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Conserved domains on  [gi|488878304|ref|WP_002790529|]
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NAD(P)H-dependent oxidoreductase [Campylobacter coli]

Protein Classification

NAD(P)H-dependent oxidoreductase( domain architecture ID 10114874)

NAD(P)H-dependent oxidoreductase, similar to nitroreductase NfsB, which catalyzes the reduction of flavin or nitrocompounds using NAD(P)H as electron donor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NfsB-like cd02149
nitroreductase similar to Escherichia coli NfsB; NAD(P)H:FMN oxidoreductase family. This ...
 5-197 6.89e-45

nitroreductase similar to Escherichia coli NfsB; NAD(P)H:FMN oxidoreductase family. This domain catalyzes the reduction of flavin, nitrocompound, quinones and azo compounds using NADH or NADPH as an electron donor. The enzyme is a homodimer, and each monomer binds a FMN as co-factor. This family includes FRase I in Vibrio fischeri, wihich reduces FMN into FMNH2 as part of the bioluminescent reaction. The family also includes oxygen-insensitive nitroreductases that use NADH or NADPH as an electron donor in the ping pong bi bi mechanism. This type of nitroreductase can be used in cancer chemotherapy to activate a range of prodrugs.


:

Pssm-ID: 380324 [Multi-domain]  Cd Length: 156  Bit Score: 146.24  E-value: 6.89e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304   5 LEIFSTRYSCRNFK-NEKLKKEDLNTILEIARLSPSSLGLEPWRFLVVQDDKKKEELAQI-CNQQQHVKNCAALIIIVSR 82
Cdd:cd02149    3 LELLNFRYATKKFDpNKKISDEDLETILEALRLSPSSFGLEPWKFLVVENPELKAKLAPAaWFNQPQIKDASHVVVFLAK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304  83 LDfldyfedklrkrdmseaeiqkrldtympflqslsqeqkisYAREQAHIALASILYSANALNIASCTIGGFDKEKLDSY 162
Cdd:cd02149   83 KD----------------------------------------WSAKQTYIALGNMLLAAAMLGIDSCPIEGFDPAKLDEI 122

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 488878304 163 LLLDTKKEKSTLAIALGYSNDEKIPqKNRFEFDKI 197
Cdd:cd02149  123 LGLDEKGYKISVMVAFGYRSEEKLP-KSRKPLEDV 156
 
Name Accession Description Interval E-value
NfsB-like cd02149
nitroreductase similar to Escherichia coli NfsB; NAD(P)H:FMN oxidoreductase family. This ...
 5-197 6.89e-45

nitroreductase similar to Escherichia coli NfsB; NAD(P)H:FMN oxidoreductase family. This domain catalyzes the reduction of flavin, nitrocompound, quinones and azo compounds using NADH or NADPH as an electron donor. The enzyme is a homodimer, and each monomer binds a FMN as co-factor. This family includes FRase I in Vibrio fischeri, wihich reduces FMN into FMNH2 as part of the bioluminescent reaction. The family also includes oxygen-insensitive nitroreductases that use NADH or NADPH as an electron donor in the ping pong bi bi mechanism. This type of nitroreductase can be used in cancer chemotherapy to activate a range of prodrugs.


Pssm-ID: 380324 [Multi-domain]  Cd Length: 156  Bit Score: 146.24  E-value: 6.89e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304   5 LEIFSTRYSCRNFK-NEKLKKEDLNTILEIARLSPSSLGLEPWRFLVVQDDKKKEELAQI-CNQQQHVKNCAALIIIVSR 82
Cdd:cd02149    3 LELLNFRYATKKFDpNKKISDEDLETILEALRLSPSSFGLEPWKFLVVENPELKAKLAPAaWFNQPQIKDASHVVVFLAK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304  83 LDfldyfedklrkrdmseaeiqkrldtympflqslsqeqkisYAREQAHIALASILYSANALNIASCTIGGFDKEKLDSY 162
Cdd:cd02149   83 KD----------------------------------------WSAKQTYIALGNMLLAAAMLGIDSCPIEGFDPAKLDEI 122

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 488878304 163 LLLDTKKEKSTLAIALGYSNDEKIPqKNRFEFDKI 197
Cdd:cd02149  123 LGLDEKGYKISVMVAFGYRSEEKLP-KSRKPLEDV 156
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
 5-198 1.96e-40

Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 134.98  E-value: 1.96e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304   5 LEIFSTRYSCRNFKNEKLKKEDLNTILEIARLSPSSLGLEPWRFLVVQDDKKKEELAQICNQ--QQHVKNCAALIIIVSR 82
Cdd:COG0778    2 LELLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEALAEanQEWVADAPVLIVVCAD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304  83 LDFldyfedklrkrdmseaeiqkrldtympflqslSQEQKISYAREQAHIALASILYSANALNIASCTIGGFDKEKLDSY 162
Cdd:COG0778   82 PDR--------------------------------SEKVPERYALLDAGIAAQNLLLAARALGLGTCWIGGFDPEKVREL 129

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 488878304 163 LLLDtKKEKSTLAIALGYSnDEKIPQKNRFEFDKIV 198
Cdd:COG0778  130 LGLP-EGEEPVALLALGYP-AEELNPRPRKPLEEVV 163
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
 11-180 7.01e-28

Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent and NAD(P)H-dependent enzymes able to metabolize nitrosubstituted compounds.


Pssm-ID: 425926 [Multi-domain]  Cd Length: 168  Bit Score: 102.86  E-value: 7.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304   11 RYSCRNFKNEKLKKEDLNTILEIARLSPSSLGLEPWRFLVVQDDKKKEELAQICNQQQHVKNCAALIIIVSRldflDYFE 90
Cdd:pfam00881   4 RRSVRKFDPEPVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLAEAALELLLVEPAAALLLLLRR----DANL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304   91 DKLRKRDMSEAEIQKRLDTYMPFLQSLSQEQKISYAREQAHIALASILYSANALNIASCTIGGFDKEKLDSYLLLDtKKE 170
Cdd:pfam00881  80 KLLLQDFLRGAPVLIVITASLSTYLRKAAERAYREALLDAGAAAQNLLLAATSLGLGSCPIGGFDAAAVRELLGLP-DDE 158

                         170
                  ....*....|
gi 488878304  171 KSTLAIALGY 180
Cdd:pfam00881 159 RLVGLIAVGY 168
PRK11053 PRK11053
oxygen-insensitive NAD(P)H nitroreductase;
10-201 8.13e-16

oxygen-insensitive NAD(P)H nitroreductase;


Pssm-ID: 182929 [Multi-domain]  Cd Length: 217  Bit Score: 72.70  E-value: 8.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304  10 TRYSCRNFK-NEKLKKEDLNTILEIARLSPSSLGLEPWRFLVVQDDKKKEELAQIC------NQQQhVKNCAALIIIVSR 82
Cdd:PRK11053   9 KRYTTKAFDpSKKLPAEQIEQIKTLLRFSPSSVNSQPWHFIVASTEEGKARIAKAAagnyafNERK-ILDASHVVVFCAK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304  83 LDFLD-YFEDKLRKRDMS------EAEIQKR------LDTYMPFLQSLSQeqkisYAREQAHIALASILYSANALNIASC 149
Cdd:PRK11053  88 TDMDDaYLELVLEQEDADgrfateEAKAAQDkgrrffADMHRKELKDLQH-----WMEKQVYLALGNLLLGAAALGIDAT 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488878304 150 TIGGFDKEKLDSYLLLDTKKEKSTLAIALGYSNDE----KIPqKNRFEFDKIVQFL 201
Cdd:PRK11053 163 PIEGFDAAILDAEFGLREKGLTSSVVVPLGYHSEEdfnaKLP-KSRLPQETIFTEI 217
 
Name Accession Description Interval E-value
NfsB-like cd02149
nitroreductase similar to Escherichia coli NfsB; NAD(P)H:FMN oxidoreductase family. This ...
 5-197 6.89e-45

nitroreductase similar to Escherichia coli NfsB; NAD(P)H:FMN oxidoreductase family. This domain catalyzes the reduction of flavin, nitrocompound, quinones and azo compounds using NADH or NADPH as an electron donor. The enzyme is a homodimer, and each monomer binds a FMN as co-factor. This family includes FRase I in Vibrio fischeri, wihich reduces FMN into FMNH2 as part of the bioluminescent reaction. The family also includes oxygen-insensitive nitroreductases that use NADH or NADPH as an electron donor in the ping pong bi bi mechanism. This type of nitroreductase can be used in cancer chemotherapy to activate a range of prodrugs.


