|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
51-460 |
0e+00 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 773.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 51 GRILTGATIGLAIAGGAYVSTADEATFCGWLFNATKVVNPFFALLDAEFAHKLAVSAAARGWVPREKRPDPAILGLEVWG 130
Cdd:PLN02826 1 GRLLTGALIGLAIAGGAYVSTVDEATFCGWLFNATKLVNPLFRLLDPETAHSLAISAAARGLVPREKRPDPSVLGVEVWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 131 RKFSNPIGLAAGFDKNAEATEGLLGMGFGFVEVGSVTPVPQEGNPKPRIFRLSQEGAIINRCGFNSEGIVVVAKRLGAQH 210
Cdd:PLN02826 81 RTFSNPIGLAAGFDKNAEAVEGLLGLGFGFVEIGSVTPLPQPGNPKPRVFRLREEGAIINRYGFNSEGIVAVAKRLGAQH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 211 GKRMLAETSaTSSSPSDDVKPGGKSGPGILGVNLGKNKTSEDAAADYVQGVHNLSQYADYLVINVSSPNTAGLRMLQGRK 290
Cdd:PLN02826 161 GKRKLDETS-SSSFSSDDVKAGGKAGPGILGVNLGKNKTSEDAAADYVQGVRALSQYADYLVINVSSPNTPGLRKLQGRK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 291 QLKDLVKKVQAARDEMQWGDEGPPPLLVKIAPDLSRGELEDIAAVALALHLDGLIISNTTVSRPDAVSNNPVATETGGLS 370
Cdd:PLN02826 240 QLKDLLKKVLAARDEMQWGEEGPPPLLVKIAPDLSKEDLEDIAAVALALGIDGLIISNTTISRPDSVLGHPHADEAGGLS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 371 GKPLFALSTNMLRDMYTLTRGKIPLIGCGGVSSGEDAYKKIRAGATLVQLYTGFAYGGPALIPQIKEELVKCLERDGFKS 450
Cdd:PLN02826 320 GKPLFDLSTEVLREMYRLTRGKIPLVGCGGVSSGEDAYKKIRAGASLVQLYTAFAYEGPALIPRIKAELAACLERDGFKS 399
|
410
....*....|
gi 26454657 451 IHEAIGADHR 460
Cdd:PLN02826 400 IQEAVGADHR 409
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
90-439 |
2.02e-180 |
|
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: 507.04 E-value: 2.02e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 90 PFFALLDAEFAHKLAVSAAARGWVPR---EKRPDPAILGLEVWGRKFSNPIGLAAGFDKNAEATEGLLGMGFGFVEVGSV 166
Cdd:cd04738 2 PLLFLLDPETAHRLAIRALKLGLGPPlllLLVYDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFVEVGTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 167 TPVPQEGNPKPRIFRLSQEGAIINRCGFNSEGIVVVAKRLGAQHGKRmlaetsatssspsddvkpggksgpGILGVNLGK 246
Cdd:cd04738 82 TPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRRPRG------------------------GPLGVNIGK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 247 NKTS--EDAAADYVQGVHNLSQYADYLVINVSSPNTAGLRMLQGRKQLKDLVKKVQAARDEMqwgdEGPPPLLVKIAPDL 324
Cdd:cd04738 138 NKDTplEDAVEDYVIGVRKLGPYADYLVVNVSSPNTPGLRDLQGKEALRELLTAVKEERNKL----GKKVPLLVKIAPDL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 325 SRGELEDIAAVALALHLDGLIISNTTVSRPDaVSNNPVATETGGLSGKPLFALSTNMLRDMYTLTRGKIPLIGCGGVSSG 404
Cdd:cd04738 214 SDEELEDIADVALEHGVDGIIATNTTISRPG-LLRSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSG 292
|
330 340 350
....*....|....*....|....*....|....*
gi 26454657 405 EDAYKKIRAGATLVQLYTGFAYGGPALIPQIKEEL 439
Cdd:cd04738 293 EDAYEKIRAGASLVQLYTGLVYEGPGLVKRIKREL 327
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
94-439 |
7.67e-121 |
|
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: 356.02 E-value: 7.67e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 94 LLDAEFAHKLAV------SAAARGWVPREKRPDPAILGLEVWGRKFSNPIGLAAGFDKNAEATEGLLGMGFGFVEVGSVT 167
Cdd:TIGR01036 10 LLDPESAHELTFqflrlgTGTPFLALLRSLFGASDPLEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAMGFGFLEIGTVT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 168 PVPQEGNPKPRIFRLSQEGAIINRCGFNSEGIVVVAKRLGAQHGKrmlaetsatssspsddvkpggksgpGILGVNLGKN 247
