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Conserved domains on  [gi|7669510|ref|NP_039249|]
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NADPH oxidase 1 isoform 2 [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

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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 ...
 297-515 1.22e-40

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: 145.53  E-value: 1.22e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510  297 ITKVVMHP-SKVLELQMNK-RGFSMEVGQYIFVNCPSI-SLLEWHPFTLTSAPEE--DFFSIHIRA-AGDWTENLIRAFE 370
Cdd:cd06186   1 IATVELLPdSDVIRLTIPKpKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDeqDTLSLIIRAkKGFTTRLLRKALK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510  371 QQYSPI-PRIEVDGPFGTASEDVFQYEVAVLVGAGIGVTPFASILKSIWYKFQCADHNLK------TKKVGHaalnFDKA 443
Cdd:cd06186  81 SPGGGVsLKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSSKTSRTRRvklvwvVRDRED----LEWF 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7669510  444 TDIvtgLKQKTSFGRPMWDNEFSTiatshpksvvGVFLCGPRTLAKSLRKCCHRyssldPRKVQFYFNKENF 515
Cdd:cd06186 157 LDE---LRAAQELEVDGEIEIYVT----------RVVVCGPPGLVDDVRNAVAK-----KGGTGVEFHEESF 210
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 66-213 1.24e-13

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


:

Pssm-ID: 426438 [Multi-domain]  Cd Length: 121  Bit Score: 67.29  E-value: 1.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510     66 LILLPvcrnLLSFLRGTCSFCSRTLRKQLDHNLTFHKLVAYMICLHTAIHIIAHLFNFdcysrsrqatdgslasilssls 145
Cdd:pfam01794   6 LALLP----LLLLLALRNNPLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYW---------------------- 59

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7669510    146 hdekkggswlnpIQSRNTTVEYVTFTSIAGLTGVIMTIALILMVTSATEFIRRSYFEVFWYTHHLFIF 213
Cdd:pfam01794  60 ------------LRFSLEGILDLLLKRPYNILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAV 115
 
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 ...
 297-515 1.22e-40

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: 145.53  E-value: 1.22e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510  297 ITKVVMHP-SKVLELQMNK-RGFSMEVGQYIFVNCPSI-SLLEWHPFTLTSAPEE--DFFSIHIRA-AGDWTENLIRAFE 370
Cdd:cd06186   1 IATVELLPdSDVIRLTIPKpKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDeqDTLSLIIRAkKGFTTRLLRKALK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510  371 QQYSPI-PRIEVDGPFGTASEDVFQYEVAVLVGAGIGVTPFASILKSIWYKFQCADHNLK------TKKVGHaalnFDKA 443
Cdd:cd06186  81 SPGGGVsLKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSSKTSRTRRvklvwvVRDRED----LEWF 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7669510  444 TDIvtgLKQKTSFGRPMWDNEFSTiatshpksvvGVFLCGPRTLAKSLRKCCHRyssldPRKVQFYFNKENF 515
Cdd:cd06186 157 LDE---LRAAQELEVDGEIEIYVT----------RVVVCGPPGLVDDVRNAVAK-----KGGTGVEFHEESF 210
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 176-417 6.32e-26

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 111.86  E-value: 6.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510   176 LTGVIMTIALILMVTSATEFIRRSYFEVFWYTHHLFIFYILglgihgiggivrgqteesmneshprkcaesFEMWDDRDS 255
Cdd:PLN02844 238 LAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHHLYIVFLI------------------------------FFLFHAGDR 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510   256 HcrrpkfeghppesWKWILAPVILYICERILRFYRSQQKVVITKVVMHPSKVLELQMNKR-GFSMEVGQYIFVNCPSISL 334
Cdd:PLN02844 288 H-------------FYMVFPGIFLFGLDKLLRIVQSRPETCILSARLFPCKAIELVLPKDpGLKYAPTSVIFMKIPSISR 354

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510   335 LEWHPFTLTSAPEED--FFSIHIRAAGDWTENLIRAFEQ-------QYSPIPrIEVDGPFGTASEDVFQYEVAVLVGAGI 405
Cdd:PLN02844 355 FQWHPFSITSSSNIDdhTMSVIIKCEGGWTNSLYNKIQAeldsetnQMNCIP-VAIEGPYGPASVDFLRYDSLLLVAGGI 433

