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKP-YKL-RRLYFIWVCRDIQSFQWFADLLYV 478
Cdd:PLN02844 407 VA------IEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILKEIASQSSSrYRFpKRVQLIYVVKKSQDICLLNPISSL 480

                        330       340
                 ....*....|....*....|..
gi 16758288  479 LHNKFWQENRpdfVNIQLYLSQ 500
Cdd:PLN02844 481 LLNQSSNQLN---LKLKVFVTQ 499
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 310-503 9.57e-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: 9.57e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288 310 TIISVINHPSDVMELRM--IKENFKARPGQYIILHCPSvsALENHPFTLTMCPTEtKATFGVHFKVVGDWTERFRDLllp 387
Cdd:COG0543   1 KVVSVERLAPDVYLLRLeaPLIALKFKPGQFVMLRVPG--DGLRRPFSIASAPRE-DGTIELHIRVVGKGTRALAEL--- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288 388 pssQDSEilpfiqsrnypKLYIDGPFGSPFEeslnYEVS----LCVAGGIGVTPFASILNTLLDdwkpyKLRRLYFIWVC 463
Cdd:COG0543  75 ---KPGD-----------ELDVRGPLGNGFP----LEDSgrpvLLVAGGTGLAPLRSLAEALLA-----RGRRVTLYLGA 131

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 16758288 464 RDiqsfqwfADLLYvLHNKFWQenrpdFVNIQLYLSQTDG 503
Cdd:COG0543 132 RT-------PEDLY-LLDELEA-----LADFRVVVTTDDG 158
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 69-205 3.74e-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: 3.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288    69 SLILLPMcrTVLAYLRGSqkVPSRRTRRLLDKSKTLHITCGITICIFSGVHVAAHLVNALNFSVnysEHFLALNAARYQN 148
Cdd:pfam01794   5 ALALLPL--LLLLALRNN--PLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSL---EGILDLLLKRPYN 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 16758288   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 ...
 311-577 2.79e-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: 169.79  E-value: 2.79e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288 311 IISVINHP-SDVMELRMIKE-NFKARPGQYIILHCPSV-SALENHPFTLTMCPTETKATFGVHFKVV-GDWTERFRDLLL 386
Cdd:cd06186   1 IATVELLPdSDVIRLTIPKPkPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEQDTLSLIIRAKkGFTTRLLRKALK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288 387 PPSSQDSeilpfiqsrnyPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDW-KPYKLRRLYFIWVCRD 465
Cdd:cd06186  81 SPGGGVS-----------LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSsKTSRTRRVKLVWVVRD 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288 466 IQSFQWFADLLyvlhnKFWQENRPDFvNIQLYLSQtdgiqkiigekyhtlnsrlfigrprwkllfdeiakcnrgktvgVF 545
Cdd:cd06186 150 REDLEWFLDEL-----RAAQELEVDG-EIEIYVTR-------------------------------------------VV 180

                       250       260       270
                ....*....|....*....|....*....|..
gi 16758288 546 CCGPSSISKTLHNLSNRNNsyGTKFEYNKESF 577
Cdd:cd06186 181 VCGPPGLVDDVRNAVAKKG--GTGVEFHEESF 210
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
423-560 6.14e-25

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 100.88  E-value: 6.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288   423 YEVSLCVAGGIGVTPFASILNTLLDDWKPYKLRRLYFIWVCRDIQSFQWFADLLYVLhnkfwQENRPDFVNIQLYLSQTD 502
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKSKKLKTKKIKFYWVVRDLSSLEWFKDVLNEL-----EELKELNIEIHIYLTGEY 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16758288   503 ----------------GIQKIIGEKYHTLNSRLFIGRPRWKLLFDEIAKCNRGKTVGVFCCGPSSISKTLHNLS 560
Cdd:pfam08030  76 eaedasdqsdssirseNFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 162-500 2.06e-17

