|
Name |
Accession |
Description |
Interval |
E-value |
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
9-350 |
9.92e-92 |
|
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];
Pssm-ID: 441673 [Multi-domain] Cd Length: 302 Bit Score: 276.22 E-value: 9.92e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 9 LGIQQPIIQAPMLGVSTPALAAAVSNAGGLGSIAITGSAAEKGRALIREVRGLTDKPFNVNLFCHRPGqadparerawld 88
Cdd:COG2070 1 LGIRYPIIQGPMAGVSTPELAAAVSNAGGLGSIAAGNLTPEALREEIRKIRELTDGPFGVNLIVHPAN------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 89 ylkPLFAEfgaeppvrlkniylsfledptLLPMLLEERPAAVSFHFGAPpRDQVRALQAVGIRVLVCATTPEEAALVEAA 168
Cdd:COG2070 69 ---PRFEE---------------------LLEVVLEEGVPVVSTSAGLP-ADLIERLKEAGIKVIPIVTSVREARKAEKA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 169 GADAVVAQGIEAGGHRGVFEpergdaaIGTLALVRLLAARGSLPVVAAGGIMDGRGIRAALELGASAVQMGTAFVLCPES 248
Cdd:COG2070 124 GADAVVAEGAEAGGHRGADE-------VSTFALVPEVRDAVDIPVIAAGGIADGRGIAAALALGADGVQMGTRFLATEES 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 249 SANAAYREALKGPRAARTALTVTMSGRSARGLPNRMFFDAAAPGVPPLPDYPFVYDATKALQtAALARGNHDFAAQWAGQ 328
Cdd:COG2070 197 PAHEAYKQALVDAKEEDTVLTRSFTGRPARALRNSFTREGLDLEAECLYPILEALTAGKRLR-AAAAEGDLEKGLLWAGQ 275
|
330 340
....*....|....*....|...
gi 15599397 329 GAALARE-LPAAELLRTLVEELR 350
Cdd:COG2070 276 GAGLIRDiLPAAELVARLVAEAE 298
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
11-280 |
2.05e-84 |
|
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: 255.49 E-value: 2.05e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 11 IQQPIIQAPMLGVSTPALAAAVSNAGGLGSIAITGSAAEKGRALIREVRGLTDKPFNVNLFCHRPGQADPArerawldyl 90
Cdd:cd04730 1 IRYPIIQAPMAGVSTPELAAAVSNAGGLGFIGAGYLTPEALRAEIRKIRALTDKPFGVNLLVPSSNPDFEA--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 91 kplfaefgaeppvrlkniylsfledptLLPMLLEERPAAVSFHFGaPPRDQVRALQAVGIRVLVCATTPEEAALVEAAGA 170
Cdd:cd04730 72 ---------------------------LLEVALEEGVPVVSFSFG-PPAEVVERLKAAGIKVIPTVTSVEEARKAEAAGA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 171 DAVVAQGIEAGGHRGVFEpergdaaIGTLALVRLLAARGSLPVVAAGGIMDGRGIRAALELGASAVQMGTAFVLCPESSA 250
Cdd:cd04730 124 DALVAQGAEAGGHRGTFD-------IGTFALVPEVRDAVDIPVIAAGGIADGRGIAAALALGADGVQMGTRFLATEESGA 196
|
250 260 270
....*....|....*....|....*....|
gi 15599397 251 NAAYREALKGPRAARTALTVTMSGRSARGL 280
Cdd:cd04730 197 SPAYKQALLAATAEDTVLTRAFSGRPARGL 226
|
|
| NMO |
pfam03060 |
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ... |
4-348 |
2.36e-75 |
|
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: 235.49 E-value: 2.36e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 4 RFTRLLGIQQPIIQAPMLGVSTPALAAAVSNAGGLGSIAITGSAAEKGRALIREVRGLTDKPFNVNLFCHRPGQADPARE 83