                        250
                 ....*....|..
gi 7669510   406 GVTPFASILKSI 417
Cdd:PLN02844 434 GITPFLSILKEI 445
FAD_binding_8 pfam08022
FAD-binding domain;
299-389 2.81e-24

FAD-binding domain;


Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 97.02  E-value: 2.81e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510    299 KVVMHPSKVLELQM--NKRGFSMEVGQYIFVNC-PSISLLEWHPFTLTSAPEEDFFSIHIRAAGDWTENLIRAFEQ--QY 373
Cdd:pfam08022   8 KVALLPDNVLKLRVskPKKPFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLSLHIKVKGGWTRKLANYLSSscPK 87

                          90       100
                  ....*....|....*....|.
gi 7669510    374 SPI-----PRIEVDGPFGTAS 389
Cdd:pfam08022  88 SPEngkdkPRVLIEGPYGPPS 108
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
260-416 3.51e-17

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 83.79  E-value: 3.51e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510  260 PKFEGHPPESWKWI---LAPVILYICERILRFYRSQQKV-VITKVVMHPSKVLELQM---NKRGFSMEVGQYIFVNCP-S 331
Cdd:COG4097 178 GPFYWSPPAGVLWAalaAAGLAAAVYSRLGRPLRSRRHPyRVESVEPEAGDVVELTLrpeGGRWLGHRAGQFAFLRFDgS 257

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510  332 ISLLEWHPFTLTSAPEED-FFSIHIRAAGDWTENLirafeQQYSPIPRIEVDGPFGTasedvFQYEVA------VLVGAG 404
Cdd:COG4097 258 PFWEEAHPFSISSAPGGDgRLRFTIKALGDFTRRL-----GRLKPGTRVYVEGPYGR-----FTFDRRdtaprqVWIAGG 327

                       170
                ....*....|..
gi 7669510  405 IGVTPFASILKS 416
Cdd:COG4097 328 IGITPFLALLRA 339
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 66-213 1.24e-13

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


Pssm-ID: 426438 [Multi-domain]  Cd Length: 121  Bit Score: 67.29  E-value: 1.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510     66 LILLPvcrnLLSFLRGTCSFCSRTLRKQLDHNLTFHKLVAYMICLHTAIHIIAHLFNFdcysrsrqatdgslasilssls 145
Cdd:pfam01794   6 LALLP----LLLLLALRNNPLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYW---------------------- 59

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7669510    146 hdekkggswlnpIQSRNTTVEYVTFTSIAGLTGVIMTIALILMVTSATEFIRRSYFEVFWYTHHLFIF 213
Cdd:pfam01794  60 ------------LRFSLEGILDLLLKRPYNILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAV 115
 
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 ...
 297-515 1.22e-40

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: 145.53  E-value: 1.22e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510  297 ITKVVMHP-SKVLELQMNK-RGFSMEVGQYIFVNCPSI-SLLEWHPFTLTSAPEE--DFFSIHIRA-AGDWTENLIRAFE 370
Cdd:cd06186   1 IATVELLPdSDVIRLTIPKpKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDeqDTLSLIIRAkKGFTTRLLRKALK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510  371 QQYSPI-PRIEVDGPFGTASEDVFQYEVAVLVGAGIGVTPFASILKSIWYKFQCADHNLK------TKKVGHaalnFDKA 443
Cdd:cd06186  81 SPGGGVsLKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSSKTSRTRRvklvwvVRDRED----LEWF 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7669510  444 TDIvtgLKQKTSFGRPMWDNEFSTiatshpksvvGVFLCGPRTLAKSLRKCCHRyssldPRKVQFYFNKENF 515
Cdd:cd06186 157 LDE---LRAAQELEVDGEIEIYVT----------RVVVCGPPGLVDDVRNAVAK-----KGGTGVEFHEESF 210
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 176-417 6.32e-26

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 111.86  E-value: 6.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510   176 LTGVIMTIALILMVTSATEFIRRSYFEVFWYTHHLFIFYILglgihgiggivrgqteesmneshprkcaesFEMWDDRDS 255
Cdd:PLN02844 238 LAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHHLYIVFLI------------------------------FFLFHAGDR 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510   256 HcrrpkfeghppesWKWILAPVILYICERILRFYRSQQKVVITKVVMHPSKVLELQMNKR-GFSMEVGQYIFVNCPSISL 334
Cdd:PLN02844 288 H-------------FYMVFPGIFLFGLDKLLRIVQSRPETCILSARLFPCKAIELVLPKDpGLKYAPTSVIFMKIPSISR 354

