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Conserved domains on  [gi|4835780|gb|AAD30246|]
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Strong similarity to gb|AF049347 berberine bridge enzyme from Berberis stolonifera [Arabidopsis thaliana]

Protein Classification

FAD-dependent oxidoreductase( domain architecture ID 11416259)

FAD-dependent oxidoreductase is an FAD/FMN-binding enzyme that catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
73-275 2.27e-22

FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];


:

Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 99.97  E-value: 2.27e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835780   73 NTTATPKPAIVIAARSESHVQAAV-ICTKSlNIQLKTRSGGHDYEGVSyishVPFF---VLDMSNLRNI-TVDPATESAW 147
Cdd:COG0277  33 NSLYRGRPDAVVRPRSTEDVAAVVrLAAEH-GVPVVPRGGGTGLAGGA----VPLDggvVLDLSRMNRIlEVDPEDRTAT 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835780  148 VGAGATLGEVYyriwEKTKSHG--FPAGVC--PTVgagghisgggygnMI-------------RKYGLSVDYVTDAKIVD 210
Cdd:COG0277 108 VEAGVTLADLN----AALAPHGlfFPPDPSsqGTA-------------TIggniatnaggprsLKYGLTRDNVLGLEVVL 170

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4835780  211 VNGQVLDRKG------MGEDMFWAINGGGGaSFGVILAFKIKLVPVPPTVTVFRVEKNLVENATEMVHKWQ 275
Cdd:COG0277 171 ADGEVVRTGGrvpknvTGYDLFWLLVGSEG-TLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRALL 240
BBE pfam08031
Berberine and berberine like; This domain is found in the berberine bridge and berberine ...
 470-527 9.98e-18

Berberine and berberine like; This domain is found in the berberine bridge and berberine bridge- like enzymes which are involved in the biosynthesis of numerous isoquinoline alkaloids. They catalyze the transformation of the N-methyl group of (S)-reticuline into the C-8 berberine bridge carbon of (S)-scoulerine.


:

Pssm-ID: 369658 [Multi-domain]  Cd Length: 45  Bit Score: 76.83  E-value: 9.98e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 4835780    470 TYINYRDLDIGVntpgpnsyrvaevFGRMYFGENFDRLVKVKTAVDPQNFFRDEQSIP 527
Cdd:pfam08031   1 AYVNYPDLDLGD-------------WGERYFGSNFERLVEVKAKYDPDNVFRNEQSIP 45
 
Name Accession Description Interval E-value
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
73-275 2.27e-22

FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];


Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 99.97  E-value: 2.27e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835780   73 NTTATPKPAIVIAARSESHVQAAV-ICTKSlNIQLKTRSGGHDYEGVSyishVPFF---VLDMSNLRNI-TVDPATESAW 147
Cdd:COG0277  33 NSLYRGRPDAVVRPRSTEDVAAVVrLAAEH-GVPVVPRGGGTGLAGGA----VPLDggvVLDLSRMNRIlEVDPEDRTAT 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835780  148 VGAGATLGEVYyriwEKTKSHG--FPAGVC--PTVgagghisgggygnMI-------------RKYGLSVDYVTDAKIVD 210
Cdd:COG0277 108 VEAGVTLADLN----AALAPHGlfFPPDPSsqGTA-------------TIggniatnaggprsLKYGLTRDNVLGLEVVL 170

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4835780  211 VNGQVLDRKG------MGEDMFWAINGGGGaSFGVILAFKIKLVPVPPTVTVFRVEKNLVENATEMVHKWQ 275
Cdd:COG0277 171 ADGEVVRTGGrvpknvTGYDLFWLLVGSEG-TLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRALL 240
BBE pfam08031
Berberine and berberine like; This domain is found in the berberine bridge and berberine ...
 470-527 9.98e-18

Berberine and berberine like; This domain is found in the berberine bridge and berberine bridge- like enzymes which are involved in the biosynthesis of numerous isoquinoline alkaloids. They catalyze the transformation of the N-methyl group of (S)-reticuline into the C-8 berberine bridge carbon of (S)-scoulerine.