Cdd:pfam03060 3 LLTDIHTIKPPVQQPMMGGISWPRLAAAVSNAGGLGVLASGYLTPDRLYQEIRKVKALTDKPFGANLFLPKPDLADPAAN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 84 raWLDYLKPLFAEFGAEPPVRlkniylsfleDPTLLPMLLEERPAAVSFHFGAPPRDQVRALQAVGIRVLVCATTPEEAA 163
Cdd:pfam03060 83 --YAKILGNNALGYNIEEGVP----------DYGKVLVDLDEGVNVVSFGFGLPPNDVVFRLHFAGVALIPTISSAKEAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 164 LVEAAGADAVVAQGIEAGGHRGVFEPErgdaAIGTLALVRLLAARGSLPVVAAGGIMDGRGIRAALELGASAVQMGTAFV 243
Cdd:pfam03060 151 IAEARGADALIVQGPEAGGHQGTPEYG----DKGLFRLVPQVPDAVDIPVIAAGGIWDRRGVAAALALGASGVQMGTRFL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 244 LCPESSANAAYREALKGPRAARTALTVTMSGRSARGLPNRMFFDAAAPGVPPLPdYPFVYDATKALQTAALARGNHD-FA 322
Cdd:pfam03060 227 LTKESGAHDAHKQKITEAGEDDTLVTSPFSGRPARALANGFLEELEEPKIATLA-YPEAHEMTKPIRAAAVRGGNREeGL 305
|
330 340
....*....|....*....|....*.
gi 15599397 323 AQWAGQGAALARELPAAELLRTLVEE 348
Cdd:pfam03060 306 LWAGQGIYRLDRIISVKELIESLTEE 331
|
|
| PRK07695 |
PRK07695 |
thiazole tautomerase TenI; |
158-260 |
2.34e-05 |
|
thiazole tautomerase TenI;
Pssm-ID: 181086 [Multi-domain] Cd Length: 201 Bit Score: 44.63 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 158 TPEEAALVEAAGADAVVAqgieagGHrgVFE-------PERGdaaigtLALVRLLAARGSLPVVAAGGIMDGRgIRAALE 230
Cdd:PRK07695 104 SLEEAIQAEKNGADYVVY------GH--VFPtdckkgvPARG------LEELSDIARALSIPVIAIGGITPEN-TRDVLA 168
|
90 100 110
....*....|....*....|....*....|..
gi 15599397 231 LGAS--AVQMGTAFVLCPESSAnAAYREALKG 260
Cdd:PRK07695 169 AGVSgiAVMSGIFSSANPYSKA-KRYAESIKK 199
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
9-350 |
9.92e-92 |
|
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];
Pssm-ID: 441673 [Multi-domain] Cd Length: 302 Bit Score: 276.22 E-value: 9.92e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 9 LGIQQPIIQAPMLGVSTPALAAAVSNAGGLGSIAITGSAAEKGRALIREVRGLTDKPFNVNLFCHRPGqadparerawld 88
Cdd:COG2070 1 LGIRYPIIQGPMAGVSTPELAAAVSNAGGLGSIAAGNLTPEALREEIRKIRELTDGPFGVNLIVHPAN------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 89 ylkPLFAEfgaeppvrlkniylsfledptLLPMLLEERPAAVSFHFGAPpRDQVRALQAVGIRVLVCATTPEEAALVEAA 168
Cdd:COG2070 69 ---PRFEE---------------------LLEVVLEEGVPVVSTSAGLP-ADLIERLKEAGIKVIPIVTSVREARKAEKA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 169 GADAVVAQGIEAGGHRGVFEpergdaaIGTLALVRLLAARGSLPVVAAGGIMDGRGIRAALELGASAVQMGTAFVLCPES 248
Cdd:COG2070 124 GADAVVAEGAEAGGHRGADE-------VSTFALVPEVRDAVDIPVIAAGGIADGRGIAAALALGADGVQMGTRFLATEES 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 249 SANAAYREALKGPRAARTALTVTMSGRSARGLPNRMFFDAAAPGVPPLPDYPFVYDATKALQtAALARGNHDFAAQWAGQ 328
Cdd:COG2070 197 PAHEAYKQALVDAKEEDTVLTRSFTGRPARALRNSFTREGLDLEAECLYPILEALTAGKRLR-AAAAEGDLEKGLLWAGQ 275
|
330 340
....*....|....*....|...
