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Conserved domains on  [gi|1889834373|ref|WP_182848630|]
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NADPH-dependent FMN reductase [Actinomadura namibiensis]

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

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];
6-159 2.20e-51

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


:

Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 162.63  E-value: 2.20e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889834373   6 RVAVIIGSTREGRFGPRVAEWFAAHARRRpELDIDLVDLAETGLPeaLTDPYADTGAPPPgPVGALAPRLAAADAFVVVT 85
Cdd:COG0431     2 KILVISGSLRPGSFNRKLARAAAELAPAA-GAEVELIDLRDLDLP--LYDEDLEADGAPP-AVKALREAIAAADGVVIVT 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889834373  86 PEYNRSIPAPLKTAIDWFYR-EWQAKPVAVVAY-GRDSGGALAAAHLRQVFAEVHAVTVPDAVLLPRYWELFAPDG 159
Cdd:COG0431    78 PEYNGSYPGVLKNALDWLSRsELAGKPVALVSTsGGARGGLRALEHLRPVLSELGAVVLPPQVSIPKAGEAFDEDG 153
 
Name Accession Description Interval E-value
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
6-159 2.20e-51

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 162.63  E-value: 2.20e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889834373   6 RVAVIIGSTREGRFGPRVAEWFAAHARRRpELDIDLVDLAETGLPeaLTDPYADTGAPPPgPVGALAPRLAAADAFVVVT 85
Cdd:COG0431     2 KILVISGSLRPGSFNRKLARAAAELAPAA-GAEVELIDLRDLDLP--LYDEDLEADGAPP-AVKALREAIAAADGVVIVT 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889834373  86 PEYNRSIPAPLKTAIDWFYR-EWQAKPVAVVAY-GRDSGGALAAAHLRQVFAEVHAVTVPDAVLLPRYWELFAPDG 159
Cdd:COG0431    78 PEYNGSYPGVLKNALDWLSRsELAGKPVALVSTsGGARGGLRALEHLRPVLSELGAVVLPPQVSIPKAGEAFDEDG 153
FMN_red pfam03358
NADPH-dependent FMN reductase;
5-153 6.05e-45

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 145.84  E-value: 6.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889834373   5 VRVAVIIGSTREGRFGPRVAEWFAAHARRrpELDIDLVDLAETGLPeaLTDPYADTGAPPPGPVGALAPRLAAADAFVVV 84
Cdd:pfam03358   1 MKILAISGSPRKGSNTRKLARWAAELLEE--GAEVELIDLADLILP--LCDEDLEEEQGDPDDVQELREKIAAADAIIIV 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889834373  85 TPEYNRSIPAPLKTAIDWF-----YREWQAKPVAVVAY-GRDSGGALAAAHLRQVFAEVHAVTVPD-AVLLPRYWE 153
Cdd:pfam03358  77 TPEYNGSVSGLLKNAIDWLsrlrgGKELRGKPVAIVSTgGGRSGGLRAVEQLRQVLAELGAIVVPSgQVAVGNATD 152
PRK00170 PRK00170
azoreductase; Reviewed
75-101 1.03e-03

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 38.34  E-value: 1.03e-03
                          10        20
                  ....*....|....*....|....*..
gi 1889834373  75 LAAADAFVVVTPEYNRSIPAPLKTAID 101
Cdd:PRK00170   84 FLAADKIVIAAPMYNFSIPTQLKAYID 110
 
Name Accession Description Interval E-value
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
6-159 2.20e-51

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 162.63  E-value: 2.20e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889834373   6 RVAVIIGSTREGRFGPRVAEWFAAHARRRpELDIDLVDLAETGLPeaLTDPYADTGAPPPgPVGALAPRLAAADAFVVVT 85
Cdd:COG0431     2 KILVISGSLRPGSFNRKLARAAAELAPAA-GAEVELIDLRDLDLP--LYDEDLEADGAPP-AVKALREAIAAADGVVIVT 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889834373  86 PEYNRSIPAPLKTAIDWFYR-EWQAKPVAVVAY-GRDSGGALAAAHLRQVFAEVHAVTVPDAVLLPRYWELFAPDG 159
Cdd:COG0431    78 PEYNGSYPGVLKNALDWLSRsELAGKPVALVSTsGGARGGLRALEHLRPVLSELGAVVLPPQVSIPKAGEAFDEDG 153
FMN_red pfam03358
NADPH-dependent FMN reductase;
5-153 6.05e-45

