NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|639690676|ref|WP_024720223|]
View 

MULTISPECIES: FMN-dependent NADH-azoreductase [Bacillus]

Protein Classification

FMN-dependent NADH-azoreductase( domain architecture ID 10011289)

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:  1.6.5.-|1.7.1.17
Gene Ontology:  GO:0010181|GO:0009055|GO:0050446|GO:0016491
SCOP:  3001217

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK00170 PRK00170
azoreductase; Reviewed
 1-210 3.20e-113

azoreductase; Reviewed


:

Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 321.46  E-value: 3.20e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639690676   1 MAKVLYITAHPHDETvSYSMATAKAFIESYKEANPSDEVVHIDLYKENIPHIDADVFAGWGKLQSgagfdTLSAEEQAKV 80
Cdd:PRK00170   1 MSKVLVIKSSILGDY-SQSMQLGDAFIEAYKEAHPDDEVTVRDLAAEPIPVLDGEVVGALGKSAE-----TLTPRQQEAV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639690676  81 ARLNELSDQFVSADKYVFVSPLWNFSFPPVLKAYIDSVAVAGKTFKYTEQGPVGLLTDKKALHIQARGGYYTEGPAaelE 160
Cdd:PRK00170  75 ALSDELLEEFLAADKIVIAAPMYNFSIPTQLKAYIDLIARAGKTFRYTENGPVGLVTGKKALLITSRGGIHKDGPT---D 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 639690676 161 AGHRYLGTIANFFGIPSFEGLIVEGHNAEPAKAEQIKADAIERAKALGKT 210
Cdd:PRK00170 152 MGVPYLKTFLGFIGITDVEFVFAEGHNYGPEKAAKIISAAKAAADELAAA 201
 
Name Accession Description Interval E-value
PRK00170 PRK00170
azoreductase; Reviewed
 1-210 3.20e-113

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 321.46  E-value: 3.20e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639690676   1 MAKVLYITAHPHDETvSYSMATAKAFIESYKEANPSDEVVHIDLYKENIPHIDADVFAGWGKLQSgagfdTLSAEEQAKV 80
Cdd:PRK00170   1 MSKVLVIKSSILGDY-SQSMQLGDAFIEAYKEAHPDDEVTVRDLAAEPIPVLDGEVVGALGKSAE-----TLTPRQQEAV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639690676  81 ARLNELSDQFVSADKYVFVSPLWNFSFPPVLKAYIDSVAVAGKTFKYTEQGPVGLLTDKKALHIQARGGYYTEGPAaelE 160
Cdd:PRK00170  75 ALSDELLEEFLAADKIVIAAPMYNFSIPTQLKAYIDLIARAGKTFRYTENGPVGLVTGKKALLITSRGGIHKDGPT---D 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 639690676 161 AGHRYLGTIANFFGIPSFEGLIVEGHNAEPAKAEQIKADAIERAKALGKT 210
Cdd:PRK00170 152 MGVPYLKTFLGFIGITDVEFVFAEGHNYGPEKAAKIISAAKAAADELAAA 201
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
1-211 8.05e-95

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


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 275.09  E-value: 8.05e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639690676   1 MAKVLYITAHPHDETvSYSMATAKAFIESYKEANPSDEVVHIDLYKENIPHIDADVFAGWGKLQSGagfdtLSAEEQAKV 80
Cdd:COG1182    1 MMKLLHIDSSPRGEG-SVSRRLADAFVAALRAAHPDDEVTYRDLAAEPLPHLDGAWLAAFFTPAEG-----RTPEQQAAL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639690676  81 ARLNELSDQFVSADKYVFVSPLWNFSFPPVLKAYIDSVAVAGKTFKYTEQGPVGLLTDKKALHIQARGGYYTEGPAAELE 160
Cdd:COG1182   75 ALSDELIDELLAADVIVIGAPMYNFGIPSQLKAWIDHIARAGRTFRYTENGPVGLLTGKKAVVITARGGVYSGGPAAGMD 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 639690676 161 AGHRYLGTIANFFGIPSFEGLIVEGHNAEPAKAEQIKADAIERAKALGKTF 211
Cdd:COG1182  155 FQTPYLRTVLGFIGITDVEFVRAEGTAAGPEAAEAALAAARAAIAELAAAL 205
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 3-207 4.54e-48

