|
Name |
Accession |
Description |
Interval |
E-value |
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
2-332 |
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: 526.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 2 PALQRLLDPESAHRLAVRVISLGLLPRATF---QDSNMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKLGFGFVEVGS 78
Cdd:cd04738 1 RPLLFLLDPETAHRLAIRALKLGLGPPLLLllvYDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFVEVGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 79 VTPQPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSAVEHRLRARQQKqtqlttdGLPLGINLGKNKTS--VDAAADYVEG 156
Cdd:cd04738 81 VTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRRPR-------GGPLGVNIGKNKDTplEDAVEDYVIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 157 VRILGPLADYLVVNVSSPNTAGLRSLQGKTELRRLLSKVLQERDALKGPqkPAVLVKIAPDLTAQDKEDIASVARELGID 236
Cdd:cd04738 154 VRKLGPYADYLVVNVSSPNTPGLRDLQGKEALRELLTAVKEERNKLGKK--VPLLVKIAPDLSDEELEDIADVALEHGVD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 237 GLIITNTTVSRPVGLQGALRSETGGLSGKPLRDLSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTA 316
Cdd:cd04738 232 GIIATNTTISRPGLLRSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTG 311
|
330
....*....|....*.
gi 1907190513 317 LTFLGPPVVARVKREL 332
Cdd:cd04738 312 LVYEGPGLVKRIKREL 327
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
4-353 |
1.57e-173 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 488.48 E-value: 1.57e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 4 LQRLLDPESAHRLAVRVISLGLLPRATFQDSNMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKLGFGFVEVGSVTPQP 83
Cdd:PLN02826 41 LFRLLDPETAHSLAISAAARGLVPREKRPDPSVLGVEVWGRTFSNPIGLAAGFDKNAEAVEGLLGLGFGFVEIGSVTPLP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 84 QEGNPRPRVFRLPEDQAVINRYGFNSHGLSAVEHRLRARQQKQTQLTTDGL----------------PLGINLGKNKTSV 147
Cdd:PLN02826 121 QPGNPKPRVFRLREEGAIINRYGFNSEGIVAVAKRLGAQHGKRKLDETSSSsfssddvkaggkagpgILGVNLGKNKTSE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 148 DAAADYVEGVRILGPLADYLVVNVSSPNTAGLRSLQGKTELRRLLSKVLQERDALKGPQ--KPAVLVKIAPDLTAQDKED 225
Cdd:PLN02826 201 DAAADYVQGVRALSQYADYLVINVSSPNTPGLRKLQGRKQLKDLLKKVLAARDEMQWGEegPPPLLVKIAPDLSKEDLED 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 226 IASVARELGIDGLIITNTTVSRPVG-LQGALRSETGGLSGKPLRDLSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKI 304
Cdd:PLN02826 281 IAAVALALGIDGLIISNTTISRPDSvLGHPHADEAGGLSGKPLFDLSTEVLREMYRLTRGKIPLVGCGGVSSGEDAYKKI 360
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1907190513 305 QAGASLVQLYTALTFLGPPVVARVKRELEALLKERGFNTVTDAIGVDHR 353
Cdd:PLN02826 361 RAGASLVQLYTAFAYEGPALIPRIKAELAACLERDGFKSIQEAVGADHR 409
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
1-332 |
1.59e-166 |
|
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: 467.72 E-value: 1.59e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 1 MPALQRLLDPESAHRLAVRVISLG------LLPRATFQDSNMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKLGFGFV 74
Cdd:TIGR01036 4 VRKLLFLLDPESAHELTFQFLRLGtgtpflALLRSLFGASDPLEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAMGFGFL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 75 EVGSVTPQPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSAVEHRLRArqqkqtqlTTDGLPLGINLGKNK--TSVDAAAD 152
Cdd:TIGR01036 84 EIGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLKR--------ARYKGPIGINIGKNKdtPSEDAKED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 153 YVEGVRILGPLADYLVVNVSSPNTAGLRSLQGKTELRRLLSKVLQERDALKGPQKPAVLVKIAPDLTAQDKEDIASVARE 232
Cdd:TIGR01036 156 YAACLRKLGPLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAVKQEQDGLRRVHRVPVLVKIAPDLTESDLEDIADSLVE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 233 LGIDGLIITNTTVSRPvGLQGALRS-ETGGLSGKPLRDLSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKIQAGASLV 311
Cdd:TIGR01036 236 LGIDGVIATNTTVSRS-LVQGPKNSdETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGASLL 314
|
330 340
....*....|....*....|.
