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Conserved domains on  [gi|490283031|ref|WP_004178896|]
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MULTISPECIES: oxygen-insensitive NAD(P)H nitroreductase [Klebsiella]

Protein Classification

NAD(P)H-dependent oxidoreductase( domain architecture ID 10793524)

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
PRK11053 PRK11053
oxygen-insensitive NAD(P)H nitroreductase;
1-217 1.97e-152

oxygen-insensitive NAD(P)H nitroreductase;


:

Pssm-ID: 182929 [Multi-domain]  Cd Length: 217  Bit Score: 421.30  E-value: 1.97e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031   1 MDIVSVALKRYSTKAFDATKKLTAGEAEQLKTLLQYSPSSTNSQPWHFIVASTDEGKARVAKAASGTYVFNERKILDASH 80
Cdd:PRK11053   1 MDIVSVAKKRYTTKAFDPSKKLPAEQIEQIKTLLRFSPSSVNSQPWHFIVASTEEGKARIAKAAAGNYAFNERKILDASH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031  81 VVVFCAKTAMDDAWLQRVVDQEEADGRFATPDAKAANHKGRTFFADMHRKELKDDDQWMAKQVYLNVGNFLLGVAAMGLD 160
Cdd:PRK11053  81 VVVFCAKTDMDDAYLELVLEQEDADGRFATEEAKAAQDKGRRFFADMHRKELKDLQHWMEKQVYLALGNLLLGAAALGID 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490283031 161 AVPIEGVDFAILDEEFDLKAQGYTSLVVVPVGHHSVEDFNATLPKSRLPQSTTITEI 217
Cdd:PRK11053 161 ATPIEGFDAAILDAEFGLREKGLTSSVVVPLGYHSEEDFNAKLPKSRLPQETIFTEI 217
 
Name Accession Description Interval E-value
PRK11053 PRK11053
oxygen-insensitive NAD(P)H nitroreductase;
1-217 1.97e-152

oxygen-insensitive NAD(P)H nitroreductase;


Pssm-ID: 182929 [Multi-domain]  Cd Length: 217  Bit Score: 421.30  E-value: 1.97e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031   1 MDIVSVALKRYSTKAFDATKKLTAGEAEQLKTLLQYSPSSTNSQPWHFIVASTDEGKARVAKAASGTYVFNERKILDASH 80
Cdd:PRK11053   1 MDIVSVAKKRYTTKAFDPSKKLPAEQIEQIKTLLRFSPSSVNSQPWHFIVASTEEGKARIAKAAAGNYAFNERKILDASH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031  81 VVVFCAKTAMDDAWLQRVVDQEEADGRFATPDAKAANHKGRTFFADMHRKELKDDDQWMAKQVYLNVGNFLLGVAAMGLD 160
Cdd:PRK11053  81 VVVFCAKTDMDDAYLELVLEQEDADGRFATEEAKAAQDKGRRFFADMHRKELKDLQHWMEKQVYLALGNLLLGAAALGID 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490283031 161 AVPIEGVDFAILDEEFDLKAQGYTSLVVVPVGHHSVEDFNATLPKSRLPQSTTITEI 217
Cdd:PRK11053 161 ATPIEGFDAAILDAEFGLREKGLTSSVVVPLGYHSEEDFNAKLPKSRLPQETIFTEI 217
NfsB-like cd02149
nitroreductase similar to Escherichia coli NfsB; NAD(P)H:FMN oxidoreductase family. This ...
 2-211 2.55e-59

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: 183.61  E-value: 2.55e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031   2 DIVSVALKRYSTKAFDATKKLTAGEAEQLKTLLQYSPSSTNSQPWHFIVASTDEGKARVAKAASgtyvFNERKILDASHV 81
Cdd:cd02149    1 NILELLNFRYATKKFDPNKKISDEDLETILEALRLSPSSFGLEPWKFLVVENPELKAKLAPAAW----FNQPQIKDASHV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031  82 VVFCAKTAmddawlqrvvdqeeadgrfatpdakaanhkgrtffadmhrkelkdddqWMAKQVYLNVGNFLLGVAAMGLDA 161
Cdd:cd02149   77 VVFLAKKD------------------------------------------------WSAKQTYIALGNMLLAAAMLGIDS 108

