NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1676317222|ref|NP_001278855|]
View 

NADPH oxidase 4 isoform d [Homo sapiens]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 245-503 8.41e-50

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: 8.41e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 245 SDVMEIRMVKE-NFKARPGQYITLHCPSV-SALENHPFTLTMCPTETKATFGVHLKIV-GDWTERFRDLLLPPSSQDSei 321
Cdd:cd06186    10 SDVIRLTIPKPkPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEQDTLSLIIRAKkGFTTRLLRKALKSPGGGVS-- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 322 lpfiqsrnyPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDW-KPYKLRRLYFIWVCRDIQSFRWFAD 400
Cdd:cd06186    88 ---------LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSsKTSRTRRVKLVWVVRDREDLEWFLD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 401 LLCMlhnkfWQENRPDYvNIQLYLSQtdgiqkiigekyhalnsrlfigrprwkllfdeiakynrgktvgVFCCGPNSLSK 480
Cdd:cd06186   159 ELRA-----AQELEVDG-EIEIYVTR-------------------------------------------VVVCGPPGLVD 189

                         250       260
                  ....*....|....*....|...
gi 1676317222 481 TLHKLSNQNNsyGTRFEYNKESF 503
Cdd:cd06186   190 DVRNAVAKKG--GTGVEFHEESF 210
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 17-131 1.78e-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: 69.99  E-value: 1.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222  17 SRRTRRLLDKSRTFHITCGVTICIFSGVHVAAHLVNALNFSVnysEDFVELNAARYRDedprkllfttvpgLTGVCMVVV 96
Cdd:pfam01794  23 EWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSL---EGILDLLLKRPYN-------------ILGIIALVL 86

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1676317222  97 LFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLT 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 ...
 245-503 8.41e-50

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: 8.41e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 245 SDVMEIRMVKE-NFKARPGQYITLHCPSV-SALENHPFTLTMCPTETKATFGVHLKIV-GDWTERFRDLLLPPSSQDSei 321
Cdd:cd06186    10 SDVIRLTIPKPkPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEQDTLSLIIRAKkGFTTRLLRKALKSPGGGVS-- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 322 lpfiqsrnyPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDW-KPYKLRRLYFIWVCRDIQSFRWFAD 400
Cdd:cd06186    88 ---------LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSsKTSRTRRVKLVWVVRDREDLEWFLD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 401 LLCMlhnkfWQENRPDYvNIQLYLSQtdgiqkiigekyhalnsrlfigrprwkllfdeiakynrgktvgVFCCGPNSLSK 480
Cdd:cd06186   159 ELRA-----AQELEVDG-EIEIYVTR-------------------------------------------VVVCGPPGLVD 189

                         250       260
                  ....*....|....*....|...
gi 1676317222 481 TLHKLSNQNNsyGTRFEYNKESF 503
Cdd:cd06186   190 DVRNAVAKKG--GTGVEFHEESF 210
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
349-486 2.81e-27

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 107.04  E-value: 2.81e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 349 YEVSLCVAGGIGVTPFASILNTLLDDWKPYKLRRLYFIWVCRDIQSFRWFADLLCML----------HNKFWQENRPDYV 418
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKSKKLKTKKIKFYWVVRDLSSLEWFKDVLNELeelkelnieiHIYLTGEYEAEDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1676317222 419 NIQLYLSQTD-GIQKIIGEKYHALNSRLFIGRPRWKLLFDEIAKYNRGKTVGVFCCGPNSLSKTLHKLS 486
Cdd:pfam08030  81 SDQSDSSIRSeNFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 88-405 1.99e-16

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 82.20  E-value: 1.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222  88 LTGVCMVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLTLHVSggllkyqtnldthppgcislnrtssqnislpe 167
Cdd:PLN02844  238 LAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHHLYIVFLIFFLFHAG-------------------------------- 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 168 yfSEHFHEPFPEGFskpaeftqhkfvkicmeeprfqanfpqtwlwisgplcLYCAERLYRYIRSNKPVTIISVMSHPSDV 247
Cdd:PLN02844  286 --DRHFYMVFPGIF-------------------------------------LFGLDKLLRIVQSRPETCILSARLFPCKA 326

