|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
1-333 |
0e+00 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 550.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 1 MYPLIKKALFNLDAENAHQFAIQSLKLFGKTPF------SLACSLPDNPTEVMGLRFKNPIGLAAGADKNGEAIDGFAKL 74
Cdd:PRK05286 2 YYPLARPLLFKLDPETAHELTIRALKRASRTPLlsllrqRLTYTDPRLPVTVMGLTFPNPVGLAAGFDKNGEAIDALGAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 75 GFGFIEVGTVTPVAQDGNPRPRQFRILEAEGIINRNGFNNLGVDVLIENVKKAKYNGILGINIGKNAITPIEHSLDDYQI 154
Cdd:PRK05286 82 GFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKAYRGIPLGINIGKNKDTPLEDAVDDYLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 155 CLRKVYPHASYVTVNISSPNTKNLRSLQYGEALDDLLRSLKAEQAQLsqkfGGYKPLVLKIAPDLTAEEIASVADSLVRH 234
Cdd:PRK05286 162 CLEKLYPYADYFTVNISSPNTPGLRDLQYGEALDELLAALKEAQAEL----HGYVPLLVKIAPDLSDEELDDIADLALEH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 235 QIDGVIAGNTTLSRDSVAGLPFADQQGGLSGKPLNALSTQLISQLFQELNGKLPIIGSGGIHSVQSGQEKINAGASLLQL 314
Cdd:PRK05286 238 GIDGVIATNTTLSRDGLKGLPNADEAGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGASLVQI 317
|
330
....*....|....*....
gi 737550408 315 YSAMIYQGPDLVRQLVRKI 333
Cdd:PRK05286 318 YSGLIYEGPGLVKEIVRGL 336
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
6-333 |
1.90e-175 |
|
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: 489.32 E-value: 1.90e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 6 KKALFNLDAENAHQFAIQSLKLFGKTPFSLACSL--PDNPTEVMGLRFKNPIGLAAGADKNGEAIDGFAKLGFGFIEVGT 83
Cdd:cd04738 1 RPLLFLLDPETAHRLAIRALKLGLGPPLLLLLVYddPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFVEVGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 84 VTPVAQDGNPRPRQFRILEAEGIINRNGFNNLGVDVLIENVKKAKY-NGILGINIGKNAITPIEHSLDDYQICLRKVYPH 162
Cdd:cd04738 81 VTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRRPrGGPLGVNIGKNKDTPLEDAVEDYVIGVRKLGPY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 163 ASYVTVNISSPNTKNLRSLQYGEALDDLLRSLKAEQAQLsqkfGGYKPLVLKIAPDLTAEEIASVADSLVRHQIDGVIAG 242
Cdd:cd04738 161 ADYLVVNVSSPNTPGLRDLQGKEALRELLTAVKEERNKL----GKKVPLLVKIAPDLSDEELEDIADVALEHGVDGIIAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 243 NTTLSRDSVAGLPFADQQGGLSGKPLNALSTQLISQLFQELNGKLPIIGSGGIHSVQSGQEKINAGASLLQLYSAMIYQG 322
Cdd:cd04738 237 NTTISRPGLLRSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTGLVYEG 316
|
330
....*....|.
