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Conserved domains on  [gi|1681035560|dbj|BBK86176|]
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NAD(P)H nitroreductase [Bacteroides uniformis]

Protein Classification

NfnB family protein( domain architecture ID 10002498)

NfnB family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
40-206 1.97e-39

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


:

Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 133.05  E-value: 1.97e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560  40 VIETIMSRRSIRQYKPQAVNRDTMQIILDCGINAPNGQNKQSWEVRVVDNPDFINGITEIYKKENpkaaedpkfKNMFRN 119
Cdd:COG0778     1 LLELLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEALAEAN---------QEWVAD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560 120 ASTVVFIANDPS------YDLSQIDCGLLGENMILSAWSMGIGSCCLGGptrfmtstPAAAEYLKKLDIPEGYQLLYCIA 193
Cdd:COG0778    72 APVLIVVCADPDrsekvpERYALLDAGIAAQNLLLAARALGLGTCWIGG--------FDPEKVRELLGLPEGEEPVALLA 143
                         170
                  ....*....|...
gi 1681035560 194 FGYPDETPAAKPR 206
Cdd:COG0778   144 LGYPAEELNPRPR 156
 
Name Accession Description Interval E-value
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
40-206 1.97e-39

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


Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 133.05  E-value: 1.97e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560  40 VIETIMSRRSIRQYKPQAVNRDTMQIILDCGINAPNGQNKQSWEVRVVDNPDFINGITEIYKKENpkaaedpkfKNMFRN 119
Cdd:COG0778     1 LLELLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEALAEAN---------QEWVAD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560 120 ASTVVFIANDPS------YDLSQIDCGLLGENMILSAWSMGIGSCCLGGptrfmtstPAAAEYLKKLDIPEGYQLLYCIA 193
Cdd:COG0778    72 APVLIVVCADPDrsekvpERYALLDAGIAAQNLLLAARALGLGTCWIGG--------FDPEKVRELLGLPEGEEPVALLA 143
                         170
                  ....*....|...
gi 1681035560 194 FGYPDETPAAKPR 206
Cdd:COG0778   144 LGYPAEELNPRPR 156
PnbA_NfnB-like cd02136
nitroreductase similar to Mycobacterium smegmatis NfnB; Members of this family utilize FMN as ...
43-206 1.43e-33

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: 117.69  E-value: 1.43e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560  43 TIMSRRSIRQYKPQAVNRDTMQIILDCGINAPNGQNKQSWEVRVVDNpdfingiteiykkenpKAAEdpKFKNMFRNAST 122
Cdd:cd02136     1 AIKSRRSVRAFKDKPVPKETIEKILEAARRAPSGKNTQPWRVYVVTG----------------KARE--RLKKAFFGAPV 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560 123 VVFIANDPSYD-LSQIDCGLLGENMILSAWSMGIGSCCLGgptrfmtstpAAAEY----LKKLDIPEGYQLLYCIAFGYP 197
Cdd:cd02136    63 ALFLTMDKVLGpWSWFDLGAFLQNLMLAAHALGLGTCPQG----------ALAGYpdvvRKELGIPDDEELVCGIALGYP 132
                         170
                  ....*....|
gi 1681035560 198 DET-PAAKPR 206
Cdd:cd02136   133 DPDaPVNQFR 142
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
44-196 7.99e-31

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: 110.94  E-value: 7.99e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560  44 IMSRRSIRQYKPQAVNRDTMQIILDCGINAPNGQNKQSWEVRVVDNPDFINGITEIYKKENPKAAEDP------------ 111
Cdd:pfam00881   1 IRQRRSVRKFDPEPVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLAEAALELLLVEPAAAlllllrrdanlk 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560 112 -KFKNMFRNASTVVFI----------ANDPSYDLSQIDCGLLGENMILSAWSMGIGSCCLGGptrfmtstPAAAEYLKKL 180
Cdd:pfam00881  81 lLLQDFLRGAPVLIVItaslstylrkAAERAYREALLDAGAAAQNLLLAATSLGLGSCPIGG--------FDAAAVRELL 152
                         170
                  ....*....|....*.
gi 1681035560 181 DIPEGYQLLYCIAFGY 196
Cdd:pfam00881 153 GLPDDERLVGLIAVGY 168
PRK10765 PRK10765
oxygen-insensitive NADPH nitroreductase;
38-211 2.51e-11

oxygen-insensitive NADPH nitroreductase;


