|
Name |
Accession |
Description |
Interval |
E-value |
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
52-386 |
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: 506.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 52 MPMVHkFVDGEDSHRWAVRAASWGLLPRFGWN-RKEYPELKCELFGREFKNPIGLAAGFDKDGQAITQLAKnSGFGLIEI 130
Cdd:cd04738 1 RPLLF-LLDPETAHRLAIRALKLGLGPPLLLLlVYDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLA-LGFGFVEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 131 GSVTPIPQPGNNRPRVFRLLEDEGVINRYGFNSDGVGRVHQRVRSARDSWVPesyayFGVNLGKNKLT--EDAKLDYEIG 208
Cdd:cd04738 79 GTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRRPRGGP-----LGVNIGKNKDTplEDAVEDYVIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 209 VNYFAPHCDYLVLNVSSPNTPGLRSMQKKSDLEKLLAYVHQALEmhKLEKQPQVFLKIAPDLIESELKDIAQVVTNKKfa 288
Cdd:cd04738 154 VRKLGPYADYLVVNVSSPNTPGLRDLQGKEALRELLTAVKEERN--KLGKKVPLLVKIAPDLSDEELEDIADVALEHG-- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 289 IDGIIVSNTTIARPDYLRSENKTETGGLSGAPVREISTECVRKIYKLTNGQIPIIGCGGVFSGADAYEKIRAGASLVQLY 368
Cdd:cd04738 230 VDGIIATNTTISRPGLLRSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLY 309
|
330
....*....|....*...
gi 17509475 369 SAFVYEGFPVIGKIKREL 386
Cdd:cd04738 310 TGLVYEGPGLVKRIKREL 327
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
46-394 |
2.76e-162 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 459.63 E-value: 2.76e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 46 FYKKAVMPMVHKFvDGEDSHRWAVRAASWGLLPRFGWNRKE-----YPELKCELFGREFKNPIGLAAGFDKDGQAITQLA 120
Cdd:PRK05286 1 MYYPLARPLLFKL-DPETAHELTIRALKRASRTPLLSLLRQrltytDPRLPVTVMGLTFPNPVGLAAGFDKNGEAIDALG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 121 KNsGFGLIEIGSVTPIPQPGNNRPRVFRLLEDEGVINRYGFNSDGVGRVHQRVRSARDSwVPesyayFGVNLGKNKLT-- 198
Cdd:PRK05286 80 AL-GFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKAYRG-IP-----LGINIGKNKDTpl 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 199 EDAKLDYEIGVNYFAPHCDYLVLNVSSPNTPGLRSMQKKSDLEKLLAYVHQAleMHKLEKQPQVFLKIAPDLIESELKDI 278
Cdd:PRK05286 153 EDAVDDYLICLEKLYPYADYFTVNISSPNTPGLRDLQYGEALDELLAALKEA--QAELHGYVPLLVKIAPDLSDEELDDI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 279 AQVVtnKKFAIDGIIVSNTTIARPDYLRSENKTETGGLSGAPVREISTECVRKIYKLTNGQIPIIGCGGVFSGADAYEKI 358
Cdd:PRK05286 231 ADLA--LEHGIDGVIATNTTLSRDGLKGLPNADEAGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKI 308
|
330 340 350
....*....|....*....|....*....|....*.
gi 17509475 359 RAGASLVQLYSAFVYEGFPVIGKIKRELVELLRKDG 394
Cdd:PRK05286 309 RAGASLVQIYSGLIYEGPGLVKEIVRGLARLLRRDG 344
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
59-386 |
1.38e-118 |
|
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: 348.31 E-value: 1.38e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 59 VDGEDSHRWAVRAASWG------LLPRFGWNRKEYPELKCelFGREFKNPIGLAAGFDKDGQAITQLAKnSGFGLIEIGS 132
Cdd:TIGR01036 11 LDPESAHELTFQFLRLGtgtpflALLRSLFGASDPLEVTV--LGLKFPNPLGLAAGFDKDGEAIDALGA-MGFGFLEIGT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 133 VTPIPQPGNNRPRVFRLLEDEGVINRYGFNSDGVGRVHQRVRSARDSWVpesyayFGVNLGKNKLT--EDAKLDYEIGVN 210
Cdd:TIGR01036 88 VTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLKRARYKGP------IGINIGKNKDTpsEDAKEDYAACLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 211 YFAPHCDYLVLNVSSPNTPGLRSMQKKSDLEKLLAYVHQALEMHKLEKQPQVFLKIAPDLIESELKDIAQVVtnKKFAID 290
Cdd:TIGR01036 162 KLGPLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAVKQEQDGLRRVHRVPVLVKIAPDLTESDLEDIADSL--VELGID 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 291 GIIVSNTTIARPDYLRSENKTETGGLSGAPVREISTECVRKIYKLTNGQIPIIGCGGVFSGADAYEKIRAGASLVQLYSA 370
Cdd:TIGR01036 240 GVIATNTTVSRSLVQGPKNSDETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGASLLQIYSG 319
|
330
....*....|....*.
