|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
5-341 |
0e+00 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 552.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 5 LYPLARASLFKMDAEDAHHLTLRALGAAGRTGLACALSARV----PDAPRTVMGLTFRNPVGLAAGLDKDGAAIDGLAAL 80
Cdd:PRK05286 2 YYPLARPLLFKLDPETAHELTIRALKRASRTPLLSLLRQRLtytdPRLPVTVMGLTFPNPVGLAAGFDKNGEAIDALGAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 81 GFGFIEVGTVTPRAQPGNPRPRMFRLPQAEALINRMGFNNHGVDQFVKNVQAARYRGILGLNIGKNADTPIERAAEDYLY 160
Cdd:PRK05286 82 GFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKAYRGIPLGINIGKNKDTPLEDAVDDYLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 161 CLERVYPFASYVTINISSPNTKNLRQLQGAGELDALLAALKDKQQRLAdlhgKLVPLALKIAPDLDDEQVKEIGDTLLRH 240
Cdd:PRK05286 162 CLEKLYPYADYFTVNISSPNTPGLRDLQYGEALDELLAALKEAQAELH----GYVPLLVKIAPDLSDEELDDIADLALEH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 241 KIEAVIATNTTLSRAAVQGLPHADEAGGLSGRPVFDASNEVIRKLHAEVGNDVPIIGVGGIFSGEDARAKLAAGAALVQL 320
Cdd:PRK05286 238 GIDGVIATNTTLSRDGLKGLPNADEAGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGASLVQI 317
|
330 340
....*....|....*....|.
gi 974648777 321 YTGFIYRGPALVSECVKAIAR 341
Cdd:PRK05286 318 YSGLIYEGPGLVKEIVRGLAR 338
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
10-339 |
8.82e-177 |
|
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: 492.78 E-value: 8.82e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 10 RASLFKMDAEDAHHLTLRALGAAGRTGLACALSARVPDAPRTVMGLTFRNPVGLAAGLDKDGAAIDGLAALGFGFIEVGT 89
Cdd:cd04738 1 RPLLFLLDPETAHRLAIRALKLGLGPPLLLLLVYDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFVEVGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 90 VTPRAQPGNPRPRMFRLPQAEALINRMGFNNHGVDQFVKNVQAARYR-GILGLNIGKNADTPIERAAEDYLYCLERVYPF 168
Cdd:cd04738 81 VTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRRPRgGPLGVNIGKNKDTPLEDAVEDYVIGVRKLGPY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 169 ASYVTINISSPNTKNLRQLQGAGELDALLAALKDKQQRLadlhGKLVPLALKIAPDLDDEQVKEIGDTLLRHKIEAVIAT 248
Cdd:cd04738 161 ADYLVVNVSSPNTPGLRDLQGKEALRELLTAVKEERNKL----GKKVPLLVKIAPDLSDEELEDIADVALEHGVDGIIAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 249 NTTLSRAAVQGLPHADEAGGLSGRPVFDASNEVIRKLHAEVGNDVPIIGVGGIFSGEDARAKLAAGAALVQLYTGFIYRG 328
Cdd:cd04738 237 NTTISRPGLLRSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTGLVYEG 316
|
330
....*....|.