Pssm-ID: 182710  Cd Length: 240  Bit Score: 61.14  E-value: 2.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560  38 NTVIETIMSRRSIRQYKPQAVNRDTMQIILDCGINAPNGQNKQ-SWEVRVVDnPDFINGITEiYKKENPKAAEDPKFknm 116
Cdd:PRK10765    2 TPTIELILSHRSIRHFTDEPISEAQREAIINAARAASSSSFLQcSSIIRITD-KALREALVE-LTGGQKYVAQAAEF--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560 117 frnastVVFIAN---------DPSYDLSQ------IDCGLLGENMILSAWSMGIGSCCLGGptrfMTSTPAAAEYLkkLD 181
Cdd:PRK10765   77 ------WVFCADfnrhlqicpDAQLGLAEqlligaVDTAIMAQNALLAAESLGLGGVYIGG----LRNNIEAVTEL--LK 144
                         170       180       190
                  ....*....|....*....|....*....|
gi 1681035560 182 IPEGYQLLYCIAFGYPDETPAAKPRNAAKV 211
Cdd:PRK10765  145 LPQHVLPLFGLCLGWPAQNPDLKPRLPASL 174
 
Name Accession Description Interval E-value
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
40-206 1.97e-39

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


Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 133.05  E-value: 1.97e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560  40 VIETIMSRRSIRQYKPQAVNRDTMQIILDCGINAPNGQNKQSWEVRVVDNPDFINGITEIYKKENpkaaedpkfKNMFRN 119
Cdd:COG0778     1 LLELLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEALAEAN---------QEWVAD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560 120 ASTVVFIANDPS------YDLSQIDCGLLGENMILSAWSMGIGSCCLGGptrfmtstPAAAEYLKKLDIPEGYQLLYCIA 193
Cdd:COG0778    72 APVLIVVCADPDrsekvpERYALLDAGIAAQNLLLAARALGLGTCWIGG--------FDPEKVRELLGLPEGEEPVALLA 143
                         170
                  ....*....|...
gi 1681035560 194 FGYPDETPAAKPR 206
Cdd:COG0778   144 LGYPAEELNPRPR 156
PnbA_NfnB-like cd02136
nitroreductase similar to Mycobacterium smegmatis NfnB; Members of this family utilize FMN as ...
43-206 1.43e-33

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: 117.69  E-value: 1.43e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560  43 TIMSRRSIRQYKPQAVNRDTMQIILDCGINAPNGQNKQSWEVRVVDNpdfingiteiykkenpKAAEdpKFKNMFRNAST 122
Cdd:cd02136     1 AIKSRRSVRAFKDKPVPKETIEKILEAARRAPSGKNTQPWRVYVVTG----------------KARE--RLKKAFFGAPV 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560 123 VVFIANDPSYD-LSQIDCGLLGENMILSAWSMGIGSCCLGgptrfmtstpAAAEY----LKKLDIPEGYQLLYCIAFGYP 197
Cdd:cd02136    63 ALFLTMDKVLGpWSWFDLGAFLQNLMLAAHALGLGTCPQG----------ALAGYpdvvRKELGIPDDEELVCGIALGYP 132
                         170
                  ....*....|
gi 1681035560 198 DET-PAAKPR 206
Cdd:cd02136   133 DPDaPVNQFR 142
nitroreductase cd02151
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
42-205 1.88e-31

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: 112.24  E-value: 1.88e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560  42 ETIMSRRSIRQYKPQAVNRDTMQIILDCGINAPNGQNKQSWEVRVVDNPDFINGITEIykkenpkaaeDPKFKNMFRNAS 121
Cdd:cd02151     1 ELLKKRRSIRKYTDEPIEEEKLEEILEAALLAPSSRNSRPVEFIVVDDKETLKKLSEC----------KPHGSAFLKGAP 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560 122 TVVFIANDPSY-DLSQIDCGLLGENMILSAWSMGIGSCCLGGPTRFMTSTPAAAEYLKK-LDIPEGYQLLYCIAFGYPDE 199
Cdd:cd02151    71 AAIVVLADTEKsDTWIEDASIAATYIQLAAESLGLGSCWIQIRNRETQDGKTAEEYVRElLGIPENYRVLCIIALGYPDE 150

                  ....*.
gi 1681035560 200 TPAAKP 205
Cdd:cd02151   151 EKPPHE 156
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
44-196 7.99e-31

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: 110.94  E-value: 7.99e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560  44 IMSRRSIRQYKPQAVNRDTMQIILDCGINAPNGQNKQSWEVRVVDNPDFINGITEIYKKENPKAAEDP------------ 111
Cdd:pfam00881   1 IRQRRSVRKFDPEPVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLAEAALELLLVEPAAAlllllrrdanlk 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560 112 -KFKNMFRNASTVVFI----------ANDPSYDLSQIDCGLLGENMILSAWSMGIGSCCLGGptrfmtstPAAAEYLKKL 180
Cdd:pfam00881  81 lLLQDFLRGAPVLIVItaslstylrkAAERAYREALLDAGAAAQNLLLAATSLGLGSCPIGG--------FDAAAVRELL 152
                         170
                  ....*....|....*.
gi 1681035560 181 DIPEGYQLLYCIAFGY 196
Cdd:pfam00881 153 GLPDDERLVGLIAVGY 168
nitroreductase_FeS-like cd02143
nitroreductases with an N-terminal iron-sulfur cluster-binding domain; Members of this family ...
44-213 4.03e-28

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: 104.48  E-value: 4.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560  44 IMSRRSIRQYKPQAVNRDTMQIILDCGINAPNGQNKQSWEVRVVDNPDFINGITEI-------YKKENPKAAEDPKFKNM 116
Cdd:cd02143     2 LRSRRSIRRYKDKPVPRETLEKLLDIARYAPTGHNSQPVHWLVVDDPEKVRRLAELvidwmreLIKEDPELAGKLFLDGI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560 117 -----------FRNASTVVFIANDPSYDLSQIDCGLLGENMILSAWSMGIGSCCLGgptRFMTstpAAAEY---LKKLDI 182
Cdd:cd02143    82 vaawekgidviLRGAPHLVVAHAPKDAPTPPVDCAIALTYLELAAPSLGLGTCWAG---FFTA---AANNYpplREALGL 155
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1681035560 183 PEGYQLLYCIAFGYPDETPAAKP-RNAAKVKF 213
Cdd:cd02143   156 PEGHKVGGAMMLGYPKYKYHRIPpRKPARVTW 187
nitroreductase cd02150
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
44-206 6.50e-28

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: 103.06  E-value: 6.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560  44 IMSRRSIRQYKPQAVNRDTMQIILDCGINAPNGQNKQSWEVRVVDNPDFINGITEIYkkenpkaaedpKFKNMFRNASTV 123
Cdd:cd02150     1 ILTRRSIRKYTDKPVEEEDIEKLLRAAMAAPSAGNQQPWHFIVVTDREKLDKIAEAH-----------PYGKMLKEAPLA 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560 124 VFIANDPS----YDLSQIDCGLLGENMILSAWSMGIGSCCLG-GPtrfmtSTPAAAEYLKKLDIPEGYQLLYCIAFGYPD 198
Cdd:cd02150    70 IVVCGDPSkekaPGYWVQDCSAATENILLAAHALGLGAVWLGvYP-----FEERVKAIREILNIPENIIPFCVIALGYPA 144

                  ....*...
gi 1681035560 199 ETPAAKPR 206
Cdd:cd02150   145 EEKEPKDR 152
Nitro_FMN_reductase cd02062
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
44-196 2.30e-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: 98.52  E-value: 2.30e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560  44 IMSRRSIRQYKPQAVNRDTMQIILDCGINAPNGQNKQSWEVRVVDNPDFINgitEIYKKENPKAAedpkfknMFRNAS-T 122
Cdd:cd02062     1 IKTRRSIRKFTDKPVPEEKLRKILEAARLAPSAGNLQPWRFIVVRDREKKE---KLAKLAAPNQK-------FIAGAPvV 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681035560 123 VVFIAN-DPSYDLSQIDCGLLGENMILSAWSMGIGSCclggptrFMTSTPAAAEYLKK-LDIPEGYQLLYCIAFGY 196
Cdd:cd02062    71 IVVVADpDKSRPWALEDAGAAAQNLLLAAAALGLGSC-------WIGGFDFREDKVRElLGIPENLRPVALIAIGY 139
nitroreductase cd20608
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
42-196 1.95e-24

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: 93.94  E-value: 1.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560  42 ETIMSRRSIRQYKPQAVNRDTMQIILDCGINAPNGQNKQSWEVRVVDNPDfinGITEIYKKENPkaaedpkFKNMFRNAS 121
Cdd:cd20608     2 EAIKTRRSVRRFSDKPVEEEKLEKILEAARLAPSWANKQCWRFIVVTDKE---TLSELAKKESP-------SNGWLKDAP 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560 122 TVVFIANDP--SYDLSQI-----DCGLLGENMILSAWSMGIGSCCLGgptrfmtstpaaAEYLKK----LDIPEGYQLLY 190
Cdd:cd20608    72 VIIVVCADPkdSGWLNGQnyylvDAAIAMQNLMLAATDLGLGTCWIG------------AFDEKKvkeiLGIPENIRVVA 139

                  ....*.
gi 1681035560 191 CIAFGY 196
Cdd:cd20608   140 LTPLGY 145
nitroreductase cd02139
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
40-206 1.56e-23

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: 92.15  E-value: 1.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560  40 VIETIMSRRSIRQYKPQAVNRDTMQIILDCGINAPNGQNKQSWEVRVVDNPDFINGITEiykkenpkAAEDPKFknmFRN 119
Cdd:cd02139     1 VYEAIKKRRSIRKYKPTPVEEEKLLRILEAARLAPSAKNRQPWRFIVVKDKELKEKLAE--------AANGQKF---IAE 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560 120 AS-TVVFIANDPSY------DLSQIDCGLLGENMILSAWSMGIGSCCLGgptrfmtstpaaA---EYLKK-LDIPEGYQL 188
Cdd:cd02139    70 APvVIVACADPSESgmgcgkPYYLVDVAIAMEHLVLAATEEGLGTCWIG------------AfdeDKVKEiLGIPEEYRV 137
                         170
                  ....*....|....*...
gi 1681035560 189 LYCIAFGYPDETPAAKPR 206
Cdd:cd02139   138 VALTPLGYPAEEPPPRPR 155
nitroreductase cd20610
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
44-196 5.48e-22

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: 88.10  E-value: 5.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560  44 IMSRRSIRQYKPQAVNRDTMQIILDCGINAPNGQNKQSWEVRVVDNPDFINGITEIYKK---------ENPKAAEDPKFK 114
Cdd:cd20610     1 IKKRRSIRKFKPDPVPKEDIEKILEAANWAPSGMNRQNWEFVVVKGGEKIEKIGISIKKkneeiarllEKVFAEKPIRFR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560 115 NMFRNAST------VVFI----ANDPSYDLSQID-CGLLGENMILSAWSMGIGSCclggptrFMTSTPAAAEYLKK-LDI 182
Cdd:cd20610    81 KFRRFFTLfggapvLVVVytepYKPPEERKPDLQsVSAAIQNLLLAAHALGLGTC-------WMTGPLYAEDEIEEiLEI 153
                         170
                  ....*....|....
gi 1681035560 183 PEGYQLLYCIAFGY 196
Cdd:cd20610   154 PDDKELVAVTPLGY 167
nitroreductase cd20609
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
39-196 1.87e-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: 380330 [Multi-domain]  Cd Length: 145  Bit Score: 83.59  E-value: 1.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560  39 TVIETIMSRRSIRQYKPQAVNRDTMQIILDCGINAPNGQNKQSWEVRVVDNPDFINGITEIYkkenpkaaedpkfkNMFR 118
Cdd:cd20609     1 DFLELAKKRYSVRKFSDKPVEKEKLDKILEAGRLAPTAVNYQPQRILVVRSEEALEKLAKAT--------------PRFF 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560 119 NASTVVFIANDPS---------YDLSQIDCGLLGENMILSAWSMGIGSCCLGGptrFmtsTPAAAEylKKLDIPEGYQLL 189
Cdd:cd20609    67 GAPLVIVVCYDKDeswkrpydgKDSGDIDAAIVATHMMLAATELGLGTCWVGN---F---DPEKVR--EAFNLPENLEPV 138

