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Conserved domains on  [gi|170089119|ref|XP_001875782|]
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uncharacterized protein LACBIDRAFT_308973 [Laccaria bicolor S238N-H82]

Protein Classification

NAD(P)H-dependent flavin oxidoreductase( domain architecture ID 11449685)

NAD(P)H-dependent flavin oxidoreductase similar to nitronate monooxygenase, an FMN-dependent enzyme that uses molecular oxygen to oxidize (anionic) alkyl nitronates and nitroalkanes to the corresponding carbonyl compounds and nitrite

CATH:  3.20.20.70
EC:  1.13.12.-
Gene Ontology:  GO:0004497|GO:0016703|GO:0010181
PubMed:  10694883

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
10-316 3.00e-106

NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];


:

Pssm-ID: 441673 [Multi-domain]  Cd Length: 302  Bit Score: 312.82  E-value: 3.00e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089119  10 LGIRIPAVQGGMQWVGVPRLVAAVSEAGGLGVLTALTQPsPEALRAAIRETRTLTSKPFGVNITLLPSinPPDYEGYARA 89
Cdd:COG2070    1 LGIRYPIIQGPMAGVSTPELAAAVSNAGGLGSIAAGNLT-PEALREEIRKIRELTDGPFGVNLIVHPA--NPRFEELLEV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089119  90 AVEEGVRIFETAGNNPGALIKYFKSNGCIVLHKCTAIRHAKSAERLGVDVISIDGLECAGHPGEDDIGGLVLMARAAKEL 169
Cdd:COG2070   78 VLEEGVPVVSTSAGLPADLIERLKEAGIKVIPIVTSVREARKAEKAGADAVVAEGAEAGGHRGADEVSTFALVPEVRDAV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089119 170 KVPFIASGGIADARGFAAALALGAAGVNMGTRFMCTVESPIHQNIKEKIVASTERDTVHIFRTLHNTARVFKNKVAMEVV 249
Cdd:COG2070  158 DIPVIAAGGIADGRGIAAALALGADGVQMGTRFLATEESPAHEAYKQALVDAKEEDTVLTRSFTGRPARALRNSFTREGL 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170089119 250 AIERRPGgakFEDVKDLVSGARGRKVYELGDPDYGIWSAGIAVGLIDDIPTCKELLERLEKQVAEII 316
Cdd:COG2070  238 DLEAECL---YPILEALTAGKRLRAAAAEGDLEKGLLWAGQGAGLIRDILPAAELVARLVAEAEAAL 301
 
Name Accession Description Interval E-value
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
10-316 3.00e-106

NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];


Pssm-ID: 441673 [Multi-domain]  Cd Length: 302  Bit Score: 312.82  E-value: 3.00e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089119  10 LGIRIPAVQGGMQWVGVPRLVAAVSEAGGLGVLTALTQPsPEALRAAIRETRTLTSKPFGVNITLLPSinPPDYEGYARA 89
Cdd:COG2070    1 LGIRYPIIQGPMAGVSTPELAAAVSNAGGLGSIAAGNLT-PEALREEIRKIRELTDGPFGVNLIVHPA--NPRFEELLEV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089119  90 AVEEGVRIFETAGNNPGALIKYFKSNGCIVLHKCTAIRHAKSAERLGVDVISIDGLECAGHPGEDDIGGLVLMARAAKEL 169
Cdd:COG2070   78 VLEEGVPVVSTSAGLPADLIERLKEAGIKVIPIVTSVREARKAEKAGADAVVAEGAEAGGHRGADEVSTFALVPEVRDAV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089119 170 KVPFIASGGIADARGFAAALALGAAGVNMGTRFMCTVESPIHQNIKEKIVASTERDTVHIFRTLHNTARVFKNKVAMEVV 249
Cdd:COG2070  158 DIPVIAAGGIADGRGIAAALALGADGVQMGTRFLATEESPAHEAYKQALVDAKEEDTVLTRSFTGRPARALRNSFTREGL 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170089119 250 AIERRPGgakFEDVKDLVSGARGRKVYELGDPDYGIWSAGIAVGLIDDIPTCKELLERLEKQVAEII 316
Cdd:COG2070  238 DLEAECL---YPILEALTAGKRLRAAAAEGDLEKGLLWAGQGAGLIRDILPAAELVARLVAEAEAAL 301
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
12-239 1.66e-75

2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.


