|
Name |
Accession |
Description |
Interval |
E-value |
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
44-372 |
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: 545.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 44 LQRFVGGETAHLMAVRLIGLGLVPR---NNYKDPTSLEVHVMGRKFQNPVGMAAGFDKHGEAVDGLYRLGFGFVEVGTVT 120
Cdd:cd04738 3 LLFLLDPETAHRLAIRALKLGLGPPlllLLVYDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFVEVGTVT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 121 PKPQDGNPKPRVFRLESDQAVINRYGFNSCGLSAVHERLKAREHvqseltkAGKPLGINLGKNKLSP--DAVSDYVEGVR 198
Cdd:cd04738 83 PRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRRP-------RGGPLGVNIGKNKDTPleDAVEDYVIGVR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 199 TLGPLADYLVVNVSSPNTPGLRDLQGKEELRHLLDKVVKERDSLriENRPPVLVKIAPDLTTQDKQDIAEVIMEVGVDGV 278
Cdd:cd04738 156 KLGPYADYLVVNVSSPNTPGLRDLQGKEALRELLTAVKEERNKL--GKKVPLLVKIAPDLSDEELEDIADVALEHGVDGI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 279 MVSNTTVSRPDTLKDPNRVETGGLSGQPLKELSTQTVREMYTLTQGKLPIVGVGGVASGQDAMDKIRAGASLVQLYTALV 358
Cdd:cd04738 234 IATNTTISRPGLLRSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTGLV 313
|
330
....*....|....
gi 56693287 359 YQGPPVVNKIKREL 372
Cdd:cd04738 314 YEGPGLVKRIKREL 327
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
15-393 |
1.32e-176 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 498.49 E-value: 1.32e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 15 IIGCGSALFLGYLTASGDECFYASALMPVLQRFVGGETAHLMAVRLIGLGLVPRNNYKDPTSLEVHVMGRKFQNPVGMAA 94
Cdd:PLN02826 12 AIAGGAYVSTVDEATFCGWLFNATKLVNPLFRLLDPETAHSLAISAAARGLVPREKRPDPSVLGVEVWGRTFSNPIGLAA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 95 GFDKHGEAVDGLYRLGFGFVEVGTVTPKPQDGNPKPRVFRLESDQAVINRYGFNSCGLSAVHERLKARE----------- 163
Cdd:PLN02826 92 GFDKNAEAVEGLLGLGFGFVEIGSVTPLPQPGNPKPRVFRLREEGAIINRYGFNSEGIVAVAKRLGAQHgkrkldetsss 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 164 ------HVQSELTKAGkPLGINLGKNKLSPDAVSDYVEGVRTLGPLADYLVVNVSSPNTPGLRDLQGKEELRHLLDKVVK 237
Cdd:PLN02826 172 sfssddVKAGGKAGPG-ILGVNLGKNKTSEDAAADYVQGVRALSQYADYLVINVSSPNTPGLRKLQGRKQLKDLLKKVLA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 238 ERDSLRI--ENRPPVLVKIAPDLTTQDKQDIAEVIMEVGVDGVMVSNTTVSRPDTLKD-PNRVETGGLSGQPLKELSTQT 314
Cdd:PLN02826 251 ARDEMQWgeEGPPPLLVKIAPDLSKEDLEDIAAVALALGIDGLIISNTTISRPDSVLGhPHADEAGGLSGKPLFDLSTEV 330
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56693287 315 VREMYTLTQGKLPIVGVGGVASGQDAMDKIRAGASLVQLYTALVYQGPPVVNKIKRELDDLLKAQGFTCVAEAVGADHK 393
Cdd:PLN02826 331 LREMYRLTRGKIPLVGCGGVSSGEDAYKKIRAGASLVQLYTAFAYEGPALIPRIKAELAACLERDGFKSIQEAVGADHR 409
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
40-372 |
9.70e-147 |
|
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: 419.96 E-value: 9.70e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 40 LMPVLQRFVGGETAHLMAVRLIGLG------LVPRNNYKDPTSLEVHVMGRKFQNPVGMAAGFDKHGEAVDGLYRLGFGF 113
Cdd:TIGR01036 3 LVRKLLFLLDPESAHELTFQFLRLGtgtpflALLRSLFGASDPLEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAMGFGF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 114 VEVGTVTPKPQDGNPKPRVFRLESDQAVINRYGFNSCGLSAVHERLKAREHvqseltkaGKPLGINLGKNKLSP--DAVS 191
Cdd:TIGR01036 83 LEIGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLKRARY--------KGPIGINIGKNKDTPseDAKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 192 DYVEGVRTLGPLADYLVVNVSSPNTPGLRDLQGKEELRHLLDKVVKERDSLRIENRPPVLVKIAPDLTTQDKQDIAEVIM 271
Cdd:TIGR01036 155 DYAACLRKLGPLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAVKQEQDGLRRVHRVPVLVKIAPDLTESDLEDIADSLV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 272 EVGVDGVMVSNTTVSRPDTLKDPNRVETGGLSGQPLKELSTQTVREMYTLTQGKLPIVGVGGVASGQDAMDKIRAGASLV 351
Cdd:TIGR01036 235 ELGIDGVIATNTTVSRSLVQGPKNSDETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGASLL 314
|
330 340
....*....|....*....|.