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510   335 LEWHPFTLTSAPEED--FFSIHIRAAGDWTENLIRAFEQ-------QYSPIPrIEVDGPFGTASEDVFQYEVAVLVGAGI 405
Cdd:PLN02844 355 FQWHPFSITSSSNIDdhTMSVIIKCEGGWTNSLYNKIQAeldsetnQMNCIP-VAIEGPYGPASVDFLRYDSLLLVAGGI 433

                        250
                 ....*....|..
gi 7669510   406 GVTPFASILKSI 417
Cdd:PLN02844 434 GITPFLSILKEI 445
FAD_binding_8 pfam08022
FAD-binding domain;
299-389 2.81e-24

FAD-binding domain;


Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 97.02  E-value: 2.81e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510    299 KVVMHPSKVLELQM--NKRGFSMEVGQYIFVNC-PSISLLEWHPFTLTSAPEEDFFSIHIRAAGDWTENLIRAFEQ--QY 373
Cdd:pfam08022   8 KVALLPDNVLKLRVskPKKPFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLSLHIKVKGGWTRKLANYLSSscPK 87

                          90       100
                  ....*....|....*....|.
gi 7669510    374 SPI-----PRIEVDGPFGTAS 389
Cdd:pfam08022  88 SPEngkdkPRVLIEGPYGPPS 108
PLN02292 PLN02292
ferric-chelate reductase
 171-419 5.77e-23

ferric-chelate reductase


Pssm-ID: 215165 [Multi-domain]  Cd Length: 702  Bit Score: 102.64  E-value: 5.77e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510   171 TSIAGLTGVIMTIALILMVTSATEFIRRSYFEVFWYTHHLFIFYILGlgihgiggivrgqteesmneshprkcaesfemw 250
Cdd:PLN02292 246 TGVSNLAGEIALVAGLVMWATTYPKIRRRFFEVFFYTHYLYIVFMLF--------------------------------- 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510   251 ddrdshcrrpkFEGHPPESWKWILAP-VILYICERILRFYRSQQKVVITKVVMHPSKVLELQMNKRGFSMEVGQYI-FVN 328
Cdd:PLN02292 293 -----------FVFHVGISFALISFPgFYIFLVDRFLRFLQSRNNVKLVSARVLPCDTVELNFSKNPMLMYSPTSImFVN 361

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510   329 CPSISLLEWHPFTLTSAP--EEDFFSIHIRAAGDWTENL--IRAFEQQYSPIPrIEVDGPFGTASEDVFQYEVAVLVGAG 404
Cdd:PLN02292 362 IPSISKLQWHPFTITSSSklEPEKLSVMIKSQGKWSTKLyhMLSSSDQIDRLA-VSVEGPYGPASTDFLRHESLVMVSGG 440

                        250
                 ....*....|....*
gi 7669510   405 IGVTPFASILKSIWY 419
Cdd:PLN02292 441 SGITPFISIIRDLIY 455
PLN02631 PLN02631
ferric-chelate reductase
 171-422 6.03e-23

ferric-chelate reductase


Pssm-ID: 178238 [Multi-domain]  Cd Length: 699  Bit Score: 102.81  E-value: 6.03e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510   171 TSIAGLTGVI-MTIALILMVTSATEFiRRSYFEVFWYTHHLFIFYILGLGIhgiggivrgqteesmneshprkcaesfem 249
Cdd:PLN02631 229 TYVPNLAGTIaMVIGIAMWVTSLPSF-RRKKFELFFYTHHLYGLYIVFYVI----------------------------- 278

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510   250 wddrdshcrrpkfegHPPESWKWILAP-VILYICERILRFYRSQQKVVITKVVMHPSKVLELQMNKR-GFSMEVGQYIFV 327
Cdd:PLN02631 279 ---------------HVGDSWFCMILPnIFLFFIDRYLRFLQSTKRSRLVSARILPSDNLELTFSKTpGLHYTPTSILFL 343

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510   328 NCPSISLLEWHPFTLTSAP--EEDFFSIHIRAAGDWTENLiraFEQQYSPIPRIEV--DGPFGTASEDVFQYEVAVLVGA 403
Cdd:PLN02631 344 HVPSISKLQWHPFTITSSSnlEKDTLSVVIRRQGSWTQKL---YTHLSSSIDSLEVstEGPYGPNSFDVSRHNSLILVSG 420