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 86.05  E-value: 2.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288  162 LTGVCMVVVLFLMVTASTYAIRVSNYDIFWYTHNLFFVFYMLLLLHVSggllkyqtnldthppgcislnrtpsqnmsiad 241
Cdd:PLN02844 238 LAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHHLYIVFLIFFLFHAG-------------------------------- 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288  242 yvSEHFHGSLPGGFskledhyqktlvkicleepkfqahfpqtwiwisgplcLYCAERLYRCIRSNKPVTIISVINHPSDV 321
Cdd:PLN02844 286 --DRHFYMVFPGIF-------------------------------------LFGLDKLLRIVQSRPETCILSARLFPCKA 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288  322 MELRMIKE-NFKARPGQYIILHCPSVSALENHPFTLTMCPTETKATFGVHFKVVGDWTERFRDLLLPPSSQDSEILPFIQ 400
Cdd:PLN02844 327 IELVLPKDpGLKYAPTSVIFMKIPSISRFQWHPFSITSSSNIDDHTMSVIIKCEGGWTNSLYNKIQAELDSETNQMNCIP 406

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288  401 SRnypklyIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKP-YKL-RRLYFIWVCRDIQSFQWFADLLYV 478
Cdd:PLN02844 407 VA------IEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILKEIASQSSSrYRFpKRVQLIYVVKKSQDICLLNPISSL 480

                        330       340
                 ....*....|....*....|..
gi 16758288  479 LHNKFWQENRpdfVNIQLYLSQ 500
Cdd:PLN02844 481 LLNQSSNQLN---LKLKVFVTQ 499
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 312-549 2.47e-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: 2.47e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288 312 ISVINHPSDVMELRMIKEN-FKARPGQYIILHCPSVSALENHPFTLTMCPTETKaTFGVHFKVV--GDWTERFRDLLLpp 388
Cdd:cd00322   1 VATEDVTDDVRLFRLQLPNgFSFKPGQYVDLHLPGDGRGLRRAYSIASSPDEEG-ELELTVKIVpgGPFSAWLHDLKP-- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288 389 ssqDSEILpfiqsrnypklyIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKPyklRRLYFIWVCRDiqs 468
Cdd:cd00322  78 ---GDEVE------------VSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPG---GEITLLYGART--- 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288 469 fqwFADLLYVlhnKFWQENRPDFVNIQLYLSQTDgiqkiigEKYHTLNSRLFIGRPRWKLLFDEIakcnrGKTVGVFCCG 548
Cdd:cd00322 137 ---PADLLFL---DELEELAKEGPNFRLVLALSR-------ESEAKLGPGGRIDREAEILALLPD-----DSGALVYICG 198


                .
gi 16758288 549 P 549
Cdd:cd00322 199 P 199
FAD_binding_8 pfam08022
FAD-binding domain;
307-416 3.70e-16

FAD-binding domain;


Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 74.29  E-value: 3.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288   307 KPVTIISVINHPSDVMELRMIKEN--FKARPGQYIILHC-PSVSALENHPFTLTMCPTETKATfgVHFKVVGDWTERFRD 383
Cdd:pfam08022   2 FGVPKAKVALLPDNVLKLRVSKPKkpFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLS--LHIKVKGGWTRKLAN 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 16758288   384 LLLPpssqdSEILPFIQSRNYPKLYIDGPFGSP 416
Cdd:pfam08022  80 YLSS-----SCPKSPENGKDKPRVLIEGPYGPP 107
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 310-503 9.57e-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: 9.57e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288 310 TIISVINHPSDVMELRM--IKENFKARPGQYIILHCPSvsALENHPFTLTMCPTEtKATFGVHFKVVGDWTERFRDLllp 387
Cdd:COG0543   1 KVVSVERLAPDVYLLRLeaPLIALKFKPGQFVMLRVPG--DGLRRPFSIASAPRE-DGTIELHIRVVGKGTRALAEL--- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288 388 pssQDSEilpfiqsrnypKLYIDGPFGSPFEeslnYEVS----LCVAGGIGVTPFASILNTLLDdwkpyKLRRLYFIWVC 463
Cdd:COG0543  75 ---KPGD-----------ELDVRGPLGNGFP----LEDSgrpvLLVAGGTGLAPLRSLAEALLA-----RGRRVTLYLGA 131

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 16758288 464 RDiqsfqwfADLLYvLHNKFWQenrpdFVNIQLYLSQTDG 503
Cdd:COG0543 132 RT-------PEDLY-LLDELEA-----LADFRVVVTTDDG 158
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 69-205 3.74e-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: 3.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288    69 SLILLPMcrTVLAYLRGSqkVPSRRTRRLLDKSKTLHITCGITICIFSGVHVAAHLVNALNFSVnysEHFLALNAARYQN 148
Cdd:pfam01794   5 ALALLPL--LLLLALRNN--PLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSL---EGILDLLLKRPYN 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 16758288   149 edprkllfttvpgLTGVCMVVVLFLMVTASTYAIRVSNYDIFWYTHNLFFVFYMLLL 205
Cdd:pfam01794  78 -------------ILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
274-465 2.03e-12

