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Conserved domains on  [gi|972776388|ref|NP_001305424|]
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iodotyrosine deiodinase 1 isoform 4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
iodotyrosine_dehalogenase cd02144
iodotyrosine dehalogenase; Iodotyrosine dehalogenase catalyzes the removal of iodine from the ...
42-203 1.28e-101

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: 291.75  E-value: 1.28e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388  42 GTAPSGAHTEPWTFVVVKDPDVKHKIRKIIEEEEEINYMKRMGHRWVTDLKKLRTNWIKEYLDTAPILILIFKQVHGFAA 121
Cdd:cd02144   32 GTAPSGANTQPWTFVVVSDPEIKRKIREAAEEEEKEFYEKRMGEEWVWDLKPLGTNWEKPYLTEAPYLIVVFKQKYGVLP 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388 122 NGKKKVHYYNEISVSIACGILLAALQNAGLVTVTTTPLNcGPRLRVLLGRPAHEKLLMLLPVGYPSKEATVPDLKRKPLD 201
Cdd:cd02144  112 DGKKKKHYYNEESVGIAVGILLAALHNAGLVTLTHTPSP-MPFLRDLLGRPKNEKPLLLLPVGYPAEDATVPDLKRKPLE 190

                 ..
gi 972776388 202 QI 203
Cdd:cd02144  191 EI 192
 
Name Accession Description Interval E-value
iodotyrosine_dehalogenase cd02144
iodotyrosine dehalogenase; Iodotyrosine dehalogenase catalyzes the removal of iodine from the ...
42-203 1.28e-101

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: 291.75  E-value: 1.28e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388  42 GTAPSGAHTEPWTFVVVKDPDVKHKIRKIIEEEEEINYMKRMGHRWVTDLKKLRTNWIKEYLDTAPILILIFKQVHGFAA 121
Cdd:cd02144   32 GTAPSGANTQPWTFVVVSDPEIKRKIREAAEEEEKEFYEKRMGEEWVWDLKPLGTNWEKPYLTEAPYLIVVFKQKYGVLP 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388 122 NGKKKVHYYNEISVSIACGILLAALQNAGLVTVTTTPLNcGPRLRVLLGRPAHEKLLMLLPVGYPSKEATVPDLKRKPLD 201
Cdd:cd02144  112 DGKKKKHYYNEESVGIAVGILLAALHNAGLVTLTHTPSP-MPFLRDLLGRPKNEKPLLLLPVGYPAEDATVPDLKRKPLE 190

                 ..
gi 972776388 202 QI 203
Cdd:cd02144  191 EI 192
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
44-203 2.20e-22

Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 88.76  E-value: 2.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388  44 APSGAHTEPWTFVVVKDPDVKHKIRKiieeeeeinYMKRMGHRWVTDlkklrtnwikeyldtAPILILIFKQVHgfaaNG 123
Cdd:COG0778   34 APSAGNLQPWRFVVVRDPELRERLAE---------ALAEANQEWVAD---------------APVLIVVCADPD----RS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388 124 KKKVHYYNEISVSIACGILLAALQNAGLVTVTTTPLNcGPRLRVLLGRPAHEKLLMLLPVGYPSKEatVPDLKRKPLDQI 203
Cdd:COG0778   86 EKVPERYALLDAGIAAQNLLLAARALGLGTCWIGGFD-PEKVRELLGLPEGEEPVALLALGYPAEE--LNPRPRKPLEEV 162
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
43-185 1.79e-10

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: 57.40  E-value: 1.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388   43 TAPSGAHTEPWTFVVVKDPDVKHKIRKIIEEEEEINymKRMGHRWVTDLKKLRTNWIKEYLDTAPILILIFKQVHGFAAN 122
Cdd:pfam00881  29 RAPSAGNLQPWRFYVVTDGELRYRLAEAALELLLVE--PAAALLLLLRRDANLKLLLQDFLRGAPVLIVITASLSTYLRK 106
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 972776388  123 GKKKVHYYNEISVSIACGILLAALQNAGLVTVTTTPLNcGPRLRVLLGRPAHEKLLMLLPVGY 185
Cdd:pfam00881 107 AAERAYREALLDAGAAAQNLLLAATSLGLGSCPIGGFD-AAAVRELLGLPDDERLVGLIAVGY 168
BluB TIGR02476
5,6-dimethylbenzimidazole synthase; A previously published hypothesis that BluB, involved in ...
43-198 6.40e-04