gi 737550408 323 PDLVRQLVRKI 333
Cdd:cd04738 317 PGLVKRIKREL 327
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
2-333 |
1.58e-160 |
|
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: 451.93 E-value: 1.58e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 2 YPLIKKALFNLDAENAHQFAIQSLKLFGKTPFSlacSLPDN--------PTEVMGLRFKNPIGLAAGADKNGEAIDGFAK 73
Cdd:TIGR01036 1 YPLVRKLLFLLDPESAHELTFQFLRLGTGTPFL---ALLRSlfgasdplEVTVLGLKFPNPLGLAAGFDKDGEAIDALGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 74 LGFGFIEVGTVTPVAQDGNPRPRQFRILEAEGIINRNGFNNLGVDVLIENVKKAKYNGILGINIGKNAITPIEHSLDDYQ 153
Cdd:TIGR01036 78 MGFGFLEIGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLKRARYKGPIGINIGKNKDTPSEDAKEDYA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 154 ICLRKVYPHASYVTVNISSPNTKNLRSLQYGEALDDLLRSLKAEQAQLSQKFggYKPLVLKIAPDLTAEEIASVADSLVR 233
Cdd:TIGR01036 158 ACLRKLGPLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAVKQEQDGLRRVH--RVPVLVKIAPDLTESDLEDIADSLVE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 234 HQIDGVIAGNTTLSRDSVAGLPFADQQGGLSGKPLNALSTQLISQLFQELNGKLPIIGSGGIHSVQSGQEKINAGASLLQ 313
Cdd:TIGR01036 236 LGIDGVIATNTTVSRSLVQGPKNSDETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGASLLQ 315
|
330 340
....*....|....*....|
gi 737550408 314 LYSAMIYQGPDLVRQLVRKI 333
Cdd:TIGR01036 316 IYSGFIYWGPPLVKEIVKEI 335
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
41-334 |
1.45e-117 |
|
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: 341.28 E-value: 1.45e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 41 DNPTEVMGLRFKNPIGLAAG-ADKNGEAIDGFAKLGFGFIEVGTVTPVAQDGNPRPRQFRILEAEGIINRNGFNNLGVDV 119
Cdd:COG0167 1 DLSVELAGLKFPNPVGLASGfFDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 120 LIENVKKAK-YNGILGINIGKNaitpiehSLDDYQICLRKVYPH-ASYVTVNISSPNTKN-LRSL-QYGEALDDLLRSLK 195
Cdd:COG0167 81 FLERLLPAKrYDVPVIVNIGGN-------TVEDYVELARRLADAgADYLELNISCPNTPGgGRALgQDPEALAELLAAVK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 196 AEQaqlsqkfggYKPLVLKIAPDLTaeEIASVADSLVRHQIDGVIAGNTTLSR--DSVAGLP-FADQQGGLSGKPLNALS 272
Cdd:COG0167 154 AAT---------DKPVLVKLAPDLT--DIVEIARAAEEAGADGVIAINTTLGRaiDLETRRPvLANEAGGLSGPALKPIA 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 737550408 273 TQLISQLFQELNGKLPIIGSGGIHSVQSGQEKINAGASLLQLYSAMIYQGPDLVRQLVRKIS 334
Cdd:COG0167 223 LRMVREVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLE 284
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
44-333 |
1.03e-85 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 259.97 E-value: 1.03e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 44 TEVMGLRFKNPIGLAAGADKNGEAIDGFAKLG-FGFIEVGTVTPVAQDGNPRPRQFRIleAEGIINRNGFNNLGVDVLIE 122
Cdd:pfam01180 4 TKIPGLDFKNPIGLASGFDKFGEEALKWLALGkFGAIEIKSVTPYPQPGNPTPRVFRL--PEGVLNRMGLNNPGLDAVLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 123 NVKK--AKYNGI-LGINIGKNAITpiehsLDDYQICLRKVYPHASYVTVNISSPNTKNLRSLQYGEALDDLLRSLKAEQA 199
Cdd:pfam01180 82 ELLKrrKEYPRPdLGINLSKAGMT-----VDDYVEVARKIGPFADYIELNVSCPNTPGLRALQTDPELAAILLKVVKEVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 200 QlsqkfggyKPLVLKIAPDLTAEEIASVADSLVR-HQIDGVIAGNTTLSR---DSVAGLPF-ADQQGGLSGKPLNALSTQ 274
Cdd:pfam01180 157 K--------VPVLVKLAPDLTDIVIIDIADVALGeDGLDGINATNTTVRGmriDLKTEKPIlANGTGGLSGPPIKPIALK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 737550408 275 LISQLFQELNGKLPIIGSGGIHSVQSGQEKINAGASLLQLYSAMIYQGPDLVRQLVRKI 333
Cdd:pfam01180 229 VIRELYQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDEL 287
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
1-333 |
0e+00 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 550.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 1 MYPLIKKALFNLDAENAHQFAIQSLKLFGKTPF------SLACSLPDNPTEVMGLRFKNPIGLAAGADKNGEAIDGFAKL 74
Cdd:PRK05286 2 YYPLARPLLFKLDPETAHELTIRALKRASRTPLlsllrqRLTYTDPRLPVTVMGLTFPNPVGLAAGFDKNGEAIDALGAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 75 GFGFIEVGTVTPVAQDGNPRPRQFRILEAEGIINRNGFNNLGVDVLIENVKKAKYNGILGINIGKNAITPIEHSLDDYQI 154
Cdd:PRK05286 82 GFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKAYRGIPLGINIGKNKDTPLEDAVDDYLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 155 CLRKVYPHASYVTVNISSPNTKNLRSLQYGEALDDLLRSLKAEQAQLsqkfGGYKPLVLKIAPDLTAEEIASVADSLVRH 234
Cdd:PRK05286 162 CLEKLYPYADYFTVNISSPNTPGLRDLQYGEALDELLAALKEAQAEL----HGYVPLLVKIAPDLSDEELDDIADLALEH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 235 QIDGVIAGNTTLSRDSVAGLPFADQQGGLSGKPLNALSTQLISQLFQELNGKLPIIGSGGIHSVQSGQEKINAGASLLQL 314
Cdd:PRK05286 238 GIDGVIATNTTLSRDGLKGLPNADEAGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGASLVQI 317
|
330
....*....|....*....
