|
Name |
Accession |
Description |
Interval |
E-value |
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
43-373 |
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: 527.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 43 PALQRLLDPESAHRLAVRVISLGLLPRATF---QDSNMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKLGFGFVEVGS 119
Cdd:cd04738 1 RPLLFLLDPETAHRLAIRALKLGLGPPLLLllvYDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFVEVGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 120 VTPQPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSAVEHRLRARQQKqtqlttdGLPLGINLGKNKTS--VDAAADYVEG 197
Cdd:cd04738 81 VTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRRPR-------GGPLGVNIGKNKDTplEDAVEDYVIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 198 VRILGPLADYLVVNVSSPNTAGLRSLQGKTELRRLLSKVLQERDALKGPqkPAVLVKIAPDLTAQDKEDIASVARELGID 277
Cdd:cd04738 154 VRKLGPYADYLVVNVSSPNTPGLRDLQGKEALRELLTAVKEERNKLGKK--VPLLVKIAPDLSDEELEDIADVALEHGVD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 278 GLIITNTTVSRPVGLQGALRSETGGLSGKPLRDLSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTA 357
Cdd:cd04738 232 GIIATNTTISRPGLLRSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTG 311
|
330
....*....|....*.
gi 9910194 358 LTFLGPPVVARVKREL 373
Cdd:cd04738 312 LVYEGPGLVKRIKREL 327
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
4-394 |
9.09e-176 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 495.80 E-value: 9.09e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 4 RQLRKRALDAAIIlGGGGLLFTSYLTATGDDHFYAEYLMPALQRLLDPESAHRLAVRVISLGLLPRATFQDSNMLEVRVL 83
Cdd:PLN02826 1 GRLLTGALIGLAI-AGGAYVSTVDEATFCGWLFNATKLVNPLFRLLDPETAHSLAISAAARGLVPREKRPDPSVLGVEVW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 84 GHKFRNPVGIAAGFDKHGEAVDGLYKLGFGFVEVGSVTPQPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSAVEHRLRAR 163
Cdd:PLN02826 80 GRTFSNPIGLAAGFDKNAEAVEGLLGLGFGFVEIGSVTPLPQPGNPKPRVFRLREEGAIINRYGFNSEGIVAVAKRLGAQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 164 QQKQTQLTTDGL----------------PLGINLGKNKTSVDAAADYVEGVRILGPLADYLVVNVSSPNTAGLRSLQGKT 227
Cdd:PLN02826 160 HGKRKLDETSSSsfssddvkaggkagpgILGVNLGKNKTSEDAAADYVQGVRALSQYADYLVINVSSPNTPGLRKLQGRK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 228 ELRRLLSKVLQERDALKGPQ--KPAVLVKIAPDLTAQDKEDIASVARELGIDGLIITNTTVSRPVG-LQGALRSETGGLS 304
Cdd:PLN02826 240 QLKDLLKKVLAARDEMQWGEegPPPLLVKIAPDLSKEDLEDIAAVALALGIDGLIISNTTISRPDSvLGHPHADEAGGLS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 305 GKPLRDLSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVKRELEALLKERGFNT 384
Cdd:PLN02826 320 GKPLFDLSTEVLREMYRLTRGKIPLVGCGGVSSGEDAYKKIRAGASLVQLYTAFAYEGPALIPRIKAELAACLERDGFKS 399
|
410
....*....|
gi 9910194 385 VTDAIGVDHR 394
Cdd:PLN02826 400 IQEAVGADHR 409
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
39-373 |
3.02e-167 |
|
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: 471.19 E-value: 3.02e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 39 EYLMPALQRLLDPESAHRLAVRVISLG------LLPRATFQDSNMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKLGF 112
Cdd:TIGR01036 1 YPLVRKLLFLLDPESAHELTFQFLRLGtgtpflALLRSLFGASDPLEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAMGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 113 GFVEVGSVTPQPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSAVEHRLRArqqkqtqlTTDGLPLGINLGKNK--TSVDA 190
Cdd:TIGR01036 81 GFLEIGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLKR--------ARYKGPIGINIGKNKdtPSEDA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 191 AADYVEGVRILGPLADYLVVNVSSPNTAGLRSLQGKTELRRLLSKVLQERDALKGPQKPAVLVKIAPDLTAQDKEDIASV 270
Cdd:TIGR01036 153 KEDYAACLRKLGPLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAVKQEQDGLRRVHRVPVLVKIAPDLTESDLEDIADS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 271 ARELGIDGLIITNTTVSRPvGLQGALRS-ETGGLSGKPLRDLSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKIQAGA 349
Cdd:TIGR01036 233 LVELGIDGVIATNTTVSRS-LVQGPKNSdETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGA 311
|
330 340
....*....|....*....|....
