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Conserved domains on  [gi|966987745|ref|XP_014970878|]
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NADPH oxidase 4 isoform X6 [Macaca mulatta]

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 ...
 237-503 8.06e-50

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


:

Pssm-ID: 99783 [Multi-domain]  Cd Length: 210  Bit Score: 169.79  E-value: 8.06e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 237 IISVISHP-SDVMEIRMVKE-NFKARPGQYIILHCPSV-SALENHPFTLTMCPTETKATFGVHLKIV-GDWTERFRDLLL 312
Cdd:cd06186    1 IATVELLPdSDVIRLTIPKPkPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEQDTLSLIIRAKkGFTTRLLRKALK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 313 PPSSQDSeilpfiqsrnyPKLYIDGPFGSPFEESLNYEISLCVAGGIGVTPFASILNTLLDDW-KPYKLRRLYFIWVCRD 391
Cdd:cd06186   81 SPGGGVS-----------LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSsKTSRTRRVKLVWVVRD 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 392 IQSFRWFADLLCMlhnkfWQENRPDYvNIQLYLSQtdgiqkiigekyhalnsrlfigrprwkllfdeiakynrgktvgVF 471
Cdd:cd06186  150 REDLEWFLDELRA-----AQELEVDG-EIEIYVTR-------------------------------------------VV 180

                        250       260       270
                 ....*....|....*....|....*....|..
gi 966987745 472 CCGPNSLSKTLHKLSNQNNsyGTRFEYNKESF 503
Cdd:cd06186  181 VCGPPGLVDDVRNAVAKKG--GTGVEFHEESF 210
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 5-131 2.68e-15

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: 72.30  E-value: 2.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745    5 LLAFLRGSQKVPSRRTRRLLDKSRTFHITCGVTICIFSGVHVAAHLVNALNFSVnysEDFVELNAARYRNedprkllftt 84
Cdd:pfam01794  11 LLLLLALRNNPLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSL---EGILDLLLKRPYN---------- 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 966987745   85 vpgLTGVCMVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLM 131
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 ...
 237-503 8.06e-50

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


Pssm-ID: 99783 [Multi-domain]  Cd Length: 210  Bit Score: 169.79  E-value: 8.06e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 237 IISVISHP-SDVMEIRMVKE-NFKARPGQYIILHCPSV-SALENHPFTLTMCPTETKATFGVHLKIV-GDWTERFRDLLL 312
Cdd:cd06186    1 IATVELLPdSDVIRLTIPKPkPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEQDTLSLIIRAKkGFTTRLLRKALK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 313 PPSSQDSeilpfiqsrnyPKLYIDGPFGSPFEESLNYEISLCVAGGIGVTPFASILNTLLDDW-KPYKLRRLYFIWVCRD 391
Cdd:cd06186   81 SPGGGVS-----------LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSsKTSRTRRVKLVWVVRD 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 392 IQSFRWFADLLCMlhnkfWQENRPDYvNIQLYLSQtdgiqkiigekyhalnsrlfigrprwkllfdeiakynrgktvgVF 471
Cdd:cd06186  150 REDLEWFLDELRA-----AQELEVDG-EIEIYVTR-------------------------------------------VV 180

                        250       260       270
                 ....*....|....*....|....*....|..
gi 966987745 472 CCGPNSLSKTLHKLSNQNNsyGTRFEYNKESF 503
Cdd:cd06186  181 VCGPPGLVDDVRNAVAKKG--GTGVEFHEESF 210
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
349-486 2.07e-26

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 104.34  E-value: 2.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745  349 YEISLCVAGGIGVTPFASILNTLLDDWKPYKLRRLYFIWVCRDIQSFRWFADLLCML----------HNKFWQENRPDYV 418
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKSKKLKTKKIKFYWVVRDLSSLEWFKDVLNELeelkelnieiHIYLTGEYEAEDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966987745  419 NIQLYLSQTD-GIQKIIGEKYHALNSRLFIGRPRWKLLFDEIAKYNRGKTVGVFCCGPNSLSKTLHKLS 486
Cdd:pfam08030  81 SDQSDSSIRSeNFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 88-405 1.77e-16