gi 17509475 371 FVYEGFPVIGKIKREL 386
Cdd:TIGR01036 320 FIYWGPPLVKEIVKEI 335
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
90-399 |
2.92e-112 |
|
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: 330.88 E-value: 2.92e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 90 LKCELFGREFKNPIGLAAGF-DKDGQAITQLAkNSGFGLIEIGSVTPIPQPGNNRPRVFRLLEDEGVINRYGFNSDGVGR 168
Cdd:COG0167 2 LSVELAGLKFPNPVGLASGFfDKNAEYIDALD-LLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 169 VHQRVRSARDSWVPesyayFGVNLGKNklTEDaklDYEIGVNYFAPH-CDYLVLNVSSPNTPG-LRSM-QKKSDLEKLLA 245
Cdd:COG0167 81 FLERLLPAKRYDVP-----VIVNIGGN--TVE---DYVELARRLADAgADYLELNISCPNTPGgGRALgQDPEALAELLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 246 YVHQALemhkleKQPqVFLKIAPDLieSELKDIAQVVtnKKFAIDGIIVSNTTIARPDYLRSEN---KTETGGLSGAPVR 322
Cdd:COG0167 151 AVKAAT------DKP-VLVKLAPDL--TDIVEIARAA--EEAGADGVIAINTTLGRAIDLETRRpvlANEAGGLSGPALK 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17509475 323 EISTECVRKIYKLTNGQIPIIGCGGVFSGADAYEKIRAGASLVQLYSAFVYEGFPVIGKIKRELVELLRKDGFSHVS 399
Cdd:COG0167 220 PIALRMVREVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSIS 296
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
90-390 |
4.61e-101 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 301.96 E-value: 4.61e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 90 LKCELFGREFKNPIGLAAGFDKDGQAITQLAKNSGFGLIEIGSVTPIPQPGNNRPRVFRLleDEGVINRYGFNSDGVGRV 169
Cdd:pfam01180 2 LATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVTPYPQPGNPTPRVFRL--PEGVLNRMGLNNPGLDAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 170 HQRVRSardsWVPESYAYF-GVNLGKNKLTEDaklDYEIGVNYFAPHCDYLVLNVSSPNTPGLRSMQKKSDLEKLLAYVH 248
Cdd:pfam01180 80 LAELLK----RRKEYPRPDlGINLSKAGMTVD---DYVEVARKIGPFADYIELNVSCPNTPGLRALQTDPELAAILLKVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 249 QALEmhklekQPQVFLKIAPDLIESELKDIAQVVTNKkFAIDGIIVSNTTIARPDY-LRSEN---KTETGGLSGAPVREI 324
Cdd:pfam01180 153 KEVS------KVPVLVKLAPDLTDIVIIDIADVALGE-DGLDGINATNTTVRGMRIdLKTEKpilANGTGGLSGPPIKPI 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17509475 325 STECVRKIYKLTNGQIPIIGCGGVFSGADAYEKIRAGASLVQLYSAFVYEGFPVIGKIKRELVELL 390
Cdd:pfam01180 226 ALKVIRELYQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| dihydoor_dh_Arch |
NF041011 |
dihydroorotate dehydrogenase PyrD; |
93-407 |
6.79e-23 |
|
dihydroorotate dehydrogenase PyrD;
Pssm-ID: 468940 Cd Length: 289 Bit Score: 97.70 E-value: 6.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 93 ELFGREFKNPIGLAAGFDKD-GQAITQLAKNSGFGLIEIGSVTPIPQPGNNRPRVFRLlEDEGVINRYGFNSDGVGRVhq 171
Cdd:NF041011 2 RLAGLELEDPLIIASGILPDvPEYIERVCEKYGPSAITTKTLTLNPLEPHKPPTVVKL-HDGCYLNAIGLGNPGIGLL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 172 rvRSARDSWVPesyayFGVNLGKNKLTEDAKLDyEIGVNYfaphCDYLVLNVSSPNTPGLRsmqkksdlEKLLAYVHQAL 251
