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Conserved domains on  [gi|488988036|ref|WP_002898814|]
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MULTISPECIES: malonic semialdehyde reductase [Klebsiella]

Protein Classification

nitroreductase family protein( domain architecture ID 10012358)

nitroreductase family protein, similar to nitroreductase which catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles by using NAD(P)H as electron donor in an obligatory two-electron transfer and FMN as cofactor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05365 PRK05365
malonic semialdehyde reductase; Provisional
 2-196 5.06e-137

malonic semialdehyde reductase; Provisional


:

Pssm-ID: 180040 [Multi-domain]  Cd Length: 195  Bit Score: 380.70  E-value: 5.06e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036   2 NDAINHTACETLFTQARTHNGWLDKPVSDAQLQAVWDLMKMGPTSANCSPARIVFVRSAEGKEKLRPTLSSGNLQKTMQA 81
Cdd:PRK05365   1 SEALDDAALDQLFTEARTHNGWLDEPVSDEQLRELYDLVKWGPTSANCSPARFVFVRSAEAKERLRPALSEGNLAKTLAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036  82 PVTAIVAWDSAFYDRLPTLFPHGDARSWFTSSPQLAEETAFRNSSLQAAYLIFACRALGLDTGPMSGFDREKVDAAFFAD 161
Cdd:PRK05365  81 PVTAIVAYDTEFHEHLPKLFPHADARSWFAGNPALAEETAFRNSSLQGAYLILAARALGLDAGPMSGFDAAAVDAEFFAG 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 488988036 162 NGWKSNLLVNIGYGDPGKLYGRLPRLSFDEACLLA 196
Cdd:PRK05365 161 TTWKSNFLVNIGYGDPAKLFPRLPRLSFDEACRIL 195
 
Name Accession Description Interval E-value
PRK05365 PRK05365
malonic semialdehyde reductase; Provisional
 2-196 5.06e-137

malonic semialdehyde reductase; Provisional


Pssm-ID: 180040 [Multi-domain]  Cd Length: 195  Bit Score: 380.70  E-value: 5.06e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036   2 NDAINHTACETLFTQARTHNGWLDKPVSDAQLQAVWDLMKMGPTSANCSPARIVFVRSAEGKEKLRPTLSSGNLQKTMQA 81
Cdd:PRK05365   1 SEALDDAALDQLFTEARTHNGWLDEPVSDEQLRELYDLVKWGPTSANCSPARFVFVRSAEAKERLRPALSEGNLAKTLAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036  82 PVTAIVAWDSAFYDRLPTLFPHGDARSWFTSSPQLAEETAFRNSSLQAAYLIFACRALGLDTGPMSGFDREKVDAAFFAD 161
Cdd:PRK05365  81 PVTAIVAYDTEFHEHLPKLFPHADARSWFAGNPALAEETAFRNSSLQGAYLILAARALGLDAGPMSGFDAAAVDAEFFAG 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 488988036 162 NGWKSNLLVNIGYGDPGKLYGRLPRLSFDEACLLA 196
Cdd:PRK05365 161 TTWKSNFLVNIGYGDPAKLFPRLPRLSFDEACRIL 195
RutE-like cd02148
nitroreductase similar to Escherichia coli RutE; A subfamily of the nitroreductase family ...
 9-193 8.14e-121

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: 339.61  E-value: 8.14e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036   9 ACETLFTQARTHNGWLDKPVSDAQLQAVWDLMKMGPTSANCSPARIVFVRSAEGKEKLRPTLSSGNLQKTMQAPVTAIVA 88
Cdd:cd02148    1 ALDQLFTEARTHNAWEDKPVSDEELRAIYDLAKWGPTAANCSPARIVFVRSAEAKERLVPHLSEGNREKTMAAPVTAILA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036  89 WDSAFYDRLPTLFPHGDARSWFTSS-PQLAEETAFRNSSLQAAYLIFACRALGLDTGPMSGFDREKVDAAFFADNGWKSN 167
Cdd:cd02148   81 YDTEFYEHLPRLFPHGDARSWFFGSgPARAEETAFRNASLQAAYFILAARALGLDCGPMSGFDAAGVDAEFFAGTRWKSN 160