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 82.59  E-value: 1.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745  88 LTGVCMVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLMLHVSGgllkyqtnldthppgcislnrtssqnislpe 167
Cdd:PLN02844 238 LAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHHLYIVFLIFFLFHAGD------------------------------- 286

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 168 yfpEHFHEPFPEEFskpeeftqntfvkicmeeprfqanfpqtwlwisgplcLYCAERLYRYIRSNKPVTIISVISHPSDV 247
Cdd:PLN02844 287 ---RHFYMVFPGIF-------------------------------------LFGLDKLLRIVQSRPETCILSARLFPCKA 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 248 MEIRMVKE-NFKARPGQYIILHCPSVSALENHPFTLTMCPTETKATFGVHLKIVGDWTERFRDLLLPPSSQDSEILPFIQ 326
Cdd:PLN02844 327 IELVLPKDpGLKYAPTSVIFMKIPSISRFQWHPFSITSSSNIDDHTMSVIIKCEGGWTNSLYNKIQAELDSETNQMNCIP 406

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 327 SRnypklyIDGPFGSPFEESLNYEISLCVAGGIGVTPFASILNTLLDDWKP-YKL-RRLYFIWVCRDIQSfrwfadlLCM 404
Cdd:PLN02844 407 VA------IEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILKEIASQSSSrYRFpKRVQLIYVVKKSQD-------ICL 473


                 .
gi 966987745 405 L 405
Cdd:PLN02844 474 L 474
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 5-131 2.68e-15

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: 72.30  E-value: 2.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745    5 LLAFLRGSQKVPSRRTRRLLDKSRTFHITCGVTICIFSGVHVAAHLVNALNFSVnysEDFVELNAARYRNedprkllftt 84
Cdd:pfam01794  11 LLLLLALRNNPLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSL---EGILDLLLKRPYN---------- 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 966987745   85 vpgLTGVCMVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLM 131
Cdd:pfam01794  78 ---ILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 236-391 6.15e-15

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 74.51  E-value: 6.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 236 TIISVISHPSDV--MEIRMVKENFKARPGQYIILHCPSvsALENHPFTLTMCPTEtKATFGVHLKIVGDWTERFRDLllp 313
Cdd:COG0543    1 KVVSVERLAPDVylLRLEAPLIALKFKPGQFVMLRVPG--DGLRRPFSIASAPRE-DGTIELHIRVVGKGTRALAEL--- 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966987745 314 pssQDSEilpfiqsrnypKLYIDGPFGSPFEESLNYEISLCVAGGIGVTPFASILNTLLDdwkpyKLRRLYFIWVCRD 391
Cdd:COG0543   75 ---KPGD-----------ELDVRGPLGNGFPLEDSGRPVLLVAGGTGLAPLRSLAEALLA-----RGRRVTLYLGART 133
 
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 ...
 237-503 8.06e-50

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


Pssm-ID: 99783 [Multi-domain]  Cd Length: 210  Bit Score: 169.79  E-value: 8.06e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 237 IISVISHP-SDVMEIRMVKE-NFKARPGQYIILHCPSV-SALENHPFTLTMCPTETKATFGVHLKIV-GDWTERFRDLLL 312
Cdd:cd06186    1 IATVELLPdSDVIRLTIPKPkPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEQDTLSLIIRAKkGFTTRLLRKALK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 313 PPSSQDSeilpfiqsrnyPKLYIDGPFGSPFEESLNYEISLCVAGGIGVTPFASILNTLLDDW-KPYKLRRLYFIWVCRD 391
Cdd:cd06186   81 SPGGGVS-----------LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSsKTSRTRRVKLVWVVRD 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 392 IQSFRWFADLLCMlhnkfWQENRPDYvNIQLYLSQtdgiqkiigekyhalnsrlfigrprwkllfdeiakynrgktvgVF 471
Cdd:cd06186  150 REDLEWFLDELRA-----AQELEVDG-EIEIYVTR-------------------------------------------VV 180

                        250       260       270
                 ....*....|....*....|....*....|..
gi 966987745 472 CCGPNSLSKTLHKLSNQNNsyGTRFEYNKESF 503
Cdd:cd06186  181 VCGPPGLVDDVRNAVAKKG--GTGVEFHEESF 210
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
349-486 2.07e-26

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 104.34  E-value: 2.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745  349 YEISLCVAGGIGVTPFASILNTLLDDWKPYKLRRLYFIWVCRDIQSFRWFADLLCML----------HNKFWQENRPDYV 418
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKSKKLKTKKIKFYWVVRDLSSLEWFKDVLNELeelkelnieiHIYLTGEYEAEDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966987745  419 NIQLYLSQTD-GIQKIIGEKYHALNSRLFIGRPRWKLLFDEIAKYNRGKTVGVFCCGPNSLSKTLHKLS 486
Cdd:pfam08030  81 SDQSDSSIRSeNFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 88-405 1.77e-16

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 82.59  E-value: 1.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745  88 LTGVCMVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLMLHVSGgllkyqtnldthppgcislnrtssqnislpe 167
Cdd:PLN02844 238 LAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHHLYIVFLIFFLFHAGD------------------------------- 286

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 168 yfpEHFHEPFPEEFskpeeftqntfvkicmeeprfqanfpqtwlwisgplcLYCAERLYRYIRSNKPVTIISVISHPSDV 247
Cdd:PLN02844 287 ---RHFYMVFPGIF-------------------------------------LFGLDKLLRIVQSRPETCILSARLFPCKA 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 248 MEIRMVKE-NFKARPGQYIILHCPSVSALENHPFTLTMCPTETKATFGVHLKIVGDWTERFRDLLLPPSSQDSEILPFIQ 326
Cdd:PLN02844 327 IELVLPKDpGLKYAPTSVIFMKIPSISRFQWHPFSITSSSNIDDHTMSVIIKCEGGWTNSLYNKIQAELDSETNQMNCIP 406

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 327 SRnypklyIDGPFGSPFEESLNYEISLCVAGGIGVTPFASILNTLLDDWKP-YKL-RRLYFIWVCRDIQSfrwfadlLCM 404
Cdd:PLN02844 407 VA------IEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILKEIASQSSSrYRFpKRVQLIYVVKKSQD-------ICL 473


                 .
gi 966987745 405 L 405
Cdd:PLN02844 474 L 474
FAD_binding_8 pfam08022
FAD-binding domain;
233-342 8.43e-16

FAD-binding domain;


Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 73.14  E-value: 8.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745  233 KPVTIISVISHPSDVMEIRMVKEN--FKARPGQYIILHC-PSVSALENHPFTLTMCPTETKATfgVHLKIVGDWTERFRD 309
Cdd:pfam08022   2 FGVPKAKVALLPDNVLKLRVSKPKkpFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLS--LHIKVKGGWTRKLAN 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 966987745  310 LLLPpssqdSEILPFIQSRNYPKLYIDGPFGSP 342
Cdd:pfam08022  80 YLSS-----SCPKSPENGKDKPRVLIEGPYGPP 107
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 5-131 2.68e-15

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: 72.30  E-value: 2.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745    5 LLAFLRGSQKVPSRRTRRLLDKSRTFHITCGVTICIFSGVHVAAHLVNALNFSVnysEDFVELNAARYRNedprkllftt 84
Cdd:pfam01794  11 LLLLLALRNNPLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSL---EGILDLLLKRPYN---------- 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 966987745   85 vpgLTGVCMVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLM 131
Cdd:pfam01794  78 ---ILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 246-475 3.90e-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: 74.41  E-value: 3.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 246 DVMEIRMVKEN-FKARPGQYIILHCPSVSALENHPFTLTMCPTETKA-TFGVHLKIVGDWTERFRDLLLppssqDSEILp 323
Cdd:cd00322    9 DVRLFRLQLPNgFSFKPGQYVDLHLPGDGRGLRRAYSIASSPDEEGElELTVKIVPGGPFSAWLHDLKP-----GDEVE- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 324 fiqsrnypklyIDGPFGSPFEESLNYEISLCVAGGIGVTPFASILNTLLDDWKPyklRRLYFIWVCRDIQSFrWFADLLC 403
Cdd:cd00322   83 -----------VSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPG---GEITLLYGARTPADL-LFLDELE 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966987745 404 MLHNKFwqenrpdyVNIQLYLSQTDGiqkiigekyhalnSRLFIGRPRWKLLFDEIAKY-NRGKTVGVFCCGP 475
Cdd:cd00322  148 ELAKEG--------PNFRLVLALSRE-------------SEAKLGPGGRIDREAEILALlPDDSGALVYICGP 199
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 236-391 6.15e-15

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 74.51  E-value: 6.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 236 TIISVISHPSDV--MEIRMVKENFKARPGQYIILHCPSvsALENHPFTLTMCPTEtKATFGVHLKIVGDWTERFRDLllp 313
Cdd:COG0543    1 KVVSVERLAPDVylLRLEAPLIALKFKPGQFVMLRVPG--DGLRRPFSIASAPRE-DGTIELHIRVVGKGTRALAEL--- 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966987745 314 pssQDSEilpfiqsrnypKLYIDGPFGSPFEESLNYEISLCVAGGIGVTPFASILNTLLDdwkpyKLRRLYFIWVCRD 391
Cdd:COG0543   75 ---KPGD-----------ELDVRGPLGNGFPLEDSGRPVLLVAGGTGLAPLRSLAEALLA-----RGRRVTLYLGART 133
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
200-391 4.94e-14

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 74.16  E-value: 4.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 200 PRFQANFPQTWLWIS-GPLCLYCAerLYRYIRSN-----KPVTIISVISHPSDVMEIRMVKEN---FKARPGQYIIL--H 268
Cdd:COG4097  178 GPFYWSPPAGVLWAAlAAAGLAAA--VYSRLGRPlrsrrHPYRVESVEPEAGDVVELTLRPEGgrwLGHRAGQFAFLrfD 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 269 CPSVSaLENHPFTLTMCPTET-KATFGVhlKIVGDWTERFRDLllPPSSqdseilpfiqsrnypKLYIDGPFGS-PFEES 346
Cdd:COG4097  256 GSPFW-EEAHPFSISSAPGGDgRLRFTI--KALGDFTRRLGRL--KPGT---------------RVYVEGPYGRfTFDRR 315

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 966987745 347 LNYEISLCVAGGIGVTPFASILNTLldDWKPYKLRRLYFIWVCRD 391
Cdd:COG4097  316 DTAPRQVWIAGGIGITPFLALLRAL--AARPGDQRPVDLFYCVRD 358
PLN02292 PLN02292
ferric-chelate reductase
 99-372 6.49e-11

ferric-chelate reductase


Pssm-ID: 215165 [Multi-domain]  Cd Length: 702  Bit Score: 64.89  E-value: 6.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745  99 LMITASTY-AIRVSNYDIFWYTHNLFFVFYMLLMLHVSggllkyqtnldthppgcislnrTSSQNISLPEYFpehfhepf 177
Cdd:PLN02292 261 LVMWATTYpKIRRRFFEVFFYTHYLYIVFMLFFVFHVG----------------------ISFALISFPGFY-------- 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 178 peefskpeeftqntfvkicmeeprfqanfpqtwlwisgplcLYCAERLYRYIRSNKPVTIISVISHPSDVMEIRMVKEN- 256
Cdd:PLN02292 311 -----------------------------------------IFLVDRFLRFLQSRNNVKLVSARVLPCDTVELNFSKNPm 349

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 257 FKARPGQYIILHCPSVSALENHPFTLTMCPTETKATFGVHLKIVGDWTERFRDLLlppSSQDSeilpfiqsRNYPKLYID 336
Cdd:PLN02292 350 LMYSPTSIMFVNIPSISKLQWHPFTITSSSKLEPEKLSVMIKSQGKWSTKLYHML---SSSDQ--------IDRLAVSVE 418

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 966987745 337 GPFGSPFEESLNYEISLCVAGGIGVTPFASILNTLL 372
Cdd:PLN02292 419 GPYGPASTDFLRHESLVMVSGGSGITPFISIIRDLI 454
PLN02631 PLN02631
ferric-chelate reductase
 219-401 9.41e-11

ferric-chelate reductase


Pssm-ID: 178238 [Multi-domain]  Cd Length: 699  Bit Score: 64.29  E-value: 9.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 219 LYCAERLYRYIRSNKPVTIISVISHPSDVMEIRMVK-ENFKARPGQYIILHCPSVSALENHPFTLTMCPTETKATFGVHL 297
Cdd:PLN02631 294 LFFIDRYLRFLQSTKRSRLVSARILPSDNLELTFSKtPGLHYTPTSILFLHVPSISKLQWHPFTITSSSNLEKDTLSVVI 373

