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Conserved domains on  [gi|489819990|ref|WP_003723799|]
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FMN-dependent NADH-azoreductase [Listeria monocytogenes]

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];
1-211 2.36e-80

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


:

Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 238.49  E-value: 2.36e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819990   1 MSKVLFIKASPLPNEvSRSSQVAETFMAEYKAKNPSDTVEELVLYNTEVPLLDLELMTAgrelqAGKAFTDLAPDVQKKL 80
Cdd:COG1182    1 MMKLLHIDSSPRGEG-SVSRRLADAFVAALRAAHPDDEVTYRDLAAEPLPHLDGAWLAA-----FFTPAEGRTPEQQAAL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819990  81 NAYNALTEQFLAADKYVFVFPLWNLGIPPLLKAYIDTFVIAGKSFRYTEHGPEALLKDKKAILIHGSGGIYSAGPTSSFT 160
Cdd:COG1182   75 ALSDELIDELLAADVIVIGAPMYNFGIPSQLKAWIDHIARAGRTFRYTENGPVGLLTGKKAVVITARGGVYSGGPAAGMD 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489819990 161 HGEPYLRTILQFIGINVVPSIFVEGIDHNPSKEAEIVAAAKAVAQESATEF 211
Cdd:COG1182  155 FQTPYLRTVLGFIGITDVEFVRAEGTAAGPEAAEAALAAARAAIAELAAAL 205
 
Name Accession Description Interval E-value
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
1-211 2.36e-80

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


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 238.49  E-value: 2.36e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819990   1 MSKVLFIKASPLPNEvSRSSQVAETFMAEYKAKNPSDTVEELVLYNTEVPLLDLELMTAgrelqAGKAFTDLAPDVQKKL 80
Cdd:COG1182    1 MMKLLHIDSSPRGEG-SVSRRLADAFVAALRAAHPDDEVTYRDLAAEPLPHLDGAWLAA-----FFTPAEGRTPEQQAAL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819990  81 NAYNALTEQFLAADKYVFVFPLWNLGIPPLLKAYIDTFVIAGKSFRYTEHGPEALLKDKKAILIHGSGGIYSAGPTSSFT 160
Cdd:COG1182   75 ALSDELIDELLAADVIVIGAPMYNFGIPSQLKAWIDHIARAGRTFRYTENGPVGLLTGKKAVVITARGGVYSGGPAAGMD 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489819990 161 HGEPYLRTILQFIGINVVPSIFVEGIDHNPSKEAEIVAAAKAVAQESATEF 211
Cdd:COG1182  155 FQTPYLRTVLGFIGITDVEFVRAEGTAAGPEAAEAALAAARAAIAELAAAL 205
PRK00170 PRK00170
azoreductase; Reviewed
 1-209 1.15e-76

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 229.01  E-value: 1.15e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819990   1 MSKVLFIKASPLPNEvSRSSQVAETFMAEYKAKNPSDTVEELVLYNTEVPLLDLELMTAGRELQAgkaftDLAPDVQKKL 80
Cdd:PRK00170   1 MSKVLVIKSSILGDY-SQSMQLGDAFIEAYKEAHPDDEVTVRDLAAEPIPVLDGEVVGALGKSAE-----TLTPRQQEAV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819990  81 NAYNALTEQFLAADKYVFVFPLWNLGIPPLLKAYIDTFVIAGKSFRYTEHGPEALLKDKKAILIHGSGGIYSAGPTSsft 160
Cdd:PRK00170  75 ALSDELLEEFLAADKIVIAAPMYNFSIPTQLKAYIDLIARAGKTFRYTENGPVGLVTGKKALLITSRGGIHKDGPTD--- 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 489819990 161 HGEPYLRTILQFIGINVVPSIFVEGIDHNPSKEAEIVAAAKAVAQESAT 209
Cdd:PRK00170 152 MGVPYLKTFLGFIGITDVEFVFAEGHNYGPEKAAKIISAAKAAADELAA 200
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 2-205 4.69e-49