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: 155.95  E-value: 4.54e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639690676    3 KVLYITAHPHDEtvSYSMATAKAFIESYKEANpsDEVVHIDLYKENIPHIDADVFAGWGklqsgagfdtlSAEEQAKVAR 82
Cdd:pfam02525   2 KILIINAHPRPG--SFSSRLADALVEALKAAG--HEVTVRDLYALFLPVLDAEDLADLT-----------YPQGAADVES 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639690676   83 LNElsdQFVSADKYVFVSPLWNFSFPPVLKAYIDSVAVAGKTFKYTEQGPVG-LLTDKKALHIQARGG---YYTE--GPA 156
Cdd:pfam02525  67 EQE---ELLAADVIVFQFPLYWFSVPALLKGWIDRVLRAGFAFKYEEGGPGGgGLLGKKVLVIVTTGGpeyAYGKggYNG 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 639690676  157 AELEAGHRYLGTIANFFGIPSFEGLIVEGHNaePAKAEQIKADAIERAKAL 207
Cdd:pfam02525 144 FSLDELLPYLRGILGFCGITDLPPFAVEGTA--GPEDEAALAEALERYEER 192
 
Name Accession Description Interval E-value
PRK00170 PRK00170
azoreductase; Reviewed
 1-210 3.20e-113

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 321.46  E-value: 3.20e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639690676   1 MAKVLYITAHPHDETvSYSMATAKAFIESYKEANPSDEVVHIDLYKENIPHIDADVFAGWGKLQSgagfdTLSAEEQAKV 80
Cdd:PRK00170   1 MSKVLVIKSSILGDY-SQSMQLGDAFIEAYKEAHPDDEVTVRDLAAEPIPVLDGEVVGALGKSAE-----TLTPRQQEAV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639690676  81 ARLNELSDQFVSADKYVFVSPLWNFSFPPVLKAYIDSVAVAGKTFKYTEQGPVGLLTDKKALHIQARGGYYTEGPAaelE 160
Cdd:PRK00170  75 ALSDELLEEFLAADKIVIAAPMYNFSIPTQLKAYIDLIARAGKTFRYTENGPVGLVTGKKALLITSRGGIHKDGPT---D 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 639690676 161 AGHRYLGTIANFFGIPSFEGLIVEGHNAEPAKAEQIKADAIERAKALGKT 210
Cdd:PRK00170 152 MGVPYLKTFLGFIGITDVEFVFAEGHNYGPEKAAKIISAAKAAADELAAA 201
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
1-211 8.05e-95

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


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 275.09  E-value: 8.05e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639690676   1 MAKVLYITAHPHDETvSYSMATAKAFIESYKEANPSDEVVHIDLYKENIPHIDADVFAGWGKLQSGagfdtLSAEEQAKV 80
Cdd:COG1182    1 MMKLLHIDSSPRGEG-SVSRRLADAFVAALRAAHPDDEVTYRDLAAEPLPHLDGAWLAAFFTPAEG-----RTPEQQAAL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639690676  81 ARLNELSDQFVSADKYVFVSPLWNFSFPPVLKAYIDSVAVAGKTFKYTEQGPVGLLTDKKALHIQARGGYYTEGPAAELE 160
Cdd:COG1182   75 ALSDELIDELLAADVIVIGAPMYNFGIPSQLKAWIDHIARAGRTFRYTENGPVGLLTGKKAVVITARGGVYSGGPAAGMD 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 639690676 161 AGHRYLGTIANFFGIPSFEGLIVEGHNAEPAKAEQIKADAIERAKALGKTF 211
Cdd:COG1182  155 FQTPYLRTVLGFIGITDVEFVRAEGTAAGPEAAEAALAAARAAIAELAAAL 205
PRK13556 PRK13556
FMN-dependent NADH-azoreductase;
1-211 5.37e-74

FMN-dependent NADH-azoreductase;


Pssm-ID: 184140 [Multi-domain]  Cd Length: 208  Bit Score: 222.33  E-value: 5.37e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639690676   1 MAKVLYITAHPHDETVSYSMATAKAFIESYKEANPSDEVVHIDLYKENIPHIDADVFAGWGKLqsGAGFDtLSAEEQAKV 80
Cdd:PRK13556   1 MSKVLFVKANNRPAEQAVSVKLYEAFLASYKEAHPNDTVVELDLYKEELPYVGVDMINGTFKA--GKGFE-LTEEEAKAV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639690676  81 ARLNELSDQFVSADKYVFVSPLWNFSFPPVLKAYIDSVAVAGKTFKYTEQGPVGLLTDKKALHIQARGGYYTEGPAAELE 160
Cdd:PRK13556  78 AVADKYLNQFLEADKVVFAFPLWNFTIPAVLHTYIDYLNRAGKTFKYTPEGPVGLIGDKKVALLNARGGVYSEGPAAEVE 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 639690676 161 AGHRYLGTIANFFGIPSFEGLIVEGHNAEPAKAEQIKADAIERAKALGKTF 211
Cdd:PRK13556 158 MAVKYVASMMGFFGVTNMETVVIEGHNQFPDKAEEIITAGLEEAAKVAAKF 208
PRK13555 PRK13555
FMN-dependent NADH-azoreductase;
1-211 1.59e-48

