|
Name |
Accession |
Description |
Interval |
E-value |
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
10-325 |
2.52e-177 |
|
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: 494.33 E-value: 2.52e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 10 WLKGLDPERAHRLGILGLKAGLGPRQRGA---DDPRLAIRLAGIDLPNPIGLAAGFDKNAEAPDALLAMGFGFVECGAVT 86
Cdd:cd04738 3 LLFLLDPETAHRLAIRALKLGLGPPLLLLlvyDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFVEVGTVT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 87 PRPQDGKPRPRIFRLEDDEAVINRMGFPNQGLARFRSNLARRARRGGVVGVNIGANLDS--EDRVADYVTCLEALQGLAQ 164
Cdd:cd04738 83 PRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRRPRGGPLGVNIGKNKDTplEDAVEDYVIGVRKLGPYAD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 165 FFTVNVSSPNTPGLRTLQSSGALDTLLAAV----AAIGSQVPVFLKIAPDIDDSEAGVMVEAVARHGLDGVIVSNTSILR 240
Cdd:cd04738 163 YLVVNVSSPNTPGLRDLQGKEALRELLTAVkeerNKLGKKVPLLVKIAPDLSDEELEDIADVALEHGVDGIIATNTTISR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 241 PESLKSANMGEAGGLSGPPIFERSTQLVRLFREAAGPDLAIIGVGGVDSADAAYAKIRAGANAIQLYTGLVYHGPGLVQQ 320
Cdd:cd04738 243 PGLLRSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTGLVYEGPGLVKR 322
|
....*
gi 2787263404 321 IKDGL 325
Cdd:cd04738 323 IKREL 327
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
2-333 |
6.33e-175 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 488.90 E-value: 6.33e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 2 MLHDKATHWLKGLDPERAHRLGILGLKAGLGPRQRGA-------DDPRLAIRLAGIDLPNPIGLAAGFDKNAEAPDALLA 74
Cdd:PRK05286 1 MYYPLARPLLFKLDPETAHELTIRALKRASRTPLLSLlrqrltyTDPRLPVTVMGLTFPNPVGLAAGFDKNGEAIDALGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 75 MGFGFVECGAVTPRPQDGKPRPRIFRLEDDEAVINRMGFPNQGLARFRSNLARRaRRGGVVGVNIGANLDS--EDRVADY 152
Cdd:PRK05286 81 LGFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKA-YRGIPLGINIGKNKDTplEDAVDDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 153 VTCLEALQGLAQFFTVNVSSPNTPGLRTLQSSGALDTLLAAVAAIGSQ----VPVFLKIAPDIDDSEAGVMVEAVARHGL 228
Cdd:PRK05286 160 LICLEKLYPYADYFTVNISSPNTPGLRDLQYGEALDELLAALKEAQAElhgyVPLLVKIAPDLSDEELDDIADLALEHGI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 229 DGVIVSNTSILRPESLKSANMGEAGGLSGPPIFERSTQLVRLFREAAGPDLAIIGVGGVDSADAAYAKIRAGANAIQLYT 308
Cdd:PRK05286 240 DGVIATNTTLSRDGLKGLPNADEAGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGASLVQIYS 319
|
330 340
....*....|....*....|....*
gi 2787263404 309 GLVYHGPGLVQQIKDGLVERLQADG 333
Cdd:PRK05286 320 GLIYEGPGLVKEIVRGLARLLRRDG 344
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
43-338 |
4.41e-120 |
|
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: 347.83 E-value: 4.41e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 43 LAIRLAGIDLPNPIGLAAGF-DKNAEAPDALLAMGFGFVECGAVTPRPQDGKPRPRIFRLEDDEAVINRMGFPNQGLARF 121
Cdd:COG0167 2 LSVELAGLKFPNPVGLASGFfDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 122 RSNLARRARRGGVVGVNIGANldsedRVADYVTCLEALQGL-AQFFTVNVSSPNTPG-LRTL-QSSGALDTLLAAVAAIg 198
Cdd:COG0167 82 LERLLPAKRYDVPVIVNIGGN-----TVEDYVELARRLADAgADYLELNISCPNTPGgGRALgQDPEALAELLAAVKAA- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 199 SQVPVFLKIAPDIDDSEAgvMVEAVARHGLDGVIVSNTSILRPESLKSAN---MGEAGGLSGPPIFERSTQLVRLFREAA 275
Cdd:COG0167 156 TDKPVLVKLAPDLTDIVE--IARAAEEAGADGVIAINTTLGRAIDLETRRpvlANEAGGLSGPALKPIALRMVREVAQAV 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2787263404 276 GPDLAIIGVGGVDSADAAYAKIRAGANAIQLYTGLVYHGPGLVQQIKDGLVERLQADGFASVS 338