Cdd:TIGR01036 90 PKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLKRARYK-------------------------GPIGINIGKN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 248 K--TSEDAAADYVQGVHNLSQYADYLVINVSSPNTAGLRMLQGRKQLKDLVKKVQAARDEMQwgDEGPPPLLVKIAPDLS 325
Cdd:TIGR01036 145 KdtPSEDAKEDYAACLRKLGPLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAVKQEQDGLR--RVHRVPVLVKIAPDLT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 326 RGELEDIAAVALALHLDGLIISNTTVSRpDAVSNNPVATETGGLSGKPLFALSTNMLRDMYTLTRGKIPLIGCGGVSSGE 405
Cdd:TIGR01036 223 ESDLEDIADSLVELGIDGVIATNTTVSR-SLVQGPKNSDETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQ 301
|
330 340 350
....*....|....*....|....*....|....
gi 26454657 406 DAYKKIRAGATLVQLYTGFAYGGPALIPQIKEEL 439
Cdd:TIGR01036 302 DALEKIRAGASLLQIYSGFIYWGPPLVKEIVKEI 335
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
127-451 |
1.03e-110 |
|
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: 328.57 E-value: 1.03e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 127 EVWGRKFSNPIGLAAGF-DKNAEATEGLLGMGFGFVEVGSVTPVPQEGNPKPRIFRLSQEGAIINRCGFNSEGIVVVAKR 205
Cdd:COG0167 5 ELAGLKFPNPVGLASGFfDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDAFLER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 206 LgaqhgkrmlaetsatssspsddvKPGGKSGPGILgVNLGKNktsedAAADYVQGVHNLSQY-ADYLVINVSSPNTAG-L 283
Cdd:COG0167 85 L-----------------------LPAKRYDVPVI-VNIGGN-----TVEDYVELARRLADAgADYLELNISCPNTPGgG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 284 RML-QGRKQLKDLVKKVQAARDemqwgdegpPPLLVKIAPDLSrgELEDIAAVALALHLDGLIISNTTVSRP-DAVSNNP 361
Cdd:COG0167 136 RALgQDPEALAELLAAVKAATD---------KPVLVKLAPDLT--DIVEIARAAEEAGADGVIAINTTLGRAiDLETRRP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 362 V-ATETGGLSGKPLFALSTNMLRDMYTLTRGKIPLIGCGGVSSGEDAYKKIRAGATLVQLYTGFAYGGPALIPQIKEELV 440
Cdd:COG0167 205 VlANEAGGLSGPALKPIALRMVREVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLE 284
|
330
....*....|.
gi 26454657 441 KCLERDGFKSI 451
Cdd:COG0167 285 AYLEEKGFSSI 295
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
124-439 |
1.24e-97 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 295.03 E-value: 1.24e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 124 LGLEVWGRKFSNPIGLAAGFDKNAEATEGLLGMG-FGFVEVGSVTPVPQEGNPKPRIFRLsqEGAIINRCGFNSEGIVVV 202
Cdd:pfam01180 2 LATKIPGLDFKNPIGLASGFDKFGEEALKWLALGkFGAIEIKSVTPYPQPGNPTPRVFRL--PEGVLNRMGLNNPGLDAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 203 AKRLgaQHGKRmlaetsatssspsddvkpggKSGPGILGVNLGKNKTSEDaaaDYVQGVHNLSQYADYLVINVSSPNTAG 282
Cdd:pfam01180 80 LAEL--LKRRK--------------------EYPRPDLGINLSKAGMTVD---DYVEVARKIGPFADYIELNVSCPNTPG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 283 LRMLQGRKQLKDLVKKVQAARDEmqwgdegpPPLLVKIAPDLSRGELEDIAAVAL-ALHLDGLIISNTTVSRP--DAVSN 359
Cdd:pfam01180 135 LRALQTDPELAAILLKVVKEVSK--------VPVLVKLAPDLTDIVIIDIADVALgEDGLDGINATNTTVRGMriDLKTE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 360 NPV-ATETGGLSGKPLFALSTNMLRDMYTLTRGKIPLIGCGGVSSGEDAYKKIRAGATLVQLYTGFAYGGPALIPQIKEE 438
Cdd:pfam01180 207 KPIlANGTGGLSGPPIKPIALKVIRELYQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDE 286
|
.
gi 26454657 439 L 439
Cdd:pfam01180 287 L 287
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
51-460 |
0e+00 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 773.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 51 GRILTGATIGLAIAGGAYVSTADEATFCGWLFNATKVVNPFFALLDAEFAHKLAVSAAARGWVPREKRPDPAILGLEVWG 130
Cdd:PLN02826 1 GRLLTGALIGLAIAGGAYVSTVDEATFCGWLFNATKLVNPLFRLLDPETAHSLAISAAARGLVPREKRPDPSVLGVEVWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 131 RKFSNPIGLAAGFDKNAEATEGLLGMGFGFVEVGSVTPVPQEGNPKPRIFRLSQEGAIINRCGFNSEGIVVVAKRLGAQH 210
Cdd:PLN02826 81 RTFSNPIGLAAGFDKNAEAVEGLLGLGFGFVEIGSVTPLPQPGNPKPRVFRLREEGAIINRYGFNSEGIVAVAKRLGAQH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 211 GKRMLAETSaTSSSPSDDVKPGGKSGPGILGVNLGKNKTSEDAAADYVQGVHNLSQYADYLVINVSSPNTAGLRMLQGRK 290
Cdd:PLN02826 161 GKRKLDETS-SSSFSSDDVKAGGKAGPGILGVNLGKNKTSEDAAADYVQGVRALSQYADYLVINVSSPNTPGLRKLQGRK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 291 QLKDLVKKVQAARDEMQWGDEGPPPLLVKIAPDLSRGELEDIAAVALALHLDGLIISNTTVSRPDAVSNNPVATETGGLS 370
Cdd:PLN02826 240 QLKDLLKKVLAARDEMQWGEEGPPPLLVKIAPDLSKEDLEDIAAVALALGIDGLIISNTTISRPDSVLGHPHADEAGGLS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 371 GKPLFALSTNMLRDMYTLTRGKIPLIGCGGVSSGEDAYKKIRAGATLVQLYTGFAYGGPALIPQIKEELVKCLERDGFKS 450
Cdd:PLN02826 320 GKPLFDLSTEVLREMYRLTRGKIPLVGCGGVSSGEDAYKKIRAGASLVQLYTAFAYEGPALIPRIKAELAACLERDGFKS 399
|
410
....*....|
gi 26454657 451 IHEAIGADHR 460
Cdd:PLN02826 400 IQEAVGADHR 409
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
90-439 |
2.02e-180 |
|
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: 507.04 E-value: 2.02e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 90 PFFALLDAEFAHKLAVSAAARGWVPR---EKRPDPAILGLEVWGRKFSNPIGLAAGFDKNAEATEGLLGMGFGFVEVGSV 166
Cdd:cd04738 2 PLLFLLDPETAHRLAIRALKLGLGPPlllLLVYDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFVEVGTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 167 TPVPQEGNPKPRIFRLSQEGAIINRCGFNSEGIVVVAKRLGAQHGKRmlaetsatssspsddvkpggksgpGILGVNLGK 246
Cdd:cd04738 82 TPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRRPRG------------------------GPLGVNIGK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 247 NKTS--EDAAADYVQGVHNLSQYADYLVINVSSPNTAGLRMLQGRKQLKDLVKKVQAARDEMqwgdEGPPPLLVKIAPDL 324
Cdd:cd04738 138 NKDTplEDAVEDYVIGVRKLGPYADYLVVNVSSPNTPGLRDLQGKEALRELLTAVKEERNKL----GKKVPLLVKIAPDL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 325 SRGELEDIAAVALALHLDGLIISNTTVSRPDaVSNNPVATETGGLSGKPLFALSTNMLRDMYTLTRGKIPLIGCGGVSSG 404
Cdd:cd04738 214 SDEELEDIADVALEHGVDGIIATNTTISRPG-LLRSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSG 292
|
330 340 350
....*....|....*....|....*....|....*