                        170       180
                 ....*....|....*....|....*.
gi 488988036 168 LLVNIGYGDPGKLYGRLPRLSFDEAC 193
Cdd:cd02148  161 LVVNLGYGDPSKLFPRLPRLDFDEAC 186
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
 11-193 5.65e-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: 131.13  E-value: 5.65e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036  11 ETLFTQARTHNGWLDKPVSDAQLQAVWDLMKMGPTSANCSPARIVFVRSAEGKEKLRPTLSSGNLQKTMQAPVTAIVAWD 90
Cdd:COG0778    2 LELLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEALAEANQEWVADAPVLIVVCAD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036  91 SAFYDRLPtlfphgdarswftsspqlaEETAFRNSSLQAAYLIFACRALGLDTGPMSGFDREKVDAAFFADNGWKSNLLV 170
Cdd:COG0778   82 PDRSEKVP-------------------ERYALLDAGIAAQNLLLAARALGLGTCWIGGFDPEKVRELLGLPEGEEPVALL 142

                        170       180
                 ....*....|....*....|...
gi 488988036 171 NIGYGDPGKlyGRLPRLSFDEAC 193
Cdd:COG0778  143 ALGYPAEEL--NPRPRKPLEEVV 163
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
 16-174 2.80e-16

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: 72.81  E-value: 2.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036   16 QARTHNGWLDKPVSDAQLQAVWDLMKMGPTSANCSPARIVFVRSAEGKEKLRPTLSSGNLQKTMQAPVTAIVAWDSAFYD 95
Cdd:pfam00881   3 QRRSVRKFDPEPVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLAEAALELLLVEPAAALLLLLRRDANLKLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036   96 RLP-------TLFPHGDARSWFTSSPQLAEETAFRNSSLQAAYLIFACRALGLDTGPMSGFDREKVDAAFFADNGWKSNL 168
Cdd:pfam00881  83 LQDflrgapvLIVITASLSTYLRKAAERAYREALLDAGAAAQNLLLAATSLGLGSCPIGGFDAAAVRELLGLPDDERLVG 162


                  ....*.
gi 488988036  169 LVNIGY 174
Cdd:pfam00881 163 LIAVGY 168
 
Name Accession Description Interval E-value
PRK05365 PRK05365
malonic semialdehyde reductase; Provisional
 2-196 5.06e-137

malonic semialdehyde reductase; Provisional


Pssm-ID: 180040 [Multi-domain]  Cd Length: 195  Bit Score: 380.70  E-value: 5.06e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036   2 NDAINHTACETLFTQARTHNGWLDKPVSDAQLQAVWDLMKMGPTSANCSPARIVFVRSAEGKEKLRPTLSSGNLQKTMQA 81
Cdd:PRK05365   1 SEALDDAALDQLFTEARTHNGWLDEPVSDEQLRELYDLVKWGPTSANCSPARFVFVRSAEAKERLRPALSEGNLAKTLAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036  82 PVTAIVAWDSAFYDRLPTLFPHGDARSWFTSSPQLAEETAFRNSSLQAAYLIFACRALGLDTGPMSGFDREKVDAAFFAD 161
Cdd:PRK05365  81 PVTAIVAYDTEFHEHLPKLFPHADARSWFAGNPALAEETAFRNSSLQGAYLILAARALGLDAGPMSGFDAAAVDAEFFAG 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 488988036 162 NGWKSNLLVNIGYGDPGKLYGRLPRLSFDEACLLA 196
Cdd:PRK05365 161 TTWKSNFLVNIGYGDPAKLFPRLPRLSFDEACRIL 195
RutE-like cd02148
nitroreductase similar to Escherichia coli RutE; A subfamily of the nitroreductase family ...
 9-193 8.14e-121

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: 339.61  E-value: 8.14e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036   9 ACETLFTQARTHNGWLDKPVSDAQLQAVWDLMKMGPTSANCSPARIVFVRSAEGKEKLRPTLSSGNLQKTMQAPVTAIVA 88
Cdd:cd02148    1 ALDQLFTEARTHNAWEDKPVSDEELRAIYDLAKWGPTAANCSPARIVFVRSAEAKERLVPHLSEGNREKTMAAPVTAILA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036  89 WDSAFYDRLPTLFPHGDARSWFTSS-PQLAEETAFRNSSLQAAYLIFACRALGLDTGPMSGFDREKVDAAFFADNGWKSN 167
Cdd:cd02148   81 YDTEFYEHLPRLFPHGDARSWFFGSgPARAEETAFRNASLQAAYFILAARALGLDCGPMSGFDAAGVDAEFFAGTRWKSN 160