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: 39.35  E-value: 6.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388   43 TAPSGAHTEPWTFVVVKDPDVKHKIRKIIEEEEEInYMKRMGHRWVTDLKKLRTNWIKEyldtAPILILIF-----KQVH 117
Cdd:TIGR02476  41 HAPSVGFSQPWRFVRVESPATREAVHALFTRANQA-AAAIYDGERASQYHRLKLEGIRE----APVQLAVFcddarGEGH 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388  118 GFAANGKKKVHYYneiSVSIACGILLAALQNAGL----VTVTTTplncgPRLRVLLGRPAHEKLLMLLPVGYPSKEATVP 193
Cdd:TIGR02476 116 GLGRHTMPEMLRY---SVACAIQNLWLAARAEGLgvgwVSILDP-----DAVRRLLGVPEGWRLVAYLCLGWPDAFYDEP 187

                  ....*
gi 972776388  194 DLKRK 198
Cdd:TIGR02476 188 ELERA 192
PRK13294 PRK13294
F420-0--gamma-glutamyl ligase; Provisional
43-91 5.61e-03

F420-0--gamma-glutamyl ligase; Provisional


Pssm-ID: 183957 [Multi-domain]  Cd Length: 448  Bit Score: 36.92  E-value: 5.61e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 972776388  43 TAPSGAHTEPWTFVVVKDPDVKHKIrkiieeeeeinyMKRMGHRWVTDL 91
Cdd:PRK13294 285 TAPAPHHTRPVRFVWLRSAAVRTRL------------LDAMRDAWRADL 321
 
Name Accession Description Interval E-value
iodotyrosine_dehalogenase cd02144
iodotyrosine dehalogenase; Iodotyrosine dehalogenase catalyzes the removal of iodine from the ...
42-203 1.28e-101

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: 291.75  E-value: 1.28e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388  42 GTAPSGAHTEPWTFVVVKDPDVKHKIRKIIEEEEEINYMKRMGHRWVTDLKKLRTNWIKEYLDTAPILILIFKQVHGFAA 121
Cdd:cd02144   32 GTAPSGANTQPWTFVVVSDPEIKRKIREAAEEEEKEFYEKRMGEEWVWDLKPLGTNWEKPYLTEAPYLIVVFKQKYGVLP 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388 122 NGKKKVHYYNEISVSIACGILLAALQNAGLVTVTTTPLNcGPRLRVLLGRPAHEKLLMLLPVGYPSKEATVPDLKRKPLD 201
Cdd:cd02144  112 DGKKKKHYYNEESVGIAVGILLAALHNAGLVTLTHTPSP-MPFLRDLLGRPKNEKPLLLLPVGYPAEDATVPDLKRKPLE 190

                 ..
gi 972776388 202 QI 203
Cdd:cd02144  191 EI 192
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
44-203 2.20e-22

Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 88.76  E-value: 2.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388  44 APSGAHTEPWTFVVVKDPDVKHKIRKiieeeeeinYMKRMGHRWVTDlkklrtnwikeyldtAPILILIFKQVHgfaaNG 123
Cdd:COG0778   34 APSAGNLQPWRFVVVRDPELRERLAE---------ALAEANQEWVAD---------------APVLIVVCADPD----RS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388 124 KKKVHYYNEISVSIACGILLAALQNAGLVTVTTTPLNcGPRLRVLLGRPAHEKLLMLLPVGYPSKEatVPDLKRKPLDQI 203
Cdd:COG0778   86 EKVPERYALLDAGIAAQNLLLAARALGLGTCWIGGFD-PEKVRELLGLPEGEEPVALLALGYPAEE--LNPRPRKPLEEV 162
Nitro_FMN_reductase cd02062
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
44-185 2.80e-14

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: 66.94  E-value: 2.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388  44 APSGAHTEPWTFVVVKDPDVKHKIRKiieeeeeinymkrmghrwvtdlkklRTNWIKEYLDTAPILILIFkqvhgfaANG 123
Cdd:cd02062   30 APSAGNLQPWRFIVVRDREKKEKLAK-------------------------LAAPNQKFIAGAPVVIVVV-------ADP 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 972776388 124 KKKVHYYnEISVSIACGILLAALQNAGLVTVTTTPLNCG-PRLRVLLGRPAHEKLLMLLPVGY 185
Cdd:cd02062   78 DKSRPWA-LEDAGAAAQNLLLAAAALGLGSCWIGGFDFReDKVRELLGIPENLRPVALIAIGY 139
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
43-185 1.79e-10

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: 57.40  E-value: 1.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388   43 TAPSGAHTEPWTFVVVKDPDVKHKIRKIIEEEEEINymKRMGHRWVTDLKKLRTNWIKEYLDTAPILILIFKQVHGFAAN 122
Cdd:pfam00881  29 RAPSAGNLQPWRFYVVTDGELRYRLAEAALELLLVE--PAAALLLLLRRDANLKLLLQDFLRGAPVLIVITASLSTYLRK 106
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 972776388  123 GKKKVHYYNEISVSIACGILLAALQNAGLVTVTTTPLNcGPRLRVLLGRPAHEKLLMLLPVGY 185
Cdd:pfam00881 107 AAERAYREALLDAGAAAQNLLLAATSLGLGSCPIGGFD-AAAVRELLGLPDDERLVGLIAVGY 168
nitroreductase cd02139
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
44-203 2.44e-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.


Pssm-ID: 380316 [Multi-domain]  Cd Length: 165  Bit Score: 54.01  E-value: 2.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388  44 APSGAHTEPWTFVVVKDPDVKHKIRKiieeeeeinymKRMGHRWVTDlkklrtnwikeyldtAPILI-LIFKQVHGFAAN 122
Cdd:cd02139   34 APSAKNRQPWRFIVVKDKELKEKLAE-----------AANGQKFIAE---------------APVVIvACADPSESGMGC 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388 123 GKKkvhyYNEISVSIACG-ILLAAlQNAGLVTvtttplnC------GPRLRVLLGRPAHEKLLMLLPVGYPSKEatVPDL 195
Cdd:cd02139   88 GKP----YYLVDVAIAMEhLVLAA-TEEGLGT-------CwigafdEDKVKEILGIPEEYRVVALTPLGYPAEE--PPPR 153

                 ....*...
gi 972776388 196 KRKPLDQI 203
Cdd:cd02139  154 PRKPLEEI 161
MhqN-like cd02137
nitroreductase family protein similar to the NAD(P)H nitroreductase MhqN; A diverse subfamily ...
43-203 3.32e-08

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: 50.70  E-value: 3.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388  43 TAPSGAHTEPWTFVVVKDPDVKHKIRKIIeeeeeinymkrMGHRWVTdlkklrtnwikeyldTAPILILIFKQvhgfaan 122
Cdd:cd02137   33 LAPSSFNLQPWRFVVVRDPELKAKLAEAA-----------YNQPQVT---------------TASAVILVLGD------- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388 123 gkkkvhyyneISVSIACGILLAALQNAGLVTVTTTPLNcGPRLRVLLGRPAHEKLLMLLPVGYPSKEAtvPDLKRKPLDQ 202
Cdd:cd02137   80 ----------LNAGLAAMNLMLAAKAKGYDTCPMGGFD-KEKVAELLNLPDRYVPVLLIAIGKAADKA--PRSGRLPVDE 146

                 .
gi 972776388 203 I 203
Cdd:cd02137  147 V 147
nitroreductase cd02151
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
44-189 4.79e-07

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: 47.53  E-value: 4.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388  44 APSGAHTEPWTFVVVKDPDVKHKIRKiieeeeeinyMKRMGhrwvtdlkklrtnwiKEYLDTAPILILIfkqvhgfAANg 123
Cdd:cd02151   32 APSSRNSRPVEFIVVDDKETLKKLSE----------CKPHG---------------SAFLKGAPAAIVV-------LAD- 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 972776388 124 KKKVHYYNEISvSIACGILLAALQNAGLVT--------VTTTPLNCGPRLRVLLGRPAHEKLLMLLPVGYPSKE 189
Cdd:cd02151   79 TEKSDTWIEDA-SIAATYIQLAAESLGLGScwiqirnrETQDGKTAEEYVRELLGIPENYRVLCIIALGYPDEE 151
nitroreductase cd03370
uncharacterized nitroreductase family proteins; Nitroreductase family containing Thermus ...
42-189 2.02e-06

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: 46.54  E-value: 2.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388  42 GTAPSGAHTEPWTFVVVKDPDVKHKIRKIIeeeeeinymkrMGHRWVTdlkklrtnwikeyldTAPILILIFKQ------ 115
Cdd:cd03370   32 GLAPSAWNIQPWRFVVVRDAELKEQLQAAA-----------YGQAQVT---------------SAPAVIVIYSDmedala 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388 116 -----VH-GFAANGKKKV-----HYYNEISVS-----------IACGILLAALQNAGLVTVTTTPLNCGpRLRVLLGRPA 173
Cdd:cd03370   86 nleetIHpGLSEERRQREaaglrGAFGKMSVEqrgqwglaqanIALGFLLLAAQSLGYDTSPMLGFDPE-KVKALLGLPE 164
                        170
                 ....*....|....*.
gi 972776388 174 HEKLLMLLPVGYPSKE 189
Cdd:cd03370  165 HVTIAALVALGKPAEE 180
nitroreductase cd20609
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
44-185 6.70e-06

