|
Name |
Accession |
Description |
Interval |
E-value |
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
17-345 |
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: 534.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 17 LQGLLDPESAHRLAVRFTSLGLLPRARF---QDSDMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKMGFGFVEIGSVT 93
Cdd:cd04738 3 LLFLLDPETAHRLAIRALKLGLGPPLLLllvYDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFVEVGTVT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 94 PKPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSVVEHRLRARQQKqakltedGLPLGVNLGKNKTS--VDAAEDYAEGVR 171
Cdd:cd04738 83 PRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRRPR-------GGPLGVNIGKNKDTplEDAVEDYVIGVR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 172 VLGPLADYLVVNVSSPNTAGLRSLQGKAELRRLLTKVLQERDGLRRvhRPAVLVKIAPDLTSQDKEDIASVVKELGIDGL 251
Cdd:cd04738 156 KLGPYADYLVVNVSSPNTPGLRDLQGKEALRELLTAVKEERNKLGK--KVPLLVKIAPDLSDEELEDIADVALEHGVDGI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 252 IVTNTTVSRPAGLQGALRSETGGLSGKPLRDLSTQTIREMYALTQGRVPIIGVGGVSSGQDALEKIRAGASLVQLYTALT 331
Cdd:cd04738 234 IATNTTISRPGLLRSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTGLV 313
|
330
....*....|....
2PRH_A 332 FWGPPVVGKVKREL 345
Cdd:cd04738 314 YEGPGLVKRIKREL 327
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
11-345 |
0e+00 |
|
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: 517.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 11 EHLMPTLQGLLDPESAHRLAVRFTSLG------LLPRARFQDSDMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKMGF 84
Cdd:TIGR01036 1 YPLVRKLLFLLDPESAHELTFQFLRLGtgtpflALLRSLFGASDPLEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAMGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 85 GFVEIGSVTPKPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSVVEHRLRArqqkqaklTEDGLPLGVNLGKNK--TSVDA 162
Cdd:TIGR01036 81 GFLEIGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLKR--------ARYKGPIGINIGKNKdtPSEDA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 163 AEDYAEGVRVLGPLADYLVVNVSSPNTAGLRSLQGKAELRRLLTKVLQERDGLRRVHRPAVLVKIAPDLTSQDKEDIASV 242
Cdd:TIGR01036 153 KEDYAACLRKLGPLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAVKQEQDGLRRVHRVPVLVKIAPDLTESDLEDIADS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 243 VKELGIDGLIVTNTTVSRPaGLQGALRS-ETGGLSGKPLRDLSTQTIREMYALTQGRVPIIGVGGVSSGQDALEKIRAGA 321
Cdd:TIGR01036 233 LVELGIDGVIATNTTVSRS-LVQGPKNSdETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGA 311
|
330 340
....*....|....*....|....
2PRH_A 322 SLVQLYTALTFWGPPVVGKVKREL 345
Cdd:TIGR01036 312 SLLQIYSGFIYWGPPLVKEIVKEI 335
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
8-366 |
6.06e-174 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 490.02 E-value: 6.06e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 8 FYAEHLMPTLQGLLDPESAHRLAVRFTSLGLLPRARFQDSDMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKMGFGFV 87
Cdd:PLN02826 32 FNATKLVNPLFRLLDPETAHSLAISAAARGLVPREKRPDPSVLGVEVWGRTFSNPIGLAAGFDKNAEAVEGLLGLGFGFV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 88 EIGSVTPKPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSVVEHRLRARQQKQAKLTEDGL----------------PLGV 151
Cdd:PLN02826 112 EIGSVTPLPQPGNPKPRVFRLREEGAIINRYGFNSEGIVAVAKRLGAQHGKRKLDETSSSsfssddvkaggkagpgILGV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 152 NLGKNKTSVDAAEDYAEGVRVLGPLADYLVVNVSSPNTAGLRSLQGKAELRRLLTKVLQERDGLRR--VHRPAVLVKIAP 229
Cdd:PLN02826 192 NLGKNKTSEDAAADYVQGVRALSQYADYLVINVSSPNTPGLRKLQGRKQLKDLLKKVLAARDEMQWgeEGPPPLLVKIAP 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 230 DLTSQDKEDIASVVKELGIDGLIVTNTTVSRPAG-LQGALRSETGGLSGKPLRDLSTQTIREMYALTQGRVPIIGVGGVS 308
Cdd:PLN02826 272 DLSKEDLEDIAAVALALGIDGLIISNTTISRPDSvLGHPHADEAGGLSGKPLFDLSTEVLREMYRLTRGKIPLVGCGGVS 351
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
2PRH_A 309 SGQDALEKIRAGASLVQLYTALTFWGPPVVGKVKRELEALLKEQGFGGVTDAIGADHR 366
Cdd:PLN02826 352 SGEDAYKKIRAGASLVQLYTAFAYEGPALIPRIKAELAACLERDGFKSIQEAVGADHR 409
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
49-349 |
1.96e-132 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 380.16 E-value: 1.96e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 49 MLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKMG-FGFVEIGSVTPKPQEGNPRPRVFRLPEDqaVINRYGFNSHGLSV 127
