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Conserved domains on  [gi|1847675378|ref|WP_172583990|]
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flavodoxin family protein [Ligilactobacillus agilis]

Protein Classification

flavodoxin family protein( domain architecture ID 10002025)

flavodoxin family protein is an electron-transfer flavoprotein, such as Methanosarcina thermophila iron-sulfur flavoprotein (Isf) and Clostridium saccharobutylicum flavodoxin, which are [4Fe-4S] cluster-binding electron-transfer flavoproteins

CATH:  3.40.50.360
Gene Ontology:  GO:0009055|GO:0010181
SCOP:  4003377

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
2-186 1.14e-20

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


:

Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 86.14  E-value: 1.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847675378   2 KVLGILGAHKEHGVTRMMLDQVLHQVQAPNTS-EIIYLEDYQIKPDIKGQPNPT------MDQIIAKLEAADVWVIAAPT 74
Cdd:COG0655     1 KILVINGSPRKNGNTAALAEAVAEGAEEAGAEvELIRLADLDIKPCIGCGGTGKcvikddMNAIYEKLLEADGIIFGSPT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847675378  75 YWGGLSGVMKNFFDclrqRLVRFDHKGgthpDKFAHKHYISLTNCYAGKwenflsgvTDASFRTIDKVLTAGGLIKIGEA 154
Cdd:COG0655    81 YFGNMSAQLKAFID----RLYALWAKG----KLLKGKVGAVFTTGGHGG--------AEATLLSLNTFLLHHGMIVVGLP 144
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1847675378 155 VQTATWGLTELAPAKQKELTK---LGQKINRATRK 186
Cdd:COG0655   145 PYGAVGGGGPGDVLDEEGLATareLGKRLAELAKK 179
 
Name Accession Description Interval E-value
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
2-186 1.14e-20

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 86.14  E-value: 1.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847675378   2 KVLGILGAHKEHGVTRMMLDQVLHQVQAPNTS-EIIYLEDYQIKPDIKGQPNPT------MDQIIAKLEAADVWVIAAPT 74
Cdd:COG0655     1 KILVINGSPRKNGNTAALAEAVAEGAEEAGAEvELIRLADLDIKPCIGCGGTGKcvikddMNAIYEKLLEADGIIFGSPT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847675378  75 YWGGLSGVMKNFFDclrqRLVRFDHKGgthpDKFAHKHYISLTNCYAGKwenflsgvTDASFRTIDKVLTAGGLIKIGEA 154
Cdd:COG0655    81 YFGNMSAQLKAFID----RLYALWAKG----KLLKGKVGAVFTTGGHGG--------AEATLLSLNTFLLHHGMIVVGLP 144
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1847675378 155 VQTATWGLTELAPAKQKELTK---LGQKINRATRK 186
Cdd:COG0655   145 PYGAVGGGGPGDVLDEEGLATareLGKRLAELAKK 179
FMN_red pfam03358
NADPH-dependent FMN reductase;
1-88 3.01e-18

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 78.82  E-value: 3.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847675378   1 MKVLGILGAHKEHGVTRMMLDQVLHQVQAPNTSEIIYLEDYQI-----KPDIKGQPNPTMDQIIAKLEAADVWVIAAPTY 75
Cdd:pfam03358   1 MKILAISGSPRKGSNTRKLARWAAELLEEGAEVELIDLADLILplcdeDLEEEQGDPDDVQELREKIAAADAIIIVTPEY 80
                          90
                  ....*....|...
gi 1847675378  76 WGGLSGVMKNFFD 88
Cdd:pfam03358  81 NGSVSGLLKNAID 93
PRK00170 PRK00170
azoreductase; Reviewed
54-88 5.00e-03

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 37.18  E-value: 5.00e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1847675378  54 TMDQIIAKLEAADVWVIAAPTYWGGLSGVMKNFFD 88
Cdd:PRK00170   76 LSDELLEEFLAADKIVIAAPMYNFSIPTQLKAYID 110
 
Name Accession Description Interval E-value
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
2-186 1.14e-20

