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Conserved domains on  [gi|488379668|ref|WP_002449053|]
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MULTISPECIES: NADPH-dependent FMN reductase [Staphylococcus]

Protein Classification

NADPH-dependent FMN reductase( domain architecture ID 10001414)

NAD(P)H-dependent FMN reductase may carry out reductase activities that are NAD(P)H-dependent and involve FMN as a cofactor, such as catalyzing the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines

CATH:  3.40.50.360
EC:  1.-.-.-
Gene Ontology:  GO:0052873|GO:0008752|GO:0050136|GO:0008753|GO:0016491|GO:0010181
PubMed:  9694845
SCOP:  4000466|3001217

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
1-157 2.35e-36

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


:

Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 124.11  E-value: 2.35e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488379668   1 MKGLIVVGSAQVGSHTNALAKYLTGQFDNHDVDVDIFDLAERPLnqlDFSGTTHSTEEIKANTKAFQDKAMEADFLIFGT 80
Cdd:COG0431    1 MKILVISGSLRPGSFNRKLARAAAELAPAAGAEVELIDLRDLDL---PLYDEDLEADGAPPAVKALREAIAAADGVVIVT 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488379668  81 PNYHGSYSGILKNALDHINMDYVKMKPVGLIGNSGGIVSSE-PLSHLRVIVRSLLGIAVPTQIATHDSDYAKLEDGTL 157
Cdd:COG0431   78 PEYNGSYPGVLKNALDWLSRSELAGKPVALVSTSGGARGGLrALEHLRPVLSELGAVVLPPQVSIPKAGEAFDEDGEL 155
 
Name Accession Description Interval E-value
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
1-157 2.35e-36

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 124.11  E-value: 2.35e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488379668   1 MKGLIVVGSAQVGSHTNALAKYLTGQFDNHDVDVDIFDLAERPLnqlDFSGTTHSTEEIKANTKAFQDKAMEADFLIFGT 80
Cdd:COG0431    1 MKILVISGSLRPGSFNRKLARAAAELAPAAGAEVELIDLRDLDL---PLYDEDLEADGAPPAVKALREAIAAADGVVIVT 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488379668  81 PNYHGSYSGILKNALDHINMDYVKMKPVGLIGNSGGIVSSE-PLSHLRVIVRSLLGIAVPTQIATHDSDYAKLEDGTL 157
Cdd:COG0431   78 PEYNGSYPGVLKNALDWLSRSELAGKPVALVSTSGGARGGLrALEHLRPVLSELGAVVLPPQVSIPKAGEAFDEDGEL 155
FMN_red pfam03358
NADPH-dependent FMN reductase;
1-140 8.42e-28

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 101.93  E-value: 8.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488379668    1 MKGLIVVGSAQVGSHTNALAKYLTGQFDNhDVDVDIFDLAERPLNQLDfsGTTHSTEEIKANTKAFQDKAMEADFLIFGT 80
Cdd:pfam03358   1 MKILAISGSPRKGSNTRKLARWAAELLEE-GAEVELIDLADLILPLCD--EDLEEEQGDPDDVQELREKIAAADAIIIVT 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488379668   81 PNYHGSYSGILKNALDHINMDYVKM----KPVGLIGNSGGIV-SSEPLSHLRVIVRSLLGIAVPT 140
Cdd:pfam03358  78 PEYNGSVSGLLKNAIDWLSRLRGGKelrgKPVAIVSTGGGRSgGLRAVEQLRQVLAELGAIVVPS 142
PRK00170 PRK00170
azoreductase; Reviewed
 14-135 9.77e-07

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 47.20  E-value: 9.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488379668  14 SHTNALAKYLTGQFDNHDVDVDI--FDLAERPLNQLD---FSG-------TTHSTEEIKANTKAFQDKAMEADFLIFGTP 81
Cdd:PRK00170  16 SQSMQLGDAFIEAYKEAHPDDEVtvRDLAAEPIPVLDgevVGAlgksaetLTPRQQEAVALSDELLEEFLAADKIVIAAP 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488379668  82 NYHGSYSGILKNALDHIN-----MDYVKMKPVGLIGN--------SGGIVSSEPLSHLRVIVRSLLG 135
Cdd:PRK00170  96 MYNFSIPTQLKAYIDLIAragktFRYTENGPVGLVTGkkallitsRGGIHKDGPTDMGVPYLKTFLG 162
 
Name Accession Description Interval E-value
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
1-157 2.35e-36