Cdd:pfam01180 1 MLATKIPGLDFKNPIGLASGFDKFGEEALKWLALGkFGAIEIKSVTPYPQPGNPTPRVFRLPEG--VLNRMGLNNPGLDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 128 VEHRLRARQQKQAKLtedglPLGVNLGKNKTSVDaaeDYAEGVRVLGPLADYLVVNVSSPNTAGLRSLQGKAELRRLLTK 207
Cdd:pfam01180 79 VLAELLKRRKEYPRP-----DLGINLSKAGMTVD---DYVEVARKIGPFADYIELNVSCPNTPGLRALQTDPELAAILLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 208 VLQErdglrrVHRPAVLVKIAPDLTSQDKEDIASVVK-ELGIDGLIVTNTTVSRPA----GLQGALRSETGGLSGKPLRD 282
Cdd:pfam01180 151 VVKE------VSKVPVLVKLAPDLTDIVIIDIADVALgEDGLDGINATNTTVRGMRidlkTEKPILANGTGGLSGPPIKP 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
2PRH_A 283 LSTQTIREMYALTQGRVPIIGVGGVSSGQDALEKIRAGASLVQLYTALTFWGPPVVGKVKRELEALL 349
Cdd:pfam01180 225 IALKVIRELYQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
50-354 |
7.39e-121 |
|
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: 350.91 E-value: 7.39e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 50 LEVRVLGHKFRNPVGIAAGF-DKHGEAVDGLYKMGFGFVEIGSVTPKPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSVV 128
Cdd:COG0167 2 LSVELAGLKFPNPVGLASGFfDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 129 EHRLRARQQKqakltedGLPLGVNLGKNktsvdAAEDYAEGVRVLGPL-ADYLVVNVSSPNTAG-LRSL-QGKAELRRLL 205
Cdd:COG0167 82 LERLLPAKRY-------DVPVIVNIGGN-----TVEDYVELARRLADAgADYLELNISCPNTPGgGRALgQDPEALAELL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 206 TKVLQERDglrrvhRPaVLVKIAPDLTsqDKEDIASVVKELGIDGLIVTNTTVSRPAGLQG---ALRSETGGLSGKPLRD 282
Cdd:COG0167 150 AAVKAATD------KP-VLVKLAPDLT--DIVEIARAAEEAGADGVIAINTTLGRAIDLETrrpVLANEAGGLSGPALKP 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
2PRH_A 283 LSTQTIREMYALTQGRVPIIGVGGVSSGQDALEKIRAGASLVQLYTALTFWGPPVVGKVKRELEALLKEQGF 354
Cdd:COG0167 221 IALRMVREVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGF 292
|
|
| dihydoor_dh_Arch |
NF041011 |
dihydroorotate dehydrogenase PyrD; |
52-366 |
8.53e-33 |
|
dihydroorotate dehydrogenase PyrD;
Pssm-ID: 468940 Cd Length: 289 Bit Score: 123.89 E-value: 8.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 52 VRVLGHKFRNPVGIAAGF----DKHGEAVDGLYKmgFGFVEIGSVTPKPQEGNPRPRVFRLPeDQAVINRYGFNSHGLSV 127
Cdd:NF041011 1 IRLAGLELEDPLIIASGIlpdvPEYIERVCEKYG--PSAITTKTLTLNPLEPHKPPTVVKLH-DGCYLNAIGLGNPGIGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 128 VEhrlrarqqkqaKLTEDGLPLGVNLGKNktSVdaaEDYAEGVRVLGPLADYLVVNVSSPNTAGLrslqgKAELRRLLTK 207
Cdd:NF041011 78 LE-----------EIRVKLCPLIVSIGGS--SL---EEIVEVAEIAEEKADAIELNLSSPNRKGY-----GASLASLVRE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 208 VLQERDGLrrVHRPaVLVKIAPdltsQDK-EDIASVVKELGIDGLIVTNTtvsrpagLQG----------ALRSETGGLS 276
Cdd:NF041011 137 IVKAVKSV--VKKP-VFVKLGP----WDNvLEIAGKALEAGADGLTLINT-------VKGmaidvesfkpVLSYGTGGIS 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 277 GKPLRDLSTQTIREMYAltQGRVPIIGVGGVSSGQDALEKIRAGASLVQLYTALTFWGPPVVGKVKRELEALLKEQGFgG 356
Cdd:NF041011 203 GKCIHPLAVRIIYDVYR--EYEAEIIGVGGVFSWRDAIELMSVGAKAVGVGTAIIDKGLSVISEIRKGLEEYLEEKGL-K 279
|
330
....*....|
2PRH_A 357 VTDAIGADHR 366
Cdd:NF041011 280 LEDIIGIAVK 289
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
17-345 |
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: 534.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 17 LQGLLDPESAHRLAVRFTSLGLLPRARF---QDSDMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKMGFGFVEIGSVT 93
Cdd:cd04738 3 LLFLLDPETAHRLAIRALKLGLGPPLLLllvYDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFVEVGTVT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 94 PKPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSVVEHRLRARQQKqakltedGLPLGVNLGKNKTS--VDAAEDYAEGVR 171
Cdd:cd04738 83 PRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRRPR-------GGPLGVNIGKNKDTplEDAVEDYVIGVR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 172 VLGPLADYLVVNVSSPNTAGLRSLQGKAELRRLLTKVLQERDGLRRvhRPAVLVKIAPDLTSQDKEDIASVVKELGIDGL 251
Cdd:cd04738 156 KLGPYADYLVVNVSSPNTPGLRDLQGKEALRELLTAVKEERNKLGK--KVPLLVKIAPDLSDEELEDIADVALEHGVDGI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 252 IVTNTTVSRPAGLQGALRSETGGLSGKPLRDLSTQTIREMYALTQGRVPIIGVGGVSSGQDALEKIRAGASLVQLYTALT 331
Cdd:cd04738 234 IATNTTISRPGLLRSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTGLV 313
|
330
....*....|....