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 86.14  E-value: 1.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847675378   2 KVLGILGAHKEHGVTRMMLDQVLHQVQAPNTS-EIIYLEDYQIKPDIKGQPNPT------MDQIIAKLEAADVWVIAAPT 74
Cdd:COG0655     1 KILVINGSPRKNGNTAALAEAVAEGAEEAGAEvELIRLADLDIKPCIGCGGTGKcvikddMNAIYEKLLEADGIIFGSPT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847675378  75 YWGGLSGVMKNFFDclrqRLVRFDHKGgthpDKFAHKHYISLTNCYAGKwenflsgvTDASFRTIDKVLTAGGLIKIGEA 154
Cdd:COG0655    81 YFGNMSAQLKAFID----RLYALWAKG----KLLKGKVGAVFTTGGHGG--------AEATLLSLNTFLLHHGMIVVGLP 144
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1847675378 155 VQTATWGLTELAPAKQKELTK---LGQKINRATRK 186
Cdd:COG0655   145 PYGAVGGGGPGDVLDEEGLATareLGKRLAELAKK 179
FMN_red pfam03358
NADPH-dependent FMN reductase;
1-88 3.01e-18

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 78.82  E-value: 3.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847675378   1 MKVLGILGAHKEHGVTRMMLDQVLHQVQAPNTSEIIYLEDYQI-----KPDIKGQPNPTMDQIIAKLEAADVWVIAAPTY 75
Cdd:pfam03358   1 MKILAISGSPRKGSNTRKLARWAAELLEEGAEVELIDLADLILplcdeDLEEEQGDPDDVQELREKIAAADAIIIVTPEY 80
                          90
                  ....*....|...
gi 1847675378  76 WGGLSGVMKNFFD 88
Cdd:pfam03358  81 NGSVSGLLKNAID 93
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
1-90 3.61e-12

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 62.48  E-value: 3.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847675378   1 MKVLGILGAHKEHGVTRMMLDQVLHQVQAPN-TSEIIYLEDYQI----KPDIKGQPNPTMDQIIAKLEAADVWVIAAPTY 75
Cdd:COG0431     1 MKILVISGSLRPGSFNRKLARAAAELAPAAGaEVELIDLRDLDLplydEDLEADGAPPAVKALREAIAAADGVVIVTPEY 80
                          90
                  ....*....|....*
gi 1847675378  76 WGGLSGVMKNFFDCL 90
Cdd:COG0431    81 NGSYPGVLKNALDWL 95
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
1-117 1.28e-06

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: 47.71  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847675378   1 MKVLgILGAHKEHG-VTRMMLDQVLHQVQApNTSEIIYLEDYQ-----IKPDIKGQPNPTMDQI-----IAKLEAADVWV 69
Cdd:pfam02525   1 MKIL-IINAHPRPGsFSSRLADALVEALKA-AGHEVTVRDLYAlflpvLDAEDLADLTYPQGAAdveseQEELLAADVIV 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1847675378  70 IAAPTYWGGLSGVMKNFFDC-LRQRLVRFDHKGGTHPDKFAHKHYISLT 117
Cdd:pfam02525  79 FQFPLYWFSVPALLKGWIDRvLRAGFAFKYEEGGPGGGGLLGKKVLVIV 127
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
55-101 1.45e-03

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


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 38.57  E-value: 1.45e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1847675378  55 MDQIIAKLEAADVWVIAAPTYWGGLSGVMKNFFDCLRQ--RLVRFDHKG 101
Cdd:COG1182    77 SDELIDELLAADVIVIGAPMYNFGIPSQLKAWIDHIARagRTFRYTENG 125
PRK00170 PRK00170
azoreductase; Reviewed
54-88 5.00e-03

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 37.18  E-value: 5.00e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1847675378  54 TMDQIIAKLEAADVWVIAAPTYWGGLSGVMKNFFD 88
Cdd:PRK00170   76 LSDELLEEFLAADKIVIAAPMYNFSIPTQLKAYID 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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