Cdd:NF041011 79 --EEIRVKLCP-----LIVSIGGSSLEEIVEVA-EIAEEK----ADAIELNLSSPNRKGYG--------ASLASLVREIV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 252 EMHKLEKQPQVFLKIAP--DLIESELKDIaqvvtnkKFAIDGIIVSNT-------TIARPDYLrsenKTETGGLSGAPVR 322
Cdd:NF041011 139 KAVKSVVKKPVFVKLGPwdNVLEIAGKAL-------EAGADGLTLINTvkgmaidVESFKPVL----SYGTGGISGKCIH 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 323 EISTECVRKIYKLTNgqIPIIGCGGVFSGADAYEKIRAGASLVQLYSAFVYEGFPVIGKIKRELVELLRKDGFShVSEAI 402
Cdd:NF041011 208 PLAVRIIYDVYREYE--AEIIGVGGVFSWRDAIELMSVGAKAVGVGTAIIDKGLSVISEIRKGLEEYLEEKGLK-LEDII 284
|
....*
gi 17509475 403 GADHR 407
Cdd:NF041011 285 GIAVK 289
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
52-386 |
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: 506.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 52 MPMVHkFVDGEDSHRWAVRAASWGLLPRFGWN-RKEYPELKCELFGREFKNPIGLAAGFDKDGQAITQLAKnSGFGLIEI 130
Cdd:cd04738 1 RPLLF-LLDPETAHRLAIRALKLGLGPPLLLLlVYDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLA-LGFGFVEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 131 GSVTPIPQPGNNRPRVFRLLEDEGVINRYGFNSDGVGRVHQRVRSARDSWVPesyayFGVNLGKNKLT--EDAKLDYEIG 208
Cdd:cd04738 79 GTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRRPRGGP-----LGVNIGKNKDTplEDAVEDYVIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 209 VNYFAPHCDYLVLNVSSPNTPGLRSMQKKSDLEKLLAYVHQALEmhKLEKQPQVFLKIAPDLIESELKDIAQVVTNKKfa 288
Cdd:cd04738 154 VRKLGPYADYLVVNVSSPNTPGLRDLQGKEALRELLTAVKEERN--KLGKKVPLLVKIAPDLSDEELEDIADVALEHG-- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 289 IDGIIVSNTTIARPDYLRSENKTETGGLSGAPVREISTECVRKIYKLTNGQIPIIGCGGVFSGADAYEKIRAGASLVQLY 368
Cdd:cd04738 230 VDGIIATNTTISRPGLLRSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLY 309
|
330
....*....|....*...
gi 17509475 369 SAFVYEGFPVIGKIKREL 386
Cdd:cd04738 310 TGLVYEGPGLVKRIKREL 327
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
46-394 |
2.76e-162 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 459.63 E-value: 2.76e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 46 FYKKAVMPMVHKFvDGEDSHRWAVRAASWGLLPRFGWNRKE-----YPELKCELFGREFKNPIGLAAGFDKDGQAITQLA 120
Cdd:PRK05286 1 MYYPLARPLLFKL-DPETAHELTIRALKRASRTPLLSLLRQrltytDPRLPVTVMGLTFPNPVGLAAGFDKNGEAIDALG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 121 KNsGFGLIEIGSVTPIPQPGNNRPRVFRLLEDEGVINRYGFNSDGVGRVHQRVRSARDSwVPesyayFGVNLGKNKLT-- 198
Cdd:PRK05286 80 AL-GFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKAYRG-IP-----LGINIGKNKDTpl 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 199 EDAKLDYEIGVNYFAPHCDYLVLNVSSPNTPGLRSMQKKSDLEKLLAYVHQAleMHKLEKQPQVFLKIAPDLIESELKDI 278
Cdd:PRK05286 153 EDAVDDYLICLEKLYPYADYFTVNISSPNTPGLRDLQYGEALDELLAALKEA--QAELHGYVPLLVKIAPDLSDEELDDI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 279 AQVVtnKKFAIDGIIVSNTTIARPDYLRSENKTETGGLSGAPVREISTECVRKIYKLTNGQIPIIGCGGVFSGADAYEKI 358
Cdd:PRK05286 231 ADLA--LEHGIDGVIATNTTLSRDGLKGLPNADEAGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKI 308
|
330 340 350
....*....|....*....|....*....|....*.