                        250
                 ....*....|....*....
gi 7669510   404 GIGVTPFASILKSIWYKFQ 422
Cdd:PLN02631 421 GSGITPFISVIRELIFQSQ 439
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 296-493 2.85e-21

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: 92.51  E-value: 2.85e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510  296 VITKVVMHPSKVLELQMNKrGFSMEVGQYIFVNCPSISLLEWHPFTLTSAP-EEDFFSIHIRAA--GDWTENLIRAFEQQ 372
Cdd:cd00322   1 VATEDVTDDVRLFRLQLPN-GFSFKPGQYVDLHLPGDGRGLRRAYSIASSPdEEGELELTVKIVpgGPFSAWLHDLKPGD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510  373 yspipRIEVDGPFGTASEDVFQYEVAVLVGAGIGVTPFASILKSIWYKFQCADHNL----KTKK-------VGHAALNFD 441
Cdd:cd00322  80 -----EVEVSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPGGEITLlygaRTPAdllfldeLEELAKEGP 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 7669510  442 KATDIVTGLKQKTSFGRPMWDN--EFSTIATSHPKSVVGVFLCGPRTLAKSLRK 493
Cdd:cd00322 155 NFRLVLALSRESEAKLGPGGRIdrEAEILALLPDDSGALVYICGPPAMAKAVRE 208
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
260-416 3.51e-17

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 83.79  E-value: 3.51e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510  260 PKFEGHPPESWKWI---LAPVILYICERILRFYRSQQKV-VITKVVMHPSKVLELQM---NKRGFSMEVGQYIFVNCP-S 331
Cdd:COG4097 178 GPFYWSPPAGVLWAalaAAGLAAAVYSRLGRPLRSRRHPyRVESVEPEAGDVVELTLrpeGGRWLGHRAGQFAFLRFDgS 257

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510  332 ISLLEWHPFTLTSAPEED-FFSIHIRAAGDWTENLirafeQQYSPIPRIEVDGPFGTasedvFQYEVA------VLVGAG 404
Cdd:COG4097 258 PFWEEAHPFSISSAPGGDgRLRFTIKALGDFTRRL-----GRLKPGTRVYVEGPYGR-----FTFDRRdtaprqVWIAGG 327

                       170
                ....*....|..
gi 7669510  405 IGVTPFASILKS 416
Cdd:COG4097 328 IGITPFLALLRA 339
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 300-515 1.40e-16

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: 78.45  E-value: 1.40e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510  300 VVMHPSKVLELQMNKRGFSMEV--GQYIFVNCPSISLLEWHPFTLTSAPEEDF-FSIHIRAAGDWTENLIRAFEqqysPI 376
Cdd:cd06198   2 RVTEVRPTTTLTLEPRGPALGHraGQFAFLRFDASGWEEPHPFTISSAPDPDGrLRFTIKALGDYTRRLAERLK----PG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510  377 PRIEVDGPFGtasedVFQYEVA----VLVGAGIGVTPFASILKSiwykFQcADHNLKTKKVGHAALNFDKATDI--VTGL 450
Cdd:cd06198  78 TRVTVEGPYG-----RFTFDDRrarqIWIAGGIGITPFLALLEA----LA-ARGDARPVTLFYCVRDPEDAVFLdeLRAL 147

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7669510  451 KQKTSF-------GRPMWDNEFSTIATSHP-KSVVGVFLCGPRTLAKSLRKCCHRYsSLDPRKvqfyFNKENF 515
Cdd:cd06198 148 AAAAGVvlhvidsPSDGRLTLEQLVRALVPdLADADVWFCGPPGMADALEKGLRAL-GVPARR----FHYERF 215
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
395-495 6.00e-16

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 75.07  E-value: 6.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510    395 YEVAVLVGAGIGVTPFASILKSIWYKFqcadHNLKTKKV-------GHAALN---------------------------- 439
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKS----KKLKTKKIkfywvvrDLSSLEwfkdvlneleelkelnieihiyltgeye 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7669510    440 -----------------FDKATDIVTGLKQKTSFGRPMWDNEFSTIATSHPKSVVGVFLCGPRTLAKSLRKCC 495
Cdd:pfam08030  77 aedasdqsdssirsenfDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 66-213 1.24e-13

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


Pssm-ID: 426438 [Multi-domain]  Cd Length: 121  Bit Score: 67.29  E-value: 1.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510     66 LILLPvcrnLLSFLRGTCSFCSRTLRKQLDHNLTFHKLVAYMICLHTAIHIIAHLFNFdcysrsrqatdgslasilssls 145
Cdd:pfam01794   6 LALLP----LLLLLALRNNPLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYW---------------------- 59