gi 56693287 352 QLYTALVYQGPPVVNKIKREL 372
Cdd:TIGR01036 315 QIYSGFIYWGPPLVKEIVKEI 335
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
76-385 |
3.88e-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: 353.22 E-value: 3.88e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 76 SLEVHVMGRKFQNPVGMAAGF-DKHGEAVDGLYRLGFGFVEVGTVTPKPQDGNPKPRVFRLESDQAVINRYGFNSCGLSA 154
Cdd:COG0167 1 DLSVELAGLKFPNPVGLASGFfDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 155 VHERLKAREhvqseltKAGKPLGINLGKNklspdAVSDYVEGVRTLGPL-ADYLVVNVSSPNTPG-LRDL-QGKEELRHL 231
Cdd:COG0167 81 FLERLLPAK-------RYDVPVIVNIGGN-----TVEDYVELARRLADAgADYLELNISCPNTPGgGRALgQDPEALAEL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 232 LDKVVKErdslrieNRPPVLVKIAPDLTtqDKQDIAEVIMEVGVDGVMVSNTTVSRPDTLKDPNRV---ETGGLSGQPLK 308
Cdd:COG0167 149 LAAVKAA-------TDKPVLVKLAPDLT--DIVEIARAAEEAGADGVIAINTTLGRAIDLETRRPVlanEAGGLSGPALK 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56693287 309 ELSTQTVREMYTLTQGKLPIVGVGGVASGQDAMDKIRAGASLVQLYTALVYQGPPVVNKIKRELDDLLKAQGFTCVA 385
Cdd:COG0167 220 PIALRMVREVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSIS 296
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
76-376 |
2.71e-119 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 348.18 E-value: 2.71e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 76 SLEVHVMGRKFQNPVGMAAGFDKHGEAVDGLYRLG-FGFVEVGTVTPKPQDGNPKPRVFRLESDqaVINRYGFNSCGLSA 154
Cdd:pfam01180 1 MLATKIPGLDFKNPIGLASGFDKFGEEALKWLALGkFGAIEIKSVTPYPQPGNPTPRVFRLPEG--VLNRMGLNNPGLDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 155 VHERLKareHVQSEltKAGKPLGINLGKNKLSpdaVSDYVEGVRTLGPLADYLVVNVSSPNTPGLRDLQGKEELRHLLDK 234
Cdd:pfam01180 79 VLAELL---KRRKE--YPRPDLGINLSKAGMT---VDDYVEVARKIGPFADYIELNVSCPNTPGLRALQTDPELAAILLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 235 VVKERDSlrienrPPVLVKIAPDLTTQDKQDIAEVIM-EVGVDGVMVSNTTVSRP--DTLKDPNRVE--TGGLSGQPLKE 309
Cdd:pfam01180 151 VVKEVSK------VPVLVKLAPDLTDIVIIDIADVALgEDGLDGINATNTTVRGMriDLKTEKPILAngTGGLSGPPIKP 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56693287 310 LSTQTVREMYTLTQGKLPIVGVGGVASGQDAMDKIRAGASLVQLYTALVYQGPPVVNKIKRELDDLL 376
Cdd:pfam01180 225 IALKVIRELYQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
44-372 |
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: 545.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 44 LQRFVGGETAHLMAVRLIGLGLVPR---NNYKDPTSLEVHVMGRKFQNPVGMAAGFDKHGEAVDGLYRLGFGFVEVGTVT 120
Cdd:cd04738 3 LLFLLDPETAHRLAIRALKLGLGPPlllLLVYDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFVEVGTVT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 121 PKPQDGNPKPRVFRLESDQAVINRYGFNSCGLSAVHERLKAREHvqseltkAGKPLGINLGKNKLSP--DAVSDYVEGVR 198
Cdd:cd04738 83 PRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRRP-------RGGPLGVNIGKNKDTPleDAVEDYVIGVR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 199 TLGPLADYLVVNVSSPNTPGLRDLQGKEELRHLLDKVVKERDSLriENRPPVLVKIAPDLTTQDKQDIAEVIMEVGVDGV 278
Cdd:cd04738 156 KLGPYADYLVVNVSSPNTPGLRDLQGKEALRELLTAVKEERNKL--GKKVPLLVKIAPDLSDEELEDIADVALEHGVDGI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 279 MVSNTTVSRPDTLKDPNRVETGGLSGQPLKELSTQTVREMYTLTQGKLPIVGVGGVASGQDAMDKIRAGASLVQLYTALV 358
Cdd:cd04738 234 IATNTTISRPGLLRSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTGLV 313
|
330
....*....|....