gi 17509475 359 RAGASLVQLYSAFVYEGFPVIGKIKRELVELLRKDG 394
Cdd:PRK05286 309 RAGASLVQIYSGLIYEGPGLVKEIVRGLARLLRRDG 344
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
17-407 |
1.25e-152 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 437.63 E-value: 1.25e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 17 GAISKSTVIVLATGIASY--TALELLYGSETFYKKAVMPMVHKFVDGEDSHRWAVRAASWGLLPRfgWNRKEYPELKCEL 94
Cdd:PLN02826 1 GRLLTGALIGLAIAGGAYvsTVDEATFCGWLFNATKLVNPLFRLLDPETAHSLAISAAARGLVPR--EKRPDPSVLGVEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 95 FGREFKNPIGLAAGFDKDGQAITQLAkNSGFGLIEIGSVTPIPQPGNNRPRVFRLLEDEGVINRYGFNSDGVGRVHQRVR 174
Cdd:PLN02826 79 WGRTFSNPIGLAAGFDKNAEAVEGLL-GLGFGFVEIGSVTPLPQPGNPKPRVFRLREEGAIINRYGFNSEGIVAVAKRLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 175 SAR--------DSWVPESYAYF----------GVNLGKNKLTEDAKLDYEIGVNYFAPHCDYLVLNVSSPNTPGLRSMQK 236
Cdd:PLN02826 158 AQHgkrkldetSSSSFSSDDVKaggkagpgilGVNLGKNKTSEDAAADYVQGVRALSQYADYLVINVSSPNTPGLRKLQG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 237 KSDLEKLLAYVHQAL-EMHKLEK-QPQVFLKIAPDLIESELKDIAQVVTnkKFAIDGIIVSNTTIARPDYLRSENK-TET 313
Cdd:PLN02826 238 RKQLKDLLKKVLAARdEMQWGEEgPPPLLVKIAPDLSKEDLEDIAAVAL--ALGIDGLIISNTTISRPDSVLGHPHaDEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 314 GGLSGAPVREISTECVRKIYKLTNGQIPIIGCGGVFSGADAYEKIRAGASLVQLYSAFVYEGFPVIGKIKRELVELLRKD 393
Cdd:PLN02826 316 GGLSGKPLFDLSTEVLREMYRLTRGKIPLVGCGGVSSGEDAYKKIRAGASLVQLYTAFAYEGPALIPRIKAELAACLERD 395
|
410
....*....|....
gi 17509475 394 GFSHVSEAIGADHR 407
Cdd:PLN02826 396 GFKSIQEAVGADHR 409
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
59-386 |
1.38e-118 |
|
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: 348.31 E-value: 1.38e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 59 VDGEDSHRWAVRAASWG------LLPRFGWNRKEYPELKCelFGREFKNPIGLAAGFDKDGQAITQLAKnSGFGLIEIGS 132
Cdd:TIGR01036 11 LDPESAHELTFQFLRLGtgtpflALLRSLFGASDPLEVTV--LGLKFPNPLGLAAGFDKDGEAIDALGA-MGFGFLEIGT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 133 VTPIPQPGNNRPRVFRLLEDEGVINRYGFNSDGVGRVHQRVRSARDSWVpesyayFGVNLGKNKLT--EDAKLDYEIGVN 210
Cdd:TIGR01036 88 VTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLKRARYKGP------IGINIGKNKDTpsEDAKEDYAACLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 211 YFAPHCDYLVLNVSSPNTPGLRSMQKKSDLEKLLAYVHQALEMHKLEKQPQVFLKIAPDLIESELKDIAQVVtnKKFAID 290
Cdd:TIGR01036 162 KLGPLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAVKQEQDGLRRVHRVPVLVKIAPDLTESDLEDIADSL--VELGID 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 291 GIIVSNTTIARPDYLRSENKTETGGLSGAPVREISTECVRKIYKLTNGQIPIIGCGGVFSGADAYEKIRAGASLVQLYSA 370
Cdd:TIGR01036 240 GVIATNTTVSRSLVQGPKNSDETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGASLLQIYSG 319
|
330
....*....|....*.
