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Conserved domains on  [gi|425854820|ref|NP_001258744|]
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NADPH oxidase 1 isoform 3 [Homo sapiens]

Protein Classification

NADPH oxidase family protein( domain architecture ID 10484952)

NADPH oxidase family protein such as ferric reductase (FRE) family protein similar to AIM14, a probable cell surface metalloreductase that may be involved in iron or copper homeostasis, and NADPH oxidase 1, a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes and other tissues

EC:  1.-.-.-
Gene Ontology:  GO:0005886|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 ...
 260-527 5.19e-51

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: 173.26  E-value: 5.19e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 260 ITKVVMHP-SKVLELQMNK-RGFSMEVGQYIFVNCPSI-SLLEWHPFTLTSAPEE--DFFSIHIRA-AGDWTENLIRAFE 333
Cdd:cd06186    1 IATVELLPdSDVIRLTIPKpKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDeqDTLSLIIRAkKGFTTRLLRKALK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 334 QQYSPI-PRIEVDGPFGTASEDVFQYEVAVLVGAGIGVTPFASILKSIWYKFQcadHNLKTKKIYFYWICRETGAFSWFN 412
Cdd:cd06186   81 SPGGGVsLKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSS---KTSRTRRVKLVWVVRDREDLEWFL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 413 NLLTSlEQEMEELGKVgflnyRLFLTgwdsnivghaalnfdkatdivtglkqktsfgrpmwdnefstiatshpksvvGVF 492
Cdd:cd06186  158 DELRA-AQELEVDGEI-----EIYVT---------------------------------------------------RVV 180

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 425854820 493 LCGPRTLAKSLRKCCHRyssldPRKVQFYFNKENF 527
Cdd:cd06186  181 VCGPPGLVDDVRNAVAK-----KGGTGVEFHEESF 210
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 48-176 3.01e-12

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: 63.44  E-value: 3.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820   48 FCSRTLRKQLDHNLTFHKLVAYMICLHTAIHIIAHLFNFdcysrsrqatdgslasilsslshdekkggswlnpIQSRNTT 127
Cdd:pfam01794  21 PLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYW----------------------------------LRFSLEG 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 425854820  128 VEYVTFTSIAGLTGVIMTIALILMVTSATEFIRRSYFEVFWYTHHLFIF 176
Cdd:pfam01794  67 ILDLLLKRPYNILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAV 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 ...
 260-527 5.19e-51

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: 173.26  E-value: 5.19e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 260 ITKVVMHP-SKVLELQMNK-RGFSMEVGQYIFVNCPSI-SLLEWHPFTLTSAPEE--DFFSIHIRA-AGDWTENLIRAFE 333
Cdd:cd06186    1 IATVELLPdSDVIRLTIPKpKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDeqDTLSLIIRAkKGFTTRLLRKALK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 334 QQYSPI-PRIEVDGPFGTASEDVFQYEVAVLVGAGIGVTPFASILKSIWYKFQcadHNLKTKKIYFYWICRETGAFSWFN 412
Cdd:cd06186   81 SPGGGVsLKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSS---KTSRTRRVKLVWVVRDREDLEWFL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 413 NLLTSlEQEMEELGKVgflnyRLFLTgwdsnivghaalnfdkatdivtglkqktsfgrpmwdnefstiatshpksvvGVF 492
Cdd:cd06186  158 DELRA-AQELEVDGEI-----EIYVT---------------------------------------------------RVV 180

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 425854820 493 LCGPRTLAKSLRKCCHRyssldPRKVQFYFNKENF 527
Cdd:cd06186  181 VCGPPGLVDDVRNAVAK-----KGGTGVEFHEESF 210
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
358-507 7.94e-38

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 135.93  E-value: 7.94e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820  358 YEVAVLVGAGIGVTPFASILKSIWYKFqcadHNLKTKKIYFYWICRETGAFSWFNNLLTSLEQEMEElgkvgFLNYRLFL 437
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKS----KKLKTKKIKFYWVVRDLSSLEWFKDVLNELEELKEL-----NIEIHIYL 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 425854820  438 TGWD--------SNIVGHAALNFDKATDIVTGLKQKTSFGRPMWDNEFSTIATSHPKSVVGVFLCGPRTLAKSLRKCC 507
Cdd:pfam08030  72 TGEYeaedasdqSDSSIRSENFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 139-380 8.33e-26