                        170       180
                 ....*....|....*....|....*.
gi 488988036 168 LLVNIGYGDPGKLYGRLPRLSFDEAC 193
Cdd:cd02148  161 LVVNLGYGDPSKLFPRLPRLDFDEAC 186
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
 11-193 5.65e-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: 131.13  E-value: 5.65e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036  11 ETLFTQARTHNGWLDKPVSDAQLQAVWDLMKMGPTSANCSPARIVFVRSAEGKEKLRPTLSSGNLQKTMQAPVTAIVAWD 90
Cdd:COG0778    2 LELLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEALAEANQEWVADAPVLIVVCAD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036  91 SAFYDRLPtlfphgdarswftsspqlaEETAFRNSSLQAAYLIFACRALGLDTGPMSGFDREKVDAAFFADNGWKSNLLV 170
Cdd:COG0778   82 PDRSEKVP-------------------ERYALLDAGIAAQNLLLAARALGLGTCWIGGFDPEKVRELLGLPEGEEPVALL 142

                        170       180
                 ....*....|....*....|...
gi 488988036 171 NIGYGDPGKlyGRLPRLSFDEAC 193
Cdd:COG0778  143 ALGYPAEEL--NPRPRKPLEEVV 163
MhqN-like cd02137
nitroreductase family protein similar to the NAD(P)H nitroreductase MhqN; A diverse subfamily ...
 25-191 2.86e-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: 74.58  E-value: 2.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036  25 DKPVSDAQLQAVWDLMKMGPTSANCSPARIVFVRSAEGKEKLRPtlSSGNLQKTMQAPVTAIVAWDsafydrlptlfphg 104
Cdd:cd02137   16 DHKIPKEELKEILELATLAPSSFNLQPWRFVVVRDPELKAKLAE--AAYNQPQVTTASAVILVLGD-------------- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036 105 darswftsspqlaeetafRNSSLQAAYLIFACRALGLDTGPMSGFDREKVDAAFFADNGWKSNLLVNIGYGDPGklYGRL 184
Cdd:cd02137   80 ------------------LNAGLAAMNLMLAAKAKGYDTCPMGGFDKEKVAELLNLPDRYVPVLLIAIGKAADK--APRS 139


                 ....*..
gi 488988036 185 PRLSFDE 191
Cdd:cd02137  140 GRLPVDE 146
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
 16-174 2.80e-16

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: 72.81  E-value: 2.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036   16 QARTHNGWLDKPVSDAQLQAVWDLMKMGPTSANCSPARIVFVRSAEGKEKLRPTLSSGNLQKTMQAPVTAIVAWDSAFYD 95
Cdd:pfam00881   3 QRRSVRKFDPEPVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLAEAALELLLVEPAAALLLLLRRDANLKLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036   96 RLP-------TLFPHGDARSWFTSSPQLAEETAFRNSSLQAAYLIFACRALGLDTGPMSGFDREKVDAAFFADNGWKSNL 168
Cdd:pfam00881  83 LQDflrgapvLIVITASLSTYLRKAAERAYREALLDAGAAAQNLLLAATSLGLGSCPIGGFDAAAVRELLGLPDDERLVG 162


                  ....*.
gi 488988036  169 LVNIGY 174
Cdd:pfam00881 163 LIAVGY 168
Nitro_FMN_reductase cd02062
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 14-174 3.67e-16

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: 71.56  E-value: 3.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036  14 FTQARTHNGWLDKPVSDAQLQAVWDLMKMGPTSANCSPARIVFVRSAEGKEKLRpTLSSGNLQKTMQAPVTAIVawdsaf 93
Cdd:cd02062    1 IKTRRSIRKFTDKPVPEEKLRKILEAARLAPSAGNLQPWRFIVVRDREKKEKLA-KLAAPNQKFIAGAPVVIVV------ 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036  94 ydrlptlfphgdarswfTSSPQLAEETAFRNSSLQAAYLIFACRALGLDTGPMSGFDR--EKVDAAFFADNGWKSNLLVN 171
Cdd:cd02062   74 -----------------VADPDKSRPWALEDAGAAAQNLLLAAAALGLGSCWIGGFDFreDKVRELLGIPENLRPVALIA 136


                 ...
gi 488988036 172 IGY 174
Cdd:cd02062  137 IGY 139
nitroreductase cd03370
uncharacterized nitroreductase family proteins; Nitroreductase family containing Thermus ...
 23-158 5.69e-14

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: 66.96  E-value: 5.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036  23 WLDKPVSDAQLQAVWDLMKMGPTSANCSPARIVFVRSAEGKEKLRpTLSSGNLQKTmQAPVTAIVAWDSAfyDRLPTL-- 100
Cdd:cd03370   14 YTQEPVPDEDLREILRLAGLAPSAWNIQPWRFVVVRDAELKEQLQ-AAAYGQAQVT-SAPAVIVIYSDME--DALANLee 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488988036 101 FPH----GDARSWFTSSPQlaeeTAFRNSSLQA-------------AYLIFACRALGLDTGPMSGFDREKVDAAF 158
Cdd:cd03370   90 TIHpglsEERRQREAAGLR----GAFGKMSVEQrgqwglaqanialGFLLLAAQSLGYDTSPMLGFDPEKVKALL 160
NfsB-like cd02149
nitroreductase similar to Escherichia coli NfsB; NAD(P)H:FMN oxidoreductase family. This ...
 26-180 5.51e-13

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: 63.42  E-value: 5.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036  26 KPVSDAQLQAVWDLMKMGPTSANCSPARIVFVRSAEGKEKLRPtLSSGNLQKTMQAPVTAIVAWDsafydrlptlfphgd 105
Cdd:cd02149   19 KKISDEDLETILEALRLSPSSFGLEPWKFLVVENPELKAKLAP-AAWFNQPQIKDASHVVVFLAK--------------- 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488988036 106 aRSWftSSPQlaeetafrnSSLQAAYLIFACRALGLDTGPMSGFDREKVDAAFFAD-NGWKSNLLVNIGYGDPGKL 180
Cdd:cd02149   83 -KDW--SAKQ---------TYIALGNMLLAAAMLGIDSCPIEGFDPAKLDEILGLDeKGYKISVMVAFGYRSEEKL 146
TdsD-like cd02138
nitroreductase similar to Burkholderia pseudomallei TdsD; A subfamily of the nitroreductase ...
 25-184 3.79e-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: 50.62  E-value: 3.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036  25 DKPVSDAQLQAVWDLMKMGPTSANCSPARIVFV-RSAEGKEKLRPTLSSGNLQKTMQAPVTAIVAWDsafydrlpTLFPH 103
Cdd:cd02138   13 PEPISEEDLLSLFEAARWAPSCFNEQPWRFVVArRDTEAFEKLLDLLAEGNQSWAKNAPVLIVVLAK--------TEFDH 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036 104 GDARSwftsspqlaeETAFRNSSLQAAYLIFACRALGLDTGPMSGFDREKVDAAFFADNGWKSNLLVNIGY-GDPGKLYG 182
Cdd:cd02138   85 NGKPN----------RYALFDTGAAVANLALQATALGLVVHQMAGFDPEKAKEALGIPDEYEPITMIAIGYpGDPESLPE 154


                 ..
gi 488988036 183 RL 184
Cdd:cd02138  155 KL 156
PRK11053 PRK11053
oxygen-insensitive NAD(P)H nitroreductase;
26-186 6.11e-06

oxygen-insensitive NAD(P)H nitroreductase;


Pssm-ID: 182929 [Multi-domain]  Cd Length: 217  Bit Score: 44.96  E-value: 6.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036  26 KPVSDAQLQAVWDLMKMGPTSANCSPARIVFVRSAEGKEKLRPTLSSG---NLQKTMQAPVTAI----VAWDSAFYDRLp 98
Cdd:PRK11053  20 KKLPAEQIEQIKTLLRFSPSSVNSQPWHFIVASTEEGKARIAKAAAGNyafNERKILDASHVVVfcakTDMDDAYLELV- 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036  99 tL--------FP-------HGDARSWFTS----SPQLAEETAFRNSSLQAAYLIFACRALGLDTGPMSGFDREKVDAAF- 158
Cdd:PRK11053  99 -LeqedadgrFAteeakaaQDKGRRFFADmhrkELKDLQHWMEKQVYLALGNLLLGAAALGIDATPIEGFDAAILDAEFg 177