gi 26454657 405 EDAYKKIRAGATLVQLYTGFAYGGPALIPQIKEEL 439
Cdd:cd04738 293 EDAYEKIRAGASLVQLYTGLVYEGPGLVKRIKREL 327
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
86-447 |
3.19e-163 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 463.86 E-value: 3.19e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 86 KVVNPFFALLDAEFAHKLAVSA-------AARGWVPREKRPDPAILGLEVWGRKFSNPIGLAAGFDKNAEATEGLLGMGF 158
Cdd:PRK05286 4 PLARPLLFKLDPETAHELTIRAlkrasrtPLLSLLRQRLTYTDPRLPVTVMGLTFPNPVGLAAGFDKNGEAIDALGALGF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 159 GFVEVGSVTPVPQEGNPKPRIFRLSQEGAIINRCGFNSEGIVVVAKRLgAQHGKRMlaetsatssspsddvkpggksgpg 238
Cdd:PRK05286 84 GFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERL-KKAYRGI------------------------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 239 ILGVNLGKNKTS--EDAAADYVQGVHNLSQYADYLVINVSSPNTAGLRMLQGRKQLKDLVKKVQAARDEMqwgdEGPPPL 316
Cdd:PRK05286 139 PLGINIGKNKDTplEDAVDDYLICLEKLYPYADYFTVNISSPNTPGLRDLQYGEALDELLAALKEAQAEL----HGYVPL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 317 LVKIAPDLSRGELEDIAAVALALHLDGLIISNTTVSRpDAVSNNPVATETGGLSGKPLFALSTNMLRDMYTLTRGKIPLI 396
Cdd:PRK05286 215 LVKIAPDLSDEELDDIADLALEHGIDGVIATNTTLSR-DGLKGLPNADEAGGLSGRPLFERSTEVIRRLYKELGGRLPII 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 26454657 397 GCGGVSSGEDAYKKIRAGATLVQLYTGFAYGGPALIPQIKEELVKCLERDG 447
Cdd:PRK05286 294 GVGGIDSAEDAYEKIRAGASLVQIYSGLIYEGPGLVKEIVRGLARLLRRDG 344
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
94-439 |
7.67e-121 |
|
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: 356.02 E-value: 7.67e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 94 LLDAEFAHKLAV------SAAARGWVPREKRPDPAILGLEVWGRKFSNPIGLAAGFDKNAEATEGLLGMGFGFVEVGSVT 167
Cdd:TIGR01036 10 LLDPESAHELTFqflrlgTGTPFLALLRSLFGASDPLEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAMGFGFLEIGTVT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 168 PVPQEGNPKPRIFRLSQEGAIINRCGFNSEGIVVVAKRLGAQHGKrmlaetsatssspsddvkpggksgpGILGVNLGKN 247
Cdd:TIGR01036 90 PKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLKRARYK-------------------------GPIGINIGKN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 248 K--TSEDAAADYVQGVHNLSQYADYLVINVSSPNTAGLRMLQGRKQLKDLVKKVQAARDEMQwgDEGPPPLLVKIAPDLS 325
Cdd:TIGR01036 145 KdtPSEDAKEDYAACLRKLGPLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAVKQEQDGLR--RVHRVPVLVKIAPDLT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 326 RGELEDIAAVALALHLDGLIISNTTVSRpDAVSNNPVATETGGLSGKPLFALSTNMLRDMYTLTRGKIPLIGCGGVSSGE 405
Cdd:TIGR01036 223 ESDLEDIADSLVELGIDGVIATNTTVSR-SLVQGPKNSDETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQ 301
|
330 340 350
....*....|....*....|....*....|....