gi 9910194 350 SLVQLYTALTFLGPPVVARVKREL 373
Cdd:TIGR01036 312 SLLQIYSGFIYWGPPLVKEIVKEI 335
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
77-377 |
3.06e-135 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 388.24 E-value: 3.06e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 77 MLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKLG-FGFVEVGSVTPQPQEGNPRPRVFRLPEDqaVINRYGFNSHGLSA 155
Cdd:pfam01180 1 MLATKIPGLDFKNPIGLASGFDKFGEEALKWLALGkFGAIEIKSVTPYPQPGNPTPRVFRLPEG--VLNRMGLNNPGLDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 156 VEHRLRARQQKQTQLttdglPLGINLGKNKTSVDaaaDYVEGVRILGPLADYLVVNVSSPNTAGLRSLQGKTELRRLLSK 235
Cdd:pfam01180 79 VLAELLKRRKEYPRP-----DLGINLSKAGMTVD---DYVEVARKIGPFADYIELNVSCPNTPGLRALQTDPELAAILLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 236 VLQERDalkgpqKPAVLVKIAPDLTAQDKEDIASVAR-ELGIDGLIITNTTVSRPV----GLQGALRSETGGLSGKPLRD 310
Cdd:pfam01180 151 VVKEVS------KVPVLVKLAPDLTDIVIIDIADVALgEDGLDGINATNTTVRGMRidlkTEKPILANGTGGLSGPPIKP 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9910194 311 LSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVKRELEALL 377
Cdd:pfam01180 225 IALKVIRELYQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
78-385 |
5.59e-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: 354.76 E-value: 5.59e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 78 LEVRVLGHKFRNPVGIAAGF-DKHGEAVDGLYKLGFGFVEVGSVTPQPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSAV 156
Cdd:COG0167 2 LSVELAGLKFPNPVGLASGFfDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 157 EHRLRARQQKQTqlttdglPLGINLGKNktsvdAAADYVEGVRILGPL-ADYLVVNVSSPNTAG-LRSL-QGKTELRRLL 233
Cdd:COG0167 82 LERLLPAKRYDV-------PVIVNIGGN-----TVEDYVELARRLADAgADYLELNISCPNTPGgGRALgQDPEALAELL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 234 SKVLQERDalkgpqKPaVLVKIAPDLTaqDKEDIASVARELGIDGLIITNTTVSRPVGLQG---ALRSETGGLSGKPLRD 310
Cdd:COG0167 150 AAVKAATD------KP-VLVKLAPDLT--DIVEIARAAEEAGADGVIAINTTLGRAIDLETrrpVLANEAGGLSGPALKP 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9910194 311 LSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVKRELEALLKERGFNTV 385
Cdd:COG0167 221 IALRMVREVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSI 295
|
|
| dihydoor_dh_Arch |
NF041011 |
dihydroorotate dehydrogenase PyrD; |
80-394 |
1.54e-33 |
|
dihydroorotate dehydrogenase PyrD;
Pssm-ID: 468940 Cd Length: 289 Bit Score: 126.59 E-value: 1.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 80 VRVLGHKFRNPVGIAAG-FDKHGEAVDGLYKL-GFGFVEVGSVTPQPQEGNPRPRVFRLPeDQAVINRYGFNSHGLSAVE 157
Cdd:NF041011 1 IRLAGLELEDPLIIASGiLPDVPEYIERVCEKyGPSAITTKTLTLNPLEPHKPPTVVKLH-DGCYLNAIGLGNPGIGLLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 158 hrlrarqqkqtQLTTDGLPLGINLGKNktSVDaaaDYVEGVRILGPLADYLVVNVSSPNTAGLrslqgKTELRRLLSKVL 237
Cdd:NF041011 80 -----------EIRVKLCPLIVSIGGS--SLE---EIVEVAEIAEEKADAIELNLSSPNRKGY-----GASLASLVREIV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 238 QErdaLKGPQKPAVLVKIAPdltaQDK-EDIASVARELGIDGLIITNTT--------VSRPVglqgaLRSETGGLSGKPL 308
Cdd:NF041011 139 KA---VKSVVKKPVFVKLGP----WDNvLEIAGKALEAGADGLTLINTVkgmaidveSFKPV-----LSYGTGGISGKCI 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 309 RDLSTQTIREMYAltQGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVKRELEALLKERGFNtVTDA 388
Cdd:NF041011 207 HPLAVRIIYDVYR--EYEAEIIGVGGVFSWRDAIELMSVGAKAVGVGTAIIDKGLSVISEIRKGLEEYLEEKGLK-LEDI 283
|
....*.
