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Conserved domains on  [gi|981685239|ref|WP_059881787|]
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nitronate monooxygenase family protein [Burkholderia stagnalis]

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 ...
 30-381 4.39e-57

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


:

Pssm-ID: 441673 [Multi-domain]  Cd Length: 302  Bit Score: 188.78  E-value: 4.39e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981685239  30 SAHRLAGSVAREGALGTIASIdlrhhhadllercraqpvratleAANLDALAREIRLAKtySDGRGMIAVNVM--KAVSA 107
Cdd:COG2070   16 STPELAAAVSNAGGLGSIAAG-----------------------NLTPEALREEIRKIR--ELTDGPFGVNLIvhPANPR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981685239 108 HADYVRVACEHGADAIVMGAGLPLDLPDLTHGHDIALIPILSDSRGialvLKKWMKKGrlPDAIVIEHPaHAGGHLGVTQ 187
Cdd:COG2070   71 FEELLEVVLEEGVPVVSTSAGLPADLIERLKEAGIKVIPIVTSVRE----ARKAEKAG--ADAVVAEGA-EAGGHRGADE 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981685239 188 LDDMhdprfdfARVldesAQVIASLglareRIPLIVAGGINSHAAVRDALAAGANAVQVGTPFAVTEEGDAHPNFKRVLA 267
Cdd:COG2070  144 VSTF-------ALV----PEVRDAV-----DIPVIAAGGIADGRGIAAALALGADGVQMGTRFLATEESPAHEAYKQALV 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981685239 268 DAGPDDIVEFVSVTGLPARAVKTPWLDRYLRNETRirnklgalkqrcptaleclsvcglrdgiekfGHFCIDTRL----- 342
Cdd:COG2070  208 DAKEEDTVLTRSFTGRPARALRNSFTREGLDLEAE-------------------------------CLYPILEALtagkr 256

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 981685239 343 --AAALRGDVANGLFFRGrEALPFGRAIRSVRDLLDLLLTG 381
Cdd:COG2070  257 lrAAAAEGDLEKGLLWAG-QGAGLIRDILPAAELVARLVAE 296
 
Name Accession Description Interval E-value
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
 30-381 4.39e-57

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


Pssm-ID: 441673 [Multi-domain]  Cd Length: 302  Bit Score: 188.78  E-value: 4.39e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981685239  30 SAHRLAGSVAREGALGTIASIdlrhhhadllercraqpvratleAANLDALAREIRLAKtySDGRGMIAVNVM--KAVSA 107
Cdd:COG2070   16 STPELAAAVSNAGGLGSIAAG-----------------------NLTPEALREEIRKIR--ELTDGPFGVNLIvhPANPR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981685239 108 HADYVRVACEHGADAIVMGAGLPLDLPDLTHGHDIALIPILSDSRGialvLKKWMKKGrlPDAIVIEHPaHAGGHLGVTQ 187
Cdd:COG2070   71 FEELLEVVLEEGVPVVSTSAGLPADLIERLKEAGIKVIPIVTSVRE----ARKAEKAG--ADAVVAEGA-EAGGHRGADE 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981685239 188 LDDMhdprfdfARVldesAQVIASLglareRIPLIVAGGINSHAAVRDALAAGANAVQVGTPFAVTEEGDAHPNFKRVLA 267
Cdd:COG2070  144 VSTF-------ALV----PEVRDAV-----DIPVIAAGGIADGRGIAAALALGADGVQMGTRFLATEESPAHEAYKQALV 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981685239 268 DAGPDDIVEFVSVTGLPARAVKTPWLDRYLRNETRirnklgalkqrcptaleclsvcglrdgiekfGHFCIDTRL----- 342
Cdd:COG2070  208 DAKEEDTVLTRSFTGRPARALRNSFTREGLDLEAE-------------------------------CLYPILEALtagkr 256