gi 56693287 359 YQGPPVVNKIKREL 372
Cdd:cd04738 314 YEGPGLVKRIKREL 327
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
15-393 |
1.32e-176 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 498.49 E-value: 1.32e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 15 IIGCGSALFLGYLTASGDECFYASALMPVLQRFVGGETAHLMAVRLIGLGLVPRNNYKDPTSLEVHVMGRKFQNPVGMAA 94
Cdd:PLN02826 12 AIAGGAYVSTVDEATFCGWLFNATKLVNPLFRLLDPETAHSLAISAAARGLVPREKRPDPSVLGVEVWGRTFSNPIGLAA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 95 GFDKHGEAVDGLYRLGFGFVEVGTVTPKPQDGNPKPRVFRLESDQAVINRYGFNSCGLSAVHERLKARE----------- 163
Cdd:PLN02826 92 GFDKNAEAVEGLLGLGFGFVEIGSVTPLPQPGNPKPRVFRLREEGAIINRYGFNSEGIVAVAKRLGAQHgkrkldetsss 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 164 ------HVQSELTKAGkPLGINLGKNKLSPDAVSDYVEGVRTLGPLADYLVVNVSSPNTPGLRDLQGKEELRHLLDKVVK 237
Cdd:PLN02826 172 sfssddVKAGGKAGPG-ILGVNLGKNKTSEDAAADYVQGVRALSQYADYLVINVSSPNTPGLRKLQGRKQLKDLLKKVLA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 238 ERDSLRI--ENRPPVLVKIAPDLTTQDKQDIAEVIMEVGVDGVMVSNTTVSRPDTLKD-PNRVETGGLSGQPLKELSTQT 314
Cdd:PLN02826 251 ARDEMQWgeEGPPPLLVKIAPDLSKEDLEDIAAVALALGIDGLIISNTTISRPDSVLGhPHADEAGGLSGKPLFDLSTEV 330
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56693287 315 VREMYTLTQGKLPIVGVGGVASGQDAMDKIRAGASLVQLYTALVYQGPPVVNKIKRELDDLLKAQGFTCVAEAVGADHK 393
Cdd:PLN02826 331 LREMYRLTRGKIPLVGCGGVSSGEDAYKKIRAGASLVQLYTAFAYEGPALIPRIKAELAACLERDGFKSIQEAVGADHR 409
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
51-380 |
9.35e-176 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 493.53 E-value: 9.35e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 51 ETAHLMAVRLIGLGLVP--------RNNYKDPtSLEVHVMGRKFQNPVGMAAGFDKHGEAVDGLYRLGFGFVEVGTVTPK 122
Cdd:PRK05286 16 ETAHELTIRALKRASRTpllsllrqRLTYTDP-RLPVTVMGLTFPNPVGLAAGFDKNGEAIDALGALGFGFVEVGTVTPR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 123 PQDGNPKPRVFRLESDQAVINRYGFNSCGLSAVHERLKARehvqseltKAGKPLGINLGKNKLSP--DAVSDYVEGVRTL 200
Cdd:PRK05286 95 PQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKA--------YRGIPLGINIGKNKDTPleDAVDDYLICLEKL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 201 GPLADYLVVNVSSPNTPGLRDLQGKEELRHLLDKVVKERDSLRieNRPPVLVKIAPDLTTQDKQDIAEVIMEVGVDGVMV 280
Cdd:PRK05286 167 YPYADYFTVNISSPNTPGLRDLQYGEALDELLAALKEAQAELH--GYVPLLVKIAPDLSDEELDDIADLALEHGIDGVIA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 281 SNTTVSRPDTLKDPNRVETGGLSGQPLKELSTQTVREMYTLTQGKLPIVGVGGVASGQDAMDKIRAGASLVQLYTALVYQ 360
Cdd:PRK05286 245 TNTTLSRDGLKGLPNADEAGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGASLVQIYSGLIYE 324
|
330 340
....*....|....*....|
gi 56693287 361 GPPVVNKIKRELDDLLKAQG 380
Cdd:PRK05286 325 GPGLVKEIVRGLARLLRRDG 344
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
40-372 |
9.70e-147 |
|
