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Conserved domains on  [gi|446744559|ref|WP_000821815|]
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MULTISPECIES: NAD(P)H-dependent oxidoreductase [Bacillus cereus group]

Protein Classification

NAD(P)H-dependent oxidoreductase( domain architecture ID 10505769)

NAD(P)H-dependent oxidoreductase which catalyzes the reduction or oxidation of a substrate coupled to the oxidation or reduction, respectively, of a nicotinamide adenine dinucleotide cofactor NAD(P)H or NAD(P)+

CATH:  3.40.50.360
EC:  1.-.-.-
Gene Ontology:  GO:0016491|GO:0010181
SCOP:  3001217

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FMN_red pfam03358
NADPH-dependent FMN reductase;
3-156 4.87e-20

NADPH-dependent FMN reductase;


:

Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 83.06  E-value: 4.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446744559    3 RILLYSGSRNNDSRTNKIINELKLHIEKYFSDIVLDIFDPIsKPLLHSTGCKNCFnrgicpsdglEGDYGRELKEIVDSA 82
Cdd:pfam03358   2 KILAISGSPRKGSNTRKLARWAAELLEEGAEVELIDLADLI-LPLCDEDLEEEQG----------DPDDVQELREKIAAA 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446744559   83 DLIIFATPVYSHNVSSDAKIFIDRLSYWGHLLKLVSKPVITVVTAES-NGGDLVEAYLYKIFSFMGATVVNSEVF 156
Cdd:pfam03358  71 DAIIIVTPEYNGSVSGLLKNAIDWLSRLRGGKELRGKPVAIVSTGGGrSGGLRAVEQLRQVLAELGAIVVPSGQV 145
 
Name Accession Description Interval E-value
FMN_red pfam03358
NADPH-dependent FMN reductase;
3-156 4.87e-20

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 83.06  E-value: 4.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446744559    3 RILLYSGSRNNDSRTNKIINELKLHIEKYFSDIVLDIFDPIsKPLLHSTGCKNCFnrgicpsdglEGDYGRELKEIVDSA 82
Cdd:pfam03358   2 KILAISGSPRKGSNTRKLARWAAELLEEGAEVELIDLADLI-LPLCDEDLEEEQG----------DPDDVQELREKIAAA 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446744559   83 DLIIFATPVYSHNVSSDAKIFIDRLSYWGHLLKLVSKPVITVVTAES-NGGDLVEAYLYKIFSFMGATVVNSEVF 156
Cdd:pfam03358  71 DAIIIVTPEYNGSVSGLLKNAIDWLSRLRGGKELRGKPVAIVSTGGGrSGGLRAVEQLRQVLAELGAIVVPSGQV 145
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
3-151 1.02e-18

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 80.36  E-value: 1.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446744559   3 RILLYSGSRNNDSRTNKIINELKLHIEKyfSDIVLDIFDPISKPLlhsTGCKNCFNRGICPSDglegDYGRELKEIVDSA 82
Cdd:COG0655    1 KILVINGSPRKNGNTAALAEAVAEGAEE--AGAEVELIRLADLDI---KPCIGCGGTGKCVIK----DDMNAIYEKLLEA 71
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446744559  83 DLIIFATPVYSHNVSSDAKIFIDRLSY-WGHLLKLVSKPVITVVTAESNGGDLVEAYLYKIFSFMGATVV 151
Cdd:COG0655   72 DGIIFGSPTYFGNMSAQLKAFIDRLYAlWAKGKLLKGKVGAVFTTGGHGGAEATLLSLNTFLLHHGMIVV 141
M14_ASTE_ASPA_like cd06230
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily; The ...
1-85 3.87e-03

Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily; The Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily belongs to the M14 family of metallocarboxypeptidases (MCPs), and includes ASTE, which catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway, and aspartoacylase (ASPA, also known as aminoacylase 2, and ACY-2; EC:3.5.1.15) which cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD.


Pssm-ID: 349449 [Multi-domain]  Cd Length: 177  Bit Score: 36.91  E-value: 3.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446744559   1 MKRIllYSGSRNNDSrTNKIINELKLHIEKyFSDIVLDifdpiskplLHSTGCKNCFNRGICPSDGLEGDYGRELKEIVD 80
Cdd:cd06230   59 LNRI--FPGDPDGSP-TERLAHELTELILK-HADALID---------LHSGGTGRLVPYAILDYDSDAREKSRELARAFG 125

                 ....*
gi 446744559  81 SADLI 85
Cdd:cd06230  126 GTPVI 130
 
Name Accession Description Interval E-value
FMN_red pfam03358
NADPH-dependent FMN reductase;
3-156 4.87e-20

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 83.06  E-value: 4.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446744559    3 RILLYSGSRNNDSRTNKIINELKLHIEKYFSDIVLDIFDPIsKPLLHSTGCKNCFnrgicpsdglEGDYGRELKEIVDSA 82
Cdd:pfam03358   2 KILAISGSPRKGSNTRKLARWAAELLEEGAEVELIDLADLI-LPLCDEDLEEEQG----------DPDDVQELREKIAAA 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446744559   83 DLIIFATPVYSHNVSSDAKIFIDRLSYWGHLLKLVSKPVITVVTAES-NGGDLVEAYLYKIFSFMGATVVNSEVF 156
Cdd:pfam03358  71 DAIIIVTPEYNGSVSGLLKNAIDWLSRLRGGKELRGKPVAIVSTGGGrSGGLRAVEQLRQVLAELGAIVVPSGQV 145
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
3-151 1.02e-18