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 111.86  E-value: 8.33e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 139 LTGVIMTIALILMVTSATEFIRRSYFEVFWYTHHLFIFYILglgihgiggivrgqteesmneshprkcaesFEMWDDRDS 218
Cdd:PLN02844 238 LAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHHLYIVFLI------------------------------FFLFHAGDR 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 219 HcrrpkfeghppesWKWILAPVILYICERILRFYRSQQKVVITKVVMHPSKVLELQMNKR-GFSMEVGQYIFVNCPSISL 297
Cdd:PLN02844 288 H-------------FYMVFPGIFLFGLDKLLRIVQSRPETCILSARLFPCKAIELVLPKDpGLKYAPTSVIFMKIPSISR 354

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 298 LEWHPFTLTSAPEED--FFSIHIRAAGDWTENLIRAFEQ-------QYSPIPrIEVDGPFGTASEDVFQYEVAVLVGAGI 368
Cdd:PLN02844 355 FQWHPFSITSSSNIDdhTMSVIIKCEGGWTNSLYNKIQAeldsetnQMNCIP-VAIEGPYGPASVDFLRYDSLLLVAGGI 433

                        250
                 ....*....|..
gi 425854820 369 GVTPFASILKSI 380
Cdd:PLN02844 434 GITPFLSILKEI 445
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
223-505 4.74e-18

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 86.49  E-value: 4.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 223 PKFEGHPPESWKWI---LAPVILYICERILRFYRSQQKV-VITKVVMHPSKVLELQM---NKRGFSMEVGQYIFVNCP-S 294
Cdd:COG4097  178 GPFYWSPPAGVLWAalaAAGLAAAVYSRLGRPLRSRRHPyRVESVEPEAGDVVELTLrpeGGRWLGHRAGQFAFLRFDgS 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 295 ISLLEWHPFTLTSAPEED-FFSIHIRAAGDWTENLirafeQQYSPIPRIEVDGPFGTasedvFQYEVA------VLVGAG 367
Cdd:COG4097  258 PFWEEAHPFSISSAPGGDgRLRFTIKALGDFTRRL-----GRLKPGTRVYVEGPYGR-----FTFDRRdtaprqVWIAGG 327

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 368 IGVTPFASILKSIwykfqcADHNLKTKKIYFYWICRETGAFSwFNNLLTSLEQEMEELgkvgflnyRLFLtgWDSNIVGH 447
Cdd:COG4097  328 IGITPFLALLRAL------AARPGDQRPVDLFYCVRDEEDAP-FLEELRALAARLAGL--------RLHL--VVSDEDGR 390

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 425854820 448 aaLNFDKATDIVTGLKQktsfgrpmWDnefstiatshpksvvgVFLCGPRTLAKSLRK 505
Cdd:COG4097  391 --LTAERLRRLVPDLAE--------AD----------------VFFCGPPGMMDALRR 422
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 48-176 3.01e-12

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: 63.44  E-value: 3.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820   48 FCSRTLRKQLDHNLTFHKLVAYMICLHTAIHIIAHLFNFdcysrsrqatdgslasilsslshdekkggswlnpIQSRNTT 127
Cdd:pfam01794  21 PLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYW----------------------------------LRFSLEG 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 425854820  128 VEYVTFTSIAGLTGVIMTIALILMVTSATEFIRRSYFEVFWYTHHLFIF 176
Cdd:pfam01794  67 ILDLLLKRPYNILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAV 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 ...
 260-527 5.19e-51

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: 173.26  E-value: 5.19e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 260 ITKVVMHP-SKVLELQMNK-RGFSMEVGQYIFVNCPSI-SLLEWHPFTLTSAPEE--DFFSIHIRA-AGDWTENLIRAFE 333
Cdd:cd06186    1 IATVELLPdSDVIRLTIPKpKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDeqDTLSLIIRAkKGFTTRLLRKALK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 334 QQYSPI-PRIEVDGPFGTASEDVFQYEVAVLVGAGIGVTPFASILKSIWYKFQcadHNLKTKKIYFYWICRETGAFSWFN 412
Cdd:cd06186   81 SPGGGVsLKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSS---KTSRTRRVKLVWVVRDREDLEWFL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 413 NLLTSlEQEMEELGKVgflnyRLFLTgwdsnivghaalnfdkatdivtglkqktsfgrpmwdnefstiatshpksvvGVF 492
Cdd:cd06186  158 DELRA-AQELEVDGEI-----EIYVT---------------------------------------------------RVV 180