                        170       180
                 ....*....|....*....|....*...
gi 488988036 159 FADNGWKSNLLVNIGYGDPGKLYGRLPR 186
Cdd:PRK11053 178 LREKGLTSSVVVPLGYHSEEDFNAKLPK 205
nitroreductase cd20609
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 25-67 2.37e-05

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: 42.38  E-value: 2.37e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 488988036  25 DKPVSDAQLQAVWDLMKMGPTSANCSPARIVFVRSAEGKEKLR 67
Cdd:cd20609   17 DKPVEKEKLDKILEAGRLAPTAVNYQPQRILVVRSEEALEKLA 59
PnbA_NfnB-like cd02136
nitroreductase similar to Mycobacterium smegmatis NfnB; Members of this family utilize FMN as ...
 24-191 7.41e-04

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: 38.34  E-value: 7.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036  24 LDKPVSDAQLQAVWDLMKMGPTSANCSPARIVFVRSAEgKEKLRptlssgnlQKTMQAPVTAIVawdsaFYDRLPTLFPH 103
Cdd:cd02136   12 KDKPVPKETIEKILEAARRAPSGKNTQPWRVYVVTGKA-RERLK--------KAFFGAPVALFL-----TMDKVLGPWSW 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036 104 GDArswftsspqlaeetafrnsSLQAAYLIFACRALGLDTGPMSGF--DREKVDAAFFADNGWKSNLLVNIGYGDPGKLY 181
Cdd:cd02136   78 FDL-------------------GAFLQNLMLAAHALGLGTCPQGALagYPDVVRKELGIPDDEELVCGIALGYPDPDAPV 138

                        170
                 ....*....|..
gi 488988036 182 GRL--PRLSFDE 191
Cdd:cd02136  139 NQFrtPREPLEE 150
NfsA-like cd02146
nitroreductase similar to Escherichia coli NfsA; This family contains NADPH-dependent flavin ...
 23-83 1.68e-03

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: 37.99  E-value: 1.68e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488988036  23 WLDKPVSDAQLQAVWDLMKMGPTSANCSPARIVFVRSAEGKEKLRPTlsSGNLQKTMQAPV 83
Cdd:cd02146   14 FTDEPLTDETLETLIAAAQSASTSSNLQAYSVIVVTDPELREKLAEL--AGNQPYVAQAPV 72
nitroreductase cd02139
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 25-154 5.88e-03

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: 35.91  E-value: 5.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036  25 DKPVSDAQLQAVWDLMKMGPTSANCSPARIVFVRSAEGKEKLRPTLssgNLQKTM-QAPVT-AIVAwdsafydrLPTLFP 102
Cdd:cd02139   16 PTPVEEEKLLRILEAARLAPSAKNRQPWRFIVVKDKELKEKLAEAA---NGQKFIaEAPVViVACA--------DPSESG 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488988036 103 HGDARSWFTSSPQLAEEtafrnsslqaaYLIFACRALGLDTGPMSGFDREKV 154
Cdd:cd02139   85 MGCGKPYYLVDVAIAME-----------HLVLAATEEGLGTCWIGAFDEDKV 125
nitroreductase cd20608
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 24-154 8.19e-03

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: 35.39  E-value: 8.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988036  24 LDKPVSDAQLQAVWDLMKMGPTSANCSPARIVFVRSAEGKEKLRPTLSSGNLQKTmQAPVTAIVAWDsafydrlptlfPH 103
Cdd:cd20608   14 SDKPVEEEKLEKILEAARLAPSWANKQCWRFIVVTDKETLSELAKKESPSNGWLK-DAPVIIVVCAD-----------PK 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488988036 104 GDARSWFTSSPQLAEETAFRNsslqaayLIFACRALGLDTGPMSGFDREKV 154
Cdd:cd20608   82 DSGWLNGQNYYLVDAAIAMQN-------LMLAATDLGLGTCWIGAFDEKKV 125
 
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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