|
Name |
Accession |
Description |
Interval |
E-value |
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
110-488 |
7.18e-163 |
|
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: 470.06 E-value: 7.18e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 110 DPESAQKLAIKVLETGLAPRD---MVDDDAVLETELFGRKLSNPIGLAAGFDKQAEAIDGLLDLGFGFIEIGSVTPEPQP 186
Cdd:cd04738 8 DPETAHRLAIRALKLGLGPPLlllLVYDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFVEVGTVTPRPQP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 187 GNPLPRYFRLIEDNACINRFGFNSQGHNVILNRLRDRIRRwllhpssvaslqdalvahpdsaradarqliathpkstsaf 266
Cdd:cd04738 88 GNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRRPR---------------------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 267 vdatdlprslrpAKMLGINLGKNKESP-EESVQDYIKGVQRLGPYADMIIVNVSSPNTPGLRRLQRRDVLQDLLTKVVNA 345
Cdd:cd04738 128 ------------GGPLGVNIGKNKDTPlEDAVEDYVIGVRKLGPYADYLVVNVSSPNTPGLRDLQGKEALRELLTAVKEE 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 346 RDGMeqshlgfsnkKVSVPLLVKIAPDLSEEELQDVADAALKSGIDGLVISNTTISRPATLRSSeNVRETGGLSGPPLKP 425
Cdd:cd04738 196 RNKL----------GKKVPLLVKIAPDLSDEELEDIADVALEHGVDGIIATNTTISRPGLLRSP-LANETGGLSGAPLKE 264
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2274522847 426 LALKALTIVNQRLQGKLPIIGCGGIASGQDALDYAKAGASAIELYTSFGYQGVGLPRRIKDEL 488
Cdd:cd04738 265 RSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTGLVYEGPGLVKRIKREL 327
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
103-496 |
1.48e-144 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 424.19 E-value: 1.48e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 103 PALKAFaDPESAQKLAIKVLETGLAP-------RDMVDDDAVLETELFGRKLSNPIGLAAGFDKQAEAIDGLLDLGFGFI 175
Cdd:PRK05286 8 PLLFKL-DPETAHELTIRALKRASRTpllsllrQRLTYTDPRLPVTVMGLTFPNPVGLAAGFDKNGEAIDALGALGFGFV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 176 EIGSVTPEPQPGNPLPRYFRLIEDNACINRFGFNSQGHNVILNRLRDRIRRWLLhpssvaslqdalvahpdsaradarql 255
Cdd:PRK05286 87 EVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKAYRGIPL-------------------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 256 iathpkstsafvdatdlprslrpakmlGINLGKNKESP-EESVQDYIKGVQRLGPYADMIIVNVSSPNTPGLRRLQRRDV 334
Cdd:PRK05286 141 ---------------------------GINIGKNKDTPlEDAVDDYLICLEKLYPYADYFTVNISSPNTPGLRDLQYGEA 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 335 LQDLLTKVVNARDGMEQShlgfsnkkvsVPLLVKIAPDLSEEELQDVADAALKSGIDGLVISNTTISRPAtLRSSENVRE 414
Cdd:PRK05286 194 LDELLAALKEAQAELHGY----------VPLLVKIAPDLSDEELDDIADLALEHGIDGVIATNTTLSRDG-LKGLPNADE 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 415 TGGLSGPPLKPLALKALTIVNQRLQGKLPIIGCGGIASGQDALDYAKAGASAIELYTSFGYQGVGLPRRIKDELVELLKA 494
Cdd:PRK05286 263 AGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGASLVQIYSGLIYEGPGLVKEIVRGLARLLRR 342
|
..
gi 2274522847 495 QG 496
Cdd:PRK05286 343 DG 344
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
110-488 |
1.41e-107 |
|
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: 328.67 E-value: 1.41e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 110 DPESAQKLAIKVLETGLA------PRDMVDDDAVLETELFGRKLSNPIGLAAGFDKQAEAIDGLLDLGFGFIEIGSVTPE 183
Cdd:TIGR01036 12 DPESAHELTFQFLRLGTGtpflalLRSLFGASDPLEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAMGFGFLEIGTVTPK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 184 PQPGNPLPRYFRLIEDNACINRFGFNSQGHNVILNRLRdrirrwllhpssvaslqdalvahpdsaradarqliATHPKst 263
Cdd:TIGR01036 92 PQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLK-----------------------------------RARYK-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 264 safvdatdLPrslrpakmLGINLGKNKESP-EESVQDYIKGVQRLGPYADMIIVNVSSPNTPGLRRLQRRDVLQDLLTKV 342
Cdd:TIGR01036 135 --------GP--------IGINIGKNKDTPsEDAKEDYAACLRKLGPLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 343 VNARDGMEQSHlgfsnkkvSVPLLVKIAPDLSEEELQDVADAALKSGIDGLVISNTTISRPaTLRSSENVRETGGLSGPP 422
Cdd:TIGR01036 199 KQEQDGLRRVH--------RVPVLVKIAPDLTESDLEDIADSLVELGIDGVIATNTTVSRS-LVQGPKNSDETGGLSGKP 269
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2274522847 423 LKPLALKALTIVNQRLQGKLPIIGCGGIASGQDALDYAKAGASAIELYTSFGYQGVGLPRRIKDEL 488
Cdd:TIGR01036 270 LQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGASLLQIYSGFIYWGPPLVKEIVKEI 335
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
138-496 |
2.02e-102 |
|
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: 313.93 E-value: 2.02e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 138 LETELFGRKLSNPIGLAAGF-DKQAEAIDGLLDLGFGFIEIGSVTPEPQPGNPLPRYFRLIEDNACINRFGFNSQGHNVI 216
Cdd:COG0167 2 LSVELAGLKFPNPVGLASGFfDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 217 LNRLRDRirrwllhpssvaslqdalvahpdsaRADARQLIathpkstsafvdatdlprslrpakmlgINLGKNkespeeS 296
Cdd:COG0167 82 LERLLPA-------------------------KRYDVPVI---------------------------VNIGGN------T 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 297 VQDYIKGVQRLGPY-ADMIIVNVSSPNTPG-LRRL-QRRDVLQDLLTKVVNARDgmeqshlgfsnkkvsVPLLVKIAPDL 373
Cdd:COG0167 104 VEDYVELARRLADAgADYLELNISCPNTPGgGRALgQDPEALAELLAAVKAATD---------------KPVLVKLAPDL 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 374 seEELQDVADAALKSGIDGLVISNTTISRPATLRSSENV--RETGGLSGPPLKPLALKALTIVNQRLQGKLPIIGCGGIA 451
Cdd:COG0167 169 --TDIVEIARAAEEAGADGVIAINTTLGRAIDLETRRPVlaNEAGGLSGPALKPIALRMVREVAQAVGGDIPIIGVGGIS 246
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2274522847 452 SGQDALDYAKAGASAIELYTSFGYQGVGLPRRIKDELVELLKAQG 496
Cdd:COG0167 247 TAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKG 291
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
137-492 |
3.62e-97 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 300.42 E-value: 3.62e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 137 VLETELFGRKLSNPIGLAAGFDKQAEAIDGLLDLG-FGFIEIGSVTPEPQPGNPLPRYFRLIEDnaCINRFGFNSQGHNV 215
Cdd:pfam01180 1 MLATKIPGLDFKNPIGLASGFDKFGEEALKWLALGkFGAIEIKSVTPYPQPGNPTPRVFRLPEG--VLNRMGLNNPGLDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 216 ILNRLRDRIRRWllhpssvaslqdalvahpdsaradarqliathpkstsafvdatdlprslrPAKMLGINLGKNKESpee 295