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 298 KIVGDWTERFRDLLlpPSSQDSeilpfiqsrnyPKLYIDGPFGSPFEESLNYEISLCVAGGIGVTPFASILNTLLDDWKP 377
Cdd:PLN02631 374 RRQGSWTQKLYTHL--SSSIDS-----------LEVSTEGPYGPNSFDVSRHNSLILVSGGSGITPFISVIRELIFQSQN 440

                        170       180
                 ....*....|....*....|....
gi 966987745 378 YKLRRLYFIWVCrdiqSFRWFADL 401
Cdd:PLN02631 441 PSTKLPDVLLVC----SFKHYHDL 460
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 243-504 1.48e-10

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


Pssm-ID: 99795 [Multi-domain]  Cd Length: 216  Bit Score: 61.12  E-value: 1.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 243 HPSDVMEIRMVKENFKARPGQYIILHCPSVSALENHPFTLTMCPTETK-ATFGVhlKIVGDWTERFRDLLLPPSsqdsei 321
Cdd:cd06198    7 RPTTTLTLEPRGPALGHRAGQFAFLRFDASGWEEPHPFTISSAPDPDGrLRFTI--KALGDYTRRLAERLKPGT------ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 322 lpfiqsrnypKLYIDGPFGSpFEESLNYEISLCVAGGIGVTPFASILNTLLDDWKPyklRRLYFIWVCRDIQSFrWFADL 401
Cdd:cd06198   79 ----------RVTVEGPYGR-FTFDDRRARQIWIAGGIGITPFLALLEALAARGDA---RPVTLFYCVRDPEDA-VFLDE 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 402 LcmlhnkfWQENRPDYVNIQLYLSQTDGiqkiigekyhalnsRLFIGRPRWKLLFDeiakynrGKTVGVFCCGPNSLSKT 481
Cdd:cd06198  144 L-------RALAAAAGVVLHVIDSPSDG--------------RLTLEQLVRALVPD-------LADADVWFCGPPGMADA 195

                        250       260
                 ....*....|....*....|...
gi 966987745 482 LHKLSNQNNSYGTRFEYnkESFS 504
Cdd:cd06198  196 LEKGLRALGVPARRFHY--ERFE 216
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
234-475 1.82e-07

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 52.10  E-value: 1.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 234 PVTIISVISHPSDVMEIRMV----KENFKARPGQYIILHCPSVSALENHPFTLTMCPTETKATFGV-------------- 295
Cdd:COG1018    5 PLRVVEVRRETPDVVSFTLEppdgAPLPRFRPGQFVTLRLPIDGKPLRRAYSLSSAPGDGRLEITVkrvpggggsnwlhd 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 296 HLKiVGDwterfrdlllppssqdseilpfiqsrnypKLYIDGPFGS---PFEESLNYeisLCVAGGIGVTPFASILNTLL 372
Cdd:COG1018   85 HLK-VGD-----------------------------TLEVSGPRGDfvlDPEPARPL---LLIAGGIGITPFLSMLRTLL 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 373 dDWKPYklRRLYFIWVCRDIQSFrWFADLLCMLHNKfwqenrpdYVNIQLYLSQTDGiqkiigekyhalnSRLFIGRPRW 452
Cdd:COG1018  132 -ARGPF--RPVTLVYGARSPADL-AFRDELEALAAR--------HPRLRLHPVLSRE-------------PAGLQGRLDA 186

                        250       260
                 ....*....|....*....|...
gi 966987745 453 KLLFDEIAKYNRGKtvgVFCCGP 475
Cdd:COG1018  187 ELLAALLPDPADAH---VYLCGP 206
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 235-367 1.69e-06