gi 737550408 315 YSAMIYQGPDLVRQLVRKI 333
Cdd:PRK05286 318 YSGLIYEGPGLVKEIVRGL 336
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
6-333 |
1.90e-175 |
|
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: 489.32 E-value: 1.90e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 6 KKALFNLDAENAHQFAIQSLKLFGKTPFSLACSL--PDNPTEVMGLRFKNPIGLAAGADKNGEAIDGFAKLGFGFIEVGT 83
Cdd:cd04738 1 RPLLFLLDPETAHRLAIRALKLGLGPPLLLLLVYddPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFVEVGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 84 VTPVAQDGNPRPRQFRILEAEGIINRNGFNNLGVDVLIENVKKAKY-NGILGINIGKNAITPIEHSLDDYQICLRKVYPH 162
Cdd:cd04738 81 VTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRRPrGGPLGVNIGKNKDTPLEDAVEDYVIGVRKLGPY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 163 ASYVTVNISSPNTKNLRSLQYGEALDDLLRSLKAEQAQLsqkfGGYKPLVLKIAPDLTAEEIASVADSLVRHQIDGVIAG 242
Cdd:cd04738 161 ADYLVVNVSSPNTPGLRDLQGKEALRELLTAVKEERNKL----GKKVPLLVKIAPDLSDEELEDIADVALEHGVDGIIAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 243 NTTLSRDSVAGLPFADQQGGLSGKPLNALSTQLISQLFQELNGKLPIIGSGGIHSVQSGQEKINAGASLLQLYSAMIYQG 322
Cdd:cd04738 237 NTTISRPGLLRSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTGLVYEG 316
|
330
....*....|.
gi 737550408 323 PDLVRQLVRKI 333
Cdd:cd04738 317 PGLVKRIKREL 327
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
2-333 |
1.58e-160 |
|
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: 451.93 E-value: 1.58e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 2 YPLIKKALFNLDAENAHQFAIQSLKLFGKTPFSlacSLPDN--------PTEVMGLRFKNPIGLAAGADKNGEAIDGFAK 73
Cdd:TIGR01036 1 YPLVRKLLFLLDPESAHELTFQFLRLGTGTPFL---ALLRSlfgasdplEVTVLGLKFPNPLGLAAGFDKDGEAIDALGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 74 LGFGFIEVGTVTPVAQDGNPRPRQFRILEAEGIINRNGFNNLGVDVLIENVKKAKYNGILGINIGKNAITPIEHSLDDYQ 153
Cdd:TIGR01036 78 MGFGFLEIGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLKRARYKGPIGINIGKNKDTPSEDAKEDYA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 154 ICLRKVYPHASYVTVNISSPNTKNLRSLQYGEALDDLLRSLKAEQAQLSQKFggYKPLVLKIAPDLTAEEIASVADSLVR 233
Cdd:TIGR01036 158 ACLRKLGPLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAVKQEQDGLRRVH--RVPVLVKIAPDLTESDLEDIADSLVE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 234 HQIDGVIAGNTTLSRDSVAGLPFADQQGGLSGKPLNALSTQLISQLFQELNGKLPIIGSGGIHSVQSGQEKINAGASLLQ 313
Cdd:TIGR01036 236 LGIDGVIATNTTVSRSLVQGPKNSDETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGASLLQ 315
|
330 340
....*....|....*....|
gi 737550408 314 LYSAMIYQGPDLVRQLVRKI 333
Cdd:TIGR01036 316 IYSGFIYWGPPLVKEIVKEI 335
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
41-334 |
1.45e-117 |
|
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: 341.28 E-value: 1.45e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 41 DNPTEVMGLRFKNPIGLAAG-ADKNGEAIDGFAKLGFGFIEVGTVTPVAQDGNPRPRQFRILEAEGIINRNGFNNLGVDV 119
Cdd:COG0167 1 DLSVELAGLKFPNPVGLASGfFDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 120 LIENVKKAK-YNGILGINIGKNaitpiehSLDDYQICLRKVYPH-ASYVTVNISSPNTKN-LRSL-QYGEALDDLLRSLK 195
Cdd:COG0167 81 FLERLLPAKrYDVPVIVNIGGN-------TVEDYVELARRLADAgADYLELNISCPNTPGgGRALgQDPEALAELLAAVK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 196 AEQaqlsqkfggYKPLVLKIAPDLTaeEIASVADSLVRHQIDGVIAGNTTLSR--DSVAGLP-FADQQGGLSGKPLNALS 272
Cdd:COG0167 154 AAT---------DKPVLVKLAPDLT--DIVEIARAAEEAGADGVIAINTTLGRaiDLETRRPvLANEAGGLSGPALKPIA 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 737550408 273 TQLISQLFQELNGKLPIIGSGGIHSVQSGQEKINAGASLLQLYSAMIYQGPDLVRQLVRKIS 334
Cdd:COG0167 223 LRMVREVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLE 284
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
12-329 |
9.47e-113 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 333.24 E-value: 9.47e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 12 LDAENAHQFAIQSLKLfGKTPfslACSLPDNP---TEVMGLRFKNPIGLAAGADKNGEAIDGFAKLGFGFIEVGTVTPVA 88
Cdd:PLN02826 45 LDPETAHSLAISAAAR-GLVP---REKRPDPSvlgVEVWGRTFSNPIGLAAGFDKNAEAVEGLLGLGFGFVEIGSVTPLP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 89 QDGNPRPRQFRILEAEGIINRNGFNNLGVDV----LIENVKKAKYN--------------------GILGINIGKNAITp 144
Cdd:PLN02826 121 QPGNPKPRVFRLREEGAIINRYGFNSEGIVAvakrLGAQHGKRKLDetssssfssddvkaggkagpGILGVNLGKNKTS- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 145 iEHSLDDYQICLRKVYPHASYVTVNISSPNTKNLRSLQYGEALDDLLRSLKAEQAQLSQKFGGYKPLVLKIAPDLTAEEI 224
Cdd:PLN02826 200 -EDAAADYVQGVRALSQYADYLVINVSSPNTPGLRKLQGRKQLKDLLKKVLAARDEMQWGEEGPPPLLVKIAPDLSKEDL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 225 ASVADSLVRHQIDGVIAGNTTLSR-DSVAGLPFADQQGGLSGKPLNALSTQLISQLFQELNGKLPIIGSGGIHSVQSGQE 303
Cdd:PLN02826 279 EDIAAVALALGIDGLIISNTTISRpDSVLGHPHADEAGGLSGKPLFDLSTEVLREMYRLTRGKIPLVGCGGVSSGEDAYK 358
|
330 340
....*....|....*....|....*.