gi 17509475 371 FVYEGFPVIGKIKREL 386
Cdd:TIGR01036 320 FIYWGPPLVKEIVKEI 335
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
90-399 |
2.92e-112 |
|
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: 330.88 E-value: 2.92e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 90 LKCELFGREFKNPIGLAAGF-DKDGQAITQLAkNSGFGLIEIGSVTPIPQPGNNRPRVFRLLEDEGVINRYGFNSDGVGR 168
Cdd:COG0167 2 LSVELAGLKFPNPVGLASGFfDKNAEYIDALD-LLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 169 VHQRVRSARDSWVPesyayFGVNLGKNklTEDaklDYEIGVNYFAPH-CDYLVLNVSSPNTPG-LRSM-QKKSDLEKLLA 245
Cdd:COG0167 81 FLERLLPAKRYDVP-----VIVNIGGN--TVE---DYVELARRLADAgADYLELNISCPNTPGgGRALgQDPEALAELLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 246 YVHQALemhkleKQPqVFLKIAPDLieSELKDIAQVVtnKKFAIDGIIVSNTTIARPDYLRSEN---KTETGGLSGAPVR 322
Cdd:COG0167 151 AVKAAT------DKP-VLVKLAPDL--TDIVEIARAA--EEAGADGVIAINTTLGRAIDLETRRpvlANEAGGLSGPALK 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17509475 323 EISTECVRKIYKLTNGQIPIIGCGGVFSGADAYEKIRAGASLVQLYSAFVYEGFPVIGKIKRELVELLRKDGFSHVS 399
Cdd:COG0167 220 PIALRMVREVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSIS 296
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
90-390 |
4.61e-101 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 301.96 E-value: 4.61e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 90 LKCELFGREFKNPIGLAAGFDKDGQAITQLAKNSGFGLIEIGSVTPIPQPGNNRPRVFRLleDEGVINRYGFNSDGVGRV 169
Cdd:pfam01180 2 LATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVTPYPQPGNPTPRVFRL--PEGVLNRMGLNNPGLDAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 170 HQRVRSardsWVPESYAYF-GVNLGKNKLTEDaklDYEIGVNYFAPHCDYLVLNVSSPNTPGLRSMQKKSDLEKLLAYVH 248
Cdd:pfam01180 80 LAELLK----RRKEYPRPDlGINLSKAGMTVD---DYVEVARKIGPFADYIELNVSCPNTPGLRALQTDPELAAILLKVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 249 QALEmhklekQPQVFLKIAPDLIESELKDIAQVVTNKkFAIDGIIVSNTTIARPDY-LRSEN---KTETGGLSGAPVREI 324
Cdd:pfam01180 153 KEVS------KVPVLVKLAPDLTDIVIIDIADVALGE-DGLDGINATNTTVRGMRIdLKTEKpilANGTGGLSGPPIKPI 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17509475 325 STECVRKIYKLTNGQIPIIGCGGVFSGADAYEKIRAGASLVQLYSAFVYEGFPVIGKIKRELVELL 390
Cdd:pfam01180 226 ALKVIRELYQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
93-385 |
5.86e-60 |
|
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: 196.42 E-value: 5.86e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 93 ELFGREFKNPIGLAAGFDKDGQAITQLAKNSGFGLIEIGSVTPIPQPGNNRPRVFRL-------LEDEGVINRYGFNSDG 165
Cdd:cd02810 2 NFLGLKLKNPFGVAAGPLLKTGELIARAAAAGFGAVVYKTVTLHPRPGNPLPRVARLppegesyPEQLGILNSFGLPNLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 166 VGRVHQRVRSARdSWVPESYAYFGVN-LGKNKLTEDAKLDYEIGVnyfaphcDYLVLNVSSPNTPGLRSM-QKKSDLEKL 243