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: 44.30  E-value: 6.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388  44 APSGAHTEPWTFVVVKDPDVKHKIRKIieeeeeinymkrmghrwvtdlkklrTNWIKEyldtAPILILIFKqVHGFAANG 123
Cdd:cd20609   35 APTAVNYQPQRILVVRSEEALEKLAKA-------------------------TPRFFG----APLVIVVCY-DKDESWKR 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 972776388 124 KKKVHYYNEISVSIACG-ILLAAlQNAGLVT--VtttplnCG---PRLRVLLGRPAHEKLLMLLPVGY 185
Cdd:cd20609   85 PYDGKDSGDIDAAIVAThMMLAA-TELGLGTcwV------GNfdpEKVREAFNLPENLEPVAILPLGY 145
nitroreductase cd02150
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
44-194 4.16e-05

nitroreductase family protein; A subfamily of the nitroreductase family containing uncharacterized proteins. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer.often found to be homodimers.


Pssm-ID: 380325 [Multi-domain]  Cd Length: 156  Bit Score: 42.20  E-value: 4.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388  44 APSGAHTEPWTFVVVKDPDVKHKIRKIIEeeeeinYMKrmghrwvtdlkklrtnwikeYLDTAPILILIfkqvhgfAANG 123
Cdd:cd02150   30 APSAGNQQPWHFIVVTDREKLDKIAEAHP------YGK--------------------MLKEAPLAIVV-------CGDP 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 972776388 124 KK-KVHYYNEISVSIAC-GILLAAlQNAGLVTVTTtplNCGPR------LRVLLGRPAHEKLLMLLPVGYPSKEATVPD 194
Cdd:cd02150   77 SKeKAPGYWVQDCSAATeNILLAA-HALGLGAVWL---GVYPFeervkaIREILNIPENIIPFCVIALGYPAEEKEPKD 151
BluB cd02145
5,6-dimethylbenzimidazole synthase; BluB catalyzes the O2-dependent conversion of FMNH2 to 5, ...
26-198 3.07e-04

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: 40.03  E-value: 3.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388  26 KWLRGLRNFMNFSIRDG----------TAPSGAHTEPWTFVVVKDPDVKHKIRKIIEEEEEINYMKRMGHRwVTDLKKLR 95
Cdd:cd02145    5 RWRRDVRHFRPDPVPEEvlerllqaahLAPSVGLMQPWRFVRVRSAATRKAVHELFQRANAEAAEMYTGER-AAQYRTLK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388  96 TnwikEYLDTAPILILIF-----KQVHGFAANGKKKVHYYneisvSIACGI----LLAALQNAGLVTVTTtpLNcgP-RL 165
Cdd:cd02145   84 L----EGIEEAPLQLAVFcdrarAGGHGLGRTTMPEMDLY-----SSVCAVqnlwLAARAEGLGVGWVSI--LD--PdEV 150
                        170       180       190
                 ....*....|....*....|....*....|...
gi 972776388 166 RVLLGRPAHEKLLMLLPVGYPSKEATVPDLKRK 198
Cdd:cd02145  151 KRLLGIPEHWEPVAYLCIGYPEFFYDEPELEQA 183
BluB TIGR02476
5,6-dimethylbenzimidazole synthase; A previously published hypothesis that BluB, involved in ...
43-198 6.40e-04

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: 39.35  E-value: 6.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388   43 TAPSGAHTEPWTFVVVKDPDVKHKIRKIIEEEEEInYMKRMGHRWVTDLKKLRTNWIKEyldtAPILILIF-----KQVH 117
Cdd:TIGR02476  41 HAPSVGFSQPWRFVRVESPATREAVHALFTRANQA-AAAIYDGERASQYHRLKLEGIRE----APVQLAVFcddarGEGH 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388  118 GFAANGKKKVHYYneiSVSIACGILLAALQNAGL----VTVTTTplncgPRLRVLLGRPAHEKLLMLLPVGYPSKEATVP 193
Cdd:TIGR02476 116 GLGRHTMPEMLRY---SVACAIQNLWLAARAEGLgvgwVSILDP-----DAVRRLLGVPEGWRLVAYLCLGWPDAFYDEP 187

                  ....*
gi 972776388  194 DLKRK 198
Cdd:TIGR02476 188 ELERA 192
nitroreductase cd20610
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
44-185 1.39e-03

nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or nitrocompounds using NAD(P)H as electron donor in a obligatory two-electron transfer, utilizing FMN or FAD as cofactor. They are often found to be homodimers. Enzymes of this family are described as NAD(P)H:FMN oxidoreductases, oxygen-insensitive nitroreductase, flavin reductase P, dihydropteridine reductase, NADH oxidase or NADH dehydrogenase.


