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Conserved domains on  [gi|549580606|gb|ERN85341|]
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hypothetical protein SEEK0793_06165 [Salmonella enterica subsp. enterica serovar Kentucky str. 20793]

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];
5-170 3.75e-55

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


:

Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 171.88  E-value: 3.75e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549580606   5 LNVVTLLGSLRKGSFNGMVARTLPKVAPA-GMTVSPL-PSIGDIPLYDADIQqEEGFPASVEALAEQIRNADGVVIVTPE 82
Cdd:COG0431    1 MKILVISGSLRPGSFNRKLARAAAELAPAaGAEVELIdLRDLDLPLYDEDLE-ADGAPPAVKALREAIAAADGVVIVTPE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549580606  83 YNYSVPGGLKNAIDWLSRlpeQPLAGKPVLIQTSSMGAIGGARCQYHLRQILVFLDAMVMNkPEFMGGVIQNKVDPQtGE 162
Cdd:COG0431   80 YNGSYPGVLKNALDWLSR---SELAGKPVALVSTSGGARGGLRALEHLRPVLSELGAVVLP-PQVSIPKAGEAFDED-GE 154

                 ....*...
gi 549580606 163 VVDQGTLD 170
Cdd:COG0431  155 LTDEELAE 162
 
Name Accession Description Interval E-value
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
5-170 3.75e-55

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 171.88  E-value: 3.75e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549580606   5 LNVVTLLGSLRKGSFNGMVARTLPKVAPA-GMTVSPL-PSIGDIPLYDADIQqEEGFPASVEALAEQIRNADGVVIVTPE 82
Cdd:COG0431    1 MKILVISGSLRPGSFNRKLARAAAELAPAaGAEVELIdLRDLDLPLYDEDLE-ADGAPPAVKALREAIAAADGVVIVTPE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549580606  83 YNYSVPGGLKNAIDWLSRlpeQPLAGKPVLIQTSSMGAIGGARCQYHLRQILVFLDAMVMNkPEFMGGVIQNKVDPQtGE 162
Cdd:COG0431   80 YNGSYPGVLKNALDWLSR---SELAGKPVALVSTSGGARGGLRALEHLRPVLSELGAVVLP-PQVSIPKAGEAFDED-GE 154

                 ....*...
gi 549580606 163 VVDQGTLD 170
Cdd:COG0431  155 LTDEELAE 162
FMN_red pfam03358
NADPH-dependent FMN reductase;
5-148 5.03e-52

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 163.56  E-value: 5.03e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549580606    5 LNVVTLLGSLRKGSFNGMVARTLPKVAPAGMTVSPLpSIGD--IPLYDADIQQEEGFPASVEALAEQIRNADGVVIVTPE 82
Cdd:pfam03358   1 MKILAISGSPRKGSNTRKLARWAAELLEEGAEVELI-DLADliLPLCDEDLEEEQGDPDDVQELREKIAAADAIIIVTPE 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 549580606   83 YNYSVPGGLKNAIDWLSRL-PEQPLAGKPVLIQTSSMGAIGGARCQYHLRQILVFLDAMVMNKPEFM 148
Cdd:pfam03358  80 YNGSVSGLLKNAIDWLSRLrGGKELRGKPVAIVSTGGGRSGGLRAVEQLRQVLAELGAIVVPSGQVA 146
PRK10569 PRK10569
NAD(P)H-dependent FMN reductase; Provisional
60-112 2.77e-09

NAD(P)H-dependent FMN reductase; Provisional


Pssm-ID: 182557  Cd Length: 191  Bit Score: 54.23  E-value: 2.77e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 549580606  60 PAsVEALAEQIRNADGVVIVTPEYNYSVPGGLKNAIDWlsrLPEQPLAGKPVL 112
Cdd:PRK10569  55 PA-LKTFTEQLAQADGLIVATPVYKASFSGALKTLLDL---LPERALEHKVVL 103
LLM_duo_CE1759 TIGR04037
LLM-partnered FMN reductase, CE1759 family; This family represents a distinct clade within ...
58-142 3.61e-06

LLM-partnered FMN reductase, CE1759 family; This family represents a distinct clade within pfam03358. That family includes enzymes such as the NADH-dependent FMN reductase MsuE. Members of the present family regularly co-occur in genomes, typically as gene pairs, with members of TIGR04036, a probable FMN-dependent member of the bacterial luciferase-like monooxygenase (LLM) family. At least one member, RF|YP_001509627.1 from Frankia sp. EAN1pec, is fused to the LLM protein. The function of these gene pairs is unknown.