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 49.49  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 235 VTIISVISHPSDVMEIRM-VKENFKARPGQYIILHCPSVSALENHPFTLTMCPTEtKATFGVhlKIVGDWTERFRDLllp 313
Cdd:PRK00054   7 MKIVENKEIAPNIYTLVLdGEKVFDMKPGQFVMVWVPGVEPLLERPISISDIDKN-EITILY--RKVGEGTKKLSKL--- 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 966987745 314 pSSQDSeilpfiqsrnypkLYIDGPFGSPFEESLNYEISLCVAGGIGVTPFASI 367
Cdd:PRK00054  81 -KEGDE-------------LDIRGPLGNGFDLEEIGGKVLLVGGGIGVAPLYEL 120
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 235-377 3.12e-06

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


Pssm-ID: 99816 [Multi-domain]  Cd Length: 233  Bit Score: 48.40  E-value: 3.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 235 VTIISVIshpsdvMEIRMVK-----ENFKARPGQYIILHCPSVSALenhPFTLTMCPTEtkatFGVHLKIVGDWTERFRD 309
Cdd:cd06220    1 VTIKEVI------DETPTVKtfvfdWDFDFKPGQFVMVWVPGVDEI---PMSLSYIDGP----NSITVKKVGEATSALHD 67

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966987745 310 LllppssqdseilpfiqsRNYPKLYIDGPFGSPFEesLNYEISLCVAGGIGVTPfasiLNTLLDDWKP 377
Cdd:cd06220   68 L-----------------KEGDKLGIRGPYGNGFE--LVGGKVLLIGGGIGIAP----LAPLAERLKK 112
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 247-368 7.82e-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: 7.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 247 VMEIRMVKENFKARPGQYIILHCPSVSALENHPFTLtMCPTETKATFGVHLKIVGDWTERFrdLLLPPSSqdseilpfiq 326
Cdd:cd06192   13 LLTIKAPLAARLFRPGQFVFLRNFESPGLERIPLSL-AGVDPEEGTISLLVEIRGPKTKLI--AELKPGE---------- 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 966987745 327 srnypKLYIDGPFGSPFEESLNYEISLCVAGGIGVTPFASIL 368
Cdd:cd06192   80 -----KLDVMGPLGNGFEGPKKGGTVLLVAGGIGLAPLLPIA 116
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 332-475 1.50e-05

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


Pssm-ID: 99780 [Multi-domain]  Cd Length: 234  Bit Score: 46.41  E-value: 1.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 332 KLYIDGPFGS-PFEESLNYEISLCVAGGIGVTPFASILNTLLDDwkPYKLRRLYFIWVCRDIQsfrwfaDLLCMLHNKFW 410
Cdd:cd06183   86 TVEIRGPFGKfEYKPNGKVKHIGMIAGGTGITPMLQLIRAILKD--PEDKTKISLLYANRTEE------DILLREELDEL 157

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966987745 411 QENRPDYVNIQLYLSQTDGIQKIigekyhalnsrlFIGRPRWKLLFDEIAKYNRGKTVgVFCCGP 475
Cdd:cd06183  158 AKKHPDRFKVHYVLSRPPEGWKG------------GVGFITKEMIKEHLPPPPSEDTL-VLVCGP 209
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 237-475 4.11e-04

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


Pssm-ID: 99817 [Multi-domain]  Cd Length: 253  Bit Score: 42.21  E-value: 4.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 237 IISVISHPSDV----MEIRMVK-ENFKARPGQYIILHCPSVSALenhPFTLTMCPTEtKATFGVHLKIVGDWTERFRDLl 311
Cdd:cd06221    1 IVEVVDETEDIktftLRLEDDDeELFTFKPGQFVMLSLPGVGEA---PISISSDPTR-RGPLELTIRRVGRVTEALHEL- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 312 lPPSSqdseilpfiqsrnypKLYIDGPFGSPF--EESLNYEIsLCVAGGIGVTPFASILNTLLDDWKPYKlrRLYFiwvc 389
Cdd:cd06221   76 -KPGD---------------TVGLRGPFGNGFpvEEMKGKDL-LLVAGGLGLAPLRSLINYILDNREDYG--KVTL---- 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 390 rdIQSFRWFADLLCMLHNKFWQenrpDYVNIQLYLSQTDGiqkIIGEKYHalnsrlfIGRPrwKLLFDEIAkYNRGKTVg 469
Cdd:cd06221  133 --LYGARTPEDLLFKEELKEWA----KRSDVEVILTVDRA---EEGWTGN-------VGLV--TDLLPELT-LDPDNTV- 192