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 425854820 493 LCGPRTLAKSLRKCCHRyssldPRKVQFYFNKENF 527
Cdd:cd06186  181 VCGPPGLVDDVRNAVAK-----KGGTGVEFHEESF 210
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
358-507 7.94e-38

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 135.93  E-value: 7.94e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820  358 YEVAVLVGAGIGVTPFASILKSIWYKFqcadHNLKTKKIYFYWICRETGAFSWFNNLLTSLEQEMEElgkvgFLNYRLFL 437
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKS----KKLKTKKIKFYWVVRDLSSLEWFKDVLNELEELKEL-----NIEIHIYL 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 425854820  438 TGWD--------SNIVGHAALNFDKATDIVTGLKQKTSFGRPMWDNEFSTIATSHPKSVVGVFLCGPRTLAKSLRKCC 507
Cdd:pfam08030  72 TGEYeaedasdqSDSSIRSENFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 139-380 8.33e-26

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 111.86  E-value: 8.33e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 139 LTGVIMTIALILMVTSATEFIRRSYFEVFWYTHHLFIFYILglgihgiggivrgqteesmneshprkcaesFEMWDDRDS 218
Cdd:PLN02844 238 LAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHHLYIVFLI------------------------------FFLFHAGDR 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 219 HcrrpkfeghppesWKWILAPVILYICERILRFYRSQQKVVITKVVMHPSKVLELQMNKR-GFSMEVGQYIFVNCPSISL 297
Cdd:PLN02844 288 H-------------FYMVFPGIFLFGLDKLLRIVQSRPETCILSARLFPCKAIELVLPKDpGLKYAPTSVIFMKIPSISR 354

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 298 LEWHPFTLTSAPEED--FFSIHIRAAGDWTENLIRAFEQ-------QYSPIPrIEVDGPFGTASEDVFQYEVAVLVGAGI 368
Cdd:PLN02844 355 FQWHPFSITSSSNIDdhTMSVIIKCEGGWTNSLYNKIQAeldsetnQMNCIP-VAIEGPYGPASVDFLRYDSLLLVAGGI 433

                        250
                 ....*....|..
gi 425854820 369 GVTPFASILKSI 380
Cdd:PLN02844 434 GITPFLSILKEI 445
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 259-505 9.36e-25

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: 102.53  E-value: 9.36e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 259 VITKVVMHPSKVLELQMNKrGFSMEVGQYIFVNCPSISLLEWHPFTLTSAP-EEDFFSIHIRAA--GDWTENLIRAFEQQ 335
Cdd:cd00322    1 VATEDVTDDVRLFRLQLPN-GFSFKPGQYVDLHLPGDGRGLRRAYSIASSPdEEGELELTVKIVpgGPFSAWLHDLKPGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 336 yspipRIEVDGPFGTASEDVFQYEVAVLVGAGIGVTPFASILKSIWYKFQcadhnlkTKKIYFYWICReTGAFSWFNNLL 415
Cdd:cd00322   80 -----EVEVSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKP-------GGEITLLYGAR-TPADLLFLDEL 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 416 TSLEQEMEelgkvgflNYRLFLTGWDSNIVGHAALNFDKATDIVTGLKQKTSFGRpmwdnefstiatshpksvvgVFLCG 495
Cdd:cd00322  147 EELAKEGP--------NFRLVLALSRESEAKLGPGGRIDREAEILALLPDDSGAL--------------------VYICG 198

                        250
                 ....*....|
gi 425854820 496 PRTLAKSLRK 505
Cdd:cd00322  199 PPAMAKAVRE 208
FAD_binding_8 pfam08022
FAD-binding domain;
262-352 3.48e-24

FAD-binding domain;


Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 97.02  E-value: 3.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820  262 KVVMHPSKVLELQM--NKRGFSMEVGQYIFVNC-PSISLLEWHPFTLTSAPEEDFFSIHIRAAGDWTENLIRAFEQ--QY 336
Cdd:pfam08022   8 KVALLPDNVLKLRVskPKKPFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLSLHIKVKGGWTRKLANYLSSscPK 87