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7669510    146 hdekkggswlnpIQSRNTTVEYVTFTSIAGLTGVIMTIALILMVTSATEFIRRSYFEVFWYTHHLFIF 213
Cdd:pfam01794  60 ------------LRFSLEGILDLLLKRPYNILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAV 115
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 306-415 3.41e-12

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 66.42  E-value: 3.41e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510  306 KVLELQMNKRGFSMEVGQYIFVNCPSisLLEWHPFTLTSAP-EEDFFSIHIRAAGDWTENLIRAFEQQyspipRIEVDGP 384
Cdd:COG0543  13 YLLRLEAPLIALKFKPGQFVMLRVPG--DGLRRPFSIASAPrEDGTIELHIRVVGKGTRALAELKPGD-----ELDVRGP 85

                        90       100       110
                ....*....|....*....|....*....|....*
gi 7669510  385 FGTAsedvFQYEV----AVLVGAGIGVTPFASILK 415
Cdd:COG0543  86 LGNG----FPLEDsgrpVLLVAGGTGLAPLRSLAE 116
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
322-417 3.33e-07

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 51.33  E-value: 3.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510  322 GQYIFVNCPSISLLEWHPFTLTSAPEEDFFSIHIR---------------AAGDwtenlirafeqqyspipRIEVDGPFG 386
Cdd:COG1018  37 GQFVTLRLPIDGKPLRRAYSLSSAPGDGRLEITVKrvpggggsnwlhdhlKVGD-----------------TLEVSGPRG 99

                        90       100       110
                ....*....|....*....|....*....|....
gi 7669510  387 TAsedVFQYEVA---VLVGAGIGVTPFASILKSI 417
Cdd:COG1018 100 DF---VLDPEPArplLLIAGGIGITPFLSMLRTL 130
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 314-448 1.11e-06

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 49.87  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510   314 KRGFSMEVGQYIFVNCPSISLLEWHPFTLtSAPEEDFFSIHIRAAGDWTENLIrafeqQYSPIPRIEVDGPFGTASEDVF 393
Cdd:PRK00054  27 EKVFDMKPGQFVMVWVPGVEPLLERPISI-SDIDKNEITILYRKVGEGTKKLS-----KLKEGDELDIRGPLGNGFDLEE 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 7669510   394 QYEVAVLVGAGIGVTPFASILKSIWYKFQCADHNL--KTKKVGHAALNFDKATDIVT 448
Cdd:PRK00054 101 IGGKVLLVGGGIGVAPLYELAKELKKKGVEVTTVLgaRTKDEVIFEEEFAKVGDVYV 157
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 307-428 3.77e-05

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 varies in orientation with respect to the NAD(P) binding domain. The N-terminal region 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: 99793 [Multi-domain]  Cd Length: 218  Bit Score: 44.92  E-value: 3.77e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510  307 VLELQMNK-RGFSMEVGQYIFVncpSISLLEW----HPFTLTSAPEEDF--FSIHIRAAGD-WTENLIRAfeqqySPIPR 378
Cdd:cd06196  15 VKRLRFDKpEGYDFTPGQATEV---AIDKPGWrdekRPFTFTSLPEDDVleFVIKSYPDHDgVTEQLGRL-----QPGDT 86

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 7669510  379 IEVDGPFGTasedvFQYE-VAVLVGAGIGVTPFASILKSIWYKFQCADHNL 428
Cdd:cd06196  87 LLIEDPWGA-----IEYKgPGVFIAGGAGITPFIAILRDLAAKGKLEGNTL 132
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 317-416 4.19e-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: 44.93  E-value: 4.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510  317 FSMEVGQYIFVNCPSISLLewhPFTLTSAPEEDffSIHIRAAGDWTENLIRAFEQQYspiprIEVDGPFGTASEDVfqYE 396
Cdd:cd06220  22 FDFKPGQFVMVWVPGVDEI---PMSLSYIDGPN--SITVKKVGEATSALHDLKEGDK-----LGIRGPYGNGFELV--GG 89

                        90       100
                ....*....|....*....|
gi 7669510  397 VAVLVGAGIGVTPFASILKS 416
Cdd:cd06220  90 KVLLIGGGIGIAPLAPLAER 109
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 295-414 1.21e-04

