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Conserved domains on  [gi|291384112|ref|XP_002708687|]
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NADPH oxidase 4 isoform X1 [Oryctolagus cuniculus]

Protein Classification

ferric reductase family protein( domain architecture ID 10484952)

ferric reductase family protein functions as an oxidoreductase, such as human NADPH oxidase 1, a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes and other tissues

EC:  1.-.-.-
Gene Ontology:  GO:0050661|GO:0016491|GO:0016020

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 311-577 4.59e-49

NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as superoxide and hydrogen peroxide. ROS were originally identified as bactericidal agents in phagocytes, but are now also implicated in cell signaling and metabolism. NOX has a 6-alpha helix heme-binding transmembrane domain fused to a flavoprotein with the nucleotide binding domain located in the cytoplasm. Duox enzymes link a peroxidase domain to the NOX domain via a single transmembrane and EF-hand Ca2+ binding sites. The flavoprotein module has a ferredoxin like FAD/NADPH binding domain. In classical phagocytic NOX2, electron transfer occurs from NADPH to FAD to the heme of cytb to oxygen leading to superoxide formation.


:

Pssm-ID: 99783 [Multi-domain]  Cd Length: 210  Bit Score: 169.02  E-value: 4.59e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 311 ILSVISHP-SDVMEIRMVKE-NFKARPGQYVILHCPSV-SALENHPFTLTMCPTEKKATFGVHLKIV-GDWTERFRDLLL 386
Cdd:cd06186    1 IATVELLPdSDVIRLTIPKPkPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEQDTLSLIIRAKkGFTTRLLRKALK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 387 PPSSQDSeilpfiqtrnyPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDW-KPYKLRRLYFIWVCRD 465
Cdd:cd06186   81 SPGGGVS-----------LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSsKTSRTRRVKLVWVVRD 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 466 IQSFCWFADLLCMlynkfWQENRPDYvNIQLYLSQtdgiqkiigekyhalnsrlfigrpqwkllfdeiakynrgktvgVF 545
Cdd:cd06186  150 REDLEWFLDELRA-----AQELEVDG-EIEIYVTR-------------------------------------------VV 180

                        250       260       270
                 ....*....|....*....|....*....|..
gi 291384112 546 CCGPNSLSKILHKLSNQSNsyGTRFEYNKESF 577
Cdd:cd06186  181 VCGPPGLVDDVRNAVAKKG--GTGVEFHEESF 210
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 69-205 2.04e-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: 66.91  E-value: 2.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112   69 SLILLPMcrTLLAYLRGSqkVPSRRTRRVLDKSRTFHITCGVTICIFSGVHVAAHLVNALNFSVNYNEDFIELNAARyrd 148
Cdd:pfam01794   5 ALALLPL--LLLLALRNN--PLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSLEGILDLLLKRPYN--- 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 291384112  149 edprkllfttvpgLTGVCMVMVLFLMVTASTYAIRVSNYDIFWYTHNLFFVFYMLLM 205
Cdd:pfam01794  78 -------------ILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
 
Name Accession Description Interval E-value
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 311-577 4.59e-49

NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as superoxide and hydrogen peroxide. ROS were originally identified as bactericidal agents in phagocytes, but are now also implicated in cell signaling and metabolism. NOX has a 6-alpha helix heme-binding transmembrane domain fused to a flavoprotein with the nucleotide binding domain located in the cytoplasm. Duox enzymes link a peroxidase domain to the NOX domain via a single transmembrane and EF-hand Ca2+ binding sites. The flavoprotein module has a ferredoxin like FAD/NADPH binding domain. In classical phagocytic NOX2, electron transfer occurs from NADPH to FAD to the heme of cytb to oxygen leading to superoxide formation.