gi 974648777 329 PALVSECVKAI 339
Cdd:cd04738 317 PGLVKRIKREL 327
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
6-339 |
9.52e-147 |
|
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate dehydrogenase exclusively for subfamily 2. It includes members from bacteria, yeast, plants etc. The subfamilies 1 and 2 share extensive homology, particularly toward the C-terminus. This subfamily has a longer N-terminal region. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273408 Cd Length: 335 Bit Score: 417.26 E-value: 9.52e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 6 YPLARASLFKMDAEDAHHLTLRALGAAGRTGLACALSARVPDA---PRTVMGLTFRNPVGLAAGLDKDGAAIDGLAALGF 82
Cdd:TIGR01036 1 YPLVRKLLFLLDPESAHELTFQFLRLGTGTPFLALLRSLFGASdplEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAMGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 83 GFIEVGTVTPRAQPGNPRPRMFRLPQAEALINRMGFNNHGVDQFVKNVQAARYRGILGLNIGKNADTPIERAAEDYLYCL 162
Cdd:TIGR01036 81 GFLEIGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLKRARYKGPIGINIGKNKDTPSEDAKEDYAACL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 163 ERVYPFASYVTINISSPNTKNLRQLQGAGELDALLAALKDKQQRLADLHGklVPLALKIAPDLDDEQVKEIGDTLLRHKI 242
Cdd:TIGR01036 161 RKLGPLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAVKQEQDGLRRVHR--VPVLVKIAPDLTESDLEDIADSLVELGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 243 EAVIATNTTLSRAAVQGLPHADEAGGLSGRPVFDASNEVIRKLHAEVGNDVPIIGVGGIFSGEDARAKLAAGAALVQLYT 322
Cdd:TIGR01036 239 DGVIATNTTVSRSLVQGPKNSDETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGASLLQIYS 318
|
330
....*....|....*..
gi 974648777 323 GFIYRGPALVSECVKAI 339
Cdd:TIGR01036 319 GFIYWGPPLVKEIVKEI 335
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
47-341 |
1.04e-110 |
|
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: 324.33 E-value: 1.04e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 47 DAPRTVMGLTFRNPVGLAAG-LDKDGAAIDGLAALGFGFIEVGTVTPRAQPGNPRPRMFRLPQAEALINRMGFNNHGVDQ 125
Cdd:COG0167 1 DLSVELAGLKFPNPVGLASGfFDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 126 FVKNVQAAR-YRGILGLNIGKNAdtpieraAEDYLYCLERVYPF-ASYVTINISSPNTKN-LRQL-QGAGELDALLAALK 201
Cdd:COG0167 81 FLERLLPAKrYDVPVIVNIGGNT-------VEDYVELARRLADAgADYLELNISCPNTPGgGRALgQDPEALAELLAAVK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 202 DKQQrladlhgklVPLALKIAPDLDDeqVKEIGDTLLRHKIEAVIATNTTLSRA--AVQGLPH-ADEAGGLSGRPVFDAS 278
Cdd:COG0167 154 AATD---------KPVLVKLAPDLTD--IVEIARAAEEAGADGVIAINTTLGRAidLETRRPVlANEAGGLSGPALKPIA 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 974648777 279 NEVIRKLHAEVGNDVPIIGVGGIFSGEDARAKLAAGAALVQLYTGFIYRGPALVSECVKAIAR 341
Cdd:COG0167 223 LRMVREVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEA 285
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
51-342 |
2.21e-86 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 262.28 E-value: 2.21e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 51 TVMGLTFRNPVGLAAGLDKDGAAIDGLAALG-FGFIEVGTVTPRAQPGNPRPRMFRLPqaEALINRMGFNNHGVD---QF 126
Cdd:pfam01180 5 KIPGLDFKNPIGLASGFDKFGEEALKWLALGkFGAIEIKSVTPYPQPGNPTPRVFRLP--EGVLNRMGLNNPGLDavlAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 127 VKNVQAARYRGILGLNIGKNADTpieraAEDYLYCLERVYPFASYVTINISSPNTKNLRQLQGAGELDALLAALKDKQQR 206
Cdd:pfam01180 83 LLKRRKEYPRPDLGINLSKAGMT-----VDDYVEVARKIGPFADYIELNVSCPNTPGLRALQTDPELAAILLKVVKEVSK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 207 ladlhgklVPLALKIAPDLDDEQVKEIGDTLLR-HKIEAVIATNTTLSRAA--VQGLPH--ADEAGGLSGRPVFDASNEV 281
Cdd:pfam01180 158 --------VPVLVKLAPDLTDIVIIDIADVALGeDGLDGINATNTTVRGMRidLKTEKPilANGTGGLSGPPIKPIALKV 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 974648777 282 IRKLHAEVGNDVPIIGVGGIFSGEDARAKLAAGAALVQLYTGFIYRGPALVSECVKAIARE 342
Cdd:pfam01180 230 IRELYQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPEL 290
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
5-341 |
