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Conserved domains on  [gi|446278033|ref|WP_000355888|]
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oxygen-insensitive NAD(P)H nitroreductase [Salmonella enterica]

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 1.82e-155

oxygen-insensitive NAD(P)H nitroreductase;


:

Pssm-ID: 182929 [Multi-domain]  Cd Length: 217  Bit Score: 429.01  E-value: 1.82e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033   1 MDIVSVALQRYSTKAFDPSKKLTAEEADKVKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYTFNERKMLDASH 80
Cdd:PRK11053   1 MDIVSVAKKRYTTKAFDPSKKLPAEQIEQIKTLLRFSPSSVNSQPWHFIVASTEEGKARIAKAAAGNYAFNERKILDASH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033  81 VVVFCAKTAMDDAWLERVVDQEDADGRFATPEAKAANDKGRRFFADMHRVSLKDDHQWMAKQVYLNVGNFLLGVAAMGLD 160
Cdd:PRK11053  81 VVVFCAKTDMDDAYLELVLEQEDADGRFATEEAKAAQDKGRRFFADMHRKELKDLQHWMEKQVYLALGNLLLGAAALGID 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446278033 161 AVPIEGFDAEVLDAEFGLKEKGYTSLVVVPVGHHSVEDFNAGLPKSRLPLETTLTEV 217
Cdd:PRK11053 161 ATPIEGFDAAILDAEFGLREKGLTSSVVVPLGYHSEEDFNAKLPKSRLPQETIFTEI 217
 
Name Accession Description Interval E-value
PRK11053 PRK11053
oxygen-insensitive NAD(P)H nitroreductase;
1-217 1.82e-155

oxygen-insensitive NAD(P)H nitroreductase;


Pssm-ID: 182929 [Multi-domain]  Cd Length: 217  Bit Score: 429.01  E-value: 1.82e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033   1 MDIVSVALQRYSTKAFDPSKKLTAEEADKVKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYTFNERKMLDASH 80
Cdd:PRK11053   1 MDIVSVAKKRYTTKAFDPSKKLPAEQIEQIKTLLRFSPSSVNSQPWHFIVASTEEGKARIAKAAAGNYAFNERKILDASH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033  81 VVVFCAKTAMDDAWLERVVDQEDADGRFATPEAKAANDKGRRFFADMHRVSLKDDHQWMAKQVYLNVGNFLLGVAAMGLD 160
Cdd:PRK11053  81 VVVFCAKTDMDDAYLELVLEQEDADGRFATEEAKAAQDKGRRFFADMHRKELKDLQHWMEKQVYLALGNLLLGAAALGID 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446278033 161 AVPIEGFDAEVLDAEFGLKEKGYTSLVVVPVGHHSVEDFNAGLPKSRLPLETTLTEV 217
Cdd:PRK11053 161 ATPIEGFDAAILDAEFGLREKGLTSSVVVPLGYHSEEDFNAKLPKSRLPQETIFTEI 217
NfsB-like cd02149
nitroreductase similar to Escherichia coli NfsB; NAD(P)H:FMN oxidoreductase family. This ...
 2-211 1.90e-62

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: 191.31  E-value: 1.90e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033   2 DIVSVALQRYSTKAFDPSKKLTAEEADKVKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAagnyTFNERKMLDASHV 81
Cdd:cd02149    1 NILELLNFRYATKKFDPNKKISDEDLETILEALRLSPSSFGLEPWKFLVVENPELKAKLAPAA----WFNQPQIKDASHV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033  82 VVFCAKTAmddawlervvdqedadgrfatpeakaandkgrrffadmhrvslkddhqWMAKQVYLNVGNFLLGVAAMGLDA 161
Cdd:cd02149   77 VVFLAKKD------------------------------------------------WSAKQTYIALGNMLLAAAMLGIDS 108

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446278033 162 VPIEGFDAEVLDAEFGLKEKGYTSLVVVPVGHHSVEDfnagLPKSRLPLE 211
Cdd:cd02149  109 CPIEGFDPAKLDEILGLDEKGYKISVMVAFGYRSEEK----LPKSRKPLE 154
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
 8-211 3.90e-35