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: 419.96 E-value: 9.70e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 40 LMPVLQRFVGGETAHLMAVRLIGLG------LVPRNNYKDPTSLEVHVMGRKFQNPVGMAAGFDKHGEAVDGLYRLGFGF 113
Cdd:TIGR01036 3 LVRKLLFLLDPESAHELTFQFLRLGtgtpflALLRSLFGASDPLEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAMGFGF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 114 VEVGTVTPKPQDGNPKPRVFRLESDQAVINRYGFNSCGLSAVHERLKAREHvqseltkaGKPLGINLGKNKLSP--DAVS 191
Cdd:TIGR01036 83 LEIGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLKRARY--------KGPIGINIGKNKDTPseDAKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 192 DYVEGVRTLGPLADYLVVNVSSPNTPGLRDLQGKEELRHLLDKVVKERDSLRIENRPPVLVKIAPDLTTQDKQDIAEVIM 271
Cdd:TIGR01036 155 DYAACLRKLGPLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAVKQEQDGLRRVHRVPVLVKIAPDLTESDLEDIADSLV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 272 EVGVDGVMVSNTTVSRPDTLKDPNRVETGGLSGQPLKELSTQTVREMYTLTQGKLPIVGVGGVASGQDAMDKIRAGASLV 351
Cdd:TIGR01036 235 ELGIDGVIATNTTVSRSLVQGPKNSDETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGASLL 314
|
330 340
....*....|....*....|.
gi 56693287 352 QLYTALVYQGPPVVNKIKREL 372
Cdd:TIGR01036 315 QIYSGFIYWGPPLVKEIVKEI 335
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
76-385 |
3.88e-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: 353.22 E-value: 3.88e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 76 SLEVHVMGRKFQNPVGMAAGF-DKHGEAVDGLYRLGFGFVEVGTVTPKPQDGNPKPRVFRLESDQAVINRYGFNSCGLSA 154
Cdd:COG0167 1 DLSVELAGLKFPNPVGLASGFfDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 155 VHERLKAREhvqseltKAGKPLGINLGKNklspdAVSDYVEGVRTLGPL-ADYLVVNVSSPNTPG-LRDL-QGKEELRHL 231
Cdd:COG0167 81 FLERLLPAK-------RYDVPVIVNIGGN-----TVEDYVELARRLADAgADYLELNISCPNTPGgGRALgQDPEALAEL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 232 LDKVVKErdslrieNRPPVLVKIAPDLTtqDKQDIAEVIMEVGVDGVMVSNTTVSRPDTLKDPNRV---ETGGLSGQPLK 308
Cdd:COG0167 149 LAAVKAA-------TDKPVLVKLAPDLT--DIVEIARAAEEAGADGVIAINTTLGRAIDLETRRPVlanEAGGLSGPALK 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56693287 309 ELSTQTVREMYTLTQGKLPIVGVGGVASGQDAMDKIRAGASLVQLYTALVYQGPPVVNKIKRELDDLLKAQGFTCVA 385
Cdd:COG0167 220 PIALRMVREVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSIS 296
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
76-376 |
2.71e-119 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 348.18 E-value: 2.71e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 76 SLEVHVMGRKFQNPVGMAAGFDKHGEAVDGLYRLG-FGFVEVGTVTPKPQDGNPKPRVFRLESDqaVINRYGFNSCGLSA 154
Cdd:pfam01180 1 MLATKIPGLDFKNPIGLASGFDKFGEEALKWLALGkFGAIEIKSVTPYPQPGNPTPRVFRLPEG--VLNRMGLNNPGLDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 155 VHERLKareHVQSEltKAGKPLGINLGKNKLSpdaVSDYVEGVRTLGPLADYLVVNVSSPNTPGLRDLQGKEELRHLLDK 234