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 490283031 162 VPIEGVDFAILDEEFDLKAQGYTSLVVVPVGHHSVEdfnaTLPKSRLPQS 211
Cdd:cd02149  109 CPIEGFDPAKLDEILGLDEKGYKISVMVAFGYRSEE----KLPKSRKPLE 154
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
 8-209 3.06e-31

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


Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 111.87  E-value: 3.06e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031   8 LKRYSTKAFDaTKKLTAGEAEQLKTLLQYSPSSTNSQPWHFIVASTDEGKARVAKAASGTyvfNERKILDASHVVVFCAK 87
Cdd:COG0778    6 LTRRSVRKFT-DKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEALAEA---NQEWVADAPVLIVVCAD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031  88 TAMDDawlqrvvdqeeadgrfatpdakaanhkgrtffadmhrkelKDDDQWMAKQVYLNVGNFLLGVAAMGLDAVPIEGV 167
Cdd:COG0778   82 PDRSE----------------------------------------KVPERYALLDAGIAAQNLLLAARALGLGTCWIGGF 121

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 490283031 168 DFAILDEEFDLKAqGYTSLVVVPVGHHSVEDFnatlPKSRLP 209
Cdd:COG0778  122 DPEKVRELLGLPE-GEEPVALLALGYPAEELN----PRPRKP 158
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
 7-193 5.38e-25

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: 95.92  E-value: 5.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031    7 ALKRYSTKAFDAtKKLTAgeaEQLKTLL---QYSPSSTNSQPWHFIVASTDEGKARVAKAASGTYVFNERKILDASHVV- 82
Cdd:pfam00881   1 IRQRRSVRKFDP-EPVPK---EVLEEILeaaRRAPSAGNLQPWRFYVVTDGELRYRLAEAALELLLVEPAAALLLLLRRd 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031   83 ---VFCAKTAMDDAWLQRVVDqeeadgrfatpdakaanhkgrTFFADMHRKELKDDDQWMAKQVYLNVGNFLLGVAAMGL 159
Cdd:pfam00881  77 anlKLLLQDFLRGAPVLIVIT---------------------ASLSTYLRKAAERAYREALLDAGAAAQNLLLAATSLGL 135

                         170       180       190
                  ....*....|....*....|....*....|....
gi 490283031  160 DAVPIEGVDFAILDEEFDLkAQGYTSLVVVPVGH 193
Cdd:pfam00881 136 GSCPIGGFDAAAVRELLGL-PDDERLVGLIAVGY 168
 
Name Accession Description Interval E-value
PRK11053 PRK11053
oxygen-insensitive NAD(P)H nitroreductase;
1-217 1.97e-152

oxygen-insensitive NAD(P)H nitroreductase;


Pssm-ID: 182929 [Multi-domain]  Cd Length: 217  Bit Score: 421.30  E-value: 1.97e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031   1 MDIVSVALKRYSTKAFDATKKLTAGEAEQLKTLLQYSPSSTNSQPWHFIVASTDEGKARVAKAASGTYVFNERKILDASH 80
Cdd:PRK11053   1 MDIVSVAKKRYTTKAFDPSKKLPAEQIEQIKTLLRFSPSSVNSQPWHFIVASTEEGKARIAKAAAGNYAFNERKILDASH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031  81 VVVFCAKTAMDDAWLQRVVDQEEADGRFATPDAKAANHKGRTFFADMHRKELKDDDQWMAKQVYLNVGNFLLGVAAMGLD 160
Cdd:PRK11053  81 VVVFCAKTDMDDAYLELVLEQEDADGRFATEEAKAAQDKGRRFFADMHRKELKDLQHWMEKQVYLALGNLLLGAAALGID 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490283031 161 AVPIEGVDFAILDEEFDLKAQGYTSLVVVPVGHHSVEDFNATLPKSRLPQSTTITEI 217
Cdd:PRK11053 161 ATPIEGFDAAILDAEFGLREKGLTSSVVVPLGYHSEEDFNAKLPKSRLPQETIFTEI 217
NfsB-like cd02149
nitroreductase similar to Escherichia coli NfsB; NAD(P)H:FMN oxidoreductase family. This ...
 2-211 2.55e-59