gi 9910194 389 IGVDHR 394
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) ... |
43-373 |
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: 527.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 43 PALQRLLDPESAHRLAVRVISLGLLPRATF---QDSNMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKLGFGFVEVGS 119
Cdd:cd04738 1 RPLLFLLDPETAHRLAIRALKLGLGPPLLLllvYDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFVEVGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 120 VTPQPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSAVEHRLRARQQKqtqlttdGLPLGINLGKNKTS--VDAAADYVEG 197
Cdd:cd04738 81 VTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRRPR-------GGPLGVNIGKNKDTplEDAVEDYVIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 198 VRILGPLADYLVVNVSSPNTAGLRSLQGKTELRRLLSKVLQERDALKGPqkPAVLVKIAPDLTAQDKEDIASVARELGID 277
Cdd:cd04738 154 VRKLGPYADYLVVNVSSPNTPGLRDLQGKEALRELLTAVKEERNKLGKK--VPLLVKIAPDLSDEELEDIADVALEHGVD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 278 GLIITNTTVSRPVGLQGALRSETGGLSGKPLRDLSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTA 357
Cdd:cd04738 232 GIIATNTTISRPGLLRSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTG 311
|
330
....*....|....*.
gi 9910194 358 LTFLGPPVVARVKREL 373
Cdd:cd04738 312 LVYEGPGLVKRIKREL 327
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
4-394 |
9.09e-176 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 495.80 E-value: 9.09e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 4 RQLRKRALDAAIIlGGGGLLFTSYLTATGDDHFYAEYLMPALQRLLDPESAHRLAVRVISLGLLPRATFQDSNMLEVRVL 83
Cdd:PLN02826 1 GRLLTGALIGLAI-AGGAYVSTVDEATFCGWLFNATKLVNPLFRLLDPETAHSLAISAAARGLVPREKRPDPSVLGVEVW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 84 GHKFRNPVGIAAGFDKHGEAVDGLYKLGFGFVEVGSVTPQPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSAVEHRLRAR 163
Cdd:PLN02826 80 GRTFSNPIGLAAGFDKNAEAVEGLLGLGFGFVEIGSVTPLPQPGNPKPRVFRLREEGAIINRYGFNSEGIVAVAKRLGAQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 164 QQKQTQLTTDGL----------------PLGINLGKNKTSVDAAADYVEGVRILGPLADYLVVNVSSPNTAGLRSLQGKT 227
Cdd:PLN02826 160 HGKRKLDETSSSsfssddvkaggkagpgILGVNLGKNKTSEDAAADYVQGVRALSQYADYLVINVSSPNTPGLRKLQGRK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 228 ELRRLLSKVLQERDALKGPQ--KPAVLVKIAPDLTAQDKEDIASVARELGIDGLIITNTTVSRPVG-LQGALRSETGGLS 304
Cdd:PLN02826 240 QLKDLLKKVLAARDEMQWGEegPPPLLVKIAPDLSKEDLEDIAAVALALGIDGLIISNTTISRPDSvLGHPHADEAGGLS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 305 GKPLRDLSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVKRELEALLKERGFNT 384
Cdd:PLN02826 320 GKPLFDLSTEVLREMYRLTRGKIPLVGCGGVSSGEDAYKKIRAGASLVQLYTAFAYEGPALIPRIKAELAACLERDGFKS 399
|
410
....*....|
gi 9910194 385 VTDAIGVDHR 394
Cdd:PLN02826 400 IQEAVGADHR 409
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
43-381 |
9.30e-168 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 472.72 E-value: 9.30e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 43 PALqRLLDPESAHRLAVRVISLGLLPRATFQ-------DSNMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKLGFGFV 115
Cdd:PRK05286 8 PLL-FKLDPETAHELTIRALKRASRTPLLSLlrqrltyTDPRLPVTVMGLTFPNPVGLAAGFDKNGEAIDALGALGFGFV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 116 EVGSVTPQPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSAVEHRLRARQQkqtqlttdGLPLGINLGKNKTSV--DAAAD 193
Cdd:PRK05286 87 EVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKAYR--------GIPLGINIGKNKDTPleDAVDD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 194 YVEGVRILGPLADYLVVNVSSPNTAGLRSLQGKTELRRLLSKVLQERDALKGPqKPaVLVKIAPDLTAQDKEDIASVARE 273
Cdd:PRK05286 159 YLICLEKLYPYADYFTVNISSPNTPGLRDLQYGEALDELLAALKEAQAELHGY-VP-LLVKIAPDLSDEELDDIADLALE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 274 LGIDGLIITNTTVSRPvGLQG-ALRSETGGLSGKPLRDLSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKIQAGASLV 352
Cdd:PRK05286 237 HGIDGVIATNTTLSRD-GLKGlPNADEAGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGASLV 315
|
330 340
....*....|....*....|....*....