Pssm-ID: 380324 [Multi-domain]  Cd Length: 156  Bit Score: 146.24  E-value: 6.89e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304   5 LEIFSTRYSCRNFK-NEKLKKEDLNTILEIARLSPSSLGLEPWRFLVVQDDKKKEELAQI-CNQQQHVKNCAALIIIVSR 82
Cdd:cd02149    3 LELLNFRYATKKFDpNKKISDEDLETILEALRLSPSSFGLEPWKFLVVENPELKAKLAPAaWFNQPQIKDASHVVVFLAK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304  83 LDfldyfedklrkrdmseaeiqkrldtympflqslsqeqkisYAREQAHIALASILYSANALNIASCTIGGFDKEKLDSY 162
Cdd:cd02149   83 KD----------------------------------------WSAKQTYIALGNMLLAAAMLGIDSCPIEGFDPAKLDEI 122

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 488878304 163 LLLDTKKEKSTLAIALGYSNDEKIPqKNRFEFDKI 197
Cdd:cd02149  123 LGLDEKGYKISVMVAFGYRSEEKLP-KSRKPLEDV 156
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
 5-198 1.96e-40

Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 134.98  E-value: 1.96e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304   5 LEIFSTRYSCRNFKNEKLKKEDLNTILEIARLSPSSLGLEPWRFLVVQDDKKKEELAQICNQ--QQHVKNCAALIIIVSR 82
Cdd:COG0778    2 LELLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEALAEanQEWVADAPVLIVVCAD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304  83 LDFldyfedklrkrdmseaeiqkrldtympflqslSQEQKISYAREQAHIALASILYSANALNIASCTIGGFDKEKLDSY 162
Cdd:COG0778   82 PDR--------------------------------SEKVPERYALLDAGIAAQNLLLAARALGLGTCWIGGFDPEKVREL 129

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 488878304 163 LLLDtKKEKSTLAIALGYSnDEKIPQKNRFEFDKIV 198
Cdd:COG0778  130 LGLP-EGEEPVALLALGYP-AEELNPRPRKPLEEVV 163
nitroreductase cd03370
uncharacterized nitroreductase family proteins; Nitroreductase family containing Thermus ...
 6-196 1.66e-33

uncharacterized nitroreductase family proteins; Nitroreductase family containing Thermus thermophilus NADH oxidase and other, uncharacterized proteins. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer.


Pssm-ID: 380327 [Multi-domain]  Cd Length: 191  Bit Score: 118.19  E-value: 1.66e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304   6 EIFSTRYSCRNFKNEKLKKEDLNTILEIARLSPSSLGLEPWRFLVVQDDKKKEELAQICNQQQHVKNCAALIIIVSRL-D 84
Cdd:cd03370    3 EAIESRRSIRKYTQEPVPDEDLREILRLAGLAPSAWNIQPWRFVVVRDAELKEQLQAAAYGQAQVTSAPAVIVIYSDMeD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304  85 FLDYFEDKLRKrDMSEAEIQKRLDTYMPFLQSLSQEQKISYAREQAHIALASILYSANALNIASCTIGGFDKEKLDSYLL 164
Cdd:cd03370   83 ALANLEETIHP-GLSEERRQREAAGLRGAFGKMSVEQRGQWGLAQANIALGFLLLAAQSLGYDTSPMLGFDPEKVKALLG 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 488878304 165 LdtkKEKSTLA--IALGYSNDEKIPqKNRFEFDK 196
Cdd:cd03370  162 L---PEHVTIAalVALGKPAEEGYP-HHRHSLER 191
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
 11-180 7.01e-28

Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent and NAD(P)H-dependent enzymes able to metabolize nitrosubstituted compounds.


Pssm-ID: 425926 [Multi-domain]  Cd Length: 168  Bit Score: 102.86  E-value: 7.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304   11 RYSCRNFKNEKLKKEDLNTILEIARLSPSSLGLEPWRFLVVQDDKKKEELAQICNQQQHVKNCAALIIIVSRldflDYFE 90
Cdd:pfam00881   4 RRSVRKFDPEPVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLAEAALELLLVEPAAALLLLLRR----DANL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304   91 DKLRKRDMSEAEIQKRLDTYMPFLQSLSQEQKISYAREQAHIALASILYSANALNIASCTIGGFDKEKLDSYLLLDtKKE 170
Cdd:pfam00881  80 KLLLQDFLRGAPVLIVITASLSTYLRKAAERAYREALLDAGAAAQNLLLAATSLGLGSCPIGGFDAAAVRELLGLP-DDE 158

                         170
                  ....*....|
gi 488878304  171 KSTLAIALGY 180
Cdd:pfam00881 159 RLVGLIAVGY 168
Nitro_FMN_reductase cd02062
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 10-180 2.15e-26

nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or nitrocompounds using NAD(P)H as electron donor in a obligatory two-electron transfer, utilizing FMN or FAD as cofactor. They are often found to be homodimers. Enzymes of this family are described as NAD(P)H:FMN oxidoreductases, oxygen-insensitive nitroreductase, flavin reductase P, dihydropteridine reductase, NADH oxidase or NADH dehydrogenase.


