|
Name |
Accession |
Description |
Interval |
E-value |
| nitroreductase |
cd20610 |
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ... |
7-190 |
1.17e-79 |
|
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: 235.25 E-value: 1.17e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 7 IYKRHSVRKFKDVSVPIEDIHKIIEAATFAPSGKNIQNWRFVVISNKEKIKQIANIIENKNADLATHLEN--EEEKVKFT 84
Cdd:cd20610 1 IKKRRSIRKFKPDPVPKEDIEKILEAANWAPSGMNRQNWEFVVVKGGEKIEKIGISIKKKNEEIARLLEKvfAEKPIRFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 85 KFVKYATFFTKAPVLILVYAGPYEatgldvlkkikaptdeihDLLKRSPLIQSVGAAMENIMLSATHLGYGTCWMTSQNY 164
Cdd:cd20610 81 KFRRFFTLFGGAPVLVVVYTEPYK------------------PPEERKPDLQSVSAAIQNLLLAAHALGLGTCWMTGPLY 142
|
170 180
....*....|....*....|....*.
gi 928931667 165 AAKEIEDFVGFkEEGYFLAAMTPLGV 190
Cdd:cd20610 143 AEDEIEEILEI-PDDKELVAVTPLGY 167
|
|
| NfnB |
COG0778 |
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ... |
4-206 |
5.03e-47 |
|
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway/BioSystem: Pyrimidine degradation
Pssm-ID: 440541 [Multi-domain] Cd Length: 163 Bit Score: 152.31 E-value: 5.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 4 LDFIYKRHSVRKFKDVSVPIEDIHKIIEAATFAPSGKNIQNWRFVVISNKEKIKQIANIIENKNADlathleneeekvkf 83
Cdd:COG0778 2 LELLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEALAEANQE-------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 84 tkfvkyatFFTKAPVLILVYAGPYEATgldvlkkiKAPTDEIHdllkrspliQSVGAAMENIMLSATHLGYGTCWMTSqn 163
Cdd:COG0778 68 --------WVADAPVLIVVCADPDRSE--------KVPERYAL---------LDAGIAAQNLLLAARALGLGTCWIGG-- 120
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 928931667 164 YAAKEIEDFVGFkEEGYFLAAMTPLGVPDGEPKSPSRKPIQEV 206
Cdd:COG0778 121 FDPEKVRELLGL-PEGEEPVALLALGYPAEELNPRPRKPLEEV 162
|
|
| Nitroreductase |
pfam00881 |
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ... |
7-189 |
8.97e-39 |
|
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: 131.36 E-value: 8.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 7 IYKRHSVRKFKDVSVPIEDIHKIIEAATFAPSGKNIQNWRFVVISNKEKIKQIANIIENKNADLATHLENEEEKVKFTKF 86
Cdd:pfam00881 1 IRQRRSVRKFDPEPVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLAEAALELLLVEPAAALLLLLRRDANLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 87 VKYATFFTKAPVLILVyagpyeaTGLDVLKKIKAPTDEIHDLLKrspliqSVGAAMENIMLSATHLGYGTCWMTSQNYAA 166
Cdd:pfam00881 81 LLLQDFLRGAPVLIVI-------TASLSTYLRKAAERAYREALL------DAGAAAQNLLLAATSLGLGSCPIGGFDAAA 147
|
170 180
....*....|....*....|...
