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Conserved domains on  [gi|2085998039|ref|WP_221874595|]
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NADPH-dependent FMN reductase [Mesobacillus maritimus]

Protein Classification

NADPH-dependent FMN reductase family protein( domain architecture ID 325)

NADPH-dependent FMN reductase family protein contains a flavodoxin-like fold, which is characterized by an open twisted/alpha beta structure consisting of five parallel beta-sheets connected by alpha-helices which surround the sheet

CATH:  3.40.50.360
Gene Ontology:  GO:0010181
SCOP:  3001217

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FMN_red super family cl00438
NADPH-dependent FMN reductase;
22-170 7.44e-60

NADPH-dependent FMN reductase;


The actual alignment was detected with superfamily member TIGR03567:

Pssm-ID: 469770 [Multi-domain]  Cd Length: 171  Bit Score: 184.01  E-value: 7.44e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085998039  22 AYLKRELVQRGGKVDELTIRDLPPEALLHAHFTDPVIQSAQNLVEHADSIIVVSPVYKASYPGLLKSFFDLIPEKGLSGK 101
Cdd:TIGR03567  20 RHAREALQEQGVEVDHLSVRDLPAEDLLFARFDSPALKAATAQVAQADGVVVATPVYKASYSGVLKALLDLLPQRALRGK 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2085998039 102 KVLPIATGGTLAHLLSLEFAFKPLFSVLGAKEVPQGVYLIDSQLSYSGNEVTFLDPVVEERVQEAVRNL 170
Cdd:TIGR03567 100 VVLPIATGGTIAHLLAVDYALKPVLSALGARHILHGVFALDSQIERQEDGPQRLDEEIKERLDEALETL 168
 
Name Accession Description Interval E-value
FMN_reduc_SsuE TIGR03567
FMN reductase, SsuE family; Members of this protein family use NAD(P)H to reduce FMN and ...
 22-170 7.44e-60

FMN reductase, SsuE family; Members of this protein family use NAD(P)H to reduce FMN and regenerate FMNH2. Members include the homodimeric, NAD(P)H-dependent enzyme SsuE from Escherichia coli, which serves as a partner to an FMNH2-dependent alkanesulfonate monooxygenase. It is induced by sulfate starvation. The NADH-dependent enzyme MsuE from Pseudomonas aeruginosa is outside the scope of this model (see model TIGR03566). [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 274653 [Multi-domain]  Cd Length: 171  Bit Score: 184.01  E-value: 7.44e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085998039  22 AYLKRELVQRGGKVDELTIRDLPPEALLHAHFTDPVIQSAQNLVEHADSIIVVSPVYKASYPGLLKSFFDLIPEKGLSGK 101
Cdd:TIGR03567  20 RHAREALQEQGVEVDHLSVRDLPAEDLLFARFDSPALKAATAQVAQADGVVVATPVYKASYSGVLKALLDLLPQRALRGK 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2085998039 102 KVLPIATGGTLAHLLSLEFAFKPLFSVLGAKEVPQGVYLIDSQLSYSGNEVTFLDPVVEERVQEAVRNL 170
Cdd:TIGR03567 100 VVLPIATGGTIAHLLAVDYALKPVLSALGARHILHGVFALDSQIERQEDGPQRLDEEIKERLDEALETL 168
PRK10569 PRK10569
NAD(P)H-dependent FMN reductase; Provisional
 22-167 1.33e-46

NAD(P)H-dependent FMN reductase; Provisional


Pssm-ID: 182557  Cd Length: 191  Bit Score: 150.91  E-value: 1.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085998039  22 AYLKRELVQRGGKVDELTIRDLPPEALLHAHFTDPVIQSAQNLVEHADSIIVVSPVYKASYPGLLKSFFDLIPEKGLSGK 101
Cdd:PRK10569   21 EYAREWLNGLGVEVYHWNLQNFAPEDLLYARFDSPALKTFTEQLAQADGLIVATPVYKASFSGALKTLLDLLPERALEHK 100

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2085998039 102 KVLPIATGGTLAHLLSLEFAFKPLFSVLGAKEVPQGVYLIDSQLSYSGNEVTFlDPVVEERVQEAV 167
Cdd:PRK10569  101 VVLPLATGGSVAHMLAVDYALKPVLSALKAQEILHGVFADDSQVIDYHHQPQF-TPNLQTRLDEAL 165
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
23-140 6.67e-30

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 107.16  E-value: 6.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085998039  23 YLKRELVQRGGKVDELTIRDLPPEAL---LHAHFTDPVIQSAQNLVEHADSIIVVSPVYKASYPGLLKSFFDLIPEKGLS 99
Cdd:COG0431    22 AAAELAPAAGAEVELIDLRDLDLPLYdedLEADGAPPAVKALREAIAAADGVVIVTPEYNGSYPGVLKNALDWLSRSELA 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2085998039 100 GKKVLPIATGGTLAHLLSLEFAFKPLFSVLGAKEVPQGVYL 140
Cdd:COG0431   102 GKPVALVSTSGGARGGLRALEHLRPVLSELGAVVLPPQVSI 142
FMN_red pfam03358
NADPH-dependent FMN reductase;
27-144 1.23e-22