                          90       100
                  ....*....|....*....|.
gi 425854820  337 SPI-----PRIEVDGPFGTAS 352
Cdd:pfam08022  88 SPEngkdkPRVLIEGPYGPPS 108
PLN02292 PLN02292
ferric-chelate reductase
 134-396 4.07e-23

ferric-chelate reductase


Pssm-ID: 215165 [Multi-domain]  Cd Length: 702  Bit Score: 103.41  E-value: 4.07e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 134 TSIAGLTGVIMTIALILMVTSATEFIRRSYFEVFWYTHHLFIFYILGlgihgiggivrgqteesmneshprkcaesfemw 213
Cdd:PLN02292 246 TGVSNLAGEIALVAGLVMWATTYPKIRRRFFEVFFYTHYLYIVFMLF--------------------------------- 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 214 ddrdshcrrpkFEGHPPESWKWILAP-VILYICERILRFYRSQQKVVITKVVMHPSKVLELQMNKRGFSMEVGQYI-FVN 291
Cdd:PLN02292 293 -----------FVFHVGISFALISFPgFYIFLVDRFLRFLQSRNNVKLVSARVLPCDTVELNFSKNPMLMYSPTSImFVN 361

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 292 CPSISLLEWHPFTLTSAP--EEDFFSIHIRAAGDWTENL--IRAFEQQYSPIPrIEVDGPFGTASEDVFQYEVAVLVGAG 367
Cdd:PLN02292 362 IPSISKLQWHPFTITSSSklEPEKLSVMIKSQGKWSTKLyhMLSSSDQIDRLA-VSVEGPYGPASTDFLRHESLVMVSGG 440

                        250       260
                 ....*....|....*....|....*....
gi 425854820 368 IGVTPFASILKSIWYKFQcaDHNLKTKKI 396
Cdd:PLN02292 441 SGITPFISIIRDLIYTSS--TETCKIPKI 467
PLN02631 PLN02631
ferric-chelate reductase
 134-385 1.54e-22

ferric-chelate reductase


Pssm-ID: 178238 [Multi-domain]  Cd Length: 699  Bit Score: 101.66  E-value: 1.54e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 134 TSIAGLTGVI-MTIALILMVTSATEFiRRSYFEVFWYTHHLFIFYILGLGIhgiggivrgqteesmneshprkcaesfem 212
Cdd:PLN02631 229 TYVPNLAGTIaMVIGIAMWVTSLPSF-RRKKFELFFYTHHLYGLYIVFYVI----------------------------- 278

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 213 wddrdshcrrpkfegHPPESWKWILAP-VILYICERILRFYRSQQKVVITKVVMHPSKVLELQMNKR-GFSMEVGQYIFV 290
Cdd:PLN02631 279 ---------------HVGDSWFCMILPnIFLFFIDRYLRFLQSTKRSRLVSARILPSDNLELTFSKTpGLHYTPTSILFL 343

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 291 NCPSISLLEWHPFTLTSAP--EEDFFSIHIRAAGDWTENLiraFEQQYSPIPRIEV--DGPFGTASEDVFQYEVAVLVGA 366
Cdd:PLN02631 344 HVPSISKLQWHPFTITSSSnlEKDTLSVVIRRQGSWTQKL---YTHLSSSIDSLEVstEGPYGPNSFDVSRHNSLILVSG 420

                        250
                 ....*....|....*....
gi 425854820 367 GIGVTPFASILKSIWYKFQ 385
Cdd:PLN02631 421 GSGITPFISVIRELIFQSQ 439
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
223-505 4.74e-18

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 86.49  E-value: 4.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 223 PKFEGHPPESWKWI---LAPVILYICERILRFYRSQQKV-VITKVVMHPSKVLELQM---NKRGFSMEVGQYIFVNCP-S 294
Cdd:COG4097  178 GPFYWSPPAGVLWAalaAAGLAAAVYSRLGRPLRSRRHPyRVESVEPEAGDVVELTLrpeGGRWLGHRAGQFAFLRFDgS 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 295 ISLLEWHPFTLTSAPEED-FFSIHIRAAGDWTENLirafeQQYSPIPRIEVDGPFGTasedvFQYEVA------VLVGAG 367
Cdd:COG4097  258 PFWEEAHPFSISSAPGGDgRLRFTIKALGDFTRRL-----GRLKPGTRVYVEGPYGR-----FTFDRRdtaprqVWIAGG 327

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 368 IGVTPFASILKSIwykfqcADHNLKTKKIYFYWICRETGAFSwFNNLLTSLEQEMEELgkvgflnyRLFLtgWDSNIVGH 447
Cdd:COG4097  328 IGITPFLALLRAL------AARPGDQRPVDLFYCVRDEEDAP-FLEELRALAARLAGL--------RLHL--VVSDEDGR 390

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 425854820 448 aaLNFDKATDIVTGLKQktsfgrpmWDnefstiatshpksvvgVFLCGPRTLAKSLRK 505
Cdd:COG4097  391 --LTAERLRRLVPDLAE--------AD----------------VFFCGPPGMMDALRR 422
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 263-527 2.69e-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: 77.68  E-value: 2.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 263 VVMHPSKVLELQMNKRGFSMEV--GQYIFVNCPSISLLEWHPFTLTSAPEEDF-FSIHIRAAGDWTENLIRAFEqqysPI 339
Cdd:cd06198    2 RVTEVRPTTTLTLEPRGPALGHraGQFAFLRFDASGWEEPHPFTISSAPDPDGrLRFTIKALGDYTRRLAERLK----PG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 340 PRIEVDGPFGtasedVFQYEVA----VLVGAGIGVTPFASILKSiwykFQCADHNlktKKIYFYWICRETGAFswfnnll 415
Cdd:cd06198   78 TRVTVEGPYG-----RFTFDDRrarqIWIAGGIGITPFLALLEA----LAARGDA---RPVTLFYCVRDPEDA------- 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 416 tSLEQEMEELGKVGFLNYRLfltgwdsnivghaalnfdkatdIVTGLKQKTSFGRPMWDNEFStIATSHpksvvgVFLCG 495
Cdd:cd06198  139 -VFLDELRALAAAAGVVLHV----------------------IDSPSDGRLTLEQLVRALVPD-LADAD------VWFCG 188

                        250       260       270
                 ....*....|....*....|....*....|..
gi 425854820 496 PRTLAKSLRKCCHRYsSLDPRKvqfyFNKENF 527
Cdd:cd06198  189 PPGMADALEKGLRAL-GVPARR----FHYERF 215
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 269-400 1.70e-12

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 67.20  E-value: 1.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 269 KVLELQMNKRGFSMEVGQYIFVNCPSisLLEWHPFTLTSAP-EEDFFSIHIRAAGDWTENLIRAFEQQyspipRIEVDGP 347
Cdd:COG0543   13 YLLRLEAPLIALKFKPGQFVMLRVPG--DGLRRPFSIASAPrEDGTIELHIRVVGKGTRALAELKPGD-----ELDVRGP 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 425854820 348 FGTAsedvFQYEV----AVLVGAGIGVTPFASILKsiwykfQCADHNlktKKIYFYW 400
Cdd:COG0543   86 LGNG----FPLEDsgrpVLLVAGGTGLAPLRSLAE------ALLARG---RRVTLYL 129
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 48-176 3.01e-12

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: 63.44  E-value: 3.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820   48 FCSRTLRKQLDHNLTFHKLVAYMICLHTAIHIIAHLFNFdcysrsrqatdgslasilsslshdekkggswlnpIQSRNTT 127
Cdd:pfam01794  21 PLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYW----------------------------------LRFSLEG 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 425854820  128 VEYVTFTSIAGLTGVIMTIALILMVTSATEFIRRSYFEVFWYTHHLFIF 176
Cdd:pfam01794  67 ILDLLLKRPYNILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAV 115
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
285-380 3.07e-07

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 51.33  E-value: 3.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 285 GQYIFVNCPSISLLEWHPFTLTSAPEEDFFSIHIR---------------AAGDwtenlirafeqqyspipRIEVDGPFG 349
Cdd:COG1018   37 GQFVTLRLPIDGKPLRRAYSLSSAPGDGRLEITVKrvpggggsnwlhdhlKVGD-----------------TLEVSGPRG 99

                         90       100       110
                 ....*....|....*....|....*....|....
gi 425854820 350 TAsedVFQYEVA---VLVGAGIGVTPFASILKSI 380
Cdd:COG1018  100 DF---VLDPEPArplLLIAGGIGITPFLSMLRTL 130
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 271-404 6.62e-07