Pssm-ID: 369658 [Multi-domain]  Cd Length: 45  Bit Score: 76.83  E-value: 9.98e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 4835780    470 TYINYRDLDIGVntpgpnsyrvaevFGRMYFGENFDRLVKVKTAVDPQNFFRDEQSIP 527
Cdd:pfam08031   1 AYVNYPDLDLGD-------------WGERYFGSNFERLVEVKAKYDPDNVFRNEQSIP 45
FAD_binding_4 pfam01565
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ...
 80-217 2.55e-15

FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.


Pssm-ID: 426326 [Multi-domain]  Cd Length: 139  Bit Score: 73.00  E-value: 2.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835780     80 PAIVIAARSESHVQAAVICTKSLNIQLKTRSGGHDYEGVSYisHVPFFVLDMSNLRNI-TVDPATESAWVGAGATLGEVY 158
Cdd:pfam01565   1 PAAVVLPESEEEVAAIVRLANENGLPVLPRGGGSSLLGGAV--QTGGIVLDLSRLNGIlEIDPEDGTATVEAGVTLGDLV 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4835780    159 yriwEKTKSHGFPAGVCPTVGAGGHISGGGYGN----MIRKYGLSVDYVTDAKIVDVNGQVLD 217
Cdd:pfam01565  79 ----RALAAKGLLLGLDPGSGIPGTVGGAIATNaggyGSEKYGLTRDNVLGLEVVLADGEVVR 137
 
Name Accession Description Interval E-value
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
73-275 2.27e-22

FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];


Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 99.97  E-value: 2.27e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835780   73 NTTATPKPAIVIAARSESHVQAAV-ICTKSlNIQLKTRSGGHDYEGVSyishVPFF---VLDMSNLRNI-TVDPATESAW 147
Cdd:COG0277  33 NSLYRGRPDAVVRPRSTEDVAAVVrLAAEH-GVPVVPRGGGTGLAGGA----VPLDggvVLDLSRMNRIlEVDPEDRTAT 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835780  148 VGAGATLGEVYyriwEKTKSHG--FPAGVC--PTVgagghisgggygnMI-------------RKYGLSVDYVTDAKIVD 210
Cdd:COG0277 108 VEAGVTLADLN----AALAPHGlfFPPDPSsqGTA-------------TIggniatnaggprsLKYGLTRDNVLGLEVVL 170

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4835780  211 VNGQVLDRKG------MGEDMFWAINGGGGaSFGVILAFKIKLVPVPPTVTVFRVEKNLVENATEMVHKWQ 275
Cdd:COG0277 171 ADGEVVRTGGrvpknvTGYDLFWLLVGSEG-TLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRALL 240
BBE pfam08031
Berberine and berberine like; This domain is found in the berberine bridge and berberine ...
 470-527 9.98e-18

Berberine and berberine like; This domain is found in the berberine bridge and berberine bridge- like enzymes which are involved in the biosynthesis of numerous isoquinoline alkaloids. They catalyze the transformation of the N-methyl group of (S)-reticuline into the C-8 berberine bridge carbon of (S)-scoulerine.


Pssm-ID: 369658 [Multi-domain]  Cd Length: 45  Bit Score: 76.83  E-value: 9.98e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 4835780    470 TYINYRDLDIGVntpgpnsyrvaevFGRMYFGENFDRLVKVKTAVDPQNFFRDEQSIP 527
Cdd:pfam08031   1 AYVNYPDLDLGD-------------WGERYFGSNFERLVEVKAKYDPDNVFRNEQSIP 45
FAD_binding_4 pfam01565
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ...
 80-217 2.55e-15

FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.


Pssm-ID: 426326 [Multi-domain]  Cd Length: 139  Bit Score: 73.00  E-value: 2.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835780     80 PAIVIAARSESHVQAAVICTKSLNIQLKTRSGGHDYEGVSYisHVPFFVLDMSNLRNI-TVDPATESAWVGAGATLGEVY 158
Cdd:pfam01565   1 PAAVVLPESEEEVAAIVRLANENGLPVLPRGGGSSLLGGAV--QTGGIVLDLSRLNGIlEIDPEDGTATVEAGVTLGDLV 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4835780    159 yriwEKTKSHGFPAGVCPTVGAGGHISGGGYGN----MIRKYGLSVDYVTDAKIVDVNGQVLD 217
Cdd:pfam01565  79 ----RALAAKGLLLGLDPGSGIPGTVGGAIATNaggyGSEKYGLTRDNVLGLEVVLADGEVVR 137
 
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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