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: 183.61  E-value: 2.55e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031   2 DIVSVALKRYSTKAFDATKKLTAGEAEQLKTLLQYSPSSTNSQPWHFIVASTDEGKARVAKAASgtyvFNERKILDASHV 81
Cdd:cd02149    1 NILELLNFRYATKKFDPNKKISDEDLETILEALRLSPSSFGLEPWKFLVVENPELKAKLAPAAW----FNQPQIKDASHV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031  82 VVFCAKTAmddawlqrvvdqeeadgrfatpdakaanhkgrtffadmhrkelkdddqWMAKQVYLNVGNFLLGVAAMGLDA 161
Cdd:cd02149   77 VVFLAKKD------------------------------------------------WSAKQTYIALGNMLLAAAMLGIDS 108

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 490283031 162 VPIEGVDFAILDEEFDLKAQGYTSLVVVPVGHHSVEdfnaTLPKSRLPQS 211
Cdd:cd02149  109 CPIEGFDPAKLDEILGLDEKGYKISVMVAFGYRSEE----KLPKSRKPLE 154
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
 8-209 3.06e-31

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


Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 111.87  E-value: 3.06e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031   8 LKRYSTKAFDaTKKLTAGEAEQLKTLLQYSPSSTNSQPWHFIVASTDEGKARVAKAASGTyvfNERKILDASHVVVFCAK 87
Cdd:COG0778    6 LTRRSVRKFT-DKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEALAEA---NQEWVADAPVLIVVCAD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031  88 TAMDDawlqrvvdqeeadgrfatpdakaanhkgrtffadmhrkelKDDDQWMAKQVYLNVGNFLLGVAAMGLDAVPIEGV 167
Cdd:COG0778   82 PDRSE----------------------------------------KVPERYALLDAGIAAQNLLLAARALGLGTCWIGGF 121

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 490283031 168 DFAILDEEFDLKAqGYTSLVVVPVGHHSVEDFnatlPKSRLP 209
Cdd:COG0778  122 DPEKVRELLGLPE-GEEPVALLALGYPAEELN----PRPRKP 158
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
 7-193 5.38e-25

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: 95.92  E-value: 5.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031    7 ALKRYSTKAFDAtKKLTAgeaEQLKTLL---QYSPSSTNSQPWHFIVASTDEGKARVAKAASGTYVFNERKILDASHVV- 82
Cdd:pfam00881   1 IRQRRSVRKFDP-EPVPK---EVLEEILeaaRRAPSAGNLQPWRFYVVTDGELRYRLAEAALELLLVEPAAALLLLLRRd 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031   83 ---VFCAKTAMDDAWLQRVVDqeeadgrfatpdakaanhkgrTFFADMHRKELKDDDQWMAKQVYLNVGNFLLGVAAMGL 159
Cdd:pfam00881  77 anlKLLLQDFLRGAPVLIVIT---------------------ASLSTYLRKAAERAYREALLDAGAAAQNLLLAATSLGL 135

                         170       180       190
                  ....*....|....*....|....*....|....
gi 490283031  160 DAVPIEGVDFAILDEEFDLkAQGYTSLVVVPVGH 193
Cdd:pfam00881 136 GSCPIGGFDAAAVRELLGL-PDDERLVGLIAVGY 168
Nitro_FMN_reductase cd02062
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 8-193 3.70e-19

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: 80.03  E-value: 3.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031   8 LKRYSTKAFDAtKKLtagEAEQLKTLL---QYSPSSTNSQPWHFIVASTDEGKARVAKAASGtyvfNERKILDASHVVVF 84
Cdd:cd02062    2 KTRRSIRKFTD-KPV---PEEKLRKILeaaRLAPSAGNLQPWRFIVVRDREKKEKLAKLAAP----NQKFIAGAPVVIVV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031  85 CAKTamddawlqrvvdqeeadgrfatpdakaanhkgrtffadmhrkelKDDDQWMAKQVYLNVGNFLLGVAAMGLDAVPI 164
Cdd:cd02062   74 VADP--------------------------------------------DKSRPWALEDAGAAAQNLLLAAAALGLGSCWI 109

                        170       180       190
                 ....*....|....*....|....*....|.
gi 490283031 165 EGVDF--AILDEEFDLKaQGYTSLVVVPVGH 193
Cdd:cd02062  110 GGFDFreDKVRELLGIP-ENLRPVALIAIGY 139
MhqN-like cd02137
nitroreductase family protein similar to the NAD(P)H nitroreductase MhqN; A diverse subfamily ...
 9-212 4.98e-18