Pssm-ID: 274935  Cd Length: 198  Bit Score: 45.35  E-value: 3.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549580606   58 GFP-ASVEALAEQIRNADGVVIVTPEYNYSVPGGLKNAIDwlsRLPEQPLAGKPVLIqtssmGAIGG-AR----CQYHLR 131
Cdd:TIGR04037  57 GFPsPALRAALDAVAGADGLIAVTPVFSASYSGLFKSFFD---VLDPDALTGKPVLI-----AATGGtPRhslvLDHAMR 128
                          90
                  ....*....|.
gi 549580606  132 QILVFLDAMVM 142
Cdd:TIGR04037 129 PLFSYLRAVVV 139
 
Name Accession Description Interval E-value
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
5-170 3.75e-55

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 171.88  E-value: 3.75e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549580606   5 LNVVTLLGSLRKGSFNGMVARTLPKVAPA-GMTVSPL-PSIGDIPLYDADIQqEEGFPASVEALAEQIRNADGVVIVTPE 82
Cdd:COG0431    1 MKILVISGSLRPGSFNRKLARAAAELAPAaGAEVELIdLRDLDLPLYDEDLE-ADGAPPAVKALREAIAAADGVVIVTPE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549580606  83 YNYSVPGGLKNAIDWLSRlpeQPLAGKPVLIQTSSMGAIGGARCQYHLRQILVFLDAMVMNkPEFMGGVIQNKVDPQtGE 162
Cdd:COG0431   80 YNGSYPGVLKNALDWLSR---SELAGKPVALVSTSGGARGGLRALEHLRPVLSELGAVVLP-PQVSIPKAGEAFDED-GE 154

                 ....*...
gi 549580606 163 VVDQGTLD 170
Cdd:COG0431  155 LTDEELAE 162
FMN_red pfam03358
NADPH-dependent FMN reductase;
5-148 5.03e-52

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 163.56  E-value: 5.03e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549580606    5 LNVVTLLGSLRKGSFNGMVARTLPKVAPAGMTVSPLpSIGD--IPLYDADIQQEEGFPASVEALAEQIRNADGVVIVTPE 82
Cdd:pfam03358   1 MKILAISGSPRKGSNTRKLARWAAELLEEGAEVELI-DLADliLPLCDEDLEEEQGDPDDVQELREKIAAADAIIIVTPE 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 549580606   83 YNYSVPGGLKNAIDWLSRL-PEQPLAGKPVLIQTSSMGAIGGARCQYHLRQILVFLDAMVMNKPEFM 148
Cdd:pfam03358  80 YNGSVSGLLKNAIDWLSRLrGGKELRGKPVAIVSTGGGRSGGLRAVEQLRQVLAELGAIVVPSGQVA 146
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
6-122 7.07e-12

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: 61.20  E-value: 7.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549580606    6 NVVTLLGSLRKGSFNGMVARTLPKVAPA-GMTV-------SPLPSIGDIPLYDADIQQeegFPASVEALAEQIRNADGVV 77
Cdd:pfam02525   2 KILIINAHPRPGSFSSRLADALVEALKAaGHEVtvrdlyaLFLPVLDAEDLADLTYPQ---GAADVESEQEELLAADVIV 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 549580606   78 IVTPEYNYSVPGGLKNAIDWL-----------SRLPEQPLAGKPVLIqTSSMGAIG 122
Cdd:pfam02525  79 FQFPLYWFSVPALLKGWIDRVlragfafkyeeGGPGGGGLLGKKVLV-IVTTGGPE 133
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
61-137 2.77e-10