Pssm-ID: 380311 [Multi-domain]  Cd Length: 139  Bit Score: 98.14  E-value: 2.15e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304  10 TRYSCRNFKNEKLKKEDLNTILEIARLSPSSLGLEPWRFLVVQDDKKKEELAQ-ICNQQQHVKNCAALIIIVSRLDFLDY 88
Cdd:cd02062    3 TRRSIRKFTDKPVPEEKLRKILEAARLAPSAGNLQPWRFIVVRDREKKEKLAKlAAPNQKFIAGAPVVIVVVADPDKSRP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304  89 fedklrkrdmseaeiqkrldtympflqslsqeqkisYAREQAHIALASILYSANALNIASCTIGGFDK--EKLDSYLLLD 166
Cdd:cd02062   83 ------------------------------------WALEDAGAAAQNLLLAAAALGLGSCWIGGFDFreDKVRELLGIP 126

                        170
                 ....*....|....
gi 488878304 167 TKKEkSTLAIALGY 180
Cdd:cd02062  127 ENLR-PVALIAIGY 139
MhqN-like cd02137
nitroreductase family protein similar to the NAD(P)H nitroreductase MhqN; A diverse subfamily ...
 5-197 6.38e-25

nitroreductase family protein similar to the NAD(P)H nitroreductase MhqN; A diverse subfamily of the nitroreductase family containing uncharacterized proteins; includes nitroreductases MhqN, YodC, YdgI, DrgA. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer.


Pssm-ID: 380314 [Multi-domain]  Cd Length: 147  Bit Score: 94.61  E-value: 6.38e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304   5 LEIFSTRYSCRNF-KNEKLKKEDLNTILEIARLSPSSLGLEPWRFLVVQDDKKKEELAQICNQQQHVKNCAALIIIVSRL 83
Cdd:cd02137    1 LEVIKSRRSVRNFdPDHKIPKEELKEILELATLAPSSFNLQPWRFVVVRDPELKAKLAEAAYNQPQVTTASAVILVLGDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304  84 DfldyfedklrkrdmseaeiqkrldtympflqslsqeqkisyareqAHIALASILYSANALNIASCTIGGFDKEKLDSYL 163
Cdd:cd02137   81 N---------------------------------------------AGLAAMNLMLAAKAKGYDTCPMGGFDKEKVAELL 115

                        170       180       190
                 ....*....|....*....|....*....|....
gi 488878304 164 LLDTKKEkSTLAIALGYSnDEKIPQKNRFEFDKI 197
Cdd:cd02137  116 NLPDRYV-PVLLIAIGKA-ADKAPRSGRLPVDEV 147
nitroreductase cd02151
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 6-189 1.02e-20

nitroreductase family protein; A subfamily of the nitroreductase family containing uncharacterized proteins. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer.often found to be homodimers..


Pssm-ID: 380326 [Multi-domain]  Cd Length: 157  Bit Score: 84.12  E-value: 1.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304   6 EIFSTRYSCRNFKNEKLKKEDLNTILEIARLSPSSLGLEPWRFLVVQDDKKKEELAQICN-QQQHVKNCAALIIIVSRLD 84
Cdd:cd02151    1 ELLKKRRSIRKYTDEPIEEEKLEEILEAALLAPSSRNSRPVEFIVVDDKETLKKLSECKPhGSAFLKGAPAAIVVLADTE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304  85 FLDYFedklrkrdmseaeiqkrldtympflqslsqeqkisyaREQAHIALASILYSANALNIASCTI---GGFDKEKLDS 161
Cdd:cd02151   81 KSDTW-------------------------------------IEDASIAATYIQLAAESLGLGSCWIqirNRETQDGKTA 123

                        170       180       190
                 ....*....|....*....|....*....|...
gi 488878304 162 --YL--LLDTKKEKSTLA-IALGYSNDEKIPQK 189
Cdd:cd02151  124 eeYVreLLGIPENYRVLCiIALGYPDEEKPPHE 156
nitroreductase cd02139
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 5-198 1.24e-20

nitroreductase family protein; A subfamily of the nitroreductase family containing uncharacterized proteins. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer.