2PRH_A 332 FWGPPVVGKVKREL 345
Cdd:cd04738 314 YEGPGLVKRIKREL 327
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
11-345 |
0e+00 |
|
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: 517.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 11 EHLMPTLQGLLDPESAHRLAVRFTSLG------LLPRARFQDSDMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKMGF 84
Cdd:TIGR01036 1 YPLVRKLLFLLDPESAHELTFQFLRLGtgtpflALLRSLFGASDPLEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAMGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 85 GFVEIGSVTPKPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSVVEHRLRArqqkqaklTEDGLPLGVNLGKNK--TSVDA 162
Cdd:TIGR01036 81 GFLEIGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLKR--------ARYKGPIGINIGKNKdtPSEDA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 163 AEDYAEGVRVLGPLADYLVVNVSSPNTAGLRSLQGKAELRRLLTKVLQERDGLRRVHRPAVLVKIAPDLTSQDKEDIASV 242
Cdd:TIGR01036 153 KEDYAACLRKLGPLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAVKQEQDGLRRVHRVPVLVKIAPDLTESDLEDIADS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 243 VKELGIDGLIVTNTTVSRPaGLQGALRS-ETGGLSGKPLRDLSTQTIREMYALTQGRVPIIGVGGVSSGQDALEKIRAGA 321
Cdd:TIGR01036 233 LVELGIDGVIATNTTVSRS-LVQGPKNSdETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGA 311
|
330 340
....*....|....*....|....
2PRH_A 322 SLVQLYTALTFWGPPVVGKVKREL 345
Cdd:TIGR01036 312 SLLQIYSGFIYWGPPLVKEIVKEI 335
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
8-366 |
6.06e-174 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 490.02 E-value: 6.06e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 8 FYAEHLMPTLQGLLDPESAHRLAVRFTSLGLLPRARFQDSDMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKMGFGFV 87
Cdd:PLN02826 32 FNATKLVNPLFRLLDPETAHSLAISAAARGLVPREKRPDPSVLGVEVWGRTFSNPIGLAAGFDKNAEAVEGLLGLGFGFV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 88 EIGSVTPKPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSVVEHRLRARQQKQAKLTEDGL----------------PLGV 151
Cdd:PLN02826 112 EIGSVTPLPQPGNPKPRVFRLREEGAIINRYGFNSEGIVAVAKRLGAQHGKRKLDETSSSsfssddvkaggkagpgILGV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 152 NLGKNKTSVDAAEDYAEGVRVLGPLADYLVVNVSSPNTAGLRSLQGKAELRRLLTKVLQERDGLRR--VHRPAVLVKIAP 229
Cdd:PLN02826 192 NLGKNKTSEDAAADYVQGVRALSQYADYLVINVSSPNTPGLRKLQGRKQLKDLLKKVLAARDEMQWgeEGPPPLLVKIAP 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 230 DLTSQDKEDIASVVKELGIDGLIVTNTTVSRPAG-LQGALRSETGGLSGKPLRDLSTQTIREMYALTQGRVPIIGVGGVS 308
Cdd:PLN02826 272 DLSKEDLEDIAAVALALGIDGLIISNTTISRPDSvLGHPHADEAGGLSGKPLFDLSTEVLREMYRLTRGKIPLVGCGGVS 351
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
2PRH_A 309 SGQDALEKIRAGASLVQLYTALTFWGPPVVGKVKRELEALLKEQGFGGVTDAIGADHR 366
Cdd:PLN02826 352 SGEDAYKKIRAGASLVQLYTAFAYEGPALIPRIKAELAACLERDGFKSIQEAVGADHR 409
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
20-353 |
9.75e-171 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 479.27 E-value: 9.75e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 20 LLDPESAHRLAVRF------TSLGLLPRARFQDSD-MLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKMGFGFVEIGSV 92
Cdd:PRK05286 12 KLDPETAHELTIRAlkrasrTPLLSLLRQRLTYTDpRLPVTVMGLTFPNPVGLAAGFDKNGEAIDALGALGFGFVEVGTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 93 TPKPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSVVEHRLRARQQkqakltedGLPLGVNLGKNKTSV--DAAEDYAEGV 170
Cdd:PRK05286 92 TPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKAYR--------GIPLGINIGKNKDTPleDAVDDYLICL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 171 RVLGPLADYLVVNVSSPNTAGLRSLQGKAELRRLLTKVLQERDGLRrvHRPAVLVKIAPDLTSQDKEDIASVVKELGIDG 250
Cdd:PRK05286 164 EKLYPYADYFTVNISSPNTPGLRDLQYGEALDELLAALKEAQAELH--GYVPLLVKIAPDLSDEELDDIADLALEHGIDG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 251 LIVTNTTVSRPAGLQGALRSETGGLSGKPLRDLSTQTIREMYALTQGRVPIIGVGGVSSGQDALEKIRAGASLVQLYTAL 330
Cdd:PRK05286 242 VIATNTTLSRDGLKGLPNADEAGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGASLVQIYSGL 321
|
330 340
....*....|....*....|...
2PRH_A 331 TFWGPPVVGKVKRELEALLKEQG 353
Cdd:PRK05286 322 IYEGPGLVKEIVRGLARLLRRDG 344
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
49-349 |
1.96e-132 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 380.16 E-value: 1.96e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 49 MLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKMG-FGFVEIGSVTPKPQEGNPRPRVFRLPEDqaVINRYGFNSHGLSV 127
Cdd:pfam01180 1 MLATKIPGLDFKNPIGLASGFDKFGEEALKWLALGkFGAIEIKSVTPYPQPGNPTPRVFRLPEG--VLNRMGLNNPGLDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 128 VEHRLRARQQKQAKLtedglPLGVNLGKNKTSVDaaeDYAEGVRVLGPLADYLVVNVSSPNTAGLRSLQGKAELRRLLTK 207
Cdd:pfam01180 79 VLAELLKRRKEYPRP-----DLGINLSKAGMTVD---DYVEVARKIGPFADYIELNVSCPNTPGLRALQTDPELAAILLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 208 VLQErdglrrVHRPAVLVKIAPDLTSQDKEDIASVVK-ELGIDGLIVTNTTVSRPA----GLQGALRSETGGLSGKPLRD 282
Cdd:pfam01180 151 VVKE------VSKVPVLVKLAPDLTDIVIIDIADVALgEDGLDGINATNTTVRGMRidlkTEKPILANGTGGLSGPPIKP 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
2PRH_A 283 LSTQTIREMYALTQGRVPIIGVGGVSSGQDALEKIRAGASLVQLYTALTFWGPPVVGKVKRELEALL 349
Cdd:pfam01180 225 IALKVIRELYQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
50-354 |
7.39e-121 |
|
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: 350.91 E-value: 7.39e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 50 LEVRVLGHKFRNPVGIAAGF-DKHGEAVDGLYKMGFGFVEIGSVTPKPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSVV 128
Cdd:COG0167 2 LSVELAGLKFPNPVGLASGFfDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 129 EHRLRARQQKqakltedGLPLGVNLGKNktsvdAAEDYAEGVRVLGPL-ADYLVVNVSSPNTAG-LRSL-QGKAELRRLL 205
Cdd:COG0167 82 LERLLPAKRY-------DVPVIVNIGGN-----TVEDYVELARRLADAgADYLELNISCPNTPGgGRALgQDPEALAELL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 206 TKVLQERDglrrvhRPaVLVKIAPDLTsqDKEDIASVVKELGIDGLIVTNTTVSRPAGLQG---ALRSETGGLSGKPLRD 282
Cdd:COG0167 150 AAVKAATD------KP-VLVKLAPDLT--DIVEIARAAEEAGADGVIAINTTLGRAIDLETrrpVLANEAGGLSGPALKP 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
2PRH_A 283 LSTQTIREMYALTQGRVPIIGVGGVSSGQDALEKIRAGASLVQLYTALTFWGPPVVGKVKRELEALLKEQGF 354
Cdd:COG0167 221 IALRMVREVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGF 292
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
52-344 |
6.59e-91 |
|
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: 274.62 E-value: 6.59e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 52 VRVLGHKFRNPVGIAAGFD-KHGEAVDGLYKMGFGFVEIGSVTPKPQEGNPRPRVFRL-------PEDQAVINRYGFNSH 123