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 88.06  E-value: 1.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085998039  27 ELVQRGGKVDELTIRDLPP----EALLHAHFTDPVIQSAQNLVEHADSIIVVSPVYKASYPGLLKSFFDLIP----EKGL 98
Cdd:pfam03358  25 ELLEEGAEVELIDLADLILplcdEDLEEEQGDPDDVQELREKIAAADAIIIVTPEYNGSVSGLLKNAIDWLSrlrgGKEL 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2085998039  99 SGKKVLPIATGGTLAHLLSLEFAFKPLFSVLGAKEVPQGVYLIDSQ 144
Cdd:pfam03358 105 RGKPVAIVSTGGGRSGGLRAVEQLRQVLAELGAIVVPSGQVAVGNA 150
 
Name Accession Description Interval E-value
FMN_reduc_SsuE TIGR03567
FMN reductase, SsuE family; Members of this protein family use NAD(P)H to reduce FMN and ...
 22-170 7.44e-60

FMN reductase, SsuE family; Members of this protein family use NAD(P)H to reduce FMN and regenerate FMNH2. Members include the homodimeric, NAD(P)H-dependent enzyme SsuE from Escherichia coli, which serves as a partner to an FMNH2-dependent alkanesulfonate monooxygenase. It is induced by sulfate starvation. The NADH-dependent enzyme MsuE from Pseudomonas aeruginosa is outside the scope of this model (see model TIGR03566). [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 274653 [Multi-domain]  Cd Length: 171  Bit Score: 184.01  E-value: 7.44e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085998039  22 AYLKRELVQRGGKVDELTIRDLPPEALLHAHFTDPVIQSAQNLVEHADSIIVVSPVYKASYPGLLKSFFDLIPEKGLSGK 101
Cdd:TIGR03567  20 RHAREALQEQGVEVDHLSVRDLPAEDLLFARFDSPALKAATAQVAQADGVVVATPVYKASYSGVLKALLDLLPQRALRGK 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2085998039 102 KVLPIATGGTLAHLLSLEFAFKPLFSVLGAKEVPQGVYLIDSQLSYSGNEVTFLDPVVEERVQEAVRNL 170
Cdd:TIGR03567 100 VVLPIATGGTIAHLLAVDYALKPVLSALGARHILHGVFALDSQIERQEDGPQRLDEEIKERLDEALETL 168
PRK10569 PRK10569
NAD(P)H-dependent FMN reductase; Provisional
 22-167 1.33e-46

NAD(P)H-dependent FMN reductase; Provisional


Pssm-ID: 182557  Cd Length: 191  Bit Score: 150.91  E-value: 1.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085998039  22 AYLKRELVQRGGKVDELTIRDLPPEALLHAHFTDPVIQSAQNLVEHADSIIVVSPVYKASYPGLLKSFFDLIPEKGLSGK 101
Cdd:PRK10569   21 EYAREWLNGLGVEVYHWNLQNFAPEDLLYARFDSPALKTFTEQLAQADGLIVATPVYKASFSGALKTLLDLLPERALEHK 100

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2085998039 102 KVLPIATGGTLAHLLSLEFAFKPLFSVLGAKEVPQGVYLIDSQLSYSGNEVTFlDPVVEERVQEAV 167
Cdd:PRK10569  101 VVLPLATGGSVAHMLAVDYALKPVLSALKAQEILHGVFADDSQVIDYHHQPQF-TPNLQTRLDEAL 165
LLM_duo_CE1759 TIGR04037
LLM-partnered FMN reductase, CE1759 family; This family represents a distinct clade within ...
 26-139 3.14e-30

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: 109.29  E-value: 3.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085998039  26 RELVQRGGKVDELTI--RDLPPE---ALLHAhFTDPVIQSAQNLVEHADSIIVVSPVYKASYPGLLKSFFDLIPEKGLSG 100
Cdd:TIGR04037  27 AALGARGEEVEVTVIelRELAHDlanAMVTG-FPSPALRAALDAVAGADGLIAVTPVFSASYSGLFKSFFDVLDPDALTG 105

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2085998039 101 KKVLPIATGGTLAHLLSLEFAFKPLFSVLGAKEVPQGVY 139
Cdd:TIGR04037 106 KPVLIAATGGTPRHSLVLDHAMRPLFSYLRAVVVPTGVF 144
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
23-140 6.67e-30