Cdd:pfam01180 79 VLAELL---KRRKE--YPRPDLGINLSKAGMT---VDDYVEVARKIGPFADYIELNVSCPNTPGLRALQTDPELAAILLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 235 VVKERDSlrienrPPVLVKIAPDLTTQDKQDIAEVIM-EVGVDGVMVSNTTVSRP--DTLKDPNRVE--TGGLSGQPLKE 309
Cdd:pfam01180 151 VVKEVSK------VPVLVKLAPDLTDIVIIDIADVALgEDGLDGINATNTTVRGMriDLKTEKPILAngTGGLSGPPIKP 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56693287 310 LSTQTVREMYTLTQGKLPIVGVGGVASGQDAMDKIRAGASLVQLYTALVYQGPPVVNKIKRELDDLL 376
Cdd:pfam01180 225 IALKVIRELYQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
79-371 |
9.54e-77 |
|
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: 239.56 E-value: 9.54e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 79 VHVMGRKFQNPVGMAAGFD-KHGEAVDGLYRLGFGFVEVGTVTPKPQDGNPKPRVFRL-------ESDQAVINRYGFNSC 150
Cdd:cd02810 1 VNFLGLKLKNPFGVAAGPLlKTGELIARAAAAGFGAVVYKTVTLHPRPGNPLPRVARLppegesyPEQLGILNSFGLPNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 151 GLSAV-HERLKAREHVQseltkaGKPLGINLGKNklspdAVSDYVEGVRTLGPL-ADYLVVNVSSPNTPGLRDL-QGKEE 227
Cdd:cd02810 81 GLDVWlQDIAKAKKEFP------GQPLIASVGGS-----SKEDYVELARKIERAgAKALELNLSCPNVGGGRQLgQDPEA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 228 LRHLLDKVVKERDslrienrPPVLVKIAPDLTTQDKQDIAEVIMEVGVDGVMVSNTTVSRPDTLKDP---NRVETGGLSG 304
Cdd:cd02810 150 VANLLKAVKAAVD-------IPLLVKLSPYFDLEDIVELAKAAERAGADGLTAINTISGRVVDLKTVgpgPKRGTGGLSG 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56693287 305 QPLKELSTQTVREMYTLTQGKLPIVGVGGVASGQDAMDKIRAGASLVQLYTALVYQGPPVVNKIKRE 371
Cdd:cd02810 223 APIRPLALRWVARLAARLQLDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKIKKE 289
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
77-392 |
2.96e-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: 139.87 E-value: 2.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 77 LEVHVMGRKFQNPVGMAAG-FDKHGEAVDGLYRLGFGFVEVGTVTPKPQDGNPKPRVfrLESDQAVINRYGFNSCGLSAV 155
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGiMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTI--VETPCGMLNAIGLQNPGVEAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 156 herlkaREHVQSELTKAGKPLGINL-GKnklSPDAVSDYVEGVRTLGPLADYLVVNVSSPNTPGLRDLQGKE-ELRHLLD 233
Cdd:TIGR01037 79 ------LEELKPVREEFPTPLIASVyGS---SVEEFAEVAEKLEKAPPYVDAYELNLSCPHVKGGGIAIGQDpELSADVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 234 KVVKERdslrieNRPPVLVKIAPDLTtqDKQDIAEVIMEVGVDGVMVSNTTVSRPDTLKDPNRV---ETGGLSGQPLKEL 310
Cdd:TIGR01037 150 KAVKDK------TDVPVFAKLSPNVT--DITEIAKAAEEAGADGLTLINTLRGMKIDIKTGKPIlanKTGGLSGPAIKPI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 311 STQTVREMYTLTQgkLPIVGVGGVASGQDAMDKIRAGASLVQLYTAlVYQGPPVVNKIKRELDDLLKAQGFTCVAEAVGA 390
Cdd:TIGR01037 222 ALRMVYDVYKMVD--IPIIGVGGITSFEDALEFLMAGASAVQVGTA-VYYRGFAFKKIIEGLIAFLKAEGFTSIEELIGI 298
|
..