Cdd:cd02810 1 VNFLGLKLKNPFGVAAGPLlKTGELIARAAAAGFGAVVYKTVTLHPRPGNPLPRVARLppegesyPEQLGILNSFGLPNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 124 GLSVVEHRLRARQQKQaklteDGLPLGVNLGKNktsvdAAEDYAEGVRVLGPL-ADYLVVNVSSPNTAGLRSL-QGKAEL 201
Cdd:cd02810 81 GLDVWLQDIAKAKKEF-----PGQPLIASVGGS-----SKEDYVELARKIERAgAKALELNLSCPNVGGGRQLgQDPEAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 202 RRLLTKVLQERDglrrvhrPAVLVKIAPDLTSQDKEDIASVVKELGIDGLIVTNTTVSRPAGLQGA---LRSETGGLSGK 278
Cdd:cd02810 151 ANLLKAVKAAVD-------IPLLVKLSPYFDLEDIVELAKAAERAGADGLTAINTISGRVVDLKTVgpgPKRGTGGLSGA 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
2PRH_A 279 PLRDLSTQTIREMYALTQGRVPIIGVGGVSSGQDALEKIRAGASLVQLYTALTFWGPPVVGKVKRE 344
Cdd:cd02810 224 PIRPLALRWVARLAARLQLDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKIKKE 289
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
49-366 |
1.50e-43 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 152.61 E-value: 1.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 49 MLEVRVLGHKFRNPVGIAAG-FDKHGEAVDGLYKMGFGFVEIGSVTPKPQEGNPRPRVFRLPedqavinrYGF-NSHGLS 126
Cdd:PRK07259 1 RLSVELPGLKLKNPVMPASGtFGFGGEYARFYDLNGLGAIVTKSTTLEPREGNPTPRIAETP--------GGMlNAIGLQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 127 ------VVEHRLRARQQKqakltedGLPLGVNL-GKNktsvdaAEDYAEGVRVLG--PLADYLVVNVSSPNTAGLRSLQG 197
Cdd:PRK07259 73 npgvdaFIEEELPWLEEF-------DTPIIANVaGST------EEEYAEVAEKLSkaPNVDAIELNISCPNVKHGGMAFG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 198 -KAELRRLLTKVLQERdglrrVHRPaVLVKIAPDLTsqDKEDIASVVKELGIDGLIVTNTTVS--------RPAglqgaL 268
Cdd:PRK07259 140 tDPELAYEVVKAVKEV-----VKVP-VIVKLTPNVT--DIVEIAKAAEEAGADGLSLINTLKGmaidiktrKPI-----L 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 269 RSETGGLSGKPLRDLSTQTIREMYALTqgRVPIIGVGGVSSGQDALEKIRAGASLVQLYTALtFWGPPVVGKVKRELEAL 348
Cdd:PRK07259 207 ANVTGGLSGPAIKPIALRMVYQVYQAV--DIPIIGMGGISSAEDAIEFIMAGASAVQVGTAN-FYDPYAFPKIIEGLEAY 283
|
330
....*....|....*...
2PRH_A 349 LKEQGFGGVTDAIGADHR 366
Cdd:PRK07259 284 LDKYGIKSIEEIVGIAHK 301
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
51-363 |
2.91e-41 |
|
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: 146.54 E-value: 2.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 51 EVRVLGHKFRNPVGIAAG-FDKHGEAVDGLYKMGFGFVEIGSVTPKPQEGNPRPRVFRLPedqavinrYGF-NSHGLSV- 127
Cdd:cd04740 1 SVELAGLRLKNPVILASGtFGFGEELSRVADLGKLGAIVTKSITLEPREGNPPPRVVETP--------GGMlNAIGLQNp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 128 -VEHrlrARQQKQAKLTEDGLPLGVNLGKnktsvDAAEDYAEGVRVLGPL-ADYLVVNVSSPNT-AGLRSLQGKAELRRL 204
Cdd:cd04740 73 gVEA---FLEELLPWLREFGTPVIASIAG-----STVEEFVEVAEKLADAgADAIELNISCPNVkGGGMAFGTDPEAVAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 205 LTKVLqerdglRRVHRPAVLVKIAPDLTsqDKEDIASVVKELGIDGLIVTNTtvsrpagLQG----------ALRSETGG 274
Cdd:cd04740 145 IVKAV------KKATDVPVIVKLTPNVT--DIVEIARAAEEAGADGLTLINT-------LKGmaidietrkpILGNVTGG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 275 LSGKPLRDLSTQTIREMYALTQgrVPIIGVGGVSSGQDALEKIRAGASLVQLYTALtFWGPPVVGKVKRELEALLKEQGF 354
Cdd:cd04740 210 LSGPAIKPIALRMVYQVYKAVE--IPIIGVGGIASGEDALEFLMAGASAVQVGTAN-FVDPEAFKEIIEGLEAYLDEEGI 286
|
....*....