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


Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 121.88  E-value: 3.90e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033   8 LQRYSTKAFDPsKKLTAEEADKVKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGnytFNERKMLDASHVVVFCAK 87
Cdd:COG0778    6 LTRRSVRKFTD-KPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEALAE---ANQEWVADAPVLIVVCAD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033  88 TAMDDawlervvdqedadgrfatpeakaandkgrrffadmhrvslKDDHQWMAKQVYLNVGNFLLGVAAMGLDAVPIEGF 167
Cdd:COG0778   82 PDRSE----------------------------------------KVPERYALLDAGIAAQNLLLAARALGLGTCWIGGF 121

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 446278033 168 DAEVLDAEFGLKEkGYTSLVVVPVGHHSVEDFnaglPKSRLPLE 211
Cdd:COG0778  122 DPEKVRELLGLPE-GEEPVALLALGYPAEELN----PRPRKPLE 160
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
 7-193 2.08e-27

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: 102.47  E-value: 2.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033    7 ALQRYSTKAFDPsKKLTAEEADKVKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYTFNERKMLDASHVV---- 82
Cdd:pfam00881   1 IRQRRSVRKFDP-EPVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLAEAALELLLVEPAAALLLLLRRdanl 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033   83 VFCAKTAMDDAWLERVVDqedadgrfatpeakaandkgrRFFADMHRVSLKDDHQWMAKQVYLNVGNFLLGVAAMGLDAV 162
Cdd:pfam00881  80 KLLLQDFLRGAPVLIVIT---------------------ASLSTYLRKAAERAYREALLDAGAAAQNLLLAATSLGLGSC 138

                         170       180       190
                  ....*....|....*....|....*....|.
gi 446278033  163 PIEGFDAEVLDAEFGLkEKGYTSLVVVPVGH 193
Cdd:pfam00881 139 PIGGFDAAAVRELLGL-PDDERLVGLIAVGY 168
 
Name Accession Description Interval E-value
PRK11053 PRK11053
oxygen-insensitive NAD(P)H nitroreductase;
1-217 1.82e-155

oxygen-insensitive NAD(P)H nitroreductase;


Pssm-ID: 182929 [Multi-domain]  Cd Length: 217  Bit Score: 429.01  E-value: 1.82e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033   1 MDIVSVALQRYSTKAFDPSKKLTAEEADKVKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYTFNERKMLDASH 80
Cdd:PRK11053   1 MDIVSVAKKRYTTKAFDPSKKLPAEQIEQIKTLLRFSPSSVNSQPWHFIVASTEEGKARIAKAAAGNYAFNERKILDASH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033  81 VVVFCAKTAMDDAWLERVVDQEDADGRFATPEAKAANDKGRRFFADMHRVSLKDDHQWMAKQVYLNVGNFLLGVAAMGLD 160
Cdd:PRK11053  81 VVVFCAKTDMDDAYLELVLEQEDADGRFATEEAKAAQDKGRRFFADMHRKELKDLQHWMEKQVYLALGNLLLGAAALGID 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446278033 161 AVPIEGFDAEVLDAEFGLKEKGYTSLVVVPVGHHSVEDFNAGLPKSRLPLETTLTEV 217
Cdd:PRK11053 161 ATPIEGFDAAILDAEFGLREKGLTSSVVVPLGYHSEEDFNAKLPKSRLPQETIFTEI 217
NfsB-like cd02149
nitroreductase similar to Escherichia coli NfsB; NAD(P)H:FMN oxidoreductase family. This ...
 2-211 1.90e-62

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: 191.31  E-value: 1.90e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033   2 DIVSVALQRYSTKAFDPSKKLTAEEADKVKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAagnyTFNERKMLDASHV 81
Cdd:cd02149    1 NILELLNFRYATKKFDPNKKISDEDLETILEALRLSPSSFGLEPWKFLVVENPELKAKLAPAA----WFNQPQIKDASHV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033  82 VVFCAKTAmddawlervvdqedadgrfatpeakaandkgrrffadmhrvslkddhqWMAKQVYLNVGNFLLGVAAMGLDA 161
Cdd:cd02149   77 VVFLAKKD------------------------------------------------WSAKQTYIALGNMLLAAAMLGIDS 108

