|
Name |
Accession |
Description |
Interval |
E-value |
| BluB |
TIGR02476 |
5,6-dimethylbenzimidazole synthase; A previously published hypothesis that BluB, involved in ... |
8-210 |
3.48e-83 |
|
5,6-dimethylbenzimidazole synthase; A previously published hypothesis that BluB, involved in cobalamin biosynthesis, is EC 1.16.8.1 (cob(II)yrinic acid a,c-diamide reductase) is now contradicted by newer work ascribing a role in 5,6-dimethylbenzimidazole (DMB) biosynthesis. The BluB protein is related to the nitroreductase family (pfam0881). [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 162875 Cd Length: 205 Bit Score: 245.81 E-value: 3.48e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 8 FSATERAAVYRAIAERRDMRHFSGGSVAPELLARLLEAAHQAPSVGLMQPWRFIRITEPALRRAIHGLVEEERGRTAEAL 87
Cdd:TIGR02476 1 FSDAERAAVYRLIRERRDVRHFRSDPVPEAVLERLLDAAHHAPSVGFSQPWRFVRVESPATREAVHALFTRANQAAAAIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 88 -GERSDEFMRLKVEGVLDCAELLVAALMDDR-ERHVFGRRTLPQMDLASLACAIQNLWLASRAEGLGMGWVSLFDPAALG 165
Cdd:TIGR02476 81 dGERASQYHRLKLEGIREAPVQLAVFCDDARgEGHGLGRHTMPEMLRYSVACAIQNLWLAARAEGLGVGWVSILDPDAVR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15596471 166 ELLGLPPGSEAVAVLCLGPVAEFYPAPMLALEGWSEPRPLAELVY 210
Cdd:TIGR02476 161 RLLGVPEGWRLVAYLCLGWPDAFYDEPELERAGWQERRPLEWRRY 205
|
|
| BluB |
cd02145 |
5,6-dimethylbenzimidazole synthase; BluB catalyzes the O2-dependent conversion of FMNH2 to 5, ... |
17-209 |
2.35e-77 |
|
5,6-dimethylbenzimidazole synthase; BluB catalyzes the O2-dependent conversion of FMNH2 to 5,6-dimethylbenzimidazole (DMB), a component of vitamin B12; is is a subfamily of the nitroreductase family; nitroreductases typically reduce their substrates by using NAD(P)H as electron donor and often use FMN as a cofactor.
Pssm-ID: 380321 Cd Length: 196 Bit Score: 230.71 E-value: 2.35e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 17 YRAIAERRDMRHFSGGSVAPELLARLLEAAHQAPSVGLMQPWRFIRITEPALRRAIHGLVEEERGRTAEAL-GERSDEFM 95
Cdd:cd02145 1 YRVIRWRRDVRHFRPDPVPEEVLERLLQAAHLAPSVGLMQPWRFVRVRSAATRKAVHELFQRANAEAAEMYtGERAAQYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 96 RLKVEGVLDCAELLVAALMDDRER-HVFGRRTLPQMDLASLACAIQNLWLASRAEGLGMGWVSLFDPAALGELLGLPPGS 174
Cdd:cd02145 81 TLKLEGIEEAPLQLAVFCDRARAGgHGLGRTTMPEMDLYSSVCAVQNLWLAARAEGLGVGWVSILDPDEVKRLLGIPEHW 160
|
170 180 190
....*....|....*....|....*....|....*
gi 15596471 175 EAVAVLCLGPVAEFYPAPMLALEGWSEPRPLAELV 209
Cdd:cd02145 161 EPVAYLCIGYPEFFYDEPELEQAGWEQRRPLEWVV 195
|
|
| NfnB |
COG0778 |
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ... |
16-197 |
3.32e-41 |
|
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway/BioSystem: Pyrimidine degradation
Pssm-ID: 440541 [Multi-domain] Cd Length: 163 Bit Score: 137.68 E-value: 3.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 16 VYRAIAERRDMRHFSGGSVAPELLARLLEAAHQAPSVGLMQPWRFIRITEPALRRAIhglveeergrtAEALGERSDEFm 95
Cdd:COG0778 1 LLELLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERL-----------AEALAEANQEW- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 96 rlkvegVLDCAELLVAALMDDRerhvfGRRTLPQMDLASLACAIQNLWLASRAEGLGMGWVSLFDPAALGELLGLPPGSE 175
Cdd:COG0778 69 ------VADAPVLIVVCADPDR-----SEKVPERYALLDAGIAAQNLLLAARALGLGTCWIGGFDPEKVRELLGLPEGEE 137
|
170 180
....*....|....*....|...
gi 15596471 176 AVAVLCLG-PVAEFYPAPMLALE 197
Cdd:COG0778 138 PVALLALGyPAEELNPRPRKPLE 160
|
|
| Nitroreductase |
pfam00881 |
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ... |
20-183 |
2.82e-31 |
|
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent and NAD(P)H-dependent enzymes able to metabolize nitrosubstituted compounds.
Pssm-ID: 425926 [Multi-domain] Cd Length: 168 Bit Score: 112.49 E-value: 2.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 20 IAERRDMRHFSGGSVAPELLARLLEAAHQAPSVGLMQPWRFIRITEPALRR----AIHGLVEEERGRTAEALGERSDEFM 95
Cdd:pfam00881 1 IRQRRSVRKFDPEPVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYrlaeAALELLLVEPAAALLLLLRRDANLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 96 RLKVEGVLDCAELLVAALMDDRERHVFGRRtLPQMDLASLACAIQNLWLASRAEGLGMGWVSLFDPAALGELLGLPPGSE 175
Cdd:pfam00881 81 LLLQDFLRGAPVLIVITASLSTYLRKAAER-AYREALLDAGAAAQNLLLAATSLGLGSCPIGGFDAAAVRELLGLPDDER 159
|
....*...
gi 15596471 176 AVAVLCLG 183
Cdd:pfam00881 160 LVGLIAVG 167
|
|
| PRK10765 |
PRK10765 |
oxygen-insensitive NADPH nitroreductase; |
20-214 |
3.26e-12 |
|
oxygen-insensitive NADPH nitroreductase;
Pssm-ID: 182710 Cd Length: 240 Bit Score: 63.45 E-value: 3.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 20 IAERRDMRHFSGGSVAPELLARLLEAAHQAPSVGLMQPWRFIRITEPALRRAIhglveeergrtAEALGERsdefmrlkv 99
Cdd:PRK10765 8 ILSHRSIRHFTDEPISEAQREAIINAARAASSSSFLQCSSIIRITDKALREAL-----------VELTGGQ--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 100 EGVLDCAELLVAALmdDRERHvfgRRTLP--QMDLASL--------ACAIQNLWLAsrAEGLGMGWVSL----FDPAALG 165
Cdd:PRK10765 68 KYVAQAAEFWVFCA--DFNRH---LQICPdaQLGLAEQlligavdtAIMAQNALLA--AESLGLGGVYIgglrNNIEAVT 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15596471 166 ELLGLPpgsEAVAVL---CLGpvaefYPA--PMLalegwsEPR-PLAELVYQNRW 214
Cdd:PRK10765 141 ELLKLP---QHVLPLfglCLG-----WPAqnPDL------KPRlPASLLVHENQY 181
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| BluB |
TIGR02476 |
5,6-dimethylbenzimidazole synthase; A previously published hypothesis that BluB, involved in ... |
8-210 |
3.48e-83 |
|
5,6-dimethylbenzimidazole synthase; A previously published hypothesis that BluB, involved in cobalamin biosynthesis, is EC 1.16.8.1 (cob(II)yrinic acid a,c-diamide reductase) is now contradicted by newer work ascribing a role in 5,6-dimethylbenzimidazole (DMB) biosynthesis. The BluB protein is related to the nitroreductase family (pfam0881). [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 162875 Cd Length: 205 Bit Score: 245.81 E-value: 3.48e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 8 FSATERAAVYRAIAERRDMRHFSGGSVAPELLARLLEAAHQAPSVGLMQPWRFIRITEPALRRAIHGLVEEERGRTAEAL 87
Cdd:TIGR02476 1 FSDAERAAVYRLIRERRDVRHFRSDPVPEAVLERLLDAAHHAPSVGFSQPWRFVRVESPATREAVHALFTRANQAAAAIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 88 -GERSDEFMRLKVEGVLDCAELLVAALMDDR-ERHVFGRRTLPQMDLASLACAIQNLWLASRAEGLGMGWVSLFDPAALG 165
Cdd:TIGR02476 81 dGERASQYHRLKLEGIREAPVQLAVFCDDARgEGHGLGRHTMPEMLRYSVACAIQNLWLAARAEGLGVGWVSILDPDAVR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15596471 166 ELLGLPPGSEAVAVLCLGPVAEFYPAPMLALEGWSEPRPLAELVY 210
Cdd:TIGR02476 161 RLLGVPEGWRLVAYLCLGWPDAFYDEPELERAGWQERRPLEWRRY 205
|
|
| BluB |
cd02145 |
5,6-dimethylbenzimidazole synthase; BluB catalyzes the O2-dependent conversion of FMNH2 to 5, ... |
17-209 |
2.35e-77 |
|
5,6-dimethylbenzimidazole synthase; BluB catalyzes the O2-dependent conversion of FMNH2 to 5,6-dimethylbenzimidazole (DMB), a component of vitamin B12; is is a subfamily of the nitroreductase family; nitroreductases typically reduce their substrates by using NAD(P)H as electron donor and often use FMN as a cofactor.
Pssm-ID: 380321 Cd Length: 196 Bit Score: 230.71 E-value: 2.35e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 17 YRAIAERRDMRHFSGGSVAPELLARLLEAAHQAPSVGLMQPWRFIRITEPALRRAIHGLVEEERGRTAEAL-GERSDEFM 95
Cdd:cd02145 1 YRVIRWRRDVRHFRPDPVPEEVLERLLQAAHLAPSVGLMQPWRFVRVRSAATRKAVHELFQRANAEAAEMYtGERAAQYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 96 RLKVEGVLDCAELLVAALMDDRER-HVFGRRTLPQMDLASLACAIQNLWLASRAEGLGMGWVSLFDPAALGELLGLPPGS 174
Cdd:cd02145 81 TLKLEGIEEAPLQLAVFCDRARAGgHGLGRTTMPEMDLYSSVCAVQNLWLAARAEGLGVGWVSILDPDEVKRLLGIPEHW 160
|
170 180 190
....*....|....*....|....*....|....*
gi 15596471 175 EAVAVLCLGPVAEFYPAPMLALEGWSEPRPLAELV 209
Cdd:cd02145 161 EPVAYLCIGYPEFFYDEPELEQAGWEQRRPLEWVV 195
|
|
| NfnB |
COG0778 |
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ... |
16-197 |
3.32e-41 |
|
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway/BioSystem: Pyrimidine degradation
Pssm-ID: 440541 [Multi-domain] Cd Length: 163 Bit Score: 137.68 E-value: 3.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 16 VYRAIAERRDMRHFSGGSVAPELLARLLEAAHQAPSVGLMQPWRFIRITEPALRRAIhglveeergrtAEALGERSDEFm 95
Cdd:COG0778 1 LLELLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERL-----------AEALAEANQEW- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 96 rlkvegVLDCAELLVAALMDDRerhvfGRRTLPQMDLASLACAIQNLWLASRAEGLGMGWVSLFDPAALGELLGLPPGSE 175
Cdd:COG0778 69 ------VADAPVLIVVCADPDR-----SEKVPERYALLDAGIAAQNLLLAARALGLGTCWIGGFDPEKVRELLGLPEGEE 137
|
170 180
....*....|....*....|...
gi 15596471 176 AVAVLCLG-PVAEFYPAPMLALE 197
Cdd:COG0778 138 PVALLALGyPAEELNPRPRKPLE 160
|
|
| Nitroreductase |
pfam00881 |
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ... |
20-183 |
2.82e-31 |
|
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent and NAD(P)H-dependent enzymes able to metabolize nitrosubstituted compounds.
Pssm-ID: 425926 [Multi-domain] Cd Length: 168 Bit Score: 112.49 E-value: 2.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 20 IAERRDMRHFSGGSVAPELLARLLEAAHQAPSVGLMQPWRFIRITEPALRR----AIHGLVEEERGRTAEALGERSDEFM 95
Cdd:pfam00881 1 IRQRRSVRKFDPEPVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYrlaeAALELLLVEPAAALLLLLRRDANLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 96 RLKVEGVLDCAELLVAALMDDRERHVFGRRtLPQMDLASLACAIQNLWLASRAEGLGMGWVSLFDPAALGELLGLPPGSE 175
Cdd:pfam00881 81 LLLQDFLRGAPVLIVITASLSTYLRKAAER-AYREALLDAGAAAQNLLLAATSLGLGSCPIGGFDAAAVRELLGLPDDER 159
|
....*...
gi 15596471 176 AVAVLCLG 183
Cdd:pfam00881 160 LVGLIAVG 167
|
|
| Nitro_FMN_reductase |
cd02062 |
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ... |
20-183 |
3.40e-24 |
|
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or nitrocompounds using NAD(P)H as electron donor in a obligatory two-electron transfer, utilizing FMN or FAD as cofactor. They are often found to be homodimers. Enzymes of this family are described as NAD(P)H:FMN oxidoreductases, oxygen-insensitive nitroreductase, flavin reductase P, dihydropteridine reductase, NADH oxidase or NADH dehydrogenase.
Pssm-ID: 380311 [Multi-domain] Cd Length: 139 Bit Score: 93.13 E-value: 3.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 20 IAERRDMRHFSGGSVAPELLARLLEAAHQAPSVGLMQPWRFIRITEPALRRAIHGLVEEERGRTAEAlgersdefmrlkv 99
Cdd:cd02062 1 IKTRRSIRKFTDKPVPEEKLRKILEAARLAPSAGNLQPWRFIVVRDREKKEKLAKLAAPNQKFIAGA------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 100 egvldcAELLVAALMDDRERHvfgrrtlpqMDLASLACAIQNLWLASRAEGLGMGWVSLFD--PAALGELLGLPPGSEAV 177
Cdd:cd02062 68 ------PVVIVVVADPDKSRP---------WALEDAGAAAQNLLLAAAALGLGSCWIGGFDfrEDKVRELLGIPENLRPV 132
|
....*.
gi 15596471 178 AVLCLG 183
Cdd:cd02062 133 ALIAIG 138
|
|
| YdjA-like |
cd02135 |
nitroreductase family protein similar to Escherichia coli YdjA; A subfamily of the ... |
19-183 |
2.47e-23 |
|
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: 91.51 E-value: 2.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 19 AIAERRDMRHFS-GGSVAPELLARLLEAAHQAPSVGLMQPWRFIRITEPALRRaihglVEEERGRTAEALGERSDEFMRL 97
Cdd:cd02135 3 LIKTRRSIRKFKlTGAPPEEQLEELLEAAMWAPNHGKLEPWRFIVVTGEGRER-----LAELLAAAAAARAPGADPEKLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 98 KVEGVLDCAELLVAALMDDRERHvfgrrTLPQM-DLASLACAIQNLWLASRAEGLGMGWVS---LFDPAALgELLGLPPG 173
Cdd:cd02135 78 KAREKALRAPVVIAVVAKPDEDP-----KVPEWeQYAAVGAAVQNLLLAAHALGLGAVWRTgpvTYDPAVR-EALGLPED 151
|
170
....*....|
gi 15596471 174 SEAVAVLCLG 183
Cdd:cd02135 152 ERIVGFLYLG 161
|
|
| nitroreductase |
cd20608 |
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ... |
19-183 |
5.64e-23 |
|
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: 90.09 E-value: 5.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 19 AIAERRDMRHFSGGSVAPELLARLLEAAHQAPSVGLMQPWRFIRITEPALRRAihglVEEERGRTAEALGErsdefmrlk 98
Cdd:cd20608 3 AIKTRRSVRRFSDKPVEEEKLEKILEAARLAPSWANKQCWRFIVVTDKETLSE----LAKKESPSNGWLKD--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 99 vegvldcAELLVAALMDDRERhvfGRRTLPQMDLASLACAIQNLWLASRAEGLGMGWVSLFDPAALGELLGLPPGSEAVA 178
Cdd:cd20608 70 -------APVIIVVCADPKDS---GWLNGQNYYLVDAAIAMQNLMLAATDLGLGTCWIGAFDEKKVKEILGIPENIRVVA 139
|
....*
gi 15596471 179 VLCLG 183
Cdd:cd20608 140 LTPLG 144
|
|
| nitroreductase |
cd02139 |
nitroreductase family protein; A subfamily of the nitroreductase family containing ... |
16-212 |
2.63e-21 |
|
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: 86.37 E-value: 2.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 16 VYRAIAERRDMRHFSGGSVAPELLARLLEAAHQAPSVGLMQPWRFIRITEPALRRAIHglveeERGRTAEALGErsdefm 95
Cdd:cd02139 1 VYEAIKKRRSIRKYKPTPVEEEKLLRILEAARLAPSAKNRQPWRFIVVKDKELKEKLA-----EAANGQKFIAE------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 96 rlkvegvldcAELLVAALMDDRERhvfGRRTLPQMDLASLACAIQNLWLASRAEGLGMGWVSLFDPAALGELLGLPPGSE 175
Cdd:cd02139 70 ----------APVVIVACADPSES---GMGCGKPYYLVDVAIAMEHLVLAATEEGLGTCWIGAFDEDKVKEILGIPEEYR 136
|
170 180 190
....*....|....*....|....*....|....*...
gi 15596471 176 AVAVLCLGPVAEfYPAPmlalegwsEPR-PLAELVYQN 212
Cdd:cd02139 137 VVALTPLGYPAE-EPPP--------RPRkPLEEIVFYE 165
|
|
| nitroreductase |
cd20610 |
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ... |
20-183 |
3.96e-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: 380331 [Multi-domain] Cd Length: 167 Bit Score: 72.70 E-value: 3.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 20 IAERRDMRHFSGGSVAPELLARLLEAAHQAPSVGLMQPWRFIRITEPALRRAIH---GLVEEERGRTAE----ALGERSD 92
Cdd:cd20610 1 IKKRRSIRKFKPDPVPKEDIEKILEAANWAPSGMNRQNWEFVVVKGGEKIEKIGisiKKKNEEIARLLEkvfaEKPIRFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 93 EFMR--LKVEGvldcAELLVAALMDDRERhVFGRRTlpqmDLASLACAIQNLWLASRAEGLGMGWVS--LFDPAALGELL 168
Cdd:cd20610 81 KFRRffTLFGG----APVLVVVYTEPYKP-PEERKP----DLQSVSAAIQNLLLAAHALGLGTCWMTgpLYAEDEIEEIL 151
|
170
....*....|....*
gi 15596471 169 GLPPGSEAVAVLCLG 183
Cdd:cd20610 152 EIPDDKELVAVTPLG 166
|
|
| nitroreductase |
cd20609 |
nitroreductase family protein; A subfamily of the nitroreductase family containing ... |
20-183 |
5.60e-15 |
|
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: 68.95 E-value: 5.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 20 IAERRDMRHFSGGSVAPELLARLLEAAHQAPSVGLMQPWRFIRITEPALRRAIHGLVEeergRTAEA------LGERSDE 93
Cdd:cd20609 6 AKKRYSVRKFSDKPVEKEKLDKILEAGRLAPTAVNYQPQRILVVRSEEALEKLAKATP----RFFGAplvivvCYDKDES 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 94 FMRlkvegvldcaellvaalMDDRERHVfgrrtlpQMDLAslaCAIQNLWLASRAEGLGMGWVSLFDPAALGELLGLPPG 173
Cdd:cd20609 82 WKR-----------------PYDGKDSG-------DIDAA---IVATHMMLAATELGLGTCWVGNFDPEKVREAFNLPEN 134
|
170
....*....|
gi 15596471 174 SEAVAVLCLG 183
Cdd:cd20609 135 LEPVAILPLG 144
|
|
| NfsA-like |
cd02146 |
nitroreductase similar to Escherichia coli NfsA; This family contains NADPH-dependent flavin ... |
23-214 |
1.29e-14 |
|
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: 69.96 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 23 RRDMRHFSGGSVAPELLARLLEAAHQAPSVGLMQPWRFIRITEPALRRAIHGLVEEER---------------GRTAEAL 87
Cdd:cd02146 8 HRSVRKFTDEPLTDETLETLIAAAQSASTSSNLQAYSVIVVTDPELREKLAELAGNQPyvaqapvflvfcadlYRHQKIA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 88 GERSdefmrlKVEGVLDCAELLVAALMDdrerhvfgrrtlpqmdlASLacAIQNLWLAsrAEGLGMGWVSL----FDPAA 163
Cdd:cd02146 88 EEAG------GKDVGLDYLESFLVGVVD-----------------AAL--AAQNALVA--AESLGLGIVYIggirNNPEE 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15596471 164 LGELLGLPPGSEAVAVLCLGpvaefYPAPMLALegwsEPR-PLAELVYQNRW 214
Cdd:cd02146 141 VIELLGLPEYVFPLFGLTVG-----HPDPTPEV----KPRlPLEAVVHEETY 183
|
|
| PnbA_NfnB-like |
cd02136 |
nitroreductase similar to Mycobacterium smegmatis NfnB; Members of this family utilize FMN as ... |
19-209 |
4.50e-14 |
|
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: 66.84 E-value: 4.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 19 AIAERRDMRHFSGGSVAPELLARLLEAAHQAPSVGLMQPWRFIRITEPALRR-------AIHGLVeeergrtaealgers 91
Cdd:cd02136 1 AIKSRRSVRAFKDKPVPKETIEKILEAARRAPSGKNTQPWRVYVVTGKARERlkkaffgAPVALF--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 92 defmrlkvegvldcaellvaalmddrerhVFGRRTLPQMDLASLACAIQNLWLASRAEGLGMGWVSLF--DPAALGELLG 169
Cdd:cd02136 66 -----------------------------LTMDKVLGPWSWFDLGAFLQNLMLAAHALGLGTCPQGALagYPDVVRKELG 116
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15596471 170 LPPGSEAVAVLCLGpvaefYPAPMLALEGWSEPR-PLAELV 209
Cdd:cd02136 117 IPDDEELVCGIALG-----YPDPDAPVNQFRTPRePLEEFV 152
|
|
| TdsD-like |
cd02138 |
nitroreductase similar to Burkholderia pseudomallei TdsD; A subfamily of the nitroreductase ... |
19-210 |
5.48e-14 |
|
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: 67.18 E-value: 5.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 19 AIAERRDMRHFSGGSVAPELLARLLEAAHQAPSVGLMQPWRFIRITEP-ALRRAIHGLVEEERGRTAEAlgersdefmrl 97
Cdd:cd02138 1 LIAERWSPRAFSPEPISEEDLLSLFEAARWAPSCFNEQPWRFVVARRDtEAFEKLLDLLAEGNQSWAKN----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 98 kvegvldcAELLVAALMDDRERHVFGRRTLPQMDLASlacAIQNLWLASRAEGL---GMGwvsLFDPAALGELLGLPPGS 174
Cdd:cd02138 70 --------APVLIVVLAKTEFDHNGKPNRYALFDTGA---AVANLALQATALGLvvhQMA---GFDPEKAKEALGIPDEY 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 15596471 175 EAVAVLCLGPVAEFYPAPMLALEGWSEPR---PLAELVY 210
Cdd:cd02138 136 EPITMIAIGYPGDPESLPEKLLEREEAPRtrkPLSEIVF 174
|
|
| PRK10765 |
PRK10765 |
oxygen-insensitive NADPH nitroreductase; |
20-214 |
3.26e-12 |
|
oxygen-insensitive NADPH nitroreductase;
Pssm-ID: 182710 Cd Length: 240 Bit Score: 63.45 E-value: 3.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 20 IAERRDMRHFSGGSVAPELLARLLEAAHQAPSVGLMQPWRFIRITEPALRRAIhglveeergrtAEALGERsdefmrlkv 99
Cdd:PRK10765 8 ILSHRSIRHFTDEPISEAQREAIINAARAASSSSFLQCSSIIRITDKALREAL-----------VELTGGQ--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 100 EGVLDCAELLVAALmdDRERHvfgRRTLP--QMDLASL--------ACAIQNLWLAsrAEGLGMGWVSL----FDPAALG 165
Cdd:PRK10765 68 KYVAQAAEFWVFCA--DFNRH---LQICPdaQLGLAEQlligavdtAIMAQNALLA--AESLGLGGVYIgglrNNIEAVT 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15596471 166 ELLGLPpgsEAVAVL---CLGpvaefYPA--PMLalegwsEPR-PLAELVYQNRW 214
Cdd:PRK10765 141 ELLKLP---QHVLPLfglCLG-----WPAqnPDL------KPRlPASLLVHENQY 181
|
|
| PRK13294 |
PRK13294 |
F420-0--gamma-glutamyl ligase; Provisional |
19-209 |
1.99e-11 |
|
F420-0--gamma-glutamyl ligase; Provisional
Pssm-ID: 183957 [Multi-domain] Cd Length: 448 Bit Score: 62.34 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 19 AIAERRDMRHFSGGSVAPELLARLLEAAHQAPSVGLMQPWRFIRITEPALRRAihgLVEEERGRTAEALgeRSDEF---- 94
Cdd:PRK13294 256 AVLLRRSVREFSDDPVDPEAVRRAVAAALTAPAPHHTRPVRFVWLRSAAVRTR---LLDAMRDAWRADL--RADGLsees 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 95 --MRLKVEGVLDCAELLVAALMDDRERHVFG--RRTLPQ--MDLASLACAIQNLWLASRAEGLGMGWVS--LFDPAALGE 166
Cdd:PRK13294 331 iaRRVRRGDILYDAPELVVPFLVPDGAHSYPdaRRTAAErtMFTVAVGAAVQNLLVALAVEGLGSCWIGstIFAADVVRA 410
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15596471 167 LLGLPPGSEAvavlcLGPVAEFYPAPMLALEgwsEPRPLAELV 209
Cdd:PRK13294 411 VLDLPADWEP-----LGAVAIGHPAEPPGPR---PPRDPGDFL 445
|
|
| nitroreductase |
cd02150 |
nitroreductase family protein; A subfamily of the nitroreductase family containing ... |
20-191 |
3.67e-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: 380325 [Multi-domain] Cd Length: 156 Bit Score: 59.15 E-value: 3.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 20 IAERRDMRHFSGGSVAPELLARLLEAAHQAPSVGLMQPWRFIRITEPALRRAIHGlVEEERGRTAEA------LGERSDE 93
Cdd:cd02150 1 ILTRRSIRKYTDKPVEEEDIEKLLRAAMAAPSAGNQQPWHFIVVTDREKLDKIAE-AHPYGKMLKEAplaivvCGDPSKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 94 fmrlKVEG--VLDCaellvaalmddrerhvfgrrtlpqmdlaslACAIQNLWLASRAEGLGMGWVSLF----DPAALGEL 167
Cdd:cd02150 80 ----KAPGywVQDC------------------------------SAATENILLAAHALGLGAVWLGVYpfeeRVKAIREI 125
|
170 180
....*....|....*....|....
gi 15596471 168 LGLPpgsEAVAVLCLGPVAefYPA 191
Cdd:cd02150 126 LNIP---ENIIPFCVIALG--YPA 144
|
|
| MhqN-like |
cd02137 |
nitroreductase family protein similar to the NAD(P)H nitroreductase MhqN; A diverse subfamily ... |
19-183 |
1.37e-10 |
|
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: 57.25 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 19 AIAERRDMRHFSGG-SVAPELLARLLEAAHQAPSVGLMQPWRFIRITEPALRRAIhglveeergrtAEALGERSdefmrl 97
Cdd:cd02137 3 VIKSRRSVRNFDPDhKIPKEELKEILELATLAPSSFNLQPWRFVVVRDPELKAKL-----------AEAAYNQP------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 98 KVEGvldcAELLVAalmddrerhVFGRRtlpqmdLASLACaiQNLWLASRAEGLGMGWVSLFDPAALGELLGLPPGSEAV 177
Cdd:cd02137 66 QVTT----ASAVIL---------VLGDL------NAGLAA--MNLMLAAKAKGYDTCPMGGFDKEKVAELLNLPDRYVPV 124
|
....*.
gi 15596471 178 AVLCLG 183
Cdd:cd02137 125 LLIAIG 130
|
|
| iodotyrosine_dehalogenase |
cd02144 |
iodotyrosine dehalogenase; Iodotyrosine dehalogenase catalyzes the removal of iodine from the ... |
16-79 |
1.66e-10 |
|
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: 57.93 E-value: 1.66e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596471 16 VYRAIAERRDMRHFSGGSVAPELLARLLEAAHQAPSVGLMQPWRFIRITEPALRRAIHGLVEEE 79
Cdd:cd02144 1 FYELMKKRRSVRDFSSEPVPREVIENAIRTAGTAPSGANTQPWTFVVVSDPEIKRKIREAAEEE 64
|
|
| nitroreductase |
cd03370 |
uncharacterized nitroreductase family proteins; Nitroreductase family containing Thermus ... |
19-187 |
3.18e-09 |
|
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: 54.63 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 19 AIAERRDMRHFSGGSVAPELLARLLEAAHQAPSVGLMQPWRFIRITEPALRRAIH------------------------- 73
Cdd:cd03370 4 AIESRRSIRKYTQEPVPDEDLREILRLAGLAPSAWNIQPWRFVVVRDAELKEQLQaaaygqaqvtsapaviviysdmeda 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 74 ----------GLVEEERGRTAEALgerSDEFMRlkvegvldcaellvaalMDDRERHVFGrrtlpqmdLASLACAIQNLW 143
Cdd:cd03370 84 lanleetihpGLSEERRQREAAGL---RGAFGK-----------------MSVEQRGQWG--------LAQANIALGFLL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15596471 144 LASRAEGLGMGWVSLFDPAALGELLGLPPGSEAVAVLCLGPVAE 187
Cdd:cd03370 136 LAAQSLGYDTSPMLGFDPEKVKALLGLPEHVTIAALVALGKPAE 179
|
|
| nitroreductase_FeS-like |
cd02143 |
nitroreductases with an N-terminal iron-sulfur cluster-binding domain; Members of this family ... |
23-191 |
8.81e-09 |
|
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: 53.25 E-value: 8.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 23 RRDMRHFSGGSVAPELLARLLEAAHQAPSVGLMQPWRFIRITEPALRRAIHGLVEEergRTAEALGERSDEFMRLKVEGV 102
Cdd:cd02143 5 RRSIRRYKDKPVPRETLEKLLDIARYAPTGHNSQPVHWLVVDDPEKVRRLAELVID---WMRELIKEDPELAGKLFLDGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 103 LDCAEL-----------LVAALMDDRERhvfgrrtLPQMDlASLACAiqNLWLASRAEGLGMGWVSLFDPAA-----LGE 166