Pssm-ID: 99783 [Multi-domain]  Cd Length: 210  Bit Score: 169.02  E-value: 4.59e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 311 ILSVISHP-SDVMEIRMVKE-NFKARPGQYVILHCPSV-SALENHPFTLTMCPTEKKATFGVHLKIV-GDWTERFRDLLL 386
Cdd:cd06186    1 IATVELLPdSDVIRLTIPKPkPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEQDTLSLIIRAKkGFTTRLLRKALK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 387 PPSSQDSeilpfiqtrnyPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDW-KPYKLRRLYFIWVCRD 465
Cdd:cd06186   81 SPGGGVS-----------LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSsKTSRTRRVKLVWVVRD 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 466 IQSFCWFADLLCMlynkfWQENRPDYvNIQLYLSQtdgiqkiigekyhalnsrlfigrpqwkllfdeiakynrgktvgVF 545
Cdd:cd06186  150 REDLEWFLDELRA-----AQELEVDG-EIEIYVTR-------------------------------------------VV 180

                        250       260       270
                 ....*....|....*....|....*....|..
gi 291384112 546 CCGPNSLSKILHKLSNQSNsyGTRFEYNKESF 577
Cdd:cd06186  181 VCGPPGLVDDVRNAVAKKG--GTGVEFHEESF 210
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
423-560 7.47e-25

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 100.49  E-value: 7.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112  423 YEVSLCVAGGIGVTPFASILNTLLDDWKPYKLRRLYFIWVCRDIQSFCWFADLLCMLynkfwQENRPDYVNIQLYLSQTD 502
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKSKKLKTKKIKFYWVVRDLSSLEWFKDVLNEL-----EELKELNIEIHIYLTGEY 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291384112  503 ----------------GIQKIIGEKYHALNSRLFIGRPQWKLLFDEIAKYNRGKTVGVFCCGPNSLSKILHKLS 560
Cdd:pfam08030  76 eaedasdqsdssirseNFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 69-500 6.92e-18

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 87.60  E-value: 6.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112  69 SLILLPMCRTL-LAYLRGSQKVPSRRtrrvldksrtFHITCGVTICIFSGVHVAAHLvnalnfsvnynedFIELNAARYR 147
Cdd:PLN02844 168 ALLLLPVLRGLaLFRLLGIQFEASVR----------YHVWLGTSMIFFATVHGASTL-------------FIWGISHHIQ 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 148 DEdPRKLLFTTVPGLTGVCMVMVLFLMVTASTYAIRVSNYDIFWYTHNLFFVFYMLLMLHVSggllkyqtnlDTHppgci 227
Cdd:PLN02844 225 DE-IWKWQKTGRIYLAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHHLYIVFLIFFLFHAG----------DRH----- 288

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 228 slnqthhqdislplhhsehlpgsflgefskpeelaqntfmkicveeprfratfpqtWLWISGPLCLYCAERLYRCIRSNK 307
Cdd:PLN02844 289 --------------------------------------------------------FYMVFPGIFLFGLDKLLRIVQSRP 312

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 308 PVTILSVISHPSDVMEIRMVKE-NFKARPGQYVILHCPSVSALENHPFTLTMCPTEKKATFGVHLKIVGDWTERFRDLLL 386
Cdd:PLN02844 313 ETCILSARLFPCKAIELVLPKDpGLKYAPTSVIFMKIPSISRFQWHPFSITSSSNIDDHTMSVIIKCEGGWTNSLYNKIQ 392

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 387 PPSSQDSEILPFIQTRnypklyIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKP-YKL-RRLYFIWVCR 464
Cdd:PLN02844 393 AELDSETNQMNCIPVA------IEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILKEIASQSSSrYRFpKRVQLIYVVK 466

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 291384112 465 DIQSFCWFADLLCMLYNKFWQENRpdyVNIQLYLSQ 500
Cdd:PLN02844 467 KSQDICLLNPISSLLLNQSSNQLN---LKLKVFVTQ 499
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 310-475 4.24e-15

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 75.28  E-value: 4.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 310 TILSVISHPSDV--MEIRMVKENFKARPGQYVILHCPSvsALENHPFTLTMCPTEKKaTFGVHLKIVGDWTERFRDLllp 387
Cdd:COG0543    1 KVVSVERLAPDVylLRLEAPLIALKFKPGQFVMLRVPG--DGLRRPFSIASAPREDG-TIELHIRVVGKGTRALAEL--- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 388 pssQDSEilpfiqtrnypKLYIDGPFGSPFEeslnYEVS----LCVAGGIGVTPFASILNTLLDdwkpyKLRRLYFIWVC 463
Cdd:COG0543   75 ---KPGD-----------ELDVRGPLGNGFP----LEDSgrpvLLVAGGTGLAPLRSLAEALLA-----RGRRVTLYLGA 131