Pssm-ID: 380316 [Multi-domain]  Cd Length: 165  Bit Score: 84.06  E-value: 1.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304   5 LEIFSTRYSCRNFKNEKLKKEDLNTILEIARLSPSSLGLEPWRFLVVQDDKKKEELAQICNQQQHVKNCAALIIIVSRld 84
Cdd:cd02139    2 YEAIKKRRSIRKYKPTPVEEEKLLRILEAARLAPSAKNRQPWRFIVVKDKELKEKLAEAANGQKFIAEAPVVIVACAD-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304  85 fldyfEDKLRKRDMSEAEIqkrLDTympflqslsqeqkiSYAREqaHIALAsilysANALNIASCTIGGFDKEKLDSylL 164
Cdd:cd02139   80 -----PSESGMGCGKPYYL---VDV--------------AIAME--HLVLA-----ATEEGLGTCWIGAFDEDKVKE--I 128

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 488878304 165 LDTKKEKSTLAI-ALGYSnDEKIPQKNRFEFDKIV 198
Cdd:cd02139  129 LGIPEEYRVVALtPLGYP-AEEPPPRPRKPLEEIV 162
nitroreductase cd20609
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 5-159 2.15e-18

nitroreductase family protein; A subfamily of the nitroreductase family containing uncharacterized proteins. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer.often found to be homodimers.


Pssm-ID: 380330 [Multi-domain]  Cd Length: 145  Bit Score: 77.81  E-value: 2.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304   5 LEIFSTRYSCRNFKNEKLKKEDLNTILEIARLSPSSLGLEPWRFLVVQDDKKKEELAQICNQQQHvkncAALIIIVSrld 84
Cdd:cd20609    3 LELAKKRYSVRKFSDKPVEKEKLDKILEAGRLAPTAVNYQPQRILVVRSEEALEKLAKATPRFFG----APLVIVVC--- 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488878304  85 fldyfedklrkRDMSEAEiqKRldtymPFLQSLSQEQKISYAREqaHIALAsilysANALNIASCTIGGFDKEKL 159
Cdd:cd20609   76 -----------YDKDESW--KR-----PYDGKDSGDIDAAIVAT--HMMLA-----ATELGLGTCWVGNFDPEKV 125
nitroreductase cd20608
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 5-180 2.30e-18

nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or nitrocompounds using NAD(P)H as electron donor in a obligatory two-electron transfer, utilizing FMN or FAD as cofactor. They are often found to be homodimers. Enzymes of this family are described as NAD(P)H:FMN oxidoreductases, oxygen-insensitive nitroreductase, flavin reductase P, dihydropteridine reductase, NADH oxidase or NADH dehydrogenase.


Pssm-ID: 380329 [Multi-domain]  Cd Length: 145  Bit Score: 77.76  E-value: 2.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304   5 LEIFSTRYSCRNFKNEKLKKEDLNTILEIARLSPSSLGLEPWRFLVVQDDKKKEELAQICNQQQHVKNCAALIIIVSrld 84
Cdd:cd20608    1 FEAIKTRRSVRRFSDKPVEEEKLEKILEAARLAPSWANKQCWRFIVVTDKETLSELAKKESPSNGWLKDAPVIIVVC--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304  85 fldyfedklrkrdmSEAEIQKRLDtympflqslsqeqKISYAREQAHIALASILYSANALNIASCTIGGFDKEKLDSylL 164
Cdd:cd20608   78 --------------ADPKDSGWLN-------------GQNYYLVDAAIAMQNLMLAATDLGLGTCWIGAFDEKKVKE--I 128

                        170
                 ....*....|....*..
gi 488878304 165 LDTKKEKSTLA-IALGY 180
Cdd:cd20608  129 LGIPENIRVVAlTPLGY 145
TdsD-like cd02138
nitroreductase similar to Burkholderia pseudomallei TdsD; A subfamily of the nitroreductase ...
 7-191 2.66e-18

nitroreductase similar to Burkholderia pseudomallei TdsD; A subfamily of the nitroreductase family containing uncharacterized proteins that are similar to Burkholderia pseudomallei TdsD, may be involved in the processing of organosulfur compounds. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer.