Pssm-ID: 240081 [Multi-domain]  Cd Length: 236  Bit Score: 231.99  E-value: 1.66e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089119  12 IRIPAVQGGMQWVGVPRLVAAVSEAGGLGVLTALTQpSPEALRAAIRETRTLTSKPFGVNITLLPSinPPDYEGYARAAV 91
Cdd:cd04730    1 IRYPIIQAPMAGVSTPELAAAVSNAGGLGFIGAGYL-TPEALRAEIRKIRALTDKPFGVNLLVPSS--NPDFEALLEVAL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089119  92 EEGVRIFETAGNNPGALIKYFKSNGCIVLHKCTAIRHAKSAERLGVDVISIDGLECAGHPGEDDIGGLVLMARAAKELKV 171
Cdd:cd04730   78 EEGVPVVSFSFGPPAEVVERLKAAGIKVIPTVTSVEEARKAEAAGADALVAQGAEAGGHRGTFDIGTFALVPEVRDAVDI 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 170089119 172 PFIASGGIADARGFAAALALGAAGVNMGTRFMCTVESPIHQNIKEKIVASTERDTVHIFRTLHNTARV 239
Cdd:cd04730  158 PVIAAGGIADGRGIAAALALGADGVQMGTRFLATEESGASPAYKQALLAATAEDTVLTRAFSGRPARG 225
NMO pfam03060
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ...
4-308 6.96e-48

Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane dioxygenase (NPD) (EC:1.13.11.32), is an FMN-dependent enzyme that uses molecular oxygen to oxidize (anionic) alkyl nitronates and, in the case of the enzyme from Neurospora crassa, (neutral) nitroalkanes to the corresponding carbonyl compounds and nitrite. Previously classified as 2-nitropropane dioxygenase, but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms. The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor. Active towards linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, towards propyl-2-nitronate. The enzyme from N. crassa can also utilize neutral nitroalkanes, but with lower activity. One atom of oxygen is incorporated into the carbonyl group of the aldehyde product. The reaction appears to involve the formation of an enzyme-bound nitronate radical and an a-peroxynitroethane species, which then decomposes, either in the active site of the enzyme or after release, to acetaldehyde and nitrite.


Pssm-ID: 367316 [Multi-domain]  Cd Length: 331  Bit Score: 164.22  E-value: 6.96e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089119    4 TPLTKLLGIRIPAVQGGMQWVGVPRLVAAVSEAGGLGVLTALTQpSPEALRAAIRETRTLTSKPFGVNITLLPSINPPDY 83
Cdd:pfam03060   2 SLLTDIHTIKPPVQQPMMGGISWPRLAAAVSNAGGLGVLASGYL-TPDRLYQEIRKVKALTDKPFGANLFLPKPDLADPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089119   84 EGYAR--------AAVEEGVRIFE---------------TAGNNPGALIKYFKSNGCIVLHKCTAIRHAKSAERLGVDVI 140
Cdd:pfam03060  81 ANYAKilgnnalgYNIEEGVPDYGkvlvdldegvnvvsfGFGLPPNDVVFRLHFAGVALIPTISSAKEARIAEARGADAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089119  141 SIDGLECAGHPGEDDIGG---LVLMARAAKELKVPFIASGGIADARGFAAALALGAAGVNMGTRFMCTVESPIHQNIKEK 217
Cdd:pfam03060 161 IVQGPEAGGHQGTPEYGDkglFRLVPQVPDAVDIPVIAAGGIWDRRGVAAALALGASGVQMGTRFLLTKESGAHDAHKQK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089119  218 IVASTERDTVHIFRTLHNTARVFKNKVAMEvvaIERRPGGAKFEDVKDLVSGARGRKVYELGDPDYGIWSAGIAVGLIDD 297
Cdd:pfam03060 241 ITEAGEDDTLVTSPFSGRPARALANGFLEE---LEEPKIATLAYPEAHEMTKPIRAAAVRGGNREEGLLWAGQGIYRLDR 317
                         330
                  ....*....|.
gi 170089119  298 IPTCKELLERL 308
Cdd:pfam03060 318 IISVKELIESL 328
 
Name Accession Description Interval E-value
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
10-316 3.00e-106

NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];


Pssm-ID: 441673 [Multi-domain]  Cd Length: 302  Bit Score: 312.82  E-value: 3.00e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089119  10 LGIRIPAVQGGMQWVGVPRLVAAVSEAGGLGVLTALTQPsPEALRAAIRETRTLTSKPFGVNITLLPSinPPDYEGYARA 89
Cdd:COG2070    1 LGIRYPIIQGPMAGVSTPELAAAVSNAGGLGSIAAGNLT-PEALREEIRKIRELTDGPFGVNLIVHPA--NPRFEELLEV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089119  90 AVEEGVRIFETAGNNPGALIKYFKSNGCIVLHKCTAIRHAKSAERLGVDVISIDGLECAGHPGEDDIGGLVLMARAAKEL 169
Cdd:COG2070   78 VLEEGVPVVSTSAGLPADLIERLKEAGIKVIPIVTSVREARKAEKAGADAVVAEGAEAGGHRGADEVSTFALVPEVRDAV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089119 170 KVPFIASGGIADARGFAAALALGAAGVNMGTRFMCTVESPIHQNIKEKIVASTERDTVHIFRTLHNTARVFKNKVAMEVV 249
Cdd:COG2070  158 DIPVIAAGGIADGRGIAAALALGADGVQMGTRFLATEESPAHEAYKQALVDAKEEDTVLTRSFTGRPARALRNSFTREGL 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170089119 250 AIERRPGgakFEDVKDLVSGARGRKVYELGDPDYGIWSAGIAVGLIDDIPTCKELLERLEKQVAEII 316
Cdd:COG2070  238 DLEAECL---YPILEALTAGKRLRAAAAEGDLEKGLLWAGQGAGLIRDILPAAELVARLVAEAEAAL 301
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
12-239 1.66e-75

2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.