                        170
                 ....*....|..
gi 291384112 464 RDIQSFCWFADL 475
Cdd:COG0543  132 RTPEDLYLLDEL 143
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 69-205 2.04e-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: 66.91  E-value: 2.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112   69 SLILLPMcrTLLAYLRGSqkVPSRRTRRVLDKSRTFHITCGVTICIFSGVHVAAHLVNALNFSVNYNEDFIELNAARyrd 148
Cdd:pfam01794   5 ALALLPL--LLLLALRNN--PLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSLEGILDLLLKRPYN--- 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 291384112  149 edprkllfttvpgLTGVCMVMVLFLMVTASTYAIRVSNYDIFWYTHNLFFVFYMLLM 205
Cdd:pfam01794  78 -------------ILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
 
Name Accession Description Interval E-value
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 311-577 4.59e-49

NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as superoxide and hydrogen peroxide. ROS were originally identified as bactericidal agents in phagocytes, but are now also implicated in cell signaling and metabolism. NOX has a 6-alpha helix heme-binding transmembrane domain fused to a flavoprotein with the nucleotide binding domain located in the cytoplasm. Duox enzymes link a peroxidase domain to the NOX domain via a single transmembrane and EF-hand Ca2+ binding sites. The flavoprotein module has a ferredoxin like FAD/NADPH binding domain. In classical phagocytic NOX2, electron transfer occurs from NADPH to FAD to the heme of cytb to oxygen leading to superoxide formation.


Pssm-ID: 99783 [Multi-domain]  Cd Length: 210  Bit Score: 169.02  E-value: 4.59e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 311 ILSVISHP-SDVMEIRMVKE-NFKARPGQYVILHCPSV-SALENHPFTLTMCPTEKKATFGVHLKIV-GDWTERFRDLLL 386
Cdd:cd06186    1 IATVELLPdSDVIRLTIPKPkPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEQDTLSLIIRAKkGFTTRLLRKALK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 387 PPSSQDSeilpfiqtrnyPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDW-KPYKLRRLYFIWVCRD 465
Cdd:cd06186   81 SPGGGVS-----------LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSsKTSRTRRVKLVWVVRD 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 466 IQSFCWFADLLCMlynkfWQENRPDYvNIQLYLSQtdgiqkiigekyhalnsrlfigrpqwkllfdeiakynrgktvgVF 545
Cdd:cd06186  150 REDLEWFLDELRA-----AQELEVDG-EIEIYVTR-------------------------------------------VV 180

                        250       260       270
                 ....*....|....*....|....*....|..
gi 291384112 546 CCGPNSLSKILHKLSNQSNsyGTRFEYNKESF 577
Cdd:cd06186  181 VCGPPGLVDDVRNAVAKKG--GTGVEFHEESF 210
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
423-560 7.47e-25

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 100.49  E-value: 7.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112  423 YEVSLCVAGGIGVTPFASILNTLLDDWKPYKLRRLYFIWVCRDIQSFCWFADLLCMLynkfwQENRPDYVNIQLYLSQTD 502
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKSKKLKTKKIKFYWVVRDLSSLEWFKDVLNEL-----EELKELNIEIHIYLTGEY 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291384112  503 ----------------GIQKIIGEKYHALNSRLFIGRPQWKLLFDEIAKYNRGKTVGVFCCGPNSLSKILHKLS 560
Cdd:pfam08030  76 eaedasdqsdssirseNFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 69-500 6.92e-18