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: 50.24  E-value: 6.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 271 LELQMNKRgFSMEVGQYIFVNCPSIsllEWHPFTLTSAPEED-FFSIHIRAA--GDWTENLIRAFEQQYSpiprIEVDGP 347
Cdd:cd06189   16 VRLKPPAP-LDFLAGQYLDLLLDDG---DKRPFSIASAPHEDgEIELHIRAVpgGSFSDYVFEELKENGL----VRIEGP 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 425854820 348 FGTASEDVFQYEVAVLVGAGIGVTPFASILKsiwykfQCADHNLKtKKIYFYWICRE 404
Cdd:cd06189   88 LGDFFLREDSDRPLILIAGGTGFAPIKSILE------HLLAQGSK-RPIHLYWGART 137
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 277-428 1.28e-06

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 49.87  E-value: 1.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 277 KRGFSMEVGQYIFVNCPSISLLEWHPFTLtSAPEEDFFSIHIRAAGDWTENLIrafeqQYSPIPRIEVDGPFGTASEDVF 356
Cdd:PRK00054  27 EKVFDMKPGQFVMVWVPGVEPLLERPISI-SDIDKNEITILYRKVGEGTKKLS-----KLKEGDELDIRGPLGNGFDLEE 100

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 425854820 357 QYEVAVLVGAGIGVTPFASILKSIWYKFQCADHNL--KTKKIYFYwicretgafswfnnlltslEQEMEELGKV 428
Cdd:PRK00054 101 IGGKVLLVGGGIGVAPLYELAKELKKKGVEVTTVLgaRTKDEVIF-------------------EEEFAKVGDV 155
FNR_like_2 cd06197
FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) ...
 303-404 2.78e-05

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: 45.46  E-value: 2.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 303 FTLTSAPE----EDFFSIHIRAAGDWTENLiraFEQQYSPIP-RIEVD-----GPFGTASEDVFQYEVAVLVGAGIGVTP 372
Cdd:cd06197   63 FTVSSAPPhdpaTDEFEITVRKKGPVTGFL---FQVARRLREqGLEVPvlgvgGEFTLSLPGEGAERKMVWIAGGVGITP 139

                         90       100       110
                 ....*....|....*....|....*....|..
gi 425854820 373 FASILKSIwykfqcADHNLKTKKIYFYWICRE 404
Cdd:cd06197  140 FLAMLRAI------LSSRNTTWDITLLWSLRE 165
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 270-391 3.88e-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: 3.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 270 VLELQMNK-RGFSMEVGQYIFVncpSISLLEW----HPFTLTSAPEEDF--FSIHIRAAGD-WTENLIRAfeqqySPIPR 341
Cdd:cd06196   15 VKRLRFDKpEGYDFTPGQATEV---AIDKPGWrdekRPFTFTSLPEDDVleFVIKSYPDHDgVTEQLGRL-----QPGDT 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 425854820 342 IEVDGPFGTasedvFQYE-VAVLVGAGIGVTPFASILKSIWYKFQCADHNL 391
Cdd:cd06196   87 LLIEDPWGA-----IEYKgPGVFIAGGAGITPFIAILRDLAAKGKLEGNTL 132
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 285-420 4.21e-05

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: 45.24  E-value: 4.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 285 GQYIFVNCPSISLLEWHP--FTLTSAPEEDFFSIHIR---------------AAGDwtenlirafeqqyspipRIEVDGP 347
Cdd:cd06184   40 GQYLSVRVKLPGLGYRQIrqYSLSDAPNGDYYRISVKrepgglvsnylhdnvKVGD-----------------VLEVSAP 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 348 FGTasedvFQYEVA-----VLVGAGIGVTPFASILKsiwykfQCADHNlKTKKIYFYWICR--ETGAF-SWFNNLLTSLE 419
Cdd:cd06184  103 AGD-----FVLDEAsdrplVLISAGVGITPMLSMLE------ALAAEG-PGRPVTFIHAARnsAVHAFrDELEELAARLP 170


                 .
gi 425854820 420 Q 420
Cdd:cd06184  171 N 171
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 280-379 4.32e-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: 4.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 280 FSMEVGQYIFVNCPSISLLewhPFTLTSAPEEDffSIHIRAAGDWTENLIRAFEQQYspiprIEVDGPFGTASEDVfqYE 359
Cdd:cd06220   22 FDFKPGQFVMVWVPGVDEI---PMSLSYIDGPN--SITVKKVGEATSALHDLKEGDK-----LGIRGPYGNGFELV--GG 89

