|
Name |
Accession |
Description |
Interval |
E-value |
| BluB |
TIGR02476 |
5,6-dimethylbenzimidazole synthase; A previously published hypothesis that BluB, involved in ... |
6-208 |
1.42e-80 |
|
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: 239.26 E-value: 1.42e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 6 FPEADREAVYRAIAERRDMRHFSGGSVAPQLLHRLLQAAHQAPSVGLMQPWRFIRISDRNLRGQIQQLVEEERVRTAEAL 85
Cdd:TIGR02476 1 FSDAERAAVYRLIRERRDVRHFRSDPVPEAVLERLLDAAHHAPSVGFSQPWRFVRVESPATREAVHALFTRANQAAAAIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 86 -GERSDQFMKLKVEGINDCAEVLVAALMDDR-ERHIFGRRTLPEMDMASLSCAIQNLWLAARVEGLGMGWVSLFEPQALA 163
Cdd:TIGR02476 81 dGERASQYHRLKLEGIREAPVQLAVFCDDARgEGHGLGRHTMPEMLRYSVACAIQNLWLAARAEGLGVGWVSILDPDAVR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489303302 164 DLLGLPPGAKPLAVLCLGPVAEFYPAPMLQLEGWTEPRPLSDMLY 208
Cdd:TIGR02476 161 RLLGVPEGWRLVAYLCLGWPDAFYDEPELERAGWQERRPLEWRRY 205
|
|
| BluB |
cd02145 |
5,6-dimethylbenzimidazole synthase; BluB catalyzes the O2-dependent conversion of FMNH2 to 5, ... |
15-205 |
6.09e-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: 229.55 E-value: 6.09e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 15 YRAIAERRDMRHFSGGSVAPQLLHRLLQAAHQAPSVGLMQPWRFIRISDRNLRGQIQQLVEEERVRTAEAL-GERSDQFM 93
Cdd:cd02145 1 YRVIRWRRDVRHFRPDPVPEEVLERLLQAAHLAPSVGLMQPWRFVRVRSAATRKAVHELFQRANAEAAEMYtGERAAQYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 94 KLKVEGINDCAEVLVAALMDDRER-HIFGRRTLPEMDMASLSCAIQNLWLAARVEGLGMGWVSLFEPQALADLLGLPPGA 172
Cdd:cd02145 81 TLKLEGIEEAPLQLAVFCDRARAGgHGLGRTTMPEMDLYSSVCAVQNLWLAARAEGLGVGWVSILDPDEVKRLLGIPEHW 160
|
170 180 190
....*....|....*....|....*....|...
gi 489303302 173 KPLAVLCLGPVAEFYPAPMLQLEGWTEPRPLSD 205
Cdd:cd02145 161 EPVAYLCIGYPEFFYDEPELEQAGWEQRRPLEW 193
|
|
| NfnB |
COG0778 |
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ... |
14-195 |
2.22e-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: 138.06 E-value: 2.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 14 VYRAIAERRDMRHFSGGSVAPQLLHRLLQAAHQAPSVGLMQPWRFIRISDRNLRGQIQQLVEEERvrtaealgersdqfm 93
Cdd:COG0778 1 LLELLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEALAEAN--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 94 klkVEGINDCAEVLVAALmdDRERHifgRRTLPEMDMASLSCAIQNLWLAARVEGLGMGWVSLFEPQALADLLGLPPGAK 173
Cdd:COG0778 66 ---QEWVADAPVLIVVCA--DPDRS---EKVPERYALLDAGIAAQNLLLAARALGLGTCWIGGFDPEKVRELLGLPEGEE 137
|
170 180
....*....|....*....|...
gi 489303302 174 PLAVLCLG-PVAEFYPAPMLQLE 195
Cdd:COG0778 138 PVALLALGyPAEELNPRPRKPLE 160
|
|
| Nitroreductase |
pfam00881 |
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ... |
18-181 |
4.27e-32 |
|
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: 114.41 E-value: 4.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 18 IAERRDMRHFSGGSVAPQLLHRLLQAAHQAPSVGLMQPWRFIRISDRNLRGQIQ----QLVEEERVRTAEALGERSDQFM 93
Cdd:pfam00881 1 IRQRRSVRKFDPEPVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLAeaalELLLVEPAAALLLLLRRDANLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 94 KLKVEGINDCAEVLVAALMDDRERHIFGRRTLPEMdMASLSCAIQNLWLAARVEGLGMGWVSLFEPQALADLLGLPPGAK 173
Cdd:pfam00881 81 LLLQDFLRGAPVLIVITASLSTYLRKAAERAYREA-LLDAGAAAQNLLLAATSLGLGSCPIGGFDAAAVRELLGLPDDER 159
|
....*...