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 981685239 343 --AAALRGDVANGLFFRGrEALPFGRAIRSVRDLLDLLLTG 381
Cdd:COG2070  257 lrAAAAEGDLEKGLLWAG-QGAGLIRDILPAAELVARLVAE 296
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
 30-288 1.14e-42

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: 149.17  E-value: 1.14e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981685239  30 SAHRLAGSVAREGALGTIASIdlrhhhadllercraqpvratleAANLDALAREIRLAKTYSDGRgmIAVNVMKAVSA-- 107
Cdd:cd04730   14 STPELAAAVSNAGGLGFIGAG-----------------------YLTPEALRAEIRKIRALTDKP--FGVNLLVPSSNpd 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981685239 108 HADYVRVACEHGADAIVMGAGLPLDLPDLTHGHDIALIPILSDSRgialVLKKWMKKGrlPDAIVIEHPaHAGGHLGVTQ 187
Cdd:cd04730   69 FEALLEVALEEGVPVVSFSFGPPAEVVERLKAAGIKVIPTVTSVE----EARKAEAAG--ADALVAQGA-EAGGHRGTFD 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981685239 188 LDDMhdprfdfARVldesAQVIASLGlarerIPLIVAGGINSHAAVRDALAAGANAVQVGTPFAVTEEGDAHPNFKRVLA 267
Cdd:cd04730  142 IGTF-------ALV----PEVRDAVD-----IPVIAAGGIADGRGIAAALALGADGVQMGTRFLATEESGASPAYKQALL 205

                        250       260
                 ....*....|....*....|.
gi 981685239 268 DAGPDDIVEFVSVTGLPARAV 288
Cdd:cd04730  206 AATAEDTVLTRAFSGRPARGL 226
NMO pfam03060
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ...
 33-301 4.97e-23

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: 98.74  E-value: 4.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981685239   33 RLAGSVAREGALGTIASidlRHHHADLLERCRAQPVRAT---LEAANLDALAREIRLAKTYSDGRGMIAVNVM--KAVSA 107
Cdd:pfam03060  26 RLAAAVSNAGGLGVLAS---GYLTPDRLYQEIRKVKALTdkpFGANLFLPKPDLADPAANYAKILGNNALGYNieEGVPD 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981685239  108 HADYVRVACEhGADAIVMGAGLPL-DLPDLTHGHDIALIPILSDSRGIALVLKKWmkkgrlPDAIVIEHPAhAGGHLGVt 186
Cdd:pfam03060 103 YGKVLVDLDE-GVNVVSFGFGLPPnDVVFRLHFAGVALIPTISSAKEARIAEARG------ADALIVQGPE-AGGHQGT- 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981685239  187 qlddmhdprfdFARVLDESAQVIASLGLARErIPLIVAGGINSHAAVRDALAAGANAVQVGTPFAVTEEGDAHPNFKRVL 266
Cdd:pfam03060 174 -----------PEYGDKGLFRLVPQVPDAVD-IPVIAAGGIWDRRGVAAALALGASGVQMGTRFLLTKESGAHDAHKQKI 241

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 981685239  267 ADAGPDDIVEFVSVTGLPARAVKTPWLDRYLRNET 301
Cdd:pfam03060 242 TEAGEDDTLVTSPFSGRPARALANGFLEELEEPKI 276
PRK04169 PRK04169
heptaprenylglyceryl phosphate synthase;
217-248 4.64e-04

heptaprenylglyceryl phosphate synthase;


Pssm-ID: 235237  Cd Length: 232  Bit Score: 41.33  E-value: 4.64e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 981685239 217 ERIPLIVAGGINSHAAVRDALAAGANAVQVGT 248
Cdd:PRK04169 183 DITPLIYGGGIRSPEQARELMAAGADTIVVGN 214
 
Name Accession Description Interval E-value
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
 30-381 4.39e-57