FMN-dependent NADH-azoreductase;


Pssm-ID: 184139 [Multi-domain]  Cd Length: 208  Bit Score: 157.59  E-value: 1.59e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639690676   1 MAKVLYITAH--PHDETVSYSMAtaKAFIESYKEANPSDEVVHIDLYKENIPHIDADVFAGWGKLQSGAgfdTLSAEEQA 78
Cdd:PRK13555   1 MSKVLFVKANdrPAEQAVSSKMY--ETFVSTYKEANPNTEITELDLFALDLPYYGNIAISGGYKRSQGM---ELTAEEEK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639690676  79 KVARLNELSDQFVSADKYVFVSPLWNFSFPPVLKAYIDSVAVAGKTFKYTEQGPVGLLTDKKALHIQARGGYYTEGPAAE 158
Cdd:PRK13555  76 AVATVDQYLNQFLEADKVVFAFPLWNFTVPAPLITYISYLSQAGKTFKYTANGPEGLAGGKKVVVLGARGSDYSSEQMAP 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 639690676 159 LEAGHRYLGTIANFFGIPSFEGLIVEGHNAEPAKAEQIKADAIERAKALGKTF 211
Cdd:PRK13555 156 MEMAVNYVTTVLGFWGITNPETVVIEGHNQYPDRSQQIVEEGLENVKKVAAKF 208
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 3-207 4.54e-48

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: 155.95  E-value: 4.54e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639690676    3 KVLYITAHPHDEtvSYSMATAKAFIESYKEANpsDEVVHIDLYKENIPHIDADVFAGWGklqsgagfdtlSAEEQAKVAR 82
Cdd:pfam02525   2 KILIINAHPRPG--SFSSRLADALVEALKAAG--HEVTVRDLYALFLPVLDAEDLADLT-----------YPQGAADVES 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639690676   83 LNElsdQFVSADKYVFVSPLWNFSFPPVLKAYIDSVAVAGKTFKYTEQGPVG-LLTDKKALHIQARGG---YYTE--GPA 156
Cdd:pfam02525  67 EQE---ELLAADVIVFQFPLYWFSVPALLKGWIDRVLRAGFAFKYEEGGPGGgGLLGKKVLVIVTTGGpeyAYGKggYNG 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 639690676  157 AELEAGHRYLGTIANFFGIPSFEGLIVEGHNaePAKAEQIKADAIERAKAL 207
Cdd:pfam02525 144 FSLDELLPYLRGILGFCGITDLPPFAVEGTA--GPEDEAALAEALERYEER 192
PRK01355 PRK01355
azoreductase; Reviewed
 1-205 2.06e-27

azoreductase; Reviewed


Pssm-ID: 234946 [Multi-domain]  Cd Length: 199  Bit Score: 102.85  E-value: 2.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639690676   1 MAKVLYITAHPHDETVSYSMATAKAFIESYKEANPSDEVVHIDLYKENiphiDADVFAgwgklqSGAGFDTLSAEEQAKv 80
Cdd:PRK01355   1 MSKVLVIKGSMVAKEKSFSSALTDKFVEEYKKVNPNDEIIILDLNETK----VGSVTL------TSENFKTFFKEEVSD- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639690676  81 arlnELSDQFVSADKYVFVSPLWNFSFPPVLKAYIDSVAVAGKTF--KYTEQG-PVGLLTDKKALHIQARG---GYYTEG 154
Cdd:PRK01355  70 ----KYINQLKSVDKVVISCPMTNFNVPATLKNYLDHIAVANKTFsyKYSKKGdAIGLLDHLKVQILTTQGaplGWYPWG 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 639690676 155 PAAEleaghrYLGTIANFFGIPSFEGLIVEGHNAEPAKA-------EQIKADAIERAK 205
Cdd:PRK01355 146 SHTN------YLEGTWEFLGAKVVDSILLAGTKVEPLSNktpkeivEEFDKEIIEKAK 197
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 3-211 4.83e-22