Cdd:cd02810 82 LDVWLQDIAKAK-KEFPGQPLIASVGgSSKEDYVELARKIERAGA-------KALELNLSCPNVGGGRQLgQDPEAVANL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 244 LAYVHQALemhklekQPQVFLKIAPDLIESELKDIAQVVTnkKFAIDGIIVSNTTIARP--DYLRSE-NKTETGGLSGAP 320
Cdd:cd02810 154 LKAVKAAV-------DIPLLVKLSPYFDLEDIVELAKAAE--RAGADGLTAINTISGRVvdLKTVGPgPKRGTGGLSGAP 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17509475 321 VREISTECVRKIYKLTNGQIPIIGCGGVFSGADAYEKIRAGASLVQLYSAFVYEGFPVIGKIKRE 385
Cdd:cd02810 225 IRPLALRWVARLAARLQLDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKIKKE 289
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
93-404 |
4.16e-36 |
|
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: 133.83 E-value: 4.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 93 ELFGREFKNPIGLAAG-FDKdGQAITQLAKNSGFGLIEIGSVTPIPQPGNNRPRVFRLleDEGVINRYGFNSDGVGRVHQ 171
Cdd:cd04740 3 ELAGLRLKNPVILASGtFGF-GEELSRVADLGKLGAIVTKSITLEPREGNPPPRVVET--PGGMLNAIGLQNPGVEAFLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 172 RVRSARDSW-VPesyayFGVNLGKNKLTEDAKLdyeigVNYFAP-HCDYLVLNVSSPNTPGlRSMQKKSDLEKLLAYVHq 249
Cdd:cd04740 80 ELLPWLREFgTP-----VIASIAGSTVEEFVEV-----AEKLADaGADAIELNISCPNVKG-GGMAFGTDPEAVAEIVK- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 250 alEMHKLEKQPqVFLKIAPDLieSELKDIAQVVTNKKfaIDGIIVSNTTIA--------RPDYlrsENKTetGGLSGAPV 321
Cdd:cd04740 148 --AVKKATDVP-VIVKLTPNV--TDIVEIARAAEEAG--ADGLTLINTLKGmaidietrKPIL---GNVT--GGLSGPAI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 322 REISTECVRKIYKLTNgqIPIIGCGGVFSGADAYEKIRAGASLVQLYSAfVYEGFPVIGKIKRELVELLRKDGFSHVSEA 401
Cdd:cd04740 216 KPIALRMVYQVYKAVE--IPIIGVGGIASGEDALEFLMAGASAVQVGTA-NFVDPEAFKEIIEGLEAYLDEEGIKSIEEL 292
|
...
gi 17509475 402 IGA 404
Cdd:cd04740 293 VGL 295
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
90-406 |
1.55e-34 |
|
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: 129.86 E-value: 1.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 90 LKCELFGREFKNPIGLAAGFDKDGQAITQLAKNSGFGLIEIGSVTPIPQPGNNRPRVFRLleDEGVINRYGFNSDGVGRV 169
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTIVET--PCGMLNAIGLQNPGVEAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 170 HQRVRSARDswvpESYAYFGVNL-GKnklTEDAKLDYEIGVNYFAPHCDYLVLNVSSPNTPGLrSMQKKSDLEkLLAYVH 248
Cdd:TIGR01037 79 LEELKPVRE----EFPTPLIASVyGS---SVEEFAEVAEKLEKAPPYVDAYELNLSCPHVKGG-GIAIGQDPE-LSADVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 249 QALEmhKLEKQPqVFLKIAPDLieSELKDIAQVVTNKkfAIDGIIVSNTTIA--------RPDYlrsenKTETGGLSGAP 320
Cdd:TIGR01037 150 KAVK--DKTDVP-VFAKLSPNV--TDITEIAKAAEEA--GADGLTLINTLRGmkidiktgKPIL-----ANKTGGLSGPA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 321 VREISTECVRKIYKLTNgqIPIIGCGGVFSGADAYEKIRAGASLVQLYSAFVYEGFpVIGKIKRELVELLRKDGFSHVSE 400
Cdd:TIGR01037 218 IKPIALRMVYDVYKMVD--IPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYRGF-AFKKIIEGLIAFLKAEGFTSIEE 294
|
....*.