gi 15599397 329 GAALARE-LPAAELLRTLVEELR 350
Cdd:COG2070 276 GAGLIRDiLPAAELVARLVAEAE 298
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
11-280 |
2.05e-84 |
|
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: 255.49 E-value: 2.05e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 11 IQQPIIQAPMLGVSTPALAAAVSNAGGLGSIAITGSAAEKGRALIREVRGLTDKPFNVNLFCHRPGQADPArerawldyl 90
Cdd:cd04730 1 IRYPIIQAPMAGVSTPELAAAVSNAGGLGFIGAGYLTPEALRAEIRKIRALTDKPFGVNLLVPSSNPDFEA--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 91 kplfaefgaeppvrlkniylsfledptLLPMLLEERPAAVSFHFGaPPRDQVRALQAVGIRVLVCATTPEEAALVEAAGA 170
Cdd:cd04730 72 ---------------------------LLEVALEEGVPVVSFSFG-PPAEVVERLKAAGIKVIPTVTSVEEARKAEAAGA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 171 DAVVAQGIEAGGHRGVFEpergdaaIGTLALVRLLAARGSLPVVAAGGIMDGRGIRAALELGASAVQMGTAFVLCPESSA 250
Cdd:cd04730 124 DALVAQGAEAGGHRGTFD-------IGTFALVPEVRDAVDIPVIAAGGIADGRGIAAALALGADGVQMGTRFLATEESGA 196
|
250 260 270
....*....|....*....|....*....|
gi 15599397 251 NAAYREALKGPRAARTALTVTMSGRSARGL 280
Cdd:cd04730 197 SPAYKQALLAATAEDTVLTRAFSGRPARGL 226
|
|
| NMO |
pfam03060 |
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ... |
4-348 |
2.36e-75 |
|
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: 235.49 E-value: 2.36e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 4 RFTRLLGIQQPIIQAPMLGVSTPALAAAVSNAGGLGSIAITGSAAEKGRALIREVRGLTDKPFNVNLFCHRPGQADPARE 83
Cdd:pfam03060 3 LLTDIHTIKPPVQQPMMGGISWPRLAAAVSNAGGLGVLASGYLTPDRLYQEIRKVKALTDKPFGANLFLPKPDLADPAAN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 84 raWLDYLKPLFAEFGAEPPVRlkniylsfleDPTLLPMLLEERPAAVSFHFGAPPRDQVRALQAVGIRVLVCATTPEEAA 163
Cdd:pfam03060 83 --YAKILGNNALGYNIEEGVP----------DYGKVLVDLDEGVNVVSFGFGLPPNDVVFRLHFAGVALIPTISSAKEAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 164 LVEAAGADAVVAQGIEAGGHRGVFEPErgdaAIGTLALVRLLAARGSLPVVAAGGIMDGRGIRAALELGASAVQMGTAFV 243
Cdd:pfam03060 151 IAEARGADALIVQGPEAGGHQGTPEYG----DKGLFRLVPQVPDAVDIPVIAAGGIWDRRGVAAALALGASGVQMGTRFL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 244 LCPESSANAAYREALKGPRAARTALTVTMSGRSARGLPNRMFFDAAAPGVPPLPdYPFVYDATKALQTAALARGNHD-FA 322
Cdd:pfam03060 227 LTKESGAHDAHKQKITEAGEDDTLVTSPFSGRPARALANGFLEELEEPKIATLA-YPEAHEMTKPIRAAAVRGGNREeGL 305
|
330 340
....*....|....*....|....*.
