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Conserved domains on  [gi|446444673|ref|WP_000522528|]
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MULTISPECIES: FMN-dependent NADH-azoreductase [Bacillus]

Protein Classification

FMN-dependent NADH-azoreductase( domain architecture ID 10014280)

FMN-dependent NADH-azoreductase catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to form the corresponding amines; requires NADH, but not NADPH, as an electron donor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13555 PRK13555
FMN-dependent NADH-azoreductase;
23-230 4.30e-141

FMN-dependent NADH-azoreductase;


:

Pssm-ID: 184139 [Multi-domain]  Cd Length: 208  Bit Score: 393.34  E-value: 4.30e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444673  23 MSKVLFVKANDRPAEQAVSSKMYETFVSTYKEANPNTEITELDLFALDLPYYGNIAISGGYKRSQGMELTAEEEKAVATV 102
Cdd:PRK13555   1 MSKVLFVKANDRPAEQAVSSKMYETFVSTYKEANPNTEITELDLFALDLPYYGNIAISGGYKRSQGMELTAEEEKAVATV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444673 103 DQYLNQFLEADKVVFAFPLWNFTVPAPLITYISYLSQAGKTFKYTANGPEGLVGGKKVVVLGARGSDYSSEQMAPMEMAV 182
Cdd:PRK13555  81 DQYLNQFLEADKVVFAFPLWNFTVPAPLITYISYLSQAGKTFKYTANGPEGLAGGKKVVVLGARGSDYSSEQMAPMEMAV 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 446444673 183 NYVTTVLGFWGITNPETVVIEGHNQYPDRSQQIVEEGLENVKKVAAKF 230
Cdd:PRK13555 161 NYVTTVLGFWGITNPETVVIEGHNQYPDRSQQIVEEGLENVKKVAAKF 208
 
Name Accession Description Interval E-value
PRK13555 PRK13555
FMN-dependent NADH-azoreductase;
23-230 4.30e-141

FMN-dependent NADH-azoreductase;


Pssm-ID: 184139 [Multi-domain]  Cd Length: 208  Bit Score: 393.34  E-value: 4.30e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444673  23 MSKVLFVKANDRPAEQAVSSKMYETFVSTYKEANPNTEITELDLFALDLPYYGNIAISGGYKRSQGMELTAEEEKAVATV 102
Cdd:PRK13555   1 MSKVLFVKANDRPAEQAVSSKMYETFVSTYKEANPNTEITELDLFALDLPYYGNIAISGGYKRSQGMELTAEEEKAVATV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444673 103 DQYLNQFLEADKVVFAFPLWNFTVPAPLITYISYLSQAGKTFKYTANGPEGLVGGKKVVVLGARGSDYSSEQMAPMEMAV 182
Cdd:PRK13555  81 DQYLNQFLEADKVVFAFPLWNFTVPAPLITYISYLSQAGKTFKYTANGPEGLAGGKKVVVLGARGSDYSSEQMAPMEMAV 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 446444673 183 NYVTTVLGFWGITNPETVVIEGHNQYPDRSQQIVEEGLENVKKVAAKF 230
Cdd:PRK13555 161 NYVTTVLGFWGITNPETVVIEGHNQYPDRSQQIVEEGLENVKKVAAKF 208
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
23-230 8.80e-88

FMN-dependent NADH-azoreductase [Energy production and conversion];


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 258.14  E-value: 8.80e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444673  23 MSKVLFVKANDRpAEQAVSSKMYETFVSTYKEANPNTEITELDLFALDLPYYGNIAISGGYKRSQGmeLTAEEEKAVATV 102
Cdd:COG1182    1 MMKLLHIDSSPR-GEGSVSRRLADAFVAALRAAHPDDEVTYRDLAAEPLPHLDGAWLAAFFTPAEG--RTPEQQAALALS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444673 103 DQYLNQFLEADKVVFAFPLWNFTVPAPLITYISYLSQAGKTFKYTANGPEGLVGGKKVVVLGARGSDYSSEQMAPMEMAV 182
Cdd:COG1182   78 DELIDELLAADVIVIGAPMYNFGIPSQLKAWIDHIARAGRTFRYTENGPVGLLTGKKAVVITARGGVYSGGPAAGMDFQT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 446444673 183 NYVTTVLGFWGITNPETVVIEGHNQYPDRSQQIVEEGLENVKKVAAKF 230
Cdd:COG1182  158 PYLRTVLGFIGITDVEFVRAEGTAAGPEAAEAALAAARAAIAELAAAL 205
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 24-225 1.50e-42

Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family includes bacterial and eukaryotic NAD(P)H dehydrogenase (quinone) EC:1.6.99.2. These enzymes catalyze the NAD(P)H-dependent two-electron reductions of quinones and protect cells against damage by free radicals and reactive oxygen species. This enzyme uses a FAD co-factor. The equation for this reaction is:- NAD(P)H + acceptor <=> NAD(P)(+) + reduced acceptor. This enzyme is also involved in the bioactivation of prodrugs used in chemotherapy. The family also includes acyl carrier protein phosphodiesterase EC:3.1.4.14. This enzyme converts holo-ACP to apo-ACP by hydrolytic cleavage of the phosphopantetheine residue from ACP. This family is related to pfam03358 and pfam00258.


Pssm-ID: 426816 [Multi-domain]  Cd Length: 193  Bit Score: 142.47  E-value: 1.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444673   24 SKVLFVKANDRPaeQAVSSKMYETFVSTYKEANpnTEITELDLFALDLPYYGNIAISGgykrsqgmeLTAEEEKAVATVD 103
Cdd:pfam02525   1 MKILIINAHPRP--GSFSSRLADALVEALKAAG--HEVTVRDLYALFLPVLDAEDLAD---------LTYPQGAADVESE 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444673  104 QylNQFLEADKVVFAFPLWNFTVPAPLITYISYLSQAGKTFKYTANGPEG-LVGGKKVVVLGARGSDYSSEQ-----MAP 177
Cdd:pfam02525  68 Q--EELLAADVIVFQFPLYWFSVPALLKGWIDRVLRAGFAFKYEEGGPGGgGLLGKKVLVIVTTGGPEYAYGkggynGFS 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 446444673  178 MEMAVNYVTTVLGFWGITNPETVVIEGHNqYPDRsQQIVEEGLENVKK 225
Cdd:pfam02525 146 LDELLPYLRGILGFCGITDLPPFAVEGTA-GPED-EAALAEALERYEE 191
 
Name Accession Description Interval E-value
PRK13555 PRK13555
FMN-dependent NADH-azoreductase;
23-230 4.30e-141

FMN-dependent NADH-azoreductase;


Pssm-ID: 184139 [Multi-domain]  Cd Length: 208  Bit Score: 393.34  E-value: 4.30e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444673  23 MSKVLFVKANDRPAEQAVSSKMYETFVSTYKEANPNTEITELDLFALDLPYYGNIAISGGYKRSQGMELTAEEEKAVATV 102
Cdd:PRK13555   1 MSKVLFVKANDRPAEQAVSSKMYETFVSTYKEANPNTEITELDLFALDLPYYGNIAISGGYKRSQGMELTAEEEKAVATV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444673 103 DQYLNQFLEADKVVFAFPLWNFTVPAPLITYISYLSQAGKTFKYTANGPEGLVGGKKVVVLGARGSDYSSEQMAPMEMAV 182
Cdd:PRK13555  81 DQYLNQFLEADKVVFAFPLWNFTVPAPLITYISYLSQAGKTFKYTANGPEGLAGGKKVVVLGARGSDYSSEQMAPMEMAV 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 446444673 183 NYVTTVLGFWGITNPETVVIEGHNQYPDRSQQIVEEGLENVKKVAAKF 230
Cdd:PRK13555 161 NYVTTVLGFWGITNPETVVIEGHNQYPDRSQQIVEEGLENVKKVAAKF 208
PRK13556 PRK13556
FMN-dependent NADH-azoreductase;
23-230 7.38e-119

FMN-dependent NADH-azoreductase;