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446278033 162 VPIEGFDAEVLDAEFGLKEKGYTSLVVVPVGHHSVEDfnagLPKSRLPLE 211
Cdd:cd02149  109 CPIEGFDPAKLDEILGLDEKGYKISVMVAFGYRSEEK----LPKSRKPLE 154
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
 8-211 3.90e-35

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


Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 121.88  E-value: 3.90e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033   8 LQRYSTKAFDPsKKLTAEEADKVKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGnytFNERKMLDASHVVVFCAK 87
Cdd:COG0778    6 LTRRSVRKFTD-KPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEALAE---ANQEWVADAPVLIVVCAD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033  88 TAMDDawlervvdqedadgrfatpeakaandkgrrffadmhrvslKDDHQWMAKQVYLNVGNFLLGVAAMGLDAVPIEGF 167
Cdd:COG0778   82 PDRSE----------------------------------------KVPERYALLDAGIAAQNLLLAARALGLGTCWIGGF 121

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 446278033 168 DAEVLDAEFGLKEkGYTSLVVVPVGHHSVEDFnaglPKSRLPLE 211
Cdd:COG0778  122 DPEKVRELLGLPE-GEEPVALLALGYPAEELN----PRPRKPLE 160
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
 7-193 2.08e-27

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: 102.47  E-value: 2.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033    7 ALQRYSTKAFDPsKKLTAEEADKVKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYTFNERKMLDASHVV---- 82
Cdd:pfam00881   1 IRQRRSVRKFDP-EPVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLAEAALELLLVEPAAALLLLLRRdanl 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033   83 VFCAKTAMDDAWLERVVDqedadgrfatpeakaandkgrRFFADMHRVSLKDDHQWMAKQVYLNVGNFLLGVAAMGLDAV 162
Cdd:pfam00881  80 KLLLQDFLRGAPVLIVIT---------------------ASLSTYLRKAAERAYREALLDAGAAAQNLLLAATSLGLGSC 138

                         170       180       190
                  ....*....|....*....|....*....|.
gi 446278033  163 PIEGFDAEVLDAEFGLkEKGYTSLVVVPVGH 193
Cdd:pfam00881 139 PIGGFDAAAVRELLGL-PDDERLVGLIAVGY 168
Nitro_FMN_reductase cd02062
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 8-193 5.14e-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: 380311 [Multi-domain]  Cd Length: 139  Bit Score: 87.35  E-value: 5.14e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033   8 LQRYSTKAFDPskklTAEEADKVKTLL---QYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYTFnerkMLDASHVVVF 84
Cdd:cd02062    2 KTRRSIRKFTD----KPVPEEKLRKILeaaRLAPSAGNLQPWRFIVVRDREKKEKLAKLAAPNQKF----IAGAPVVIVV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033  85 CAKTamddawlervvdqedadgrfatpeakaandkgrrffadmhrvslKDDHQWMAKQVYLNVGNFLLGVAAMGLDAVPI 164
Cdd:cd02062   74 VADP--------------------------------------------DKSRPWALEDAGAAAQNLLLAAAALGLGSCWI 109

                        170       180       190
                 ....*....|....*....|....*....|.
gi 446278033 165 EGFD--AEVLDAEFGLKEkGYTSLVVVPVGH 193
Cdd:cd02062  110 GGFDfrEDKVRELLGIPE-NLRPVALIAIGY 139
MhqN-like cd02137
nitroreductase family protein similar to the NAD(P)H nitroreductase MhqN; A diverse subfamily ...
 9-212 9.85e-21