Pssm-ID: 380315 [Multi-domain]  Cd Length: 174  Bit Score: 78.35  E-value: 2.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304   7 IFSTRYSCRNFKNEKLKKEDLNTILEIARLSPSSLGLEPWRFLVVQDD----KKKEELAQICNQQQhVKNCAALIIIVSR 82
Cdd:cd02138    1 LIAERWSPRAFSPEPISEEDLLSLFEAARWAPSCFNEQPWRFVVARRDteafEKLLDLLAEGNQSW-AKNAPVLIVVLAK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304  83 ldflDYFEDKLRKRDmseaeiqkrldtympflqslsqeqkisYAREQAHIALASILYSANALNIASCTIGGFDKEKLDSY 162
Cdd:cd02138   80 ----TEFDHNGKPNR---------------------------YALFDTGAAVANLALQATALGLVVHQMAGFDPEKAKEA 128

                        170       180       190
                 ....*....|....*....|....*....|
gi 488878304 163 LLLDTKKEKSTLaIALGY-SNDEKIPQKNR 191
Cdd:cd02138  129 LGIPDEYEPITM-IAIGYpGDPESLPEKLL 157
PnbA_NfnB-like cd02136
nitroreductase similar to Mycobacterium smegmatis NfnB; Members of this family utilize FMN as ...
 10-191 1.58e-17

nitroreductase similar to Mycobacterium smegmatis NfnB; Members of this family utilize FMN as a cofactor and catalyze reduction of a variety of nitroaromatic compounds, including nitrofurans, nitrobenzens, nitrophenol, nitrobenzoate and quinones by using either NADH or NADPH as a source of reducing equivalents in an obligatory two-election transfer mechanism. The enzyme is typically a homodimer. Mycobacterium smegmatis nitroreductase NfnB plays a role in resistance to benzothiazinone.


Pssm-ID: 380313 [Multi-domain]  Cd Length: 152  Bit Score: 75.70  E-value: 1.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304  10 TRYSCRNFKNEKLKKEDLNTILEIARLSPSSLGLEPWRFLVVQdDKKKEELAQIcnqqqhVKNCAALIIIvsrldFLDYF 89
Cdd:cd02136    4 SRRSVRAFKDKPVPKETIEKILEAARRAPSGKNTQPWRVYVVT-GKARERLKKA------FFGAPVALFL-----TMDKV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304  90 EDKLRKRDMSeaeiqkrldtympflqslsqeqkisyareqahIALASILYSANALNIASCTIG---GFDKEKLDSYLLLD 166
Cdd:cd02136   72 LGPWSWFDLG--------------------------------AFLQNLMLAAHALGLGTCPQGalaGYPDVVRKELGIPD 119

                        170       180
                 ....*....|....*....|....*
gi 488878304 167 TKKEKstLAIALGYSNDEKIPQKNR 191
Cdd:cd02136  120 DEELV--CGIALGYPDPDAPVNQFR 142
PRK11053 PRK11053
oxygen-insensitive NAD(P)H nitroreductase;
10-201 8.13e-16

oxygen-insensitive NAD(P)H nitroreductase;


Pssm-ID: 182929 [Multi-domain]  Cd Length: 217  Bit Score: 72.70  E-value: 8.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304  10 TRYSCRNFK-NEKLKKEDLNTILEIARLSPSSLGLEPWRFLVVQDDKKKEELAQIC------NQQQhVKNCAALIIIVSR 82
Cdd:PRK11053   9 KRYTTKAFDpSKKLPAEQIEQIKTLLRFSPSSVNSQPWHFIVASTEEGKARIAKAAagnyafNERK-ILDASHVVVFCAK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304  83 LDFLD-YFEDKLRKRDMS------EAEIQKR------LDTYMPFLQSLSQeqkisYAREQAHIALASILYSANALNIASC 149
Cdd:PRK11053  88 TDMDDaYLELVLEQEDADgrfateEAKAAQDkgrrffADMHRKELKDLQH-----WMEKQVYLALGNLLLGAAALGIDAT 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488878304 150 TIGGFDKEKLDSYLLLDTKKEKSTLAIALGYSNDE----KIPqKNRFEFDKIVQFL 201
Cdd:PRK11053 163 PIEGFDAAILDAEFGLREKGLTSSVVVPLGYHSEEdfnaKLP-KSRLPQETIFTEI 217
NfsA-like cd02146
nitroreductase similar to Escherichia coli NfsA; This family contains NADPH-dependent flavin ...
 11-198 3.43e-15

nitroreductase similar to Escherichia coli NfsA; This family contains NADPH-dependent flavin reductase and oxygen-insensitive nitroreductase. These enzymes are homodimeric flavoproteins that contain one FMN per monomer as a cofactor. Flavin reductase catalyzes the reduction of flavin by using NADPH as an electron donor. Oxygen-insensitive nitroreductase, such as NfsA protein in Escherichia coli, catalyzes reduction of nitrocompounds using NADPH as electron donor.