gi 489303302 174 PLAVLCLG 181
Cdd:pfam00881 160 LVGLIAVG 167
|
|
| PRK13294 |
PRK13294 |
F420-0--gamma-glutamyl ligase; Provisional |
2-209 |
1.44e-13 |
|
F420-0--gamma-glutamyl ligase; Provisional
Pssm-ID: 183957 [Multi-domain] Cd Length: 448 Bit Score: 68.50 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 2 TDNAFPEADREAVYRaiaeRRDMRHFSGGSVAPQLLHRLLQAAHQAPSVGLMQPWRFIRISDRNLRgqiQQLVEEERVRT 81
Cdd:PRK13294 245 TAEALELGRREAVLL----RRSVREFSDDPVDPEAVRRAVAAALTAPAPHHTRPVRFVWLRSAAVR---TRLLDAMRDAW 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 82 AEALgeRSDQFMKLKVEG-------INDCAEVLVAAL-MDDRERHIFGRRTLPEMDM--ASLSCAIQNLWLAARVEGLGM 151
Cdd:PRK13294 318 RADL--RADGLSEESIARrvrrgdiLYDAPELVVPFLvPDGAHSYPDARRTAAERTMftVAVGAAVQNLLVALAVEGLGS 395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489303302 152 GWVS--LFEPQALADLLGLPPGAKPLAVLCLG-PVAEFYPAPmlqlegwtePRPLSDMLYE 209
Cdd:PRK13294 396 CWIGstIFAADVVRAVLDLPADWEPLGAVAIGhPAEPPGPRP---------PRDPGDFLVE 447
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| BluB |
TIGR02476 |
5,6-dimethylbenzimidazole synthase; A previously published hypothesis that BluB, involved in ... |
6-208 |
1.42e-80 |
|
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: 239.26 E-value: 1.42e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 6 FPEADREAVYRAIAERRDMRHFSGGSVAPQLLHRLLQAAHQAPSVGLMQPWRFIRISDRNLRGQIQQLVEEERVRTAEAL 85
Cdd:TIGR02476 1 FSDAERAAVYRLIRERRDVRHFRSDPVPEAVLERLLDAAHHAPSVGFSQPWRFVRVESPATREAVHALFTRANQAAAAIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 86 -GERSDQFMKLKVEGINDCAEVLVAALMDDR-ERHIFGRRTLPEMDMASLSCAIQNLWLAARVEGLGMGWVSLFEPQALA 163
Cdd:TIGR02476 81 dGERASQYHRLKLEGIREAPVQLAVFCDDARgEGHGLGRHTMPEMLRYSVACAIQNLWLAARAEGLGVGWVSILDPDAVR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489303302 164 DLLGLPPGAKPLAVLCLGPVAEFYPAPMLQLEGWTEPRPLSDMLY 208
Cdd:TIGR02476 161 RLLGVPEGWRLVAYLCLGWPDAFYDEPELERAGWQERRPLEWRRY 205
|
|
| BluB |
cd02145 |
5,6-dimethylbenzimidazole synthase; BluB catalyzes the O2-dependent conversion of FMNH2 to 5, ... |
15-205 |
6.09e-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: 229.55 E-value: 6.09e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 15 YRAIAERRDMRHFSGGSVAPQLLHRLLQAAHQAPSVGLMQPWRFIRISDRNLRGQIQQLVEEERVRTAEAL-GERSDQFM 93
Cdd:cd02145 1 YRVIRWRRDVRHFRPDPVPEEVLERLLQAAHLAPSVGLMQPWRFVRVRSAATRKAVHELFQRANAEAAEMYtGERAAQYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 94 KLKVEGINDCAEVLVAALMDDRER-HIFGRRTLPEMDMASLSCAIQNLWLAARVEGLGMGWVSLFEPQALADLLGLPPGA 172
Cdd:cd02145 81 TLKLEGIEEAPLQLAVFCDRARAGgHGLGRTTMPEMDLYSSVCAVQNLWLAARAEGLGVGWVSILDPDEVKRLLGIPEHW 160
|
170 180 190
....*....|....*....|....*....|...
gi 489303302 173 KPLAVLCLGPVAEFYPAPMLQLEGWTEPRPLSD 205
Cdd:cd02145 161 EPVAYLCIGYPEFFYDEPELEQAGWEQRRPLEW 193
|
|
| NfnB |
COG0778 |
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ... |
14-195 |
2.22e-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: 138.06 E-value: 2.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 14 VYRAIAERRDMRHFSGGSVAPQLLHRLLQAAHQAPSVGLMQPWRFIRISDRNLRGQIQQLVEEERvrtaealgersdqfm 93
Cdd:COG0778 1 LLELLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEALAEAN--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 94 klkVEGINDCAEVLVAALmdDRERHifgRRTLPEMDMASLSCAIQNLWLAARVEGLGMGWVSLFEPQALADLLGLPPGAK 173
Cdd:COG0778 66 ---QEWVADAPVLIVVCA--DPDRS---EKVPERYALLDAGIAAQNLLLAARALGLGTCWIGGFDPEKVRELLGLPEGEE 137
|
170 180
....*....|....*....|...
gi 489303302 174 PLAVLCLG-PVAEFYPAPMLQLE 195
Cdd:COG0778 138 PVALLALGyPAEELNPRPRKPLE 160
|
|
| Nitroreductase |
pfam00881 |
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ... |
18-181 |
4.27e-32 |
|
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: 114.41 E-value: 4.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 18 IAERRDMRHFSGGSVAPQLLHRLLQAAHQAPSVGLMQPWRFIRISDRNLRGQIQ----QLVEEERVRTAEALGERSDQFM 93
Cdd:pfam00881 1 IRQRRSVRKFDPEPVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLAeaalELLLVEPAAALLLLLRRDANLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 94 KLKVEGINDCAEVLVAALMDDRERHIFGRRTLPEMdMASLSCAIQNLWLAARVEGLGMGWVSLFEPQALADLLGLPPGAK 173
Cdd:pfam00881 81 LLLQDFLRGAPVLIVITASLSTYLRKAAERAYREA-LLDAGAAAQNLLLAATSLGLGSCPIGGFDAAAVRELLGLPDDER 159
|
....*...
gi 489303302 174 PLAVLCLG 181
Cdd:pfam00881 160 LVGLIAVG 167
|
|
| Nitro_FMN_reductase |
cd02062 |
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ... |
18-181 |
1.99e-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: 93.52 E-value: 1.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 18 IAERRDMRHFSGGSVAPQLLHRLLQAAHQAPSVGLMQPWRFIRISDRNLRGQIqqlveeervrtaEALGERSDQFMKlkv 97
Cdd:cd02062 1 IKTRRSIRKFTDKPVPEEKLRKILEAARLAPSAGNLQPWRFIVVRDREKKEKL------------AKLAAPNQKFIA--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 98 egindCAEVLVAALMDDRErhifgrrtLPEMDMASLSCAIQNLWLAARVEGLGMGWVSLF--EPQALADLLGLPPGAKPL 175
Cdd:cd02062 66 -----GAPVVIVVVADPDK--------SRPWALEDAGAAAQNLLLAAAALGLGSCWIGGFdfREDKVRELLGIPENLRPV 132
|
....*.
gi 489303302 176 AVLCLG 181
Cdd:cd02062 133 ALIAIG 138
|
|
| YdjA-like |
cd02135 |
nitroreductase family protein similar to Escherichia coli YdjA; A subfamily of the ... |
17-181 |
3.28e-22 |
|
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: 88.43 E-value: 3.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 17 AIAERRDMRHFS-GGSVAPQLLHRLLQAAHQAPSVGLMQPWRFIRISDRNLRGQIQQLVEEERVRTAEALGERSDQFMKL 95
Cdd:cd02135 3 LIKTRRSIRKFKlTGAPPEEQLEELLEAAMWAPNHGKLEPWRFIVVTGEGRERLAELLAAAAAARAPGADPEKLEKAREK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 96 KVEgindcAEVLVAALMDDRERHifgrrTLPEM-DMASLSCAIQNLWLAARVEGLGMGWVS---LFEPqALADLLGLPPG 171
Cdd:cd02135 83 ALR-----APVVIAVVAKPDEDP-----KVPEWeQYAAVGAAVQNLLLAAHALGLGAVWRTgpvTYDP-AVREALGLPED 151
|
170
....*....|
gi 489303302 172 AKPLAVLCLG 181
Cdd:cd02135 152 ERIVGFLYLG 161
|
|
| nitroreductase |
cd02139 |
nitroreductase family protein; A subfamily of the nitroreductase family containing ... |
14-210 |
2.26e-19 |
|
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: 81.36 E-value: 2.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 14 VYRAIAERRDMRHFSGGSVAPQLLHRLLQAAHQAPSVGLMQPWRFIRISDRNLRgqiQQLVEEerVRTAEALGErsdqfm 93
Cdd:cd02139 1 VYEAIKKRRSIRKYKPTPVEEEKLLRILEAARLAPSAKNRQPWRFIVVKDKELK---EKLAEA--ANGQKFIAE------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 94 klkvegindcAEVLVAALMDDRERhifGRRTLPEMDMASLSCAIQNLWLAARVEGLGMGWVSLFEPQALADLLGLPPGAK 173
Cdd:cd02139 70 ----------APVVIVACADPSES---GMGCGKPYYLVDVAIAMEHLVLAATEEGLGTCWIGAFDEDKVKEILGIPEEYR 136
|
170 180 190
....*....|....*....|....*....|....*..
gi 489303302 174 PLAVLCLGPVAEfYPAPmlqlegwTEPRPLSDMLYEN 210
Cdd:cd02139 137 VVALTPLGYPAE-EPPP-------RPRKPLEEIVFYE 165
|
|
| nitroreductase |
cd20608 |
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ... |
17-181 |
4.49e-19 |
|
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or nitrocompounds using NAD(P)H as electron donor in a obligatory two-electron transfer, utilizing FMN or FAD as cofactor. They are often found to be homodimers. Enzymes of this family are described as NAD(P)H:FMN oxidoreductases, oxygen-insensitive nitroreductase, flavin reductase P, dihydropteridine reductase, NADH oxidase or NADH dehydrogenase.
Pssm-ID: 380329 [Multi-domain] Cd Length: 145 Bit Score: 80.07 E-value: 4.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 17 AIAERRDMRHFSGGSVAPQLLHRLLQAAHQAPSVGLMQPWRFIRISDRnlrgqiqqlveeervRTAEALGERSDQFMKLK 96
Cdd:cd20608 3 AIKTRRSVRRFSDKPVEEEKLEKILEAARLAPSWANKQCWRFIVVTDK---------------ETLSELAKKESPSNGWL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 97 VEgindcAEVLVAALMDDRERhifGRRTLPEMDMASLSCAIQNLWLAARVEGLGMGWVSLFEPQALADLLGLPPGAKPLA 176
Cdd:cd20608 68 KD-----APVIIVVCADPKDS---GWLNGQNYYLVDAAIAMQNLMLAATDLGLGTCWIGAFDEKKVKEILGIPENIRVVA 139
|
....*
gi 489303302 177 VLCLG 181
Cdd:cd20608 140 LTPLG 144
|
|
| nitroreductase |
cd02150 |
nitroreductase family protein; A subfamily of the nitroreductase family containing ... |
18-189 |
2.09e-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: 380325 [Multi-domain] Cd Length: 156 Bit Score: 70.32 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 18 IAERRDMRHFSGGSVAPQLLHRLLQAAHQAPSVGLMQPWRFIRISDRNLRGQIqqlveeervrtAEALgersdQFMKLKV 97
Cdd:cd02150 1 ILTRRSIRKYTDKPVEEEDIEKLLRAAMAAPSAGNQQPWHFIVVTDREKLDKI-----------AEAH-----PYGKMLK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 98 EgiNDCAeVLVAAlmdDRErhifgRRTLPEMDMASLSCAIQNLWLAARVEGLGMGWVSLF----EPQALADLLGLPPGAK 173
Cdd:cd02150 65 E--APLA-IVVCG---DPS-----KEKAPGYWVQDCSAATENILLAAHALGLGAVWLGVYpfeeRVKAIREILNIPENII 133
|
170
....*....|....*.
gi 489303302 174 PLAVLCLGpvaefYPA 189
Cdd:cd02150 134 PFCVIALG-----YPA 144
|
|
| nitroreductase |
cd20610 |
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ... |
18-181 |
5.23e-15 |
|
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: 69.61 E-value: 5.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 18 IAERRDMRHFSGGSVAPQLLHRLLQAAHQAPSVGLMQPWRFIRISDrnlrGQIQQLVEEERVRTAEALGERSDQFMKLKV 97
Cdd:cd20610 1 IKKRRSIRKFKPDPVPKEDIEKILEAANWAPSGMNRQNWEFVVVKG----GEKIEKIGISIKKKNEEIARLLEKVFAEKP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 98 EGI---------NDCAEVLVAALMDDRERhIFGRRTlpemDMASLSCAIQNLWLAARVEGLGMGWVS--LFEPQALADLL 166
Cdd:cd20610 77 IRFrkfrrfftlFGGAPVLVVVYTEPYKP-PEERKP----DLQSVSAAIQNLLLAAHALGLGTCWMTgpLYAEDEIEEIL 151
|
170
....*....|....*
gi 489303302 167 GLPPGAKPLAVLCLG 181
Cdd:cd20610 152 EIPDDKELVAVTPLG 166
|
|
| PnbA_NfnB-like |
cd02136 |
nitroreductase similar to Mycobacterium smegmatis NfnB; Members of this family utilize FMN as ... |
17-190 |
2.89e-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: 67.23 E-value: 2.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 17 AIAERRDMRHFSGGSVAPQLLHRLLQAAHQAPSVGLMQPWRFIRISDRNLrgqiqqlveeERVRTAealgersdQFMklk 96
Cdd:cd02136 1 AIKSRRSVRAFKDKPVPKETIEKILEAARRAPSGKNTQPWRVYVVTGKAR----------ERLKKA--------FFG--- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 97 vegindcAEVLVAALMDdrerhifgrRTLPEMDMASLSCAIQNLWLAARVEGLGMGWVSLF--EPQALADLLGLPPGAKP 174
Cdd:cd02136 60 -------APVALFLTMD---------KVLGPWSWFDLGAFLQNLMLAAHALGLGTCPQGALagYPDVVRKELGIPDDEEL 123
|
170
....*....|....*.
gi 489303302 175 LAVLCLGpvaefYPAP 190
Cdd:cd02136 124 VCGIALG-----YPDP 134
|
|
| NfsA-like |
cd02146 |
nitroreductase similar to Escherichia coli NfsA; This family contains NADPH-dependent flavin ... |
21-212 |
2.96e-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: 68.80 E-value: 2.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 21 RRDMRHFSGGSVAPQLLHRLLQAAHQAPSVGLMQPWRFIRISDRNLRGQIQQLveeervrtaeALGERSdqfmklkvegI 100
Cdd:cd02146 8 HRSVRKFTDEPLTDETLETLIAAAQSASTSSNLQAYSVIVVTDPELREKLAEL----------AGNQPY----------V 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 101 NDCAEVLVaALMD--------DRERHIFGRRTLPEMDMASL---SCAIQNLWLAArvEGLGMGWVSL----FEPQALADL 165
Cdd:cd02146 68 AQAPVFLV-FCADlyrhqkiaEEAGGKDVGLDYLESFLVGVvdaALAAQNALVAA--ESLGLGIVYIggirNNPEEVIEL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489303302 166 LGLPPGAKPLAVLCLGpvaefYPAPMLQLegwtEPR-PLSDMLYENVW 212
Cdd:cd02146 145 LGLPEYVFPLFGLTVG-----HPDPTPEV----KPRlPLEAVVHEETY 183
|
|
| PRK13294 |
PRK13294 |
F420-0--gamma-glutamyl ligase; Provisional |
2-209 |
1.44e-13 |
|
F420-0--gamma-glutamyl ligase; Provisional
Pssm-ID: 183957 [Multi-domain] Cd Length: 448 Bit Score: 68.50 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 2 TDNAFPEADREAVYRaiaeRRDMRHFSGGSVAPQLLHRLLQAAHQAPSVGLMQPWRFIRISDRNLRgqiQQLVEEERVRT 81
Cdd:PRK13294 245 TAEALELGRREAVLL----RRSVREFSDDPVDPEAVRRAVAAALTAPAPHHTRPVRFVWLRSAAVR---TRLLDAMRDAW 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 82 AEALgeRSDQFMKLKVEG-------INDCAEVLVAAL-MDDRERHIFGRRTLPEMDM--ASLSCAIQNLWLAARVEGLGM 151
Cdd:PRK13294 318 RADL--RADGLSEESIARrvrrgdiLYDAPELVVPFLvPDGAHSYPDARRTAAERTMftVAVGAAVQNLLVALAVEGLGS 395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489303302 152 GWVS--LFEPQALADLLGLPPGAKPLAVLCLG-PVAEFYPAPmlqlegwtePRPLSDMLYE 209
Cdd:PRK13294 396 CWIGstIFAADVVRAVLDLPADWEPLGAVAIGhPAEPPGPRP---------PRDPGDFLVE 447
|
|
| nitroreductase |
cd20609 |
nitroreductase family protein; A subfamily of the nitroreductase family containing ... |
18-181 |
2.68e-12 |
|
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: 62.02 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 18 IAERRDMRHFSGGSVAPQLLHRLLQAAHQAPSVGLMQPWRFIrisdrnlrgqiqqlVeeerVRTAEALgersdqfmklkv 97
Cdd:cd20609 6 AKKRYSVRKFSDKPVEKEKLDKILEAGRLAPTAVNYQPQRIL--------------V----VRSEEAL------------ 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 98 EGINDCAE--------VLVAALMDDRERHIFGRRTLPEMDmasLSCAIQNLWLAARVEGLGMGWVSLFEPQALADLLGLP 169
Cdd:cd20609 56 EKLAKATPrffgaplvIVVCYDKDESWKRPYDGKDSGDID---AAIVATHMMLAATELGLGTCWVGNFDPEKVREAFNLP 132
|
170
....*....|..
gi 489303302 170 PGAKPLAVLCLG 181
Cdd:cd20609 133 ENLEPVAILPLG 144
|
|
| PRK10765 |
PRK10765 |
oxygen-insensitive NADPH nitroreductase; |
18-210 |
5.89e-12 |
|
oxygen-insensitive NADPH nitroreductase;
Pssm-ID: 182710 Cd Length: 240 Bit Score: 62.68 E-value: 5.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 18 IAERRDMRHFSGGSVAPQLLHRLLQAAHQAPSVGLMQPWRFIRISDRNLRGQI------QQLVEEervrtaealgersdq 91
Cdd:PRK10765 8 ILSHRSIRHFTDEPISEAQREAIINAARAASSSSFLQCSSIIRITDKALREALveltggQKYVAQ--------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 92 fmklkvegindCAEVLVAALmdDRERHifgRRTLPE--MDMASLS------CAI--QNLWLAArvEGLGMGWVSL----F 157
Cdd:PRK10765 73 -----------AAEFWVFCA--DFNRH---LQICPDaqLGLAEQLligavdTAImaQNALLAA--ESLGLGGVYIgglrN 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489303302 158 EPQALADLLGLPPGAKPLAVLCLGpvaefYPAPMLQLegwtEPR-PLSDMLYEN 210
Cdd:PRK10765 135 NIEAVTELLKLPQHVLPLFGLCLG-----WPAQNPDL----KPRlPASLLVHEN 179
|
|
| TdsD-like |
cd02138 |
nitroreductase similar to Burkholderia pseudomallei TdsD; A subfamily of the nitroreductase ... |
17-208 |
6.79e-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: 61.41 E-value: 6.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 17 AIAERRDMRHFSGGSVAPQLLHRLLQAAHQAPSVGLMQPWRFIrISDRNlrgqiqqlvEEERVRTAEALGERSDQFMKlk 96
Cdd:cd02138 1 LIAERWSPRAFSPEPISEEDLLSLFEAARWAPSCFNEQPWRFV-VARRD---------TEAFEKLLDLLAEGNQSWAK-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 97 vegindCAEVLVAAL-MDDRERHIFGRRTlpemdmASLSC--AIQNLWLAARVEGL---GMGwvsLFEPQALADLLGLPP 170
Cdd:cd02138 69 ------NAPVLIVVLaKTEFDHNGKPNRY------ALFDTgaAVANLALQATALGLvvhQMA---GFDPEKAKEALGIPD 133
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489303302 171 GAKPLAVLCLGPVAEFYPAPMLQLEGWTEPR---PLSDMLY 208
Cdd:cd02138 134 EYEPITMIAIGYPGDPESLPEKLLEREEAPRtrkPLSEIVF 174
|
|
| iodotyrosine_dehalogenase |
cd02144 |
iodotyrosine dehalogenase; Iodotyrosine dehalogenase catalyzes the removal of iodine from the ... |
14-206 |
1.32e-11 |
|
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: 61.01 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 14 VYRAIAERRDMRHFSGGSVAPQLLHRLLQAAHQAPSVGLMQPWRFIRISDRNLRGQIQQLVE-EERVRTAEalgERSDQF 92
Cdd:cd02144 1 FYELMKKRRSVRDFSSEPVPREVIENAIRTAGTAPSGANTQPWTFVVVSDPEIKRKIREAAEeEEKEFYEK---RMGEEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 93 MK-LKVEGIN------DCAEVLVAalmddrerhIFGRRTLPEMDMASLSC--AIQNLWLAArveglGM--------GWVS 155
Cdd:cd02144 78 VWdLKPLGTNwekpylTEAPYLIV---------VFKQKYGVLPDGKKKKHyyNEESVGIAV-----GIllaalhnaGLVT 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489303302 156 L----FEPQALADLLGLPPGAKPLAVLclgPVAefYPApmlqlEGWTEP----RPLSDM 206
Cdd:cd02144 144 LthtpSPMPFLRDLLGRPKNEKPLLLL---PVG--YPA-----EDATVPdlkrKPLEEI 192
|
|
| MhqN-like |
cd02137 |
nitroreductase family protein similar to the NAD(P)H nitroreductase MhqN; A diverse subfamily ... |
17-181 |
4.99e-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: 55.71 E-value: 4.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 17 AIAERRDMRHFSGG-SVAPQLLHRLLQAAHQAPSVGLMQPWRFIRISDRNLRGQIQQLV-EEERVRTAEALgersdqfmk 94
Cdd:cd02137 3 VIKSRRSVRNFDPDhKIPKEELKEILELATLAPSSFNLQPWRFVVVRDPELKAKLAEAAyNQPQVTTASAV--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 95 lkvegindcaeVLVAALMDdrerhifgrrtlpemdmASLscAIQNLWLAARVEGLGMGWVSLFEPQALADLLGLPPGAKP 174
Cdd:cd02137 74 -----------ILVLGDLN-----------------AGL--AAMNLMLAAKAKGYDTCPMGGFDKEKVAELLNLPDRYVP 123
|
....*..
gi 489303302 175 LAVLCLG 181
Cdd:cd02137 124 VLLIAIG 130
|
|
| nitroreductase |
cd02151 |
nitroreductase family protein; A subfamily of the nitroreductase family containing ... |
17-189 |
2.84e-09 |
|
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: 54.08 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 17 AIAERRDMRHFSGGSVAPQLLHRLLQAAHQAPSVGLMQPWRFIRISDRNLrgqIQQLveeervrtaealgERSDQFMKLK 96
Cdd:cd02151 2 LLKKRRSIRKYTDEPIEEEKLEEILEAALLAPSSRNSRPVEFIVVDDKET---LKKL-------------SECKPHGSAF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 97 VEGINdcAEVLVAALMDDRERHIfgrrtlpEmDmASLSCAiqNLWLAARVEGLGMGWVSLFE---------PQALADLLG 167
Cdd:cd02151 66 LKGAP--AAIVVLADTEKSDTWI-------E-D-ASIAAT--YIQLAAESLGLGSCWIQIRNretqdgktaEEYVRELLG 132
|
170 180
....*....|....*....|..