gi 9910194 353 QLYTALTFLGPPVVARVKRELEALLKERG 381
Cdd:PRK05286 316 QIYSGLIYEGPGLVKEIVRGLARLLRRDG 344
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
39-373 |
3.02e-167 |
|
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: 471.19 E-value: 3.02e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 39 EYLMPALQRLLDPESAHRLAVRVISLG------LLPRATFQDSNMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKLGF 112
Cdd:TIGR01036 1 YPLVRKLLFLLDPESAHELTFQFLRLGtgtpflALLRSLFGASDPLEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAMGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 113 GFVEVGSVTPQPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSAVEHRLRArqqkqtqlTTDGLPLGINLGKNK--TSVDA 190
Cdd:TIGR01036 81 GFLEIGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLKR--------ARYKGPIGINIGKNKdtPSEDA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 191 AADYVEGVRILGPLADYLVVNVSSPNTAGLRSLQGKTELRRLLSKVLQERDALKGPQKPAVLVKIAPDLTAQDKEDIASV 270
Cdd:TIGR01036 153 KEDYAACLRKLGPLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAVKQEQDGLRRVHRVPVLVKIAPDLTESDLEDIADS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 271 ARELGIDGLIITNTTVSRPvGLQGALRS-ETGGLSGKPLRDLSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKIQAGA 349
Cdd:TIGR01036 233 LVELGIDGVIATNTTVSRS-LVQGPKNSdETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGA 311
|
330 340
....*....|....*....|....
gi 9910194 350 SLVQLYTALTFLGPPVVARVKREL 373
Cdd:TIGR01036 312 SLLQIYSGFIYWGPPLVKEIVKEI 335
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
77-377 |
3.06e-135 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 388.24 E-value: 3.06e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 77 MLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKLG-FGFVEVGSVTPQPQEGNPRPRVFRLPEDqaVINRYGFNSHGLSA 155
Cdd:pfam01180 1 MLATKIPGLDFKNPIGLASGFDKFGEEALKWLALGkFGAIEIKSVTPYPQPGNPTPRVFRLPEG--VLNRMGLNNPGLDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 156 VEHRLRARQQKQTQLttdglPLGINLGKNKTSVDaaaDYVEGVRILGPLADYLVVNVSSPNTAGLRSLQGKTELRRLLSK 235
Cdd:pfam01180 79 VLAELLKRRKEYPRP-----DLGINLSKAGMTVD---DYVEVARKIGPFADYIELNVSCPNTPGLRALQTDPELAAILLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 236 VLQERDalkgpqKPAVLVKIAPDLTAQDKEDIASVAR-ELGIDGLIITNTTVSRPV----GLQGALRSETGGLSGKPLRD 310
Cdd:pfam01180 151 VVKEVS------KVPVLVKLAPDLTDIVIIDIADVALgEDGLDGINATNTTVRGMRidlkTEKPILANGTGGLSGPPIKP 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9910194 311 LSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVKRELEALL 377
Cdd:pfam01180 225 IALKVIRELYQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
78-385 |
5.59e-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: 354.76 E-value: 5.59e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 78 LEVRVLGHKFRNPVGIAAGF-DKHGEAVDGLYKLGFGFVEVGSVTPQPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSAV 156
Cdd:COG0167 2 LSVELAGLKFPNPVGLASGFfDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 157 EHRLRARQQKQTqlttdglPLGINLGKNktsvdAAADYVEGVRILGPL-ADYLVVNVSSPNTAG-LRSL-QGKTELRRLL 233