gi 1907190513 312 QLYTALTFLGPPVVARVKREL 332
Cdd:TIGR01036 315 QIYSGFIYWGPPLVKEIVKEI 335
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
36-336 |
4.57e-135 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 386.32 E-value: 4.57e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 36 MLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKLG-FGFVEVGSVTPQPQEGNPRPRVFRLPEDqaVINRYGFNSHGLSA 114
Cdd:pfam01180 1 MLATKIPGLDFKNPIGLASGFDKFGEEALKWLALGkFGAIEIKSVTPYPQPGNPTPRVFRLPEG--VLNRMGLNNPGLDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 115 VEHRLRARQQKQTQLttdglPLGINLGKNKTSVDaaaDYVEGVRILGPLADYLVVNVSSPNTAGLRSLQGKTELRRLLSK 194
Cdd:pfam01180 79 VLAELLKRRKEYPRP-----DLGINLSKAGMTVD---DYVEVARKIGPFADYIELNVSCPNTPGLRALQTDPELAAILLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 195 VLQERDalkgpqKPAVLVKIAPDLTAQDKEDIASVAR-ELGIDGLIITNTTVSRPV----GLQGALRSETGGLSGKPLRD 269
Cdd:pfam01180 151 VVKEVS------KVPVLVKLAPDLTDIVIIDIADVALgEDGLDGINATNTTVRGMRidlkTEKPILANGTGGLSGPPIKP 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907190513 270 LSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVKRELEALL 336
Cdd:pfam01180 225 IALKVIRELYQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
37-344 |
2.01e-122 |
|
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: 354.38 E-value: 2.01e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 37 LEVRVLGHKFRNPVGIAAGF-DKHGEAVDGLYKLGFGFVEVGSVTPQPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSAV 115
Cdd:COG0167 2 LSVELAGLKFPNPVGLASGFfDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 116 EHRLRARQQKQTqlttdglPLGINLGKNktsvdAAADYVEGVRILGPL-ADYLVVNVSSPNTAG-LRSL-QGKTELRRLL 192
Cdd:COG0167 82 LERLLPAKRYDV-------PVIVNIGGN-----TVEDYVELARRLADAgADYLELNISCPNTPGgGRALgQDPEALAELL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 193 SKVLQERDalkgpqKPaVLVKIAPDLTaqDKEDIASVARELGIDGLIITNTTVSRPVGLQG---ALRSETGGLSGKPLRD 269
Cdd:COG0167 150 AAVKAATD------KP-VLVKLAPDLT--DIVEIARAAEEAGADGVIAINTTLGRAIDLETrrpVLANEAGGLSGPALKP 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907190513 270 LSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVKRELEALLKERGFNTV 344
Cdd:COG0167 221 IALRMVREVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSI 295
|
|
| dihydoor_dh_Arch |
NF041011 |
dihydroorotate dehydrogenase PyrD; |
39-353 |
1.73e-33 |
|
dihydroorotate dehydrogenase PyrD;
Pssm-ID: 468940 Cd Length: 289 Bit Score: 125.43 E-value: 1.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 39 VRVLGHKFRNPVGIAAG-FDKHGEAVDGLYKL-GFGFVEVGSVTPQPQEGNPRPRVFRLPeDQAVINRYGFNSHGLSAVE 116
Cdd:NF041011 1 IRLAGLELEDPLIIASGiLPDVPEYIERVCEKyGPSAITTKTLTLNPLEPHKPPTVVKLH-DGCYLNAIGLGNPGIGLLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 117 hrlrarqqkqtQLTTDGLPLGINLGKNktSVDaaaDYVEGVRILGPLADYLVVNVSSPNTAGLrslqgKTELRRLLSKVL 196
Cdd:NF041011 80 -----------EIRVKLCPLIVSIGGS--SLE---EIVEVAEIAEEKADAIELNLSSPNRKGY-----GASLASLVREIV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 197 QErdaLKGPQKPAVLVKIAPdltaQDK-EDIASVARELGIDGLIITNTT--------VSRPVglqgaLRSETGGLSGKPL 267
Cdd:NF041011 139 KA---VKSVVKKPVFVKLGP----WDNvLEIAGKALEAGADGLTLINTVkgmaidveSFKPV-----LSYGTGGISGKCI 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 268 RDLSTQTIREMYAltQGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVKRELEALLKERGFNtVTDA 347
Cdd:NF041011 207 HPLAVRIIYDVYR--EYEAEIIGVGGVFSWRDAIELMSVGAKAVGVGTAIIDKGLSVISEIRKGLEEYLEEKGLK-LEDI 283
|
....*.
gi 1907190513 348 IGVDHR 353
Cdd:NF041011 284 IGIAVK 289
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
2-332 |
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: 526.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 2 PALQRLLDPESAHRLAVRVISLGLLPRATF---QDSNMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKLGFGFVEVGS 78
Cdd:cd04738 1 RPLLFLLDPETAHRLAIRALKLGLGPPLLLllvYDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFVEVGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 79 VTPQPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSAVEHRLRARQQKqtqlttdGLPLGINLGKNKTS--VDAAADYVEG 156
Cdd:cd04738 81 VTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRRPR-------GGPLGVNIGKNKDTplEDAVEDYVIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 157 VRILGPLADYLVVNVSSPNTAGLRSLQGKTELRRLLSKVLQERDALKGPqkPAVLVKIAPDLTAQDKEDIASVARELGID 236
Cdd:cd04738 154 VRKLGPYADYLVVNVSSPNTPGLRDLQGKEALRELLTAVKEERNKLGKK--VPLLVKIAPDLSDEELEDIADVALEHGVD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 237 GLIITNTTVSRPVGLQGALRSETGGLSGKPLRDLSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTA 316
Cdd:cd04738 232 GIIATNTTISRPGLLRSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTG 311
|
330
....*....|....*.
gi 1907190513 317 LTFLGPPVVARVKREL 332
Cdd:cd04738 312 LVYEGPGLVKRIKREL 327
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
4-353 |
1.57e-173 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 488.48 E-value: 1.57e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 4 LQRLLDPESAHRLAVRVISLGLLPRATFQDSNMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKLGFGFVEVGSVTPQP 83
Cdd:PLN02826 41 LFRLLDPETAHSLAISAAARGLVPREKRPDPSVLGVEVWGRTFSNPIGLAAGFDKNAEAVEGLLGLGFGFVEIGSVTPLP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 84 QEGNPRPRVFRLPEDQAVINRYGFNSHGLSAVEHRLRARQQKQTQLTTDGL----------------PLGINLGKNKTSV 147
Cdd:PLN02826 121 QPGNPKPRVFRLREEGAIINRYGFNSEGIVAVAKRLGAQHGKRKLDETSSSsfssddvkaggkagpgILGVNLGKNKTSE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 148 DAAADYVEGVRILGPLADYLVVNVSSPNTAGLRSLQGKTELRRLLSKVLQERDALKGPQ--KPAVLVKIAPDLTAQDKED 225
Cdd:PLN02826 201 DAAADYVQGVRALSQYADYLVINVSSPNTPGLRKLQGRKQLKDLLKKVLAARDEMQWGEegPPPLLVKIAPDLSKEDLED 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 226 IASVARELGIDGLIITNTTVSRPVG-LQGALRSETGGLSGKPLRDLSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKI 304
Cdd:PLN02826 281 IAAVALALGIDGLIISNTTISRPDSvLGHPHADEAGGLSGKPLFDLSTEVLREMYRLTRGKIPLVGCGGVSSGEDAYKKI 360
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1907190513 305 QAGASLVQLYTALTFLGPPVVARVKRELEALLKERGFNTVTDAIGVDHR 353
Cdd:PLN02826 361 RAGASLVQLYTAFAYEGPALIPRIKAELAACLERDGFKSIQEAVGADHR 409
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
2-340 |
1.64e-168 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 473.11 E-value: 1.64e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 2 PALqRLLDPESAHRLAVRVISLGLLPRATFQ-------DSNMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKLGFGFV 74
Cdd:PRK05286 8 PLL-FKLDPETAHELTIRALKRASRTPLLSLlrqrltyTDPRLPVTVMGLTFPNPVGLAAGFDKNGEAIDALGALGFGFV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 75 EVGSVTPQPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSAVEHRLRARQQkqtqlttdGLPLGINLGKNKTSV--DAAAD 152
Cdd:PRK05286 87 EVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKAYR--------GIPLGINIGKNKDTPleDAVDD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 153 YVEGVRILGPLADYLVVNVSSPNTAGLRSLQGKTELRRLLSKVLQERDALKGPqKPaVLVKIAPDLTAQDKEDIASVARE 232
Cdd:PRK05286 159 YLICLEKLYPYADYFTVNISSPNTPGLRDLQYGEALDELLAALKEAQAELHGY-VP-LLVKIAPDLSDEELDDIADLALE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 233 LGIDGLIITNTTVSRPvGLQG-ALRSETGGLSGKPLRDLSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKIQAGASLV 311
Cdd:PRK05286 237 HGIDGVIATNTTLSRD-GLKGlPNADEAGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGASLV 315
|
330 340
....*....|....*....|....*....
gi 1907190513 312 QLYTALTFLGPPVVARVKRELEALLKERG 340
Cdd:PRK05286 316 QIYSGLIYEGPGLVKEIVRGLARLLRRDG 344
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
1-332 |
1.59e-166 |
|
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: 467.72 E-value: 1.59e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 1 MPALQRLLDPESAHRLAVRVISLG------LLPRATFQDSNMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKLGFGFV 74
Cdd:TIGR01036 4 VRKLLFLLDPESAHELTFQFLRLGtgtpflALLRSLFGASDPLEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAMGFGFL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 75 EVGSVTPQPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSAVEHRLRArqqkqtqlTTDGLPLGINLGKNK--TSVDAAAD 152
Cdd:TIGR01036 84 EIGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLKR--------ARYKGPIGINIGKNKdtPSEDAKED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 153 YVEGVRILGPLADYLVVNVSSPNTAGLRSLQGKTELRRLLSKVLQERDALKGPQKPAVLVKIAPDLTAQDKEDIASVARE 232
Cdd:TIGR01036 156 YAACLRKLGPLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAVKQEQDGLRRVHRVPVLVKIAPDLTESDLEDIADSLVE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 233 LGIDGLIITNTTVSRPvGLQGALRS-ETGGLSGKPLRDLSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKIQAGASLV 311
Cdd:TIGR01036 236 LGIDGVIATNTTVSRS-LVQGPKNSdETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGASLL 314
|
330 340
....*....|....*....|.
gi 1907190513 312 QLYTALTFLGPPVVARVKREL 332
Cdd:TIGR01036 315 QIYSGFIYWGPPLVKEIVKEI 335
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
36-336 |
4.57e-135 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 386.32 E-value: 4.57e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 36 MLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKLG-FGFVEVGSVTPQPQEGNPRPRVFRLPEDqaVINRYGFNSHGLSA 114
Cdd:pfam01180 1 MLATKIPGLDFKNPIGLASGFDKFGEEALKWLALGkFGAIEIKSVTPYPQPGNPTPRVFRLPEG--VLNRMGLNNPGLDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 115 VEHRLRARQQKQTQLttdglPLGINLGKNKTSVDaaaDYVEGVRILGPLADYLVVNVSSPNTAGLRSLQGKTELRRLLSK 194
Cdd:pfam01180 79 VLAELLKRRKEYPRP-----DLGINLSKAGMTVD---DYVEVARKIGPFADYIELNVSCPNTPGLRALQTDPELAAILLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 195 VLQERDalkgpqKPAVLVKIAPDLTAQDKEDIASVAR-ELGIDGLIITNTTVSRPV----GLQGALRSETGGLSGKPLRD 269
Cdd:pfam01180 151 VVKEVS------KVPVLVKLAPDLTDIVIIDIADVALgEDGLDGINATNTTVRGMRidlkTEKPILANGTGGLSGPPIKP 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907190513 270 LSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVKRELEALL 336
Cdd:pfam01180 225 IALKVIRELYQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
37-344 |
2.01e-122 |
|
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: 354.38 E-value: 2.01e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 37 LEVRVLGHKFRNPVGIAAGF-DKHGEAVDGLYKLGFGFVEVGSVTPQPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSAV 115
Cdd:COG0167 2 LSVELAGLKFPNPVGLASGFfDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 116 EHRLRARQQKQTqlttdglPLGINLGKNktsvdAAADYVEGVRILGPL-ADYLVVNVSSPNTAG-LRSL-QGKTELRRLL 192
Cdd:COG0167 82 LERLLPAKRYDV-------PVIVNIGGN-----TVEDYVELARRLADAgADYLELNISCPNTPGgGRALgQDPEALAELL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 193 SKVLQERDalkgpqKPaVLVKIAPDLTaqDKEDIASVARELGIDGLIITNTTVSRPVGLQG---ALRSETGGLSGKPLRD 269
Cdd:COG0167 150 AAVKAATD------KP-VLVKLAPDLT--DIVEIARAAEEAGADGVIAINTTLGRAIDLETrrpVLANEAGGLSGPALKP 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907190513 270 LSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVKRELEALLKERGFNTV 344
Cdd:COG0167 221 IALRMVREVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSI 295
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
39-331 |
1.48e-92 |
|
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: 278.08 E-value: 1.48e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 39 VRVLGHKFRNPVGIAAGFD-KHGEAVDGLYKLGFGFVEVGSVTPQPQEGNPRPRVFRL-------PEDQAVINRYGFNSH 110
Cdd:cd02810 1 VNFLGLKLKNPFGVAAGPLlKTGELIARAAAAGFGAVVYKTVTLHPRPGNPLPRVARLppegesyPEQLGILNSFGLPNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 111 GLSAVEHRLRARQQKqtqltTDGLPLGINLGKNktsvdAAADYVEGVRILGPL-ADYLVVNVSSPNTAGLRSL-QGKTEL 188
Cdd:cd02810 81 GLDVWLQDIAKAKKE-----FPGQPLIASVGGS-----SKEDYVELARKIERAgAKALELNLSCPNVGGGRQLgQDPEAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 189 RRLLSKVLQERDalkgpqkPAVLVKIAPDLTAQDKEDIASVARELGIDGLIITNTTVSRPVGL---QGALRSETGGLSGK 265
Cdd:cd02810 151 ANLLKAVKAAVD-------IPLLVKLSPYFDLEDIVELAKAAERAGADGLTAINTISGRVVDLktvGPGPKRGTGGLSGA 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907190513 266 PLRDLSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVKRE 331
Cdd:cd02810 224 PIRPLALRWVARLAARLQLDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKIKKE 289
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
38-350 |
4.10e-44 |
|
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: 153.47 E-value: 4.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 38 EVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKLG-FGFVEVGSVTPQPQEGNPRPRVFRLPedqavinrYGF-NSHGLS-- 113
Cdd:cd04740 1 SVELAGLRLKNPVILASGTFGFGEELSRVADLGkLGAIVTKSITLEPREGNPPPRVVETP--------GGMlNAIGLQnp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 114 AVEHrlrARQQKQTQLTTDGLPLGINLGKNktSVDaaaDYVEGVRILGPL-ADYLVVNVSSPNT-AGLRSLQGKTEL-RR 190
Cdd:cd04740 73 GVEA---FLEELLPWLREFGTPVIASIAGS--TVE---EFVEVAEKLADAgADAIELNISCPNVkGGGMAFGTDPEAvAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 191 LLSKVlqeRDALKGPqkpaVLVKIAPDLTaqDKEDIASVARELGIDGLIITNTTVS--------RPVglqgaLRSETGGL 262
Cdd:cd04740 145 IVKAV---KKATDVP----VIVKLTPNVT--DIVEIARAAEEAGADGLTLINTLKGmaidietrKPI-----LGNVTGGL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 263 SG---KPLrdlstqTIREMYALTQGT-IPIIGVGGVSSGQDALEKIQAGASLVQLYTALtFLGPPVVARVKRELEALLKE 338
Cdd:cd04740 211 SGpaiKPI------ALRMVYQVYKAVeIPIIGVGGIASGEDALEFLMAGASAVQVGTAN-FVDPEAFKEIIEGLEAYLDE 283
|
330
....*....|..
gi 1907190513 339 RGFNTVTDAIGV 350
Cdd:cd04740 284 EGIKSIEELVGL 295
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
36-353 |
4.05e-42 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 148.37 E-value: 4.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 36 MLEVRVLGHKFRNPVGIAAG-FDKHGEAVDGLYKLGFGFVEVGSVTPQPQEGNPRPRVFRLPedqavinrYGF-NSHGLS 113
Cdd:PRK07259 1 RLSVELPGLKLKNPVMPASGtFGFGGEYARFYDLNGLGAIVTKSTTLEPREGNPTPRIAETP--------GGMlNAIGLQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 114 --AVEHrlrARQQKQTQLTTDGLPLGINL-GKNktsvdaAADYVEGVRILG--PLADYLVVNVSSPNTAGLRSLQG-KTE 187
Cdd:PRK07259 73 npGVDA---FIEEELPWLEEFDTPIIANVaGST------EEEYAEVAEKLSkaPNVDAIELNISCPNVKHGGMAFGtDPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 188 L-RRLLSKVlqeRDALKGPqkpaVLVKIAPDLTaqDKEDIASVARELGIDGLIITNTTVS--------RPVglqgaLRSE 258
Cdd:PRK07259 144 LaYEVVKAV---KEVVKVP----VIVKLTPNVT--DIVEIAKAAEEAGADGLSLINTLKGmaidiktrKPI-----LANV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 259 TGGLSGKPLRDLSTQTIREMYALTQgtIPIIGVGGVSSGQDALEKIQAGASLVQLYTALtFLGPPVVARVKRELEALLKE 338
Cdd:PRK07259 210 TGGLSGPAIKPIALRMVYQVYQAVD--IPIIGMGGISSAEDAIEFIMAGASAVQVGTAN-FYDPYAFPKIIEGLEAYLDK 286
|
330
....*....|....*
gi 1907190513 339 RGFNTVTDAIGVDHR 353
Cdd:PRK07259 287 YGIKSIEEIVGIAHK 301
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
37-352 |
6.06e-42 |
|
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: 147.96 E-value: 6.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 37 LEVRVLGHKFRNPVGIAAG-FDKHGEAVDGLYKLGFGFVEVGSVTPQPQEGNPRPRVFRLPedQAVINRYGFNSHGLSAV 115
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGiMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTIVETP--CGMLNAIGLQNPGVEAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 116 EHRLRarqqkqtqLTTDGLPLGINLGKNKTSVDAAADYVEGVRILGPLADYLVVNVSSPNTAGLRSLQGKTElrRLLSKV 195
Cdd:TIGR01037 79 LEELK--------PVREEFPTPLIASVYGSSVEEFAEVAEKLEKAPPYVDAYELNLSCPHVKGGGIAIGQDP--ELSADV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 196 LqerDALKGPQKPAVLVKIAPDLTaqDKEDIASVARELGIDGLIITNTTVSRPVGLQGA---LRSETGGLSGKPLRDLST 272
Cdd:TIGR01037 149 V---KAVKDKTDVPVFAKLSPNVT--DITEIAKAAEEAGADGLTLINTLRGMKIDIKTGkpiLANKTGGLSGPAIKPIAL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 273 QTIREMYALTQgtIPIIGVGGVSSGQDALEKIQAGASLVQLYTALtFLGPPVVARVKRELEALLKERGFNTVTDAIGVDH 352
Cdd:TIGR01037 224 RMVYDVYKMVD--IPIIGVGGITSFEDALEFLMAGASAVQVGTAV-YYRGFAFKKIIEGLIAFLKAEGFTSIEELIGIAH 300
|
|
| dihydoor_dh_Arch |
NF041011 |
dihydroorotate dehydrogenase PyrD; |
39-353 |
1.73e-33 |
|
dihydroorotate dehydrogenase PyrD;
Pssm-ID: 468940 Cd Length: 289 Bit Score: 125.43 E-value: 1.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 39 VRVLGHKFRNPVGIAAG-FDKHGEAVDGLYKL-GFGFVEVGSVTPQPQEGNPRPRVFRLPeDQAVINRYGFNSHGLSAVE 116
Cdd:NF041011 1 IRLAGLELEDPLIIASGiLPDVPEYIERVCEKyGPSAITTKTLTLNPLEPHKPPTVVKLH-DGCYLNAIGLGNPGIGLLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 117 hrlrarqqkqtQLTTDGLPLGINLGKNktSVDaaaDYVEGVRILGPLADYLVVNVSSPNTAGLrslqgKTELRRLLSKVL 196
Cdd:NF041011 80 -----------EIRVKLCPLIVSIGGS--SLE---EIVEVAEIAEEKADAIELNLSSPNRKGY-----GASLASLVREIV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 197 QErdaLKGPQKPAVLVKIAPdltaQDK-EDIASVARELGIDGLIITNTT--------VSRPVglqgaLRSETGGLSGKPL 267
Cdd:NF041011 139 KA---VKSVVKKPVFVKLGP----WDNvLEIAGKALEAGADGLTLINTVkgmaidveSFKPV-----LSYGTGGISGKCI 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 268 RDLSTQTIREMYAltQGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVKRELEALLKERGFNtVTDA 347
Cdd:NF041011 207 HPLAVRIIYDVYR--EYEAEIIGVGGVFSWRDAIELMSVGAKAVGVGTAIIDKGLSVISEIRKGLEEYLEEKGLK-LEDI 283
|
....*.
gi 1907190513 348 IGVDHR 353
Cdd:NF041011 284 IGIAVK 289
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
36-349 |
1.30e-22 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 96.18 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 36 MLEVRVLGHKFRNPVGIAAG-FDKHGEAVDGLYKLGFGFVEVGSVTPQPQEGNPRPRVFRLPedQAVINRYGFNSHGLSA 114
Cdd:PRK02506 1 STSTQIAGFKFDNCLMNAAGvYCMTKEELEEVEASAAGAFVTKSATLEPRPGNPEPRYADTP--LGSINSMGLPNLGFDY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 115 VEHRLRARQQKQTQLTTDGLPLGINLGKNKTSVDAAADyvegvrilgplADY--LV-VNVSSPNtaglrsLQGKTEL--- 188
Cdd:PRK02506 79 YLDYVLELQKKGPNKPHFLSVVGLSPEETHTILKKIQA-----------SDFngLVeLNLSCPN------VPGKPQIayd 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 189 ----RRLLSKVLQERdalkgpQKPAVlVKIAP--DLTAQDKedIASVARELGID----------GLII---TNTTVSRPv 249
Cdd:PRK02506 142 fettEQILEEVFTYF------TKPLG-VKLPPyfDIVHFDQ--AAAIFNKFPLAfvncinsignGLVIdpeDETVVIKP- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 250 glqgalRSETGGLSGKPLRDLSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVK 329
Cdd:PRK02506 212 ------KNGFGGIGGDYIKPTALANVRAFYQRLNPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLT 285
|
330 340
....*....|....*....|
gi 1907190513 330 RELEALLKERGFNTVTDAIG 349
Cdd:PRK02506 286 KELKAIMAEKGYQSLEDFRG 305
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
39-336 |
1.01e-21 |
|
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: 93.54 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 39 VRVLGHKFRNPVGIAAG-FDKHGEAVDGLYKLGFGFVEVGSVTPQPQEGNPRPRVFRLPEdqavinrYGFNSHGLS--AV 115
Cdd:cd04741 1 VTPPGLTISPPLMNAAGpWCTTLEDLLELAASSTGAVTTRSSTLAGRPGNPEPRYYAFPL-------GSINSLGLPnlGL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 116 EHRLRARQQKQTQLTTDGLPLGINLgkNKTSVDAAADYVEGVRILGPLADYLVVNVSSPNTAGLRSLQ-GKTELRRLLSK 194
Cdd:cd04741 74 DYYLEYIRTISDGLPGSAKPFFISV--TGSAEDIAAMYKKIAAHQKQFPLAMELNLSCPNVPGKPPPAyDFDATLEYLTA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 195 VlqeRDALKGPqkpaVLVKIAP--DLTAQDkeDIASV--ARELGIDGLIITNTT----VSRPVGLQGALRSETG--GLSG 264
Cdd:cd04741 152 V---KAAYSIP----VGVKTPPytDPAQFD--TLAEAlnAFACPISFITATNTLgnglVLDPERETVVLKPKTGfgGLAG 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907190513 265 KPLRDLSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVKRELEALL 336
Cdd:cd04741 223 AYLHPLALGNVRTFRRLLPSEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEKELEDIW 294
|
|
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
37-332 |
6.98e-15 |
|
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: 74.24 E-value: 6.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 37 LEVRVLGHKFRNPVGIAAGFDKH-GEAVDGLYKLGFGFVEVGSVTP-QPQEGNPRPRVFRLP-EDQAVInryGFNSHGLS 113
Cdd:cd02940 2 LSVTFCGIKFPNPFGLASAPPTTsYPMIRRAFEAGWGGAVTKTLGLdKDIVTNVSPRIARLRtSGRGQI---GFNNIELI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 114 AvEHRLRARQQKQTQLTTD----GLPLGINLGKNKTSVDAAADYVE--GvrilgplADYLVVNVSSPntaglrslQGKTE 187
Cdd:cd02940 79 S-EKPLEYWLKEIRELKKDfpdkILIASIMCEYNKEDWTELAKLVEeaG-------ADALELNFSCP--------HGMPE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 188 lRRLLSKVLQERDALK--------GPQKPaVLVKIAPDLTaqDKEDIASVARELGIDGLIITNTTVS---------RP-V 249
Cdd:cd02940 143 -RGMGAAVGQDPELVEeicrwvreAVKIP-VIAKLTPNIT--DIREIARAAKEGGADGVSAINTVNSlmgvdldgtPPaP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 250 GLQGalRSETGGLSGKPLRDLSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVK 329
Cdd:cd02940 219 GVEG--KTTYGGYSGPAVKPIALRAVSQIARAPEPGLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMC 296
|
...
gi 1907190513 330 REL 332
Cdd:cd02940 297 TGL 299
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
210-349 |
1.03e-10 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 62.65 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 210 VLVKIAPDLTaqdkeDI---ASVARELGIDGLIITNTTVS-----------RP-VGLQGALrsetGGLSGKPLRDLSTQT 274
Cdd:PRK08318 171 VIVKLTPNIT-----DIrepARAAKRGGADAVSLINTINSitgvdldrmipMPiVNGKSSH----GGYCGPAVKPIALNM 241
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907190513 275 IREMY--ALTQGtIPIIGVGGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVKRELEALLKERGFNTVTDAIG 349
Cdd:PRK08318 242 VAEIArdPETRG-LPISGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISGLSHYMDEKGFASLEDMVG 317
|
|
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
210-350 |
5.73e-09 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 57.15 E-value: 5.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 210 VLVKIAPDLTaqDKEDIASVARELGIDGLIITNTTVS-RPVGLQgALRSE--------TGGLSGKPLRDLS----TQTIR 276
Cdd:PLN02495 185 VWAKMTPNIT--DITQPARVALKSGCEGVAAINTIMSvMGINLD-TLRPEpcvegystPGGYSSKAVRPIAlakvMAIAK 261
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907190513 277 EMYALTQGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVKRELEALLKERGFNTVTDAIGV 350
Cdd:PLN02495 262 MMKSEFPEDRSLSGIGGVETGGDAAEFILLGADTVQVCTGVMMHGYPLVKNLCAELQDFMKKHNFSSIEDFRGA 335
|
|
| DHOD_like |
cd04739 |
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
190-346 |
3.56e-06 |
|
Dihydroorotate dehydrogenase (DHOD) like proteins. 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. This subgroup has the conserved FMN binding site, but lacks some catalytic residues and may therefore be inactive.
Pssm-ID: 240090 Cd Length: 325 Bit Score: 47.99 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 190 RLLSKVlqeRDALKGPqkpaVLVKIAPDLTAqdkedIASVAREL---GIDGLIITN------------TTVSRPVglqga 254
Cdd:cd04739 153 DILRAV---KSAVTIP----VAVKLSPFFSA-----LAHMAKQLdaaGADGLVLFNrfyqpdidletlEVVPNLL----- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 255 lRSETGGLSGkPLRdlstqTIREMYALTQgtIPIIGVGGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVKRELEA 334
Cdd:cd04739 216 -LSSPAEIRL-PLR-----WIAILSGRVK--ASLAASGGVHDAEDVVKYLLAGADVVMTTSALLRHGPDYIGTLLAGLEA 286
|
170
....*....|..
gi 1907190513 335 LLKERGFNTVTD 346
Cdd:cd04739 287 WMEEHGYESVQQ 298
|
|
| PRK07565 |
PRK07565 |
dihydroorotate dehydrogenase-like protein; |
292-349 |
9.08e-06 |
|
dihydroorotate dehydrogenase-like protein;
Pssm-ID: 236051 Cd Length: 334 Bit Score: 46.78 E-value: 9.08e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907190513 292 GGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVKRELEALLKERGFNTVTDAIG 349
Cdd:PRK07565 246 TGVHDAEDVIKMLLAGADVVMIASALLRHGPDYIGTILRGLEDWMERHGYESLQQFRG 303
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
283-317 |
1.38e-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: 40.27 E-value: 1.38e-03
10 20 30
....*....|....*....|....*....|....*
gi 1907190513 283 QGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTAL 317
Cdd:cd04735 282 AGRLPLIAVGSINTPDDALEALETGADLVAIGRGL 316
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
57-313 |
2.62e-03 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 38.72 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 57 DKHGEAVDGLYKLGFGFVEVGSVTPQPQEGNPRPRVFrlpedqavinrygfnshglsavehrlrARQQKQTQlttdGLPL 136
Cdd:cd04722 12 GDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEV---------------------------LKEVAAET----DLPL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 137 GINLGKNktsvDAAADYVEGVRILGPL-ADYLVVNVSSPNTAGlrslqgktELRRLLSKVLQERDALKgpqkpaVLVKIA 215
Cdd:cd04722 61 GVQLAIN----DAAAAVDIAAAAARAAgADGVEIHGAVGYLAR--------EDLELIRELREAVPDVK------VVVKLS 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 216 PDLtaqdkEDIASVARELGIDGLIITNttvSRPVGLQGALRSETGGLSGKPLRDLStqtiremyaltqgtIPIIGVGGVS 295
Cdd:cd04722 123 PTG-----ELAAAAAEEAGVDEVGLGN---GGGGGGGRDAVPIADLLLILAKRGSK--------------VPVIAGGGIN 180
|
250
....*....|....*...
gi 1907190513 296 SGQDALEKIQAGASLVQL 313
Cdd:cd04722 181 DPEDAAEALALGADGVIV 198
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
212-317 |
2.76e-03 |
|
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.
Pssm-ID: 240081 [Multi-domain] Cd Length: 236 Bit Score: 38.62 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190513 212 VKIAPDLTAqdkEDIASVARELGIDGLIItnttvsrpvglQGAlrsETGGLSGKPLRDLST--QTIREMYaltqgTIPII 289
Cdd:cd04730 103 IKVIPTVTS---VEEARKAEAAGADALVA-----------QGA---EAGGHRGTFDIGTFAlvPEVRDAV-----DIPVI 160
|
90 100
....*....|....*....|....*...
gi 1907190513 290 GVGGVSSGQDALEKIQAGASLVQLYTAL 317
Cdd:cd04730 161 AAGGIADGRGIAAALALGADGVQMGTRF 188
|
|
| |