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 145.84  E-value: 6.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889834373   5 VRVAVIIGSTREGRFGPRVAEWFAAHARRrpELDIDLVDLAETGLPeaLTDPYADTGAPPPGPVGALAPRLAAADAFVVV 84
Cdd:pfam03358   1 MKILAISGSPRKGSNTRKLARWAAELLEE--GAEVELIDLADLILP--LCDEDLEEEQGDPDDVQELREKIAAADAIIIV 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889834373  85 TPEYNRSIPAPLKTAIDWF-----YREWQAKPVAVVAY-GRDSGGALAAAHLRQVFAEVHAVTVPD-AVLLPRYWE 153
Cdd:pfam03358  77 TPEYNGSVSGLLKNAIDWLsrlrgGKELRGKPVAIVSTgGGRSGGLRAVEQLRQVLAELGAIVVPSgQVAVGNATD 152
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
6-187 2.91e-10

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 56.86  E-value: 2.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889834373   6 RVAVIIGSTREG---RfgpRVAEWFAAHARRrPELDIDLVDLAETGLpEALTDPYADTGAPPPGPVGALAPRLAAADAFV 82
Cdd:COG0655     1 KILVINGSPRKNgntA---ALAEAVAEGAEE-AGAEVELIRLADLDI-KPCIGCGGTGKCVIKDDMNAIYEKLLEADGII 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889834373  83 VVTPEYNRSIPAPLKTAIDWFYREWQA------KPVAVVAYGRDSGGALAAAHLRQvFAEVHAVTVPDavlLPRYWELFA 156
Cdd:COG0655    76 FGSPTYFGNMSAQLKAFIDRLYALWAKgkllkgKVGAVFTTGGHGGAEATLLSLNT-FLLHHGMIVVG---LPPYGAVGG 151
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1889834373 157 PDGSwpkpTADREAALKTTLDQ---LIWWAHALR 187
Cdd:COG0655   152 GGPG----DVLDEEGLATARELgkrLAELAKKLK 181
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
6-105 1.67e-07

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: 49.25  E-value: 1.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889834373   6 RVAVIIGSTREGRFGPRVAEWFAAHARRRpELDIDLVDLAETGLPEALTDPYADTGAP-PPGPVGALAPRLAAADAFVVV 84
Cdd:pfam02525   2 KILIINAHPRPGSFSSRLADALVEALKAA-GHEVTVRDLYALFLPVLDAEDLADLTYPqGAADVESEQEELLAADVIVFQ 80
                          90       100
                  ....*....|....*....|.
gi 1889834373  85 TPEYNRSIPAPLKTAIDWFYR 105
Cdd:pfam02525  81 FPLYWFSVPALLKGWIDRVLR 101
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
23-101 7.77e-06

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


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 44.74  E-value: 7.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889834373  23 VAEWFAAHarrrPELDIDLVDLAETGLPEaLTDPYADTGAPPPGP-----------VGALAPRLAAADAFVVVTPEYNRS 91
Cdd:COG1182    26 VAALRAAH----PDDEVTYRDLAAEPLPH-LDGAWLAAFFTPAEGrtpeqqaalalSDELIDELLAADVIVIGAPMYNFG 100
                          90
                  ....*....|
gi 1889834373  92 IPAPLKTAID 101
Cdd:COG1182   101 IPSQLKAWID 110
PRK00170 PRK00170
azoreductase; Reviewed
75-101 1.03e-03

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 38.34  E-value: 1.03e-03
                          10        20
                  ....*....|....*....|....*..
gi 1889834373  75 LAAADAFVVVTPEYNRSIPAPLKTAID 101
Cdd:PRK00170   84 FLAADKIVIAAPMYNFSIPTQLKAYID 110
 
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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