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 107.16  E-value: 6.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085998039  23 YLKRELVQRGGKVDELTIRDLPPEAL---LHAHFTDPVIQSAQNLVEHADSIIVVSPVYKASYPGLLKSFFDLIPEKGLS 99
Cdd:COG0431    22 AAAELAPAAGAEVELIDLRDLDLPLYdedLEADGAPPAVKALREAIAAADGVVIVTPEYNGSYPGVLKNALDWLSRSELA 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2085998039 100 GKKVLPIATGGTLAHLLSLEFAFKPLFSVLGAKEVPQGVYL 140
Cdd:COG0431   102 GKPVALVSTSGGARGGLRALEHLRPVLSELGAVVLPPQVSI 142
FMN_red pfam03358
NADPH-dependent FMN reductase;
27-144 1.23e-22

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 88.06  E-value: 1.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085998039  27 ELVQRGGKVDELTIRDLPP----EALLHAHFTDPVIQSAQNLVEHADSIIVVSPVYKASYPGLLKSFFDLIP----EKGL 98
Cdd:pfam03358  25 ELLEEGAEVELIDLADLILplcdEDLEEEQGDPDDVQELREKIAAADAIIIVTPEYNGSVSGLLKNAIDWLSrlrgGKEL 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2085998039  99 SGKKVLPIATGGTLAHLLSLEFAFKPLFSVLGAKEVPQGVYLIDSQ 144
Cdd:pfam03358 105 RGKPVAIVSTGGGRSGGLRAVEQLRQVLAELGAIVVPSGQVAVGNA 150
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 24-135 7.15e-10

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: 55.42  E-value: 7.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085998039  24 LKRELVQRGGKVDELTIRDLPPEALLHAHFTD-------PVIQSAQNLVEHADSIIVVSPVYKASYPGLLKSFFDLI--- 93
Cdd:pfam02525  23 LVEALKAAGHEVTVRDLYALFLPVLDAEDLADltypqgaADVESEQEELLAADVIVFQFPLYWFSVPALLKGWIDRVlra 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2085998039  94 -----------PEKGLSGKKVLPIATGGTLAHL--------LSLEFAFKPL---FSVLGAKEVP 135
Cdd:pfam02525 103 gfafkyeeggpGGGGLLGKKVLVIVTTGGPEYAygkggyngFSLDELLPYLrgiLGFCGITDLP 166
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 24-125 1.72e-09

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 54.46  E-value: 1.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085998039  24 LKRELVQRGGKVdelTIRDL-----PP----EALLHAHFTDPVIQSAQNLVEHADSIIVVSPVYKASYPGLLKSFFDLI- 93
Cdd:COG2249    22 AAEGLEAAGHEV---TVHDLyaegfDPvlsaADFYRDGPLPIDVAAEQELLLWADHLVFQFPLWWYSMPALLKGWIDRVl 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2085998039  94 ------------PEKGLSGKKVLPIATGGTLAHLLSLEFAFKPL 125
Cdd:COG2249    99 tpgfaygygggyPGGLLKGKKALLVVTTGGPEEAYSRLGYGGPI 142
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 26-170 1.57e-07

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 48.77  E-value: 1.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085998039  26 RELVQRGGKVDELTIRDL---PPEALLHAH---FTDPVIQSAQNLVEhADSIIVVSPVYKASYPGLLKSFFD-----LIP 94
Cdd:COG0655    24 EGAEEAGAEVELIRLADLdikPCIGCGGTGkcvIKDDMNAIYEKLLE-ADGIIFGSPTYFGNMSAQLKAFIDrlyalWAK 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2085998039  95 EKGLSGKKVLPIATGGT---LAHLLSLEFAFKplfsVLGAKEVPQGVYliDSQLSYSGNEVtfLDPVVEERVQEAVRNL 170
Cdd:COG0655   103 GKLLKGKVGAVFTTGGHggaEATLLSLNTFLL----HHGMIVVGLPPY--GAVGGGGPGDV--LDEEGLATARELGKRL 173
FldA COG0716
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ...
 65-111 3.92e-05

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


Pssm-ID: 440480 [Multi-domain]  Cd Length: 135  Bit Score: 41.43  E-value: 3.92e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2085998039  65 VEHADSIIVVSPVYKASYPGLLKSFFDLIPEKgLSGKKVLPIATGGT 111
Cdd:COG0716    41 LEDYDLLILGTPTWAGELPDDWEDFLEELKED-LSGKKVALFGTGDS 86
PRK00170 PRK00170
azoreductase; Reviewed
 36-110 1.69e-04

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 40.65  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085998039  36 DELTIRDL-----------------PPEALLHAHFTDPVIQSAQNLVE--HADSIIVVSPVYKASYPGLLKSFFDLI--- 93
Cdd:PRK00170   36 DEVTVRDLaaepipvldgevvgalgKSAETLTPRQQEAVALSDELLEEflAADKIVIAAPMYNFSIPTQLKAYIDLIara 115

                          90       100
                  ....*....|....*....|....*..
gi 2085998039  94 ----------PEKGLSGKKVLPIATGG 110
Cdd:PRK00170  116 gktfrytengPVGLVTGKKALLITSRG 142
 
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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