gi 26454657 406 DAYKKIRAGATLVQLYTGFAYGGPALIPQIKEEL 439
Cdd:TIGR01036 302 DALEKIRAGASLLQIYSGFIYWGPPLVKEIVKEI 335
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
127-451 |
1.03e-110 |
|
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: 328.57 E-value: 1.03e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 127 EVWGRKFSNPIGLAAGF-DKNAEATEGLLGMGFGFVEVGSVTPVPQEGNPKPRIFRLSQEGAIINRCGFNSEGIVVVAKR 205
Cdd:COG0167 5 ELAGLKFPNPVGLASGFfDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDAFLER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 206 LgaqhgkrmlaetsatssspsddvKPGGKSGPGILgVNLGKNktsedAAADYVQGVHNLSQY-ADYLVINVSSPNTAG-L 283
Cdd:COG0167 85 L-----------------------LPAKRYDVPVI-VNIGGN-----TVEDYVELARRLADAgADYLELNISCPNTPGgG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 284 RML-QGRKQLKDLVKKVQAARDemqwgdegpPPLLVKIAPDLSrgELEDIAAVALALHLDGLIISNTTVSRP-DAVSNNP 361
Cdd:COG0167 136 RALgQDPEALAELLAAVKAATD---------KPVLVKLAPDLT--DIVEIARAAEEAGADGVIAINTTLGRAiDLETRRP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 362 V-ATETGGLSGKPLFALSTNMLRDMYTLTRGKIPLIGCGGVSSGEDAYKKIRAGATLVQLYTGFAYGGPALIPQIKEELV 440
Cdd:COG0167 205 VlANEAGGLSGPALKPIALRMVREVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLE 284
|
330
....*....|.
gi 26454657 441 KCLERDGFKSI 451
Cdd:COG0167 285 AYLEEKGFSSI 295
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
124-439 |
1.24e-97 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 295.03 E-value: 1.24e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 124 LGLEVWGRKFSNPIGLAAGFDKNAEATEGLLGMG-FGFVEVGSVTPVPQEGNPKPRIFRLsqEGAIINRCGFNSEGIVVV 202
Cdd:pfam01180 2 LATKIPGLDFKNPIGLASGFDKFGEEALKWLALGkFGAIEIKSVTPYPQPGNPTPRVFRL--PEGVLNRMGLNNPGLDAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 203 AKRLgaQHGKRmlaetsatssspsddvkpggKSGPGILGVNLGKNKTSEDaaaDYVQGVHNLSQYADYLVINVSSPNTAG 282
Cdd:pfam01180 80 LAEL--LKRRK--------------------EYPRPDLGINLSKAGMTVD---DYVEVARKIGPFADYIELNVSCPNTPG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 283 LRMLQGRKQLKDLVKKVQAARDEmqwgdegpPPLLVKIAPDLSRGELEDIAAVAL-ALHLDGLIISNTTVSRP--DAVSN 359
Cdd:pfam01180 135 LRALQTDPELAAILLKVVKEVSK--------VPVLVKLAPDLTDIVIIDIADVALgEDGLDGINATNTTVRGMriDLKTE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 360 NPV-ATETGGLSGKPLFALSTNMLRDMYTLTRGKIPLIGCGGVSSGEDAYKKIRAGATLVQLYTGFAYGGPALIPQIKEE 438
Cdd:pfam01180 207 KPIlANGTGGLSGPPIKPIALKVIRELYQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDE 286
|
.
gi 26454657 439 L 439
Cdd:pfam01180 287 L 287
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
130-438 |
1.01e-54 |
|
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: 184.09 E-value: 1.01e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 130 GRKFSNPIGLAAGFD-KNAEATEGLLGMGFGFVEVGSVTPVPQEGNPKPRIFRLSQEG-------AIINRCGFNSEGIVV 201
Cdd:cd02810 5 GLKLKNPFGVAAGPLlKTGELIARAAAAGFGAVVYKTVTLHPRPGNPLPRVARLPPEGesypeqlGILNSFGLPNLGLDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 202 VAkrlgaqhgkrmlaetsatssspsDDVKPGGKSGPG-ILGVNLGKNktsedAAADYVQGVHNLSQY-ADYLVINVSSPN 279
Cdd:cd02810 85 WL-----------------------QDIAKAKKEFPGqPLIASVGGS-----SKEDYVELARKIERAgAKALELNLSCPN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 280 TAGLRML-QGRKQLKDLVKKVQAARDemqwgdegpPPLLVKIAPDLSRGELEDIAAVALALHLDGLIISNTTVSRPdAVS 358
Cdd:cd02810 137 VGGGRQLgQDPEAVANLLKAVKAAVD---------IPLLVKLSPYFDLEDIVELAKAAERAGADGLTAINTISGRV-VDL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 359 NNPVA---TETGGLSGKPLFALSTNMLRDMYTLTRGKIPLIGCGGVSSGEDAYKKIRAGATLVQLYTGFAYGGPALIPQI 435
Cdd:cd02810 207 KTVGPgpkRGTGGLSGAPIRPLALRWVARLAARLQLDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKI 286
|
...