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 80.36  E-value: 1.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446744559   3 RILLYSGSRNNDSRTNKIINELKLHIEKyfSDIVLDIFDPISKPLlhsTGCKNCFNRGICPSDglegDYGRELKEIVDSA 82
Cdd:COG0655    1 KILVINGSPRKNGNTAALAEAVAEGAEE--AGAEVELIRLADLDI---KPCIGCGGTGKCVIK----DDMNAIYEKLLEA 71
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446744559  83 DLIIFATPVYSHNVSSDAKIFIDRLSY-WGHLLKLVSKPVITVVTAESNGGDLVEAYLYKIFSFMGATVV 151
Cdd:COG0655   72 DGIIFGSPTYFGNMSAQLKAFIDRLYAlWAKGKLLKGKVGAVFTTGGHGGAEATLLSLNTFLLHHGMIVV 141
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
2-157 1.83e-12

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 63.25  E-value: 1.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446744559   2 KRILLYSGSRNNDSRTNKIINELKLHIEKyfSDIVLDIFDPISKPLLHstgckncFNRGIcPSDGLEGDYgRELKEIVDS 81
Cdd:COG0431    1 MKILVISGSLRPGSFNRKLARAAAELAPA--AGAEVELIDLRDLDLPL-------YDEDL-EADGAPPAV-KALREAIAA 69
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446744559  82 ADLIIFATPVYSHNVSSDAKIFIDRLSY--WGHllklvsKPV-ITVVTAESNGGDLVEAYLYKIFSFMGATVVNSEVFL 157
Cdd:COG0431   70 ADGVVIVTPEYNGSYPGVLKNALDWLSRseLAG------KPVaLVSTSGGARGGLRALEHLRPVLSELGAVVLPPQVSI 142
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
2-156 1.36e-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: 47.33  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446744559    2 KRILLYSGSRNNDSRTNKIINELKLHIEKYFSDI-VLDIFDpiskpllhstgcknCFNRGICPSDGLEGDYGRELKEI-- 78
Cdd:pfam02525   1 MKILIINAHPRPGSFSSRLADALVEALKAAGHEVtVRDLYA--------------LFLPVLDAEDLADLTYPQGAADVes 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446744559   79 ----VDSADLIIFATPVYSHNVSSDAKIFIDRL-------SYWGHLL---KLVSKPVITVVTA------------ESNGG 132
Cdd:pfam02525  67 eqeeLLAADVIVFQFPLYWFSVPALLKGWIDRVlragfafKYEEGGPgggGLLGKKVLVIVTTggpeyaygkggyNGFSL 146
                         170       180
                  ....*....|....*....|....
gi 446744559  133 DLVEAYLYKIFSFMGATVVNSEVF 156
Cdd:pfam02525 147 DELLPYLRGILGFCGITDLPPFAV 170
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
1-151 5.14e-06

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


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 45.89  E-value: 5.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446744559   1 MKRILLYSGS-RNNDSRTNKIINELklhIEKY------FSDIVLDIFD----PISKPLLHSTGCkncfnrgicPSDGLEG 69
Cdd:COG1182    1 MMKLLHIDSSpRGEGSVSRRLADAF---VAALraahpdDEVTYRDLAAeplpHLDGAWLAAFFT---------PAEGRTP 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446744559  70 DYGRELK---EIVD---SADLIIFATPVYSHNVSSDAKIFIDRLS------------YWGhLLKlvSKPVItVVTAesNG 131
Cdd:COG1182   69 EQQAALAlsdELIDellAADVIVIGAPMYNFGIPSQLKAWIDHIAragrtfrytengPVG-LLT--GKKAV-VITA--RG 142
                        170       180       190
                 ....*....|....*....|....*....|
gi 446744559 132 G----------DLVEAYLYKIFSFMGATVV 151
Cdd:COG1182  143 GvysggpaagmDFQTPYLRTVLGFIGITDV 172
FldA COG0716
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ...
69-156 1.93e-04

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


Pssm-ID: 440480 [Multi-domain]  Cd Length: 135  Bit Score: 40.27  E-value: 1.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446744559  69 GDYGRELKEI-------VDSADLIIFATPVYSHNVSSDAKIFIDRLSYwghllKLVSKPVITVVTAESNGGDLVEAYLYK 141
Cdd:COG0716   24 GAAGVDLFEIedadlddLEDYDLLILGTPTWAGELPDDWEDFLEELKE-----DLSGKKVALFGTGDSSGYGDALGELKE 98
                         90
                 ....*....|....*
gi 446744559 142 IFSFMGATVVNSEVF 156
Cdd:COG0716   99 LLEEKGAKVVGGYDF 113
M14_ASTE_ASPA_like cd06230
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily; The ...
1-85 3.87e-03

Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily; The Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily belongs to the M14 family of metallocarboxypeptidases (MCPs), and includes ASTE, which catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway, and aspartoacylase (ASPA, also known as aminoacylase 2, and ACY-2; EC:3.5.1.15) which cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD.


Pssm-ID: 349449 [Multi-domain]  Cd Length: 177  Bit Score: 36.91  E-value: 3.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446744559   1 MKRIllYSGSRNNDSrTNKIINELKLHIEKyFSDIVLDifdpiskplLHSTGCKNCFNRGICPSDGLEGDYGRELKEIVD 80
Cdd:cd06230   59 LNRI--FPGDPDGSP-TERLAHELTELILK-HADALID---------LHSGGTGRLVPYAILDYDSDAREKSRELARAFG 125

                 ....*
gi 446744559  81 SADLI 85
Cdd:cd06230  126 GTPVI 130
 
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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