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 124.11  E-value: 2.35e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488379668   1 MKGLIVVGSAQVGSHTNALAKYLTGQFDNHDVDVDIFDLAERPLnqlDFSGTTHSTEEIKANTKAFQDKAMEADFLIFGT 80
Cdd:COG0431    1 MKILVISGSLRPGSFNRKLARAAAELAPAAGAEVELIDLRDLDL---PLYDEDLEADGAPPAVKALREAIAAADGVVIVT 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488379668  81 PNYHGSYSGILKNALDHINMDYVKMKPVGLIGNSGGIVSSE-PLSHLRVIVRSLLGIAVPTQIATHDSDYAKLEDGTL 157
Cdd:COG0431   78 PEYNGSYPGVLKNALDWLSRSELAGKPVALVSTSGGARGGLrALEHLRPVLSELGAVVLPPQVSIPKAGEAFDEDGEL 155
FMN_red pfam03358
NADPH-dependent FMN reductase;
1-140 8.42e-28

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 101.93  E-value: 8.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488379668    1 MKGLIVVGSAQVGSHTNALAKYLTGQFDNhDVDVDIFDLAERPLNQLDfsGTTHSTEEIKANTKAFQDKAMEADFLIFGT 80
Cdd:pfam03358   1 MKILAISGSPRKGSNTRKLARWAAELLEE-GAEVELIDLADLILPLCD--EDLEEEQGDPDDVQELREKIAAADAIIIVT 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488379668   81 PNYHGSYSGILKNALDHINMDYVKM----KPVGLIGNSGGIV-SSEPLSHLRVIVRSLLGIAVPT 140
Cdd:pfam03358  78 PEYNGSVSGLLKNAIDWLSRLRGGKelrgKPVAIVSTGGGRSgGLRAVEQLRQVLAELGAIVVPS 142
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 1-120 1.72e-13

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: 65.43  E-value: 1.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488379668    1 MKGLIVVGSAQVGSHTNALAKYLTGQFDNHDVDVDIFDLAERPLNQLDFSG-TTHSTEEIKANTKAFQDKAMEADFLIFG 79
Cdd:pfam02525   1 MKILIINAHPRPGSFSSRLADALVEALKAAGHEVTVRDLYALFLPVLDAEDlADLTYPQGAADVESEQEELLAADVIVFQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 488379668   80 TPNYHGSYSGILKNALDHI-------NMDYVKMKPVGLIGNSGGIVSS 120
Cdd:pfam02525  81 FPLYWFSVPALLKGWIDRVlragfafKYEEGGPGGGGLLGKKVLVIVT 128
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 4-116 1.32e-12

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 63.02  E-value: 1.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488379668   4 LIVVGSAQVGSHTNALAKYLTGQFDNHDVDVDIFDLAERPLNQLDFSGTTHsTEEIKANTKAFQDKAMEADFLIFGTPNY 83
Cdd:COG0655    3 LVINGSPRKNGNTAALAEAVAEGAEEAGAEVELIRLADLDIKPCIGCGGTG-KCVIKDDMNAIYEKLLEADGIIFGSPTY 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 488379668  84 HGSYSGILKNALDHI-----NMDYVKMKPVGLIGNSGG 116
Cdd:COG0655   82 FGNMSAQLKAFIDRLyalwaKGKLLKGKVGAVFTTGGH 119
PRK00170 PRK00170
azoreductase; Reviewed
 14-135 9.77e-07

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 47.20  E-value: 9.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488379668  14 SHTNALAKYLTGQFDNHDVDVDI--FDLAERPLNQLD---FSG-------TTHSTEEIKANTKAFQDKAMEADFLIFGTP 81
Cdd:PRK00170  16 SQSMQLGDAFIEAYKEAHPDDEVtvRDLAAEPIPVLDgevVGAlgksaetLTPRQQEAVALSDELLEEFLAADKIVIAAP 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488379668  82 NYHGSYSGILKNALDHIN-----MDYVKMKPVGLIGN--------SGGIVSSEPLSHLRVIVRSLLG 135
Cdd:PRK00170  96 MYNFSIPTQLKAYIDLIAragktFRYTENGPVGLVTGkkallitsRGGIHKDGPTDMGVPYLKTFLG 162
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
1-126 7.10e-05

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


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 41.65  E-value: 7.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488379668   1 MKGLIVVGSAQV-GSHTNALAKYLTGQF--DNHDVDVDIFDLAERPLNQLD-------FSGTTHSTEEIKAnTKAFQDKA 70
Cdd:COG1182    2 MKLLHIDSSPRGeGSVSRRLADAFVAALraAHPDDEVTYRDLAAEPLPHLDgawlaafFTPAEGRTPEQQA-ALALSDEL 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488379668  71 ----MEADFLIFGTPNYHGSYSGILKNALDHINMD-----YVKMKPVGLIGN--------SGGIVSSEPLSHL 126
Cdd:COG1182   81 idelLAADVIVIGAPMYNFGIPSQLKAWIDHIARAgrtfrYTENGPVGLLTGkkavvitaRGGVYSGGPAAGM 153
FldA COG0716
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ...
 4-175 1.09e-03

Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440480 [Multi-domain]  Cd Length: 135  Bit Score: 37.58  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488379668   4 LIVVGSaqVGSHTNALAKYLTGQFDnhDVDVDIFDLAERPLNQLDfsgtthsteeikantkafqdkamEADFLIFGTPNY 83
Cdd:COG0716    2 LIVYGS--TTGNTEKVAEAIAEALG--AAGVDLFEIEDADLDDLE-----------------------DYDLLILGTPTW 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488379668  84 HGSYSGILKNALDHINMDyVKMKPVGLIGNSGGIVSSEPLSHLRVIVRSLLGIAVPTQIATHDsdyakledgtLYLNDEE 163
Cdd:COG0716   55 AGELPDDWEDFLEELKED-LSGKKVALFGTGDSSGYGDALGELKELLEEKGAKVVGGYDFEGS----------KAPDAED 123

                        170
                 ....*....|..
gi 488379668 164 FQLRAKLFVDQI 175
Cdd:COG0716  124 TEERAEEWLKQL 135
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 4-92 1.18e-03

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 37.90  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488379668   4 LIVVGSAQVGSHTNALAKYLTGQFDNHDVDVDIFDLAERPLNQLDFSGTTHSTEEIKANTKAFQDKAMEADFLIFGTPNY 83
Cdd:COG2249    3 LIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLYAEGFDPVLSAADFYRDGPLPIDVAAEQELLLWADHLVFQFPLW 82


                 ....*....
gi 488379668  84 HGSYSGILK 92
Cdd:COG2249   83 WYSMPALLK 91
NorV COG0426
Flavorubredoxin [Energy production and conversion];
15-133 2.40e-03

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 37.89  E-value: 2.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488379668  15 HTNALAKYLTGQFDNHDVDVDIFDLAErplnqldfsgtTHSTEEIKAntkafqdkAMEADFLIFGTPNYHGSYSGILKNA 94
Cdd:COG0426  259 NTEKMAEAIAEGLTEEGVKVKLYDLEK-----------TDPSEIITE--------IFDAKGIVIGSPTYNGGAFPPIADL 319

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488379668  95 LDHINMDYVKMKPVGLIGNSGGivSSEPLSHLRVIVRSL 133
Cdd:COG0426  320 LGYLKGLAPKNKLAGAFGSYGW--SGEAVKLLEEKLEDA 356
PRK10569 PRK10569
NAD(P)H-dependent FMN reductase; Provisional
 1-96 3.54e-03

NAD(P)H-dependent FMN reductase; Provisional


Pssm-ID: 182557  Cd Length: 191  Bit Score: 36.89  E-value: 3.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488379668   1 MKGLIVVGSAQVGSHTNALAKYLTGQFDNHDVDVdifdlaeRPLNQLDFsgttHSTEEIKAN-----TKAFQDKAMEADF 75
Cdd:PRK10569   1 MRVITLAGSPRFPSRSSALLEYAREWLNGLGVEV-------YHWNLQNF----APEDLLYARfdspaLKTFTEQLAQADG 69

                         90       100
                 ....*....|....*....|.
gi 488379668  76 LIFGTPNYHGSYSGILKNALD 96
Cdd:PRK10569  70 LIVATPVYKASFSGALKTLLD 90
PRK01355 PRK01355
azoreductase; Reviewed
 2-98 6.77e-03

azoreductase; Reviewed


Pssm-ID: 234946 [Multi-domain]  Cd Length: 199  Bit Score: 35.83  E-value: 6.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488379668   2 KGLIVVGS--AQVGSHTNALAKYLTGQF--DNHDVDVDIFDLAERPLNQLDFSGTTHSTEEIKANTKAFQDKAMEADFLI 77
Cdd:PRK01355   3 KVLVIKGSmvAKEKSFSSALTDKFVEEYkkVNPNDEIIILDLNETKVGSVTLTSENFKTFFKEEVSDKYINQLKSVDKVV 82

                         90       100
                 ....*....|....*....|.
gi 488379668  78 FGTPNYHGSYSGILKNALDHI 98
Cdd:PRK01355  83 ISCPMTNFNVPATLKNYLDHI 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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