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 87.60  E-value: 6.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112  69 SLILLPMCRTL-LAYLRGSQKVPSRRtrrvldksrtFHITCGVTICIFSGVHVAAHLvnalnfsvnynedFIELNAARYR 147
Cdd:PLN02844 168 ALLLLPVLRGLaLFRLLGIQFEASVR----------YHVWLGTSMIFFATVHGASTL-------------FIWGISHHIQ 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 148 DEdPRKLLFTTVPGLTGVCMVMVLFLMVTASTYAIRVSNYDIFWYTHNLFFVFYMLLMLHVSggllkyqtnlDTHppgci 227
Cdd:PLN02844 225 DE-IWKWQKTGRIYLAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHHLYIVFLIFFLFHAG----------DRH----- 288

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 228 slnqthhqdislplhhsehlpgsflgefskpeelaqntfmkicveeprfratfpqtWLWISGPLCLYCAERLYRCIRSNK 307
Cdd:PLN02844 289 --------------------------------------------------------FYMVFPGIFLFGLDKLLRIVQSRP 312

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 308 PVTILSVISHPSDVMEIRMVKE-NFKARPGQYVILHCPSVSALENHPFTLTMCPTEKKATFGVHLKIVGDWTERFRDLLL 386
Cdd:PLN02844 313 ETCILSARLFPCKAIELVLPKDpGLKYAPTSVIFMKIPSISRFQWHPFSITSSSNIDDHTMSVIIKCEGGWTNSLYNKIQ 392

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 387 PPSSQDSEILPFIQTRnypklyIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKP-YKL-RRLYFIWVCR 464
Cdd:PLN02844 393 AELDSETNQMNCIPVA------IEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILKEIASQSSSrYRFpKRVQLIYVVK 466

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 291384112 465 DIQSFCWFADLLCMLYNKFWQENRpdyVNIQLYLSQ 500
Cdd:PLN02844 467 KSQDICLLNPISSLLLNQSSNQLN---LKLKVFVTQ 499
FAD_binding_8 pfam08022
FAD-binding domain;
307-416 3.77e-16

FAD-binding domain;


Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 74.29  E-value: 3.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112  307 KPVTILSVISHPSDVMEIRMVKEN--FKARPGQYVILHC-PSVSALENHPFTLTMCPTEKKATfgVHLKIVGDWTERFRD 383
Cdd:pfam08022   2 FGVPKAKVALLPDNVLKLRVSKPKkpFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLS--LHIKVKGGWTRKLAN 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 291384112  384 LLLPpssqdSEILPFIQTRNYPKLYIDGPFGSP 416
Cdd:pfam08022  80 YLSS-----SCPKSPENGKDKPRVLIEGPYGPP 107
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 320-549 3.36e-15

Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in many organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


Pssm-ID: 99778 [Multi-domain]  Cd Length: 223  Bit Score: 74.79  E-value: 3.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 320 DVMEIRMVKEN-FKARPGQYVILHCPSVSALENHPFTLTMCPTEKKA-TFGVHLKIVGDWTERFRDLLLppssqDSEILp 397
Cdd:cd00322    9 DVRLFRLQLPNgFSFKPGQYVDLHLPGDGRGLRRAYSIASSPDEEGElELTVKIVPGGPFSAWLHDLKP-----GDEVE- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 398 fiqtrnypklyIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKPyklRRLYFIWVCRDIQsfcwfadllC 477
Cdd:cd00322   83 -----------VSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPG---GEITLLYGARTPA---------D 139

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291384112 478 MLYNKFWQENRPDYVNIQLYLSQTDGiqkiigekyhalnSRLFIGRPQWKLLFDEIAKY-NRGKTVGVFCCGP 549
Cdd:cd00322  140 LLFLDELEELAKEGPNFRLVLALSRE-------------SEAKLGPGGRIDREAEILALlPDDSGALVYICGP 199
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 310-475 4.24e-15