gi 15599397 323 AQWAGQGAALARELPAAELLRTLVEE 348
Cdd:pfam03060 306 LWAGQGIYRLDRIISVKELIESLTEE 331
|
|
| NPD_PKS |
cd04743 |
2-Nitropropane dioxygenase (NPD)-like domain, associated with polyketide synthases (PKS). NPD ... |
14-278 |
3.07e-10 |
|
2-Nitropropane dioxygenase (NPD)-like domain, associated with polyketide synthases (PKS). NPD is part of the nitroalkaneoxidizing enzyme family, that catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDPs are members 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: 240094 Cd Length: 320 Bit Score: 60.60 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 14 PIIQAPMLGVS-TPALAAAVSNAGGLGSIAITGSAAEKGRALIREVRG-LTDKPFNVNLFCHRPgQADPARERAWLDYLK 91
Cdd:cd04743 4 PIVQGPMTRVSdVAEFAVAVAEGGGLPFIALALMRGEQVKALLEETAElLGDKPWGVGILGFVD-TELRAAQLAVVRAIK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 92 PLFAefgaeppvrlkniylsfledptllpMLLEERPaavsfhfgapprDQVRALQAVGIRVLVCATTPEEAALVEAAGAD 171
Cdd:cd04743 83 PTFA-------------------------LIAGGRP------------DQARALEAIGISTYLHVPSPGLLKQFLENGAR 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 172 AVVAQGIEAGGHRGvfepERGDAAIGTLALVRLLA-----ARGSLPVVAAGGIMDGRGIRAALELGAS--------AVQM 238
Cdd:cd04743 126 KFIFEGRECGGHVG----PRSSFVLWESAIDALLAangpdKAGKIHLLFAGGIHDERSAAMVSALAAPlaergakvGVLM 201
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 15599397 239 GTAFVLCPESSANAAY-----REALKgprAARTALTVTMSGRSAR 278
Cdd:cd04743 202 GTAYLFTEEAVSAGAIlptfqDQAIA---ATRTALLETGPGHATR 243
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
162-243 |
9.16e-09 |
|
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: 55.85 E-value: 9.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 162 AALVEAAGADAVVA----QGIEAGGHRGvfEPERGDAAIG---------TLALVRLLAAR--GSLPVVAAGGIMDGRGIR 226
Cdd:COG0167 175 ARAAEEAGADGVIAinttLGRAIDLETR--RPVLANEAGGlsgpalkpiALRMVREVAQAvgGDIPIIGVGGISTAEDAL 252
|
90
....*....|....*..
gi 15599397 227 AALELGASAVQMGTAFV 243
Cdd:COG0167 253 EFILAGASAVQVGTALF 269
|
|
| PRK07695 |
PRK07695 |
thiazole tautomerase TenI; |
158-260 |
2.34e-05 |
|
thiazole tautomerase TenI;
Pssm-ID: 181086 [Multi-domain] Cd Length: 201 Bit Score: 44.63 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 158 TPEEAALVEAAGADAVVAqgieagGHrgVFE-------PERGdaaigtLALVRLLAARGSLPVVAAGGIMDGRgIRAALE 230
Cdd:PRK07695 104 SLEEAIQAEKNGADYVVY------GH--VFPtdckkgvPARG------LEELSDIARALSIPVIAIGGITPEN-TRDVLA 168
|
90 100 110
....*....|....*....|....*....|..
gi 15599397 231 LGAS--AVQMGTAFVLCPESSAnAAYREALKG 260
Cdd:PRK07695 169 AGVSgiAVMSGIFSSANPYSKA-KRYAESIKK 199
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
15-240 |
4.23e-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: 44.11 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 15 IIQAPMLGVSTPALAAAVSNAGGLGSIAI--------TGSAAEKGRALIREVRGLTDKPFNVNLFCHRPGQADP----AR 82
Cdd:cd04722 1 VILALLAGGPSGDPVELAKAAAEAGADAIivgtrssdPEEAETDDKEVLKEVAAETDLPLGVQLAINDAAAAVDiaaaAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 83 ERAWLDYLkplfaEFGAEPPVRlkniylsfledptllpmlleerpaavsFHFGAPPRDQVR-ALQAVGIRVLVCATTPEE 161
Cdd:cd04722 81 RAAGADGV-----EIHGAVGYL---------------------------AREDLELIRELReAVPDVKVVVKLSPTGELA 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599397 162 AALVEAAGADAVVAQGIEAGGHRGvfepergDAAIGTLALVRLLAARGSLPVVAAGGIMDGRGIRAALELGASAVQMGT 240
Cdd:cd04722 129 AAAAEEAGVDEVGLGNGGGGGGGR-------DAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
41-242 |
4.83e-05 |
|
Dihydroorotate dehydrogenase (DHOD) class 1A 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: 240092 Cd Length: 294 Bit Score: 44.62 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 41 IAITGSAAEKGRALIREVRglTDKPFN----VNLFC-HRPGQADPARERAWLD-YLKPLFAEFGaePPVRLKniyLSFLE 114
Cdd:cd04741 96 ISVTGSAEDIAAMYKKIAA--HQKQFPlameLNLSCpNVPGKPPPAYDFDATLeYLTAVKAAYS--IPVGVK---TPPYT 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 115 DPTLLPML---LEERPAAVSFhfgapprdqVRALQAVGiRVLVCATTPEEAALVeaagadavVAQGIeaGGHRGvfeper 191
Cdd:cd04741 169 DPAQFDTLaeaLNAFACPISF---------ITATNTLG-NGLVLDPERETVVLK--------PKTGF--GGLAG------ 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15599397 192 gdAAIGTLALVRLLAARGSLP----VVAAGGIMDGRGIRAALELGASAVQMGTAF 242
Cdd:cd04741 223 --AYLHPLALGNVRTFRRLLPseiqIIGVGGVLDGRGAFRMRLAGASAVQVGTAL 275
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
6-243 |
6.35e-05 |
|
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only]; FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440915 [Multi-domain] Cd Length: 357 Bit Score: 44.35 E-value: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 6 TRLLG--IQQPIIQAPMlGVSTP-------ALAAAVSNAG---GLGSIAITGsaaekgralIREVRGLTDKPFNVNLFCH 73
Cdd:COG1304 63 TTLLGkrLAAPFLIAPM-GGGGLahpdgelALARAAAAAGipmGLSTQSTTS---------LEEVAAAAPAPLWFQLYVP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 74 R-PGQADPARERAWLdylkplfAEFGA--------EPPVRLKNIYLSFLEDPTLLPMLLEERPAAVSFHFGAPPRDQVRA 144
Cdd:COG1304 133 KdRGFTDDLLRRAEA-------AGADAlvltvdtpVLGRRERDLREGFSQPPRLTPRNLLEAATHPRWALGLASLAAWLD 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 145 LQAVG------IRVLVCAT----------TPEEAALVEAAGADAVVAQGieAGGhRGVfepergDAAIGTL-ALVRLLAA 207
Cdd:COG1304 206 TNFDPsltwddIAWLRERWpgplivkgvlSPEDARRAVDAGVDGIDVSN--HGG-RQL------DGGPPTIdALPEIRAA 276
|
250 260 270
....*....|....*....|....*....|....*..
gi 15599397 208 RGS-LPVVAAGGIMDGRGIRAALELGASAVQMGTAFV 243
Cdd:COG1304 277 VGGrIPVIADGGIRRGLDVAKALALGADAVGLGRPFL 313
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
162-243 |
1.31e-04 |
|
Dihydroorotate dehydrogenase (DHOD) class 2. 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, their cellular location and their natural electron acceptor used to reoxidize the flavin group. Members of class 1 are cytosolic enzymes and multimers, while class 2 enzymes are membrane associated, monomeric and use respiratory quinones as their physiological electron acceptors.