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: 84.21  E-value: 9.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033   9 QRYSTKAFDPSKKLTAEEADKVKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAagnytFNERKMLDASHVVVFCAkt 88
Cdd:cd02137    6 SRRSVRNFDPDHKIPKEELKEILELATLAPSSFNLQPWRFVVVRDPELKAKLAEAA-----YNQPQVTTASAVILVLG-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033  89 amddawlervvdqedadgrfatpeakaanDKGRRFFAdmhrvslkddhqwmakqvylnvGNFLLGVAAMGLDAVPIEGFD 168
Cdd:cd02137   79 -----------------------------DLNAGLAA----------------------MNLMLAAKAKGYDTCPMGGFD 107

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 446278033 169 AEVLDAEFGLkEKGYTSLVVVPVGHHSVEdfnaGLPKSRLPLET 212
Cdd:cd02137  108 KEKVAELLNL-PDRYVPVLLIAIGKAADK----APRSGRLPVDE 146
nitroreductase cd03370
uncharacterized nitroreductase family proteins; Nitroreductase family containing Thermus ...
 38-211 2.03e-13

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: 65.80  E-value: 2.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033  38 PSSTNSQPWHFIVASTEEGKARVAKSAagnytFNERKMLDASHVVVFCAKtaMDDAwLERVVDqedadgrFATP----EA 113
Cdd:cd03370   35 PSAWNIQPWRFVVVRDAELKEQLQAAA-----YGQAQVTSAPAVIVIYSD--MEDA-LANLEE-------TIHPglseER 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033 114 KAANDKG-RRFFADMhrvSLKDDHQWMAKQVYLNVGNFLLGVAAMGLDAVPIEGFDAEVLDAEFGLKEKgYTSLVVVPVG 192
Cdd:cd03370  100 RQREAAGlRGAFGKM---SVEQRGQWGLAQANIALGFLLLAAQSLGYDTSPMLGFDPEKVKALLGLPEH-VTIAALVALG 175

                        170
                 ....*....|....*....
gi 446278033 193 HHSVEdfnaGLPKSRLPLE 211
Cdd:cd03370  176 KPAEE----GYPHHRHSLE 190
TdsD-like cd02138
nitroreductase similar to Burkholderia pseudomallei TdsD; A subfamily of the nitroreductase ...
 10-211 1.27e-12

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: 63.33  E-value: 1.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033  10 RYSTKAFDPsKKLTAEEadkVKTLL---QYSPSSTNSQPWHFIVASTE-EGKARVAKSAAGnytFNERKMLDASHVVVFC 85
Cdd:cd02138    5 RWSPRAFSP-EPISEED---LLSLFeaaRWAPSCFNEQPWRFVVARRDtEAFEKLLDLLAE---GNQSWAKNAPVLIVVL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033  86 AKTAMDDawlervvdqedadgrfatpeakaaNDKGRRFFadMHRVSlkddhqwMAkqvylnVGNFLLGVAAMGLDAVPIE 165
Cdd:cd02138   78 AKTEFDH------------------------NGKPNRYA--LFDTG-------AA------VANLALQATALGLVVHQMA 118

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446278033 166 GFDAEVLDAEFGLKEkGYTSLVVVPVGHHS-VEDFNAGL------PKSRLPLE 211
Cdd:cd02138  119 GFDPEKAKEALGIPD-EYEPITMIAIGYPGdPESLPEKLlereeaPRTRKPLS 170
RutE-like cd02148
nitroreductase similar to Escherichia coli RutE; A subfamily of the nitroreductase family ...
 12-193 1.19e-11

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: 61.12  E-value: 1.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033  12 STKAFDPsKKLTAEEADKVKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNytfNERKMLDASHVVVFCAKTAMD 91
Cdd:cd02148   11 THNAWED-KPVSDEELRAIYDLAKWGPTAANCSPARIVFVRSAEAKERLVPHLSEG---NREKTMAAPVTAILAYDTEFY 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033  92 DaWLERVVDQEDADGRFATPEAKAANDKGRRFFAdmhrvslkddhqwmakqvyLNVGNFLLGVAAMGLDAVPIEGFDAEV 171
Cdd:cd02148   87 E-HLPRLFPHGDARSWFFGSGPARAEETAFRNAS-------------------LQAAYFILAARALGLDCGPMSGFDAAG 146