2PRH_A 355 GGVTDAIGA 363
Cdd:cd04740 287 KSIEELVGL 295
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
50-365 |
1.80e-38 |
|
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: 139.49 E-value: 1.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 50 LEVRVLGHKFRNPVGIAAG-FDKHGEAVDGLYKMGFGFVEIGSVTPKPQEGNPRPRVFRLPedQAVINRYGFNSHGLSVV 128
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGiMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTIVETP--CGMLNAIGLQNPGVEAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 129 EHRLRArqqkqaKLTEDGLPLGVNL-GKnktSVDAAEDYAEGVRVLGPLADYLVVNVSSPNTAGLRSLQGK-AELRRLLT 206
Cdd:TIGR01037 79 LEELKP------VREEFPTPLIASVyGS---SVEEFAEVAEKLEKAPPYVDAYELNLSCPHVKGGGIAIGQdPELSADVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 207 KVLQERdglrrVHRPaVLVKIAPDLTsqDKEDIASVVKELGIDGLIVTNTTVSRPAGLQGA---LRSETGGLSGKPLRDL 283
Cdd:TIGR01037 150 KAVKDK-----TDVP-VFAKLSPNVT--DITEIAKAAEEAGADGLTLINTLRGMKIDIKTGkpiLANKTGGLSGPAIKPI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 284 STQTIREMYALTQgrVPIIGVGGVSSGQDALEKIRAGASLVQLYTALtFWGPPVVGKVKRELEALLKEQGFGGVTDAIGA 363
Cdd:TIGR01037 222 ALRMVYDVYKMVD--IPIIGVGGITSFEDALEFLMAGASAVQVGTAV-YYRGFAFKKIIEGLIAFLKAEGFTSIEELIGI 298
|
..
2PRH_A 364 DH 365
Cdd:TIGR01037 299 AH 300
|
|
| dihydoor_dh_Arch |
NF041011 |
dihydroorotate dehydrogenase PyrD; |
52-366 |
8.53e-33 |
|
dihydroorotate dehydrogenase PyrD;
Pssm-ID: 468940 Cd Length: 289 Bit Score: 123.89 E-value: 8.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 52 VRVLGHKFRNPVGIAAGF----DKHGEAVDGLYKmgFGFVEIGSVTPKPQEGNPRPRVFRLPeDQAVINRYGFNSHGLSV 127
Cdd:NF041011 1 IRLAGLELEDPLIIASGIlpdvPEYIERVCEKYG--PSAITTKTLTLNPLEPHKPPTVVKLH-DGCYLNAIGLGNPGIGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 128 VEhrlrarqqkqaKLTEDGLPLGVNLGKNktSVdaaEDYAEGVRVLGPLADYLVVNVSSPNTAGLrslqgKAELRRLLTK 207
Cdd:NF041011 78 LE-----------EIRVKLCPLIVSIGGS--SL---EEIVEVAEIAEEKADAIELNLSSPNRKGY-----GASLASLVRE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 208 VLQERDGLrrVHRPaVLVKIAPdltsQDK-EDIASVVKELGIDGLIVTNTtvsrpagLQG----------ALRSETGGLS 276
Cdd:NF041011 137 IVKAVKSV--VKKP-VFVKLGP----WDNvLEIAGKALEAGADGLTLINT-------VKGmaidvesfkpVLSYGTGGIS 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 277 GKPLRDLSTQTIREMYAltQGRVPIIGVGGVSSGQDALEKIRAGASLVQLYTALTFWGPPVVGKVKRELEALLKEQGFgG 356
Cdd:NF041011 203 GKCIHPLAVRIIYDVYR--EYEAEIIGVGGVFSWRDAIELMSVGAKAVGVGTAIIDKGLSVISEIRKGLEEYLEEKGL-K 279
|
330
....*....|
2PRH_A 357 VTDAIGADHR 366
Cdd:NF041011 280 LEDIIGIAVK 289
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
52-349 |
9.23e-22 |
|
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: 93.93 E-value: 9.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 52 VRVLGHKFRNPVGIAAG-FDKHGEAVDGLYKMGFGFVEIGSVTPKPQEGNPRPRVFRLPedQAVINRYGFNSHGLSVVEH 130
Cdd:cd04741 1 VTPPGLTISPPLMNAAGpWCTTLEDLLELAASSTGAVTTRSSTLAGRPGNPEPRYYAFP--LGSINSLGLPNLGLDYYLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 131 RLRARQQKQAkltEDGLPLGVNLgkNKTSVDAAEDYAEGVRVLGPLADYLVVNVSSPNTAGL--RSLQGKAeLRRLLTKV 208
Cdd:cd04741 79 YIRTISDGLP---GSAKPFFISV--TGSAEDIAAMYKKIAAHQKQFPLAMELNLSCPNVPGKppPAYDFDA-TLEYLTAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 209 LQerdglrrVHRPAVLVKIAPDLTSQDKEDIASVVKE--LGIDGLIVTNTT----VSRPAGLQGALRSETG--GLSGKPL 280
Cdd:cd04741 153 KA-------AYSIPVGVKTPPYTDPAQFDTLAEALNAfaCPISFITATNTLgnglVLDPERETVVLKPKTGfgGLAGAYL 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
2PRH_A 281 RDLSTQTIREMYALTQGRVPIIGVGGVSSGQDALEKIRAGASLVQLYTALTFWGPPVVGKVKRELEALL 349
Cdd:cd04741 226 HPLALGNVRTFRRLLPSEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEKELEDIW 294
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