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 69.15  E-value: 2.03e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288 274 PKFQAHFPQTWIWIS---GPLCLYCAERLYRCIRSNK-PVTIISVINHPSDVMELRM---IKENFKARPGQYIIL--HCP 344
Cdd:COG4097 178 GPFYWSPPAGVLWAAlaaAGLAAAVYSRLGRPLRSRRhPYRVESVEPEAGDVVELTLrpeGGRWLGHRAGQFAFLrfDGS 257

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288 345 SVSaLENHPFTLTMCPTET-KATFGVhfKVVGDWTERFRDLllPPSSqdseilpfiqsrnypKLYIDGPFGS-PFEESLN 422
Cdd:COG4097 258 PFW-EEAHPFSISSAPGGDgRLRFTI--KALGDFTRRLGRL--KPGT---------------RVYVEGPYGRfTFDRRDT 317

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 16758288 423 YEVSLCVAGGIGVTPFASILNTLldDWKPYKLRRLYFIWVCRD 465
Cdd:COG4097 318 APRQVWIAGGIGITPFLALLRAL--AARPGDQRPVDLFYCVRD 358
PLN02631 PLN02631
ferric-chelate reductase
 279-478 2.57e-10

ferric-chelate reductase


Pssm-ID: 178238 [Multi-domain]  Cd Length: 699  Bit Score: 63.14  E-value: 2.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288  279 HFPQTWIWISGP-LCLYCAERLYRCIRSNKPVTIISVINHPSDVMELRMIK-ENFKARPGQYIILHCPSVSALENHPFTL 356
Cdd:PLN02631 279 HVGDSWFCMILPnIFLFFIDRYLRFLQSTKRSRLVSARILPSDNLELTFSKtPGLHYTPTSILFLHVPSISKLQWHPFTI 358

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288  357 TMCPTETKATFGVHFKVVGDWTERFRDLLlpPSSQDSEilpfiqsrnypKLYIDGPFGSPFEESLNYEVSLCVAGGIGVT 436
Cdd:PLN02631 359 TSSSNLEKDTLSVVIRRQGSWTQKLYTHL--SSSIDSL-----------EVSTEGPYGPNSFDVSRHNSLILVSGGSGIT 425

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 16758288  437 PFASILNTLLDDWKPYKLRRLYFIWVCrdiqSFQWFADLLYV 478
Cdd:PLN02631 426 PFISVIRELIFQSQNPSTKLPDVLLVC----SFKHYHDLAFL 463
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 317-558 3.63e-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: 3.63e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288 317 HPSDVMELRMIKENFKARPGQYIILHCPSVSALENHPFTLTMCPTETK-ATFGVhfKVVGDWTERFRDLLLPPSsqdsei 395
Cdd:cd06198   7 RPTTTLTLEPRGPALGHRAGQFAFLRFDASGWEEPHPFTISSAPDPDGrLRFTI--KALGDYTRRLAERLKPGT------ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288 396 lpfiqsrnypKLYIDGPFGSpFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKPyklRRLYFIWVCRDIQSFqWFADL 475
Cdd:cd06198  79 ----------RVTVEGPYGR-FTFDDRRARQIWIAGGIGITPFLALLEALAARGDA---RPVTLFYCVRDPEDA-VFLDE 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288 476 LyvlhnkfWQENRPDFVNIQLYLSQTDGiqkiigekyhtlnsRLFIGRPRWKLLFDeiakcnrGKTVGVFCCGPSSISKT 555
Cdd:cd06198 144 L-------RALAAAAGVVLHVIDSPSDG--------------RLTLEQLVRALVPD-------LADADVWFCGPPGMADA 195


                ...
gi 16758288 556 LHN 558
Cdd:cd06198 196 LEK 198
PLN02292 PLN02292
ferric-chelate reductase
 173-446 1.38e-09

ferric-chelate reductase


Pssm-ID: 215165 [Multi-domain]  Cd Length: 702  Bit Score: 61.04  E-value: 1.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288  173 LMVTASTY-AIRVSNYDIFWYTHNLFFVFYMLLLLHVSggllkyqtnldthppgcISlnrtpsqnmsiadyvseHFHGSL 251
Cdd:PLN02292 261 LVMWATTYpKIRRRFFEVFFYTHYLYIVFMLFFVFHVG-----------------IS-----------------FALISF 306