gi 56693287 391 DH 392
Cdd:TIGR01037 299 AH 300
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
78-390 |
2.23e-37 |
|
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: 137.30 E-value: 2.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 78 EVHVMGRKFQNPVGMAAGFDKHGEAVDGLYRLG-FGFVEVGTVTPKPQDGNPKPRVFrlESDQAVINRYGFNSCGLSAvh 156
Cdd:cd04740 1 SVELAGLRLKNPVILASGTFGFGEELSRVADLGkLGAIVTKSITLEPREGNPPPRVV--ETPGGMLNAIGLQNPGVEA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 157 erlkAREHVQSELTKAGKPLGINLGKnklspDAVSDYVEGVRTLGPL-ADYLVVNVSSPNTP-GLRDLQGKEELRHLLDK 234
Cdd:cd04740 77 ----FLEELLPWLREFGTPVIASIAG-----STVEEFVEVAEKLADAgADAIELNISCPNVKgGGMAFGTDPEAVAEIVK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 235 VVKERDSLrienrpPVLVKIAPDLTtqDKQDIAEVIMEVGVDGVMVSNTtvsrpdtLK----DPNRVE------TGGLSG 304
Cdd:cd04740 148 AVKKATDV------PVIVKLTPNVT--DIVEIARAAEEAGADGLTLINT-------LKgmaiDIETRKpilgnvTGGLSG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 305 QPLKELSTQTVREMYTLTqgKLPIVGVGGVASGQDAMDKIRAGASLVQLYTAlVYQGPPVVNKIKRELDDLLKAQGFTCV 384
Cdd:cd04740 213 PAIKPIALRMVYQVYKAV--EIPIIGVGGIASGEDALEFLMAGASAVQVGTA-NFVDPEAFKEIIEGLEAYLDEEGIKSI 289
|
....*.
gi 56693287 385 AEAVGA 390
Cdd:cd04740 290 EELVGL 295
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
77-393 |
3.12e-33 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 126.03 E-value: 3.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 77 LEVHVMGRKFQNPVGMAAG-FDKHGEAVDGLYRLGFGFVEVGTVTPKPQDGNPKPRVFRLESdqavinryGF-NSCGLS- 153
Cdd:PRK07259 2 LSVELPGLKLKNPVMPASGtFGFGGEYARFYDLNGLGAIVTKSTTLEPREGNPTPRIAETPG--------GMlNAIGLQn 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 154 -----AVHERLKAREhvqseltKAGKPLGINLGKNklSPDavsDYVEGVRTLG--PLADYLVVNVSSPN----------T 216
Cdd:PRK07259 74 pgvdaFIEEELPWLE-------EFDTPIIANVAGS--TEE---EYAEVAEKLSkaPNVDAIELNISCPNvkhggmafgtD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 217 PGLrdlqgkeelrhlLDKVVKE-RDSLRIenrpPVLVKIAPDLTtqDKQDIAEVIMEVGVDGVMVSNTTVS-RPDT-LKD 293
Cdd:PRK07259 142 PEL------------AYEVVKAvKEVVKV----PVIVKLTPNVT--DIVEIAKAAEEAGADGLSLINTLKGmAIDIkTRK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 294 P---NRveTGGLSGQPLKELSTQTVREMYTLTqgKLPIVGVGGVASGQDAMDKIRAGASLVQLYTAlVYQGPPVVNKIKR 370
Cdd:PRK07259 204 PilaNV--TGGLSGPAIKPIALRMVYQVYQAV--DIPIIGMGGISSAEDAIEFIMAGASAVQVGTA-NFYDPYAFPKIIE 278
|
330 340
....*....|....*....|...