The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons using oxygen as the oxidant. Electron transfer is from NADH via FAD (in the oxygenase reductase) and an [2FE-2S] ferredoxin center (fused to the FAD/NADH domain and/or discrete) to the oxygenase. Dioxygenases add both atoms of oxygen to the substrate, while mono-oxygenases (aka mixed oxygenases) add one atom to the substrate and one atom to water. In dioxygenases, Class I enzymes are 2 component, containing a reductase with Rieske type [2Fe-2S] redox centers and an oxygenase. Class II are 3 component, having discrete flavin and ferredoxin proteins and an oxygenase. Class III have 2 [2Fe-2S] centers, one fused to the flavin domain and the other separate.


Pssm-ID: 99784 [Multi-domain]  Cd Length: 224  Bit Score: 43.35  E-value: 1.21e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510  295 VVITKVVMHPSKVLELQMNKrGFSMEVGQYIFVNCPSISLLeWHPFTLTSAPEED-FFSIHIRAA-GDWTENLIRAFEQq 372
Cdd:cd06187   1 VVSVERLTHDIAVVRLQLDQ-PLPFWAGQYVNVTVPGRPRT-WRAYSPANPPNEDgEIEFHVRAVpGGRVSNALHDELK- 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 7669510  373 ysPIPRIEVDGPFGTAS-EDVFQYEVaVLVGAGIGVTPFASIL 414
Cdd:cd06187  78 --VGDRVRLSGPYGTFYlRRDHDRPV-LCIAGGTGLAPLRAIV 117
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 322-417 1.21e-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: 43.70  E-value: 1.21e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510  322 GQYIFVNCPSISLLEWHP--FTLTSAPEEDFFSIHIR---------------AAGDwtenlirafeqqyspipRIEVDGP 384
Cdd:cd06184  40 GQYLSVRVKLPGLGYRQIrqYSLSDAPNGDYYRISVKrepgglvsnylhdnvKVGD-----------------VLEVSAP 102

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 7669510  385 FGTasedvFQYEVA-----VLVGAGIGVTPFASILKSI 417
Cdd:cd06184 103 AGD-----FVLDEAsdrplVLISAGVGITPMLSMLEAL 135
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 322-415 1.33e-04

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: 43.47  E-value: 1.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510  322 GQYIFVNCPSISLLEWHPFTLTSA-PEEDFFSIHIRAAGDWTENLIRAFEQQYspiprIEVDGPFGTASEDVFQYEVAVL 400
Cdd:cd06192  28 GQFVFLRNFESPGLERIPLSLAGVdPEEGTISLLVEIRGPKTKLIAELKPGEK-----LDVMGPLGNGFEGPKKGGTVLL 102

                        90
                ....*....|....*
gi 7669510  401 VGAGIGVTPFASILK 415
Cdd:cd06192 103 VAGGIGLAPLLPIAK 117
FNR_like_2 cd06197
FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) ...
 340-417 4.99e-04

FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) 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 have a variety of physiological functions in a variety of organisms including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which varies 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 two electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


Pssm-ID: 99794  Cd Length: 220  Bit Score: 41.61  E-value: 4.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510  340 FTLTSAPE----EDFFSIHIRAAGDWTENLiraFEQQYSPIP-RIEVD-----GPFGTASEDVFQYEVAVLVGAGIGVTP 409
Cdd:cd06197  63 FTVSSAPPhdpaTDEFEITVRKKGPVTGFL---FQVARRLREqGLEVPvlgvgGEFTLSLPGEGAERKMVWIAGGVGITP 139


                ....*...
gi 7669510  410 FASILKSI 417
Cdd:cd06197 140 FLAMLRAI 147
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 308-417 5.86e-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: 38.30  E-value: 5.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669510  308 LELQMNKRgFSMEVGQYIFVNCPSIsllEWHPFTLTSAPEED-FFSIHIRAA--GDWTENLIRAFEQQYSpiprIEVDGP 384
Cdd:cd06189  16 VRLKPPAP-LDFLAGQYLDLLLDDG---DKRPFSIASAPHEDgEIELHIRAVpgGSFSDYVFEELKENGL----VRIEGP 87

                        90       100       110
                ....*....|....*....|....*....|...
gi 7669510  385 FGTASEDVFQYEVAVLVGAGIGVTPFASILKSI 417
Cdd:cd06189  88 LGDFFLREDSDRPLILIAGGTGFAPIKSILEHL 120
 
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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