gi 928931667 167 keIEDFVGFkEEGYFLAAMTPLG 189
Cdd:pfam00881 148 --VRELLGL-PDDERLVGLIAVG 167
|
|
| BluB |
TIGR02476 |
5,6-dimethylbenzimidazole synthase; A previously published hypothesis that BluB, involved in ... |
4-198 |
1.41e-07 |
|
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: 49.75 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 4 LDFIYKRHSVRKFKDVSVPIEDIHKIIEAATFAPSGKNIQNWRFVVISNKEKIKQIANIIENKNADLATHLENEEEKVkf 83
Cdd:TIGR02476 10 YRLIRERRDVRHFRSDPVPEAVLERLLDAAHHAPSVGFSQPWRFVRVESPATREAVHALFTRANQAAAAIYDGERASQ-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 84 tkfvkYATF----FTKAPVLILVYAGPYEATGldvlkkikaptdeiHDLLKRS-P--LIQSVGAAMENIMLSATHLGYGT 156
Cdd:TIGR02476 88 -----YHRLklegIREAPVQLAVFCDDARGEG--------------HGLGRHTmPemLRYSVACAIQNLWLAARAEGLGV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 928931667 157 CWMTSqnYAAKEIEDFVGFKeEGYFLAAMTPLGVPDGEPKSP 198
Cdd:TIGR02476 149 GWVSI--LDPDAVRRLLGVP-EGWRLVAYLCLGWPDAFYDEP 187
|
|
| PRK11053 |
PRK11053 |
oxygen-insensitive NAD(P)H nitroreductase; |
1-60 |
7.59e-05 |
|
oxygen-insensitive NAD(P)H nitroreductase;
Pssm-ID: 182929 [Multi-domain] Cd Length: 217 Bit Score: 42.27 E-value: 7.59e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 928931667 1 MKNLDFIYKRHSVRKFkDVS--VPIEDIHKIIEAATFAPSGKNIQNWRFVVISNKEKIKQIA 60
Cdd:PRK11053 1 MDIVSVAKKRYTTKAF-DPSkkLPAEQIEQIKTLLRFSPSSVNSQPWHFIVASTEEGKARIA 61
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| nitroreductase |
cd20610 |
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ... |
7-190 |
1.17e-79 |
|
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: 235.25 E-value: 1.17e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 7 IYKRHSVRKFKDVSVPIEDIHKIIEAATFAPSGKNIQNWRFVVISNKEKIKQIANIIENKNADLATHLEN--EEEKVKFT 84
Cdd:cd20610 1 IKKRRSIRKFKPDPVPKEDIEKILEAANWAPSGMNRQNWEFVVVKGGEKIEKIGISIKKKNEEIARLLEKvfAEKPIRFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 85 KFVKYATFFTKAPVLILVYAGPYEatgldvlkkikaptdeihDLLKRSPLIQSVGAAMENIMLSATHLGYGTCWMTSQNY 164
Cdd:cd20610 81 KFRRFFTLFGGAPVLVVVYTEPYK------------------PPEERKPDLQSVSAAIQNLLLAAHALGLGTCWMTGPLY 142
|
170 180
....*....|....*....|....*.
gi 928931667 165 AAKEIEDFVGFkEEGYFLAAMTPLGV 190
Cdd:cd20610 143 AEDEIEEILEI-PDDKELVAVTPLGY 167
|
|
| NfnB |
COG0778 |
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ... |
4-206 |
5.03e-47 |
|
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway/BioSystem: Pyrimidine degradation
Pssm-ID: 440541 [Multi-domain] Cd Length: 163 Bit Score: 152.31 E-value: 5.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 4 LDFIYKRHSVRKFKDVSVPIEDIHKIIEAATFAPSGKNIQNWRFVVISNKEKIKQIANIIENKNADlathleneeekvkf 83
Cdd:COG0778 2 LELLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEALAEANQE-------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 84 tkfvkyatFFTKAPVLILVYAGPYEATgldvlkkiKAPTDEIHdllkrspliQSVGAAMENIMLSATHLGYGTCWMTSqn 163
Cdd:COG0778 68 --------WVADAPVLIVVCADPDRSE--------KVPERYAL---------LDAGIAAQNLLLAARALGLGTCWIGG-- 120
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 928931667 164 YAAKEIEDFVGFkEEGYFLAAMTPLGVPDGEPKSPSRKPIQEV 206
Cdd:COG0778 121 FDPEKVRELLGL-PEGEEPVALLALGYPAEELNPRPRKPLEEV 162
|
|
| Nitroreductase |
pfam00881 |
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ... |
7-189 |
8.97e-39 |
|
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: 131.36 E-value: 8.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 7 IYKRHSVRKFKDVSVPIEDIHKIIEAATFAPSGKNIQNWRFVVISNKEKIKQIANIIENKNADLATHLENEEEKVKFTKF 86
Cdd:pfam00881 1 IRQRRSVRKFDPEPVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLAEAALELLLVEPAAALLLLLRRDANLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 87 VKYATFFTKAPVLILVyagpyeaTGLDVLKKIKAPTDEIHDLLKrspliqSVGAAMENIMLSATHLGYGTCWMTSQNYAA 166
Cdd:pfam00881 81 LLLQDFLRGAPVLIVI-------TASLSTYLRKAAERAYREALL------DAGAAAQNLLLAATSLGLGSCPIGGFDAAA 147
|
170 180
....*....|....*....|...
gi 928931667 167 keIEDFVGFkEEGYFLAAMTPLG 189
Cdd:pfam00881 148 --VRELLGL-PDDERLVGLIAVG 167
|
|
| nitroreductase |
cd02139 |
nitroreductase family protein; A subfamily of the nitroreductase family containing ... |
4-206 |
4.02e-38 |
|
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: 129.51 E-value: 4.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 4 LDFIYKRHSVRKFKDVSVPIEDIHKIIEAATFAPSGKNIQNWRFVVISNKEKIKQIANIIENKNadlathleneeekvkf 83
Cdd:cd02139 2 YEAIKKRRSIRKYKPTPVEEEKLLRILEAARLAPSAKNRQPWRFIVVKDKELKEKLAEAANGQK---------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 84 tkfvkyatFFTKAPVLILVYAGPYEATGLDVlkkikaptdeihdllKRSPLIqSVGAAMENIMLSATHLGYGTCWMTSqn 163
Cdd:cd02139 66 --------FIAEAPVVIVACADPSESGMGCG---------------KPYYLV-DVAIAMEHLVLAATEEGLGTCWIGA-- 119
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 928931667 164 YAAKEIEDFVGFKEEgYFLAAMTPLGVPDGEPKSPSRKPIQEV 206
Cdd:cd02139 120 FDEDKVKEILGIPEE-YRVVALTPLGYPAEEPPPRPRKPLEEI 161
|
|
| Nitro_FMN_reductase |
cd02062 |
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ... |
7-189 |
2.45e-34 |
|
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: 118.94 E-value: 2.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 7 IYKRHSVRKFKDVSVPIEDIHKIIEAATFAPSGKNIQNWRFVVISNKEKIKQIANIIEnknadlathleneeekvkftkf 86
Cdd:cd02062 1 IKTRRSIRKFTDKPVPEEKLRKILEAARLAPSAGNLQPWRFIVVRDREKKEKLAKLAA---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 87 vKYATFFTKAPVLILVYAGPYEAtgldvlkkikaptdeihdllkRSPLIQSVGAAMENIMLSATHLGYGTCWMTSQNYAA 166
Cdd:cd02062 59 -PNQKFIAGAPVVIVVVADPDKS---------------------RPWALEDAGAAAQNLLLAAAALGLGSCWIGGFDFRE 116
|
170 180
....*....|....*....|...
gi 928931667 167 KEIEDFVGFkEEGYFLAAMTPLG 189
Cdd:cd02062 117 DKVRELLGI-PENLRPVALIAIG 138
|
|
| PnbA_NfnB-like |
cd02136 |
nitroreductase similar to Mycobacterium smegmatis NfnB; Members of this family utilize FMN as ... |
7-206 |
9.94e-30 |
|
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: 107.67 E-value: 9.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 7 IYKRHSVRKFKDVSVPIEDIHKIIEAATFAPSGKNIQNWRFVVISNK--EKIKQIaniienknadlathleneeekvkft 84
Cdd:cd02136 2 IKSRRSVRAFKDKPVPKETIEKILEAARRAPSGKNTQPWRVYVVTGKarERLKKA------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 85 kfvkyatFFTkAPVLILVYagpyeatgldvLKKIKAPTDeihdllkrsplIQSVGAAMENIMLSATHLGYGTCWmtsQNY 164
Cdd:cd02136 57 -------FFG-APVALFLT-----------MDKVLGPWS-----------WFDLGAFLQNLMLAAHALGLGTCP---QGA 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 928931667 165 AAK---EIEDFVGFKEEGYFLAAMtPLGVPDGE----PKSPSRKPIQEV 206
Cdd:cd02136 104 LAGypdVVRKELGIPDDEELVCGI-ALGYPDPDapvnQFRTPREPLEEF 151
|
|
| nitroreductase |
cd02150 |
nitroreductase family protein; A subfamily of the nitroreductase family containing ... |
7-200 |
3.08e-28 |
|
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: 103.83 E-value: 3.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 7 IYKRHSVRKFKDVSVPIEDIHKIIEAATFAPSGKNIQNWRFVVISNKEKIKQIAniienknadlathleneeekvkftKF 86
Cdd:cd02150 1 ILTRRSIRKYTDKPVEEEDIEKLLRAAMAAPSAGNQQPWHFIVVTDREKLDKIA------------------------EA 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 87 VKYATFFTKAPVLILVYAGPyeatgldvlkkikaptdeihDLLKRSPL-IQSVGAAMENIMLSATHLGYGTCWMtsqnyA 165
Cdd:cd02150 57 HPYGKMLKEAPLAIVVCGDP--------------------SKEKAPGYwVQDCSAATENILLAAHALGLGAVWL-----G 111
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 928931667 166 AKEIEDFV-GFKE-----EGYFLAAMTPLGVPDGEPKSPSR 200
Cdd:cd02150 112 VYPFEERVkAIREilnipENIIPFCVIALGYPAEEKEPKDR 152
|
|
| nitroreductase |
cd20608 |
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ... |
4-189 |
8.63e-27 |
|
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: 99.72 E-value: 8.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 4 LDFIYKRHSVRKFKDVSVPIEDIHKIIEAATFAPSGKNIQNWRFVVISNKEKIKQIAniienknadlathleneeekvKF 83
Cdd:cd20608 1 FEAIKTRRSVRRFSDKPVEEEKLEKILEAARLAPSWANKQCWRFIVVTDKETLSELA---------------------KK 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 84 TKFVKyaTFFTKAPVLILVYAGPYEATGLDVLKKIKAptdeihdllkrspliqSVGAAMENIMLSATHLGYGTCWMTSQN 163
Cdd:cd20608 60 ESPSN--GWLKDAPVIIVVCADPKDSGWLNGQNYYLV----------------DAAIAMQNLMLAATDLGLGTCWIGAFD 121
|
170 180
....*....|....*....|....*..
gi 928931667 164 YA-AKEIedfVGFKEEGYFLaAMTPLG 189
Cdd:cd20608 122 EKkVKEI---LGIPENIRVV-ALTPLG 144
|
|
| nitroreductase |
cd02151 |
nitroreductase family protein; A subfamily of the nitroreductase family containing ... |
5-197 |
1.89e-26 |
|
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: 99.14 E-value: 1.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 5 DFIYKRHSVRKFKDVSVPIEDIHKIIEAATFAPSGKNIQNWRFVVISNKEKIKQIANIienknadlathleneeeKVKFT 84
Cdd:cd02151 1 ELLKKRRSIRKYTDEPIEEEKLEEILEAALLAPSSRNSRPVEFIVVDDKETLKKLSEC-----------------KPHGS 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 85 KFVKyatfftKAPVLILVYAGPyeaTGLDVLkkikaptdeIHDLlkrspliqSVgaAMENIMLSATHLGYGTCW------ 158
Cdd:cd02151 64 AFLK------GAPAAIVVLADT---EKSDTW---------IEDA--------SI--AATYIQLAAESLGLGSCWiqirnr 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 928931667 159 MTSQNyaaKEIEDFVgfKE-----EGYFLAAMTPLGVPDGEPKS 197
Cdd:cd02151 116 ETQDG---KTAEEYV--REllgipENYRVLCIIALGYPDEEKPP 154
|
|
| YdjA-like |
cd02135 |
nitroreductase family protein similar to Escherichia coli YdjA; A subfamily of the ... |
4-189 |
3.32e-25 |
|
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: 96.13 E-value: 3.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 4 LDFIYKRHSVRKFKD-VSVPIEDIHKIIEAATFAPSGKNIQNWRFVVISNKEKikqianiiENKNADLATHLENEEEKVK 82
Cdd:cd02135 1 LELIKTRRSIRKFKLtGAPPEEQLEELLEAAMWAPNHGKLEPWRFIVVTGEGR--------ERLAELLAAAAAARAPGAD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 83 FTKFVKYATFFTKAPVLILVYAGPYEatgldvlkKIKAPTDEihDLLkrspliqSVGAAMENIMLSATHLGYGTCWMTSQ 162
Cdd:cd02135 73 PEKLEKAREKALRAPVVIAVVAKPDE--------DPKVPEWE--QYA-------AVGAAVQNLLLAAHALGLGAVWRTGP 135
|
170 180
....*....|....*....|....*..
gi 928931667 163 NYAAKEIEDFVGFkEEGYFLAAMTPLG 189
Cdd:cd02135 136 VTYDPAVREALGL-PEDERIVGFLYLG 161
|
|
| nitroreductase |
cd20609 |
nitroreductase family protein; A subfamily of the nitroreductase family containing ... |
4-189 |
4.15e-24 |
|
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: 92.84 E-value: 4.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 4 LDFIYKRHSVRKFKDVSVPIEDIHKIIEAATFAPSGKNIQNWRFVVISNKEKIKQIANIienknadlathleneeekvkf 83
Cdd:cd20609 3 LELAKKRYSVRKFSDKPVEKEKLDKILEAGRLAPTAVNYQPQRILVVRSEEALEKLAKA--------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 84 tkfvkYATFFTkAPVLILVYAGPYEATgldvlkkiKAPTDeihdllKRSPLIQSVGAAMENIMLSATHLGYGTCWMTsqN 163
Cdd:cd20609 62 -----TPRFFG-APLVIVVCYDKDESW--------KRPYD------GKDSGDIDAAIVATHMMLAATELGLGTCWVG--N 119
|
170 180
....*....|....*....|....*.
gi 928931667 164 YAAKEIEDFVGFkEEGYFLAAMTPLG 189
Cdd:cd20609 120 FDPEKVREAFNL-PENLEPVAILPLG 144
|
|
| MhqN-like |
cd02137 |
nitroreductase family protein similar to the NAD(P)H nitroreductase MhqN; A diverse subfamily ... |
4-206 |
9.74e-23 |
|
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: 89.22 E-value: 9.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 4 LDFIYKRHSVRKF-KDVSVPIEDIHKIIEAATFAPSGKNIQNWRFVVISNKEKIKQIANIIENKNAdlathleneeekvk 82
Cdd:cd02137 1 LEVIKSRRSVRNFdPDHKIPKEELKEILELATLAPSSFNLQPWRFVVVRDPELKAKLAEAAYNQPQ-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 83 ftkfvkyatfFTKAPVLILVyagpyeatgldvlkkikaPTDeihdllkrspliQSVGAAMENIMLSATHLGYGTCWMTSQ 162
Cdd:cd02137 67 ----------VTTASAVILV------------------LGD------------LNAGLAAMNLMLAAKAKGYDTCPMGGF 106
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 928931667 163 NYAA-KEIedfvgFK-EEGYFLAAMTPLGVPDGEPKSPSRKPIQEV 206
Cdd:cd02137 107 DKEKvAEL-----LNlPDRYVPVLLIAIGKAADKAPRSGRLPVDEV 147
|
|
| nitroreductase_FeS-like |
cd02143 |
nitroreductases with an N-terminal iron-sulfur cluster-binding domain; Members of this family ... |
6-193 |
1.49e-21 |
|
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: 87.53 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 6 FIYKRHSVRKFKDVSVPIEDIHKIIEAATFAPSGKNIQNWRFVVISNKEKIKQIANIIENKNADLATHLENEEEKVKFTK 85
Cdd:cd02143 1 LLRSRRSIRRYKDKPVPRETLEKLLDIARYAPTGHNSQPVHWLVVDDPEKVRRLAELVIDWMRELIKEDPELAGKLFLDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 86 FVKYA-----TFFTKAPVLILVYAGPYEATgldvlkkikAPTDeihdllkrsPLIqsvgaAMENIMLSATHLGYGTCWMt 160
Cdd:cd02143 81 IVAAWekgidVILRGAPHLVVAHAPKDAPT---------PPVD---------CAI-----ALTYLELAAPSLGLGTCWA- 136
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 928931667 161 sqnyaakeiedfvgfkeeGYFLAAMT---P----LGVPDG 193
Cdd:cd02143 137 ------------------GFFTAAANnypPlreaLGLPEG 158
|
|
| iodotyrosine_dehalogenase |
cd02144 |
iodotyrosine dehalogenase; Iodotyrosine dehalogenase catalyzes the removal of iodine from the ... |
4-206 |
1.17e-20 |
|
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: 85.28 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 4 LDFIYKRHSVRKFKDVSVPIEDIHKIIEAATFAPSGKNIQNWRFVVISN---KEKIKQIANIIENKN-ADLATHLENEEE 79
Cdd:cd02144 2 YELMKKRRSVRDFSSEPVPREVIENAIRTAGTAPSGANTQPWTFVVVSDpeiKRKIREAAEEEEKEFyEKRMGEEWVWDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 80 KVKFTKFVKyaTFFTKAPVLILVYAGPYEATglDVLKKIKAPTDEIhdllkrspliqSVGAAMeNIMLSATH-LGYGTCW 158
Cdd:cd02144 82 KPLGTNWEK--PYLTEAPYLIVVFKQKYGVL--PDGKKKKHYYNEE-----------SVGIAV-GILLAALHnAGLVTLT 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 928931667 159 MTSQNyaAKEIEDFVGFkEEGYFLAAMTPLGVPDGEPKSPS--RKPIQEV 206
Cdd:cd02144 146 HTPSP--MPFLRDLLGR-PKNEKPLLLLPVGYPAEDATVPDlkRKPLEEI 192
|
|
| nitroreductase |
cd03370 |
uncharacterized nitroreductase family proteins; Nitroreductase family containing Thermus ... |
7-194 |
2.95e-16 |
|
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: 73.51 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 7 IYKRHSVRKFKDVSVPIEDIHKIIEAATFAPSGKNIQNWRFVVISN---KEKIKQIAniienknadlathleNEEEKVkf 83
Cdd:cd03370 5 IESRRSIRKYTQEPVPDEDLREILRLAGLAPSAWNIQPWRFVVVRDaelKEQLQAAA---------------YGQAQV-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 84 tkfvkyatffTKAPVLILVYAgpyeatglDVLKKIKAPTDEIHDLL---KRSPLIQSV---------------GAAMENI 145
Cdd:cd03370 68 ----------TSAPAVIVIYS--------DMEDALANLEETIHPGLseeRRQREAAGLrgafgkmsveqrgqwGLAQANI 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 928931667 146 -----MLSATHLGYGTCWMtsqnyaakeiedfVGFKEEGY----------FLAAMTPLGVPDGE 194
Cdd:cd03370 130 algflLLAAQSLGYDTSPM-------------LGFDPEKVkallglpehvTIAALVALGKPAEE 180
|
|
| TdsD-like |
cd02138 |
nitroreductase similar to Burkholderia pseudomallei TdsD; A subfamily of the nitroreductase ... |
7-210 |
3.62e-15 |
|
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: 70.27 E-value: 3.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 7 IYKRHSVRKFKDVSVPIEDIHKIIEAATFAPSGKNIQNWRFVVISNKEKI-KQIANIIENKNADLATHleneeekvkftk 85
Cdd:cd02138 2 IAERWSPRAFSPEPISEEDLLSLFEAARWAPSCFNEQPWRFVVARRDTEAfEKLLDLLAEGNQSWAKN------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 86 fvkyatfftkAPVLILVYAgpyeATGLDvlKKIKAPTDEIHDLlkrspliqsvGAAMENIMLSATHLGYGTCWMTsqnya 165
Cdd:cd02138 70 ----------APVLIVVLA----KTEFD--HNGKPNRYALFDT----------GAAVANLALQATALGLVVHQMA----- 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 928931667 166 akeiedfvGFKEEgyflAAMTPLGVPDGEpkspsrkpiqEVMTII 210
Cdd:cd02138 119 --------GFDPE----KAKEALGIPDEY----------EPITMI 141
|
|
| BluB |
cd02145 |
5,6-dimethylbenzimidazole synthase; BluB catalyzes the O2-dependent conversion of FMNH2 to 5, ... |
7-198 |
3.18e-14 |
|
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: 68.15 E-value: 3.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 7 IYKRHSVRKFKDVSVPIEDIHKIIEAATFAPSGKNIQNWRFVVISNKEKIKQIANIIENKNADLATHLENEEEKvkftkf 86
Cdd:cd02145 4 IRWRRDVRHFRPDPVPEEVLERLLQAAHLAPSVGLMQPWRFVRVRSAATRKAVHELFQRANAEAAEMYTGERAA------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 87 vKYATF----FTKAPVLILVYAGPYEATGLDVLKKIKAPTDEihdllkrspliQSVGAAMENIMLSATHLGYGTCWMTSQ 162
Cdd:cd02145 78 -QYRTLklegIEEAPLQLAVFCDRARAGGHGLGRTTMPEMDL-----------YSSVCAVQNLWLAARAEGLGVGWVSIL 145
|
170 180 190
....*....|....*....|....*....|....*.
gi 928931667 163 NYaaKEIEDFVGFKEEGYFLAAMTpLGVPDGEPKSP 198
Cdd:cd02145 146 DP--DEVKRLLGIPEHWEPVAYLC-IGYPEFFYDEP 178
|
|
| NfsB-like |
cd02149 |
nitroreductase similar to Escherichia coli NfsB; NAD(P)H:FMN oxidoreductase family. This ... |
4-206 |
8.27e-14 |
|
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: 66.12 E-value: 8.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 4 LDFIYKRHSVRKFkDVSVPI--EDIHKIIEAATFAPSGKNIQNWRFVVISNKEKIKQIAniienknadlathleneeekv 81
Cdd:cd02149 3 LELLNFRYATKKF-DPNKKIsdEDLETILEALRLSPSSFGLEPWKFLVVENPELKAKLA--------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 82 KFTKFVKYAtfFTKAPVLILVyagpyeatgldvlkkikaptdeihdLLKRSPLIQSVGAAMENIMLSATHLGYGTCWMTS 161
Cdd:cd02149 61 PAAWFNQPQ--IKDASHVVVF-------------------------LAKKDWSAKQTYIALGNMLLAAAMLGIDSCPIEG 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 928931667 162 QNYAAKEiEDFvGFKEEGYFLAAMTPLGVPDGEPKSPSRKPIQEV 206
Cdd:cd02149 114 FDPAKLD-EIL-GLDEKGYKISVMVAFGYRSEEKLPKSRKPLEDV 156
|
|
| NfsA-like |
cd02146 |
nitroreductase similar to Escherichia coli NfsA; This family contains NADPH-dependent flavin ... |
4-206 |
4.69e-13 |
|
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: 65.34 E-value: 4.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 4 LDFIYKRHSVRKFKDVSVPIEDIHKIIEAATFAPSGKNIQNWRFVVISNKEKIKQIANIIENKnadlathleneeekvkf 83
Cdd:cd02146 2 IETILNHRSVRKFTDEPLTDETLETLIAAAQSASTSSNLQAYSVIVVTDPELREKLAELAGNQ----------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 84 tKFVKyatfftKAPVLiLVYAGPYEATGLdVLKKIKAPTDEIHDLlkRSPLIQSVGAAM--ENIMLSATHLGYGTCWMTS 161
Cdd:cd02146 65 -PYVA------QAPVF-LVFCADLYRHQK-IAEEAGGKDVGLDYL--ESFLVGVVDAALaaQNALVAAESLGLGIVYIGG 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 928931667 162 QNYAAKEIEDFVGFKEEGYFLAAMTpLGVPDGEPKSPSRKPIQEV 206
Cdd:cd02146 134 IRNNPEEVIELLGLPEYVFPLFGLT-VGHPDPTPEVKPRLPLEAV 177
|
|
| TM1586_NiRdase |
pfam14512 |
Putative TM nitroreductase; Compared with the more traditional NADH oxidase/flavin reductase ... |
7-206 |
8.55e-09 |
|
Putative TM nitroreductase; Compared with the more traditional NADH oxidase/flavin reductase family, this family is a duplication, consisting of two similar domains arranged as the subunits of the dimeric NADH oxidase/flavin reductase with one conserved active site.