gi 26454657 436 KEE 438
Cdd:cd02810 287 KKE 289
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
127-457 |
1.93e-33 |
|
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: 127.67 E-value: 1.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 127 EVWGRKFSNPIGLAAG-FDKNAEATEGLLGMGFGFVEVGSVTPVPQEGNPKPRIFRLSqeGAIINRCGFNSEGIVVVAKR 205
Cdd:cd04740 3 ELAGLRLKNPVILASGtFGFGEELSRVADLGKLGAIVTKSITLEPREGNPPPRVVETP--GGMLNAIGLQNPGVEAFLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 206 LG---AQHGKRMLAETSAtsSSPSDDVKpggksgpgilgvnlgknktsedaAADYVQGVHnlsqyADYLVINVSSPNTAG 282
Cdd:cd04740 81 LLpwlREFGTPVIASIAG--STVEEFVE-----------------------VAEKLADAG-----ADAIELNISCPNVKG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 283 LRMLQGR--KQLKDLVKKVQAARDEmqwgdegppPLLVKIAPDLSRgeLEDIAAVALALHLDGLIISNT-TVSRPDAVSN 359
Cdd:cd04740 131 GGMAFGTdpEAVAEIVKAVKKATDV---------PVIVKLTPNVTD--IVEIARAAEEAGADGLTLINTlKGMAIDIETR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 360 NPV-ATETGGLSGKPLFALSTNMLRDMYTLTrgKIPLIGCGGVSSGEDAYKKIRAGATLVQLYTGfAYGGPALIPQIKEE 438
Cdd:cd04740 200 KPIlGNVTGGLSGPAIKPIALRMVYQVYKAV--EIPIIGVGGIASGEDALEFLMAGASAVQVGTA-NFVDPEAFKEIIEG 276
|
330
....*....|....*....
gi 26454657 439 LVKCLERDGFKSIHEAIGA 457
Cdd:cd04740 277 LEAYLDEEGIKSIEELVGL 295
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
124-460 |
2.09e-31 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 122.18 E-value: 2.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 124 LGLEVWGRKFSNPIGLAAG-FDKNAEATEGLLGMGFGFVEVGSVTPVPQEGNPKPRIFRLsqEGAIINRCGFNSEGIVVV 202
Cdd:PRK07259 2 LSVELPGLKLKNPVMPASGtFGFGGEYARFYDLNGLGAIVTKSTTLEPREGNPTPRIAET--PGGMLNAIGLQNPGVDAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 203 AKRLG---AQHGKRMLAETsatssspsddvkpGGKSgpgilgvnlgknktsedaAADYVQGVHNLSQY--ADYLVINVSS 277
Cdd:PRK07259 80 IEEELpwlEEFDTPIIANV-------------AGST------------------EEEYAEVAEKLSKApnVDAIELNISC 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 278 PNTAGLRMLQGRKQ--LKDLVKKVQAARDEmqwgdegppPLLVKIAPDLSRgeLEDIAAVALALHLDGLIISNTTVS-RP 354
Cdd:PRK07259 129 PNVKHGGMAFGTDPelAYEVVKAVKEVVKV---------PVIVKLTPNVTD--IVEIAKAAEEAGADGLSLINTLKGmAI 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 355 DAVSNNPV-ATETGGLSGKPLFALSTNMLRDMYTLTrgKIPLIGCGGVSSGEDAYKKIRAGATLVQLYTGFaYGGPALIP 433
Cdd:PRK07259 198 DIKTRKPIlANVTGGLSGPAIKPIALRMVYQVYQAV--DIPIIGMGGISSAEDAIEFIMAGASAVQVGTAN-FYDPYAFP 274
|
330 340
....*....|....*....|....*..