                        170       180
                 ....*....|....*....|..
gi 446278033 172 LDAEFgLKEKGYTSLVVVPVGH 193
Cdd:cd02148  147 VDAEF-FAGTRWKSNLVVNLGY 167
PRK05365 PRK05365
malonic semialdehyde reductase; Provisional
 33-211 2.95e-11

malonic semialdehyde reductase; Provisional


Pssm-ID: 180040 [Multi-domain]  Cd Length: 195  Bit Score: 60.21  E-value: 2.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033  33 LLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNytfNERKMLDASHVVVFcaktAMDDAW---LERVVDQEDADGRFA 109
Cdd:PRK05365  38 LVKWGPTSANCSPARFVFVRSAEAKERLRPALSEG---NLAKTLAAPVTAIV----AYDTEFhehLPKLFPHADARSWFA 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033 110 TPEAKAAndkgrrffadmhrvslkddhqWMAKQ-VYLNVGNFLLGVAAMGLDAVPIEGFDAEVLDAEFgLKEKGYTSLVV 188
Cdd:PRK05365 111 GNPALAE---------------------ETAFRnSSLQGAYLILAARALGLDAGPMSGFDAAAVDAEF-FAGTTWKSNFL 168

                        170       180
                 ....*....|....*....|....
gi 446278033 189 VPVGHhsvEDFNAGLPKS-RLPLE 211
Cdd:PRK05365 169 VNIGY---GDPAKLFPRLpRLSFD 189
nitroreductase cd20609
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 6-193 8.39e-11

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: 57.78  E-value: 8.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033   6 VALQRYSTKAFDPsKKLtaeEADKVKTLL---QYSPSSTNSQPWHFIVASTEEGKARVAKSAagNYTFNerkmldASHVV 82
Cdd:cd20609    5 LAKKRYSVRKFSD-KPV---EKEKLDKILeagRLAPTAVNYQPQRILVVRSEEALEKLAKAT--PRFFG------APLVI 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033  83 VFCAKTamDDAWlERVVDQEDadgrfatpeakaandkgrrfFADMHrVSLKDDHqwMakqvylnvgnfLLGVAAMGLDAV 162
Cdd:cd20609   73 VVCYDK--DESW-KRPYDGKD--------------------SGDID-AAIVATH--M-----------MLAATELGLGTC 115

                        170       180       190
                 ....*....|....*....|....*....|.
gi 446278033 163 PIEGFDAEVLDAEFGLKEkGYTSLVVVPVGH 193
Cdd:cd20609  116 WVGNFDPEKVREAFNLPE-NLEPVAILPLGY 145
nitroreductase cd02139
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 10-86 1.54e-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.


Pssm-ID: 380316 [Multi-domain]  Cd Length: 165  Bit Score: 52.09  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033  10 RYSTKAFDPskklTAEEADKVKTLL---QYSPSSTNSQPWHFIVASTEEGKARVAKsAAGNYTFnerkMLDASHVVVFCA 86
Cdd:cd02139    8 RRSIRKYKP----TPVEEEKLLRILeaaRLAPSAKNRQPWRFIVVKDKELKEKLAE-AANGQKF----IAEAPVVIVACA 78
PnbA_NfnB-like cd02136
nitroreductase similar to Mycobacterium smegmatis NfnB; Members of this family utilize FMN as ...
 6-96 2.98e-08

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: 51.05  E-value: 2.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033   6 VALQRYSTKAFDPsKKLTAEEADKVKTLLQYSPSSTNSQPWHFIVASteeGKARVAKSAAgnytfnerkMLDASHVVVFC 85
Cdd:cd02136    1 AIKSRRSVRAFKD-KPVPKETIEKILEAARRAPSGKNTQPWRVYVVT---GKARERLKKA---------FFGAPVALFLT 67