Pssm-ID: 380322 [Multi-domain]  Cd Length: 229  Bit Score: 71.11  E-value: 3.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304  11 RYSCRNFKNEKLKKEDLNTILEIARLSPSSLGLEPWRFLVVQDDKKKEELAQICNQQQHVKNCAALIIIVSrldfldyfe 90
Cdd:cd02146    8 HRSVRKFTDEPLTDETLETLIAAAQSASTSSNLQAYSVIVVTDPELREKLAELAGNQPYVAQAPVFLVFCA--------- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304  91 DKLRKRDMSEAEIQK--RLDTYMPFLQSLSqeqkisyareQAHIALASILYSANALNIASCTIGGF--DKEKLDSYLLLd 166
Cdd:cd02146   79 DLYRHQKIAEEAGGKdvGLDYLESFLVGVV----------DAALAAQNALVAAESLGLGIVYIGGIrnNPEEVIELLGL- 147

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 488878304 167 tkkEKSTLAI---ALGYSnDEKIPQKNRFEFDKIV 198
Cdd:cd02146  148 ---PEYVFPLfglTVGHP-DPTPEVKPRLPLEAVV 178
nitroreductase cd02150
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 10-192 3.84e-13

nitroreductase family protein; A subfamily of the nitroreductase family containing uncharacterized proteins. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer.often found to be homodimers.


Pssm-ID: 380325 [Multi-domain]  Cd Length: 156  Bit Score: 64.16  E-value: 3.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304  10 TRYSCRNFKNEKLKKEDLNTILEIARLSPSSLGLEPWRFLVVQDDKKKEELAQICNQQQHVKNcAALIIIV----SRLDF 85
Cdd:cd02150    3 TRRSIRKYTDKPVEEEDIEKLLRAAMAAPSAGNQQPWHFIVVTDREKLDKIAEAHPYGKMLKE-APLAIVVcgdpSKEKA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304  86 LDYFEdklrkRDMSeaeiqkrldtympflqslsqeqkisyareqahIALASILYSANALNIASCTIGGFDKEKLdsylll 165
Cdd:cd02150   82 PGYWV-----QDCS--------------------------------AATENILLAAHALGLGAVWLGVYPFEER------ 118

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 488878304 166 dTKKEKSTL----------AIALGYSNDEKIPqKNRF 192
Cdd:cd02150  119 -VKAIREILnipeniipfcVIALGYPAEEKEP-KDRF 153
iodotyrosine_dehalogenase cd02144
iodotyrosine dehalogenase; Iodotyrosine dehalogenase catalyzes the removal of iodine from the ...
 5-64 2.67e-12

iodotyrosine dehalogenase; Iodotyrosine dehalogenase catalyzes the removal of iodine from the 3, 5 positions of L-tyosine in thyroid, liver and kidney, using NADPH as electron donor. This enzyme is a homolog of the nitroreductase family. These enzymes are usually homodimers.


Pssm-ID: 380320  Cd Length: 192  Bit Score: 62.55  E-value: 2.67e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304   5 LEIFSTRYSCRNFKNEKLKKEDLNTILEIARLSPSSLGLEPWRFLVVQDDKKKEELAQIC 64
Cdd:cd02144    2 YELMKKRRSVRDFSSEPVPREVIENAIRTAGTAPSGANTQPWTFVVVSDPEIKRKIREAA 61
nitroreductase cd20610
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 11-61 2.12e-11

nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or nitrocompounds using NAD(P)H as electron donor in a obligatory two-electron transfer, utilizing FMN or FAD as cofactor. They are often found to be homodimers. Enzymes of this family are described as NAD(P)H:FMN oxidoreductases, oxygen-insensitive nitroreductase, flavin reductase P, dihydropteridine reductase, NADH oxidase or NADH dehydrogenase.


Pssm-ID: 380331 [Multi-domain]  Cd Length: 167  Bit Score: 59.60  E-value: 2.12e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488878304  11 RYSCRNFKNEKLKKEDLNTILEIARLSPSSLGLEPWRFLVVQDDKKKEELA 61
Cdd:cd20610    4 RRSIRKFKPDPVPKEDIEKILEAANWAPSGMNRQNWEFVVVKGGEKIEKIG 54
nitroreductase_FeS-like cd02143
nitroreductases with an N-terminal iron-sulfur cluster-binding domain; Members of this family ...
 10-64 2.72e-08

nitroreductases with an N-terminal iron-sulfur cluster-binding domain; Members of this family utilize FMN as a cofactor. This family may be involved in the reduction of flavin or nitroaromatic compounds via an obligatory two-electron transfer. Nitroreductase is homodimer. Each subunit contains one FMN molecule.