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288  252 PGGFskledhyqktlvkicleepkfqahfpqtwiwisgplcLYCAERLYRCIRSNKPVTIISVINHPSDVMELRMIKEN- 330
Cdd:PLN02292 307 PGFY-------------------------------------IFLVDRFLRFLQSRNNVKLVSARVLPCDTVELNFSKNPm 349

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288  331 FKARPGQYIILHCPSVSALENHPFTLTMCPTETKATFGVHFKVVGDWTERFRDLLlppSSQDSeilpfiqsRNYPKLYID 410
Cdd:PLN02292 350 LMYSPTSIMFVNIPSISKLQWHPFTITSSSKLEPEKLSVMIKSQGKWSTKLYHML---SSSDQ--------IDRLAVSVE 418

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 16758288  411 GPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLL 446
Cdd:PLN02292 419 GPYGPASTDFLRHESLVMVSGGSGITPFISIIRDLI 454
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 309-441 8.38e-07

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 50.64  E-value: 8.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288  309 VTIISVINHPSDVMELRM-IKENFKARPGQYIILHCPSVSALENHPFTLTMCPTEtKATFGVhfKVVGDWTERFRDLllp 387
Cdd:PRK00054   7 MKIVENKEIAPNIYTLVLdGEKVFDMKPGQFVMVWVPGVEPLLERPISISDIDKN-EITILY--RKVGEGTKKLSKL--- 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 16758288  388 pSSQDSeilpfiqsrnypkLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASI 441
Cdd:PRK00054  81 -KEGDE-------------LDIRGPLGNGFDLEEIGGKVLLVGGGIGVAPLYEL 120
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
308-476 2.60e-06

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 48.63  E-value: 2.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288 308 PVTIISVINHPSDVMELRM----IKENFKARPGQYIILHCPSVSALENHPFTLTMCPTETKATFGV------------HF 371
Cdd:COG1018   5 PLRVVEVRRETPDVVSFTLeppdGAPLPRFRPGQFVTLRLPIDGKPLRRAYSLSSAPGDGRLEITVkrvpggggsnwlHD 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288 372 KV-VGDwterfrdlllppssqdseilpfiqsrnypKLYIDGPFGS---PFEESLNYevsLCVAGGIGVTPFASILNTLLd 447
Cdd:COG1018  85 HLkVGD-----------------------------TLEVSGPRGDfvlDPEPARPL---LLIAGGIGITPFLSMLRTLL- 131

                       170       180
                ....*....|....*....|....*....
gi 16758288 448 DWKPYklRRLYFIWVCRDIQSFQwFADLL 476
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 ...
 309-451 1.31e-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: 1.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288 309 VTIISVINHPSDVMELRMiKENFKARPGQYIILHCPSVSALenhPFTLTMCPTEtkatFGVHFKVVGDWTERFRDLllpp 388
Cdd:cd06220   1 VTIKEVIDETPTVKTFVF-DWDFDFKPGQFVMVWVPGVDEI---PMSLSYIDGP----NSITVKKVGEATSALHDL---- 68

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758288 389 ssqdseilpfiqsRNYPKLYIDGPFGSPFEesLNYEVSLCVAGGIGVTPfasiLNTLLDDWKP 451
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 ...
 406-549 3.05e-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: 3.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288 406 KLYIDGPFGS-PFEESLNYEVSLCVAGGIGVTPFASILNTLLDDwkPYKLRRLYFIWVCR---DIqsfqWFADLLyvlhn 481
Cdd:cd06183  86 TVEIRGPFGKfEYKPNGKVKHIGMIAGGTGITPMLQLIRAILKD--PEDKTKISLLYANRteeDI----LLREEL----- 154