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 248 MEIRMVKE-NFKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHLKIVGDWTERFRDLLLPPSSQDSEILPFIQ 326
Cdd:PLN02844  327 IELVLPKDpGLKYAPTSVIFMKIPSISRFQWHPFSITSSSNIDDHTMSVIIKCEGGWTNSLYNKIQAELDSETNQMNCIP 406

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 327 SRnypklyIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKP-YKL-RRLYFIWVCRDIQSfrwfadlLCM 404
Cdd:PLN02844  407 VA------IEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILKEIASQSSSrYRFpKRVQLIYVVKKSQD-------ICL 473


                  .
gi 1676317222 405 L 405
Cdd:PLN02844  474 L 474
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
200-391 1.17e-14

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 76.09  E-value: 1.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 200 PRFQANFPQTWLWIS-GPLCLYCAerLYRYIRSN-----KPVTIISVMSHPSDVMEIRMVKEN---FKARPGQ--YITLH 268
Cdd:COG4097   178 GPFYWSPPAGVLWAAlAAAGLAAA--VYSRLGRPlrsrrHPYRVESVEPEAGDVVELTLRPEGgrwLGHRAGQfaFLRFD 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 269 CPSVSaLENHPFTLTMCPTET-KATFGVhlKIVGDWTERFRDLllPPSSqdseilpfiqsrnypKLYIDGPFGS-PFEES 346
Cdd:COG4097   256 GSPFW-EEAHPFSISSAPGGDgRLRFTI--KALGDFTRRLGRL--KPGT---------------RVYVEGPYGRfTFDRR 315

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1676317222 347 LNYEVSLCVAGGIGVTPFASILNTLldDWKPYKLRRLYFIWVCRD 391
Cdd:COG4097   316 DTAPRQVWIAGGIGITPFLALLRAL--AARPGDQRPVDLFYCVRD 358
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 17-131 1.78e-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: 69.99  E-value: 1.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222  17 SRRTRRLLDKSRTFHITCGVTICIFSGVHVAAHLVNALNFSVnysEDFVELNAARYRDedprkllfttvpgLTGVCMVVV 96
Cdd:pfam01794  23 EWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSL---EGILDLLLKRPYN-------------ILGIIALVL 86

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1676317222  97 LFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLT 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 ...
 245-503 8.41e-50

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: 8.41e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 245 SDVMEIRMVKE-NFKARPGQYITLHCPSV-SALENHPFTLTMCPTETKATFGVHLKIV-GDWTERFRDLLLPPSSQDSei 321
Cdd:cd06186    10 SDVIRLTIPKPkPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEQDTLSLIIRAKkGFTTRLLRKALKSPGGGVS-- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 322 lpfiqsrnyPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDW-KPYKLRRLYFIWVCRDIQSFRWFAD 400
Cdd:cd06186    88 ---------LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSsKTSRTRRVKLVWVVRDREDLEWFLD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 401 LLCMlhnkfWQENRPDYvNIQLYLSQtdgiqkiigekyhalnsrlfigrprwkllfdeiakynrgktvgVFCCGPNSLSK 480
Cdd:cd06186   159 ELRA-----AQELEVDG-EIEIYVTR-------------------------------------------VVVCGPPGLVD 189

                         250       260
                  ....*....|....*....|...
gi 1676317222 481 TLHKLSNQNNsyGTRFEYNKESF 503
Cdd:cd06186   190 DVRNAVAKKG--GTGVEFHEESF 210
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
349-486 2.81e-27

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 107.04  E-value: 2.81e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 349 YEVSLCVAGGIGVTPFASILNTLLDDWKPYKLRRLYFIWVCRDIQSFRWFADLLCML----------HNKFWQENRPDYV 418
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKSKKLKTKKIKFYWVVRDLSSLEWFKDVLNELeelkelnieiHIYLTGEYEAEDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1676317222 419 NIQLYLSQTD-GIQKIIGEKYHALNSRLFIGRPRWKLLFDEIAKYNRGKTVGVFCCGPNSLSKTLHKLS 486
Cdd:pfam08030  81 SDQSDSSIRSeNFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 88-405 1.99e-16

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 82.20  E-value: 1.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222  88 LTGVCMVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLTLHVSggllkyqtnldthppgcislnrtssqnislpe 167
Cdd:PLN02844  238 LAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHHLYIVFLIFFLFHAG-------------------------------- 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 168 yfSEHFHEPFPEGFskpaeftqhkfvkicmeeprfqanfpqtwlwisgplcLYCAERLYRYIRSNKPVTIISVMSHPSDV 247
Cdd:PLN02844  286 --DRHFYMVFPGIF-------------------------------------LFGLDKLLRIVQSRPETCILSARLFPCKA 326

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 248 MEIRMVKE-NFKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHLKIVGDWTERFRDLLLPPSSQDSEILPFIQ 326
Cdd:PLN02844  327 IELVLPKDpGLKYAPTSVIFMKIPSISRFQWHPFSITSSSNIDDHTMSVIIKCEGGWTNSLYNKIQAELDSETNQMNCIP 406

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 327 SRnypklyIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKP-YKL-RRLYFIWVCRDIQSfrwfadlLCM 404
Cdd:PLN02844  407 VA------IEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILKEIASQSSSrYRFpKRVQLIYVVKKSQD-------ICL 473


                  .
gi 1676317222 405 L 405
Cdd:PLN02844  474 L 474
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 246-475 2.72e-15

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: 75.18  E-value: 2.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 246 DVMEIRMVKEN-FKARPGQYITLHCPSVSALENHPFTLTMCPTETKA-TFGVHLKIVGDWTERFRDLLLppssqDSEILp 323
Cdd:cd00322     9 DVRLFRLQLPNgFSFKPGQYVDLHLPGDGRGLRRAYSIASSPDEEGElELTVKIVPGGPFSAWLHDLKP-----GDEVE- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 324 fiqsrnypklyIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKPyklRRLYFIWVCRDIQSFrWFADLLC 403
Cdd:cd00322    83 -----------VSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPG---GEITLLYGARTPADL-LFLDELE 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1676317222 404 MLHNKFwqenrpdyVNIQLYLSQTDGiqkiigekyhalnSRLFIGRPRWKLLFDEIAKY-NRGKTVGVFCCGP 475
Cdd:cd00322   148 ELAKEG--------PNFRLVLALSRE-------------SEAKLGPGGRIDREAEILALlPDDSGALVYICGP 199
FAD_binding_8 pfam08022
FAD-binding domain;
233-342 2.90e-15

FAD-binding domain;


Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 71.60  E-value: 2.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 233 KPVTIISVMSHPSDVMEIRMVKEN--FKARPGQYITLHC-PSVSALENHPFTLTMCPTETKATfgVHLKIVGDWTERFRD 309
Cdd:pfam08022   2 FGVPKAKVALLPDNVLKLRVSKPKkpFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLS--LHIKVKGGWTRKLAN 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1676317222 310 LLLPpssqdSEILPFIQSRNYPKLYIDGPFGSP 342
Cdd:pfam08022  80 YLSS-----SCPKSPENGKDKPRVLIEGPYGPP 107
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
200-391 1.17e-14

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 76.09  E-value: 1.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 200 PRFQANFPQTWLWIS-GPLCLYCAerLYRYIRSN-----KPVTIISVMSHPSDVMEIRMVKEN---FKARPGQ--YITLH 268
Cdd:COG4097   178 GPFYWSPPAGVLWAAlAAAGLAAA--VYSRLGRPlrsrrHPYRVESVEPEAGDVVELTLRPEGgrwLGHRAGQfaFLRFD 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 269 CPSVSaLENHPFTLTMCPTET-KATFGVhlKIVGDWTERFRDLllPPSSqdseilpfiqsrnypKLYIDGPFGS-PFEES 346
Cdd:COG4097   256 GSPFW-EEAHPFSISSAPGGDgRLRFTI--KALGDFTRRLGRL--KPGT---------------RVYVEGPYGRfTFDRR 315

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1676317222 347 LNYEVSLCVAGGIGVTPFASILNTLldDWKPYKLRRLYFIWVCRD 391
Cdd:COG4097   316 DTAPRQVWIAGGIGITPFLALLRAL--AARPGDQRPVDLFYCVRD 358
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 17-131 1.78e-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: 69.99  E-value: 1.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222  17 SRRTRRLLDKSRTFHITCGVTICIFSGVHVAAHLVNALNFSVnysEDFVELNAARYRDedprkllfttvpgLTGVCMVVV 96
Cdd:pfam01794  23 EWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSL---EGILDLLLKRPYN-------------ILGIIALVL 86

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1676317222  97 LFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLT 131
Cdd:pfam01794  87 LVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 236-391 3.65e-13

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 69.12  E-value: 3.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 236 TIISVMSHPSDV--MEIRMVKENFKARPGQYITLHCPSvsALENHPFTLTMCPTEtKATFGVHLKIVGDWTERFRDLllp 313
Cdd:COG0543     1 KVVSVERLAPDVylLRLEAPLIALKFKPGQFVMLRVPG--DGLRRPFSIASAPRE-DGTIELHIRVVGKGTRALAEL--- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 314 pssQDSEilpfiqsrnypKLYIDGPFGSPFEeslnYEVS----LCVAGGIGVTPFASILNTLLDdwkpyKLRRLYFIWVC 389
Cdd:COG0543    75 ---KPGD-----------ELDVRGPLGNGFP----LEDSgrpvLLVAGGTGLAPLRSLAEALLA-----RGRRVTLYLGA 131


                  ..
gi 1676317222 390 RD 391
Cdd:COG0543   132 RT 133
PLN02292 PLN02292
ferric-chelate reductase
 99-372 6.21e-11

ferric-chelate reductase


Pssm-ID: 215165 [Multi-domain]  Cd Length: 702  Bit Score: 64.89  E-value: 6.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222  99 LMITASTY-AIRVSNYDIFWYTHNLFFVFYMLLTLHVSggllkyqtnldthppgcislnrTSSQNISLPEYFsehfhepf 177
Cdd:PLN02292  261 LVMWATTYpKIRRRFFEVFFYTHYLYIVFMLFFVFHVG----------------------ISFALISFPGFY-------- 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 178 pegfskpaeftqhkfvkicmeeprfqanfpqtwlwisgplcLYCAERLYRYIRSNKPVTIISVMSHPSDVMEIRMVKEN- 256
Cdd:PLN02292  311 -----------------------------------------IFLVDRFLRFLQSRNNVKLVSARVLPCDTVELNFSKNPm 349

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 257 FKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHLKIVGDWTERFRDLLlppSSQDSeilpfiqsRNYPKLYID 336
Cdd:PLN02292  350 LMYSPTSIMFVNIPSISKLQWHPFTITSSSKLEPEKLSVMIKSQGKWSTKLYHML---SSSDQ--------IDRLAVSVE 418

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1676317222 337 GPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLL 372
Cdd:PLN02292  419 GPYGPASTDFLRHESLVMVSGGSGITPFISIIRDLI 454
PLN02631 PLN02631
ferric-chelate reductase
 219-401 8.93e-11

ferric-chelate reductase


Pssm-ID: 178238 [Multi-domain]  Cd Length: 699  Bit Score: 64.29  E-value: 8.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 219 LYCAERLYRYIRSNKPVTIISVMSHPSDVMEIRMVK-ENFKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHL 297
Cdd:PLN02631  294 LFFIDRYLRFLQSTKRSRLVSARILPSDNLELTFSKtPGLHYTPTSILFLHVPSISKLQWHPFTITSSSNLEKDTLSVVI 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 298 KIVGDWTERFRDLLlpPSSQDSeilpfiqsrnyPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKP 377
Cdd:PLN02631  374 RRQGSWTQKLYTHL--SSSIDS-----------LEVSTEGPYGPNSFDVSRHNSLILVSGGSGITPFISVIRELIFQSQN 440