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 88.74  E-value: 4.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639690676   3 KVLYITAHPHDEtvSYSMATAKAFIESYKEANpsDEVVHIDLYKENI-PHIDADVFAGWGKLQsgagFDTlsAEEQAKVA 81
Cdd:COG2249    1 KILIIYAHPDPS--SFNAALAEAAAEGLEAAG--HEVTVHDLYAEGFdPVLSAADFYRDGPLP----IDV--AAEQELLL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639690676  82 RlnelsdqfvsADKYVFVSPLWNFSFPPVLKAYIDSVAVAGKTFKYTEQGPVGLLTDKKALHIQ---------ARGGYYt 152
Cdd:COG2249   71 W----------ADHLVFQFPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYPGGLLKGKKALLVVttggpeeaySRLGYG- 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 639690676 153 egpaaelEAGHRYLG-TIANFFGIPSFEGLIVegHNAEPAKAEQIKAdAIERAKALGKTF 211
Cdd:COG2249  140 -------GPIEELLFrGTLGYCGMKVLPPFVL--YGVDRSSDEERAA-WLERVRELLAAL 189
PRK09739 PRK09739
NAD(P)H oxidoreductase;
1-209 1.32e-08

NAD(P)H oxidoreductase;


Pssm-ID: 236620 [Multi-domain]  Cd Length: 199  Bit Score: 52.78  E-value: 1.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639690676   1 MAKVLYITAHPHDEtvSYSMATAKAFIESYKEAnpSDEVVHIDLYKEN----IPHIDADVFAGWGKlqsgagfdTLSAEE 76
Cdd:PRK09739   3 SMRIYLVWAHPRHD--SLTAKVAEAIHQRAQER--GHQVEELDLYRSGfdpvLTPEDEPDWKNPDK--------RYSPEV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639690676  77 QAKVARLNElsdqfvsADKYVFVSPLWNFSFPPVLKAYIDSVAVAGktFKYteqGPVGLLTDKKALHIQARGG------- 149
Cdd:PRK09739  71 HQLYSELLE-------HDALVFVFPLWWYSFPAMLKGYIDRVWNNG--LAY---GDGHKLPFNKVRWVALVGGskesfvk 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 639690676 150 -YYTEGPAAELEAGhrylgtIANFFGIPS------FEGLIVEGHNAEPAKAEQIKADAIERAKALGK 209
Cdd:PRK09739 139 rGWEKNMSDYLNVG------MASYLGIEDsdvtflYNTLVFDGEELHASHYQSLLSQAREMVDALAK 199
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
17-137 3.63e-08

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 50.92  E-value: 3.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639690676  17 SYSMATAKAFIESYKEANpsDEVVHIDLYKENIPHIDADVfagwgklqsgagfdtlsaEEQAKVARLNELSDQFVSADKY 96
Cdd:COG0431   14 SFNRKLARAAAELAPAAG--AEVELIDLRDLDLPLYDEDL------------------EADGAPPAVKALREAIAAADGV 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 639690676  97 VFVSPLWNFSFPPVLKAYIDSV---AVAGKtfkyteqgPVGLLT 137
Cdd:COG0431   74 VIVTPEYNGSYPGVLKNALDWLsrsELAGK--------PVALVS 109
FMN_red pfam03358
NADPH-dependent FMN reductase;
3-116 5.40e-06

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 44.54  E-value: 5.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639690676    3 KVLYITAHPHDEtvSYSMATAKAFIEsykEANPSDEVVHIDLYKENIPHIDADVfagwgklqsgagfdtlsAEEQAKVAR 82
Cdd:pfam03358   2 KILAISGSPRKG--SNTRKLARWAAE---LLEEGAEVELIDLADLILPLCDEDL-----------------EEEQGDPDD 59

                          90       100       110
                  ....*....|....*....|....*....|....
gi 639690676   83 LNELSDQFVSADKYVFVSPLWNFSFPPVLKAYID 116
Cdd:pfam03358  60 VQELREKIAAADAIIIVTPEYNGSVSGLLKNAID 93
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 3-209 1.78e-04

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 40.68  E-value: 1.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639690676   3 KVLYITAHPHDETVSYSMAtaKAFIESYKEANPsdEVVHIDLYKENIPHIDADVFAGWGKLQSGagfdtlsaeeqakvar 82
Cdd:COG0655    1 KILVINGSPRKNGNTAALA--EAVAEGAEEAGA--EVELIRLADLDIKPCIGCGGTGKCVIKDD---------------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639690676  83 LNELSDQFVSADKYVFVSPLWNFSFPPVLKAYIDsvavagKTFKYTEQGpvGLLTDKKAlhiqarGGYYTegpaAELEAG 162
Cdd:COG0655   61 MNAIYEKLLEADGIIFGSPTYFGNMSAQLKAFID------RLYALWAKG--KLLKGKVG------AVFTT----GGHGGA 122

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 639690676 163 HRYLGTIANFFGIPSFE--GLIVEGHNAEPAKAEQIKADAIERAKALGK 209
Cdd:COG0655  123 EATLLSLNTFLLHHGMIvvGLPPYGAVGGGGPGDVLDEEGLATARELGK 171
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH