|
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: 559.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 1 MLYSLARPLLFSLAPERAHELTLSLLKSSHK---MGLMRQKTV----AKPVTCMGIEFPNPVGLAAGLDKNGAYIDALAG 73
Cdd:PRK05286 1 MYYPLARPLLFKLDPETAHELTIRALKRASRtplLSLLRQRLTytdpRLPVTVMGLTFPNPVGLAAGFDKNGEAIDALGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 74 LGFGFIEIGTITPRPQAGNPHPRLFRIPQAKAIINRMGFNNDGVDQLIENVKAAKFKGILGINIGKNADTPVENAVDDYL 153
Cdd:PRK05286 81 LGFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKAYRGIPLGINIGKNKDTPLEDAVDDYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 154 ICLEKVYNYASYITVNISSPNTKNLRSLQSGDALTELLQTLKQRQLELAeehqHYVPLVLKVAPDLDPEDIQFIAKQLLQ 233
Cdd:PRK05286 161 ICLEKLYPYADYFTVNISSPNTPGLRDLQYGEALDELLAALKEAQAELH----GYVPLLVKIAPDLSDEELDDIADLALE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 234 FKIDGLIVTNTTLSREGVENLPHGDEAGGLSGAPVFEKSTACLAAFSAALKGEIPLIGVGGILSGEQAVAKKNAGASLVQ 313
Cdd:PRK05286 237 HGIDGVIATNTTLSRDGLKGLPNADEAGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGASLVQ 316
|
330 340
....*....|....*....|
gi 491113019 314 VYSGLIYAGPELVQDCVNAL 333
Cdd:PRK05286 317 IYSGLIYEGPGLVKEIVRGL 336
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
7-333 |
0e+00 |
|
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: 506.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 7 RPLLFSLAPERAHELTLSLLKSSHKMGLMRQKTVAKP---VTCMGIEFPNPVGLAAGLDKNGAYIDALAGLGFGFIEIGT 83
Cdd:cd04738 1 RPLLFLLDPETAHRLAIRALKLGLGPPLLLLLVYDDPrleVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFVEVGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 84 ITPRPQAGNPHPRLFRIPQAKAIINRMGFNNDGVDQLIENVKAAK-FKGILGINIGKNADTPVENAVDDYLICLEKVYNY 162
Cdd:cd04738 81 VTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRRpRGGPLGVNIGKNKDTPLEDAVEDYVIGVRKLGPY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 163 ASYITVNISSPNTKNLRSLQSGDALTELLQTLKQRQLELAeehqHYVPLVLKVAPDLDPEDIQFIAKQLLQFKIDGLIVT 242
Cdd:cd04738 161 ADYLVVNVSSPNTPGLRDLQGKEALRELLTAVKEERNKLG----KKVPLLVKIAPDLSDEELEDIADVALEHGVDGIIAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 243 NTTLSREGVENLPHGDEAGGLSGAPVFEKSTACLAAFSAALKGEIPLIGVGGILSGEQAVAKKNAGASLVQVYSGLIYAG 322
Cdd:cd04738 237 NTTISRPGLLRSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTGLVYEG 316
|
330
....*....|.