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


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 57.06  E-value: 2.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549580606  61 ASVEALAEQIRNADGVVIVTPEYNYSVPGGLKNAIDWLSRL----------PEQPLAGKPVLIQTSSMGAI-GGARCQY- 128
Cdd:COG1182   75 ALSDELIDELLAADVIVIGAPMYNFGIPSQLKAWIDHIARAgrtfrytengPVGLLTGKKAVVITARGGVYsGGPAAGMd 154
                         90
                 ....*....|...
gi 549580606 129 ----HLRQILVFL 137
Cdd:COG1182  155 fqtpYLRTVLGFI 167
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
46-143 1.83e-09

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 54.55  E-value: 1.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549580606  46 IPLYDADIQQEEGFPAS--------VEALAEQIRNADGVVIVTPEYNYSVPGGLKNAIDWLSRL--PEQPLAGKPVLIQT 115
Cdd:COG0655   36 IRLADLDIKPCIGCGGTgkcvikddMNAIYEKLLEADGIIFGSPTYFGNMSAQLKAFIDRLYALwaKGKLLKGKVGAVFT 115
                         90       100
                 ....*....|....*....|....*...
gi 549580606 116 SSmGAIGGARCqyhLRQILVFLDAMVMN 143
Cdd:COG0655  116 TG-GHGGAEAT---LLSLNTFLLHHGMI 139
PRK10569 PRK10569
NAD(P)H-dependent FMN reductase; Provisional
60-112 2.77e-09

NAD(P)H-dependent FMN reductase; Provisional


Pssm-ID: 182557  Cd Length: 191  Bit Score: 54.23  E-value: 2.77e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 549580606  60 PAsVEALAEQIRNADGVVIVTPEYNYSVPGGLKNAIDWlsrLPEQPLAGKPVL 112
Cdd:PRK10569  55 PA-LKTFTEQLAQADGLIVATPVYKASFSGALKTLLDL---LPERALEHKVVL 103
PRK00170 PRK00170
azoreductase; Reviewed
45-119 1.91e-08

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 51.82  E-value: 1.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549580606  45 DIPLYDADI--------------QQEEgfPASVEALAEQIRNADGVVIVTPEYNYSVPGGLKNAIDWLSRL--------- 101
Cdd:PRK00170  47 PIPVLDGEVvgalgksaetltprQQEA--VALSDELLEEFLAADKIVIAAPMYNFSIPTQLKAYIDLIARAgktfryten 124
                         90
                 ....*....|....*....
gi 549580606 102 -PEQPLAGKPVLIQTSSMG 119
Cdd:PRK00170 125 gPVGLVTGKKALLITSRGG 143
LLM_duo_CE1759 TIGR04037
LLM-partnered FMN reductase, CE1759 family; This family represents a distinct clade within ...
58-142 3.61e-06

LLM-partnered FMN reductase, CE1759 family; This family represents a distinct clade within pfam03358. That family includes enzymes such as the NADH-dependent FMN reductase MsuE. Members of the present family regularly co-occur in genomes, typically as gene pairs, with members of TIGR04036, a probable FMN-dependent member of the bacterial luciferase-like monooxygenase (LLM) family. At least one member, RF|YP_001509627.1 from Frankia sp. EAN1pec, is fused to the LLM protein. The function of these gene pairs is unknown.


Pssm-ID: 274935  Cd Length: 198  Bit Score: 45.35  E-value: 3.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549580606   58 GFP-ASVEALAEQIRNADGVVIVTPEYNYSVPGGLKNAIDwlsRLPEQPLAGKPVLIqtssmGAIGG-AR----CQYHLR 131
Cdd:TIGR04037  57 GFPsPALRAALDAVAGADGLIAVTPVFSASYSGLFKSFFD---VLDPDALTGKPVLI-----AATGGtPRhslvLDHAMR 128
                          90
                  ....*....|.
gi 549580606  132 QILVFLDAMVM 142
Cdd:TIGR04037 129 PLFSYLRAVVV 139
PRK01355 PRK01355
azoreductase; Reviewed
68-96 6.40e-03

azoreductase; Reviewed


Pssm-ID: 234946 [Multi-domain]  Cd Length: 199  Bit Score: 35.83  E-value: 6.40e-03
                         10        20
                 ....*....|....*....|....*....
gi 549580606  68 EQIRNADGVVIVTPEYNYSVPGGLKNAID 96
Cdd:PRK01355  73 NQLKSVDKVVISCPMTNFNVPATLKNYLD 101
 
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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