Cdd:pfam01180 79 VLAELLKRRKEY--------------------------------------------------PRPDLGINLSKAGMT--- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 296 sVQDYIKGVQRLGPYADMIIVNVSSPNTPGLRRLQRRDVLQDLLTKVVNARDgmeqshlgfsnkkvSVPLLVKIAPDLSE 375
Cdd:pfam01180 106 -VDDYVEVARKIGPFADYIELNVSCPNTPGLRALQTDPELAAILLKVVKEVS--------------KVPVLVKLAPDLTD 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 376 EELQDVAD-AALKSGIDGLVISNTTISRPA-TLRSSENVRE--TGGLSGPPLKPLALKALTIVNQRLQGKLPIIGCGGIA 451
Cdd:pfam01180 171 IVIIDIADvALGEDGLDGINATNTTVRGMRiDLKTEKPILAngTGGLSGPPIKPIALKVIRELYQRTGPEIPIIGVGGIE 250
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2274522847 452 SGQDALDYAKAGASAIELYTSFGYQGVGLPRRIKDELVELL 492
Cdd:pfam01180 251 SGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
110-488 |
7.18e-163 |
|
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: 470.06 E-value: 7.18e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 110 DPESAQKLAIKVLETGLAPRD---MVDDDAVLETELFGRKLSNPIGLAAGFDKQAEAIDGLLDLGFGFIEIGSVTPEPQP 186
Cdd:cd04738 8 DPETAHRLAIRALKLGLGPPLlllLVYDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFVEVGTVTPRPQP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 187 GNPLPRYFRLIEDNACINRFGFNSQGHNVILNRLRDRIRRwllhpssvaslqdalvahpdsaradarqliathpkstsaf 266
Cdd:cd04738 88 GNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRRPR---------------------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 267 vdatdlprslrpAKMLGINLGKNKESP-EESVQDYIKGVQRLGPYADMIIVNVSSPNTPGLRRLQRRDVLQDLLTKVVNA 345
Cdd:cd04738 128 ------------GGPLGVNIGKNKDTPlEDAVEDYVIGVRKLGPYADYLVVNVSSPNTPGLRDLQGKEALRELLTAVKEE 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 346 RDGMeqshlgfsnkKVSVPLLVKIAPDLSEEELQDVADAALKSGIDGLVISNTTISRPATLRSSeNVRETGGLSGPPLKP 425
Cdd:cd04738 196 RNKL----------GKKVPLLVKIAPDLSDEELEDIADVALEHGVDGIIATNTTISRPGLLRSP-LANETGGLSGAPLKE 264
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2274522847 426 LALKALTIVNQRLQGKLPIIGCGGIASGQDALDYAKAGASAIELYTSFGYQGVGLPRRIKDEL 488
Cdd:cd04738 265 RSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTGLVYEGPGLVKRIKREL 327
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
103-496 |
1.48e-144 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 424.19 E-value: 1.48e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 103 PALKAFaDPESAQKLAIKVLETGLAP-------RDMVDDDAVLETELFGRKLSNPIGLAAGFDKQAEAIDGLLDLGFGFI 175
Cdd:PRK05286 8 PLLFKL-DPETAHELTIRALKRASRTpllsllrQRLTYTDPRLPVTVMGLTFPNPVGLAAGFDKNGEAIDALGALGFGFV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 176 EIGSVTPEPQPGNPLPRYFRLIEDNACINRFGFNSQGHNVILNRLRDRIRRWLLhpssvaslqdalvahpdsaradarql 255
Cdd:PRK05286 87 EVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKAYRGIPL-------------------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 256 iathpkstsafvdatdlprslrpakmlGINLGKNKESP-EESVQDYIKGVQRLGPYADMIIVNVSSPNTPGLRRLQRRDV 334
Cdd:PRK05286 141 ---------------------------GINIGKNKDTPlEDAVDDYLICLEKLYPYADYFTVNISSPNTPGLRDLQYGEA 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 335 LQDLLTKVVNARDGMEQShlgfsnkkvsVPLLVKIAPDLSEEELQDVADAALKSGIDGLVISNTTISRPAtLRSSENVRE 414
Cdd:PRK05286 194 LDELLAALKEAQAELHGY----------VPLLVKIAPDLSDEELDDIADLALEHGIDGVIATNTTLSRDG-LKGLPNADE 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 415 TGGLSGPPLKPLALKALTIVNQRLQGKLPIIGCGGIASGQDALDYAKAGASAIELYTSFGYQGVGLPRRIKDELVELLKA 494
Cdd:PRK05286 263 AGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGASLVQIYSGLIYEGPGLVKEIVRGLARLLRR 342
|
..
gi 2274522847 495 QG 496
Cdd:PRK05286 343 DG 344
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
103-504 |
1.99e-142 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 421.07 E-value: 1.99e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 103 PALKAFaDPESAQKLAIKVLETGLAPRDMVDDDAVLETELFGRKLSNPIGLAAGFDKQAEAIDGLLDLGFGFIEIGSVTP 182
Cdd:PLN02826 40 PLFRLL-DPETAHSLAISAAARGLVPREKRPDPSVLGVEVWGRTFSNPIGLAAGFDKNAEAVEGLLGLGFGFVEIGSVTP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 183 EPQPGNPLPRYFRLIEDNACINRFGFNSQGHNVILNRLRDRIRRWLLHPSSVASLQDALVAHPDSARADarqliathpks 262
Cdd:PLN02826 119 LPQPGNPKPRVFRLREEGAIINRYGFNSEGIVAVAKRLGAQHGKRKLDETSSSSFSSDDVKAGGKAGPG----------- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 263 tsafvdatdlprslrpakMLGINLGKNKESpEESVQDYIKGVQRLGPYADMIIVNVSSPNTPGLRRLQRRDVLQDLLTKV 342
Cdd:PLN02826 188 ------------------ILGVNLGKNKTS-EDAAADYVQGVRALSQYADYLVINVSSPNTPGLRKLQGRKQLKDLLKKV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 343 VNARDGMEQSHLGfsnkkvSVPLLVKIAPDLSEEELQDVADAALKSGIDGLVISNTTISRPATLRSSENVRETGGLSGPP 422
Cdd:PLN02826 249 LAARDEMQWGEEG------PPPLLVKIAPDLSKEDLEDIAAVALALGIDGLIISNTTISRPDSVLGHPHADEAGGLSGKP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 423 LKPLALKALTIVNQRLQGKLPIIGCGGIASGQDALDYAKAGASAIELYTSFGYQGVGLPRRIKDELVELLKAQG-KTWKQ 501
Cdd:PLN02826 323 LFDLSTEVLREMYRLTRGKIPLVGCGGVSSGEDAYKKIRAGASLVQLYTAFAYEGPALIPRIKAELAACLERDGfKSIQE 402
|
...
gi 2274522847 502 VVG 504
Cdd:PLN02826 403 AVG 405
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
110-488 |
1.41e-107 |
|
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: 328.67 E-value: 1.41e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 110 DPESAQKLAIKVLETGLA------PRDMVDDDAVLETELFGRKLSNPIGLAAGFDKQAEAIDGLLDLGFGFIEIGSVTPE 183
Cdd:TIGR01036 12 DPESAHELTFQFLRLGTGtpflalLRSLFGASDPLEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAMGFGFLEIGTVTPK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 184 PQPGNPLPRYFRLIEDNACINRFGFNSQGHNVILNRLRdrirrwllhpssvaslqdalvahpdsaradarqliATHPKst 263
Cdd:TIGR01036 92 PQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLK-----------------------------------RARYK-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 264 safvdatdLPrslrpakmLGINLGKNKESP-EESVQDYIKGVQRLGPYADMIIVNVSSPNTPGLRRLQRRDVLQDLLTKV 342
Cdd:TIGR01036 135 --------GP--------IGINIGKNKDTPsEDAKEDYAACLRKLGPLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 343 VNARDGMEQSHlgfsnkkvSVPLLVKIAPDLSEEELQDVADAALKSGIDGLVISNTTISRPaTLRSSENVRETGGLSGPP 422
Cdd:TIGR01036 199 KQEQDGLRRVH--------RVPVLVKIAPDLTESDLEDIADSLVELGIDGVIATNTTVSRS-LVQGPKNSDETGGLSGKP 269
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2274522847 423 LKPLALKALTIVNQRLQGKLPIIGCGGIASGQDALDYAKAGASAIELYTSFGYQGVGLPRRIKDEL 488
Cdd:TIGR01036 270 LQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGASLLQIYSGFIYWGPPLVKEIVKEI 335
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
138-496 |
2.02e-102 |
|
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: 313.93 E-value: 2.02e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 138 LETELFGRKLSNPIGLAAGF-DKQAEAIDGLLDLGFGFIEIGSVTPEPQPGNPLPRYFRLIEDNACINRFGFNSQGHNVI 216
Cdd:COG0167 2 LSVELAGLKFPNPVGLASGFfDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 217 LNRLRDRirrwllhpssvaslqdalvahpdsaRADARQLIathpkstsafvdatdlprslrpakmlgINLGKNkespeeS 296
Cdd:COG0167 82 LERLLPA-------------------------KRYDVPVI---------------------------VNIGGN------T 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 297 VQDYIKGVQRLGPY-ADMIIVNVSSPNTPG-LRRL-QRRDVLQDLLTKVVNARDgmeqshlgfsnkkvsVPLLVKIAPDL 373
Cdd:COG0167 104 VEDYVELARRLADAgADYLELNISCPNTPGgGRALgQDPEALAELLAAVKAATD---------------KPVLVKLAPDL 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 374 seEELQDVADAALKSGIDGLVISNTTISRPATLRSSENV--RETGGLSGPPLKPLALKALTIVNQRLQGKLPIIGCGGIA 451
Cdd:COG0167 169 --TDIVEIARAAEEAGADGVIAINTTLGRAIDLETRRPVlaNEAGGLSGPALKPIALRMVREVAQAVGGDIPIIGVGGIS 246
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2274522847 452 SGQDALDYAKAGASAIELYTSFGYQGVGLPRRIKDELVELLKAQG 496
Cdd:COG0167 247 TAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKG 291
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
137-492 |
3.62e-97 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 300.42 E-value: 3.62e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 137 VLETELFGRKLSNPIGLAAGFDKQAEAIDGLLDLG-FGFIEIGSVTPEPQPGNPLPRYFRLIEDnaCINRFGFNSQGHNV 215
Cdd:pfam01180 1 MLATKIPGLDFKNPIGLASGFDKFGEEALKWLALGkFGAIEIKSVTPYPQPGNPTPRVFRLPEG--VLNRMGLNNPGLDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 216 ILNRLRDRIRRWllhpssvaslqdalvahpdsaradarqliathpkstsafvdatdlprslrPAKMLGINLGKNKESpee 295
Cdd:pfam01180 79 VLAELLKRRKEY--------------------------------------------------PRPDLGINLSKAGMT--- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 296 sVQDYIKGVQRLGPYADMIIVNVSSPNTPGLRRLQRRDVLQDLLTKVVNARDgmeqshlgfsnkkvSVPLLVKIAPDLSE 375
Cdd:pfam01180 106 -VDDYVEVARKIGPFADYIELNVSCPNTPGLRALQTDPELAAILLKVVKEVS--------------KVPVLVKLAPDLTD 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 376 EELQDVAD-AALKSGIDGLVISNTTISRPA-TLRSSENVRE--TGGLSGPPLKPLALKALTIVNQRLQGKLPIIGCGGIA 451
Cdd:pfam01180 171 IVIIDIADvALGEDGLDGINATNTTVRGMRiDLKTEKPILAngTGGLSGPPIKPIALKVIRELYQRTGPEIPIIGVGGIE 250
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2274522847 452 SGQDALDYAKAGASAIELYTSFGYQGVGLPRRIKDELVELL 492
Cdd:pfam01180 251 SGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
140-487 |
2.41e-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: 203.74 E-value: 2.41e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 140 TELFGRKLSNPIGLAAGFDKQA-EAIDGLLDLGFGFIEIGSVTPEPQPGNPLPRYFRL-------IEDNACINRFGFNSQ 211
Cdd:cd02810 1 VNFLGLKLKNPFGVAAGPLLKTgELIARAAAAGFGAVVYKTVTLHPRPGNPLPRVARLppegesyPEQLGILNSFGLPNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 212 GhnvilnrlrdrIRRWLlhpssvaslQDALVAHPDsaradarqliathpkstsafvdATDLPrslrpakmLGINLGKNke 291
Cdd:cd02810 81 G-----------LDVWL---------QDIAKAKKE----------------------FPGQP--------LIASVGGS-- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 292 SPEESVQDYIKgVQRLGpyADMIIVNVSSPNTPGLRRL-QRRDVLQDLLTKVVNArdgmeqshlgfsnkkVSVPLLVKIA 370
Cdd:cd02810 109 SKEDYVELARK-IERAG--AKALELNLSCPNVGGGRQLgQDPEAVANLLKAVKAA---------------VDIPLLVKLS 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 371 PDLSEEELQDVADAALKSGIDGLVISNTTISRPATLRSSE--NVRETGGLSGPPLKPLALKALTIVNQRLQGKLPIIGCG 448
Cdd:cd02810 171 PYFDLEDIVELAKAAERAGADGLTAINTISGRVVDLKTVGpgPKRGTGGLSGAPIRPLALRWVARLAARLQLDIPIIGVG 250
|
330 340 350
....*....|....*....|....*....|....*....
gi 2274522847 449 GIASGQDALDYAKAGASAIELYTSFGYQGVGLPRRIKDE 487
Cdd:cd02810 251 GIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKIKKE 289
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
139-504 |
1.20e-35 |
|
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: 136.14 E-value: 1.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 139 ETELFGRKLSNPIGLAAGFDKQAEAIDGLLDLG-FGFIEIGSVTPEPQPGNPLPRyfrLIEDNAC-INRFGFNSQGHNVI 216
Cdd:cd04740 1 SVELAGLRLKNPVILASGTFGFGEELSRVADLGkLGAIVTKSITLEPREGNPPPR---VVETPGGmLNAIGLQNPGVEAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 217 LNRLRDRIRRWllhpssvaslqdalvahpdsaradARQLIAthpkSTSAfvdatdlprslrpakmlginlgknkespeES 296
Cdd:cd04740 78 LEELLPWLREF------------------------GTPVIA----SIAG-----------------------------ST 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 297 VQDYIKGVQRLGPY-ADMIIVNVSSPNTPGLRRL--QRRDVLQDLLTKVVnardgmeqshlgfsnKKVSVPLLVKIAPDL 373
Cdd:cd04740 101 VEEFVEVAEKLADAgADAIELNISCPNVKGGGMAfgTDPEAVAEIVKAVK---------------KATDVPVIVKLTPNV 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 374 SeeELQDVADAALKSGIDGLVISNT-------TISRPATLrssENVreTGGLSGPPLKPLALKALTIVNQRLqgKLPIIG 446
Cdd:cd04740 166 T--DIVEIARAAEEAGADGLTLINTlkgmaidIETRKPIL---GNV--TGGLSGPAIKPIALRMVYQVYKAV--EIPIIG 236
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2274522847 447 CGGIASGQDALDYAKAGASAIELYTSfGYQGVGLPRRIKDELVELLKAQG-KTWKQVVG 504
Cdd:cd04740 237 VGGIASGEDALEFLMAGASAVQVGTA-NFVDPEAFKEIIEGLEAYLDEEGiKSIEELVG 294
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
138-504 |
2.50e-33 |
|
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: 129.86 E-value: 2.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 138 LETELFGRKLSNPIGLAAG-FDKQAEAIDGLLDLGFGFIEIGSVTPEPQPGNPLPRyfrlIEDNAC--INRFGFNSQGHN 214
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGiMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPT----IVETPCgmLNAIGLQNPGVE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 215 VILNRLRDRIRrwllhpssvaslqdalvahpdsaradarqliathpkstsafvdatDLPRSLrPAKMLGinlgknkESPE 294
Cdd:TIGR01037 77 AFLEELKPVRE---------------------------------------------EFPTPL-IASVYG-------SSVE 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 295 ESVqDYIKGVQRLGPYADMIIVNVSSPN--TPGLRRLQRRDVLQDLLTKVvnardgmeqshlgfsNKKVSVPLLVKIAPD 372
Cdd:TIGR01037 104 EFA-EVAEKLEKAPPYVDAYELNLSCPHvkGGGIAIGQDPELSADVVKAV---------------KDKTDVPVFAKLSPN 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 373 LSEeeLQDVADAALKSGIDGLVISNTTISRPATLRSSENV--RETGGLSGPPLKPLALKALTIVNQRLQgkLPIIGCGGI 450
Cdd:TIGR01037 168 VTD--ITEIAKAAEEAGADGLTLINTLRGMKIDIKTGKPIlaNKTGGLSGPAIKPIALRMVYDVYKMVD--IPIIGVGGI 243
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2274522847 451 ASGQDALDYAKAGASAIELYTSFGYQGVgLPRRIKDELVELLKAQG-KTWKQVVG 504
Cdd:TIGR01037 244 TSFEDALEFLMAGASAVQVGTAVYYRGF-AFKKIIEGLIAFLKAEGfTSIEELIG 297
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
138-504 |
7.78e-29 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 116.79 E-value: 7.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 138 LETELFGRKLSNPIGLAAG-FDKQAEAIDgLLDL-GFGFIEIGSVTPEPQPGNPLPRYFRLieDNACINRFGFNSQGHNV 215
Cdd:PRK07259 2 LSVELPGLKLKNPVMPASGtFGFGGEYAR-FYDLnGLGAIVTKSTTLEPREGNPTPRIAET--PGGMLNAIGLQNPGVDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 216 ILNRLRDRIRRWLLHpssvaslqdalvahpdsaradarqLIAthpkstSAFvdatdlprslrpakmlginlGknkESPEE 295
Cdd:PRK07259 79 FIEEELPWLEEFDTP------------------------IIA------NVA--------------------G---STEEE 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 296 svqdYIKGVQRLGPY--ADMIIVNVSSPNTP--GLRRLQRRDVLQDLLTKVVNArdgmeqshlgfsnkkVSVPLLVKIAP 371
Cdd:PRK07259 106 ----YAEVAEKLSKApnVDAIELNISCPNVKhgGMAFGTDPELAYEVVKAVKEV---------------VKVPVIVKLTP 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 372 DLSEeeLQDVADAALKSGIDGLVISNTTIS--------RPATlrssENVreTGGLSGPPLKPLALKALTIVNQRLqgKLP 443
Cdd:PRK07259 167 NVTD--IVEIAKAAEEAGADGLSLINTLKGmaidiktrKPIL----ANV--TGGLSGPAIKPIALRMVYQVYQAV--DIP 236
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2274522847 444 IIGCGGIASGQDALDYAKAGASAIELYTSFgYQGVGLPRRIKDELVELLKAQG-KTWKQVVG 504
Cdd:PRK07259 237 IIGMGGISSAEDAIEFIMAGASAVQVGTAN-FYDPYAFPKIIEGLEAYLDKYGiKSIEEIVG 297
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
144-492 |
3.04e-18 |
|
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: 85.84 E-value: 3.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 144 GRKLSNPIGLAAG-FDKQAEAIDGLLDLGFGFIEIGSVTPEPQPGNPLPRYFRLieDNACINRFGFNSQGHNVILNRLRD 222
Cdd:cd04741 5 GLTISPPLMNAAGpWCTTLEDLLELAASSTGAVTTRSSTLAGRPGNPEPRYYAF--PLGSINSLGLPNLGLDYYLEYIRT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 223 RirrwllhpssvaslqdalvahPDSARADARQLIAThpkstsafvdatdlprslrpakMLGinlgknkeSPEESVQDYIK 302
Cdd:cd04741 83 I---------------------SDGLPGSAKPFFIS----------------------VTG--------SAEDIAAMYKK 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 303 GVQRLGPYADMIIVNVSSPNTPGL-RRLQRRDVLQDLLTKVVNArdgmeqshlgfsnkkVSVPLLVKIAPDLSEEELQDV 381
Cdd:cd04741 112 IAAHQKQFPLAMELNLSCPNVPGKpPPAYDFDATLEYLTAVKAA---------------YSIPVGVKTPPYTDPAQFDTL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 382 ADA--ALKSGI----------DGLVIsnTTISRPATLRSSENVretGGLSGPPLKPLALKALTIVNQRLQGKLPIIGCGG 449
Cdd:cd04741 177 AEAlnAFACPIsfitatntlgNGLVL--DPERETVVLKPKTGF---GGLAGAYLHPLALGNVRTFRRLLPSEIQIIGVGG 251
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2274522847 450 IASGQDALDYAKAGASAIELYTSFGYQGVGLPRRIKDELVELL 492
Cdd:cd04741 252 VLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEKELEDIW 294
|
|
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
301-488 |
2.74e-16 |
|
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: 80.02 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 301 IKGVQRLGpyADMIIVNVSSPNTPGLRRLQRrDVLQD--LLTKVVnardgmeqshlGFSNKKVSVPLLVKIAPDLSEeeL 378
Cdd:cd02940 119 AKLVEEAG--ADALELNFSCPHGMPERGMGA-AVGQDpeLVEEIC-----------RWVREAVKIPVIAKLTPNITD--I 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 379 QDVADAALKSGIDGLVISNTTIS----RPATLRSSENV--RET-GGLSGPPLKPLALKALTIVNQRLQGKLPIIGCGGIA 451
Cdd:cd02940 183 REIARAAKEGGADGVSAINTVNSlmgvDLDGTPPAPGVegKTTyGGYSGPAVKPIALRAVSQIARAPEPGLPISGIGGIE 262
|
170 180 190
....*....|....*....|....*....|....*..
gi 2274522847 452 SGQDALDYAKAGASAIELYTSFGYQGVGLPRRIKDEL 488
Cdd:cd02940 263 SWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
138-498 |
1.29e-15 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 78.07 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 138 LETELFGRKLSNPIGLAAG-FDKQAEAIDGLLDLGFGFIEIGSVTPEPQPGNPLPRYFRLieDNACINRFGFNSQGHNVI 216
Cdd:PRK02506 2 TSTQIAGFKFDNCLMNAAGvYCMTKEELEEVEASAAGAFVTKSATLEPRPGNPEPRYADT--PLGSINSMGLPNLGFDYY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 217 LNRLRDRirrwllhpssvaslqdalvahpdsaradarqliATHPKSTSAFVDATDLprslrpakmlginlgknkeSPEES 296
Cdd:PRK02506 80 LDYVLEL---------------------------------QKKGPNKPHFLSVVGL-------------------SPEET 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 297 VqDYIKGVQRLGpYADMIIVNVSSPNTPGLRRLQRR-DVLQDLLTKVvnardgmeqshlgFS-NKKvsvPLLVKIAPDLS 374
Cdd:PRK02506 108 H-TILKKIQASD-FNGLVELNLSCPNVPGKPQIAYDfETTEQILEEV-------------FTyFTK---PLGVKLPPYFD 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 375 EEELqDVADAALK-----------SGIDGLVI---SNTTISRPATlrssenvrETGGLSGPPLKPLALKALTIVNQRLQG 440
Cdd:PRK02506 170 IVHF-DQAAAIFNkfplafvncinSIGNGLVIdpeDETVVIKPKN--------GFGGIGGDYIKPTALANVRAFYQRLNP 240
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2274522847 441 KLPIIGCGGIASGQDALDYAKAGASAIELYTSFGYQGVGLPRRIKDELVELLKAQGKT 498
Cdd:PRK02506 241 SIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAIMAEKGYQ 298
|
|
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
355-496 |
4.09e-10 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 62.16 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 355 GFSNKKVSVPLLVKIAPDLSEeeLQDVADAALKSGIDGLVISNTTISRPA----TLR---SSENVRETGGLSGPPLKPLA 427
Cdd:PLN02495 175 GWINAKATVPVWAKMTPNITD--ITQPARVALKSGCEGVAAINTIMSVMGinldTLRpepCVEGYSTPGGYSSKAVRPIA 252
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2274522847 428 LKALTIVNQRLQGKLP----IIGCGGIASGQDALDYAKAGASAIELYTSFGYQGVGLPRRIKDELVELLKAQG 496
Cdd:PLN02495 253 LAKVMAIAKMMKSEFPedrsLSGIGGVETGGDAAEFILLGADTVQVCTGVMMHGYPLVKNLCAELQDFMKKHN 325
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
361-492 |
6.33e-07 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 52.25 E-value: 6.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 361 VSVPLLVKIAPDLSEeeLQDVADAALKSGIDGLVISNTT-------ISRPATLRSSENVRETGGLSGPPLKPLALKALTI 433
Cdd:PRK08318 167 SRLPVIVKLTPNITD--IREPARAAKRGGADAVSLINTInsitgvdLDRMIPMPIVNGKSSHGGYCGPAVKPIALNMVAE 244
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2274522847 434 V--NQRLQGkLPIIGCGGIASGQDALDYAKAGASAIELYTS---FGYqgvglprRIKDELVELL 492
Cdd:PRK08318 245 IarDPETRG-LPISGIGGIETWRDAAEFILLGAGTVQVCTAamqYGF-------RIVEDMISGL 300
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
359-466 |
1.57e-05 |
|
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only]; FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440915 [Multi-domain] Cd Length: 357 Bit Score: 47.43 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 359 KKVSVPLLVKiapdlseeELQDVADA--ALKSGIDGLVISNTtisrpatlrssenvretGG--L-SGPPlkplALKALTI 433
Cdd:COG1304 222 ERWPGPLIVK--------GVLSPEDArrAVDAGVDGIDVSNH-----------------GGrqLdGGPP----TIDALPE 272
|
90 100 110
....*....|....*....|....*....|....*.
gi 2274522847 434 VNQRLQGKLPIIGCGGIASGQDAldyAKA---GASA 466
Cdd:COG1304 273 IRAAVGGRIPVIADGGIRRGLDV---AKAlalGADA 305
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
371-473 |
8.43e-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: 38.73 E-value: 8.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274522847 371 PDLSEEELQDVADAALKSGIDGLVISnttisrpatLRSSENVRETGGLSGPPLKPLalkaltiVNQRLQGKLPIIGCGGI 450
Cdd:cd04735 230 PGIRMEDTLALVDKLADKGLDYLHIS---------LWDFDRKSRRGRDDNQTIMEL-------VKERIAGRLPLIAVGSI 293
|
90 100
....*....|....*....|...
gi 2274522847 451 ASGQDALDYAKAGASAIELYTSF 473
Cdd:cd04735 294 NTPDDALEALETGADLVAIGRGL 316
|
|
| |