                  ....*..
gi 1681035560 190 YCIAFGY 196
Cdd:cd20609   139 AILPLGY 145
NfsA-like cd02146
nitroreductase similar to Escherichia coli NfsA; This family contains NADPH-dependent flavin ...
40-206 4.52e-19

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: 81.90  E-value: 4.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560  40 VIETIMSRRSIRQYKPQAVNRDTMQIILDCGINAPNGQNKQSWEVRVVDNPDFINGITEI-----YKKENP--------- 105
Cdd:cd02146     1 TIETILNHRSVRKFTDEPLTDETLETLIAAAQSASTSSNLQAYSVIVVTDPELREKLAELagnqpYVAQAPvflvfcadl 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560 106 ----KAAEDpkfknmfrnASTVVFIANDP-SYDLSQIDCGLLGENMILSAWSMGIGSCCLGGPTRfmtstpAAAEYLKKL 180
Cdd:cd02146    81 yrhqKIAEE---------AGGKDVGLDYLeSFLVGVVDAALAAQNALVAAESLGLGIVYIGGIRN------NPEEVIELL 145
                         170       180
                  ....*....|....*....|....*.
gi 1681035560 181 DIPEGYQLLYCIAFGYPDETPAAKPR 206
Cdd:cd02146   146 GLPEYVFPLFGLTVGHPDPTPEVKPR 171
MhqN-like cd02137
nitroreductase family protein similar to the NAD(P)H nitroreductase MhqN; A diverse subfamily ...
42-206 1.35e-17

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: 76.12  E-value: 1.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560  42 ETIMSRRSIRQYKPQA-VNRDTMQIILDCGINAPNGQNKQSWEVRVVDNPDfingiteiyKKEN--PKAAEDPKFKnmfr 118
Cdd:cd02137     2 EVIKSRRSVRNFDPDHkIPKEELKEILELATLAPSSFNLQPWRFVVVRDPE---------LKAKlaEAAYNQPQVT---- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560 119 NASTVVFIANDpsydlsqIDCGLLGENMILSAWSMGIGSCCLGGPtrfmtSTPAAAEYLKkldIPEGYQLLYCIAFGYPD 198
Cdd:cd02137    69 TASAVILVLGD-------LNAGLAAMNLMLAAKAKGYDTCPMGGF-----DKEKVAELLN---LPDRYVPVLLIAIGKAA 133

                  ....*...
gi 1681035560 199 ETPAAKPR 206
Cdd:cd02137   134 DKAPRSGR 141
YdjA-like cd02135
nitroreductase family protein similar to Escherichia coli YdjA; A subfamily of the ...
41-196 5.56e-15

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: 69.55  E-value: 5.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560  41 IETIMSRRSIRQYK-PQAVNRDTMQIILDCGINAPNGQNKQSWEVRVVDNP---DFINGITEIYKKENPKAAED--PKFK 114
Cdd:cd02135     1 LELIKTRRSIRKFKlTGAPPEEQLEELLEAAMWAPNHGKLEPWRFIVVTGEgreRLAELLAAAAAARAPGADPEklEKAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560 115 NMFRNASTVVFI--ANDPSYDLSQID----CGLLGENMILSAWSMGIGSCCLggpTRFMTSTPAAAEylkKLDIPEGYQL 188
Cdd:cd02135    81 EKALRAPVVIAVvaKPDEDPKVPEWEqyaaVGAAVQNLLLAAHALGLGAVWR---TGPVTYDPAVRE---ALGLPEDERI 154

                  ....*...
gi 1681035560 189 LYCIAFGY 196
Cdd:cd02135   155 VGFLYLGT 162
PRK10765 PRK10765
oxygen-insensitive NADPH nitroreductase;
38-211 2.51e-11

oxygen-insensitive NADPH nitroreductase;


Pssm-ID: 182710  Cd Length: 240  Bit Score: 61.14  E-value: 2.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560  38 NTVIETIMSRRSIRQYKPQAVNRDTMQIILDCGINAPNGQNKQ-SWEVRVVDnPDFINGITEiYKKENPKAAEDPKFknm 116
Cdd:PRK10765    2 TPTIELILSHRSIRHFTDEPISEAQREAIINAARAASSSSFLQcSSIIRITD-KALREALVE-LTGGQKYVAQAAEF--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560 117 frnastVVFIAN---------DPSYDLSQ------IDCGLLGENMILSAWSMGIGSCCLGGptrfMTSTPAAAEYLkkLD 181
Cdd:PRK10765   77 ------WVFCADfnrhlqicpDAQLGLAEqlligaVDTAIMAQNALLAAESLGLGGVYIGG----LRNNIEAVTEL--LK 144
                         170       180       190
                  ....*....|....*....|....*....|
gi 1681035560 182 IPEGYQLLYCIAFGYPDETPAAKPRNAAKV 211
Cdd:PRK10765  145 LPQHVLPLFGLCLGWPAQNPDLKPRLPASL 174
TM1586_NiRdase pfam14512
Putative TM nitroreductase; Compared with the more traditional NADH oxidase/flavin reductase ...
39-210 6.22e-11

Putative TM nitroreductase; Compared with the more traditional NADH oxidase/flavin reductase family, this family is a duplication, consisting of two similar domains arranged as the subunits of the dimeric NADH oxidase/flavin reductase with one conserved active site.


Pssm-ID: 405236 [Multi-domain]  Cd Length: 214  Bit Score: 59.61  E-value: 6.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560  39 TVIETIMSRRSIRQYKPQAVNRDTMQIILD--CGINAPNGQNKQSwevrVVDNPDfingiteiykkenpkaAEDPKFKN- 115
Cdd:pfam14512   1 NLYEAIFKRHSVRKYTDEPIPEELLEELKNaiDEINKLSGLNIQL----VIDDPD----------------AFKGKAKYg 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560 116 MFRNA-STVVFIANDpsYDLSQIDCGLLGENMILSAWSMGIGSCCLGGPtrfmtstpaaaeYLK---KLDIPEGYQLLYC 191
Cdd:pfam14512  61 KFKGVpNYIAAYGEK--DDDLLENAGYYGEQIVLYATALGLGTCWVGGT------------YSKskvKAKIKKGEKLVIV 126
                         170
                  ....*....|....*....
gi 1681035560 192 IAFGYPDETPAAKPRNAAK 210
Cdd:pfam14512 127 IAFGYGATKGVRAKRKPLD 145
NfsB-like cd02149
nitroreductase similar to Escherichia coli NfsB; NAD(P)H:FMN oxidoreductase family. This ...
39-206 1.36e-10

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: 57.65  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560  39 TVIETIMSRRSIRQYKPQA-VNRDTMQIILDCGINAPNGQNKQSWEVRVVDNPDFingiteiyKKENPKAAedPKFKNMF 117
Cdd:cd02149     1 NILELLNFRYATKKFDPNKkISDEDLETILEALRLSPSSFGLEPWKFLVVENPEL--------KAKLAPAA--WFNQPQI 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560 118 RNASTVVFIANDPSYDLSQ--IDCGllgeNMILSAWSMGIGSCCLGGptrFmtstpAAAEYLKKLDIPE-GYQLLYCIAF 194
Cdd:cd02149    71 KDASHVVVFLAKKDWSAKQtyIALG----NMLLAAAMLGIDSCPIEG---F-----DPAKLDEILGLDEkGYKISVMVAF 138
                         170
                  ....*....|..
gi 1681035560 195 GYPDETPAAKPR 206
Cdd:cd02149   139 GYRSEEKLPKSR 150
nitroreductase cd03370
uncharacterized nitroreductase family proteins; Nitroreductase family containing Thermus ...
40-91 1.79e-08

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: 52.32  E-value: 1.79e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1681035560  40 VIETIMSRRSIRQYKPQAVNRDTMQIILDCGINAPNGQNKQSWEVRVVDNPD 91
Cdd:cd03370     1 VKEAIESRRSIRKYTQEPVPDEDLREILRLAGLAPSAWNIQPWRFVVVRDAE 52
TdsD-like cd02138
nitroreductase similar to Burkholderia pseudomallei TdsD; A subfamily of the nitroreductase ...
44-199 1.12e-07