0e+00 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 552.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 5 LYPLARASLFKMDAEDAHHLTLRALGAAGRTGLACALSARV----PDAPRTVMGLTFRNPVGLAAGLDKDGAAIDGLAAL 80
Cdd:PRK05286 2 YYPLARPLLFKLDPETAHELTIRALKRASRTPLLSLLRQRLtytdPRLPVTVMGLTFPNPVGLAAGFDKNGEAIDALGAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 81 GFGFIEVGTVTPRAQPGNPRPRMFRLPQAEALINRMGFNNHGVDQFVKNVQAARYRGILGLNIGKNADTPIERAAEDYLY 160
Cdd:PRK05286 82 GFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKAYRGIPLGINIGKNKDTPLEDAVDDYLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 161 CLERVYPFASYVTINISSPNTKNLRQLQGAGELDALLAALKDKQQRLAdlhgKLVPLALKIAPDLDDEQVKEIGDTLLRH 240
Cdd:PRK05286 162 CLEKLYPYADYFTVNISSPNTPGLRDLQYGEALDELLAALKEAQAELH----GYVPLLVKIAPDLSDEELDDIADLALEH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 241 KIEAVIATNTTLSRAAVQGLPHADEAGGLSGRPVFDASNEVIRKLHAEVGNDVPIIGVGGIFSGEDARAKLAAGAALVQL 320
Cdd:PRK05286 238 GIDGVIATNTTLSRDGLKGLPNADEAGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGASLVQI 317
|
330 340
....*....|....*....|.
gi 974648777 321 YTGFIYRGPALVSECVKAIAR 341
Cdd:PRK05286 318 YSGLIYEGPGLVKEIVRGLAR 338
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
10-339 |
8.82e-177 |
|
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: 492.78 E-value: 8.82e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 10 RASLFKMDAEDAHHLTLRALGAAGRTGLACALSARVPDAPRTVMGLTFRNPVGLAAGLDKDGAAIDGLAALGFGFIEVGT 89
Cdd:cd04738 1 RPLLFLLDPETAHRLAIRALKLGLGPPLLLLLVYDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFVEVGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 90 VTPRAQPGNPRPRMFRLPQAEALINRMGFNNHGVDQFVKNVQAARYR-GILGLNIGKNADTPIERAAEDYLYCLERVYPF 168
Cdd:cd04738 81 VTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRRPRgGPLGVNIGKNKDTPLEDAVEDYVIGVRKLGPY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 169 ASYVTINISSPNTKNLRQLQGAGELDALLAALKDKQQRLadlhGKLVPLALKIAPDLDDEQVKEIGDTLLRHKIEAVIAT 248
Cdd:cd04738 161 ADYLVVNVSSPNTPGLRDLQGKEALRELLTAVKEERNKL----GKKVPLLVKIAPDLSDEELEDIADVALEHGVDGIIAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 249 NTTLSRAAVQGLPHADEAGGLSGRPVFDASNEVIRKLHAEVGNDVPIIGVGGIFSGEDARAKLAAGAALVQLYTGFIYRG 328
Cdd:cd04738 237 NTTISRPGLLRSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTGLVYEG 316
|
330
....*....|.
gi 974648777 329 PALVSECVKAI 339
Cdd:cd04738 317 PGLVKRIKREL 327
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
6-339 |
9.52e-147 |
|
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate dehydrogenase exclusively for subfamily 2. It includes members from bacteria, yeast, plants etc. The subfamilies 1 and 2 share extensive homology, particularly toward the C-terminus. This subfamily has a longer N-terminal region. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273408 Cd Length: 335 Bit Score: 417.26 E-value: 9.52e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 6 YPLARASLFKMDAEDAHHLTLRALGAAGRTGLACALSARVPDA---PRTVMGLTFRNPVGLAAGLDKDGAAIDGLAALGF 82
Cdd:TIGR01036 1 YPLVRKLLFLLDPESAHELTFQFLRLGTGTPFLALLRSLFGASdplEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAMGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 83 GFIEVGTVTPRAQPGNPRPRMFRLPQAEALINRMGFNNHGVDQFVKNVQAARYRGILGLNIGKNADTPIERAAEDYLYCL 162
Cdd:TIGR01036 81 GFLEIGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLKRARYKGPIGINIGKNKDTPSEDAKEDYAACL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 163 ERVYPFASYVTINISSPNTKNLRQLQGAGELDALLAALKDKQQRLADLHGklVPLALKIAPDLDDEQVKEIGDTLLRHKI 242
Cdd:TIGR01036 161 RKLGPLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAVKQEQDGLRRVHR--VPVLVKIAPDLTESDLEDIADSLVELGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 243 EAVIATNTTLSRAAVQGLPHADEAGGLSGRPVFDASNEVIRKLHAEVGNDVPIIGVGGIFSGEDARAKLAAGAALVQLYT 322
Cdd:TIGR01036 239 DGVIATNTTVSRSLVQGPKNSDETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGASLLQIYS 318
|
330
....*....|....*..
gi 974648777 323 GFIYRGPALVSECVKAI 339
Cdd:TIGR01036 319 GFIYWGPPLVKEIVKEI 335
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
47-341 |
1.04e-110 |
|
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: 324.33 E-value: 1.04e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 47 DAPRTVMGLTFRNPVGLAAG-LDKDGAAIDGLAALGFGFIEVGTVTPRAQPGNPRPRMFRLPQAEALINRMGFNNHGVDQ 125
Cdd:COG0167 1 DLSVELAGLKFPNPVGLASGfFDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 126 FVKNVQAAR-YRGILGLNIGKNAdtpieraAEDYLYCLERVYPF-ASYVTINISSPNTKN-LRQL-QGAGELDALLAALK 201
Cdd:COG0167 81 FLERLLPAKrYDVPVIVNIGGNT-------VEDYVELARRLADAgADYLELNISCPNTPGgGRALgQDPEALAELLAAVK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 202 DKQQrladlhgklVPLALKIAPDLDDeqVKEIGDTLLRHKIEAVIATNTTLSRA--AVQGLPH-ADEAGGLSGRPVFDAS 278
Cdd:COG0167 154 AATD---------KPVLVKLAPDLTD--IVEIARAAEEAGADGVIAINTTLGRAidLETRRPVlANEAGGLSGPALKPIA 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 974648777 279 NEVIRKLHAEVGNDVPIIGVGGIFSGEDARAKLAAGAALVQLYTGFIYRGPALVSECVKAIAR 341
Cdd:COG0167 223 LRMVREVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEA 285
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
1-333 |
1.65e-105 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 315.14 E-value: 1.65e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 1 MFSSLYPLARAslfkMDAEDAHHLTLRALgaagRTGLACALSARVPDAPRT-VMGLTFRNPVGLAAGLDKDGAAIDGLAA 79
Cdd:PLN02826 34 ATKLVNPLFRL----LDPETAHSLAISAA----ARGLVPREKRPDPSVLGVeVWGRTFSNPIGLAAGFDKNAEAVEGLLG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 80 LGFGFIEVGTVTPRAQPGNPRPRMFRLPQAEALINRMGFNNHGVDQFVKNVQAAR------------------------Y 135
Cdd:PLN02826 106 LGFGFVEIGSVTPLPQPGNPKPRVFRLREEGAIINRYGFNSEGIVAVAKRLGAQHgkrkldetssssfssddvkaggkaG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 136 RGILGLNIGKNADTpiERAAEDYLYCLERVYPFASYVTINISSPNTKNLRQLQGAGELDALLAALKDKQQRLADLHGKLV 215
Cdd:PLN02826 186 PGILGVNLGKNKTS--EDAAADYVQGVRALSQYADYLVINVSSPNTPGLRKLQGRKQLKDLLKKVLAARDEMQWGEEGPP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 216 PLALKIAPDLDDEQVKEIGDTLLRHKIEAVIATNTTLSR-AAVQGLPHADEAGGLSGRPVFDASNEVIRKLHAEVGNDVP 294
Cdd:PLN02826 264 PLLVKIAPDLSKEDLEDIAAVALALGIDGLIISNTTISRpDSVLGHPHADEAGGLSGKPLFDLSTEVLREMYRLTRGKIP 343
|
330 340 350
....*....|....*....|....*....|....*....
gi 974648777 295 IIGVGGIFSGEDARAKLAAGAALVQLYTGFIYRGPALVS 333
Cdd:PLN02826 344 LVGCGGVSSGEDAYKKIRAGASLVQLYTAFAYEGPALIP 382
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
51-342 |
2.21e-86 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 262.28 E-value: 2.21e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 51 TVMGLTFRNPVGLAAGLDKDGAAIDGLAALG-FGFIEVGTVTPRAQPGNPRPRMFRLPqaEALINRMGFNNHGVD---QF 126
Cdd:pfam01180 5 KIPGLDFKNPIGLASGFDKFGEEALKWLALGkFGAIEIKSVTPYPQPGNPTPRVFRLP--EGVLNRMGLNNPGLDavlAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 127 VKNVQAARYRGILGLNIGKNADTpieraAEDYLYCLERVYPFASYVTINISSPNTKNLRQLQGAGELDALLAALKDKQQR 206
Cdd:pfam01180 83 LLKRRKEYPRPDLGINLSKAGMT-----VDDYVEVARKIGPFADYIELNVSCPNTPGLRALQTDPELAAILLKVVKEVSK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 207 ladlhgklVPLALKIAPDLDDEQVKEIGDTLLR-HKIEAVIATNTTLSRAA--VQGLPH--ADEAGGLSGRPVFDASNEV 281
Cdd:pfam01180 158 --------VPVLVKLAPDLTDIVIIDIADVALGeDGLDGINATNTTVRGMRidLKTEKPilANGTGGLSGPPIKPIALKV 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 974648777 282 IRKLHAEVGNDVPIIGVGGIFSGEDARAKLAAGAALVQLYTGFIYRGPALVSECVKAIARE 342
Cdd:pfam01180 230 IRELYQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPEL 290
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
51-337 |
2.21e-60 |
|
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: 195.27 E-value: 2.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 51 TVMGLTFRNPVGLAAGLD-KDGAAIDGLAALGFGFIEVGTVTPRAQPGNPRPRMFRL-------PQAEALINRMGFNNHG 122
Cdd:cd02810 2 NFLGLKLKNPFGVAAGPLlKTGELIARAAAAGFGAVVYKTVTLHPRPGNPLPRVARLppegesyPEQLGILNSFGLPNLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 123 VDQFVKNVQAARY---RGILGLNIGKNAdtpieraAEDYLYCLERVYPF-ASYVTINISSPNTKNLRQL-QGAGELDALL 197
Cdd:cd02810 82 LDVWLQDIAKAKKefpGQPLIASVGGSS-------KEDYVELARKIERAgAKALELNLSCPNVGGGRQLgQDPEAVANLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 198 AALKDKQQrladlhgklVPLALKIAPDLDDEQVKEIGDTLLRHKIEAVIATNTTLSRAAVQ---GLPHADEAGGLSGRPV 274
Cdd:cd02810 155 KAVKAAVD---------IPLLVKLSPYFDLEDIVELAKAAERAGADGLTAINTISGRVVDLktvGPGPKRGTGGLSGAPI 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 974648777 275 FDASNEVIRKLHAEVGNDVPIIGVGGIFSGEDARAKLAAGAALVQLYTGFIYRGPALVSECVK 337
Cdd:cd02810 226 RPLALRWVARLAARLQLDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKIKK 288
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
54-306 |
5.77e-21 |
|
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: 91.46 E-value: 5.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 54 GLTFRNPVGLAAGLDKDGAAIDGLAALG-FGFIEVGTVTPRAQPGNPRPRMFRLPQAeaLINRMGFNNHGVDQFVKNVQA 132
Cdd:cd04740 6 GLRLKNPVILASGTFGFGEELSRVADLGkLGAIVTKSITLEPREGNPPPRVVETPGG--MLNAIGLQNPGVEAFLEELLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 133 ARyrgilglnigKNADTPI-----ERAAEDYLYCLERVYPF-ASYVTINISSPNTKNLRQLQGAG--ELDALLAALKDKq 204
Cdd:cd04740 84 WL----------REFGTPViasiaGSTVEEFVEVAEKLADAgADAIELNISCPNVKGGGMAFGTDpeAVAEIVKAVKKA- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 205 qrlADlhgklVPLALKIAPDLDDeqVKEIGDTLLRHKIEAVIATNTtlsraaVQGL--------PH-ADEAGGLSGRPVF 275
Cdd:cd04740 153 ---TD-----VPVIVKLTPNVTD--IVEIARAAEEAGADGLTLINT------LKGMaidietrkPIlGNVTGGLSGPAIK 216
|
250 260 270
....*....|....*....|....*....|.
gi 974648777 276 DASNEVIRKLHAEVgnDVPIIGVGGIFSGED 306
Cdd:cd04740 217 PIALRMVYQVYKAV--EIPIIGVGGIASGED 245
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
54-306 |
6.88e-19 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 85.59 E-value: 6.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 54 GLTFRNPVGLAAG-LDKDGAAIDGLAALGFGFIEVGTVTPRAQPGNPRPRMFRLPQaeALINRMGFNNHGVDQFVKNVQA 132
Cdd:PRK07259 8 GLKLKNPVMPASGtFGFGGEYARFYDLNGLGAIVTKSTTLEPREGNPTPRIAETPG--GMLNAIGLQNPGVDAFIEEELP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 133 ARyrgilglnigKNADTPI-----ERAAEDYLYCLERV--YPFASYVTINISSPNTKnlrqlQGA---GELDALLAALKD 202
Cdd:PRK07259 86 WL----------EEFDTPIianvaGSTEEEYAEVAEKLskAPNVDAIELNISCPNVK-----HGGmafGTDPELAYEVVK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 203 KQQRLADlhgklVPLALKIAPDLDDeqVKEIGDTLLRHKIEAVIATNTTL-------SRAAVQGlphaDEAGGLSGRPVF 275
Cdd:PRK07259 151 AVKEVVK-----VPVIVKLTPNVTD--IVEIAKAAEEAGADGLSLINTLKgmaidikTRKPILA----NVTGGLSGPAIK 219
|
250 260 270
....*....|....*....|....*....|.
gi 974648777 276 DASNEVIRKLHAEVgnDVPIIGVGGIFSGED 306
Cdd:PRK07259 220 PIALRMVYQVYQAV--DIPIIGMGGISSAED 248
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
54-340 |
8.74e-19 |
|
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 dihydroorotate dehydrogenases while excluding the closely related subfamily 2 (TIGR01036). This family also includes a number of uncharacterized proteins and a domain of dihydropyrimidine dehydrogenase. The uncharacterized proteins might all be dihydroorotate dehydrogenase.
Pssm-ID: 130109 [Multi-domain] Cd Length: 300 Bit Score: 85.17 E-value: 8.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 54 GLTFRNPVGLAAGLDKDGAAIDGLAAL-GFGFIEVGTVTPRAQPGNPRPRMFRLPQAeaLINRMGFNNHGVDQFVKNVQA 132
Cdd:TIGR01037 7 GIRFKNPLILASGIMGSGVESLRRIDRsGAGAVVTKSIGLEPRPGYRNPTIVETPCG--MLNAIGLQNPGVEAFLEELKP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 133 ARY---RGILGLNIGKNADTPIERAAEdylycLERVYPFASYVTINISSPNTKnlrqlqGAG-------ELDA-LLAALK 201
Cdd:TIGR01037 85 VREefpTPLIASVYGSSVEEFAEVAEK-----LEKAPPYVDAYELNLSCPHVK------GGGiaigqdpELSAdVVKAVK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 202 DKQQrladlhgklVPLALKIAPDLDDeqVKEIGDTLLRHKIEAVIATNTTLSRAA--VQGLPH-ADEAGGLSGRPVFDAS 278
Cdd:TIGR01037 154 DKTD---------VPVFAKLSPNVTD--ITEIAKAAEEAGADGLTLINTLRGMKIdiKTGKPIlANKTGGLSGPAIKPIA 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 974648777 279 NEVIRKLHAEVgnDVPIIGVGGIFSGEDARAKLAAGAALVQLYTGFIYRGPALVSECVKAIA 340
Cdd:TIGR01037 223 LRMVYDVYKMV--DIPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYRGFAFKKIIEGLIA 282
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
50-330 |
9.67e-16 |
|
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: 76.59 E-value: 9.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 50 RTVMGLTFRNPVGLAAG-LDKDGAAIDGLAALGFGFIEVGTVTPRAQPGNPRPRMFRLPQAEalINRMGFNNHGVDQFVK 128
Cdd:cd04741 1 VTPPGLTISPPLMNAAGpWCTTLEDLLELAASSTGAVTTRSSTLAGRPGNPEPRYYAFPLGS--INSLGLPNLGLDYYLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 129 NVQAARYRGilgLNIGKNADTPIERAAEDYLYCLERV----YPFASYVTINISSPNTKNLRQLqgAGELDALLAALKDKQ 204
Cdd:cd04741 79 YIRTISDGL---PGSAKPFFISVTGSAEDIAAMYKKIaahqKQFPLAMELNLSCPNVPGKPPP--AYDFDATLEYLTAVK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 205 QRLAdlhgklVPLALKIAPDLDDEQVKEIGDTLLRHK--IEAVIATNT-------TLSRAAVQgLPHADEAGGLSGRPVF 275
Cdd:cd04741 154 AAYS------IPVGVKTPPYTDPAQFDTLAEALNAFAcpISFITATNTlgnglvlDPERETVV-LKPKTGFGGLAGAYLH 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 974648777 276 DASNEVIRKLHAEVGNDVPIIGVGGIFSGEDARAKLAAGAALVQLYTGFIYRGPA 330
Cdd:cd04741 227 PLALGNVRTFRRLLPSEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPK 281
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
89-345 |
6.84e-06 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 47.26 E-value: 6.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 89 TVTPRAQPGNPRPRMFRLPQAEalINRMGFNNHGVDQFVKNVQAARYRG--------ILGLNIGKNADtpIERAAEDYly 160
Cdd:PRK02506 44 SATLEPRPGNPEPRYADTPLGS--INSMGLPNLGFDYYLDYVLELQKKGpnkphflsVVGLSPEETHT--ILKKIQAS-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 161 clervyPFASYVTINISSPNTKNLRQLqgAGELDALLAALKdkqqRLADLHGKlvPLALKIAPDLDDEQVKEIGDTLLRH 240
Cdd:PRK02506 118 ------DFNGLVELNLSCPNVPGKPQI--AYDFETTEQILE----EVFTYFTK--PLGVKLPPYFDIVHFDQAAAIFNKF 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 241 KIEAVIATNTTLSraavqGL---PHADEA--------GGLSG---RPVFDASnevIRKLHAEVGNDVPIIGVGGIFSGED 306
Cdd:PRK02506 184 PLAFVNCINSIGN-----GLvidPEDETVvikpkngfGGIGGdyiKPTALAN---VRAFYQRLNPSIQIIGTGGVKTGRD 255
|
250 260 270
....*....|....*....|....*....|....*....
gi 974648777 307 ARAKLAAGAALVQLYTGFIYRGPAlvseCVKAIARERTA 345
Cdd:PRK02506 256 AFEHILCGASMVQVGTALHKEGPA----VFERLTKELKA 290
|
|
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
215-306 |
7.39e-03 |
|
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. 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 the dimer interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.
Pssm-ID: 239244 Cd Length: 299 Bit Score: 37.65 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974648777 215 VPLALKIAPDLDDeqVKEIGDTLLRHKIEAVIATNTTLSRAAV-----QGLPHADE---AGGLSG---RPVfdASNEV-- 281
Cdd:cd02940 169 IPVIAKLTPNITD--IREIARAAKEGGADGVSAINTVNSLMGVdldgtPPAPGVEGkttYGGYSGpavKPI--ALRAVsq 244
|
90 100
....*....|....*....|....*
gi 974648777 282 IRKlHAEVGndVPIIGVGGIFSGED 306
Cdd:cd02940 245 IAR-APEPG--LPISGIGGIESWED 266
|
|
| |