Cdd:COG0167 82 LERLLPAKRYDV-------PVIVNIGGN-----TVEDYVELARRLADAgADYLELNISCPNTPGgGRALgQDPEALAELL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 234 SKVLQERDalkgpqKPaVLVKIAPDLTaqDKEDIASVARELGIDGLIITNTTVSRPVGLQG---ALRSETGGLSGKPLRD 310
Cdd:COG0167 150 AAVKAATD------KP-VLVKLAPDLT--DIVEIARAAEEAGADGVIAINTTLGRAIDLETrrpVLANEAGGLSGPALKP 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9910194 311 LSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVKRELEALLKERGFNTV 385
Cdd:COG0167 221 IALRMVREVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSI 295
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
80-372 |
4.94e-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: 278.47 E-value: 4.94e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 80 VRVLGHKFRNPVGIAAGFD-KHGEAVDGLYKLGFGFVEVGSVTPQPQEGNPRPRVFRL-------PEDQAVINRYGFNSH 151
Cdd:cd02810 1 VNFLGLKLKNPFGVAAGPLlKTGELIARAAAAGFGAVVYKTVTLHPRPGNPLPRVARLppegesyPEQLGILNSFGLPNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 152 GLSAVEHRLRARQQKqtqltTDGLPLGINLGKNktsvdAAADYVEGVRILGPL-ADYLVVNVSSPNTAGLRSL-QGKTEL 229
Cdd:cd02810 81 GLDVWLQDIAKAKKE-----FPGQPLIASVGGS-----SKEDYVELARKIERAgAKALELNLSCPNVGGGRQLgQDPEAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 230 RRLLSKVLQERDalkgpqkPAVLVKIAPDLTAQDKEDIASVARELGIDGLIITNTTVSRPVGL---QGALRSETGGLSGK 306
Cdd:cd02810 151 ANLLKAVKAAVD-------IPLLVKLSPYFDLEDIVELAKAAERAGADGLTAINTISGRVVDLktvGPGPKRGTGGLSGA 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9910194 307 PLRDLSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVKRE 372
Cdd:cd02810 224 PIRPLALRWVARLAARLQLDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKIKKE 289
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
79-391 |
3.62e-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: 155.01 E-value: 3.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 79 EVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKLG-FGFVEVGSVTPQPQEGNPRPRVFRLPedqavinrYGF-NSHGLS-- 154
Cdd:cd04740 1 SVELAGLRLKNPVILASGTFGFGEELSRVADLGkLGAIVTKSITLEPREGNPPPRVVETP--------GGMlNAIGLQnp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 155 AVEHrlrARQQKQTQLTTDGLPLGINLGKNktSVDaaaDYVEGVRILGPL-ADYLVVNVSSPNT-AGLRSLQGKTEL-RR 231
Cdd:cd04740 73 GVEA---FLEELLPWLREFGTPVIASIAGS--TVE---EFVEVAEKLADAgADAIELNISCPNVkGGGMAFGTDPEAvAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 232 LLSKVlqeRDALKGPqkpaVLVKIAPDLTaqDKEDIASVARELGIDGLIITNTTVS--------RPVglqgaLRSETGGL 303
Cdd:cd04740 145 IVKAV---KKATDVP----VIVKLTPNVT--DIVEIARAAEEAGADGLTLINTLKGmaidietrKPI-----LGNVTGGL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 304 SG---KPLrdlstqTIREMYALTQGT-IPIIGVGGVSSGQDALEKIQAGASLVQLYTALtFLGPPVVARVKRELEALLKE 379
Cdd:cd04740 211 SGpaiKPI------ALRMVYQVYKAVeIPIIGVGGIASGEDALEFLMAGASAVQVGTAN-FVDPEAFKEIIEGLEAYLDE 283
|
330
....*....|..
gi 9910194 380 RGFNTVTDAIGV 391
Cdd:cd04740 284 EGIKSIEELVGL 295
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
77-394 |
4.14e-42 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 149.53 E-value: 4.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 77 MLEVRVLGHKFRNPVGIAAG-FDKHGEAVDGLYKLGFGFVEVGSVTPQPQEGNPRPRVFRLPedqavinrYGF-NSHGLS 154
Cdd:PRK07259 1 RLSVELPGLKLKNPVMPASGtFGFGGEYARFYDLNGLGAIVTKSTTLEPREGNPTPRIAETP--------GGMlNAIGLQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 155 --AVEHrlrARQQKQTQLTTDGLPLGINL-GKNktsvdaAADYVEGVRILG--PLADYLVVNVSSPNTAGLRSLQG-KTE 228
Cdd:PRK07259 73 npGVDA---FIEEELPWLEEFDTPIIANVaGST------EEEYAEVAEKLSkaPNVDAIELNISCPNVKHGGMAFGtDPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 229 L-RRLLSKVlqeRDALKGPqkpaVLVKIAPDLTaqDKEDIASVARELGIDGLIITNTTVS--------RPVglqgaLRSE 299
Cdd:PRK07259 144 LaYEVVKAV---KEVVKVP----VIVKLTPNVT--DIVEIAKAAEEAGADGLSLINTLKGmaidiktrKPI-----LANV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 300 TGGLSGKPLRDLSTQTIREMYALTQgtIPIIGVGGVSSGQDALEKIQAGASLVQLYTALtFLGPPVVARVKRELEALLKE 379
Cdd:PRK07259 210 TGGLSGPAIKPIALRMVYQVYQAVD--IPIIGMGGISSAEDAIEFIMAGASAVQVGTAN-FYDPYAFPKIIEGLEAYLDK 286
|
330
....*....|....*
gi 9910194 380 RGFNTVTDAIGVDHR 394
Cdd:PRK07259 287 YGIKSIEEIVGIAHK 301
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
78-393 |
8.10e-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: 148.73 E-value: 8.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 78 LEVRVLGHKFRNPVGIAAG-FDKHGEAVDGLYKLGFGFVEVGSVTPQPQEGNPRPRVFRLPedQAVINRYGFNSHGLSAV 156
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGiMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTIVETP--CGMLNAIGLQNPGVEAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 157 EHRLRarqqkqtqLTTDGLPLGINLGKNKTSVDAAADYVEGVRILGPLADYLVVNVSSPNTAGLRSLQGKTElrRLLSKV 236
Cdd:TIGR01037 79 LEELK--------PVREEFPTPLIASVYGSSVEEFAEVAEKLEKAPPYVDAYELNLSCPHVKGGGIAIGQDP--ELSADV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 237 LqerDALKGPQKPAVLVKIAPDLTaqDKEDIASVARELGIDGLIITNTTVSRPVGLQGA---LRSETGGLSGKPLRDLST 313
Cdd:TIGR01037 149 V---KAVKDKTDVPVFAKLSPNVT--DITEIAKAAEEAGADGLTLINTLRGMKIDIKTGkpiLANKTGGLSGPAIKPIAL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 314 QTIREMYALTQgtIPIIGVGGVSSGQDALEKIQAGASLVQLYTALtFLGPPVVARVKRELEALLKERGFNTVTDAIGVDH 393
Cdd:TIGR01037 224 RMVYDVYKMVD--IPIIGVGGITSFEDALEFLMAGASAVQVGTAV-YYRGFAFKKIIEGLIAFLKAEGFTSIEELIGIAH 300
|
|
| dihydoor_dh_Arch |
NF041011 |
dihydroorotate dehydrogenase PyrD; |
80-394 |
1.54e-33 |
|
dihydroorotate dehydrogenase PyrD;
Pssm-ID: 468940 Cd Length: 289 Bit Score: 126.59 E-value: 1.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 80 VRVLGHKFRNPVGIAAG-FDKHGEAVDGLYKL-GFGFVEVGSVTPQPQEGNPRPRVFRLPeDQAVINRYGFNSHGLSAVE 157
Cdd:NF041011 1 IRLAGLELEDPLIIASGiLPDVPEYIERVCEKyGPSAITTKTLTLNPLEPHKPPTVVKLH-DGCYLNAIGLGNPGIGLLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 158 hrlrarqqkqtQLTTDGLPLGINLGKNktSVDaaaDYVEGVRILGPLADYLVVNVSSPNTAGLrslqgKTELRRLLSKVL 237
Cdd:NF041011 80 -----------EIRVKLCPLIVSIGGS--SLE---EIVEVAEIAEEKADAIELNLSSPNRKGY-----GASLASLVREIV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 238 QErdaLKGPQKPAVLVKIAPdltaQDK-EDIASVARELGIDGLIITNTT--------VSRPVglqgaLRSETGGLSGKPL 308
Cdd:NF041011 139 KA---VKSVVKKPVFVKLGP----WDNvLEIAGKALEAGADGLTLINTVkgmaidveSFKPV-----LSYGTGGISGKCI 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 309 RDLSTQTIREMYAltQGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVKRELEALLKERGFNtVTDA 388
Cdd:NF041011 207 HPLAVRIIYDVYR--EYEAEIIGVGGVFSWRDAIELMSVGAKAVGVGTAIIDKGLSVISEIRKGLEEYLEEKGLK-LEDI 283
|
....*.
gi 9910194 389 IGVDHR 394
Cdd:NF041011 284 IGIAVK 289
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
77-390 |
2.07e-22 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 96.56 E-value: 2.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 77 MLEVRVLGHKFRNPVGIAAG-FDKHGEAVDGLYKLGFGFVEVGSVTPQPQEGNPRPRVFRLPedQAVINRYGFNSHGLSA 155
Cdd:PRK02506 1 STSTQIAGFKFDNCLMNAAGvYCMTKEELEEVEASAAGAFVTKSATLEPRPGNPEPRYADTP--LGSINSMGLPNLGFDY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 156 VEHRLRARQQKQTQLTTDGLPLGINLGKNKTSVDAAADyvegvrilgplADY--LV-VNVSSPNtaglrsLQGKTEL--- 229
Cdd:PRK02506 79 YLDYVLELQKKGPNKPHFLSVVGLSPEETHTILKKIQA-----------SDFngLVeLNLSCPN------VPGKPQIayd 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 230 ----RRLLSKVLQERdalkgpQKPAVlVKIAP--DLTAQDKedIASVARELGID----------GLII---TNTTVSRPv 290
Cdd:PRK02506 142 fettEQILEEVFTYF------TKPLG-VKLPPyfDIVHFDQ--AAAIFNKFPLAfvncinsignGLVIdpeDETVVIKP- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 291 glqgalRSETGGLSGKPLRDLSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVK 370
Cdd:PRK02506 212 ------KNGFGGIGGDYIKPTALANVRAFYQRLNPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLT 285
|
330 340
....*....|....*....|
gi 9910194 371 RELEALLKERGFNTVTDAIG 390
Cdd:PRK02506 286 KELKAIMAEKGYQSLEDFRG 305
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
80-377 |
1.71e-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: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 80 VRVLGHKFRNPVGIAAG-FDKHGEAVDGLYKLGFGFVEVGSVTPQPQEGNPRPRVFRLPEdqavinrYGFNSHGLS--AV 156
Cdd:cd04741 1 VTPPGLTISPPLMNAAGpWCTTLEDLLELAASSTGAVTTRSSTLAGRPGNPEPRYYAFPL-------GSINSLGLPnlGL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 157 EHRLRARQQKQTQLTTDGLPLGINLgkNKTSVDAAADYVEGVRILGPLADYLVVNVSSPNTAGLRSLQ-GKTELRRLLSK 235
Cdd:cd04741 74 DYYLEYIRTISDGLPGSAKPFFISV--TGSAEDIAAMYKKIAAHQKQFPLAMELNLSCPNVPGKPPPAyDFDATLEYLTA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 236 VlqeRDALKGPqkpaVLVKIAP--DLTAQDkeDIASV--ARELGIDGLIITNTT----VSRPVGLQGALRSETG--GLSG 305
Cdd:cd04741 152 V---KAAYSIP----VGVKTPPytDPAQFD--TLAEAlnAFACPISFITATNTLgnglVLDPERETVVLKPKTGfgGLAG 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9910194 306 KPLRDLSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVKRELEALL 377
Cdd:cd04741 223 AYLHPLALGNVRTFRRLLPSEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEKELEDIW 294
|
|
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
78-373 |
9.60e-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: 9.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 78 LEVRVLGHKFRNPVGIAAGFDKH-GEAVDGLYKLGFGFVEVGSVTP-QPQEGNPRPRVFRLP-EDQAVInryGFNSHGLS 154
Cdd:cd02940 2 LSVTFCGIKFPNPFGLASAPPTTsYPMIRRAFEAGWGGAVTKTLGLdKDIVTNVSPRIARLRtSGRGQI---GFNNIELI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 155 AvEHRLRARQQKQTQLTTD----GLPLGINLGKNKTSVDAAADYVE--GvrilgplADYLVVNVSSPntaglrslQGKTE 228
Cdd:cd02940 79 S-EKPLEYWLKEIRELKKDfpdkILIASIMCEYNKEDWTELAKLVEeaG-------ADALELNFSCP--------HGMPE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 229 lRRLLSKVLQERDALK--------GPQKPaVLVKIAPDLTaqDKEDIASVARELGIDGLIITNTTVS---------RP-V 290
Cdd:cd02940 143 -RGMGAAVGQDPELVEeicrwvreAVKIP-VIAKLTPNIT--DIREIARAAKEGGADGVSAINTVNSlmgvdldgtPPaP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 291 GLQGalRSETGGLSGKPLRDLSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVK 370
Cdd:cd02940 219 GVEG--KTTYGGYSGPAVKPIALRAVSQIARAPEPGLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMC 296
|
...
gi 9910194 371 REL 373
Cdd:cd02940 297 TGL 299
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
251-390 |
1.37e-10 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 62.65 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 251 VLVKIAPDLTaqdkeDI---ASVARELGIDGLIITNTTVS-----------RP-VGLQGALrsetGGLSGKPLRDLSTQT 315
Cdd:PRK08318 171 VIVKLTPNIT-----DIrepARAAKRGGADAVSLINTINSitgvdldrmipMPiVNGKSSH----GGYCGPAVKPIALNM 241
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9910194 316 IREMY--ALTQGtIPIIGVGGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVKRELEALLKERGFNTVTDAIG 390
Cdd:PRK08318 242 VAEIArdPETRG-LPISGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISGLSHYMDEKGFASLEDMVG 317
|
|
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
251-391 |
7.27e-09 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 57.15 E-value: 7.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 251 VLVKIAPDLTaqDKEDIASVARELGIDGLIITNTTVS-RPVGLQgALRSE--------TGGLSGKPLRDLS----TQTIR 317
Cdd:PLN02495 185 VWAKMTPNIT--DITQPARVALKSGCEGVAAINTIMSvMGINLD-TLRPEpcvegystPGGYSSKAVRPIAlakvMAIAK 261
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9910194 318 EMYALTQGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVKRELEALLKERGFNTVTDAIGV 391
Cdd:PLN02495 262 MMKSEFPEDRSLSGIGGVETGGDAAEFILLGADTVQVCTGVMMHGYPLVKNLCAELQDFMKKHNFSSIEDFRGA 335
|
|
| DHOD_like |
cd04739 |
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
231-387 |
5.31e-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: 5.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 231 RLLSKVlqeRDALKGPqkpaVLVKIAPDLTAqdkedIASVAREL---GIDGLIITN------------TTVSRPVglqga 295
Cdd:cd04739 153 DILRAV---KSAVTIP----VAVKLSPFFSA-----LAHMAKQLdaaGADGLVLFNrfyqpdidletlEVVPNLL----- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 296 lRSETGGLSGkPLRdlstqTIREMYALTQgtIPIIGVGGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVKRELEA 375
Cdd:cd04739 216 -LSSPAEIRL-PLR-----WIAILSGRVK--ASLAASGGVHDAEDVVKYLLAGADVVMTTSALLRHGPDYIGTLLAGLEA 286
|
170
....*....|..
gi 9910194 376 LLKERGFNTVTD 387
Cdd:cd04739 287 WMEEHGYESVQQ 298
|
|
| PRK07565 |
PRK07565 |
dihydroorotate dehydrogenase-like protein; |
333-390 |
1.21e-05 |
|
dihydroorotate dehydrogenase-like protein;
Pssm-ID: 236051 Cd Length: 334 Bit Score: 46.78 E-value: 1.21e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 9910194 333 GGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVKRELEALLKERGFNTVTDAIG 390
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 ... |
324-358 |
1.62e-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: 1.62e-03
10 20 30
....*....|....*....|....*....|....*
gi 9910194 324 QGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTAL 358
Cdd:cd04735 282 AGRLPLIAVGSINTPDDALEALETGADLVAIGRGL 316
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
98-354 |
3.02e-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: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 98 DKHGEAVDGLYKLGFGFVEVGSVTPQPQEGNPRPRVFrlpedqavinrygfnshglsavehrlrARQQKQTQlttdGLPL 177
Cdd:cd04722 12 GDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEV---------------------------LKEVAAET----DLPL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 178 GINLGKNktsvDAAADYVEGVRILGPL-ADYLVVNVSSPNTAGlrslqgktELRRLLSKVLQERDALKgpqkpaVLVKIA 256
Cdd:cd04722 61 GVQLAIN----DAAAAVDIAAAAARAAgADGVEIHGAVGYLAR--------EDLELIRELREAVPDVK------VVVKLS 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 257 PDLtaqdkEDIASVARELGIDGLIITNttvSRPVGLQGALRSETGGLSGKPLRDLStqtiremyaltqgtIPIIGVGGVS 336
Cdd:cd04722 123 PTG-----ELAAAAAEEAGVDEVGLGN---GGGGGGGRDAVPIADLLLILAKRGSK--------------VPVIAGGGIN 180
|
250
....*....|....*...
gi 9910194 337 SGQDALEKIQAGASLVQL 354
Cdd:cd04722 181 DPEDAAEALALGADGVIV 198
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
253-358 |
3.78e-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: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910194 253 VKIAPDLTAqdkEDIASVARELGIDGLIItnttvsrpvglQGAlrsETGGLSGKPLRDLST--QTIREMYaltqgTIPII 330
Cdd:cd04730 103 IKVIPTVTS---VEEARKAEAAGADALVA-----------QGA---EAGGHRGTFDIGTFAlvPEVRDAV-----DIPVI 160
|
90 100
....*....|....*....|....*...
gi 9910194 331 GVGGVSSGQDALEKIQAGASLVQLYTAL 358
Cdd:cd04730 161 AAGGIADGRGIAAALALGADGVQMGTRF 188
|
|
| |