                 ....*.
gi 966987745 470 VFCCGP 475
Cdd:cd06221  193 AIVCGP 198
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 355-401 4.79e-04

FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain containing a B-type heme fused with a ferredoxin reductase-like FAD/NAD-binding domain. Flavohemoglobins detoxify nitric oxide (NO) via an NO dioxygenase reaction. The hemoglobin domain adopts a globin fold with an embedded heme molecule. Flavohemoglobins also have a C-terminal reductase domain with bindiing sites for FAD and NAD(P)H. This domain catalyzes the conversion of NO + O2 + NAD(P)H to NO3- + NAD(P)+. Instead of the oxygen transport function of hemoglobins, flavohemoglobins seem to act in NO dioxygenation and NO signalling.


Pssm-ID: 99781  Cd Length: 247  Bit Score: 41.77  E-value: 4.79e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 966987745 355 VAGGIGVTPFASILNTLLDDWKPyklRRLYFIWVCRDIQS--FR-WFADL 401
Cdd:cd06184  119 ISAGVGITPMLSMLEALAAEGPG---RPVTFIHAARNSAVhaFRdELEEL 165
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 235-418 1.11e-03

NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron transfer from iron complexes or iron proteins. Structurally similar to ferredoxin reductases, but with only 15% sequence identity, flavin reductases reduce FAD, FMN, or riboflavin via NAD(P)H. Flavin is used as a substrate, rather than a tightly bound prosthetic group as in flavoenzymes; weaker binding is due to the absence of a binding site for the AMP moeity of FAD.


Pssm-ID: 99786 [Multi-domain]  Cd Length: 224  Bit Score: 40.61  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 235 VTIISVISHpsDVMEIR-MVKENFKARPGQYIILHCPSVSALenhPFTLTMCPTETkATFGVHLKIVGDWteRFRDlllp 313
Cdd:cd06189    3 VESIEPLND--DVYRVRlKPPAPLDFLAGQYLDLLLDDGDKR---PFSIASAPHED-GEIELHIRAVPGG--SFSD---- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 314 pssqdsEILPFIQSRNypKLYIDGPFGSPFEESLNYEISLCVAGGIGVTPFASILNTLLDDwkpyKLRR-LYFIWVCRDI 392
Cdd:cd06189   71 ------YVFEELKENG--LVRIEGPLGDFFLREDSDRPLILIAGGTGFAPIKSILEHLLAQ----GSKRpIHLYWGARTE 138

                        170       180
                 ....*....|....*....|....*...
gi 966987745 393 QSFrwFADLLCmlhnKFWQENRP--DYV 418
Cdd:cd06189  139 EDL--YLDELL----EAWAEAHPnfTYV 160
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 355-429 2.28e-03

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


Pssm-ID: 425503 [Multi-domain]  Cd Length: 109  Bit Score: 37.62  E-value: 2.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966987745  355 VAGGIGVTPFASILNTLLDDWKPykLRRLYFIWVCRDiqsfrwFADLLCMLHNKFWQENRPDYVNIQLYLSQTDG 429
Cdd:pfam00175   2 IAGGTGIAPVRSMLRAILEDPKD--PTQVVLVFGNRN------EDDILYREELDELAEKHPGRLTVVYVVSRPEA 68
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 245-391 4.48e-03

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


Pssm-ID: 99787  Cd Length: 232  Bit Score: 38.77  E-value: 4.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987745 245 SDVMEIRMVKE---NFkaRPGQYIILHCP--------SVSALENHPFTLTmcptetkatFGVHLKIVGDWTERFRDLLlP 313
Cdd:cd06190    9 HDVAEFRFALDgpaDF--LPGQYALLALPgvegaraySMANLANASGEWE---------FIIKRKPGGAASNALFDNL-E 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966987745 314 PSSQdseilpfiqsrnypkLYIDGPFGSPFEESLNYEISLCVAGGIGVTPFASILNTLLDDWKPYKlRRLYFIWVCRD 391
Cdd:cd06190   77 PGDE---------------LELDGPYGLAYLRPDEDRDIVCIAGGSGLAPMLSILRGAARSPYLSD-RPVDLFYGGRT 138
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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