gi 17509475 401 AIGADH 406
Cdd:TIGR01037 295 LIGIAH 300
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
90-407 |
6.60e-30 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 117.17 E-value: 6.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 90 LKCELFGREFKNPIGLAAG-FDKdGQAITQLAKNSGFGLIEIGSVTPIPQPGNNRPRVFRLleDEGVINRYGFNSDGVGR 168
Cdd:PRK07259 2 LSVELPGLKLKNPVMPASGtFGF-GGEYARFYDLNGLGAIVTKSTTLEPREGNPTPRIAET--PGGMLNAIGLQNPGVDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 169 VHQRVRSARDSW-----------VPESYAYFGVNLGKnkltedakldyeigvnyfAPHCDYLVLNVSSPNTP--GLRSMQ 235
Cdd:PRK07259 79 FIEEELPWLEEFdtpiianvagsTEEEYAEVAEKLSK------------------APNVDAIELNISCPNVKhgGMAFGT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 236 KKSDLEKLLAYVHQALemhkleKQPqVFLKIAPDLieSELKDIAQVVTNKKfaIDGIIVSNTTIA--------RPDYlrs 307
Cdd:PRK07259 141 DPELAYEVVKAVKEVV------KVP-VIVKLTPNV--TDIVEIAKAAEEAG--ADGLSLINTLKGmaidiktrKPIL--- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 308 ENKTetGGLSGAPVREISTECVRKIYKLTNgqIPIIGCGGVFSGADAYEKIRAGASLVQLYSAfVYEGFPVIGKIKRELV 387
Cdd:PRK07259 207 ANVT--GGLSGPAIKPIALRMVYQVYQAVD--IPIIGMGGISSAEDAIEFIMAGASAVQVGTA-NFYDPYAFPKIIEGLE 281
|
330 340
....*....|....*....|
gi 17509475 388 ELLRKDGFSHVSEAIGADHR 407
Cdd:PRK07259 282 AYLDKYGIKSIEEIVGIAHK 301
|
|
| dihydoor_dh_Arch |
NF041011 |
dihydroorotate dehydrogenase PyrD; |
93-407 |
6.79e-23 |
|
dihydroorotate dehydrogenase PyrD;
Pssm-ID: 468940 Cd Length: 289 Bit Score: 97.70 E-value: 6.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 93 ELFGREFKNPIGLAAGFDKD-GQAITQLAKNSGFGLIEIGSVTPIPQPGNNRPRVFRLlEDEGVINRYGFNSDGVGRVhq 171
Cdd:NF041011 2 RLAGLELEDPLIIASGILPDvPEYIERVCEKYGPSAITTKTLTLNPLEPHKPPTVVKL-HDGCYLNAIGLGNPGIGLL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 172 rvRSARDSWVPesyayFGVNLGKNKLTEDAKLDyEIGVNYfaphCDYLVLNVSSPNTPGLRsmqkksdlEKLLAYVHQAL 251
Cdd:NF041011 79 --EEIRVKLCP-----LIVSIGGSSLEEIVEVA-EIAEEK----ADAIELNLSSPNRKGYG--------ASLASLVREIV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 252 EMHKLEKQPQVFLKIAP--DLIESELKDIaqvvtnkKFAIDGIIVSNT-------TIARPDYLrsenKTETGGLSGAPVR 322
Cdd:NF041011 139 KAVKSVVKKPVFVKLGPwdNVLEIAGKAL-------EAGADGLTLINTvkgmaidVESFKPVL----SYGTGGISGKCIH 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 323 EISTECVRKIYKLTNgqIPIIGCGGVFSGADAYEKIRAGASLVQLYSAFVYEGFPVIGKIKRELVELLRKDGFShVSEAI 402
Cdd:NF041011 208 PLAVRIIYDVYREYE--AEIIGVGGVFSWRDAIELMSVGAKAVGVGTAIIDKGLSVISEIRKGLEEYLEEKGLK-LEDII 284
|
....*
gi 17509475 403 GADHR 407
Cdd:NF041011 285 GIAVK 289
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
314-403 |
4.36e-19 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 87.32 E-value: 4.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 314 GGLSGAPVREISTECVRKIYKLTNGQIPIIGCGGVFSGADAYEKIRAGASLVQLYSAFVYEGFPVIGKIKRELVELLRKD 393
Cdd:PRK02506 216 GGIGGDYIKPTALANVRAFYQRLNPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAIMAEK 295
|
90
....*....|
gi 17509475 394 GFSHVSEAIG 403
Cdd:PRK02506 296 GYQSLEDFRG 305
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
221-390 |
6.71e-15 |
|
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: 74.67 E-value: 6.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 221 LNVSSPNTPGlrsMQKksdleklLAYVHQALEMHkLEKQPQVF-----LKIAPDLIESELKDIAQVVTNKKFAIDGIIVS 295
Cdd:cd04741 125 LNLSCPNVPG---KPP-------PAYDFDATLEY-LTAVKAAYsipvgVKTPPYTDPAQFDTLAEALNAFACPISFITAT 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 296 NTtIARPDYLRSEN-------KTETGGLSGAPVREISTECVRKIYKLTNGQIPIIGCGGVFSGADAYEKIRAGASLVQLY 368
Cdd:cd04741 194 NT-LGNGLVLDPERetvvlkpKTGFGGLAGAYLHPLALGNVRTFRRLLPSEIQIIGVGGVLDGRGAFRMRLAGASAVQVG 272
|
170 180
....*....|....*....|..