49-362 |
1.18e-18 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 85.39 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 49 MLEVRVLGHKFRNPVGIAAG-FDKHGEAVDGLYKMGFGFVEIGSVTPKPQEGNPRPRVFRLPedQAVINRYGFNSHGLSV 127
Cdd:PRK02506 1 STSTQIAGFKFDNCLMNAAGvYCMTKEELEEVEASAAGAFVTKSATLEPRPGNPEPRYADTP--LGSINSMGLPNLGFDY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 128 VEHRLRARQQKQAKLtedglPL-----GVNLGKNKTSVDAAEDyaegvrvlgplADY--LV-VNVSSPNtaglrsLQGKA 199
Cdd:PRK02506 79 YLDYVLELQKKGPNK-----PHflsvvGLSPEETHTILKKIQA-----------SDFngLVeLNLSCPN------VPGKP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 200 EL-------RRLLTKVLQErdglrrVHRPAVlVKIAP--DLTSQDKedIASVVKELGIDGLivtNTTVSRPAGLQGALRS 270
Cdd:PRK02506 137 QIaydfettEQILEEVFTY------FTKPLG-VKLPPyfDIVHFDQ--AAAIFNKFPLAFV---NCINSIGNGLVIDPED 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 271 ET---------GGLSGKPLRDLSTQTIREMYALTQGRVPIIGVGGVSSGQDALEKIRAGASLVQLYTALTFWGPPVVGKV 341
Cdd:PRK02506 205 ETvvikpkngfGGIGGDYIKPTALANVRAFYQRLNPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERL 284
|
330 340
....*....|....*....|.
2PRH_A 342 KRELEALLKEQGFGGVTDAIG 362
Cdd:PRK02506 285 TKELKAIMAEKGYQSLEDFRG 305
|
|
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
50-345 |
4.63e-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: 77.71 E-value: 4.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 50 LEVRVLGHKFRNPVGIAAGfdkhgeAVDGLYKM-------GFGFVEIGSVTP-KPQEGNPRPRVFRLP-EDQAVInryGF 120
Cdd:cd02940 2 LSVTFCGIKFPNPFGLASA------PPTTSYPMirrafeaGWGGAVTKTLGLdKDIVTNVSPRIARLRtSGRGQI---GF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 121 NSHGLsVVEHRLRARQQKQAKLTED--GLPLGVNL--GKNKtsvDAAEDYAEGVRVLGplADYLVVNVSSPntaglrslQ 196
Cdd:cd02940 73 NNIEL-ISEKPLEYWLKEIRELKKDfpDKILIASImcEYNK---EDWTELAKLVEEAG--ADALELNFSCP--------H 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 197 GKAElRRLLTKVLQERDGLRRVHR--------PaVLVKIAPDLTsqDKEDIASVVKELGIDGLIVTNTTVS--------- 259
Cdd:cd02940 139 GMPE-RGMGAAVGQDPELVEEICRwvreavkiP-VIAKLTPNIT--DIREIARAAKEGGADGVSAINTVNSlmgvdldgt 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 260 RPA-GLQGalRSETGGLSGKPLRDLSTQTIREMYALTQGRVPIIGVGGVSSGQDALEKIRAGASLVQLYTALTFWGPPVV 338
Cdd:cd02940 215 PPApGVEG--KTTYGGYSGPAVKPIALRAVSQIARAPEPGLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIV 292
|
....*..
2PRH_A 339 GKVKREL 345
Cdd:cd02940 293 DDMCTGL 299
|
|
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
223-363 |
1.12e-08 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 56.38 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 223 VLVKIAPDLTsqDKEDIASVVKELGIDGLIVTNTTVSRPAGLQGALRSE--------TGGLSGKPLRDLSTQTIREMYAL 294
Cdd:PLN02495 185 VWAKMTPNIT--DITQPARVALKSGCEGVAAINTIMSVMGINLDTLRPEpcvegystPGGYSSKAVRPIALAKVMAIAKM 262
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
2PRH_A 295 TQGRVP----IIGVGGVSSGQDALEKIRAGASLVQLYTALTFWGPPVVGKVKRELEALLKEQGFGGVTDAIGA 363
Cdd:PLN02495 263 MKSEFPedrsLSGIGGVETGGDAAEFILLGADTVQVCTGVMMHGYPLVKNLCAELQDFMKKHNFSSIEDFRGA 335
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
216-362 |
2.33e-08 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 55.34 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 216 RRVHRPAVLVKIAPDLTsqdkeDI---ASVVKELGIDGLIVTNTTVS-------RPAGL-----QGALrsetGGLSGKPL 280
Cdd:PRK08318 164 KRGSRLPVIVKLTPNIT-----DIrepARAAKRGGADAVSLINTINSitgvdldRMIPMpivngKSSH----GGYCGPAV 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 281 RDLSTQTIREMYALTQ-GRVPIIGVGGVSSGQDALEKIRAGASLVQLYTALTFWGPPVVGKVKRELEALLKEQGFGGVTD 359
Cdd:PRK08318 235 KPIALNMVAEIARDPEtRGLPISGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISGLSHYMDEKGFASLED 314
|
...