Pssm-ID: 184140 [Multi-domain]  Cd Length: 208  Bit Score: 336.73  E-value: 7.38e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444673  23 MSKVLFVKANDRPAEQAVSSKMYETFVSTYKEANPNTEITELDLFALDLPYYGNIAISGGYKRSQGMELTAEEEKAVATV 102
Cdd:PRK13556   1 MSKVLFVKANNRPAEQAVSVKLYEAFLASYKEAHPNDTVVELDLYKEELPYVGVDMINGTFKAGKGFELTEEEAKAVAVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444673 103 DQYLNQFLEADKVVFAFPLWNFTVPAPLITYISYLSQAGKTFKYTANGPEGLVGGKKVVVLGARGSDYSSEQMAPMEMAV 182
Cdd:PRK13556  81 DKYLNQFLEADKVVFAFPLWNFTIPAVLHTYIDYLNRAGKTFKYTPEGPVGLIGDKKVALLNARGGVYSEGPAAEVEMAV 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 446444673 183 NYVTTVLGFWGITNPETVVIEGHNQYPDRSQQIVEEGLENVKKVAAKF 230
Cdd:PRK13556 161 KYVASMMGFFGVTNMETVVIEGHNQFPDKAEEIITAGLEEAAKVAAKF 208
PRK00170 PRK00170
azoreductase; Reviewed
 23-228 3.97e-88

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 258.67  E-value: 3.97e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444673  23 MSKVLFVKANDRpAEQAVSSKMYETFVSTYKEANPNTEITELDLFALDLPYYGNIAISGGYKRSQgmELTAEEEKAVATV 102
Cdd:PRK00170   1 MSKVLVIKSSIL-GDYSQSMQLGDAFIEAYKEAHPDDEVTVRDLAAEPIPVLDGEVVGALGKSAE--TLTPRQQEAVALS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444673 103 DQYLNQFLEADKVVFAFPLWNFTVPAPLITYISYLSQAGKTFKYTANGPEGLVGGKKVVVLGARGSDYSSEqmaPMEMAV 182
Cdd:PRK00170  78 DELLEEFLAADKIVIAAPMYNFSIPTQLKAYIDLIARAGKTFRYTENGPVGLVTGKKALLITSRGGIHKDG---PTDMGV 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446444673 183 NYVTTVLGFWGITNPETVVIEGHNQYPDRSQQIVEEGLENVKKVAA 228
Cdd:PRK00170 155 PYLKTFLGFIGITDVEFVFAEGHNYGPEKAAKIISAAKAAADELAA 200
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
23-230 8.80e-88

FMN-dependent NADH-azoreductase [Energy production and conversion];


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 258.14  E-value: 8.80e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444673  23 MSKVLFVKANDRpAEQAVSSKMYETFVSTYKEANPNTEITELDLFALDLPYYGNIAISGGYKRSQGmeLTAEEEKAVATV 102
Cdd:COG1182    1 MMKLLHIDSSPR-GEGSVSRRLADAFVAALRAAHPDDEVTYRDLAAEPLPHLDGAWLAAFFTPAEG--RTPEQQAALALS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444673 103 DQYLNQFLEADKVVFAFPLWNFTVPAPLITYISYLSQAGKTFKYTANGPEGLVGGKKVVVLGARGSDYSSEQMAPMEMAV 182
Cdd:COG1182   78 DELIDELLAADVIVIGAPMYNFGIPSQLKAWIDHIARAGRTFRYTENGPVGLLTGKKAVVITARGGVYSGGPAAGMDFQT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 446444673 183 NYVTTVLGFWGITNPETVVIEGHNQYPDRSQQIVEEGLENVKKVAAKF 230
Cdd:COG1182  158 PYLRTVLGFIGITDVEFVRAEGTAAGPEAAEAALAAARAAIAELAAAL 205
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 24-225 1.50e-42

Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family includes bacterial and eukaryotic NAD(P)H dehydrogenase (quinone) EC:1.6.99.2. These enzymes catalyze the NAD(P)H-dependent two-electron reductions of quinones and protect cells against damage by free radicals and reactive oxygen species. This enzyme uses a FAD co-factor. The equation for this reaction is:- NAD(P)H + acceptor <=> NAD(P)(+) + reduced acceptor. This enzyme is also involved in the bioactivation of prodrugs used in chemotherapy. The family also includes acyl carrier protein phosphodiesterase EC:3.1.4.14. This enzyme converts holo-ACP to apo-ACP by hydrolytic cleavage of the phosphopantetheine residue from ACP. This family is related to pfam03358 and pfam00258.