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16758288 482 KFWQENRPDFVNIQLYLSQTDGIQKIigekyhtlnsrlFIGRPRWKLLFDEIAKCNRGKTVgVFCCGP 549
Cdd:cd06183 155 DELAKKHPDRFKVHYVLSRPPEGWKG------------GVGFITKEMIKEHLPPPPSEDTL-VLVCGP 209
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 329-549 3.31e-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: 3.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288 329 ENFKARPGQYIILHCPSVSALenhPFTLTMCPTEtKATFGVHFKVVGDWTERFRDLllPPSSqdseilpfiqsrnypKLY 408
Cdd:cd06221  24 ELFTFKPGQFVMLSLPGVGEA---PISISSDPTR-RGPLELTIRRVGRVTEALHEL--KPGD---------------TVG 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288 409 IDGPFGSPF--EESLNYEVsLCVAGGIGVTPFASILNTLLDDWKPYKlrRLYFIWVCRDIQsfqwfaDLLYVLHNKFWQE 486
Cdd:cd06221  83 LRGPFGNGFpvEEMKGKDL-LLVAGGLGLAPLRSLINYILDNREDYG--KVTLLYGARTPE------DLLFKEELKEWAK 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758288 487 NrpdfVNIQLYLSQTDGiqkIIGEKYHTlnsrlfiGRPrwKLLFDEIAkCNRGKTVgVFCCGP 549
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 ...
 429-481 6.68e-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: 6.68e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 16758288 429 VAGGIGVTPFASILNTLLDDWKPyklRRLYFIWVCRDIQS--F-QWFADLLYVLHN 481
Cdd:cd06184 119 ISAGVGITPMLSMLEALAAEGPG---RPVTFIHAARNSAVhaFrDELEELAARLPN 171
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 309-491 1.36e-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: 1.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288 309 VTIISVINHpsDVMELR-MIKENFKARPGQYIILHCPSVSALenhPFTLTMCPTETkATFGVHFKVVGDWteRFRDlllp 387
Cdd:cd06189   3 VESIEPLND--DVYRVRlKPPAPLDFLAGQYLDLLLDDGDKR---PFSIASAPHED-GEIELHIRAVPGG--SFSD---- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288 388 pssqdsEILPFIQSRNypKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDwkpyKLRR-LYFIWVCRDI 466
Cdd:cd06189  71 ------YVFEELKENG--LVRIEGPLGDFFLREDSDRPLILIAGGTGFAPIKSILEHLLAQ----GSKRpIHLYWGARTE 138

                       170       180
                ....*....|....*....|....*
gi 16758288 467 qsfqwfADLLYVLHNKFWQENRPDF 491
Cdd:cd06189 139 ------EDLYLDELLEAWAEAHPNF 157
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
 311-438 2.34e-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: 2.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288 311 IISVINHPSDVMELRMIKEN--FKARPGQYIILHCPSVSA-LENHPFTLTMCpTETKATFGVHFKVVGDWTERFRDLllp 387
Cdd:cd06218   1 VLSNREIADDIYRLVLEAPEiaAAAKPGQFVMLRVPDGSDpLLRRPISIHDV-DPEEGTITLLYKVVGKGTRLLSEL--- 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 16758288 388 pSSQDS-EILpfiqsrnypklyidGPFGSPFEESLNYEVSLCVAGGIGVTPF 438
Cdd:cd06218  77 -KAGDElDVL--------------GPLGNGFDLPDDDGKVLLVGGGIGIAPL 113
DHOD_e_trans_like1 cd06219
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 332-442 4.01e-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: 4.01e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758288 332 KARPGQYIIlhcpsVSALENH---PFTLTMCPTEtKATFGVHFKVVGDWTERFRDLllppsSQDSEIlpfiqsrnypkLY 408
Cdd:cd06219  26 KAKPGQFVI-----VRADEKGeriPLTIADWDPE-KGTITIVVQVVGKSTRELATL-----EEGDKI-----------HD 83

                        90       100       110
                ....*....|....*....|....*....|....
gi 16758288 409 IDGPFGSPFeESLNYEVSLCVAGGIGVTPFASIL 442
Cdd:cd06219  84 VVGPLGKPS-EIENYGTVVFVGGGVGIAPIYPIA 116
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 406-479 4.49e-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: 4.49e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16758288 406 KLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKPYKlRRLYFIWVCRDIQSFqWFADLLYVL 479
Cdd:cd06190  80 ELELDGPYGLAYLRPDEDRDIVCIAGGSGLAPMLSILRGAARSPYLSD-RPVDLFYGGRTPSDL-CALDELSAL 151
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 429-503 5.23e-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: 5.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16758288   429 VAGGIGVTPFASILNTLLDDWKPykLRRLYFIWVCRDiqsfqwFADLLYVLHNKFWQENRPDFVNIQLYLSQTDG 503
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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