Cdd:cd02143 82 VAAWEKgidvilrgaphLVVAHAPKDAP-------TPPVD-CAIALT--YLELAAPSLGLGTCWAGFFTAAAnnyppLRE 151
|
170 180
....*....|....*....|....*
gi 15596471 167 LLGLPPGSEAVAVLCLGpvaefYPA 191
Cdd:cd02143 152 ALGLPEGHKVGGAMMLG-----YPK 171
|
|
| nitroreductase |
cd02151 |
nitroreductase family protein; A subfamily of the nitroreductase family containing ... |
19-191 |
1.33e-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: 52.15 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 19 AIAERRDMRHFSGGSVAPELLARLLEAAHQAPSVGLMQPWRFIRITEPALRRAIhglveeergrtaealgERSDEFMRLK 98
Cdd:cd02151 2 LLKKRRSIRKYTDEPIEEEKLEEILEAALLAPSSRNSRPVEFIVVDDKETLKKL----------------SECKPHGSAF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 99 VEGvldcAELLVAALMDDRERHVFgrrtlpqMDLASLACAiqNLWLASRAEGLGMGWVSLFD-PAALG--------ELLG 169
Cdd:cd02151 66 LKG----APAAIVVLADTEKSDTW-------IEDASIAAT--YIQLAAESLGLGSCWIQIRNrETQDGktaeeyvrELLG 132
|
170 180
....*....|....*....|..
gi 15596471 170 LPPGSEAVAVLCLGpvaefYPA 191
Cdd:cd02151 133 IPENYRVLCIIALG-----YPD 149
|
|
| FbiB_C-like |
cd20607 |
nitroreductase family domain similar to the C-terminal domain of F420:gamma-glutamyl ligase ... |
56-191 |
2.36e-05 |
|
nitroreductase family domain similar to the C-terminal domain of F420:gamma-glutamyl ligase FbiB; 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. Mycobacterium tuberculosis FbiB, is a two-domain protein and produces F420 with predominantly 5 to 7 L-glutamate residues in the poly-gamma-glutamate tail, its C-terminal domain is homologous to FMN-dependent nitroreductases.
Pssm-ID: 380328 [Multi-domain] Cd Length: 155 Bit Score: 42.84 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 56 QPWRFIRITEPALRRA---------IHGLVEEerGRTAEALGERSDEFMRLKvegvlDCAELLVAALMDDRErHVF--GR 124
Cdd:cd20607 5 RPWRFVWLQDPAIRKElldrmadrwEADLTGD--GLTPEAIARRVSRGQILY-----DAPEVVIPFLVPDGA-HTYpdAR 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596471 125 RTLPQMDLASLA--CAIQNLWLASRAEGLGMGWVS--LFDPAALGELLGLPPGSEAvavlcLGPVAEFYPA 191
Cdd:cd20607 77 RTDAEHTMFTVAvgAAVQALLVALAVRGLGSCWIGstIFAPDVVRDELDLPDDWEP-----LGAIAIGYPL 142
|
|
| NfsB-like |
cd02149 |
nitroreductase similar to Escherichia coli NfsB; NAD(P)H:FMN oxidoreductase family. This ... |
33-183 |
1.86e-04 |
|
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: 40.31 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596471 33 SVAPELLARLLEAAHQAPSVGLMQPWRFIRITEPALRRAIHglveeergrtaealgeRSDEFMRLKVEgvlDCAEL-LVA 111
Cdd:cd02149 20 KISDEDLETILEALRLSPSSFGLEPWKFLVVENPELKAKLA----------------PAAWFNQPQIK---DASHVvVFL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596471 112 ALMDDRERHVFgrRTLPQMDL--ASL---ACAIqnlwlasraEGlgmgwvslFDPAALGELLGLPP-GSEAVAVLCLG 183
Cdd:cd02149 81 AKKDWSAKQTY--IALGNMLLaaAMLgidSCPI---------EG--------FDPAKLDEILGLDEkGYKISVMVAFG 139
|
|
| |