                         170       180
                  ....*....|....*....|....
gi 1676317222 378 YKLRRLYFIWVCrdiqSFRWFADL 401
Cdd:PLN02631  441 PSTKLPDVLLVC----SFKHYHDL 460
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 243-504 1.26e-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: 61.12  E-value: 1.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 243 HPSDVMEIRMVKENFKARPGQYITLHCPSVSALENHPFTLTMCPTETK-ATFGVhlKIVGDWTERFRDLLLPPSsqdsei 321
Cdd:cd06198     7 RPTTTLTLEPRGPALGHRAGQFAFLRFDASGWEEPHPFTISSAPDPDGrLRFTI--KALGDYTRRLAERLKPGT------ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 322 lpfiqsrnypKLYIDGPFGSpFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKPyklRRLYFIWVCRDIQSFrWFADL 401
Cdd:cd06198    79 ----------RVTVEGPYGR-FTFDDRRARQIWIAGGIGITPFLALLEALAARGDA---RPVTLFYCVRDPEDA-VFLDE 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 402 LcmlhnkfWQENRPDYVNIQLYLSQTDGiqkiigekyhalnsRLFIGRPRWKLLFDeiakynrGKTVGVFCCGPNSLSKT 481
Cdd:cd06198   144 L-------RALAAAAGVVLHVIDSPSDG--------------RLTLEQLVRALVPD-------LADADVWFCGPPGMADA 195

                         250       260
                  ....*....|....*....|...
gi 1676317222 482 LHKLSNQNNSYGTRFEYnkESFS 504
Cdd:cd06198   196 LEKGLRALGVPARRFHY--ERFE 216
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
234-475 6.11e-07

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 50.56  E-value: 6.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 234 PVTIISVMSHPSDVMEIRMV----KENFKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGV-------------- 295
Cdd:COG1018     5 PLRVVEVRRETPDVVSFTLEppdgAPLPRFRPGQFVTLRLPIDGKPLRRAYSLSSAPGDGRLEITVkrvpggggsnwlhd 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 296 HLKiVGDwterfrdlllppssqdseilpfiqsrnypKLYIDGPFGS---PFEESLNYevsLCVAGGIGVTPFASILNTLL 372
Cdd:COG1018    85 HLK-VGD-----------------------------TLEVSGPRGDfvlDPEPARPL---LLIAGGIGITPFLSMLRTLL 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 373 dDWKPYklRRLYFIWVCRDIQSFrWFADLLCMLHNKfwqenrpdYVNIQLYLSQTDGiqkiigekyhalnSRLFIGRPRW 452
Cdd:COG1018   132 -ARGPF--RPVTLVYGARSPADL-AFRDELEALAAR--------HPRLRLHPVLSRE-------------PAGLQGRLDA 186

                         250       260
                  ....*....|....*....|...
gi 1676317222 453 KLLFDEIAKYNRGKtvgVFCCGP 475
Cdd:COG1018   187 ELLAALLPDPADAH---VYLCGP 206
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 235-377 4.07e-06

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: 48.01  E-value: 4.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 235 VTIISVmshpsdVMEIRMVK-----ENFKARPGQYITLHCPSVSALenhPFTLTMCPTEtkatFGVHLKIVGDWTERFRD 309
Cdd:cd06220     1 VTIKEV------IDETPTVKtfvfdWDFDFKPGQFVMVWVPGVDEI---PMSLSYIDGP----NSITVKKVGEATSALHD 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1676317222 310 LllppssqdseilpfiqsRNYPKLYIDGPFGSPFEesLNYEVSLCVAGGIGVTPfasiLNTLLDDWKP 377
Cdd:cd06220    68 L-----------------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 1.28e-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: 46.41  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 332 KLYIDGPFGS-PFEESLNYEVSLCVAGGIGVTPFASILNTLLDDwkPYKLRRLYFIWVCRDIQsfrwfaDLLCMLHNKFW 410
Cdd:cd06183    86 TVEIRGPFGKfEYKPNGKVKHIGMIAGGTGITPMLQLIRAILKD--PEDKTKISLLYANRTEE------DILLREELDEL 157

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1676317222 411 QENRPDYVNIQLYLSQTDGIQKIigekyhalnsrlFIGRPRWKLLFDEIAKYNRGKTVgVFCCGP 475
Cdd:cd06183   158 AKKHPDRFKVHYVLSRPPEGWKG------------GVGFITKEMIKEHLPPPPSEDTL-VLVCGP 209
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 254-367 1.61e-05

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 46.40  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 254 KENFKARPGQYITLHCPSVSALENHPFTLTMCPTEtKATFGVhlKIVGDWTERFRDLllppSSQDSeilpfiqsrnypkL 333
Cdd:PRK00054   27 EKVFDMKPGQFVMVWVPGVEPLLERPISISDIDKN-EITILY--RKVGEGTKKLSKL----KEGDE-------------L 86