gi 489303302 168 LPPGAKPLAVLCLGpvaefYPA 189
Cdd:cd02151 133 IPENYRVLCIIALG-----YPD 149
|
|
| nitroreductase |
cd03370 |
uncharacterized nitroreductase family proteins; Nitroreductase family containing Thermus ... |
17-185 |
1.34e-08 |
|
uncharacterized nitroreductase family proteins; Nitroreductase family containing Thermus thermophilus NADH oxidase and other, uncharacterized proteins. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer.
Pssm-ID: 380327 [Multi-domain] Cd Length: 191 Bit Score: 52.71 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 17 AIAERRDMRHFSGGSVAPQLLHRLLQAAHQAPSVGLMQPWRFIRISDRNLRGQIQQLV-EEERVRTAEA-LGERSDqfMK 94
Cdd:cd03370 4 AIESRRSIRKYTQEPVPDEDLREILRLAGLAPSAWNIQPWRFVVVRDAELKEQLQAAAyGQAQVTSAPAvIVIYSD--ME 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 95 lkvEGINDCAEVLVAALMDDRE-------RHIFGRRTLPEMD---MASLSCAIQNLWLAARveGLGMGWVSL--FEPQAL 162
Cdd:cd03370 82 ---DALANLEETIHPGLSEERRqreaaglRGAFGKMSVEQRGqwgLAQANIALGFLLLAAQ--SLGYDTSPMlgFDPEKV 156
|
170 180
....*....|....*....|...
gi 489303302 163 ADLLGLPPGAKPLAVLCLGPVAE 185
Cdd:cd03370 157 KALLGLPEHVTIAALVALGKPAE 179
|
|
| FbiB_C-like |
cd20607 |
nitroreductase family domain similar to the C-terminal domain of F420:gamma-glutamyl ligase ... |
54-189 |
2.71e-07 |
|
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: 48.62 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 54 QPWRFIRISDRnlrGQIQQLVEEERVR----------TAEALGERSDQFMKLKveginDCAEVLVAALMDDRErHIF--G 121
Cdd:cd20607 5 RPWRFVWLQDP---AIRKELLDRMADRweadltgdglTPEAIARRVSRGQILY-----DAPEVVIPFLVPDGA-HTYpdA 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489303302 122 RRTLPEMDMASLS--CAIQNLWLAARVEGLGMGWVS--LFEPQALADLLGLPPGAKPlavlcLGPVAEFYPA 189
Cdd:cd20607 76 RRTDAEHTMFTVAvgAAVQALLVALAVRGLGSCWIGstIFAPDVVRDELDLPDDWEP-----LGAIAIGYPL 142
|
|
| nitroreductase_FeS-like |
cd02143 |
nitroreductases with an N-terminal iron-sulfur cluster-binding domain; Members of this family ... |
21-189 |
3.33e-07 |
|
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: 48.62 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 21 RRDMRHFSGGSVAPQLLHRLLQAAHQAPSVGLMQPWRFIRISDRNlrgQIQQLVeEERVRTAEALGERSDQF-MKLKVEG 99
Cdd:cd02143 5 RRSIRRYKDKPVPRETLEKLLDIARYAPTGHNSQPVHWLVVDDPE---KVRRLA-ELVIDWMRELIKEDPELaGKLFLDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303302 100 INDCAE-----------VLVAALMDDrerhifgrrtlpEMDMASLSCAI--QNLWLAARVEGLGMGW-------VSLFEP 159
Cdd:cd02143 81 IVAAWEkgidvilrgapHLVVAHAPK------------DAPTPPVDCAIalTYLELAAPSLGLGTCWagfftaaANNYPP 148
|
170 180 190
....*....|....*....|....*....|
gi 489303302 160 qaLADLLGLPPGAKPLAVLCLGpvaefYPA 189
Cdd:cd02143 149 --LREALGLPEGHKVGGAMMLG-----YPK 171
|
|
| |