gi 56693287 371 ELDDLLKAQGFTCVAEAVGADHK 393
Cdd:PRK07259 279 GLEAYLDKYGIKSIEEIVGIAHK 301
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
79-376 |
6.31e-23 |
|
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: 97.78 E-value: 6.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 79 VHVMGRKFQNPVGMAAG-FDKHGEAVDGLYRLGFGFVEVGTVTPKPQDGNPKPRVFRLESdqavinrYGFNSCGLS--AV 155
Cdd:cd04741 1 VTPPGLTISPPLMNAAGpWCTTLEDLLELAASSTGAVTTRSSTLAGRPGNPEPRYYAFPL-------GSINSLGLPnlGL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 156 HERLKAREHVQSELTKAGKPLGINLgkNKLSPDAVSDYVEGVRTLGPLADYLVVNVSSPNTPGlrdlqgKEELRHLLDKV 235
Cdd:cd04741 74 DYYLEYIRTISDGLPGSAKPFFISV--TGSAEDIAAMYKKIAAHQKQFPLAMELNLSCPNVPG------KPPPAYDFDAT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 236 VKERDSLRIENRPPVLVKIAPdLTTQDKQDIAEVIMEVGVDGVMVSNTTVSRPDTLK-DPNRVET--------GGLSGQP 306
Cdd:cd04741 146 LEYLTAVKAAYSIPVGVKTPP-YTDPAQFDTLAEALNAFACPISFITATNTLGNGLVlDPERETVvlkpktgfGGLAGAY 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 307 LKELSTQTVREMYTLTQGKLPIVGVGGVASGQDAMDKIRAGASLVQLYTALVYQGPPVVNKIKRELDDLL 376
Cdd:cd04741 225 LHPLALGNVRTFRRLLPSEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEKELEDIW 294
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
76-389 |
6.55e-21 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 92.32 E-value: 6.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 76 SLEVHVMGRKFQNPVGMAAG-FDKHGEAVDGLYRLGFGFVEVGTVTPKPQDGNPKPRVFRLEsdqavinrYG-FNSCGLS 153
Cdd:PRK02506 1 STSTQIAGFKFDNCLMNAAGvYCMTKEELEEVEASAAGAFVTKSATLEPRPGNPEPRYADTP--------LGsINSMGLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 154 avHERLKAREHVQSELTKAGKPLGINLGKNKLSPDAVSDYVEGVRTlgplADY--LV-VNVSSPNTPGlrdlqgKEELRH 230
Cdd:PRK02506 73 --NLGFDYYLDYVLELQKKGPNKPHFLSVVGLSPEETHTILKKIQA----SDFngLVeLNLSCPNVPG------KPQIAY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 231 LLDKVVKERDSLRIENRPPVLVKIAP--DLTTQDKqdIAEVIMEVGVDGV----MVSNTTVSRPDTlkdpnrvET----- 299
Cdd:PRK02506 141 DFETTEQILEEVFTYFTKPLGVKLPPyfDIVHFDQ--AAAIFNKFPLAFVncinSIGNGLVIDPED-------ETvvikp 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 300 ----GGLSGQPLKELSTQTVREMYTLTQGKLPIVGVGGVASGQDAMDKIRAGASLVQLYTALVYQGPPVVNKIKRELDDL 375
Cdd:PRK02506 212 kngfGGIGGDYIKPTALANVRAFYQRLNPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAI 291
|
330
....*....|....
gi 56693287 376 LKAQGFTCVAEAVG 389
Cdd:PRK02506 292 MAEKGYQSLEDFRG 305
|
|
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
77-372 |
7.80e-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: 77.32 E-value: 7.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 77 LEVHVMGRKFQNPVGMAAGFDKH-GEAVDGLYRLGFGFVEVGTVTP-KPQDGNPKPRVFRL-ESDQAVInryGFNSCGL- 152
Cdd:cd02940 2 LSVTFCGIKFPNPFGLASAPPTTsYPMIRRAFEAGWGGAVTKTLGLdKDIVTNVSPRIARLrTSGRGQI---GFNNIELi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 153 --SAVHERLKAREHVQSELTKagKPL--GINLGKNKlspDAVSDYVEGVRTLGplADYLVVNVSSPNTPGLRDL-----Q 223
Cdd:cd02940 79 seKPLEYWLKEIRELKKDFPD--KILiaSIMCEYNK---EDWTELAKLVEEAG--ADALELNFSCPHGMPERGMgaavgQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 224 GKEelrhLLDKVVKE-RDSLRIenrpPVLVKIAPDLTtqDKQDIAEVIMEVGVDGVMVSNT--TVSRPDTLKDPN----- 295
Cdd:cd02940 152 DPE----LVEEICRWvREAVKI----PVIAKLTPNIT--DIREIARAAKEGGADGVSAINTvnSLMGVDLDGTPPapgve 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56693287 296 -RVETGGLSGQPLKELSTQTVREMYTLTQGKLPIVGVGGVASGQDAMDKIRAGASLVQLYTALVYQGPPVVNKIKREL 372
Cdd:cd02940 222 gKTTYGGYSGPAVKPIALRAVSQIARAPEPGLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
|
|
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