2PRH_A 360 AIG 362
Cdd:PRK08318 315 MVG 317
|
|
| PRK07565 |
PRK07565 |
dihydroorotate dehydrogenase-like protein; |
223-363 |
1.19e-06 |
|
dihydroorotate dehydrogenase-like protein;
Pssm-ID: 236051 Cd Length: 334 Bit Score: 49.87 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 223 VLVKIAPDLTSqdkedIASVVKEL---GIDGL-----------------IVTNTTVSRPAGLQGALRSeTGGLSGKplrd 282
Cdd:PRK07565 168 VAVKLSPYFSN-----LANMAKRLdaaGADGLvlfnrfyqpdidletleVVPGLVLSTPAELRLPLRW-IAILSGR---- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 283 lstqtIREMYALTqgrvpiigvGGVSSGQDALEKIRAGASLVQLYTALTFWGPPVVGKVKRELEALLKEQGFGGVTDAIG 362
Cdd:PRK07565 238 -----VGADLAAT---------TGVHDAEDVIKMLLAGADVVMIASALLRHGPDYIGTILRGLEDWMERHGYESLQQFRG 303
|
.
2PRH_A 363 A 363
Cdd:PRK07565 304 S 304
|
|
| DHOD_like |
cd04739 |
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
293-359 |
1.16e-05 |
|
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: 46.84 E-value: 1.16e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
2PRH_A 293 ALTQGRVP--IIGVGGVSSGQDALEKIRAGASLVQLYTALTFWGPPVVGKVKRELEALLKEQGFGGVTD 359
Cdd:cd04739 230 AILSGRVKasLAASGGVHDAEDVVKYLLAGADVVMTTSALLRHGPDYIGTLLAGLEAWMEEHGYESVQQ 298
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
296-346 |
9.89e-04 |
|
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: 40.66 E-value: 9.89e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
2PRH_A 296 QGRVPIIGVGGVSSGQDALEKIRAGASLVQLYTALtFWGPPVVGKVK--RELE 346
Cdd:cd04735 282 AGRLPLIAVGSINTPDDALEALETGADLVAIGRGL-LVDPDWVEKIKegREDE 333
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
225-330 |
2.34e-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: 39.00 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 225 VKIAPDLTSqdkEDIASVVKELGIDGLIVtnttvsrpaglQGAlrsETGGLSGKPLRDLST--QTIREMYaltqgRVPII 302
Cdd:cd04730 103 IKVIPTVTS---VEEARKAEAAGADALVA-----------QGA---EAGGHRGTFDIGTFAlvPEVRDAV-----DIPVI 160
|
90 100
....*....|....*....|....*...
2PRH_A 303 GVGGVSSGQDALEKIRAGASLVQLYTAL 330
Cdd:cd04730 161 AAGGIADGRGIAAALALGADGVQMGTRF 188
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
70-326 |
3.17e-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: 38.34 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 70 DKHGEAVDGLYKMGFGFVEIGSVTPKPQEGNPRPRVFRlpedqavinrygfnshglsvvehrlrarqqkQAKLTEDGLPL 149
Cdd:cd04722 12 GDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEVL-------------------------------KEVAAETDLPL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 150 GVNLGKNKTsVDAAEDYAEGVRVLGplADYLVVNVSSPNTAGlrslqgkaELRRLLTKVLQERDGLrrvhrpAVLVKIAP 229
Cdd:cd04722 61 GVQLAINDA-AAAVDIAAAAARAAG--ADGVEIHGAVGYLAR--------EDLELIRELREAVPDV------KVVVKLSP 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PRH_A 230 DLtsqdkEDIASVVKELGIDGLIVTNttvSRPAGLQGALRSETGglsgkplrdlstqtIREMYALTQGRVPIIGVGGVSS 309
Cdd:cd04722 124 TG-----ELAAAAAEEAGVDEVGLGN---GGGGGGGRDAVPIAD--------------LLLILAKRGSKVPVIAGGGIND 181
|
250
....*....|....*..
2PRH_A 310 GQDALEKIRAGASLVQL 326
Cdd:cd04722 182 PEDAAEALALGADGVIV 198
|
|
| |