Pssm-ID: 240081 [Multi-domain]  Cd Length: 236  Bit Score: 231.99  E-value: 1.66e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089119  12 IRIPAVQGGMQWVGVPRLVAAVSEAGGLGVLTALTQpSPEALRAAIRETRTLTSKPFGVNITLLPSinPPDYEGYARAAV 91
Cdd:cd04730    1 IRYPIIQAPMAGVSTPELAAAVSNAGGLGFIGAGYL-TPEALRAEIRKIRALTDKPFGVNLLVPSS--NPDFEALLEVAL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089119  92 EEGVRIFETAGNNPGALIKYFKSNGCIVLHKCTAIRHAKSAERLGVDVISIDGLECAGHPGEDDIGGLVLMARAAKELKV 171
Cdd:cd04730   78 EEGVPVVSFSFGPPAEVVERLKAAGIKVIPTVTSVEEARKAEAAGADALVAQGAEAGGHRGTFDIGTFALVPEVRDAVDI 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 170089119 172 PFIASGGIADARGFAAALALGAAGVNMGTRFMCTVESPIHQNIKEKIVASTERDTVHIFRTLHNTARV 239
Cdd:cd04730  158 PVIAAGGIADGRGIAAALALGADGVQMGTRFLATEESGASPAYKQALLAATAEDTVLTRAFSGRPARG 225
NMO pfam03060
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ...
4-308 6.96e-48

Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane dioxygenase (NPD) (EC:1.13.11.32), is an FMN-dependent enzyme that uses molecular oxygen to oxidize (anionic) alkyl nitronates and, in the case of the enzyme from Neurospora crassa, (neutral) nitroalkanes to the corresponding carbonyl compounds and nitrite. Previously classified as 2-nitropropane dioxygenase, but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms. The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor. Active towards linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, towards propyl-2-nitronate. The enzyme from N. crassa can also utilize neutral nitroalkanes, but with lower activity. One atom of oxygen is incorporated into the carbonyl group of the aldehyde product. The reaction appears to involve the formation of an enzyme-bound nitronate radical and an a-peroxynitroethane species, which then decomposes, either in the active site of the enzyme or after release, to acetaldehyde and nitrite.


Pssm-ID: 367316 [Multi-domain]  Cd Length: 331  Bit Score: 164.22  E-value: 6.96e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089119    4 TPLTKLLGIRIPAVQGGMQWVGVPRLVAAVSEAGGLGVLTALTQpSPEALRAAIRETRTLTSKPFGVNITLLPSINPPDY 83
Cdd:pfam03060   2 SLLTDIHTIKPPVQQPMMGGISWPRLAAAVSNAGGLGVLASGYL-TPDRLYQEIRKVKALTDKPFGANLFLPKPDLADPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089119   84 EGYAR--------AAVEEGVRIFE---------------TAGNNPGALIKYFKSNGCIVLHKCTAIRHAKSAERLGVDVI 140
Cdd:pfam03060  81 ANYAKilgnnalgYNIEEGVPDYGkvlvdldegvnvvsfGFGLPPNDVVFRLHFAGVALIPTISSAKEARIAEARGADAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089119  141 SIDGLECAGHPGEDDIGG---LVLMARAAKELKVPFIASGGIADARGFAAALALGAAGVNMGTRFMCTVESPIHQNIKEK 217
Cdd:pfam03060 161 IVQGPEAGGHQGTPEYGDkglFRLVPQVPDAVDIPVIAAGGIWDRRGVAAALALGASGVQMGTRFLLTKESGAHDAHKQK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089119  218 IVASTERDTVHIFRTLHNTARVFKNKVAMEvvaIERRPGGAKFEDVKDLVSGARGRKVYELGDPDYGIWSAGIAVGLIDD 297
Cdd:pfam03060 241 ITEAGEDDTLVTSPFSGRPARALANGFLEE---LEEPKIATLAYPEAHEMTKPIRAAAVRGGNREEGLLWAGQGIYRLDR 317
                         330
                  ....*....|.
gi 170089119  298 IPTCKELLERL 308
Cdd:pfam03060 318 IISVKELIESL 328
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
26-183 7.51e-05

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 42.96  E-value: 7.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089119  26 VPRLVAAVSEAGGLGVLTALTQPSPEALRAAIRETRTLTSKPFGVNITLLPSINPPDYEG-YARAAVEEGVRIFETAGNN 104
Cdd:cd04722   18 AKAAAEAGADAIIVGTRSSDPEEAETDDKEVLKEVAAETDLPLGVQLAINDAAAAVDIAAaAARAAGADGVEIHGAVGYL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089119 105 PGALIKYFKS-----NGCIVLHKCTAIRH--AKSAERLGVDVISIDGLECAGHPGEDDIGGLVLMARAAKELKVPFIASG 177
Cdd:cd04722   98 AREDLELIRElreavPDVKVVVKLSPTGElaAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRGSKVPVIAGG 177

                 ....*.
gi 170089119 178 GIADAR 183
Cdd:cd04722  178 GINDPE 183
 
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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