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: 77.28  E-value: 4.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031   9 KRYSTKAFDATKKLTAGEAEQLKTLLQYSPSSTNSQPWHFIVASTDEGKARVAKAAsgtyvFNERKILDASHVVVFCAkt 88
Cdd:cd02137    6 SRRSVRNFDPDHKIPKEELKEILELATLAPSSFNLQPWRFVVVRDPELKAKLAEAA-----YNQPQVTTASAVILVLG-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031  89 amddawlqrvvdqeeadgrfatpdakaanhkgrtffadmhrkelkDDDQWMAKQvylnvgNFLLGVAAMGLDAVPIEGVD 168
Cdd:cd02137   79 ---------------------------------------------DLNAGLAAM------NLMLAAKAKGYDTCPMGGFD 107

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 490283031 169 FAILDEEFDLKAQgYTSLVVVPVGHHSVEDfnatLPKSRLPQST 212
Cdd:cd02137  108 KEKVAELLNLPDR-YVPVLLIAIGKAADKA----PRSGRLPVDE 146
PRK05365 PRK05365
malonic semialdehyde reductase; Provisional
 28-193 3.99e-12

malonic semialdehyde reductase; Provisional


Pssm-ID: 180040 [Multi-domain]  Cd Length: 195  Bit Score: 62.52  E-value: 3.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031  28 EQLKT---LLQYSPSSTNSQPWHFIVASTDEGKARVAKAASGTyvfNERKILDASHVVVFcaktAMDDAW---LQRVVDQ 101
Cdd:PRK05365  30 EQLRElydLVKWGPTSANCSPARFVFVRSAEAKERLRPALSEG---NLAKTLAAPVTAIV----AYDTEFhehLPKLFPH 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031 102 EEADGRFATPDAKAAnhkgRTFFADMHrkelkdddqwmakqvyLNVGNFLLGVAAMGLDAVPIEGVDFAILDEEFdLKAQ 181
Cdd:PRK05365 103 ADARSWFAGNPALAE----ETAFRNSS----------------LQGAYLILAARALGLDAGPMSGFDAAAVDAEF-FAGT 161

                        170
                 ....*....|..
gi 490283031 182 GYTSLVVVPVGH 193
Cdd:PRK05365 162 TWKSNFLVNIGY 173
nitroreductase cd20609
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 6-94 2.52e-10

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: 56.63  E-value: 2.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031   6 VALKRYSTKAFDATKKltagEAEQLKTLL---QYSPSSTNSQPWHFIVASTDEGKARVAKAASGTYvfnerkilDASHVV 82
Cdd:cd20609    5 LAKKRYSVRKFSDKPV----EKEKLDKILeagRLAPTAVNYQPQRILVVRSEEALEKLAKATPRFF--------GAPLVI 72

                         90
                 ....*....|..
gi 490283031  83 VFCAKTamDDAW 94
Cdd:cd20609   73 VVCYDK--DESW 82
nitroreductase cd02139
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 9-86 9.21e-10

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: 55.55  E-value: 9.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031   9 KRYSTKAFdatkKLTAGEAEQLKTLL---QYSPSSTNSQPWHFIVASTDEGKARVAKAASGtyvfnERKILDASHVVVFC 85
Cdd:cd02139    7 KRRSIRKY----KPTPVEEEKLLRILeaaRLAPSAKNRQPWRFIVVKDKELKEKLAEAANG-----QKFIAEAPVVIVAC 77


                 .
gi 490283031  86 A 86
Cdd:cd02139   78 A 78
TdsD-like cd02138
nitroreductase similar to Burkholderia pseudomallei TdsD; A subfamily of the nitroreductase ...
 8-198 1.05e-08

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: 52.55  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031   8 LKRYSTKAFDATKKltagEAEQLKTLL---QYSPSSTNSQPWHFIVAST-DEGKARVAKAASGtyvFNERKILDASHVVV 83
Cdd:cd02138    3 AERWSPRAFSPEPI----SEEDLLSLFeaaRWAPSCFNEQPWRFVVARRdTEAFEKLLDLLAE---GNQSWAKNAPVLIV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031  84 FCAKTAMDDAwlqrvvdqeEADGRFATPDAKAAnhkgrtffadmhrkelkdddqwmakqvylnVGNFLLGVAAMGLDAVP 163
Cdd:cd02138   76 VLAKTEFDHN---------GKPNRYALFDTGAA------------------------------VANLALQATALGLVVHQ 116