Pssm-ID: 380319 [Multi-domain]  Cd Length: 187  Bit Score: 51.32  E-value: 2.72e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488878304  10 TRYSCRNFKNEKLKKEDLNTILEIARLSPSSLGLEPWRFLVVQDDKKKEELAQIC 64
Cdd:cd02143    4 SRRSIRRYKDKPVPRETLEKLLDIARYAPTGHNSQPVHWLVVDDPEKVRRLAELV 58
YdjA-like cd02135
nitroreductase family protein similar to Escherichia coli YdjA; A subfamily of the ...
 5-58 8.70e-07

nitroreductase family protein similar to Escherichia coli YdjA; A subfamily of the nitroreductase family containing uncharacterized proteins that are similar to nitroreductase YdjA from Escherichia coli. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer. Members of this family are also called NADH dehydrogenase, oxygen-insensitive NAD(P)H nitrogenase or dihydropteridine reductase.


Pssm-ID: 380312 [Multi-domain]  Cd Length: 162  Bit Score: 46.83  E-value: 8.70e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488878304   5 LEIFSTRYSCRNFK-NEKLKKEDLNTILEIARLSPSSLGLEPWRFLVVQDDKKKE 58
Cdd:cd02135    1 LELIKTRRSIRKFKlTGAPPEEQLEELLEAAMWAPNHGKLEPWRFIVVTGEGRER 55
RutE-like cd02148
nitroreductase similar to Escherichia coli RutE; A subfamily of the nitroreductase family ...
 17-195 1.26e-06

nitroreductase similar to Escherichia coli RutE; A subfamily of the nitroreductase family containing uncharacterized proteins that are similar to nitroreductase. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer. RutE is involved in the utilization of uracil as the sole nitrogen source; it appears to have the same function as YdfG, which reduces malonic semialdehyde to 3-hydroxypropionic acid.


Pssm-ID: 380323 [Multi-domain]  Cd Length: 186  Bit Score: 46.86  E-value: 1.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304  17 FKNEKLKKEDLNTILEIARLSPSSLGLEPWRFLVVQDDKKKEELAQ--ICNQQQHVKNCAALIIIVSRLDFLDYFEdklr 94
Cdd:cd02148   15 WEDKPVSDEELRAIYDLAKWGPTAANCSPARIVFVRSAEAKERLVPhlSEGNREKTMAAPVTAILAYDTEFYEHLP---- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488878304  95 krdmseaeiqkRLDTYMP----FLQSlSQEQKISYAREQAHIALASILYSANALNIASCTIGGFDKEKLDSYLLLDTkKE 170
Cdd:cd02148   91 -----------RLFPHGDarswFFGS-GPARAEETAFRNASLQAAYFILAARALGLDCGPMSGFDAAGVDAEFFAGT-RW 157

                        170       180
                 ....*....|....*....|....*.
gi 488878304 171 KSTLAIALGYSNDEKI-PQKNRFEFD 195
Cdd:cd02148  158 KSNLVVNLGYGDPSKLfPRLPRLDFD 183
BluB cd02145
5,6-dimethylbenzimidazole synthase; BluB catalyzes the O2-dependent conversion of FMNH2 to 5, ...
 6-66 2.29e-04

5,6-dimethylbenzimidazole synthase; BluB catalyzes the O2-dependent conversion of FMNH2 to 5,6-dimethylbenzimidazole (DMB), a component of vitamin B12; is is a subfamily of the nitroreductase family; nitroreductases typically reduce their substrates by using NAD(P)H as electron donor and often use FMN as a cofactor.


Pssm-ID: 380321  Cd Length: 196  Bit Score: 40.42  E-value: 2.29e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488878304   6 EIFSTRYSCRNFKNEKLKKEDLNTILEIARLSPSsLGL-EPWRFLVVQDDKKKE---ELAQICNQ 66
Cdd:cd02145    2 RVIRWRRDVRHFRPDPVPEEVLERLLQAAHLAPS-VGLmQPWRFVRVRSAATRKavhELFQRANA 65
PRK10765 PRK10765
oxygen-insensitive NADPH nitroreductase;
1-74 1.06e-03

oxygen-insensitive NADPH nitroreductase;


Pssm-ID: 182710  Cd Length: 240  Bit Score: 38.80  E-value: 1.06e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488878304   1 MKTELE-IFSTRySCRNFKNEKLKKEDLNTILEIARLSPSSLGLEPWRFLVVQDDKKKEELAQICNQQQHVKNCA 74
Cdd:PRK10765   1 MTPTIElILSHR-SIRHFTDEPISEAQREAIINAARAASSSSFLQCSSIIRITDKALREALVELTGGQKYVAQAA 74
 
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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