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: 49.85  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560  44 IMSRRSIRQYKPQAVNRDTMQIILDCGINAPNGQNKQSWEVRVVDNPDfingitEIYKK-------ENPKAAedpkfknm 116
Cdd:cd02138     2 IAERWSPRAFSPEPISEEDLLSLFEAARWAPSCFNEQPWRFVVARRDT------EAFEKlldllaeGNQSWA-------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560 117 fRNASTVVFIANDPSYDLS-------QIDCGLLGENMILSAWSMGIGSCCLGGptrFmtsTPAAAEylKKLDIPEGYQLL 189
Cdd:cd02138    68 -KNAPVLIVVLAKTEFDHNgkpnryaLFDTGAAVANLALQATALGLVVHQMAG---F---DPEKAK--EALGIPDEYEPI 138
                         170
                  ....*....|
gi 1681035560 190 YCIAFGYPDE 199
Cdd:cd02138   139 TMIAIGYPGD 148
iodotyrosine_dehalogenase cd02144
iodotyrosine dehalogenase; Iodotyrosine dehalogenase catalyzes the removal of iodine from the ...
40-199 6.97e-07

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: 47.92  E-value: 6.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560  40 VIETIMSRRSIRQYKPQAVNRDTMQIILDCGINAPNGQNKQSWEVRVVDNPDFINGITEI--------YKKENPK-AAED 110
Cdd:cd02144     1 FYELMKKRRSVRDFSSEPVPREVIENAIRTAGTAPSGANTQPWTFVVVSDPEIKRKIREAaeeeekefYEKRMGEeWVWD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560 111 PKFKNMfrNAS----------TVVFiandpSYDLSQIDCGLLGENM--ILSAW-SMGI--------GSCCLggptrfmTS 169
Cdd:cd02144    81 LKPLGT--NWEkpylteapylIVVF-----KQKYGVLPDGKKKKHYynEESVGiAVGIllaalhnaGLVTL-------TH 146
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1681035560 170 TPAAAEYLKK-LDIPEGYQLLYCIAFGYPDE 199
Cdd:cd02144   147 TPSPMPFLRDlLGRPKNEKPLLLLPVGYPAE 177
PRK14851 PRK14851
hypothetical protein; Provisional
40-155 1.08e-03

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 39.46  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560  40 VIETIMSRRSIRQY-----KPQAVNRDT------MQIILDCGINAPNGQNKQSWEVRVVDNpdfingitEIYKKENPKAa 108
Cdd:PRK14851  294 YVQNVLIRNTDQARvrepePPVSVAHFDslpqgvGDYILQAGIQAPSGDNVQPWQFALAGN--------DIHLYLDPEA- 364
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1681035560 109 eDPKFKNMFRNASTvvfiandpsydlsqIDCGLLGENMILSAWSMGI 155
Cdd:PRK14851  365 -DVSFFNVRQTASI--------------ISCGAVMENMRIAATTFGL 396
McbC_SagB-like_oxidoreductase cd02142
oxidase similar to the microcin B17 processing protein McbC; This family is the oxidase domain ...
33-162 2.84e-03

oxidase similar to the microcin B17 processing protein McbC; This family is the oxidase domain of NRPS (non-ribosomal peptide synthetase) and other systems that modify polypeptides by cyclizing a thioester to form a ring. These include EpoB, part of the epothilone biosynthesis pathway; TubD, part of the tubulysin biosynthesis pathway, MtsD, part of the myxothiozol biosynthesis pathway; IndC, part of the indigoidine biosynthesis pathway and TfxB, part of the trifitoxin processing pathway. All are FMN-dependent and oxidize the product of the cyclization of thioesters in short polypeptides.


Pssm-ID: 380318  Cd Length: 200  Bit Score: 37.40  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560  33 NESKENTVIETIMSRRSIRQYKPQAVNRDTMQIILDCGIN--------APNGQNKQSWEVRVVDNPdfINGITE-IYK-- 101
Cdd:cd02142    13 ALLATLDLSEALLNRRSRRTFSSEPLTLRELSRLAARGIPgsgyglrpYPSAGALYPIEVYVIVKN--VEGLPAgIYHyd 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035560 102 -KEN-----------PKAAEDPKFKNMFRNAS-TVVFIAN---------DPSYDLSQIDCGLLGENMILSAWSMGIGSCC 159
Cdd:cd02142    91 pKRHrlvliregdfrLDLAHAAGNQAAFGSAAfSLIIVARferiawkygERAYRYILLEAGHLAQNLYLAATALGLGLCA 170

                  ...
gi 1681035560 160 LGG 162
Cdd:cd02142   171 IGA 173
 
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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