Pssm-ID: 426816 [Multi-domain]  Cd Length: 193  Bit Score: 142.47  E-value: 1.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444673   24 SKVLFVKANDRPaeQAVSSKMYETFVSTYKEANpnTEITELDLFALDLPYYGNIAISGgykrsqgmeLTAEEEKAVATVD 103
Cdd:pfam02525   1 MKILIINAHPRP--GSFSSRLADALVEALKAAG--HEVTVRDLYALFLPVLDAEDLAD---------LTYPQGAADVESE 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444673  104 QylNQFLEADKVVFAFPLWNFTVPAPLITYISYLSQAGKTFKYTANGPEG-LVGGKKVVVLGARGSDYSSEQ-----MAP 177
Cdd:pfam02525  68 Q--EELLAADVIVFQFPLYWFSVPALLKGWIDRVLRAGFAFKYEEGGPGGgGLLGKKVLVIVTTGGPEYAYGkggynGFS 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 446444673  178 MEMAVNYVTTVLGFWGITNPETVVIEGHNqYPDRsQQIVEEGLENVKK 225
Cdd:pfam02525 146 LDELLPYLRGILGFCGITDLPPFAVEGTA-GPED-EAALAEALERYEE 191
PRK01355 PRK01355
azoreductase; Reviewed
 23-230 4.27e-24

azoreductase; Reviewed


Pssm-ID: 234946 [Multi-domain]  Cd Length: 199  Bit Score: 94.76  E-value: 4.27e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444673  23 MSKVLFVKANDRPAEQAVSSKMYETFVSTYKEANPNTEITELDLFALDLpyyGNIAISggykrSQGMELTAEEEKavatV 102
Cdd:PRK01355   1 MSKVLVIKGSMVAKEKSFSSALTDKFVEEYKKVNPNDEIIILDLNETKV---GSVTLT-----SENFKTFFKEEV----S 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444673 103 DQYLNQFLEADKVVFAFPLWNFTVPAPLITYISYLSQAGKTF--KYTANGPE-GLVGGKKVVVLGARGsdySSEQMAPME 179
Cdd:PRK01355  69 DKYINQLKSVDKVVISCPMTNFNVPATLKNYLDHIAVANKTFsyKYSKKGDAiGLLDHLKVQILTTQG---APLGWYPWG 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446444673 180 MAVNYVTTVLGFWGITNPETVVIEG------HNQYPdrsQQIVEEGLENVKKVAAKF 230
Cdd:PRK01355 146 SHTNYLEGTWEFLGAKVVDSILLAGtkveplSNKTP---KEIVEEFDKEIIEKAKNF 199
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 25-179 1.54e-06

Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction only];


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 47.14  E-value: 1.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444673  25 KVLFVKANdrPAEQAVSSKMYETFVSTYKEANpnTEITELDLFALDLPyygniAISGGYKRSQGMELTAEeekavatVDQ 104
Cdd:COG2249    1 KILIIYAH--PDPSSFNAALAEAAAEGLEAAG--HEVTVHDLYAEGFD-----PVLSAADFYRDGPLPID-------VAA 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444673 105 YLNQFLEADKVVFAFPLWNFTVPAPLITYI----SYlsqaGKTFKYTANGPEGLVGGKKVVVL---GARGSDYSSEQM-A 176
Cdd:COG2249   65 EQELLLWADHLVFQFPLWWYSMPALLKGWIdrvlTP----GFAYGYGGGYPGGLLKGKKALLVvttGGPEEAYSRLGYgG 140


                 ...
gi 446444673 177 PME 179
Cdd:COG2249  141 PIE 143
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
60-221 3.65e-03

NAD(P)H-dependent FMN reductase [Energy production and conversion];


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 36.67  E-value: 3.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444673  60 EITELDLFALDLPYYGNiaisggykrsqgmelTAEEEKAVATVDQYLNQFLEADKVVFAFPLWNFTVPAPLITYISYLSQ 139
Cdd:COG0431   33 EVELIDLRDLDLPLYDE---------------DLEADGAPPAVKALREAIAAADGVVIVTPEYNGSYPGVLKNALDWLSR 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444673 140 AGktFKytangpeglvgGKKVVVLGARGSDYSSeqmapmEMAVNYVTTVLGFWG-ITNPETVVIEGHNQYPDRSQQIVEE 218
Cdd:COG0431   98 SE--LA-----------GKPVALVSTSGGARGG------LRALEHLRPVLSELGaVVLPPQVSIPKAGEAFDEDGELTDE 158


                 ...
gi 446444673 219 GLE 221
Cdd:COG0431  159 ELA 161
 
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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