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1676317222 334 YIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASI 367
Cdd:PRK00054   87 DIRGPLGNGFDLEEIGGKVLLVGGGIGVAPLYEL 120
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 247-368 2.47e-05

FAD/NAD binding domain (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) which then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99789 [Multi-domain]  Cd Length: 243  Bit Score: 45.78  E-value: 2.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 247 VMEIRMVKENFKARPGQYITLHCPSVSALENHPFTLtMCPTETKATFGVHLKIVGDWTERFrdLLLPPSSqdseilpfiq 326
Cdd:cd06192    13 LLTIKAPLAARLFRPGQFVFLRNFESPGLERIPLSL-AGVDPEEGTISLLVEIRGPKTKLI--AELKPGE---------- 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1676317222 327 srnypKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASIL 368
Cdd:cd06192    80 -----KLDVMGPLGNGFEGPKKGGTVLLVAGGIGLAPLLPIA 116
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 355-401 4.79e-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: 4.79e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1676317222 355 VAGGIGVTPFASILNTLLDDWKPyklRRLYFIWVCRDIQS--FR-WFADL 401
Cdd:cd06184   119 ISAGVGITPMLSMLEALAAEGPG---RPVTFIHAARNSAVhaFRdELEEL 165
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 332-475 6.17e-04

Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural similarity to ferredoxin reductase and sequence similarity to dihydroorotate dehydrogenases. Clostridium pasteurianum inducible dissimilatory type sulfite reductase is linked to ferredoxin and reduces NH2OH and SeO3 at a lesser rate than it's normal substate SO3(2-). Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+.


Pssm-ID: 99817 [Multi-domain]  Cd Length: 253  Bit Score: 41.44  E-value: 6.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 332 KLYIDGPFGSPF--EESLNYEVsLCVAGGIGVTPFASILNTLLDDWKPYKlrRLYFiwvcrdIQSFRWFADLLCMLHNKF 409
Cdd:cd06221    80 TVGLRGPFGNGFpvEEMKGKDL-LLVAGGLGLAPLRSLINYILDNREDYG--KVTL------LYGARTPEDLLFKEELKE 150

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1676317222 410 WQenrpDYVNIQLYLSQTDGiqkIIGEKYHalnsrlfIGRPrwKLLFDEIAkYNRGKTVgVFCCGP 475
Cdd:cd06221   151 WA----KRSDVEVILTVDRA---EEGWTGN-------VGLV--TDLLPELT-LDPDNTV-AIVCGP 198
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 235-418 1.93e-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: 39.84  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 235 VTIISVMSHpsDVMEIR-MVKENFKARPGQYITLHCPSVSALenhPFTLTMCPTETkATFGVHLKIVGDWteRFRDlllp 313
Cdd:cd06189     3 VESIEPLND--DVYRVRlKPPAPLDFLAGQYLDLLLDDGDKR---PFSIASAPHED-GEIELHIRAVPGG--SFSD---- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 314 pssqdsEILPFIQSRNypKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDwkpyKLRR-LYFIWVCRDI 392
Cdd:cd06189    71 ------YVFEELKENG--LVRIEGPLGDFFLREDSDRPLILIAGGTGFAPIKSILEHLLAQ----GSKRpIHLYWGARTE 138

                         170       180
                  ....*....|....*....|....*...
gi 1676317222 393 QSFrwFADLLCmlhnKFWQENRP--DYV 418
Cdd:cd06189   139 EDL--YLDELL----EAWAEAHPnfTYV 160
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 355-429 2.28e-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: 37.62  E-value: 2.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1676317222 355 VAGGIGVTPFASILNTLLDDWKPykLRRLYFIWVCRDiqsfrwFADLLCMLHNKFWQENRPDYVNIQLYLSQTDG 429
Cdd:pfam00175   2 IAGGTGIAPVRSMLRAILEDPKD--PTQVVLVFGNRN------EDDILYREELDELAEKHPGRLTVVYVVSRPEA 68
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 332-391 4.69e-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: 38.77  E-value: 4.69e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317222 332 KLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKPYKlRRLYFIWVCRD 391
Cdd:cd06190    80 ELELDGPYGLAYLRPDEDRDIVCIAGGSGLAPMLSILRGAARSPYLSD-RPVDLFYGGRT 138
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH