|
Name |
Accession |
Description |
Interval |
E-value |
| iodotyrosine_dehalogenase |
cd02144 |
iodotyrosine dehalogenase; Iodotyrosine dehalogenase catalyzes the removal of iodine from the ... |
89-281 |
1.75e-119 |
|
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: 339.90 E-value: 1.75e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 89 FYELLNKRRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKIREIIEEEEEINYMKRMGKRWVTD 168
Cdd:cd02144 1 FYELMKKRRSVRDFSSEPVPREVIENAIRTAGTAPSGANTQPWTFVVVSDPEIKRKIREAAEEEEKEFYEKRMGEEWVWD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 169 LKKLRTNWIKEYLDTAPVLILIFKQVHGFAANGKKKVHYYNEISVSIACGLLLAALQNAGLVTVTTTPLNcGPRLRVLLG 248
Cdd:cd02144 81 LKPLGTNWEKPYLTEAPYLIVVFKQKYGVLPDGKKKKHYYNEESVGIAVGILLAALHNAGLVTLTHTPSP-MPFLRDLLG 159
|
170 180 190
....*....|....*....|....*....|...
gi 21312562 249 RPSHEKLLVLLPVGYPSRDATVPDLKRKALDQI 281
Cdd:cd02144 160 RPKNEKPLLLLPVGYPAEDATVPDLKRKPLEEI 192
|
|
| NfnB |
COG0778 |
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ... |
89-281 |
5.97e-33 |
|
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway/BioSystem: Pyrimidine degradation
Pssm-ID: 440541 [Multi-domain] Cd Length: 163 Bit Score: 118.42 E-value: 5.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 89 FYELLNKRRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKIReiieeeeeiNYMKRMGKRWVTD 168
Cdd:COG0778 1 LLELLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLA---------EALAEANQEWVAD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 169 lkklrtnwikeyldtAPVLILIFKQVHgfaaNGKKKVHYYNEISVSIACGLLLAALQNAGLVTVTTTPLNcGPRLRVLLG 248
Cdd:COG0778 72 ---------------APVLIVVCADPD----RSEKVPERYALLDAGIAAQNLLLAARALGLGTCWIGGFD-PEKVRELLG 131
|
170 180 190
....*....|....*....|....*....|...
gi 21312562 249 RPSHEKLLVLLPVGYPsrDATVPDLKRKALDQI 281
Cdd:COG0778 132 LPEGEEPVALLALGYP--AEELNPRPRKPLEEV 162
|
|
| Nitroreductase |
pfam00881 |
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ... |
93-263 |
1.83e-19 |
|
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: 83.21 E-value: 1.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 93 LNKRRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKIREIIEEEEEINymKRMGKRWVTDLKKL 172
Cdd:pfam00881 1 IRQRRSVRKFDPEPVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLAEAALELLLVE--PAAALLLLLRRDAN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 173 RTNWIKEYLDTAPVLILIFKQVHGFAANGKKKVHYYNEISVSIACGLLLAALQNAGLVTVTTTPLNcGPRLRVLLGRPSH 252
Cdd:pfam00881 79 LKLLLQDFLRGAPVLIVITASLSTYLRKAAERAYREALLDAGAAAQNLLLAATSLGLGSCPIGGFD-AAAVRELLGLPDD 157
|
170
....*....|.
gi 21312562 253 EKLLVLLPVGY 263
Cdd:pfam00881 158 ERLVGLIAVGY 168
|
|
| BluB |
TIGR02476 |
5,6-dimethylbenzimidazole synthase; A previously published hypothesis that BluB, involved in ... |
89-276 |
2.82e-12 |
|
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: 64.38 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 89 FYELLNKRRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKIREIIEEEEEInYMKRMGKRWVTD 168
Cdd:TIGR02476 9 VYRLIRERRDVRHFRSDPVPEAVLERLLDAAHHAPSVGFSQPWRFVRVESPATREAVHALFTRANQA-AAAIYDGERASQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 169 LKKLRTNWIKEyldtAPVLILIF-----KQVHGFAANGKKKVHYYneiSVSIACGLLLAALQNAGL----VTVTTTplnc 239
Cdd:TIGR02476 88 YHRLKLEGIRE----APVQLAVFcddarGEGHGLGRHTMPEMLRY---SVACAIQNLWLAARAEGLgvgwVSILDP---- 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 21312562 240 gPRLRVLLGRPSHEKLLVLLPVGYPSRDATVPDLKRK 276
Cdd:TIGR02476 157 -DAVRRLLGVPEGWRLVAYLCLGWPDAFYDEPELERA 192
|
|
| PRK13294 |
PRK13294 |
F420-0--gamma-glutamyl ligase; Provisional |
96-169 |
3.00e-09 |
|
F420-0--gamma-glutamyl ligase; Provisional
Pssm-ID: 183957 [Multi-domain] Cd Length: 448 Bit Score: 57.33 E-value: 3.00e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21312562 96 RRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKIreiieeeeeinyMKRMGKRWVTDL 169
Cdd:PRK13294 260 RRSVREFSDDPVDPEAVRRAVAAALTAPAPHHTRPVRFVWLRSAAVRTRL------------LDAMRDAWRADL 321
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| iodotyrosine_dehalogenase |
cd02144 |
iodotyrosine dehalogenase; Iodotyrosine dehalogenase catalyzes the removal of iodine from the ... |
89-281 |
1.75e-119 |
|
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: 339.90 E-value: 1.75e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 89 FYELLNKRRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKIREIIEEEEEINYMKRMGKRWVTD 168
Cdd:cd02144 1 FYELMKKRRSVRDFSSEPVPREVIENAIRTAGTAPSGANTQPWTFVVVSDPEIKRKIREAAEEEEKEFYEKRMGEEWVWD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 169 LKKLRTNWIKEYLDTAPVLILIFKQVHGFAANGKKKVHYYNEISVSIACGLLLAALQNAGLVTVTTTPLNcGPRLRVLLG 248
Cdd:cd02144 81 LKPLGTNWEKPYLTEAPYLIVVFKQKYGVLPDGKKKKHYYNEESVGIAVGILLAALHNAGLVTLTHTPSP-MPFLRDLLG 159
|
170 180 190
....*....|....*....|....*....|...
gi 21312562 249 RPSHEKLLVLLPVGYPSRDATVPDLKRKALDQI 281
Cdd:cd02144 160 RPKNEKPLLLLPVGYPAEDATVPDLKRKPLEEI 192
|
|
| NfnB |
COG0778 |
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ... |
89-281 |
5.97e-33 |
|
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway/BioSystem: Pyrimidine degradation
Pssm-ID: 440541 [Multi-domain] Cd Length: 163 Bit Score: 118.42 E-value: 5.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 89 FYELLNKRRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKIReiieeeeeiNYMKRMGKRWVTD 168
Cdd:COG0778 1 LLELLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLA---------EALAEANQEWVAD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 169 lkklrtnwikeyldtAPVLILIFKQVHgfaaNGKKKVHYYNEISVSIACGLLLAALQNAGLVTVTTTPLNcGPRLRVLLG 248
Cdd:COG0778 72 ---------------APVLIVVCADPD----RSEKVPERYALLDAGIAAQNLLLAARALGLGTCWIGGFD-PEKVRELLG 131
|
170 180 190
....*....|....*....|....*....|...
gi 21312562 249 RPSHEKLLVLLPVGYPsrDATVPDLKRKALDQI 281
Cdd:COG0778 132 LPEGEEPVALLALGYP--AEELNPRPRKPLEEV 162
|
|
| Nitro_FMN_reductase |
cd02062 |
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ... |
93-263 |
9.02e-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: 380311 [Multi-domain] Cd Length: 139 Bit Score: 91.20 E-value: 9.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 93 LNKRRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKIReiieeeeeinymkrmgkrwvtdlkkL 172
Cdd:cd02062 1 IKTRRSIRKFTDKPVPEEKLRKILEAARLAPSAGNLQPWRFIVVRDREKKEKLA-------------------------K 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 173 RTNWIKEYLDTAPVLILIFkqvhgfaANGKKKVHYYnEISVSIACGLLLAALQNAGLVTVTTTPLNCG-PRLRVLLGRPS 251
Cdd:cd02062 56 LAAPNQKFIAGAPVVIVVV-------ADPDKSRPWA-LEDAGAAAQNLLLAAAALGLGSCWIGGFDFReDKVRELLGIPE 127
|
170
....*....|..
gi 21312562 252 HEKLLVLLPVGY 263
Cdd:cd02062 128 NLRPVALIAIGY 139
|
|
| Nitroreductase |
pfam00881 |
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ... |
93-263 |
1.83e-19 |
|
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: 83.21 E-value: 1.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 93 LNKRRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKIREIIEEEEEINymKRMGKRWVTDLKKL 172
Cdd:pfam00881 1 IRQRRSVRKFDPEPVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLAEAALELLLVE--PAAALLLLLRRDAN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 173 RTNWIKEYLDTAPVLILIFKQVHGFAANGKKKVHYYNEISVSIACGLLLAALQNAGLVTVTTTPLNcGPRLRVLLGRPSH 252
Cdd:pfam00881 79 LKLLLQDFLRGAPVLIVITASLSTYLRKAAERAYREALLDAGAAAQNLLLAATSLGLGSCPIGGFD-AAAVRELLGLPDD 157
|
170
....*....|.
gi 21312562 253 EKLLVLLPVGY 263
Cdd:pfam00881 158 ERLVGLIAVGY 168
|
|
| nitroreductase |
cd02139 |
nitroreductase family protein; A subfamily of the nitroreductase family containing ... |
89-281 |
4.32e-18 |
|
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: 79.44 E-value: 4.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 89 FYELLNKRRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKIReiieeeeeinyMKRMGKRWVTD 168
Cdd:cd02139 1 VYEAIKKRRSIRKYKPTPVEEEKLLRILEAARLAPSAKNRQPWRFIVVKDKELKEKLA-----------EAANGQKFIAE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 169 lkklrtnwikeyldtAPVLI-LIFKQVHGFAANGKKkvhyYNEISVSIACG-LLLAAlQNAGLVTvtttplnC------G 240
Cdd:cd02139 70 ---------------APVVIvACADPSESGMGCGKP----YYLVDVAIAMEhLVLAA-TEEGLGT-------CwigafdE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 21312562 241 PRLRVLLGRPSHEKLLVLLPVGYPsrDATVPDLKRKALDQI 281
Cdd:cd02139 123 DKVKEILGIPEEYRVVALTPLGYP--AEEPPPRPRKPLEEI 161
|
|
| nitroreductase |
cd02151 |
nitroreductase family protein; A subfamily of the nitroreductase family containing ... |
91-264 |
1.89e-17 |
|
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: 77.57 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 91 ELLNKRRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKIREiieeeeeinyMKRMGkrwvtdlk 170
Cdd:cd02151 1 ELLKKRRSIRKYTDEPIEEEKLEEILEAALLAPSSRNSRPVEFIVVDDKETLKKLSE----------CKPHG-------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 171 klrtnwiKEYLDTAPVLILIfkqvhgfAANgKKKVHYYNEISvSIACGLLLAALQNAGLVT--------VTTTPLNCGPR 242
Cdd:cd02151 63 -------SAFLKGAPAAIVV-------LAD-TEKSDTWIEDA-SIAATYIQLAAESLGLGScwiqirnrETQDGKTAEEY 126
|
170 180
....*....|....*....|..
gi 21312562 243 LRVLLGRPSHEKLLVLLPVGYP 264
Cdd:cd02151 127 VRELLGIPENYRVLCIIALGYP 148
|
|
| nitroreductase |
cd20609 |
nitroreductase family protein; A subfamily of the nitroreductase family containing ... |
88-263 |
1.16e-14 |
|
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: 69.34 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 88 EFYELLNKRRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKIREIieeeeeinymkrmgkrwvt 167
Cdd:cd20609 1 DFLELAKKRYSVRKFSDKPVEKEKLDKILEAGRLAPTAVNYQPQRILVVRSEEALEKLAKA------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 168 dlkklrTNWIKEyldtAPVLILIFKqVHGFAANGKKKVHYYNEISVSIACG-LLLAAlQNAGLVT--VtttplnCG---P 241
Cdd:cd20609 62 ------TPRFFG----APLVIVVCY-DKDESWKRPYDGKDSGDIDAAIVAThMMLAA-TELGLGTcwV------GNfdpE 123
|
170 180
....*....|....*....|..
gi 21312562 242 RLRVLLGRPSHEKLLVLLPVGY 263
Cdd:cd20609 124 KVREAFNLPENLEPVAILPLGY 145
|
|
| PnbA_NfnB-like |
cd02136 |
nitroreductase similar to Mycobacterium smegmatis NfnB; Members of this family utilize FMN as ... |
92-276 |
2.06e-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: 69.15 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 92 LLNKRRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKhkireiieeeeeinymkrmgkrwvtDLKK 171
Cdd:cd02136 1 AIKSRRSVRAFKDKPVPKETIEKILEAARRAPSGKNTQPWRVYVVTGKARE-------------------------RLKK 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 172 LrtnwikeyLDTAPVLILIFkqvhgfaanGKKKVHYYNEISVSIACG-LLLAAlQNAGLVTVtttPLNCGPR----LRVL 246
Cdd:cd02136 56 A--------FFGAPVALFLT---------MDKVLGPWSWFDLGAFLQnLMLAA-HALGLGTC---PQGALAGypdvVRKE 114
|
170 180 190
....*....|....*....|....*....|
gi 21312562 247 LGRPSHEKLLVLLPVGYPSRDATVPDLKRK 276
Cdd:cd02136 115 LGIPDDEELVCGIALGYPDPDAPVNQFRTP 144
|
|
| nitroreductase |
cd20610 |
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ... |
95-263 |
6.69e-13 |
|
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: 65.38 E-value: 6.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 95 KRRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKIrEIIEEEEEINYMKRMGKrwVTDLKKLR- 173
Cdd:cd20610 3 KRRSIRKFKPDPVPKEDIEKILEAANWAPSGMNRQNWEFVVVKGGEKIEKI-GISIKKKNEEIARLLEK--VFAEKPIRf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 174 TNWIK--EYLDTAPVLILIFKQVHgfaangkKKVHYYNEI--SVSIAC-GLLLAAlQNAGLVTV-TTTPLNCGPRLRVLL 247
Cdd:cd20610 80 RKFRRffTLFGGAPVLVVVYTEPY-------KPPEERKPDlqSVSAAIqNLLLAA-HALGLGTCwMTGPLYAEDEIEEIL 151
|
170
....*....|....*.
gi 21312562 248 GRPSHEKLLVLLPVGY 263
Cdd:cd20610 152 EIPDDKELVAVTPLGY 167
|
|
| BluB |
TIGR02476 |
5,6-dimethylbenzimidazole synthase; A previously published hypothesis that BluB, involved in ... |
89-276 |
2.82e-12 |
|
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: 64.38 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 89 FYELLNKRRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKIREIIEEEEEInYMKRMGKRWVTD 168
Cdd:TIGR02476 9 VYRLIRERRDVRHFRSDPVPEAVLERLLDAAHHAPSVGFSQPWRFVRVESPATREAVHALFTRANQA-AAAIYDGERASQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 169 LKKLRTNWIKEyldtAPVLILIF-----KQVHGFAANGKKKVHYYneiSVSIACGLLLAALQNAGL----VTVTTTplnc 239
Cdd:TIGR02476 88 YHRLKLEGIRE----APVQLAVFcddarGEGHGLGRHTMPEMLRY---SVACAIQNLWLAARAEGLgvgwVSILDP---- 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 21312562 240 gPRLRVLLGRPSHEKLLVLLPVGYPSRDATVPDLKRK 276
Cdd:TIGR02476 157 -DAVRRLLGVPEGWRLVAYLCLGWPDAFYDEPELERA 192
|
|
| nitroreductase |
cd02150 |
nitroreductase family protein; A subfamily of the nitroreductase family containing ... |
95-264 |
3.93e-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: 380325 [Multi-domain] Cd Length: 156 Bit Score: 63.00 E-value: 3.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 95 KRRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKIREIIEeeeeinYMKrmgkrwvtdlkklrt 174
Cdd:cd02150 3 TRRSIRKYTDKPVEEEDIEKLLRAAMAAPSAGNQQPWHFIVVTDREKLDKIAEAHP------YGK--------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 175 nwikeYLDTAPVLILIfkqvhgfAANGKK-KVHYYNEISVSIAC-GLLLAAlQNAGLVTVTTtplNCGPR------LRVL 246
Cdd:cd02150 62 -----MLKEAPLAIVV-------CGDPSKeKAPGYWVQDCSAATeNILLAA-HALGLGAVWL---GVYPFeervkaIREI 125
|
170
....*....|....*...
gi 21312562 247 LGRPSHEKLLVLLPVGYP 264
Cdd:cd02150 126 LNIPENIIPFCVIALGYP 143
|
|
| MhqN-like |
cd02137 |
nitroreductase family protein similar to the NAD(P)H nitroreductase MhqN; A diverse subfamily ... |
91-281 |
4.34e-12 |
|
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: 62.64 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 91 ELLNKRRSVRFISSEH-VPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKIREIIeeeeeinymkrMGKRWVTdl 169
Cdd:cd02137 2 EVIKSRRSVRNFDPDHkIPKEELKEILELATLAPSSFNLQPWRFVVVRDPELKAKLAEAA-----------YNQPQVT-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 170 kklrtnwikeyldTAPVLILIFKQvhgfaangkkkvhyyneISVSIACGLLLAALQNAGLVTVTTTPLNcGPRLRVLLGR 249
Cdd:cd02137 69 -------------TASAVILVLGD-----------------LNAGLAAMNLMLAAKAKGYDTCPMGGFD-KEKVAELLNL 117
|
170 180 190
....*....|....*....|....*....|..
gi 21312562 250 PSHEKLLVLLPVGYPSRDAtvPDLKRKALDQI 281
Cdd:cd02137 118 PDRYVPVLLIAIGKAADKA--PRSGRLPVDEV 147
|
|
| BluB |
cd02145 |
5,6-dimethylbenzimidazole synthase; BluB catalyzes the O2-dependent conversion of FMNH2 to 5, ... |
90-280 |
8.29e-11 |
|
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: 60.06 E-value: 8.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 90 YELLNKRRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMK---HKIREIIEEEEEINYMKRMGKRWV 166
Cdd:cd02145 1 YRVIRWRRDVRHFRPDPVPEEVLERLLQAAHLAPSVGLMQPWRFVRVRSAATRkavHELFQRANAEAAEMYTGERAAQYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 167 TdLKklrtnwiKEYLDTAPVLILIF-----KQVHGFAANGKKKVHYYNeiSVSIACGLLLAA-LQNAGLVTVTTtpLNcg 240
Cdd:cd02145 81 T-LK-------LEGIEEAPLQLAVFcdrarAGGHGLGRTTMPEMDLYS--SVCAVQNLWLAArAEGLGVGWVSI--LD-- 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 21312562 241 P-RLRVLLGRPSHEKLLVLLPVGYPSRDATVPDLKRKALDQ 280
Cdd:cd02145 147 PdEVKRLLGIPEHWEPVAYLCIGYPEFFYDEPELEQAGWEQ 187
|
|
| nitroreductase |
cd03370 |
uncharacterized nitroreductase family proteins; Nitroreductase family containing Thermus ... |
91-267 |
9.49e-11 |
|
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: 59.64 E-value: 9.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 91 ELLNKRRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKIREIIeeeeeinymkrMGKRWVTdlk 170
Cdd:cd03370 3 EAIESRRSIRKYTQEPVPDEDLREILRLAGLAPSAWNIQPWRFVVVRDAELKEQLQAAA-----------YGQAQVT--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 171 klrtnwikeyldTAPVLILIFKQ-----------VH-GFAANGKKKV-----HYYNEISVS-----------IACGLLLA 222
Cdd:cd03370 69 ------------SAPAVIVIYSDmedalanleetIHpGLSEERRQREaaglrGAFGKMSVEqrgqwglaqanIALGFLLL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 21312562 223 ALQNAGLVTVTTTPLNCGpRLRVLLGRPSHEKLLVLLPVGYPSRD 267
Cdd:cd03370 137 AAQSLGYDTSPMLGFDPE-KVKALLGLPEHVTIAALVALGKPAEE 180
|
|
| YdjA-like |
cd02135 |
nitroreductase family protein similar to Escherichia coli YdjA; A subfamily of the ... |
91-263 |
1.66e-10 |
|
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: 58.38 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 91 ELLNKRRSVR-FISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKIREIIEEeeeinYMKRMGKRWVTDL 169
Cdd:cd02135 2 ELIKTRRSIRkFKLTGAPPEEQLEELLEAAMWAPNHGKLEPWRFIVVTGEGRERLAELLAAA-----AAARAPGADPEKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 170 KKLRTNWIKeyldtAPVLILIFKQVHGfaanGKKKVHYYNEISVSIACGLLLAALQNAGLVTV-TTTPLNCGPRLRVLLG 248
Cdd:cd02135 77 EKAREKALR-----APVVIAVVAKPDE----DPKVPEWEQYAAVGAAVQNLLLAAHALGLGAVwRTGPVTYDPAVREALG 147
|
170
....*....|....*
gi 21312562 249 RPSHEKLLVLLPVGY 263
Cdd:cd02135 148 LPEDERIVGFLYLGT 162
|
|
| nitroreductase |
cd20608 |
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ... |
90-263 |
6.42e-10 |
|
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: 56.57 E-value: 6.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 90 YELLNKRRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDpdmKHKIREIIEEEEEINymkrmgkRWVTDl 169
Cdd:cd20608 1 FEAIKTRRSVRRFSDKPVEEEKLEKILEAARLAPSWANKQCWRFIVVTD---KETLSELAKKESPSN-------GWLKD- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 170 kklrtnwikeyldtAPVLIlifkqvhgfAANGKKKV------HYYNEISVSIACGLLLAALQNAGLVTVTTTPLNcGPRL 243
Cdd:cd20608 70 --------------APVII---------VVCADPKDsgwlngQNYYLVDAAIAMQNLMLAATDLGLGTCWIGAFD-EKKV 125
|
170 180
....*....|....*....|
gi 21312562 244 RVLLGRPSHEKLLVLLPVGY 263
Cdd:cd20608 126 KEILGIPENIRVVALTPLGY 145
|
|
| PRK13294 |
PRK13294 |
F420-0--gamma-glutamyl ligase; Provisional |
96-169 |
3.00e-09 |
|
F420-0--gamma-glutamyl ligase; Provisional
Pssm-ID: 183957 [Multi-domain] Cd Length: 448 Bit Score: 57.33 E-value: 3.00e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21312562 96 RRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKIreiieeeeeinyMKRMGKRWVTDL 169
Cdd:PRK13294 260 RRSVREFSDDPVDPEAVRRAVAAALTAPAPHHTRPVRFVWLRSAAVRTRL------------LDAMRDAWRADL 321
|
|
| TdsD-like |
cd02138 |
nitroreductase similar to Burkholderia pseudomallei TdsD; A subfamily of the nitroreductase ... |
92-281 |
1.59e-08 |
|
nitroreductase similar to Burkholderia pseudomallei TdsD; A subfamily of the nitroreductase family containing uncharacterized proteins that are similar to Burkholderia pseudomallei TdsD, may be involved in the processing of organosulfur compounds. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer.
Pssm-ID: 380315 [Multi-domain] Cd Length: 174 Bit Score: 52.93 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 92 LLNKRRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKireiieeeEEINYMKRMGKRWVTDlkk 171
Cdd:cd02138 1 LIAERWSPRAFSPEPISEEDLLSLFEAARWAPSCFNEQPWRFVVARRDTEAFE--------KLLDLLAEGNQSWAKN--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312562 172 lrtnwikeyldtAPVLILIFKQVHgFAANGKKKVHYynEISVSIACGLLLAALQNAGLVtvtttplnCGP-------RLR 244
Cdd:cd02138 70 ------------APVLIVVLAKTE-FDHNGKPNRYA--LFDTGAAVANLALQATALGLV--------VHQmagfdpeKAK 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21312562 245 VLLGRPSHEKLLVLLPVGYPSRDATVPDL---------KRKALDQI 281
Cdd:cd02138 127 EALGIPDEYEPITMIAIGYPGDPESLPEKllereeaprTRKPLSEI 172
|
|
| nitroreductase_FeS-like |
cd02143 |
nitroreductases with an N-terminal iron-sulfur cluster-binding domain; Members of this family ... |
92-163 |
2.05e-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: 50.16 E-value: 2.05e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21312562 92 LLNKRRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKIReiieeEEEINYMKRMGK 163
Cdd:cd02143 1 LLRSRRSIRRYKDKPVPRETLEKLLDIARYAPTGHNSQPVHWLVVDDPEKVRRLA-----ELVIDWMRELIK 67
|
|
| NfsA-like |
cd02146 |
nitroreductase similar to Escherichia coli NfsA; This family contains NADPH-dependent flavin ... |
91-145 |
7.77e-07 |
|
nitroreductase similar to Escherichia coli NfsA; This family contains NADPH-dependent flavin reductase and oxygen-insensitive nitroreductase. These enzymes are homodimeric flavoproteins that contain one FMN per monomer as a cofactor. Flavin reductase catalyzes the reduction of flavin by using NADPH as an electron donor. Oxygen-insensitive nitroreductase, such as NfsA protein in Escherichia coli, catalyzes reduction of nitrocompounds using NADPH as electron donor.
Pssm-ID: 380322 [Multi-domain] Cd Length: 229 Bit Score: 48.77 E-value: 7.77e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 21312562 91 ELLNKRRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKI 145
Cdd:cd02146 3 ETILNHRSVRKFTDEPLTDETLETLIAAAQSASTSSNLQAYSVIVVTDPELREKL 57
|
|
| NfsB-like |
cd02149 |
nitroreductase similar to Escherichia coli NfsB; NAD(P)H:FMN oxidoreductase family. This ... |
91-146 |
3.86e-06 |
|
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: 45.71 E-value: 3.86e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 21312562 91 ELLNKRRSVR-FISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKIR 146
Cdd:cd02149 4 ELLNFRYATKkFDPNKKISDEDLETILEALRLSPSSFGLEPWKFLVVENPELKAKLA 60
|
|
| |