Pssm-ID: 240089 Cd Length: 327 Bit Score: 43.26 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 162 AALVEAAGADAVVA--------------QGIEAGGHRG--VFEPergdaaigTLALVRLLAAR--GSLPVVAAGGIMDGR 223
Cdd:cd04738 222 ADVALEHGVDGIIAtnttisrpgllrspLANETGGLSGapLKER--------STEVLRELYKLtgGKIPIIGVGGISSGE 293
|
90 100
....*....|....*....|
gi 15599397 224 GIRAALELGASAVQMGTAFV 243
Cdd:cd04738 294 DAYEKIRAGASLVQLYTGLV 313
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
162-243 |
1.61e-04 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 43.23 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 162 AALVEAAGADAVVA--------------QGIEAGG--HRGVFEPergdaaigTLALVRLLAAR--GSLPVVAAGGIMDGR 223
Cdd:PRK05286 231 ADLALEHGIDGVIAtnttlsrdglkglpNADEAGGlsGRPLFER--------STEVIRRLYKElgGRLPIIGVGGIDSAE 302
|
90 100
....*....|....*....|
gi 15599397 224 GIRAALELGASAVQMGTAFV 243
Cdd:PRK05286 303 DAYEKIRAGASLVQIYSGLI 322
|
|
| TMP-TENI |
pfam02581 |
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ... |
138-242 |
5.77e-04 |
|
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl)thiazole phosphate to yield thiamine phosphate. This Pfam family also includes the regulatory protein TENI, a protein from Bacillus subtilis that regulates the production of several extracellular enzymes by reducing alkaline protease production. While TenI shows high sequence similarity with thiamin phosphate synthase, the purified protein has no thiamin phosphate synthase activity. Instead, it is a thiazole tautomerase.
Pssm-ID: 426849 [Multi-domain] Cd Length: 180 Bit Score: 40.22 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 138 PRDQVRALQAVGIRVLVCATTPEEAALVEAAGADAVVAqgieagGHrgVFE-PERGDAAIGTLALVRLLAARGSLPVVAA 216
Cdd:pfam02581 84 PVAEARELLGPDLIIGVSTHTLEEALEAEALGADYIGF------GP--IFPtPTKPDAPPLGLEGLKAIAEAVEIPVVAI 155
|
90 100
....*....|....*....|....*.
gi 15599397 217 GGIMDGRgIRAALELGASAVQMGTAF 242
Cdd:pfam02581 156 GGITPEN-VPEVIEAGADGVAVVSAI 180
|
|
| PRK04302 |
PRK04302 |
triosephosphate isomerase; Provisional |
142-243 |
7.96e-04 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 235274 Cd Length: 223 Bit Score: 40.24 E-value: 7.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 142 VRALQAVGIRVLVCATTPEEAALVEAAGADAVVaqgIEA----GGHRGV--FEPERgdaAIGTLALVRllAARGSLPVVA 215
Cdd:PRK04302 107 VERAKKLGLESVVCVNNPETSAAAAALGPDYVA---VEPpeliGTGIPVskAKPEV---VEDAVEAVK--KVNPDVKVLC 178
|
90 100
....*....|....*....|....*...
gi 15599397 216 AGGIMDGRGIRAALELGASAVQMGTAFV 243
Cdd:PRK04302 179 GAGISTGEDVKAALELGADGVLLASGVV 206
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
162-242 |
1.63e-03 |
|
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: 39.64 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 162 AALVEAAGADAVVA--------------QGIEAGGHRGVfeperGDAAIGTLAL--VRLLAAR--GSLPVVAAGGIMDGR 223
Cdd:cd02810 182 AKAAERAGADGLTAintisgrvvdlktvGPGPKRGTGGL-----SGAPIRPLALrwVARLAARlqLDIPIIGVGGIDSGE 256
|
90
....*....|....*....
gi 15599397 224 GIRAALELGASAVQMGTAF 242
Cdd:cd02810 257 DVLEMLMAGASAVQVATAL 275
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
160-249 |
1.73e-03 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 39.75 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 160 EEAALVEAAGADAVVA----QG----IEAG----GHR--GVFEPergdaAIGTLAL--VRLLAARGSLPVVAAGGIMDGR 223
Cdd:PRK07259 173 EIAKAAEEAGADGLSLintlKGmaidIKTRkpilANVtgGLSGP-----AIKPIALrmVYQVYQAVDIPIIGMGGISSAE 247
|
90 100
....*....|....*....|....*....