                         90       100
                 ....*....|....*....|
gi 425854820 360 VAVLVGAGIGVTPFASILKS 379
Cdd:cd06220   90 KVLLIGGGIGIAPLAPLAER 109
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 258-377 1.25e-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: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 258 VVITKVVMHPSKVLELQMNKrGFSMEVGQYIFVNCPSISLLeWHPFTLTSAPEED-FFSIHIRAA-GDWTENLIRAFEQq 335
Cdd:cd06187    1 VVSVERLTHDIAVVRLQLDQ-PLPFWAGQYVNVTVPGRPRT-WRAYSPANPPNEDgEIEFHVRAVpGGRVSNALHDELK- 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 425854820 336 ysPIPRIEVDGPFGTAS-EDVFQYEVaVLVGAGIGVTPFASIL 377
Cdd:cd06187   78 --VGDRVRLSGPYGTFYlRRDHDRPV-LCIAGGTGLAPLRAIV 117
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 285-378 1.37e-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: 1.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 285 GQYIFVNCPSISLLEWHPFTLTSA-PEEDFFSIHIRAAGDWTENLIRAFEQQYspiprIEVDGPFGTASEDVFQYEVAVL 363
Cdd:cd06192   28 GQFVFLRNFESPGLERIPLSLAGVdPEEGTISLLVEIRGPKTKLIAELKPGEK-----LDVMGPLGNGFEGPKKGGTVLL 102

                         90
                 ....*....|....*
gi 425854820 364 VGAGIGVTPFASILK 378
Cdd:cd06192  103 VAGGIGLAPLLPIAK 117
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 278-403 2.10e-03

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal portion of the FAD/NAD binding domain contains most of the NADP(H) binding residues and the N-terminal sub-domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. In this ferredoxin like sub-group, the FAD/NAD sub-domains is typically fused to a C-terminal iron-sulfur binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins which act as electron carriers in photosynthesis and ferredoxins which participate in redox chains from bacteria to mammals. Ferredoxin reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99811 [Multi-domain]  Cd Length: 231  Bit Score: 39.88  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 278 RGFSMEVGQYIFVNCPsISL-LEWHPFTLTSAP-EEDFFSIHIRAAGD-----W-TENLirafeqqySPIPRIEVDGPFG 349
Cdd:cd06215   24 SLFAYKPGQFLTLELE-IDGeTVYRAYTLSSSPsRPDSLSITVKRVPGglvsnWlHDNL--------KVGDELWASGPAG 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 425854820 350 TASEDVFQYEVAVLVGAGIGVTPFASILKSIwykfqcADHNLKTkKIYFYWICR 403
Cdd:cd06215   95 EFTLIDHPADKLLLLSAGSGITPMMSMARWL------LDTRPDA-DIVFIHSAR 141
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
 278-403 2.87e-03

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 39.79  E-value: 2.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 278 RGFSMEVGQYIFVNCPSISLLewhPFTLTSAP-EEDFFSIHIRAAGDWTEnliraFEQQYSPIPRIEVDGPFGTA-SEDV 355
Cdd:PRK08345  34 ESFTFKPGQFVQVTIPGVGEV---PISICSSPtRKGFFELCIRRAGRVTT-----VIHRLKEGDIVGVRGPYGNGfPVDE 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 425854820 356 FQYEVAVLVGAGIGVTPFASILksiWYKFqcaDHNLKTKKIYFYWICR 403
Cdd:PRK08345 106 MEGMDLLLIAGGLGMAPLRSVL---LYAM---DNRWKYGNITLIYGAK 147
fre PRK08051
FMN reductase; Validated
 280-405 3.21e-03

FMN reductase; Validated


Pssm-ID: 236142 [Multi-domain]  Cd Length: 232  Bit Score: 39.45  E-value: 3.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425854820 280 FSMEVGQYIFVncpSISLLEWHPFTLTSAP-EEDFFSIHIRAAGD---WTENLIRAFEQQYspiprIEVDGPFGTA---- 351
Cdd:PRK08051  28 FSFRAGQYLMV---VMGEKDKRPFSIASTPrEKGFIELHIGASELnlyAMAVMERILKDGE-----IEVDIPHGDAwlre 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 425854820 352 -SEdvfqyEVAVLVGAGIGVTPFASILKsiwykfQCADHNlKTKKIYFYWICRET 405
Cdd:PRK08051 100 eSE-----RPLLLIAGGTGFSYARSILL------TALAQG-PNRPITLYWGGREE 142
 
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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