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 75.28  E-value: 4.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 310 TILSVISHPSDV--MEIRMVKENFKARPGQYVILHCPSvsALENHPFTLTMCPTEKKaTFGVHLKIVGDWTERFRDLllp 387
Cdd:COG0543    1 KVVSVERLAPDVylLRLEAPLIALKFKPGQFVMLRVPG--DGLRRPFSIASAPREDG-TIELHIRVVGKGTRALAEL--- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 388 pssQDSEilpfiqtrnypKLYIDGPFGSPFEeslnYEVS----LCVAGGIGVTPFASILNTLLDdwkpyKLRRLYFIWVC 463
Cdd:COG0543   75 ---KPGD-----------ELDVRGPLGNGFP----LEDSgrpvLLVAGGTGLAPLRSLAEALLA-----RGRRVTLYLGA 131

                        170
                 ....*....|..
gi 291384112 464 RDIQSFCWFADL 475
Cdd:COG0543  132 RTPEDLYLLDEL 143
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
274-465 1.74e-13

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 72.62  E-value: 1.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 274 PRFRATFPQTWLWIS---GPLCLYCAERLYRCIRSNK-PVTILSVISHPSDVMEIRMVKEN---FKARPGQYVIL--HCP 344
Cdd:COG4097  178 GPFYWSPPAGVLWAAlaaAGLAAAVYSRLGRPLRSRRhPYRVESVEPEAGDVVELTLRPEGgrwLGHRAGQFAFLrfDGS 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 345 SVSaLENHPFTLTMCPTEK-KATFGVhlKIVGDWTERFRDLllPPSSqdseilpfiqtrnypKLYIDGPFGS-PFEESLN 422
Cdd:COG4097  258 PFW-EEAHPFSISSAPGGDgRLRFTI--KALGDFTRRLGRL--KPGT---------------RVYVEGPYGRfTFDRRDT 317

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 291384112 423 YEVSLCVAGGIGVTPFASILNTLldDWKPYKLRRLYFIWVCRD 465
Cdd:COG4097  318 APRQVWIAGGIGITPFLALLRAL--AARPGDQRPVDLFYCVRD 358
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 69-205 2.04e-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: 66.91  E-value: 2.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112   69 SLILLPMcrTLLAYLRGSqkVPSRRTRRVLDKSRTFHITCGVTICIFSGVHVAAHLVNALNFSVNYNEDFIELNAARyrd 148
Cdd:pfam01794   5 ALALLPL--LLLLALRNN--PLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSLEGILDLLLKRPYN--- 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 291384112  149 edprkllfttvpgLTGVCMVMVLFLMVTASTYAIRVSNYDIFWYTHNLFFVFYMLLM 205
Cdd:pfam01794  78 -------------ILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 317-578 8.86e-10

NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) domain, which varies in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99795 [Multi-domain]  Cd Length: 216  Bit Score: 58.81  E-value: 8.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 317 HPSDVMEIRMVKENFKARPGQYVILHCPSVSALENHPFTLTMCPTEKK-ATFGVhlKIVGDWTERFRDLLLPPSsqdsei 395
Cdd:cd06198    7 RPTTTLTLEPRGPALGHRAGQFAFLRFDASGWEEPHPFTISSAPDPDGrLRFTI--KALGDYTRRLAERLKPGT------ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 396 lpfiqtrnypKLYIDGPFGSpFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKPyklRRLYFIWVCRDIQSFcWFADL 475
Cdd:cd06198   79 ----------RVTVEGPYGR-FTFDDRRARQIWIAGGIGITPFLALLEALAARGDA---RPVTLFYCVRDPEDA-VFLDE 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 476 LCmlynkfwqenrpdyvniqlylsqtdGIQKIIGEKYHALNSRLfIGRPQWKLLFDEIAKynRGKTVGVFCCGPNSLSKI 555
Cdd:cd06198  144 LR-------------------------ALAAAAGVVLHVIDSPS-DGRLTLEQLVRALVP--DLADADVWFCGPPGMADA 195

                        250       260
                 ....*....|....*....|...
gi 291384112 556 LHKLSNQSNSYGTRFEYnkESFS 578
Cdd:cd06198  196 LEKGLRALGVPARRFHY--ERFE 216
PLN02631 PLN02631
ferric-chelate reductase
 293-446 9.49e-10

ferric-chelate reductase


Pssm-ID: 178238 [Multi-domain]  Cd Length: 699  Bit Score: 61.60  E-value: 9.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 293 LYCAERLYRCIRSNKPVTILSVISHPSDVMEIRMVK-ENFKARPGQYVILHCPSVSALENHPFTLTMCPTEKKATFGVHL 371
Cdd:PLN02631 294 LFFIDRYLRFLQSTKRSRLVSARILPSDNLELTFSKtPGLHYTPTSILFLHVPSISKLQWHPFTITSSSNLEKDTLSVVI 373