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: 158.27  E-value: 4.69e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819990    2 SKVLFIKASPLPNevSRSSQVAETFMAEYKAKNpsDTVEELVLYNTEVPLLDLELMtagrelqAGKAFTDLAPDVQkkln 81
Cdd:pfam02525   1 MKILIINAHPRPG--SFSSRLADALVEALKAAG--HEVTVRDLYALFLPVLDAEDL-------ADLTYPQGAADVE---- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819990   82 aynALTEQFLAADKYVFVFPLWNLGIPPLLKAYIDTFVIAGKSFRYTEHGPEA-LLKDKKAILIHGSGGIYSA-----GP 155
Cdd:pfam02525  66 ---SEQEELLAADVIVFQFPLYWFSVPALLKGWIDRVLRAGFAFKYEEGGPGGgGLLGKKVLVIVTTGGPEYAygkggYN 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 489819990  156 TSSFTHGEPYLRTILQFIGINVVPSIFVEGIdHNPSKEAEIVAAAKAVAQ 205
Cdd:pfam02525 143 GFSLDELLPYLRGILGFCGITDLPPFAVEGT-AGPEDEAALAEALERYEE 191
 
Name Accession Description Interval E-value
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
1-211 2.36e-80

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


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 238.49  E-value: 2.36e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819990   1 MSKVLFIKASPLPNEvSRSSQVAETFMAEYKAKNPSDTVEELVLYNTEVPLLDLELMTAgrelqAGKAFTDLAPDVQKKL 80
Cdd:COG1182    1 MMKLLHIDSSPRGEG-SVSRRLADAFVAALRAAHPDDEVTYRDLAAEPLPHLDGAWLAA-----FFTPAEGRTPEQQAAL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819990  81 NAYNALTEQFLAADKYVFVFPLWNLGIPPLLKAYIDTFVIAGKSFRYTEHGPEALLKDKKAILIHGSGGIYSAGPTSSFT 160
Cdd:COG1182   75 ALSDELIDELLAADVIVIGAPMYNFGIPSQLKAWIDHIARAGRTFRYTENGPVGLLTGKKAVVITARGGVYSGGPAAGMD 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489819990 161 HGEPYLRTILQFIGINVVPSIFVEGIDHNPSKEAEIVAAAKAVAQESATEF 211
Cdd:COG1182  155 FQTPYLRTVLGFIGITDVEFVRAEGTAAGPEAAEAALAAARAAIAELAAAL 205
PRK00170 PRK00170
azoreductase; Reviewed
 1-209 1.15e-76

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 229.01  E-value: 1.15e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819990   1 MSKVLFIKASPLPNEvSRSSQVAETFMAEYKAKNPSDTVEELVLYNTEVPLLDLELMTAGRELQAgkaftDLAPDVQKKL 80
Cdd:PRK00170   1 MSKVLVIKSSILGDY-SQSMQLGDAFIEAYKEAHPDDEVTVRDLAAEPIPVLDGEVVGALGKSAE-----TLTPRQQEAV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819990  81 NAYNALTEQFLAADKYVFVFPLWNLGIPPLLKAYIDTFVIAGKSFRYTEHGPEALLKDKKAILIHGSGGIYSAGPTSsft 160
Cdd:PRK00170  75 ALSDELLEEFLAADKIVIAAPMYNFSIPTQLKAYIDLIARAGKTFRYTENGPVGLVTGKKALLITSRGGIHKDGPTD--- 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 489819990 161 HGEPYLRTILQFIGINVVPSIFVEGIDHNPSKEAEIVAAAKAVAQESAT 209
Cdd:PRK00170 152 MGVPYLKTFLGFIGITDVEFVFAEGHNYGPEKAAKIISAAKAAADELAA 200
PRK13556 PRK13556
FMN-dependent NADH-azoreductase;
1-211 1.79e-54

FMN-dependent NADH-azoreductase;


Pssm-ID: 184140 [Multi-domain]  Cd Length: 208  Bit Score: 172.64  E-value: 1.79e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819990   1 MSKVLFIKASPLPNEVSRSSQVAETFMAEYKAKNPSDTVEELVLYNTEVPLLDLELMTAGreLQAGKAFtDLAPDVQKKL 80
Cdd:PRK13556   1 MSKVLFVKANNRPAEQAVSVKLYEAFLASYKEAHPNDTVVELDLYKEELPYVGVDMINGT--FKAGKGF-ELTEEEAKAV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819990  81 NAYNALTEQFLAADKYVFVFPLWNLGIPPLLKAYIDTFVIAGKSFRYTEHGPEALLKDKKAILIHGSGGIYSAGPTSSFT 160
Cdd:PRK13556  78 AVADKYLNQFLEADKVVFAFPLWNFTIPAVLHTYIDYLNRAGKTFKYTPEGPVGLIGDKKVALLNARGGVYSEGPAAEVE 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489819990 161 HGEPYLRTILQFIGINVVPSIFVEGIDHNPSKEAEIVAAAKAVAQESATEF 211
Cdd:PRK13556 158 MAVKYVASMMGFFGVTNMETVVIEGHNQFPDKAEEIITAGLEEAAKVAAKF 208
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 2-205 4.69e-49

