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Conserved domains on  [gi|503048878|ref|WP_013283854|]
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FMN-dependent NADH-azoreductase [Micromonospora aurantiaca]

Protein Classification

FMN-dependent NADH-azoreductase( domain architecture ID 10003095)

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

CATH:  3.40.50.360
EC:  1.-.-.-
Gene Ontology:  GO:0009055|GO:0050446|GO:0016491|GO:0050136|GO:0008753|GO:0010181
PubMed:  24915188
SCOP:  3001217

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
1-207 1.02e-70

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


:

Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 214.22  E-value: 1.02e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503048878   1 MAHLLHIDSSITGERSVSRRLTARAADAWRAAHPDGTVTYRDLGQNPLPHLDTASGLARMVPPDQHTPEQQASWRLTEEV 80
Cdd:COG1182    1 MMKLLHIDSSPRGEGSVSRRLADAFVAALRAAHPDDEVTYRDLAAEPLPHLDGAWLAAFFTPAEGRTPEQQAALALSDEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503048878  81 VAEVKRADTVLLGLPLYNYGPPSSVKSWVDHLIAPGI--AYDPVTNAGLLGDRQFVVLVSRGGGYGAGtPREGWDHAEPW 158
Cdd:COG1182   81 IDELLAADVIVIGAPMYNFGIPSQLKAWIDHIARAGRtfRYTENGPVGLLTGKKAVVITARGGVYSGG-PAAGMDFQTPY 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 503048878 159 LPHGLSLTGL-EPRFICAELTLApvNPAMAeliplfEQSLAAAERAVDEL 207
Cdd:COG1182  160 LRTVLGFIGItDVEFVRAEGTAA--GPEAA------EAALAAARAAIAEL 201
 
Name Accession Description Interval E-value
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
1-207 1.02e-70

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


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 214.22  E-value: 1.02e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503048878   1 MAHLLHIDSSITGERSVSRRLTARAADAWRAAHPDGTVTYRDLGQNPLPHLDTASGLARMVPPDQHTPEQQASWRLTEEV 80
Cdd:COG1182    1 MMKLLHIDSSPRGEGSVSRRLADAFVAALRAAHPDDEVTYRDLAAEPLPHLDGAWLAAFFTPAEGRTPEQQAALALSDEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503048878  81 VAEVKRADTVLLGLPLYNYGPPSSVKSWVDHLIAPGI--AYDPVTNAGLLGDRQFVVLVSRGGGYGAGtPREGWDHAEPW 158
Cdd:COG1182   81 IDELLAADVIVIGAPMYNFGIPSQLKAWIDHIARAGRtfRYTENGPVGLLTGKKAVVITARGGVYSGG-PAAGMDFQTPY 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 503048878 159 LPHGLSLTGL-EPRFICAELTLApvNPAMAeliplfEQSLAAAERAVDEL 207
Cdd:COG1182  160 LRTVLGFIGItDVEFVRAEGTAA--GPEAA------EAALAAARAAIAEL 201
PRK00170 PRK00170
azoreductase; Reviewed
 1-207 4.98e-31

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 112.68  E-value: 4.98e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503048878   1 MAHLLHIDSSITGERSVSRRLTARAADAWRAAHPDGTVTYRDLGQNPLPHLD--TASGLArmvPPDQH-TPEQQASWRLT 77
Cdd:PRK00170   1 MSKVLVIKSSILGDYSQSMQLGDAFIEAYKEAHPDDEVTVRDLAAEPIPVLDgeVVGALG---KSAETlTPRQQEAVALS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503048878  78 EEVVAEVKRADTVLLGLPLYNYGPPSSVKSWVDHLIAPGIAYD-----PVtnaGLLGDRQFVVLVSRGGGYgAGTPRegw 152
Cdd:PRK00170  78 DELLEEFLAADKIVIAAPMYNFSIPTQLKAYIDLIARAGKTFRytengPV---GLVTGKKALLITSRGGIH-KDGPT--- 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 503048878 153 DHAEPWLPHGLSLTGL-EPRFICAElTLApVNPAMAeliplfEQSLAAAERAVDEL 207
Cdd:PRK00170 151 DMGVPYLKTFLGFIGItDVEFVFAE-GHN-YGPEKA------AKIISAAKAAADEL 198
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 3-207 7.86e-27

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: 101.64  E-value: 7.86e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503048878    3 HLLHIDSSITGeRSVSRRLTARAADAWRAAHpdGTVTYRDLGQNPLPHLDTASGLARmvppdqhTPEQQASWRLTEEvvA 82
Cdd:pfam02525   2 KILIINAHPRP-GSFSSRLADALVEALKAAG--HEVTVRDLYALFLPVLDAEDLADL-------TYPQGAADVESEQ--E 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503048878   83 EVKRADTVLLGLPLYNYGPPSSVKSWVDHLIAPGIAYDPVTNA---GLLGDRQFVVLVSRGGG---YGA-GTPREGWDHA 155
Cdd:pfam02525  70 ELLAADVIVFQFPLYWFSVPALLKGWIDRVLRAGFAFKYEEGGpggGGLLGKKVLVIVTTGGPeyaYGKgGYNGFSLDEL 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 503048878  156 EPWLPHGLSLTGLEP-RFICAELTLAPVNpamaeliplfEQSLAAAERAVDEL 207
Cdd:pfam02525 150 LPYLRGILGFCGITDlPPFAVEGTAGPED----------EAALAEALERYEER 192
 
Name Accession Description Interval E-value
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
1-207 1.02e-70

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


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 214.22  E-value: 1.02e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503048878   1 MAHLLHIDSSITGERSVSRRLTARAADAWRAAHPDGTVTYRDLGQNPLPHLDTASGLARMVPPDQHTPEQQASWRLTEEV 80
Cdd:COG1182    1 MMKLLHIDSSPRGEGSVSRRLADAFVAALRAAHPDDEVTYRDLAAEPLPHLDGAWLAAFFTPAEGRTPEQQAALALSDEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503048878  81 VAEVKRADTVLLGLPLYNYGPPSSVKSWVDHLIAPGI--AYDPVTNAGLLGDRQFVVLVSRGGGYGAGtPREGWDHAEPW 158
Cdd:COG1182   81 IDELLAADVIVIGAPMYNFGIPSQLKAWIDHIARAGRtfRYTENGPVGLLTGKKAVVITARGGVYSGG-PAAGMDFQTPY 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 503048878 159 LPHGLSLTGL-EPRFICAELTLApvNPAMAeliplfEQSLAAAERAVDEL 207
Cdd:COG1182  160 LRTVLGFIGItDVEFVRAEGTAA--GPEAA------EAALAAARAAIAEL 201
PRK00170 PRK00170
azoreductase; Reviewed
 1-207 4.98e-31

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 112.68  E-value: 4.98e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503048878   1 MAHLLHIDSSITGERSVSRRLTARAADAWRAAHPDGTVTYRDLGQNPLPHLD--TASGLArmvPPDQH-TPEQQASWRLT 77
Cdd:PRK00170   1 MSKVLVIKSSILGDYSQSMQLGDAFIEAYKEAHPDDEVTVRDLAAEPIPVLDgeVVGALG---KSAETlTPRQQEAVALS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503048878  78 EEVVAEVKRADTVLLGLPLYNYGPPSSVKSWVDHLIAPGIAYD-----PVtnaGLLGDRQFVVLVSRGGGYgAGTPRegw 152
Cdd:PRK00170  78 DELLEEFLAADKIVIAAPMYNFSIPTQLKAYIDLIARAGKTFRytengPV---GLVTGKKALLITSRGGIH-KDGPT--- 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 503048878 153 DHAEPWLPHGLSLTGL-EPRFICAElTLApVNPAMAeliplfEQSLAAAERAVDEL 207
Cdd:PRK00170 151 DMGVPYLKTFLGFIGItDVEFVFAE-GHN-YGPEKA------AKIISAAKAAADEL 198
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 3-207 7.86e-27

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: 101.64  E-value: 7.86e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503048878    3 HLLHIDSSITGeRSVSRRLTARAADAWRAAHpdGTVTYRDLGQNPLPHLDTASGLARmvppdqhTPEQQASWRLTEEvvA 82
Cdd:pfam02525   2 KILIINAHPRP-GSFSSRLADALVEALKAAG--HEVTVRDLYALFLPVLDAEDLADL-------TYPQGAADVESEQ--E 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503048878   83 EVKRADTVLLGLPLYNYGPPSSVKSWVDHLIAPGIAYDPVTNA---GLLGDRQFVVLVSRGGG---YGA-GTPREGWDHA 155
Cdd:pfam02525  70 ELLAADVIVFQFPLYWFSVPALLKGWIDRVLRAGFAFKYEEGGpggGGLLGKKVLVIVTTGGPeyaYGKgGYNGFSLDEL 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 503048878  156 EPWLPHGLSLTGLEP-RFICAELTLAPVNpamaeliplfEQSLAAAERAVDEL 207
Cdd:pfam02525 150 LPYLRGILGFCGITDlPPFAVEGTAGPED----------EAALAEALERYEER 192
PRK13556 PRK13556
FMN-dependent NADH-azoreductase;
1-146 3.02e-13

FMN-dependent NADH-azoreductase;


Pssm-ID: 184140 [Multi-domain]  Cd Length: 208  Bit Score: 65.94  E-value: 3.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503048878   1 MAHLLHIDSS-ITGERSVSRRLTARAADAWRAAHPDGTVTYRDLGQNPLPHLDtASGLARMVPPDQH---TPEQQASWRL 76
Cdd:PRK13556   1 MSKVLFVKANnRPAEQAVSVKLYEAFLASYKEAHPNDTVVELDLYKEELPYVG-VDMINGTFKAGKGfelTEEEAKAVAV 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503048878  77 TEEVVAEVKRADTVLLGLPLYNYGPPSSVKSWVDHLIAPGIA--YDPVTNAGLLGDRQFVVLVSRGGGYGAG 146
Cdd:PRK13556  80 ADKYLNQFLEADKVVFAFPLWNFTIPAVLHTYIDYLNRAGKTfkYTPEGPVGLIGDKKVALLNARGGVYSEG 151
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 62-150 1.00e-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: 1.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503048878  62 PPDQHTPEQQASWRLTEEVVAE---VKRADTVLLGLPLYNYGPPSSVKSWVDHLIAPGIAYDPVTNA--GLLGDRQFVVL 136
Cdd:COG2249   44 DPVLSAADFYRDGPLPIDVAAEqelLLWADHLVFQFPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYpgGLLKGKKALLV 123

                         90
                 ....*....|....
gi 503048878 137 VSrgggygAGTPRE 150
Cdd:COG2249  124 VT------TGGPEE 131
PRK13555 PRK13555
FMN-dependent NADH-azoreductase;
13-145 7.95e-06

FMN-dependent NADH-azoreductase;


Pssm-ID: 184139 [Multi-domain]  Cd Length: 208  Bit Score: 45.11  E-value: 7.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503048878  13 GERSVSRRLTARAADAWRAAHPDGTVTYRDLGQNPLPHL--DTASGLARMVPPDQHTPEQQASWRLTEEVVAEVKRADTV 90
Cdd:PRK13555  14 AEQAVSSKMYETFVSTYKEANPNTEITELDLFALDLPYYgnIAISGGYKRSQGMELTAEEEKAVATVDQYLNQFLEADKV 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 503048878  91 LLGLPLYNYGPPSSVKSWVDHLIAPGIAYDPVTNA--GLLGDRQFVVLVSRGGGYGA 145
Cdd:PRK13555  94 VFAFPLWNFTVPAPLITYISYLSQAGKTFKYTANGpeGLAGGKKVVVLGARGSDYSS 150
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
33-112 8.62e-04

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 38.60  E-value: 8.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503048878  33 HPDGTVTYRDLGQNPLPHLDTAsglarmvPPDQHTPEQQASWRlteevvAEVKRADTVLLGLPLYNYGPPSSVKSWVDHL 112
Cdd:COG0431   29 AAGAEVELIDLRDLDLPLYDED-------LEADGAPPAVKALR------EAIAAADGVVIVTPEYNGSYPGVLKNALDWL 95
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 78-147 1.32e-03

Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and conversion];


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 38.37  E-value: 1.32e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503048878  78 EEVVAEVKRADTVLLGLPLYNYGPPSSVKSWVDHLiapgiaYDPVTNAGLLGDRQFVVLVSrGGGYGAGT 147
Cdd:COG0655   62 NAIYEKLLEADGIIFGSPTYFGNMSAQLKAFIDRL------YALWAKGKLLKGKVGAVFTT-GGHGGAEA 124
FMN_red pfam03358
NADPH-dependent FMN reductase;
42-115 1.45e-03

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 37.60  E-value: 1.45e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503048878   42 DLGQNPLPHLDTAsglarmVPPDQHTPEQqaswrlTEEVVAEVKRADTVLLGLPLYNYGPPSSVKSWVDHLIAP 115
Cdd:pfam03358  37 DLADLILPLCDED------LEEEQGDPDD------VQELREKIAAADAIIIVTPEYNGSVSGLLKNAIDWLSRL 98
PRK01355 PRK01355
azoreductase; Reviewed
 1-112 5.75e-03

azoreductase; Reviewed


Pssm-ID: 234946 [Multi-domain]  Cd Length: 199  Bit Score: 36.60  E-value: 5.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503048878   1 MAHLLHIDSSITG-ERSVSRRLTARAADAWRAAHPDGTVTYRDLgqNPLPHldtasglARMVPPDQHTPEQqaswrLTEE 79
Cdd:PRK01355   1 MSKVLVIKGSMVAkEKSFSSALTDKFVEEYKKVNPNDEIIILDL--NETKV-------GSVTLTSENFKTF-----FKEE 66

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 503048878  80 V----VAEVKRADTVLLGLPLYNYGPPSSVKSWVDHL 112
Cdd:PRK01355  67 VsdkyINQLKSVDKVVISCPMTNFNVPATLKNYLDHI 103
 
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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