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291384112 372 KIVGDWTERFRDLLlpPSSQDSeilpfiqtrnyPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLL 446
Cdd:PLN02631 374 RRQGSWTQKLYTHL--SSSIDS-----------LEVSTEGPYGPNSFDVSRHNSLILVSGGSGITPFISVIRELI 435
PLN02292 PLN02292
ferric-chelate reductase
 173-446 1.03e-09

ferric-chelate reductase


Pssm-ID: 215165 [Multi-domain]  Cd Length: 702  Bit Score: 61.42  E-value: 1.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 173 LMVTASTY-AIRVSNYDIFWYTHNLFFVFYMLLMLHVSggllkyqtnldthppgcISlnqthHQDISLPLHHsehlpgsf 251
Cdd:PLN02292 261 LVMWATTYpKIRRRFFEVFFYTHYLYIVFMLFFVFHVG-----------------IS-----FALISFPGFY-------- 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 252 lgefskpeelaqntfmkicveeprfratfpqtwlwisgplcLYCAERLYRCIRSNKPVTILSVISHPSDVMEIRMVKEN- 330
Cdd:PLN02292 311 -----------------------------------------IFLVDRFLRFLQSRNNVKLVSARVLPCDTVELNFSKNPm 349

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 331 FKARPGQYVILHCPSVSALENHPFTLTMCPTEKKATFGVHLKIVGDWTERFRDLLlppSSQDSeilpfiqtRNYPKLYID 410
Cdd:PLN02292 350 LMYSPTSIMFVNIPSISKLQWHPFTITSSSKLEPEKLSVMIKSQGKWSTKLYHML---SSSDQ--------IDRLAVSVE 418

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 291384112 411 GPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLL 446
Cdd:PLN02292 419 GPYGPASTDFLRHESLVMVSGGSGITPFISIIRDLI 454
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
308-549 5.71e-08

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 53.64  E-value: 5.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 308 PVTILSVISHPSDVMEIRMV----KENFKARPGQYVILHCPSVSALENHPFTLTMCPTEKKATFGV-------------- 369
Cdd:COG1018    5 PLRVVEVRRETPDVVSFTLEppdgAPLPRFRPGQFVTLRLPIDGKPLRRAYSLSSAPGDGRLEITVkrvpggggsnwlhd 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 370 HLKiVGDwterfrdlllppssqdseilpfiqtrnypKLYIDGPFGS---PFEESLNYevsLCVAGGIGVTPFASILNTLL 446
Cdd:COG1018   85 HLK-VGD-----------------------------TLEVSGPRGDfvlDPEPARPL---LLIAGGIGITPFLSMLRTLL 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 447 dDWKPYklRRLYFIWVCRDIQSFCwFADLLcmlynkfwQENRPDYVNIQLYLSQTDGiqkiigekyhalnSRLFIGRPQW 526
Cdd:COG1018  132 -ARGPF--RPVTLVYGARSPADLA-FRDEL--------EALAARHPRLRLHPVLSRE-------------PAGLQGRLDA 186

                        250       260
                 ....*....|....*....|...
gi 291384112 527 KLLFDEIAKYNRGKtvgVFCCGP 549
Cdd:COG1018  187 ELLAALLPDPADAH---VYLCGP 206
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 309-441 1.23e-06

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 49.87  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 309 VTILSVISHPSDVMEIRM-VKENFKARPGQYVILHCPSVSALENHPFTLtmC-PTEKKATFGVhlKIVGDWTERFRDLll 386
Cdd:PRK00054   7 MKIVENKEIAPNIYTLVLdGEKVFDMKPGQFVMVWVPGVEPLLERPISI--SdIDKNEITILY--RKVGEGTKKLSKL-- 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 291384112 387 ppSSQDSeilpfiqtrnypkLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASI 441
Cdd:PRK00054  81 --KEGDE-------------LDIRGPLGNGFDLEEIGGKVLLVGGGIGVAPLYEL 120
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 406-559 2.11e-06

Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as an electron donor. Like ferredoxin reductases, these proteins have an N-terminal FAD binding subdomain and a C-terminal NADH binding subdomain, separated by a cleft, which accepts FAD. The NADH-binding moiety interacts with part of the FAD and resembles a Rossmann fold. However, NAD is bound differently than in canonical Rossmann fold proteins. Nitrate reductases, flavoproteins similar to pyridine nucleotide cytochrome reductases, catalyze the reduction of nitrate to nitrite. The enzyme can be divided into three functional fragments that bind the cofactors molybdopterin, heme-iron, and FAD/NADH.


Pssm-ID: 99780 [Multi-domain]  Cd Length: 234  Bit Score: 49.10  E-value: 2.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 406 KLYIDGPFGS-PFEESLNYEVSLCVAGGIGVTPFASILNTLLDDwkPYKLRRLYFIWVCRDIQSfCWFADLLcmlynKFW 484
Cdd:cd06183   86 TVEIRGPFGKfEYKPNGKVKHIGMIAGGTGITPMLQLIRAILKD--PEDKTKISLLYANRTEED-ILLREEL-----DEL 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 485 QENRPDYVNIQLYLSQTDGIQKIigekyhalnsrlFIGRPQWKLLFDEIAKYNRGKTVgVFCCGPN-----SLSKILHKL 559
Cdd:cd06183  158 AKKHPDRFKVHYVLSRPPEGWKG------------GVGFITKEMIKEHLPPPPSEDTL-VLVCGPPpmiegAVKGLLKEL 224
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 321-451 2.23e-06

FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster.


Pssm-ID: 99816 [Multi-domain]  Cd Length: 233  Bit Score: 49.17  E-value: 2.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 321 VMEIRMVK-----ENFKARPGQYVILHCPSVSALenhPFTLTMCPTEKkatfGVHLKIVGDWTERFRDLllppssqdsei 395
Cdd:cd06220    7 IDETPTVKtfvfdWDFDFKPGQFVMVWVPGVDEI---PMSLSYIDGPN----SITVKKVGEATSALHDL----------- 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 291384112 396 lpfiqtRNYPKLYIDGPFGSPFEesLNYEVSLCVAGGIGVTPfasiLNTLLDDWKP 451
Cdd:cd06220   69 ------KEGDKLGIRGPYGNGFE--LVGGKVLLIGGGIGIAP----LAPLAERLKK 112
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 321-442 9.66e-06

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: 47.32  E-value: 9.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 321 VMEIRMVKENFKARPGQYVILHCPSVSALENHPFTLtMCPTEKKATFGVHLKIVGDWTERFrdLLLPPSSqdseilpfiq 400
Cdd:cd06192   13 LLTIKAPLAARLFRPGQFVFLRNFESPGLERIPLSL-AGVDPEEGTISLLVEIRGPKTKLI--AELKPGE---------- 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 291384112 401 trnypKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASIL 442
Cdd:cd06192   80 -----KLDVMGPLGNGFEGPKKGGTVLLVAGGIGLAPLLPIA 116
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 311-549 1.39e-05