Pssm-ID: 405236 [Multi-domain] Cd Length: 214 Bit Score: 53.45 E-value: 8.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 7 IYKRHSVRKFKDVSVPiEDIHKIIEAAtfapsgkniqnwrfvvisnkekIKQIaniieNKNADLATHLENEEEKvKFTKF 86
Cdd:pfam14512 6 IFKRHSVRKYTDEPIP-EELLEELKNA----------------------IDEI-----NKLSGLNIQLVIDDPD-AFKGK 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 87 VKYAtFFTKAPVLILVYAGPYEatGLDVLkkikaptdeihdllkrspliqsVGAAMENIMLSATHLGYGTCW---MTSQN 163
Cdd:pfam14512 57 AKYG-KFKGVPNYIAAYGEKDD--DLLEN----------------------AGYYGEQIVLYATALGLGTCWvggTYSKS 111
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 928931667 164 YAAKEIEDfvgfkeeGYFLAAMTPLGVPDGEPKSPSRKPIQEV 206
Cdd:pfam14512 112 KVKAKIKK-------GEKLVIVIAFGYGATKGVRAKRKPLDEL 147
|
|
| BluB |
TIGR02476 |
5,6-dimethylbenzimidazole synthase; A previously published hypothesis that BluB, involved in ... |
4-198 |
1.41e-07 |
|
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: 49.75 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 4 LDFIYKRHSVRKFKDVSVPIEDIHKIIEAATFAPSGKNIQNWRFVVISNKEKIKQIANIIENKNADLATHLENEEEKVkf 83
Cdd:TIGR02476 10 YRLIRERRDVRHFRSDPVPEAVLERLLDAAHHAPSVGFSQPWRFVRVESPATREAVHALFTRANQAAAAIYDGERASQ-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928931667 84 tkfvkYATF----FTKAPVLILVYAGPYEATGldvlkkikaptdeiHDLLKRS-P--LIQSVGAAMENIMLSATHLGYGT 156
Cdd:TIGR02476 88 -----YHRLklegIREAPVQLAVFCDDARGEG--------------HGLGRHTmPemLRYSVACAIQNLWLAARAEGLGV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 928931667 157 CWMTSqnYAAKEIEDFVGFKeEGYFLAAMTPLGVPDGEPKSP 198
Cdd:TIGR02476 149 GWVSI--LDPDAVRRLLGVP-EGWRLVAYLCLGWPDAFYDEP 187
|
|
| PRK11053 |
PRK11053 |
oxygen-insensitive NAD(P)H nitroreductase; |
1-60 |
7.59e-05 |
|
oxygen-insensitive NAD(P)H nitroreductase;
Pssm-ID: 182929 [Multi-domain] Cd Length: 217 Bit Score: 42.27 E-value: 7.59e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 928931667 1 MKNLDFIYKRHSVRKFkDVS--VPIEDIHKIIEAATFAPSGKNIQNWRFVVISNKEKIKQIA 60
Cdd:PRK11053 1 MDIVSVAKKRYTTKAF-DPSkkLPAEQIEQIKTLLRFSPSSVNSQPWHFIVASTEEGKARIA 61
|
|
| FbiB_C-like |
cd20607 |
nitroreductase family domain similar to the C-terminal domain of F420:gamma-glutamyl ligase ... |
137-202 |
1.04e-04 |
|
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: 40.92 E-value: 1.04e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 928931667 137 SVGAAMENIMLSATHLGYGTCWMTSQNYAAKEIEDFVGFKEEGYFLAAMTpLGVPDGEPksPSRKP 202
Cdd:cd20607 88 AVGAAVQALLVALAVRGLGSCWIGSTIFAPDVVRDELDLPDDWEPLGAIA-IGYPLEPP--PPRPP 150
|
|
| PRK14852 |
PRK14852 |
hypothetical protein; Provisional |
21-48 |
6.69e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 184854 [Multi-domain] Cd Length: 989 Bit Score: 40.06 E-value: 6.69e-04
10 20
....*....|....*....|....*...
gi 928931667 21 VPIEDIHKIIEAATFAPSGKNIQNWRFV 48
Cdd:PRK14852 611 IPLETLHYVARAAMQAPSGDNVQPWRFV 638
|
|
| |