249-390 |
6.63e-12 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 66.40 E-value: 6.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 249 PVLVKIAPDLTtqDKQDIAEVIMEVGVDGVMVSNTTVS----RPDTLKDPNRVE----TGGLSGQPLKELSTQTVREMYT 320
Cdd:PLN02495 184 PVWAKMTPNIT--DITQPARVALKSGCEGVAAINTIMSvmgiNLDTLRPEPCVEgystPGGYSSKAVRPIALAKVMAIAK 261
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56693287 321 LTQGKLP----IVGVGGVASGQDAMDKIRAGASLVQLYTALVYQGPPVVNKIKRELDDLLKAQGFTCVAEAVGA 390
Cdd:PLN02495 262 MMKSEFPedrsLSGIGGVETGGDAAEFILLGADTVQVCTGVMMHGYPLVKNLCAELQDFMKKHNFSSIEDFRGA 335
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
247-396 |
9.21e-11 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 63.04 E-value: 9.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 247 RPPVLVKIAPDLTtqdkqDI---AEVIMEVGVDGVMVSNTTVSRpdTLKDPNRVET----------GGLSGQPLKELSTQ 313
Cdd:PRK08318 168 RLPVIVKLTPNIT-----DIrepARAAKRGGADAVSLINTINSI--TGVDLDRMIPmpivngksshGGYCGPAVKPIALN 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 314 TVREMYTLTQGK-LPIVGVGGVASGQDAMDKIRAGASLVQLYTALVYQGPPVVNKIKRELDDLLKAQGFTCVAEAVG-AD 391
Cdd:PRK08318 241 MVAEIARDPETRgLPISGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISGLSHYMDEKGFASLEDMVGlAV 320
|
....*
gi 56693287 392 HKTTE 396
Cdd:PRK08318 321 PNVTD 325
|
|
| PRK07565 |
PRK07565 |
dihydroorotate dehydrogenase-like protein; |
204-386 |
4.61e-07 |
|
dihydroorotate dehydrogenase-like protein;
Pssm-ID: 236051 Cd Length: 334 Bit Score: 51.41 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 204 ADYLVVNV-SSPNTPglrDLQGKE-ELRHL--LDKVvkeRDSLRIenrpPVLVKIAPDLTTQdkQDIAEVIMEVGVDGV- 278
Cdd:PRK07565 128 ADALELNIyYLPTDP---DISGAEvEQRYLdiLRAV---KSAVSI----PVAVKLSPYFSNL--ANMAKRLDAAGADGLv 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 279 ----------------MVSNTTVSRPDTLKDPNRvETGGLSGQPlkelstqtvremytltqgKLPIVGVGGVASGQDAMD 342
Cdd:PRK07565 196 lfnrfyqpdidletleVVPGLVLSTPAELRLPLR-WIAILSGRV------------------GADLAATTGVHDAEDVIK 256
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 56693287 343 KIRAGASLVQLYTALVYQGPPVVNKIKRELDDLLKAQGFTCVAE 386
Cdd:PRK07565 257 MLLAGADVVMIASALLRHGPDYIGTILRGLEDWMERHGYESLQQ 300
|
|
| DHOD_like |
cd04739 |
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
204-386 |
5.11e-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: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 204 ADYLVVNVSSpnTPGLRDLQGKE-ELRHLlDKVVKERDSLRIenrpPVLVKIAPDLTTQdkQDIAEVIMEVGVDGV---- 278
Cdd:cd04739 126 ADALELNIYA--LPTDPDISGAEvEQRYL-DILRAVKSAVTI----PVAVKLSPFFSAL--AHMAKQLDAAGADGLvlfn 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 279 -------------MVSNTTVSRPDTLKDPNRvETGGLSGQPlkelstqtvremytltqgKLPIVGVGGVASGQDAMDKIR 345
Cdd:cd04739 197 rfyqpdidletleVVPNLLLSSPAEIRLPLR-WIAILSGRV------------------KASLAASGGVHDAEDVVKYLL 257
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 56693287 346 AGASLVQLYTALVYQGPPVVNKIKRELDDLLKAQGFTCVAE 386
Cdd:cd04739 258 AGADVVMTTSALLRHGPDYIGTLLAGLEAWMEEHGYESVQQ 298
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
256-398 |
1.16e-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: 43.74 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693287 256 PDLTTQDKQDIAEVIMEVGVDGVMVSNTtvsrpDTLKDPNRVETGGlsgQPLKELSTQTVremytltQGKLPIVGVGGVA 335
Cdd:cd04735 230 PGIRMEDTLALVDKLADKGLDYLHISLW-----DFDRKSRRGRDDN---QTIMELVKERI-------AGRLPLIAVGSIN 294
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56693287 336 SGQDAMDKIRAGASLVQLYTALVYQgPPVVNKIKRELDDLLKAQgftcVAEAVGADHKTTEKM 398
Cdd:cd04735 295 TPDDALEALETGADLVAIGRGLLVD-PDWVEKIKEGREDEINLE----IDPDDLEELKIPPAL 352
|
|
| |