gi 17509475 369 SAFVYEGFPVIGKIKRELVELL 390
Cdd:cd04741 273 TALGKEGPKVFARIEKELEDIW 294
|
|
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
198-386 |
2.29e-10 |
|
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: 61.15 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 198 TEDAKLDYEIGVnyfaphcDYLVLNVSSPNTPGLRSM-----QKKSDLEKLLAYVHQALEMhklekqPqVFLKIAPDLie 272
Cdd:cd02940 116 TELAKLVEEAGA-------DALELNFSCPHGMPERGMgaavgQDPELVEEICRWVREAVKI------P-VIAKLTPNI-- 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 273 SELKDIAQVVtnKKFAIDGIIVSNT-----------TIARPDylrSENKTETGGLSGAPVREISTECVRKIYKLTNGQIP 341
Cdd:cd02940 180 TDIREIARAA--KEGGADGVSAINTvnslmgvdldgTPPAPG---VEGKTTYGGYSGPAVKPIALRAVSQIARAPEPGLP 254
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17509475 342 IIGCGGVFSGADAYEKIRAGASLVQLYSAFVYEGFPVIGKIKREL 386
Cdd:cd02940 255 ISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
|
|
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
303-404 |
4.68e-08 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 54.46 E-value: 4.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 303 DYLRSENKTE----TGGLSGAPVREISTECVRKIYKLTNGQIP----IIGCGGVFSGADAYEKIRAGASLVQLYSAFVYE 374
Cdd:PLN02495 226 DTLRPEPCVEgystPGGYSSKAVRPIALAKVMAIAKMMKSEFPedrsLSGIGGVETGGDAAEFILLGADTVQVCTGVMMH 305
|
90 100 110
....*....|....*....|....*....|
gi 17509475 375 GFPVIGKIKRELVELLRKDGFSHVSEAIGA 404
Cdd:PLN02495 306 GYPLVKNLCAELQDFMKKHNFSSIEDFRGA 335
|
|
| PRK07565 |
PRK07565 |
dihydroorotate dehydrogenase-like protein; |
339-404 |
4.03e-06 |
|
dihydroorotate dehydrogenase-like protein;
Pssm-ID: 236051 Cd Length: 334 Bit Score: 48.32 E-value: 4.03e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17509475 339 QIPIIGCGGVFSGADAYEKIRAGASLVQLYSAFVYEGFPVIGKIKRELVELLRKDGFSHVSEAIGA 404
Cdd:PRK07565 239 GADLAATTGVHDAEDVIKMLLAGADVVMIASALLRHGPDYIGTILRGLEDWMERHGYESLQQFRGS 304
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
314-403 |
2.92e-05 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 46.09 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509475 314 GGLSGAPVREISTECVRKIYKLTN-GQIPIIGCGGVFSGADAYEKIRAGASLVQLYSAFVYEGFPVIGKIKRELVELLRK 392
Cdd:PRK08318 227 GGYCGPAVKPIALNMVAEIARDPEtRGLPISGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISGLSHYMDE 306
|
90
....*....|.
gi 17509475 393 DGFSHVSEAIG 403
Cdd:PRK08318 307 KGFASLEDMVG 317
|
|
| DHOD_like |
cd04739 |
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
339-400 |
1.28e-04 |
|
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: 43.76 E-value: 1.28e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17509475 339 QIPIIGCGGVFSGADAYEKIRAGASLVQLYSAFVYEGFPVIGKIKRELVELLRKDGFSHVSE 400
Cdd:cd04739 237 KASLAASGGVHDAEDVVKYLLAGADVVMTTSALLRHGPDYIGTLLAGLEAWMEEHGYESVQQ 298
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
332-374 |
8.50e-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: 37.96 E-value: 8.50e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 17509475 332 IYKLTNGQIPIIGCGGVFSGADAYEKIRAGASLVQLYSAFVYE 374
Cdd:cd04735 277 VKERIAGRLPLIAVGSINTPDDALEALETGADLVAIGRGLLVD 319
|
|
| |