gi 15599397 224 girAALEL---GASAVQMGTAFVLCPESS 249
Cdd:PRK07259 248 ---DAIEFimaGASAVQVGTANFYDPYAF 273
|
|
| ThiE |
COG0352 |
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
138-260 |
2.19e-03 |
|
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate synthase is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 440121 [Multi-domain] Cd Length: 206 Bit Score: 38.63 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 138 PRDQVRALQAVGIRVLVCATTPEEAALVEAAGADAVVAqgieagGHrgVFE----PERGDAAigTLALVRLLAARGSLPV 213
Cdd:COG0352 89 PVAEARALLGPDLIIGVSCHSLEEALRAEEAGADYVGF------GP--VFPtptkPGAPPPL--GLEGLAWWAELVEIPV 158
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 15599397 214 VAAGGIMDGRgIRAALELGASAVQMGTAFVLCPESSANA-AYREALKG 260
Cdd:COG0352 159 VAIGGITPEN-AAEVLAAGADGVAVISAIWGAPDPAAAArELRAALEA 205
|
|
| PRK11840 |
PRK11840 |
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional |
144-291 |
2.20e-03 |
|
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional
Pssm-ID: 236998 [Multi-domain] Cd Length: 326 Bit Score: 39.35 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 144 ALQAVGIRVLV-CATTPEEAALVEAAGADAVVAQGIEAGGHRGVFEPergdaaigtlALVRLLAARGSLPVVAAGGIMDG 222
Cdd:PRK11840 192 ILVKEGFQVMVyCSDDPIAAKRLEDAGAVAVMPLGAPIGSGLGIQNP----------YTIRLIVEGATVPVLVDAGVGTA 261
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599397 223 RGIRAALELGASAVQMGTAFVlcpessanaayrEALKGPRAARTALTVTMSGRSAR---GLPNRMFFDAAAP 291
Cdd:PRK11840 262 SDAAVAMELGCDGVLMNTAIA------------EAKNPVLMARAMKLAVEAGRLAYlagRMPRRRYADPSSP 321
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
162-241 |
6.10e-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: 37.91 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 162 AALVEAAGADAVVA--------------QGIEAGGHRGVFEPergdaAIGTLAL--VRLLAARGSLPVVAAGGIMDGRgi 225
Cdd:cd04740 172 ARAAEEAGADGLTLintlkgmaidietrKPILGNVTGGLSGP-----AIKPIALrmVYQVYKAVEIPIIGVGGIASGE-- 244
|
90
....*....|....*....
gi 15599397 226 rAALEL---GASAVQMGTA 241
Cdd:cd04740 245 -DALEFlmaGASAVQVGTA 262
|
|
| PLN02274 |
PLN02274 |
inosine-5'-monophosphate dehydrogenase |
205-242 |
6.31e-03 |
|
inosine-5'-monophosphate dehydrogenase
Pssm-ID: 215154 [Multi-domain] Cd Length: 505 Bit Score: 38.50 E-value: 6.31e-03
10 20 30
....*....|....*....|....*....|....*...
gi 15599397 205 LAARGSLPVVAAGGIMDGRGIRAALELGASAVQMGTAF 242
Cdd:PLN02274 346 IAAQHGVPVIADGGISNSGHIVKALTLGASTVMMGSFL 383
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
158-248 |
7.68e-03 |
|
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: 37.88 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599397 158 TPEEAALVEAAGADAVVAqGIEAGGH---RGVfepergdAAIG-----TLALVRLLAARGSLPVVAAGGIMDGRGIRAAL 229
Cdd:cd00381 145 TAEAARDLIDAGADGVKV-GIGPGSIcttRIV-------TGVGvpqatAVADVAAAARDYGVPVIADGGIRTSGDIVKAL 216
|
90
....*....|....*....
gi 15599397 230 ELGASAVQMGTAFVLCPES 248
Cdd:cd00381 217 AAGADAVMLGSLLAGTDES 235
|
|
| |