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 490283031 164 IEGVDFAILDEEFDLkAQGYTSLVVVPVGHHSVED 198
Cdd:cd02138  117 MAGFDPEKAKEALGI-PDEYEPITMIAIGYPGDPE 150
RutE-like cd02148
nitroreductase similar to Escherichia coli RutE; A subfamily of the nitroreductase family ...
 20-193 3.64e-08

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: 51.49  E-value: 3.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031  20 KKLTAGEAEQLKTLLQYSPSSTNSQPWHFIVASTDEGKARVAKAASGtyvFNERKILDASHVVVFCAKTAMDDaWLQRVV 99
Cdd:cd02148   18 KPVSDEELRAIYDLAKWGPTAANCSPARIVFVRSAEAKERLVPHLSE---GNREKTMAAPVTAILAYDTEFYE-HLPRLF 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031 100 DQEEADGRFATPDAKAANhkgrtffadmhrkelkdddqWMAKQ-VYLNVGNFLLGVAAMGLDAVPIEGVDFAILDEEFdL 178
Cdd:cd02148   94 PHGDARSWFFGSGPARAE--------------------ETAFRnASLQAAYFILAARALGLDCGPMSGFDAAGVDAEF-F 152

                        170
                 ....*....|....*
gi 490283031 179 KAQGYTSLVVVPVGH 193
Cdd:cd02148  153 AGTRWKSNLVVNLGY 167
nitroreductase cd02151
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 26-96 5.93e-08

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: 50.22  E-value: 5.93e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490283031  26 EAEQLKTLLQY---SPSSTNSQPWHFIVASTDEGKARVAKAASGTYVFnerkILDASHVVVFCAKTAMDDAWLQ 96
Cdd:cd02151   18 EEEKLEEILEAallAPSSRNSRPVEFIVVDDKETLKKLSECKPHGSAF----LKGAPAAIVVLADTEKSDTWIE 87
nitroreductase cd03370
uncharacterized nitroreductase family proteins; Nitroreductase family containing Thermus ...
 25-197 7.21e-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: 50.78  E-value: 7.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031  25 GEAEQLKTLLQYSPSSTNSQPWHFIVASTDEGKARVAKAAsgtyvFNERKILDASHVVVFCAKtaMDDAwLQRVVDQEEA 104
Cdd:cd03370   22 EDLREILRLAGLAPSAWNIQPWRFVVVRDAELKEQLQAAA-----YGQAQVTSAPAVIVIYSD--MEDA-LANLEETIHP 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031 105 DGrfaTPDAKAANHKG-RTFFADMHRKELKdddQWMAKQVYLNVGNFLLGVAAMGLDAVPIEGVDFAILDEEFDLKAQgY 183
Cdd:cd03370   94 GL---SEERRQREAAGlRGAFGKMSVEQRG---QWGLAQANIALGFLLLAAQSLGYDTSPMLGFDPEKVKALLGLPEH-V 166

                        170       180
                 ....*....|....*....|....
gi 490283031 184 TSLVVVPVGH----------HSVE 197
Cdd:cd03370  167 TIAALVALGKpaeegyphhrHSLE 190
nitroreductase cd20608
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 26-95 2.07e-07

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: 48.49  E-value: 2.07e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490283031  26 EAEQLKTLL---QYSPSSTNSQPWHFIVASTDEGKARVAKAASgtYVFNERKilDASHVVVFCAKTAmDDAWL 95
Cdd:cd20608   19 EEEKLEKILeaaRLAPSWANKQCWRFIVVTDKETLSELAKKES--PSNGWLK--DAPVIIVVCADPK-DSGWL 86
PnbA_NfnB-like cd02136
nitroreductase similar to Mycobacterium smegmatis NfnB; Members of this family utilize FMN as ...
 6-96 4.65e-07