                         90
                 ....*....|.
gi 446278033  86 AKTAMDDAWLE 96
Cdd:cd02136   68 MDKVLGPWSWF 78
nitroreductase cd20608
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 10-96 1.66e-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: 48.87  E-value: 1.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033  10 RYSTKAFdpSKKLTAEEadKVKTLL---QYSPSSTNSQPWHFIVASTEEGKARVAKSAagNYTFNERKmlDASHVVVFCA 86
Cdd:cd20608    7 RRSVRRF--SDKPVEEE--KLEKILeaaRLAPSWANKQCWRFIVVTDKETLSELAKKE--SPSNGWLK--DAPVIIVVCA 78

                         90
                 ....*....|
gi 446278033  87 KTAmDDAWLE 96
Cdd:cd20608   79 DPK-DSGWLN 87
nitroreductase cd02151
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 21-96 3.95e-07

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: 47.91  E-value: 3.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033  21 KLTAE--EADKVKTLLQY---SPSSTNSQPWHFIVASTEEGKARVA--KSAAGnytfnerKML-DASHVVVFCAKTAMDD 92
Cdd:cd02151   11 KYTDEpiEEEKLEEILEAallAPSSRNSRPVEFIVVDDKETLKKLSecKPHGS-------AFLkGAPAAIVVLADTEKSD 83


                 ....
gi 446278033  93 AWLE 96
Cdd:cd02151   84 TWIE 87
NfsA-like cd02146
nitroreductase similar to Escherichia coli NfsA; This family contains NADPH-dependent flavin ...
 8-216 6.86e-07

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: 48.39  E-value: 6.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033   8 LQRYSTKAFDPsKKLTAEEADKVKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKsaagnYTFNERKMLDASHVVVFCAK 87
Cdd:cd02146    6 LNHRSVRKFTD-EPLTDETLETLIAAAQSASTSSNLQAYSVIVVTDPELREKLAE-----LAGNQPYVAQAPVFLVFCAD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033  88 TAmddawlervvdqedadgRFATPEAKAANDKGRRFFADMHRVSLKDdhqwmakqVYLNVGNFLLGVAAMGLDAVPIEGF 167
Cdd:cd02146   80 LY-----------------RHQKIAEEAGGKDVGLDYLESFLVGVVD--------AALAAQNALVAAESLGLGIVYIGGI 134

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446278033 168 --DAEVLDAEFGLKEKgytslvVVP-----VGHhsvEDFNAGLpKSRLPLETTLTE 216
Cdd:cd02146  135 rnNPEEVIELLGLPEY------VFPlfgltVGH---PDPTPEV-KPRLPLEAVVHE 180
nitroreductase cd02150
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 26-193 2.44e-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: 45.67  E-value: 2.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033  26 EADKVKTLLQ---YSPSSTNSQPWHFIVASTEEGKARVAKsaAGNYTfnerKML-DASHVVVFCA---KTAMDDAWlerV 98
Cdd:cd02150   16 EEEDIEKLLRaamAAPSAGNQQPWHFIVVTDREKLDKIAE--AHPYG----KMLkEAPLAIVVCGdpsKEKAPGYW---V 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446278033  99 VDqedadgrfatpeAKAAndkgrrffadmhrvslkddhqwmakqvylnVGNFLLGVAAMGLDAV-----PIEGfDAEVLD 173
Cdd:cd02150   87 QD------------CSAA------------------------------TENILLAAHALGLGAVwlgvyPFEE-RVKAIR 123

                        170       180
                 ....*....|....*....|
gi 446278033 174 AEFGLKEkGYTSLVVVPVGH 193
Cdd:cd02150  124 EILNIPE-NIIPFCVIALGY 142
McbC_SagB-like_oxidoreductase cd02142
oxidase similar to the microcin B17 processing protein McbC; This family is the oxidase domain ...
 148-193 4.77e-04

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: 39.71  E-value: 4.77e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446278033 148 GNFLLGVAAMGLDAVPIEGFDAEVLDAEFGLKEKGYTSLVVVPVGH 193
Cdd:cd02142  155 QNLYLAATALGLGLCAIGAFDDDALRELLGLDEVEEVVLYAFVVGG 200
 
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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