gi 26454657 434 QIKEELVKCLERDGFKSIHEAIGADHR 460
Cdd:PRK07259 275 KIIEGLEAYLDKYGIKSIEEIVGIAHK 301
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
124-459 |
2.08e-30 |
|
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: 119.46 E-value: 2.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 124 LGLEVWGRKFSNPIGLAAG-FDKNAEATEGLLGMGFGFVEVGSVTPVPQEGNPKPRIFRLSqeGAIINRCGFNSEGIVVV 202
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGiMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTIVETP--CGMLNAIGLQNPGVEAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 203 AKRLgaqhgkrmlaetsatssspsddvKPGGKSGPGILGVNL-GKnktSEDAAADYVQGVHNLSQYADYLVINVSSPN-- 279
Cdd:TIGR01037 79 LEEL-----------------------KPVREEFPTPLIASVyGS---SVEEFAEVAEKLEKAPPYVDAYELNLSCPHvk 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 280 TAGLRMLQGRKQLKDLVKKVQAARDEmqwgdegppPLLVKIAPDLSrgeleDIAAVALALH---LDGLIISNTTVS-RPD 355
Cdd:TIGR01037 133 GGGIAIGQDPELSADVVKAVKDKTDV---------PVFAKLSPNVT-----DITEIAKAAEeagADGLTLINTLRGmKID 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 356 AVSNNPV-ATETGGLSGKPLFALSTNMLRDMYTLTrgKIPLIGCGGVSSGEDAYKKIRAGATLVQLYTGFAYGGPALiPQ 434
Cdd:TIGR01037 199 IKTGKPIlANKTGGLSGPAIKPIALRMVYDVYKMV--DIPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYRGFAF-KK 275
|
330 340
....*....|....*....|....*
gi 26454657 435 IKEELVKCLERDGFKSIHEAIGADH 459
Cdd:TIGR01037 276 IIEGLIAFLKAEGFTSIEELIGIAH 300
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
130-439 |
1.91e-14 |
|
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: 73.51 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 130 GRKFSNPIGLAAG-FDKNAEATEGLLGMGFGFVEVGSVTPVPQEGNPKPRIFRLSQegAIINRCGFNSEGIvvvakrlga 208
Cdd:cd04741 5 GLTISPPLMNAAGpWCTTLEDLLELAASSTGAVTTRSSTLAGRPGNPEPRYYAFPL--GSINSLGLPNLGL--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 209 qhgkRMLAETSATSSspsDDVKPGGKsgPGILGVNlgknKTSEDAAADYVQGVHNLSQYADYLVINVSSPNTAGLRMLQ- 287
Cdd:cd04741 74 ----DYYLEYIRTIS---DGLPGSAK--PFFISVT----GSAEDIAAMYKKIAAHQKQFPLAMELNLSCPNVPGKPPPAy 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 288 GRKQLKDLVKKVQAArdemqwgdeGPPPLLVKIAPDLSRGELEDIAAvALALHLDGL-------IISNTTVSRPDAVSNN 360
Cdd:cd04741 141 DFDATLEYLTAVKAA---------YSIPVGVKTPPYTDPAQFDTLAE-ALNAFACPIsfitatnTLGNGLVLDPERETVV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 361 -PVATETGGLSGKPLFALSTNMLRDMYTLTRGKIPLIGCGGVSSGEDAYKKIRAGATLVQLYTGFAYGGPALIPQIKEEL 439
Cdd:cd04741 211 lKPKTGFGGLAGAYLHPLALGNVRTFRRLLPSEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEKEL 290
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
367-456 |
6.17e-14 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 72.29 E-value: 6.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 367 GGLSG---KPlFALSTnmLRDMYTLTRGKIPLIGCGGVSSGEDAYKKIRAGATLVQLYTGFAYGGPALIPQIKEELVKCL 443
Cdd:PRK02506 216 GGIGGdyiKP-TALAN--VRAFYQRLNPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAIM 292
|
90
....*....|...