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: 47.58  E-value: 4.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031   6 VALKRYSTKAFDaTKKLtagEAEQLKTLL---QYSPSSTNSQPWHFIVAsTDEGKARVAKAAsgtyvfnerkiLDASHVV 82
Cdd:cd02136    1 AIKSRRSVRAFK-DKPV---PKETIEKILeaaRRAPSGKNTQPWRVYVV-TGKARERLKKAF-----------FGAPVAL 64

                         90
                 ....*....|....
gi 490283031  83 VFCAKTAMDDAWLQ 96
Cdd:cd02136   65 FLTMDKVLGPWSWF 78
nitroreductase cd02150
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 26-193 1.11e-06

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: 46.83  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031  26 EAEQLKTLLQ---YSPSSTNSQPWHFIVASTDEGKARVAKAASGTyvfneRKILDASHVVVFCA---KTAMDDAWLQrvv 99
Cdd:cd02150   16 EEEDIEKLLRaamAAPSAGNQQPWHFIVVTDREKLDKIAEAHPYG-----KMLKEAPLAIVVCGdpsKEKAPGYWVQ--- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031 100 dqeeadgrfatpDAKAAnhkgrtffadmhrkelkdddqwmakqvylnVGNFLLGVAAMGLDAV-----PIEGvDFAILDE 174
Cdd:cd02150   88 ------------DCSAA------------------------------TENILLAAHALGLGAVwlgvyPFEE-RVKAIRE 124

                        170
                 ....*....|....*....
gi 490283031 175 EFDLKAQgYTSLVVVPVGH 193
Cdd:cd02150  125 ILNIPEN-IIPFCVIALGY 142
NfsA-like cd02146
nitroreductase similar to Escherichia coli NfsA; This family contains NADPH-dependent flavin ...
 8-86 5.15e-04

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: 39.91  E-value: 5.15e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490283031   8 LKRYSTKAFDAtKKLTAGEAEQLKTLLQYSPSSTNSQPWHFIVASTDEGKARVAKAAsgtyvFNERKILDASHVVVFCA 86
Cdd:cd02146    6 LNHRSVRKFTD-EPLTDETLETLIAAAQSASTSSNLQAYSVIVVTDPELREKLAELA-----GNQPYVAQAPVFLVFCA 78
YdjA-like cd02135
nitroreductase family protein similar to Escherichia coli YdjA; A subfamily of the ...
 8-162 8.50e-04

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: 38.74  E-value: 8.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031   8 LKRYSTKAFDATkklTAGEAEQLKTLLQ---YSPSSTNSQPWHFIVAsTDEGKAR-----VAKAASGTYVFNERKI---- 75
Cdd:cd02135    5 KTRRSIRKFKLT---GAPPEEQLEELLEaamWAPNHGKLEPWRFIVV-TGEGRERlaellAAAAAARAPGADPEKLekar 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490283031  76 ---LDASHVVVFCAKTAmddawlqrvvdqeeadgrfatpdakaanhkgrtffadmHRKELKDDDQWMAkqvylnVG---- 148
Cdd:cd02135   81 ekaLRAPVVIAVVAKPD--------------------------------------EDPKVPEWEQYAA------VGaavq 116

                        170
                 ....*....|....
gi 490283031 149 NFLLGVAAMGLDAV 162
Cdd:cd02135  117 NLLLAAHALGLGAV 130
iodotyrosine_dehalogenase cd02144
iodotyrosine dehalogenase; Iodotyrosine dehalogenase catalyzes the removal of iodine from the ...
 23-64 1.38e-03

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: 38.29  E-value: 1.38e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 490283031  23 TAGEAeqlktllqysPSSTNSQPWHFIVASTDEGKARVAKAA 64
Cdd:cd02144   30 TAGTA----------PSGANTQPWTFVVVSDPEIKRKIREAA 61
nitroreductase_FeS-like cd02143
nitroreductases with an N-terminal iron-sulfur cluster-binding domain; Members of this family ...
 26-94 3.62e-03

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: 37.07  E-value: 3.62e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490283031  26 EAEQLKTLLQ---YSPSSTNSQPWHFIVAstdEGKARVAKAASGTYVFNERKILDASHVVVFCAKTAMDDAW 94
Cdd:cd02143   17 PRETLEKLLDiarYAPTGHNSQPVHWLVV---DDPEKVRRLAELVIDWMRELIKEDPELAGKLFLDGIVAAW 85
 
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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