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


Pssm-ID: 99817 [Multi-domain]  Cd Length: 253  Bit Score: 46.83  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 311 ILSVISHPSDV----MEIRMVK-ENFKARPGQYVILHCPSVSALenhPFTLTMCPTEKKaTFGVHLKIVGDWTERFRDLl 385
Cdd:cd06221    1 IVEVVDETEDIktftLRLEDDDeELFTFKPGQFVMLSLPGVGEA---PISISSDPTRRG-PLELTIRRVGRVTEALHEL- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 386 lPPSSqdseilpfiqtrnypKLYIDGPFGSPF--EESLNYEVsLCVAGGIGVTPFASILNTLLDDWKPYKlrRLYFIWVC 463
Cdd:cd06221   76 -KPGD---------------TVGLRGPFGNGFpvEEMKGKDL-LLVAGGLGLAPLRSLINYILDNREDYG--KVTLLYGA 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 464 RDIQSFCWFADLlcmlynKFWQenrpDYVNIQLYLSQTDGiqkIIGEKYHalnsrlfIGRPQwkLLFDEIAkYNRGKTVg 543
Cdd:cd06221  137 RTPEDLLFKEEL------KEWA----KRSDVEVILTVDRA---EEGWTGN-------VGLVT--DLLPELT-LDPDNTV- 192


                 ....*.
gi 291384112 544 VFCCGP 549
Cdd:cd06221  193 AIVCGP 198
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 319-479 7.59e-05

Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates toluene and forms p-cresol as part of a three component toluene-4-monoxygenase system. Electron transfer is from NADH to an NADH:ferredoxin oxidoreductase (TmoF in P. mendocina) to ferredoxin to an iron-containing oxygenase. TmoF is homologous to other mono- and dioxygenase systems within the ferredoxin reductase family.


Pssm-ID: 99787  Cd Length: 232  Bit Score: 44.55  E-value: 7.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 319 SDVMEIRMVKE---NFkaRPGQYVILHCP--------SVSALENHPFTLTmcptekkatFGVHLKIVGdwteRFRDLLlp 387
Cdd:cd06190    9 HDVAEFRFALDgpaDF--LPGQYALLALPgvegaraySMANLANASGEWE---------FIIKRKPGG----AASNAL-- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 388 pssqdseilpFIQTRNYPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKPYKlRRLYFIWVCRDIQ 467
Cdd:cd06190   72 ----------FDNLEPGDELELDGPYGLAYLRPDEDRDIVCIAGGSGLAPMLSILRGAARSPYLSD-RPVDLFYGGRTPS 140

                        170
                 ....*....|..
gi 291384112 468 SFCwFADLLCML 479
Cdd:cd06190  141 DLC-ALDELSAL 151
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 429-476 1.26e-03

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: 40.62  E-value: 1.26e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 291384112 429 VAGGIGVTPFASILNTLLDDWKPyklRRLYFIWVCRDIQSFCwFADLL 476
Cdd:cd06184  119 ISAGVGITPMLSMLEALAAEGPG---RPVTFIHAARNSAVHA-FRDEL 162
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
 327-458 4.79e-03

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 39.40  E-value: 4.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112 327 VKENFKARPGQYVILHCPSVSAlenhpFTLTMCPTE-KKATFGVHLKIVGDWTERFRDLllppssQDSEILpfiqtrnyp 405
Cdd:PRK08345  32 LAESFTFKPGQFVQVTIPGVGE-----VPISICSSPtRKGFFELCIRRAGRVTTVIHRL------KEGDIV--------- 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 291384112 406 klYIDGPFGS--PFEESLNYEVsLCVAGGIGVTPFASILNTLLDD-WKPYKLRRLY 458
Cdd:PRK08345  92 --GVRGPYGNgfPVDEMEGMDL-LLIAGGLGMAPLRSVLLYAMDNrWKYGNITLIY 144
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 429-549 5.82e-03

Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have essentially no similarity.


Pssm-ID: 425503 [Multi-domain]  Cd Length: 109  Bit Score: 36.85  E-value: 5.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291384112  429 VAGGIGVTPFASILNTLLDDWKPykLRRLYFIWVCRDiqsfcwFADLLCMLYNKFWQENRPDYVNIQLYLSQTDGiqkii 508
Cdd:pfam00175   2 IAGGTGIAPVRSMLRAILEDPKD--PTQVVLVFGNRN------EDDILYREELDELAEKHPGRLTVVYVVSRPEA----- 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 291384112  509 gekyhalNSRLFIGRPQwKLLFDEIAKYNRGKTVgVFCCGP 549
Cdd:pfam00175  69 -------GWTGGKGRVQ-DALLEDHLSLPDEETH-VYVCGP 100
 
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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