gi 737550408 304 KINAGASLLQLYSAMIYQGPDLVRQL 329
Cdd:PLN02826 359 KIRAGASLVQLYTAFAYEGPALIPRI 384
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
44-333 |
1.03e-85 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 259.97 E-value: 1.03e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 44 TEVMGLRFKNPIGLAAGADKNGEAIDGFAKLG-FGFIEVGTVTPVAQDGNPRPRQFRIleAEGIINRNGFNNLGVDVLIE 122
Cdd:pfam01180 4 TKIPGLDFKNPIGLASGFDKFGEEALKWLALGkFGAIEIKSVTPYPQPGNPTPRVFRL--PEGVLNRMGLNNPGLDAVLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 123 NVKK--AKYNGI-LGINIGKNAITpiehsLDDYQICLRKVYPHASYVTVNISSPNTKNLRSLQYGEALDDLLRSLKAEQA 199
Cdd:pfam01180 82 ELLKrrKEYPRPdLGINLSKAGMT-----VDDYVEVARKIGPFADYIELNVSCPNTPGLRALQTDPELAAILLKVVKEVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 200 QlsqkfggyKPLVLKIAPDLTAEEIASVADSLVR-HQIDGVIAGNTTLSR---DSVAGLPF-ADQQGGLSGKPLNALSTQ 274
Cdd:pfam01180 157 K--------VPVLVKLAPDLTDIVIIDIADVALGeDGLDGINATNTTVRGmriDLKTEKPIlANGTGGLSGPPIKPIALK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 737550408 275 LISQLFQELNGKLPIIGSGGIHSVQSGQEKINAGASLLQLYSAMIYQGPDLVRQLVRKI 333
Cdd:pfam01180 229 VIRELYQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDEL 287
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
44-332 |
7.32e-75 |
|
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: 232.24 E-value: 7.32e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 44 TEVMGLRFKNPIGLAAGAD-KNGEAIDGFAKLGFGFIEVGTVTPVAQDGNPRPRQFRI-------LEAEGIINRNGFNNL 115
Cdd:cd02810 1 VNFLGLKLKNPFGVAAGPLlKTGELIARAAAAGFGAVVYKTVTLHPRPGNPLPRVARLppegesyPEQLGILNSFGLPNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 116 GVDVLIENVKKAKYNG---ILGINIGKNaitpiehSLDDYQICLRKVYP-HASYVTVNISSPNTKNLRSL-QYGEALDDL 190
Cdd:cd02810 81 GLDVWLQDIAKAKKEFpgqPLIASVGGS-------SKEDYVELARKIERaGAKALELNLSCPNVGGGRQLgQDPEAVANL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 191 LRSLKAEQaqlsqkfggYKPLVLKIAPDLTAEEIASVADSLVRHQIDGVIAGNTTLSR---DSVAGLPFADQQGGLSGKP 267
Cdd:cd02810 154 LKAVKAAV---------DIPLLVKLSPYFDLEDIVELAKAAERAGADGLTAINTISGRvvdLKTVGPGPKRGTGGLSGAP 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 737550408 268 LNALSTQLISQLFQELNGKLPIIGSGGIHSVQSGQEKINAGASLLQLYSAMIYQGPDLVRQLVRK 332
Cdd:cd02810 225 IRPLALRWVARLAARLQLDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKIKKE 289
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
43-333 |
2.57e-25 |
|
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: 103.01 E-value: 2.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 43 PTEVMGLRFKNPIGLAAGADKNGEAIDGFAKLG-FGFIEVGTVTPVAQDGNPRPRqfrILEAE-GIINRNGFNNLGVDVL 120
Cdd:cd04740 1 SVELAGLRLKNPVILASGTFGFGEELSRVADLGkLGAIVTKSITLEPREGNPPPR---VVETPgGMLNAIGLQNPGVEAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 121 IENVKKA--KYNGILGINIGKnaitpieHSLDDYQICLRKVYP-HASYVTVNISSPNTKNlRSLQYG---EALDDLLRSL 194
Cdd:cd04740 78 LEELLPWlrEFGTPVIASIAG-------STVEEFVEVAEKLADaGADAIELNISCPNVKG-GGMAFGtdpEAVAEIVKAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 195 KAEQAqlsqkfggyKPLVLKIAPDLTaeEIASVADSLVRHQIDGVIAGNTT--LSRDSVAGLP-FADQQGGLSGKPLNAL 271