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


Pssm-ID: 441673 [Multi-domain]  Cd Length: 302  Bit Score: 188.78  E-value: 4.39e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981685239  30 SAHRLAGSVAREGALGTIASIdlrhhhadllercraqpvratleAANLDALAREIRLAKtySDGRGMIAVNVM--KAVSA 107
Cdd:COG2070   16 STPELAAAVSNAGGLGSIAAG-----------------------NLTPEALREEIRKIR--ELTDGPFGVNLIvhPANPR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981685239 108 HADYVRVACEHGADAIVMGAGLPLDLPDLTHGHDIALIPILSDSRGialvLKKWMKKGrlPDAIVIEHPaHAGGHLGVTQ 187
Cdd:COG2070   71 FEELLEVVLEEGVPVVSTSAGLPADLIERLKEAGIKVIPIVTSVRE----ARKAEKAG--ADAVVAEGA-EAGGHRGADE 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981685239 188 LDDMhdprfdfARVldesAQVIASLglareRIPLIVAGGINSHAAVRDALAAGANAVQVGTPFAVTEEGDAHPNFKRVLA 267
Cdd:COG2070  144 VSTF-------ALV----PEVRDAV-----DIPVIAAGGIADGRGIAAALALGADGVQMGTRFLATEESPAHEAYKQALV 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981685239 268 DAGPDDIVEFVSVTGLPARAVKTPWLDRYLRNETRirnklgalkqrcptaleclsvcglrdgiekfGHFCIDTRL----- 342
Cdd:COG2070  208 DAKEEDTVLTRSFTGRPARALRNSFTREGLDLEAE-------------------------------CLYPILEALtagkr 256

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 981685239 343 --AAALRGDVANGLFFRGrEALPFGRAIRSVRDLLDLLLTG 381
Cdd:COG2070  257 lrAAAAEGDLEKGLLWAG-QGAGLIRDILPAAELVARLVAE 296
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
 30-288 1.14e-42

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: 149.17  E-value: 1.14e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981685239  30 SAHRLAGSVAREGALGTIASIdlrhhhadllercraqpvratleAANLDALAREIRLAKTYSDGRgmIAVNVMKAVSA-- 107
Cdd:cd04730   14 STPELAAAVSNAGGLGFIGAG-----------------------YLTPEALRAEIRKIRALTDKP--FGVNLLVPSSNpd 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981685239 108 HADYVRVACEHGADAIVMGAGLPLDLPDLTHGHDIALIPILSDSRgialVLKKWMKKGrlPDAIVIEHPaHAGGHLGVTQ 187
Cdd:cd04730   69 FEALLEVALEEGVPVVSFSFGPPAEVVERLKAAGIKVIPTVTSVE----EARKAEAAG--ADALVAQGA-EAGGHRGTFD 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981685239 188 LDDMhdprfdfARVldesAQVIASLGlarerIPLIVAGGINSHAAVRDALAAGANAVQVGTPFAVTEEGDAHPNFKRVLA 267
Cdd:cd04730  142 IGTF-------ALV----PEVRDAVD-----IPVIAAGGIADGRGIAAALALGADGVQMGTRFLATEESGASPAYKQALL 205

                        250       260
                 ....*....|....*....|.
gi 981685239 268 DAGPDDIVEFVSVTGLPARAV 288
Cdd:cd04730  206 AATAEDTVLTRAFSGRPARGL 226
NMO pfam03060
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ...
 33-301 4.97e-23

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: 98.74  E-value: 4.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981685239   33 RLAGSVAREGALGTIASidlRHHHADLLERCRAQPVRAT---LEAANLDALAREIRLAKTYSDGRGMIAVNVM--KAVSA 107
Cdd:pfam03060  26 RLAAAVSNAGGLGVLAS---GYLTPDRLYQEIRKVKALTdkpFGANLFLPKPDLADPAANYAKILGNNALGYNieEGVPD 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981685239  108 HADYVRVACEhGADAIVMGAGLPL-DLPDLTHGHDIALIPILSDSRGIALVLKKWmkkgrlPDAIVIEHPAhAGGHLGVt 186
Cdd:pfam03060 103 YGKVLVDLDE-GVNVVSFGFGLPPnDVVFRLHFAGVALIPTISSAKEARIAEARG------ADALIVQGPE-AGGHQGT- 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981685239  187 qlddmhdprfdFARVLDESAQVIASLGLARErIPLIVAGGINSHAAVRDALAAGANAVQVGTPFAVTEEGDAHPNFKRVL 266
Cdd:pfam03060 174 -----------PEYGDKGLFRLVPQVPDAVD-IPVIAAGGIWDRRGVAAALALGASGVQMGTRFLLTKESGAHDAHKQKI 241