gi 26454657 444 ERDGFKSIHEAIG 456
Cdd:PRK02506 293 AEKGYQSLEDFRG 305
|
|
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
268-423 |
1.50e-07 |
|
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: 52.67 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 268 ADYLVINVSSPNTAGLR-MLQGRKQLKDLVKKVqaardeMQWGDEGPP-PLLVKIAPDLsrGELEDIAAVALALHLDGLI 345
Cdd:cd02940 127 ADALELNFSCPHGMPERgMGAAVGQDPELVEEI------CRWVREAVKiPVIAKLTPNI--TDIREIARAAKEGGADGVS 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 346 ISNT--TVSRPDAVSNNPVA-----TETGGLSGKPLFALSTNMLRDMYTLTRGKIPLIGCGGVSSGEDAYKKIRAGATLV 418
Cdd:cd02940 199 AINTvnSLMGVDLDGTPPAPgvegkTTYGGYSGPAVKPIALRAVSQIARAPEPGLPISGIGGIESWEDAAEFLLLGASVV 278
|
....*
gi 26454657 419 QLYTG 423
Cdd:cd02940 279 QVCTA 283
|
|
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
315-457 |
5.72e-06 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 48.30 E-value: 5.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 315 PLLVKIAPDLSrgeleDI---AAVALALHLDGLIISNTTVS---------RPDAVSNNPvaTETGGLSGK---PL-FALS 378
Cdd:PLN02495 184 PVWAKMTPNIT-----DItqpARVALKSGCEGVAAINTIMSvmginldtlRPEPCVEGY--STPGGYSSKavrPIaLAKV 256
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26454657 379 TNMLRDMYTLTRGKIPLIGCGGVSSGEDAYKKIRAGATLVQLYTGFAYGGPALIPQIKEELVKCLERDGFKSIHEAIGA 457
Cdd:PLN02495 257 MAIAKMMKSEFPEDRSLSGIGGVETGGDAAEFILLGADTVQVCTGVMMHGYPLVKNLCAELQDFMKKHNFSSIEDFRGA 335
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
315-456 |
1.65e-05 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 46.86 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26454657 315 PLLVKIAPDLSrgeleDIAAVALALHL---DGLIISNT----TVSRPDAVSNNPVATETGGLSG------KPLfALstNM 381
Cdd:PRK08318 170 PVIVKLTPNIT-----DIREPARAAKRggaDAVSLINTinsiTGVDLDRMIPMPIVNGKSSHGGycgpavKPI-AL--NM 241
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26454657 382 LRDMYT--LTRGkIPLIGCGGVSSGEDAYKKIRAGATLVQLYTGFAYGGPALIPQIKEELVKCLERDGFKSIHEAIG 456
Cdd:PRK08318 242 VAEIARdpETRG-LPISGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISGLSHYMDEKGFASLEDMVG 317
|
|
| DHOD_like |
cd04739 |
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
390-453 |
2.97e-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: 45.68 E-value: 2.97e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26454657 390 RGKIPLIGCGGVSSGEDAYKKIRAGATLVQLYTGFAYGGPALIPQIKEELVKCLERDGFKSIHE 453
Cdd:cd04739 235 RVKASLAASGGVHDAEDVVKYLLAGADVVMTTSALLRHGPDYIGTLLAGLEAWMEEHGYESVQQ 298
|
|
| PRK07565 |
PRK07565 |
dihydroorotate dehydrogenase-like protein; |
390-457 |
7.57e-05 |
|
dihydroorotate dehydrogenase-like protein;
Pssm-ID: 236051 Cd Length: 334 Bit Score: 44.47 E-value: 7.57e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26454657 390 RGKIPLIGCGGVSSGEDAYKKIRAGATLVQLYTGFAYGGPALIPQIKEELVKCLERDGFKSIHEAIGA 457
Cdd:PRK07565 237 RVGADLAATTGVHDAEDVIKMLLAGADVVMIASALLRHGPDYIGTILRGLEDWMERHGYESLQQFRGS 304
|
|
| |