Cdd:cd04740 150 KKATD---------VPVIVKLTPNVT--DIVEIARAAEEAGADGLTLINTLkgMAIDIETRKPiLGNVTGGLSGPAIKPI 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 737550408 272 STQLISQLFQELngKLPIIGSGGIHSVQSGQEKINAGASLLQLYSAmIYQGPDLVRQLVRKI 333
Cdd:cd04740 219 ALRMVYQVYKAV--EIPIIGVGGIASGEDALEFLMAGASAVQVGTA-NFVDPEAFKEIIEGL 277
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
44-333 |
2.56e-23 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 97.53 E-value: 2.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 44 TEVMGLRFKNPIGLAAG-ADKNGEAIDGFAKLGFGFIEVGTVTPVAQDGNPRPRqfrILEAE-GIINRNGFNNLGVDVLI 121
Cdd:PRK07259 4 VELPGLKLKNPVMPASGtFGFGGEYARFYDLNGLGAIVTKSTTLEPREGNPTPR---IAETPgGMLNAIGLQNPGVDAFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 122 EN--VKKAKYNGILGINIGKNaitpiehSLDDYQICLRKV--YPHASYVTVNISSPNTKnlrslQYGEALD---DLLRSL 194
Cdd:PRK07259 81 EEelPWLEEFDTPIIANVAGS-------TEEEYAEVAEKLskAPNVDAIELNISCPNVK-----HGGMAFGtdpELAYEV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 195 KAEQAQLSQKfggykPLVLKIAPDLTaeEIASVADSLVRHQIDGVIAGNTTL--SRDSVAGLP-FADQQGGLSGKPLNAL 271
Cdd:PRK07259 149 VKAVKEVVKV-----PVIVKLTPNVT--DIVEIAKAAEEAGADGLSLINTLKgmAIDIKTRKPiLANVTGGLSGPAIKPI 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 737550408 272 STQLISQLFQELngKLPIIGSGGIHSVQSGQEKINAGASLLQLYSAmIYQGPDLVRQLVRKI 333
Cdd:PRK07259 222 ALRMVYQVYQAV--DIPIIGMGGISSAEDAIEFIMAGASAVQVGTA-NFYDPYAFPKIIEGL 280
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
44-322 |
1.36e-22 |
|
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: 95.57 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 44 TEVMGLRFKNPIGLAAGA-DKNGEAIDGFAKLGFGFIEVGTVTPVAQDGNPRPRqfrILEAE-GIINRNGFNNLGVDVLI 121
Cdd:TIGR01037 3 VELFGIRFKNPLILASGImGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPT---IVETPcGMLNAIGLQNPGVEAFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 122 ENVKKA--KYNGILGINIgknaitpIEHSLDDY-QIC--LRKVYPHASYVTVNISSPNTKNLrSLQYGEALDDLLRSLKA 196
Cdd:TIGR01037 80 EELKPVreEFPTPLIASV-------YGSSVEEFaEVAekLEKAPPYVDAYELNLSCPHVKGG-GIAIGQDPELSADVVKA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 197 EQAQLSqkfggyKPLVLKIAPDLTaeEIASVADSLVRHQIDGVIAGNTT--LSRDSVAGLP-FADQQGGLSGKPLNALST 273
Cdd:TIGR01037 152 VKDKTD------VPVFAKLSPNVT--DITEIAKAAEEAGADGLTLINTLrgMKIDIKTGKPiLANKTGGLSGPAIKPIAL 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 737550408 274 QLISQLFQELNgkLPIIGSGGIHSVQSGQEKINAGASLLQLYSAMIYQG 322
Cdd:TIGR01037 224 RMVYDVYKMVD--IPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYRG 270
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
48-324 |
1.14e-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: 78.91 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 48 GLRFKNPIGLAAG-ADKNGEAIDGFAKLGFGFIEVGTVTPVAQDGNPRPRQFRIleAEGIINRNGFNNLGVDVLIENVKK 126
Cdd:cd04741 5 GLTISPPLMNAAGpWCTTLEDLLELAASSTGAVTTRSSTLAGRPGNPEPRYYAF--PLGSINSLGLPNLGLDYYLEYIRT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 127 -AKYNGILGinigKNAITPIEHSLDDYQICLRKVYPHASYVT----VNISSPNTKNLRSLQY-GEALDDLLRSLKAEQAq 200
Cdd:cd04741 83 iSDGLPGSA----KPFFISVTGSAEDIAAMYKKIAAHQKQFPlameLNLSCPNVPGKPPPAYdFDATLEYLTAVKAAYS- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 201 lsqkfggyKPLVLKIAPDLTAEEIASVADSLVRHQ--IDGVIAGNT-------TLSRDSVAgLPFADQQGGLSGKPLNAL 271
Cdd:cd04741 158 --------IPVGVKTPPYTDPAQFDTLAEALNAFAcpISFITATNTlgnglvlDPERETVV-LKPKTGFGGLAGAYLHPL 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 737550408 272 STQLISQLFQELNGKLPIIGSGGIHSVQSGQEKINAGASLLQLYSAMIYQGPD 324
Cdd:cd04741 229 ALGNVRTFRRLLPSEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPK 281
|
|
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
44-329 |
3.22e-10 |
|
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: 59.99 E-value: 3.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 44 TEVMGLRFKNPIGLAAG-----ADKNGEAIDGfaklGFGFIEVGTVTPvaqDG----NPRPRQFRIL-EAEGIInrnGFN 113
Cdd:cd02940 4 VTFCGIKFPNPFGLASAppttsYPMIRRAFEA----GWGGAVTKTLGL---DKdivtNVSPRIARLRtSGRGQI---GFN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 114 NLgvdVLIENvKKAKYN----GILGINIGKNA-ITPI--EHSLDDYQICLRKVYPH-ASYVTVNISSPNTKNLRSL---- 181
Cdd:cd02940 74 NI---ELISE-KPLEYWlkeiRELKKDFPDKIlIASImcEYNKEDWTELAKLVEEAgADALELNFSCPHGMPERGMgaav 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 182 -QYGEALDDLLRSLKaEQAQLsqkfggykPLVLKIAPDLTaeEIASVADSLVRHQIDGVIAGNTTLS-----RDSVAGLP 255
Cdd:cd02940 150 gQDPELVEEICRWVR-EAVKI--------PVIAKLTPNIT--DIREIARAAKEGGADGVSAINTVNSlmgvdLDGTPPAP 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 737550408 256 FADQQ---GGLSGKPLNALSTQLISQLFQELNGKLPIIGSGGIHSVQSGQEKINAGASLLQLYSAMIYQGPDLVRQL 329
Cdd:cd02940 219 GVEGKttyGGYSGPAVKPIALRAVSQIARAPEPGLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDM 295
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
44-323 |
8.04e-08 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 53.03 E-value: 8.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 44 TEVMGLRFKNPIGLAAGAD-KNGEAIDGFAKLGFGFIEVGTVTPVAQDGNPRPRQFRIleAEGIINRNGFNNLGVDVLIE 122
Cdd:PRK02506 4 TQIAGFKFDNCLMNAAGVYcMTKEELEEVEASAAGAFVTKSATLEPRPGNPEPRYADT--PLGSINSMGLPNLGFDYYLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 123 NVKKAKYngilginigKNAITPIEHSL-----DDYQICLRKVypHASY----VTVNISSPNTKNLRSLQYG-EALDDLLR 192
Cdd:PRK02506 82 YVLELQK---------KGPNKPHFLSVvglspEETHTILKKI--QASDfnglVELNLSCPNVPGKPQIAYDfETTEQILE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737550408 193 SLKAEqaqlsqkfgGYKPLVLKIAPDLTAEEIASVADSLVRHQIDGVIA----GNT---TLSRDSVAGLPfADQQGGLSG 265
Cdd:PRK02506 151 EVFTY---------FTKPLGVKLPPYFDIVHFDQAAAIFNKFPLAFVNCinsiGNGlviDPEDETVVIKP-KNGFGGIGG 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 737550408 266 ---KPLnALSTqlISQLFQELNGKLPIIGSGGIHSVQSGQEKINAGASLLQLYSAMIYQGP 323
Cdd:PRK02506 221 dyiKPT-ALAN--VRAFYQRLNPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGP 278
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
261-326 |
5.86e-06 |
|
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: 47.59 E-value: 5.86e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 737550408 261 GGLSGKPLNALSTQLISQLFQE-LNGKLPIIGSGGIHSVQSGQEKINAGASLLQLYSAMIYQgPDLV 326
Cdd:cd04735 258 DFDRKSRRGRDDNQTIMELVKErIAGRLPLIAVGSINTPDDALEALETGADLVAIGRGLLVD-PDWV 323
|
|
| |