gi 491113019 323 PELVQDCVNAL 333
Cdd:cd04738 317 PGLVKRIKREL 327
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
3-333 |
1.09e-141 |
|
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: 403.78 E-value: 1.09e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 3 YSLARPLLFSLAPERAHELT---LSLLKSSHKMGLMRQKTVAK---PVTCMGIEFPNPVGLAAGLDKNGAYIDALAGLGF 76
Cdd:TIGR01036 1 YPLVRKLLFLLDPESAHELTfqfLRLGTGTPFLALLRSLFGASdplEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAMGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 77 GFIEIGTITPRPQAGNPHPRLFRIPQAKAIINRMGFNNDGVDQLIENVKAAKFKGILGINIGKNADTPVENAVDDYLICL 156
Cdd:TIGR01036 81 GFLEIGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLKRARYKGPIGINIGKNKDTPSEDAKEDYAACL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 157 EKVYNYASYITVNISSPNTKNLRSLQSGDALTELLQTLKQRQLELAEehQHYVPLVLKVAPDLDPEDIQFIAKQLLQFKI 236
Cdd:TIGR01036 161 RKLGPLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAVKQEQDGLRR--VHRVPVLVKIAPDLTESDLEDIADSLVELGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 237 DGLIVTNTTLSREGVENLPHGDEAGGLSGAPVFEKSTACLAAFSAALKGEIPLIGVGGILSGEQAVAKKNAGASLVQVYS 316
Cdd:TIGR01036 239 DGVIATNTTVSRSLVQGPKNSDETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGASLLQIYS 318
|
330
....*....|....*..
gi 491113019 317 GLIYAGPELVQDCVNAL 333
Cdd:TIGR01036 319 GFIYWGPPLVKEIVKEI 335
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
43-333 |
8.61e-119 |
|
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: 344.36 E-value: 8.61e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 43 PVTCMGIEFPNPVGLAAG-LDKNGAYIDALAGLGFGFIEIGTITPRPQAGNPHPRLFRIPQAKAIINRMGFNNDGVDQLI 121
Cdd:COG0167 3 SVELAGLKFPNPVGLASGfFDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDAFL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 122 ENVKAAK-FKGILGINIGKnadtpveNAVDDYLICLEKVYNY-ASYITVNISSPNTKN-LRSL-QSGDALTELLQTLKQR 197
Cdd:COG0167 83 ERLLPAKrYDVPVIVNIGG-------NTVEDYVELARRLADAgADYLELNISCPNTPGgGRALgQDPEALAELLAAVKAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 198 QlelaeehqhYVPLVLKVAPDLdpEDIQFIAKQLLQFKIDGLIVTNTTLSRE-GVEN-LPH-GDEAGGLSGAPVFEKSTA 274
Cdd:COG0167 156 T---------DKPVLVKLAPDL--TDIVEIARAAEEAGADGVIAINTTLGRAiDLETrRPVlANEAGGLSGPALKPIALR 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 491113019 275 CLAAFSAALKGEIPLIGVGGILSGEQAVAKKNAGASLVQVYSGLIYAGPELVQDCVNAL 333
Cdd:COG0167 225 MVREVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGL 283
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
44-323 |
3.23e-81 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 248.42 E-value: 3.23e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 44 VTCMGIEFPNPVGLAAGLDKNGAYIDALAGLG-FGFIEIGTITPRPQAGNPHPRLFRIPQAkaIINRMGFNNDGVDQLIE 122
Cdd:pfam01180 4 TKIPGLDFKNPIGLASGFDKFGEEALKWLALGkFGAIEIKSVTPYPQPGNPTPRVFRLPEG--VLNRMGLNNPGLDAVLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 123 NVKA---AKFKGILGINIGKNADTpvenaVDDYLICLEKVYNYASYITVNISSPNTKNLRSLQSGDALT-ELLQTLKQRq 198
Cdd:pfam01180 82 ELLKrrkEYPRPDLGINLSKAGMT-----VDDYVEVARKIGPFADYIELNVSCPNTPGLRALQTDPELAaILLKVVKEV- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 199 lelaeehqHYVPLVLKVAPDLDPEDIQFIAKQLL-QFKIDGLIVTNTTLSREG--VENLPHGDE--AGGLSGAPVFEKST 273
Cdd:pfam01180 156 --------SKVPVLVKLAPDLTDIVIIDIADVALgEDGLDGINATNTTVRGMRidLKTEKPILAngTGGLSGPPIKPIAL 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 491113019 274 ACLAAFSAALKGEIPLIGVGGILSGEQAVAKKNAGASLVQVYSGLIYAGP 323
Cdd:pfam01180 228 KVIRELYQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGP 277
|
|
| |
|
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: 559.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 1 MLYSLARPLLFSLAPERAHELTLSLLKSSHK---MGLMRQKTV----AKPVTCMGIEFPNPVGLAAGLDKNGAYIDALAG 73
Cdd:PRK05286 1 MYYPLARPLLFKLDPETAHELTIRALKRASRtplLSLLRQRLTytdpRLPVTVMGLTFPNPVGLAAGFDKNGEAIDALGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 74 LGFGFIEIGTITPRPQAGNPHPRLFRIPQAKAIINRMGFNNDGVDQLIENVKAAKFKGILGINIGKNADTPVENAVDDYL 153
Cdd:PRK05286 81 LGFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKAYRGIPLGINIGKNKDTPLEDAVDDYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 154 ICLEKVYNYASYITVNISSPNTKNLRSLQSGDALTELLQTLKQRQLELAeehqHYVPLVLKVAPDLDPEDIQFIAKQLLQ 233
Cdd:PRK05286 161 ICLEKLYPYADYFTVNISSPNTPGLRDLQYGEALDELLAALKEAQAELH----GYVPLLVKIAPDLSDEELDDIADLALE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 234 FKIDGLIVTNTTLSREGVENLPHGDEAGGLSGAPVFEKSTACLAAFSAALKGEIPLIGVGGILSGEQAVAKKNAGASLVQ 313
Cdd:PRK05286 237 HGIDGVIATNTTLSRDGLKGLPNADEAGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGASLVQ 316
|
330 340
....*....|....*....|
gi 491113019 314 VYSGLIYAGPELVQDCVNAL 333
Cdd:PRK05286 317 IYSGLIYEGPGLVKEIVRGL 336
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
7-333 |
0e+00 |
|
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: 506.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 7 RPLLFSLAPERAHELTLSLLKSSHKMGLMRQKTVAKP---VTCMGIEFPNPVGLAAGLDKNGAYIDALAGLGFGFIEIGT 83
Cdd:cd04738 1 RPLLFLLDPETAHRLAIRALKLGLGPPLLLLLVYDDPrleVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFVEVGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 84 ITPRPQAGNPHPRLFRIPQAKAIINRMGFNNDGVDQLIENVKAAK-FKGILGINIGKNADTPVENAVDDYLICLEKVYNY 162
Cdd:cd04738 81 VTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRRpRGGPLGVNIGKNKDTPLEDAVEDYVIGVRKLGPY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 163 ASYITVNISSPNTKNLRSLQSGDALTELLQTLKQRQLELAeehqHYVPLVLKVAPDLDPEDIQFIAKQLLQFKIDGLIVT 242
Cdd:cd04738 161 ADYLVVNVSSPNTPGLRDLQGKEALRELLTAVKEERNKLG----KKVPLLVKIAPDLSDEELEDIADVALEHGVDGIIAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 243 NTTLSREGVENLPHGDEAGGLSGAPVFEKSTACLAAFSAALKGEIPLIGVGGILSGEQAVAKKNAGASLVQVYSGLIYAG 322
Cdd:cd04738 237 NTTISRPGLLRSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTGLVYEG 316
|
330
....*....|.
gi 491113019 323 PELVQDCVNAL 333
Cdd:cd04738 317 PGLVKRIKREL 327
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
3-333 |
1.09e-141 |
|
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: 403.78 E-value: 1.09e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 3 YSLARPLLFSLAPERAHELT---LSLLKSSHKMGLMRQKTVAK---PVTCMGIEFPNPVGLAAGLDKNGAYIDALAGLGF 76
Cdd:TIGR01036 1 YPLVRKLLFLLDPESAHELTfqfLRLGTGTPFLALLRSLFGASdplEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAMGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 77 GFIEIGTITPRPQAGNPHPRLFRIPQAKAIINRMGFNNDGVDQLIENVKAAKFKGILGINIGKNADTPVENAVDDYLICL 156
Cdd:TIGR01036 81 GFLEIGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLKRARYKGPIGINIGKNKDTPSEDAKEDYAACL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 157 EKVYNYASYITVNISSPNTKNLRSLQSGDALTELLQTLKQRQLELAEehQHYVPLVLKVAPDLDPEDIQFIAKQLLQFKI 236
Cdd:TIGR01036 161 RKLGPLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAVKQEQDGLRR--VHRVPVLVKIAPDLTESDLEDIADSLVELGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 237 DGLIVTNTTLSREGVENLPHGDEAGGLSGAPVFEKSTACLAAFSAALKGEIPLIGVGGILSGEQAVAKKNAGASLVQVYS 316
Cdd:TIGR01036 239 DGVIATNTTVSRSLVQGPKNSDETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGASLLQIYS 318
|
330
....*....|....*..
gi 491113019 317 GLIYAGPELVQDCVNAL 333
Cdd:TIGR01036 319 GFIYWGPPLVKEIVKEI 335
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
43-333 |
8.61e-119 |
|
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: 344.36 E-value: 8.61e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 43 PVTCMGIEFPNPVGLAAG-LDKNGAYIDALAGLGFGFIEIGTITPRPQAGNPHPRLFRIPQAKAIINRMGFNNDGVDQLI 121
Cdd:COG0167 3 SVELAGLKFPNPVGLASGfFDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDAFL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 122 ENVKAAK-FKGILGINIGKnadtpveNAVDDYLICLEKVYNY-ASYITVNISSPNTKN-LRSL-QSGDALTELLQTLKQR 197
Cdd:COG0167 83 ERLLPAKrYDVPVIVNIGG-------NTVEDYVELARRLADAgADYLELNISCPNTPGgGRALgQDPEALAELLAAVKAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 198 QlelaeehqhYVPLVLKVAPDLdpEDIQFIAKQLLQFKIDGLIVTNTTLSRE-GVEN-LPH-GDEAGGLSGAPVFEKSTA 274
Cdd:COG0167 156 T---------DKPVLVKLAPDL--TDIVEIARAAEEAGADGVIAINTTLGRAiDLETrRPVlANEAGGLSGPALKPIALR 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 491113019 275 CLAAFSAALKGEIPLIGVGGILSGEQAVAKKNAGASLVQVYSGLIYAGPELVQDCVNAL 333
Cdd:COG0167 225 MVREVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGL 283
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
2-326 |
1.93e-111 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 329.78 E-value: 1.93e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 2 LYSLARPLLFSLAPERAHELTLSLLKSSHKMGLMRQKTVAKPVTCMGIEFPNPVGLAAGLDKNGAYIDALAGLGFGFIEI 81
Cdd:PLN02826 34 ATKLVNPLFRLLDPETAHSLAISAAARGLVPREKRPDPSVLGVEVWGRTFSNPIGLAAGFDKNAEAVEGLLGLGFGFVEI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 82 GTITPRPQAGNPHPRLFRIPQAKAIINRMGFNNDGVDQLIENVKAAKFK------------------------GILGINI 137
Cdd:PLN02826 114 GSVTPLPQPGNPKPRVFRLREEGAIINRYGFNSEGIVAVAKRLGAQHGKrkldetssssfssddvkaggkagpGILGVNL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 138 GKNADTpvENAVDDYLICLEKVYNYASYITVNISSPNTKNLRSLQSGDALTELLQTLKQRQLELAEEHQHYVPLVLKVAP 217
Cdd:PLN02826 194 GKNKTS--EDAAADYVQGVRALSQYADYLVINVSSPNTPGLRKLQGRKQLKDLLKKVLAARDEMQWGEEGPPPLLVKIAP 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 218 DLDPEDIQFIAKQLLQFKIDGLIVTNTTLSR-EGVENLPHGDEAGGLSGAPVFEKSTACLAAFSAALKGEIPLIGVGGIL 296
Cdd:PLN02826 272 DLSKEDLEDIAAVALALGIDGLIISNTTISRpDSVLGHPHADEAGGLSGKPLFDLSTEVLREMYRLTRGKIPLVGCGGVS 351
|
330 340 350
....*....|....*....|....*....|
gi 491113019 297 SGEQAVAKKNAGASLVQVYSGLIYAGPELV 326
Cdd:PLN02826 352 SGEDAYKKIRAGASLVQLYTAFAYEGPALI 381
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
44-323 |
3.23e-81 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 248.42 E-value: 3.23e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 44 VTCMGIEFPNPVGLAAGLDKNGAYIDALAGLG-FGFIEIGTITPRPQAGNPHPRLFRIPQAkaIINRMGFNNDGVDQLIE 122
Cdd:pfam01180 4 TKIPGLDFKNPIGLASGFDKFGEEALKWLALGkFGAIEIKSVTPYPQPGNPTPRVFRLPEG--VLNRMGLNNPGLDAVLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 123 NVKA---AKFKGILGINIGKNADTpvenaVDDYLICLEKVYNYASYITVNISSPNTKNLRSLQSGDALT-ELLQTLKQRq 198
Cdd:pfam01180 82 ELLKrrkEYPRPDLGINLSKAGMT-----VDDYVEVARKIGPFADYIELNVSCPNTPGLRALQTDPELAaILLKVVKEV- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 199 lelaeehqHYVPLVLKVAPDLDPEDIQFIAKQLL-QFKIDGLIVTNTTLSREG--VENLPHGDE--AGGLSGAPVFEKST 273
Cdd:pfam01180 156 --------SKVPVLVKLAPDLTDIVIIDIADVALgEDGLDGINATNTTVRGMRidLKTEKPILAngTGGLSGPPIKPIAL 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 491113019 274 ACLAAFSAALKGEIPLIGVGGILSGEQAVAKKNAGASLVQVYSGLIYAGP 323
Cdd:pfam01180 228 KVIRELYQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGP 277
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
44-328 |
1.41e-68 |
|
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: 216.07 E-value: 1.41e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 44 VTCMGIEFPNPVGLAAGLD-KNGAYIDALAGLGFGFIEIGTITPRPQAGNPHPRLFRI-------PQAKAIINRMGFNND 115
Cdd:cd02810 1 VNFLGLKLKNPFGVAAGPLlKTGELIARAAAAGFGAVVYKTVTLHPRPGNPLPRVARLppegesyPEQLGILNSFGLPNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 116 GVDQLIENVKAAKFKG---ILGINIGKNAdtpvenaVDDYLICLEKVYNY-ASYITVNISSPNTKNLRSL-QSGDALTEL 190
Cdd:cd02810 81 GLDVWLQDIAKAKKEFpgqPLIASVGGSS-------KEDYVELARKIERAgAKALELNLSCPNVGGGRQLgQDPEAVANL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 191 LQTLKQRQlelaeehqhYVPLVLKVAPDLDPEDIQFIAKQLLQFKIDGLIVTNTTLSREGVEN---LPHGDEAGGLSGAP 267
Cdd:cd02810 154 LKAVKAAV---------DIPLLVKLSPYFDLEDIVELAKAAERAGADGLTAINTISGRVVDLKtvgPGPKRGTGGLSGAP 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491113019 268 VFEKSTACLAAFSAALKGEIPLIGVGGILSGEQAVAKKNAGASLVQVYSGLIYAGPELVQD 328
Cdd:cd02810 225 IRPLALRWVARLAARLQLDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRK 285
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
48-324 |
1.85e-24 |
|
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: 100.70 E-value: 1.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 48 GIEFPNPVGLAAGLDKNGAYIDALAGLG-FGFIEIGTITPRPQAGNPHPRLFRIPQakAIINRMGFNNDGVDQLIENVKA 126
Cdd:cd04740 6 GLRLKNPVILASGTFGFGEELSRVADLGkLGAIVTKSITLEPREGNPPPRVVETPG--GMLNAIGLQNPGVEAFLEELLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 127 AKfkgilginigKNADTPV-----ENAVDDYLICLEKVYNY-ASYITVNISSPNTKNLRSL--QSGDALTELLQTLKqRQ 198
Cdd:cd04740 84 WL----------REFGTPViasiaGSTVEEFVEVAEKLADAgADAIELNISCPNVKGGGMAfgTDPEAVAEIVKAVK-KA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 199 LElaeehqhyVPLVLKVAPDLDpeDIQFIAKQLLQFKIDGLIVTNTTL-------SREGVenLphGDEAGGLSGAPVFEK 271
Cdd:cd04740 153 TD--------VPVIVKLTPNVT--DIVEIARAAEEAGADGLTLINTLKgmaidieTRKPI--L--GNVTGGLSGPAIKPI 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 491113019 272 STACLAAFSAALkgEIPLIGVGGILSGEQAVAKKNAGASLVQVYSGLIYaGPE 324
Cdd:cd04740 219 ALRMVYQVYKAV--EIPIIGVGGIASGEDALEFLMAGASAVQVGTANFV-DPE 268
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
48-322 |
8.32e-21 |
|
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: 90.57 E-value: 8.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 48 GIEFPNPVGLAAG-LDKNGAYIDALAGLGFGFIEIGTITPRPQAGNPHPRLFRIPQAkaIINRMGFNNDGVDQLIENVKA 126
Cdd:TIGR01037 7 GIRFKNPLILASGiMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTIVETPCG--MLNAIGLQNPGVEAFLEELKP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 127 AKF---KGILGINIGKNADTPVENAVDdylicLEKVYNYASYITVNISSPNTKNLRSL--QSGDALTELLQTLKQRQlel 201
Cdd:TIGR01037 85 VREefpTPLIASVYGSSVEEFAEVAEK-----LEKAPPYVDAYELNLSCPHVKGGGIAigQDPELSADVVKAVKDKT--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 202 aeehqhYVPLVLKVAPDLdpEDIQFIAKQLLQFKIDGLIVTNTTLS-----REGVENLphGDEAGGLSGAPVfeKSTACL 276
Cdd:TIGR01037 157 ------DVPVFAKLSPNV--TDITEIAKAAEEAGADGLTLINTLRGmkidiKTGKPIL--ANKTGGLSGPAI--KPIALR 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 491113019 277 AAFSAALKGEIPLIGVGGILSGEQAVAKKNAGASLVQVYSGLIYAG 322
Cdd:TIGR01037 225 MVYDVYKMVDIPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYRG 270
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
48-324 |
1.09e-19 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 87.51 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 48 GIEFPNPVGLAAG-LDKNGAYIDALAGLGFGFIEIGTITPRPQAGNPHPRLFRIPQakAIINRMGFNNDGVDQLIENVKA 126
Cdd:PRK07259 8 GLKLKNPVMPASGtFGFGGEYARFYDLNGLGAIVTKSTTLEPREGNPTPRIAETPG--GMLNAIGLQNPGVDAFIEEELP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 127 AKfkgilginigKNADTPV-----ENAVDDYLICLEKV--YNYASYITVNISSPNTKnlrslQSGDAL---TELLQTLKQ 196
Cdd:PRK07259 86 WL----------EEFDTPIianvaGSTEEEYAEVAEKLskAPNVDAIELNISCPNVK-----HGGMAFgtdPELAYEVVK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 197 RQLELAEehqhyVPLVLKVAPDLDpeDIQFIAKQLLQFKIDGLIVTNTTL-------SREGVenLPHGdeAGGLSGAPVf 269
Cdd:PRK07259 151 AVKEVVK-----VPVIVKLTPNVT--DIVEIAKAAEEAGADGLSLINTLKgmaidikTRKPI--LANV--TGGLSGPAI- 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 491113019 270 eKSTACLAAFSAALKGEIPLIGVGGILSGEQAVAKKNAGASLVQVYSGlIYAGPE 324
Cdd:PRK07259 219 -KPIALRMVYQVYQAVDIPIIGMGGISSAEDAIEFIMAGASAVQVGTA-NFYDPY 271
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
44-323 |
6.16e-17 |
|
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: 79.68 E-value: 6.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 44 VTCMGIEFPNPVGLAAG-LDKNGAYIDALAGLGFGFIEIGTITPRPQAGNPHPRLFRIPQAKaiINRMGFNNDGVDQLIE 122
Cdd:cd04741 1 VTPPGLTISPPLMNAAGpWCTTLEDLLELAASSTGAVTTRSSTLAGRPGNPEPRYYAFPLGS--INSLGLPNLGLDYYLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 123 NVKAakfkgilgINIGKNADTP-----VENAVDDYLICLEKV----YNYASYITVNISSPNTKNLRSLQ-SGDALTELLQ 192
Cdd:cd04741 79 YIRT--------ISDGLPGSAKpffisVTGSAEDIAAMYKKIaahqKQFPLAMELNLSCPNVPGKPPPAyDFDATLEYLT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 193 TLKQrqlelaeehqHY-VPLVLKVAPDLDPEDIQFIAKQLLQFK--IDGLIVTNT-------TLSREGVEnLPHGDEAGG 262
Cdd:cd04741 151 AVKA----------AYsIPVGVKTPPYTDPAQFDTLAEALNAFAcpISFITATNTlgnglvlDPERETVV-LKPKTGFGG 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491113019 263 LSGAPVFEKSTACLAAFSAALKGEIPLIGVGGILSGEQAVAKKNAGASLVQVYSGLIYAGP 323
Cdd:cd04741 220 LAGAYLHPLALGNVRTFRRLLPSEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGP 280
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
48-325 |
6.77e-12 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 65.36 E-value: 6.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 48 GIEFPNPVGLAAGldkngAY---IDALAGLG---FGFIEIGTITPRPQAGNPHPRLFRIPQAKaiINRMGFNNDGVDQLI 121
Cdd:PRK02506 8 GFKFDNCLMNAAG-----VYcmtKEELEEVEasaAGAFVTKSATLEPRPGNPEPRYADTPLGS--INSMGLPNLGFDYYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 122 ENVKAAKFKG--------ILGINIgknadtpvenavDDYLICLEKV--YNYASYITVNISSPNTKNLRSL-----QSGDA 186
Cdd:PRK02506 81 DYVLELQKKGpnkphflsVVGLSP------------EETHTILKKIqaSDFNGLVELNLSCPNVPGKPQIaydfeTTEQI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 187 LTELLQTLKQrqlelaeehqhyvPLVLKVAPDLDPEDIQFIAKQLLQFKID----------GLIVTNTTlsrEGVENLPH 256
Cdd:PRK02506 149 LEEVFTYFTK-------------PLGVKLPPYFDIVHFDQAAAIFNKFPLAfvncinsignGLVIDPED---ETVVIKPK 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491113019 257 GDeAGGLSGAPVfeKSTAcLA---AFSAALKGEIPLIGVGGILSGEQAVAKKNAGASLVQVYSGLIYAGPEL 325
Cdd:PRK02506 213 NG-FGGIGGDYI--KPTA-LAnvrAFYQRLNPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAV 280
|
|
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
44-333 |
1.61e-08 |
|
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: 54.98 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 44 VTCMGIEFPNPVGLAAGLDKNGAY-----IDAlaglGFGFIEIGTITP-RPQAGNPHPRLFRIPqaKAIINRMGFNNdgV 117
Cdd:cd02940 4 VTFCGIKFPNPFGLASAPPTTSYPmirraFEA----GWGGAVTKTLGLdKDIVTNVSPRIARLR--TSGRGQIGFNN--I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 118 DQLIENVKAAKFKGILGINigknADTP---------VENAVDDYLICLEKVYNY-ASYITVNISSPNTKNLRSL-----Q 182
Cdd:cd02940 76 ELISEKPLEYWLKEIRELK----KDFPdkiliasimCEYNKEDWTELAKLVEEAgADALELNFSCPHGMPERGMgaavgQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 183 SGDALTELLQTLKQrqlelaeehQHYVPLVLKVAPDLdpEDIQFIAKQLLQFKIDGLIVTNTTLSREGVE-----NLPHG 257
Cdd:cd02940 152 DPELVEEICRWVRE---------AVKIPVIAKLTPNI--TDIREIARAAKEGGADGVSAINTVNSLMGVDldgtpPAPGV 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491113019 258 DE---AGGLSGAPVFEKSTACLAAFSAALKGEIPLIGVGGILSGEQAVAKKNAGASLVQVYSGLIYAGPELVQDCVNAL 333
Cdd:cd02940 221 EGkttYGGYSGPAVKPIALRAVSQIARAPEPGLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
|
|
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
210-321 |
9.60e-04 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 40.78 E-value: 9.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 210 PLVLKVApdLDPEDiqfiAKQLLQFKIDGLIVTNttlsregvenlpHGDEAggLSGAPvfekSTA-CLAAFSAALKGEIP 288
Cdd:PRK11197 247 PMVIKGI--LDPED----ARDAVRFGADGIVVSN------------HGGRQ--LDGVL----SSArALPAIADAVKGDIT 302
|
90 100 110
....*....|....*....|....*....|...
gi 491113019 289 LIGVGGILSGEQAVAKKNAGASLVQVYSGLIYA 321
Cdd:PRK11197 303 ILADSGIRNGLDVVRMIALGADTVLLGRAFVYA 335
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
282-327 |
1.78e-03 |
|
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: 39.89 E-value: 1.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 491113019 282 ALKGEIPLIGVGGILSGEQAVAKKNAGASLVQVYSGLIYaGPELVQ 327
Cdd:cd04735 280 RIAGRLPLIAVGSINTPDDALEALETGADLVAIGRGLLV-DPDWVE 324
|
|
| PcrB |
COG1646 |
Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism]; |
259-332 |
4.03e-03 |
|
Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];
Pssm-ID: 441252 Cd Length: 241 Bit Score: 38.22 E-value: 4.03e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491113019 259 EAGGLSGAPVfekSTACLAAFSAALkGEIPLIGVGGILSGEQAVAKKNAGASLVQVysG-LIYAGPELVQDCVNA 332
Cdd:COG1646 173 EYGSGAGEPV---DPEMVKAVKKAL-EDTPLIYGGGIRSPEKAREMAEAGADTIVV--GnAIEEDPDLALETVEA 241
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
185-252 |
7.11e-03 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380501 [Multi-domain] Cd Length: 266 Bit Score: 37.51 E-value: 7.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491113019 185 DALTELLQTLKQRqlelaeehqhyvPLVLKVAPDLDPEDIqfiAKQLLQFKIDGLIVTNTTLSREGVE 252
Cdd:cd06278 19 EELSRALQARGLR------------PLLFNVDDEDDVDDA---LRQLLQYRVDGVIVTSATLSSELAE 71
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
174-266 |
7.99e-03 |
|
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380465 [Multi-domain] Cd Length: 423 Bit Score: 37.95 E-value: 7.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113019 174 NTKNLR-SLQSGDALTELLQTLKQRQLELaEEHQHyVPLVlkvapdldpeDIQFIA--KQLLqfkIDGLIVtnttlsreg 250
Cdd:cd19543 290 NTLPVRvRLDPDQTVLELLKDLQAQQLEL-REHEY-VPLY----------EIQAWSegKQAL---FDHLLV--------- 345
|
90
....*....|....*.
gi 491113019 251 VENLPHGDEAGGLSGA 266
Cdd:cd19543 346 FENYPVDESLEEEQDE 361
|
|
| |