Pssm-ID: 380331 [Multi-domain]  Cd Length: 167  Bit Score: 38.03  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388  44 APSGAHTEPWTFVVVKDPDVKHKIrKIIEEEEEINYMKRMghRWVTDLKKLR-TNWIK--EYLDTAPILILIFKQVHgfa 120
Cdd:cd20610   30 APSGMNRQNWEFVVVKGGEKIEKI-GISIKKKNEEIARLL--EKVFAEKPIRfRKFRRffTLFGGAPVLVVVYTEPY--- 103
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 972776388 121 angkKKVHYYNEI--SVSIAC-GILLAAlQNAGLVTV-TTTPLNCGPRLRVLLGRPAHEKLLMLLPVGY 185
Cdd:cd20610  104 ----KPPEERKPDlqSVSAAIqNLLLAA-HALGLGTCwMTGPLYAEDEIEEILEIPDDKELVAVTPLGY 167
nitroreductase cd20608
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
22-185 2.66e-03

nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or nitrocompounds using NAD(P)H as electron donor in a obligatory two-electron transfer, utilizing FMN or FAD as cofactor. They are often found to be homodimers. Enzymes of this family are described as NAD(P)H:FMN oxidoreductases, oxygen-insensitive nitroreductase, flavin reductase P, dihydropteridine reductase, NADH oxidase or NADH dehydrogenase.


Pssm-ID: 380329 [Multi-domain]  Cd Length: 145  Bit Score: 36.93  E-value: 2.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388  22 ILRRkwlRGLRNFMNFSIRDGT----------APSGAHTEPWTFVVVKDPDVKHKIRKIieeeeeinymkrmghrwvtdl 91
Cdd:cd20608    4 IKTR---RSVRRFSDKPVEEEKlekileaarlAPSWANKQCWRFIVVTDKETLSELAKK--------------------- 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388  92 kklrTNWIKEYLDTAPILIlifkqvhgfAANGKKKV------HYYNEISVSIACGILLAALQNAGLVTVTTTPLNcGPRL 165
Cdd:cd20608   60 ----ESPSNGWLKDAPVII---------VVCADPKDsgwlngQNYYLVDAAIAMQNLMLAATDLGLGTCWIGAFD-EKKV 125
                        170       180
                 ....*....|....*....|
gi 972776388 166 RVLLGRPAHEKLLMLLPVGY 185
Cdd:cd20608  126 KEILGIPENIRVVALTPLGY 145
YdjA-like cd02135
nitroreductase family protein similar to Escherichia coli YdjA; A subfamily of the ...
44-185 4.31e-03

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: 36.43  E-value: 4.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972776388  44 APSGAHTEPWTFVVvkdpdVKHKIRKIIEEEEEINYMKRMGHRWVTDLKKLRTNWIKeyldtAPILILIFKQVHGfaanG 123
Cdd:cd02135   34 APNHGKLEPWRFIV-----VTGEGRERLAELLAAAAAARAPGADPEKLEKAREKALR-----APVVIAVVAKPDE----D 99
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 972776388 124 KKKVHYYNEISVSIAC-GILLAALQnAGLVTV-TTTPLNCGPRLRVLLGRPAHEKLLMLLPVGY 185
Cdd:cd02135  100 PKVPEWEQYAAVGAAVqNLLLAAHA-LGLGAVwRTGPVTYDPAVREALGLPEDERIVGFLYLGT 162
PRK13294 PRK13294
F420-0--gamma-glutamyl ligase; Provisional
43-91 5.61e-03

F420-0--gamma-glutamyl ligase; Provisional


Pssm-ID: 183957 [Multi-domain]  Cd Length: 448  Bit Score: 36.92  E-value: 5.61e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 972776388  43 TAPSGAHTEPWTFVVVKDPDVKHKIrkiieeeeeinyMKRMGHRWVTDL 91
Cdd:PRK13294 285 TAPAPHHTRPVRFVWLRSAAVRTRL------------LDAMRDAWRADL 321
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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