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: 158.27  E-value: 4.69e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819990    2 SKVLFIKASPLPNevSRSSQVAETFMAEYKAKNpsDTVEELVLYNTEVPLLDLELMtagrelqAGKAFTDLAPDVQkkln 81
Cdd:pfam02525   1 MKILIINAHPRPG--SFSSRLADALVEALKAAG--HEVTVRDLYALFLPVLDAEDL-------ADLTYPQGAADVE---- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819990   82 aynALTEQFLAADKYVFVFPLWNLGIPPLLKAYIDTFVIAGKSFRYTEHGPEA-LLKDKKAILIHGSGGIYSA-----GP 155
Cdd:pfam02525  66 ---SEQEELLAADVIVFQFPLYWFSVPALLKGWIDRVLRAGFAFKYEEGGPGGgGLLGKKVLVIVTTGGPEYAygkggYN 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 489819990  156 TSSFTHGEPYLRTILQFIGINVVPSIFVEGIdHNPSKEAEIVAAAKAVAQ 205
Cdd:pfam02525 143 GFSLDELLPYLRGILGFCGITDLPPFAVEGT-AGPEDEAALAEALERYEE 191
PRK13555 PRK13555
FMN-dependent NADH-azoreductase;
1-211 8.63e-37

FMN-dependent NADH-azoreductase;


Pssm-ID: 184139 [Multi-domain]  Cd Length: 208  Bit Score: 127.55  E-value: 8.63e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819990   1 MSKVLFIKASPLPNEVSRSSQVAETFMAEYKAKNPSDTVEELVLYNTEVPLLDLELMTAGRELQAGkafTDLAPDVQKKL 80
Cdd:PRK13555   1 MSKVLFVKANDRPAEQAVSSKMYETFVSTYKEANPNTEITELDLFALDLPYYGNIAISGGYKRSQG---MELTAEEEKAV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819990  81 NAYNALTEQFLAADKYVFVFPLWNLGIPPLLKAYIDTFVIAGKSFRYTEHGPEALLKDKKAILIHGSGGIYSAGPTSSFT 160
Cdd:PRK13555  78 ATVDQYLNQFLEADKVVFAFPLWNFTVPAPLITYISYLSQAGKTFKYTANGPEGLAGGKKVVVLGARGSDYSSEQMAPME 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489819990 161 HGEPYLRTILQFIGINVVPSIFVEGIDHNPSKEAEIVAAAKAVAQESATEF 211
Cdd:PRK13555 158 MAVNYVTTVLGFWGITNPETVVIEGHNQYPDRSQQIVEEGLENVKKVAAKF 208
PRK01355 PRK01355
azoreductase; Reviewed
 1-211 2.85e-25

azoreductase; Reviewed


Pssm-ID: 234946 [Multi-domain]  Cd Length: 199  Bit Score: 97.46  E-value: 2.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819990   1 MSKVLFIKASPLPNEVSRSSQVAETFMAEYKAKNPSDTVEELVLYNTEVPLLDLelmtagrelqAGKAFTDLAPDVQKKl 80
Cdd:PRK01355   1 MSKVLVIKGSMVAKEKSFSSALTDKFVEEYKKVNPNDEIIILDLNETKVGSVTL----------TSENFKTFFKEEVSD- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819990  81 naynALTEQFLAADKYVFVFPLWNLGIPPLLKAYIDTFVIAGKSF--RYTEHGPEALLKDKKAILIHGSGGiysaGPTSS 158
Cdd:PRK01355  70 ----KYINQLKSVDKVVISCPMTNFNVPATLKNYLDHIAVANKTFsyKYSKKGDAIGLLDHLKVQILTTQG----APLGW 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489819990 159 FTHGE--PYLRTILQFIGINVVPSIFVEG--IDHNPSKE-AEIVAAAKAVAQESATEF 211
Cdd:PRK01355 142 YPWGShtNYLEGTWEFLGAKVVDSILLAGtkVEPLSNKTpKEIVEEFDKEIIEKAKNF 199
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 3-205 5.07e-17