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 981685239  267 ADAGPDDIVEFVSVTGLPARAVKTPWLDRYLRNET 301
Cdd:pfam03060 242 TEAGEDDTLVTSPFSGRPARALANGFLEELEEPKI 276
DHOD_DHPD_FMN cd02810
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ...
 76-248 7.14e-06

Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass its homodimeric interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.


Pssm-ID: 239204 [Multi-domain]  Cd Length: 289  Bit Score: 47.35  E-value: 7.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981685239  76 NLDALAREIRLAKTYSDGRGMIAVNVMKAVSAHADYVRVACEHGADAIVMGAGLPLDLPDLTHGHDIALIPILSD----S 151
Cdd:cd02810   81 GLDVWLQDIAKAKKEFPGQPLIASVGGSSKEDYVELARKIERAGAKALELNLSCPNVGGGRQLGQDPEAVANLLKavkaA 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981685239 152 RGIALvlkkWMKKGRLPDAIVIEHPAHAGGHLGVTQL---DDMHDPRFDFARV----------------LDESAQVIASL 212
Cdd:cd02810  161 VDIPL----LVKLSPYFDLEDIVELAKAAERAGADGLtaiNTISGRVVDLKTVgpgpkrgtgglsgapiRPLALRWVARL 236

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 981685239 213 GLARE-RIPLIVAGGINSHAAVRDALAAGANAVQVGT 248
Cdd:cd02810  237 AARLQlDIPIIGVGGIDSGEDVLEMLMAGASAVQVAT 273
PcrB COG1646
Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];
217-258 6.59e-05

Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];


Pssm-ID: 441252  Cd Length: 241  Bit Score: 44.00  E-value: 6.59e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 981685239 217 ERIPLIVAGGINSHAAVRDALAAGANAVQVGTpfAVTEEGDA 258
Cdd:COG1646  195 EDTPLIYGGGIRSPEKAREMAEAGADTIVVGN--AIEEDPDL 234
OYE_like_4_FMN cd04735
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ...
 218-284 1.14e-04

Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 240086 [Multi-domain]  Cd Length: 353  Bit Score: 43.74  E-value: 1.14e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 981685239 218 RIPLIVAGGINSHAAVRDALAAGANAVQVGTPFAVteegdaHPNFKRVLADAGPDDIVEFVSVTGLP 284
Cdd:cd04735  284 RLPLIAVGSINTPDDALEALETGADLVAIGRGLLV------DPDWVEKIKEGREDEINLEIDPDDLE 344
IMPDH cd00381
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ...
 215-255 3.38e-04

IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.


Pssm-ID: 238223 [Multi-domain]  Cd Length: 325  Bit Score: 42.12  E-value: 3.38e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 981685239 215 ARER-IPLIVAGGINSHAAVRDALAAGANAVQVGTPFAVTEE 255
Cdd:cd00381  193 ARDYgVPVIADGGIRTSGDIVKALAAGADAVMLGSLLAGTDE 234
PRK04169 PRK04169
heptaprenylglyceryl phosphate synthase;
217-248 4.64e-04

heptaprenylglyceryl phosphate synthase;


Pssm-ID: 235237  Cd Length: 232  Bit Score: 41.33  E-value: 4.64e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 981685239 217 ERIPLIVAGGINSHAAVRDALAAGANAVQVGT 248
Cdd:PRK04169 183 DITPLIYGGGIRSPEQARELMAAGADTIVVGN 214
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 218-254 1.02e-03

Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate dehydrogenase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 439937 [Multi-domain]  Cd Length: 296  Bit Score: 40.83  E-value: 1.02e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 981685239 218 RIPLIVAGGINSHAAVRDALAAGANAVQVGT------PFAVTE 254
Cdd:COG0167  236 DIPIIGVGGISTAEDALEFILAGASAVQVGTalfyegPGLVRR 278
DHOD_1B_like cd04740
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ...
 219-278 1.17e-03

Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively.


Pssm-ID: 240091 [Multi-domain]  Cd Length: 296  Bit Score: 40.61  E-value: 1.17e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 981685239 219 IPLIVAGGINSHAAVRDALAAGANAVQVGT-----PFAVTEEGDahpNFKRVLADAGPDDIVEFV 278
Cdd:cd04740  232 IPIIGVGGIASGEDALEFLMAGASAVQVGTanfvdPEAFKEIIE---GLEAYLDEEGIKSIEELV 293
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 200-248 1.36e-03

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: 39.49  E-value: 1.36e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 981685239 200 RVLDESAQVIASLGLARERIPLIVAGGINSHAAVRDALAAGANAVQVGT 248
Cdd:cd04722  152 RDAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
 218-253 1.65e-03

N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.


Pssm-ID: 240080 [Multi-domain]  Cd Length: 219  Bit Score: 39.48  E-value: 1.65e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 981685239 218 RIPLIVAGGINSHAAVRDALAAGANAVQVGTpfAVT 253
Cdd:cd04729  177 GIPVIAEGRINSPEQAAKALELGADAVVVGS--AIT 210
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 215-255 1.65e-03

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 40.34  E-value: 1.65e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 981685239 215 ARER-IPLIVAGGINSHAAVRDALAAGANAVQVGTPFAVTEE 255
Cdd:PTZ00314 340 ARERgVPCIADGGIKNSGDICKALALGADCVMLGSLLAGTEE 381
PRK05286 PRK05286
quinone-dependent dihydroorotate dehydrogenase;
201-250 3.81e-03

quinone-dependent dihydroorotate dehydrogenase;


Pssm-ID: 235388  Cd Length: 344  Bit Score: 38.99  E-value: 3.81e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 981685239 201 VLDESAQVIASL-GLARERIPLIVAGGINSHAAVRDALAAGANAVQVGTPF 250
Cdd:PRK05286 271 LFERSTEVIRRLyKELGGRLPIIGVGGIDSAEDAYEKIRAGASLVQIYSGL 321
PRK07259 PRK07259
dihydroorotate dehydrogenase;
218-248 6.10e-03

dihydroorotate dehydrogenase;


Pssm-ID: 235982  Cd Length: 301  Bit Score: 38.21  E-value: 6.10e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 981685239 218 RIPLIVAGGINShaaVRDAL---AAGANAVQVGT 248
Cdd:PRK07259 234 DIPIIGMGGISS---AEDAIefiMAGASAVQVGT 264
PLN02826 PLN02826
dihydroorotate dehydrogenase
 214-278 8.38e-03

dihydroorotate dehydrogenase


Pssm-ID: 178421  Cd Length: 409  Bit Score: 38.18  E-value: 8.38e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 981685239 214 LARERIPLIVAGGINSHAAVRDALAAGANAVQVGTPFAvtEEGDAH-PNFKRVLADAGPDDIVEFV 278
Cdd:PLN02826 337 LTRGKIPLVGCGGVSSGEDAYKKIRAGASLVQLYTAFA--YEGPALiPRIKAELAACLERDGFKSI 400
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
219-253 9.06e-03

putative N-acetylmannosamine-6-phosphate 2-epimerase;


Pssm-ID: 234907  Cd Length: 221  Bit Score: 37.43  E-value: 9.06e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 981685239 219 IPLIVAGGINSHAAVRDALAAGANAVQVGTpfAVT 253
Cdd:PRK01130 174 CPVIAEGRINTPEQAKKALELGAHAVVVGG--AIT 206
 
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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