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 75.65  E-value: 5.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819990   3 KVLFIKASPLPNEVSRSsqVAETFMAEYKAKNpsDTVEELVLYNTEVPLLdlelMTAGRELQAGKAFTDLApDVQKKLna 82
Cdd:COG2249    1 KILIIYAHPDPSSFNAA--LAEAAAEGLEAAG--HEVTVHDLYAEGFDPV----LSAADFYRDGPLPIDVA-AEQELL-- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819990  83 ynalteqfLAADKYVFVFPLWNLGIPPLLKAYID-TFViAGKSFRYTEHGPEALLKDKKAILIhGSGGiysaGPTSSFTH 161
Cdd:COG2249   70 --------LWADHLVFQFPLWWYSMPALLKGWIDrVLT-PGFAYGYGGGYPGGLLKGKKALLV-VTTG----GPEEAYSR 135

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489819990 162 GEPY-------LRTILQFIGINVVPSIFVEGIDHnpSKEAEIVAAAKAVAQ 205
Cdd:COG2249  136 LGYGgpieellFRGTLGYCGMKVLPPFVLYGVDR--SSDEERAAWLERVRE 184
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
3-200 3.52e-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: 3.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819990   3 KVLFIKASPLPNevSRSSQVAETFMAEykAKNPSDTVEELVLYNTEVPLLDLELMTAGrelqagkaftdLAPDVQkklna 82
Cdd:COG0431    2 KILVISGSLRPG--SFNRKLARAAAEL--APAAGAEVELIDLRDLDLPLYDEDLEADG-----------APPAVK----- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819990  83 ynALTEQFLAADKYVFVFPLWNLGIPPLLKAYIDtfviagksfryteHGPEALLKDKKAILIHGSGGiySAGPTSSFTHg 162
Cdd:COG0431   62 --ALREAIAAADGVVIVTPEYNGSYPGVLKNALD-------------WLSRSELAGKPVALVSTSGG--ARGGLRALEH- 123

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 489819990 163 epyLRTILQFIGINVVP-SIFVEGIDHNPSKEAEIVAAA 200
Cdd:COG0431  124 ---LRPVLSELGAVVLPpQVSIPKAGEAFDEDGELTDEE 159
FMN_red pfam03358
NADPH-dependent FMN reductase;
3-183 1.16e-06

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 46.46  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819990    3 KVLFIKASPLPNevSRSSQVAETFMAEYKAKNpsdTVEELVLYNTEVPLLDLELMTAGRElqagkaftdlAPDVQkklna 82
Cdd:pfam03358   2 KILAISGSPRKG--SNTRKLARWAAELLEEGA---EVELIDLADLILPLCDEDLEEEQGD----------PDDVQ----- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819990   83 ynALTEQFLAADKYVFVFPLWNLGIPPLLKAYIDtfviagksfRYTEHGPEALLKDKKAILIHGSGGIYSAGptssftHG 162
Cdd:pfam03358  62 --ELREKIAAADAIIIVTPEYNGSVSGLLKNAID---------WLSRLRGGKELRGKPVAIVSTGGGRSGGL------RA 124

                         170       180
                  ....*....|....*....|.
gi 489819990  163 EPYLRTILQFIGINVVPSIFV 183
Cdd:pfam03358 125 VEQLRQVLAELGAIVVPSGQV 145
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 84-205 3.30e-06

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 45.69  E-value: 3.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819990  84 NALTEQFLAADKYVFVFPLWNLGIPPLLKAYIDTFviagksfrYTEHGPEALLKDKKAILI-HGSGGiysaGPTSSFThg 162
Cdd:COG0655   62 NAIYEKLLEADGIIFGSPTYFGNMSAQLKAFIDRL--------YALWAKGKLLKGKVGAVFtTGGHG----GAEATLL-- 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 489819990 163 epYLRTILQFIGINVVPSIF---VEGIDHNPSKEAEIVAAAKAVAQ 205
Cdd:COG0655  128 --SLNTFLLHHGMIVVGLPPygaVGGGGPGDVLDEEGLATARELGK 171
PRK09739 PRK09739
NAD(P)H oxidoreductase;
1-116 4.75e-06

NAD(P)H oxidoreductase;


Pssm-ID: 236620 [Multi-domain]  Cd Length: 199  Bit Score: 45.46  E-value: 4.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819990   1 MSKVLFIKASPLPNevSRSSQVAETFMAEykAKNPSDTVEELVLYNTEV-PLL------DLElmtagrelQAGKAFTdla 73
Cdd:PRK09739   3 SMRIYLVWAHPRHD--SLTAKVAEAIHQR--AQERGHQVEELDLYRSGFdPVLtpedepDWK--------NPDKRYS--- 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489819990  74 PDVQKklnaynaLTEQFLAADKYVFVFPLWNLGIPPLLKAYID 116
Cdd:PRK09739  68 PEVHQ-------LYSELLEHDALVFVFPLWWYSFPAMLKGYID 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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