Cdd:COG0167 234 GGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSIS 296
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
9-325 |
4.41e-111 |
|
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: 326.74 E-value: 4.41e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 9 HWLKGLDPERAHRLGILGLKAGLGP-------RQRGADDPrLAIRLAGIDLPNPIGLAAGFDKNAEAPDALLAMGFGFVE 81
Cdd:TIGR01036 6 KLLFLLDPESAHELTFQFLRLGTGTpflallrSLFGASDP-LEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAMGFGFLE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 82 CGAVTPRPQDGKPRPRIFRLEDDEAVINRMGFPNQGLARFRSNLaRRARRGGVVGVNIGANLD--SEDRVADYVTCLEAL 159
Cdd:TIGR01036 85 IGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERL-KRARYKGPIGINIGKNKDtpSEDAKEDYAACLRKL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 160 QGLAQFFTVNVSSPNTPGLRTLQSSGALDTLLAAVAAIGS------QVPVFLKIAPDIDDSEAGVMVEAVARHGLDGVIV 233
Cdd:TIGR01036 164 GPLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAVKQEQDglrrvhRVPVLVKIAPDLTESDLEDIADSLVELGIDGVIA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 234 SNTSILRPESLKSANMGEAGGLSGPPIFERSTQLVRLFREAAGPDLAIIGVGGVDSADAAYAKIRAGANAIQLYTGLVYH 313
Cdd:TIGR01036 244 TNTTVSRSLVQGPKNSDETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGASLLQIYSGFIYW 323
|
330
....*....|..
gi 2787263404 314 GPGLVQQIKDGL 325
Cdd:TIGR01036 324 GPPLVKEIVKEI 335
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
42-329 |
4.46e-89 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 268.83 E-value: 4.46e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 42 RLAIRLAGIDLPNPIGLAAGFDKNAEAPDALLAMG-FGFVECGAVTPRPQDGKPRPRIFRLEDDeaVINRMGFPNQGLAR 120
Cdd:pfam01180 1 MLATKIPGLDFKNPIGLASGFDKFGEEALKWLALGkFGAIEIKSVTPYPQPGNPTPRVFRLPEG--VLNRMGLNNPGLDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 121 FRSNLARRARR--GGVVGVNIGANLDSEDrvaDYVTCLEALQGLAQFFTVNVSSPNTPGLRTLQSSGALDTLLAAVAAIG 198
Cdd:pfam01180 79 VLAELLKRRKEypRPDLGINLSKAGMTVD---DYVEVARKIGPFADYIELNVSCPNTPGLRALQTDPELAAILLKVVKEV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 199 SQVPVFLKIAPDIDDSE-AGVMVEAVARHGLDGVIVSNTSILRP------ESLKSANmgEAGGLSGPPIFERSTQLVRLF 271
Cdd:pfam01180 156 SKVPVLVKLAPDLTDIViIDIADVALGEDGLDGINATNTTVRGMridlktEKPILAN--GTGGLSGPPIKPIALKVIREL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2787263404 272 REAAGPDLAIIGVGGVDSADAAYAKIRAGANAIQLYTGLVYHGPGLVQQIKDGLVERL 329
Cdd:pfam01180 234 YQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| dihydoor_dh_Arch |
NF041011 |
dihydroorotate dehydrogenase PyrD; |
45-344 |
1.73e-21 |
|
dihydroorotate dehydrogenase PyrD;
Pssm-ID: 468940 Cd Length: 289 Bit Score: 92.69 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 45 IRLAGIDLPNPIGLAAGFdknaeAPDALLAM-------GFGFVECGAVTPRPQDGKPRPRIFRLEDDeAVINRMGFPNQG 117
Cdd:NF041011 1 IRLAGLELEDPLIIASGI-----LPDVPEYIervcekyGPSAITTKTLTLNPLEPHKPPTVVKLHDG-CYLNAIGLGNPG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 118 LarfrsNLARRARRGGV-VGVNIGANldSEDrvaDYVTCLEALQGLAQFFTVNVSSPNTPGLrTLQSSGALDTLLAAVAA 196
Cdd:NF041011 75 I-----GLLEEIRVKLCpLIVSIGGS--SLE---EIVEVAEIAEEKADAIELNLSSPNRKGY-GASLASLVREIVKAVKS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 197 IgSQVPVFLKIAP--DIDDSeAGVMVEAvarhGLDGVIVSNT---SILRPESLKSANMGEAGGLSGPPIFERSTQLVR-L 270
Cdd:NF041011 144 V-VKKPVFVKLGPwdNVLEI-AGKALEA----GADGLTLINTvkgMAIDVESFKPVLSYGTGGISGKCIHPLAVRIIYdV 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2787263404 271 FREAAGPdlaIIGVGGVDSADAAYAKIRAGANAIQLYTGLVYHGPGLVQQIKDGLVERLQADGFAsVSEAVGAG 344
Cdd:NF041011 218 YREYEAE---IIGVGGVFSWRDAIELMSVGAKAVGVGTAIIDKGLSVISEIRKGLEEYLEEKGLK-LEDIIGIA 287
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
10-325 |
2.52e-177 |
|
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: 494.33 E-value: 2.52e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 10 WLKGLDPERAHRLGILGLKAGLGPRQRGA---DDPRLAIRLAGIDLPNPIGLAAGFDKNAEAPDALLAMGFGFVECGAVT 86
Cdd:cd04738 3 LLFLLDPETAHRLAIRALKLGLGPPLLLLlvyDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFVEVGTVT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 87 PRPQDGKPRPRIFRLEDDEAVINRMGFPNQGLARFRSNLARRARRGGVVGVNIGANLDS--EDRVADYVTCLEALQGLAQ 164
Cdd:cd04738 83 PRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRRPRGGPLGVNIGKNKDTplEDAVEDYVIGVRKLGPYAD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 165 FFTVNVSSPNTPGLRTLQSSGALDTLLAAV----AAIGSQVPVFLKIAPDIDDSEAGVMVEAVARHGLDGVIVSNTSILR 240
Cdd:cd04738 163 YLVVNVSSPNTPGLRDLQGKEALRELLTAVkeerNKLGKKVPLLVKIAPDLSDEELEDIADVALEHGVDGIIATNTTISR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 241 PESLKSANMGEAGGLSGPPIFERSTQLVRLFREAAGPDLAIIGVGGVDSADAAYAKIRAGANAIQLYTGLVYHGPGLVQQ 320
Cdd:cd04738 243 PGLLRSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTGLVYEGPGLVKR 322
|
....*
gi 2787263404 321 IKDGL 325
Cdd:cd04738 323 IKREL 327
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
2-333 |
6.33e-175 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 488.90 E-value: 6.33e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 2 MLHDKATHWLKGLDPERAHRLGILGLKAGLGPRQRGA-------DDPRLAIRLAGIDLPNPIGLAAGFDKNAEAPDALLA 74
Cdd:PRK05286 1 MYYPLARPLLFKLDPETAHELTIRALKRASRTPLLSLlrqrltyTDPRLPVTVMGLTFPNPVGLAAGFDKNGEAIDALGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 75 MGFGFVECGAVTPRPQDGKPRPRIFRLEDDEAVINRMGFPNQGLARFRSNLARRaRRGGVVGVNIGANLDS--EDRVADY 152
Cdd:PRK05286 81 LGFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKA-YRGIPLGINIGKNKDTplEDAVDDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 153 VTCLEALQGLAQFFTVNVSSPNTPGLRTLQSSGALDTLLAAVAAIGSQ----VPVFLKIAPDIDDSEAGVMVEAVARHGL 228
Cdd:PRK05286 160 LICLEKLYPYADYFTVNISSPNTPGLRDLQYGEALDELLAALKEAQAElhgyVPLLVKIAPDLSDEELDDIADLALEHGI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 229 DGVIVSNTSILRPESLKSANMGEAGGLSGPPIFERSTQLVRLFREAAGPDLAIIGVGGVDSADAAYAKIRAGANAIQLYT 308
Cdd:PRK05286 240 DGVIATNTTLSRDGLKGLPNADEAGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGASLVQIYS 319
|
330 340
....*....|....*....|....*
gi 2787263404 309 GLVYHGPGLVQQIKDGLVERLQADG 333
Cdd:PRK05286 320 GLIYEGPGLVKEIVRGLARLLRRDG 344
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
43-338 |
4.41e-120 |
|
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: 347.83 E-value: 4.41e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 43 LAIRLAGIDLPNPIGLAAGF-DKNAEAPDALLAMGFGFVECGAVTPRPQDGKPRPRIFRLEDDEAVINRMGFPNQGLARF 121
Cdd:COG0167 2 LSVELAGLKFPNPVGLASGFfDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 122 RSNLARRARRGGVVGVNIGANldsedRVADYVTCLEALQGL-AQFFTVNVSSPNTPG-LRTL-QSSGALDTLLAAVAAIg 198
Cdd:COG0167 82 LERLLPAKRYDVPVIVNIGGN-----TVEDYVELARRLADAgADYLELNISCPNTPGgGRALgQDPEALAELLAAVKAA- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 199 SQVPVFLKIAPDIDDSEAgvMVEAVARHGLDGVIVSNTSILRPESLKSAN---MGEAGGLSGPPIFERSTQLVRLFREAA 275
Cdd:COG0167 156 TDKPVLVKLAPDLTDIVE--IARAAEEAGADGVIAINTTLGRAIDLETRRpvlANEAGGLSGPALKPIALRMVREVAQAV 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2787263404 276 GPDLAIIGVGGVDSADAAYAKIRAGANAIQLYTGLVYHGPGLVQQIKDGLVERLQADGFASVS 338
Cdd:COG0167 234 GGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSIS 296
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
7-343 |
2.07e-116 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 342.87 E-value: 2.07e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 7 ATHWLKGLDPERAHRLGILGLKAGLGPRQRGADDPRLAIRLAGIDLPNPIGLAAGFDKNAEAPDALLAMGFGFVECGAVT 86
Cdd:PLN02826 38 VNPLFRLLDPETAHSLAISAAARGLVPREKRPDPSVLGVEVWGRTFSNPIGLAAGFDKNAEAVEGLLGLGFGFVEIGSVT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 87 PRPQDGKPRPRIFRLEDDEAVINRMGFPNQGLARFRSNLARRAR-----------------------RGGVVGVNIGANL 143
Cdd:PLN02826 118 PLPQPGNPKPRVFRLREEGAIINRYGFNSEGIVAVAKRLGAQHGkrkldetssssfssddvkaggkaGPGILGVNLGKNK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 144 DSEDRVADYVTCLEALQGLAQFFTVNVSSPNTPGLRTLQSSGALDTLLAAVAAI--------GSQVPVFLKIAPDIDDSE 215
Cdd:PLN02826 198 TSEDAAADYVQGVRALSQYADYLVINVSSPNTPGLRKLQGRKQLKDLLKKVLAArdemqwgeEGPPPLLVKIAPDLSKED 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 216 AGVMVEAVARHGLDGVIVSNTSILRPESLKSANM-GEAGGLSGPPIFERSTQLVR-LFREAAGpDLAIIGVGGVDSADAA 293
Cdd:PLN02826 278 LEDIAAVALALGIDGLIISNTTISRPDSVLGHPHaDEAGGLSGKPLFDLSTEVLReMYRLTRG-KIPLVGCGGVSSGEDA 356
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2787263404 294 YAKIRAGANAIQLYTGLVYHGPGLVQQIKDGLVERLQADGFASVSEAVGA 343
Cdd:PLN02826 357 YKKIRAGASLVQLYTAFAYEGPALIPRIKAELAACLERDGFKSIQEAVGA 406
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
9-325 |
4.41e-111 |
|
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: 326.74 E-value: 4.41e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 9 HWLKGLDPERAHRLGILGLKAGLGP-------RQRGADDPrLAIRLAGIDLPNPIGLAAGFDKNAEAPDALLAMGFGFVE 81
Cdd:TIGR01036 6 KLLFLLDPESAHELTFQFLRLGTGTpflallrSLFGASDP-LEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAMGFGFLE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 82 CGAVTPRPQDGKPRPRIFRLEDDEAVINRMGFPNQGLARFRSNLaRRARRGGVVGVNIGANLD--SEDRVADYVTCLEAL 159
Cdd:TIGR01036 85 IGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERL-KRARYKGPIGINIGKNKDtpSEDAKEDYAACLRKL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 160 QGLAQFFTVNVSSPNTPGLRTLQSSGALDTLLAAVAAIGS------QVPVFLKIAPDIDDSEAGVMVEAVARHGLDGVIV 233
Cdd:TIGR01036 164 GPLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAVKQEQDglrrvhRVPVLVKIAPDLTESDLEDIADSLVELGIDGVIA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 234 SNTSILRPESLKSANMGEAGGLSGPPIFERSTQLVRLFREAAGPDLAIIGVGGVDSADAAYAKIRAGANAIQLYTGLVYH 313
Cdd:TIGR01036 244 TNTTVSRSLVQGPKNSDETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGASLLQIYSGFIYW 323
|
330
....*....|..
gi 2787263404 314 GPGLVQQIKDGL 325
Cdd:TIGR01036 324 GPPLVKEIVKEI 335
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
42-329 |
4.46e-89 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 268.83 E-value: 4.46e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 42 RLAIRLAGIDLPNPIGLAAGFDKNAEAPDALLAMG-FGFVECGAVTPRPQDGKPRPRIFRLEDDeaVINRMGFPNQGLAR 120
Cdd:pfam01180 1 MLATKIPGLDFKNPIGLASGFDKFGEEALKWLALGkFGAIEIKSVTPYPQPGNPTPRVFRLPEG--VLNRMGLNNPGLDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 121 FRSNLARRARR--GGVVGVNIGANLDSEDrvaDYVTCLEALQGLAQFFTVNVSSPNTPGLRTLQSSGALDTLLAAVAAIG 198
Cdd:pfam01180 79 VLAELLKRRKEypRPDLGINLSKAGMTVD---DYVEVARKIGPFADYIELNVSCPNTPGLRALQTDPELAAILLKVVKEV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 199 SQVPVFLKIAPDIDDSE-AGVMVEAVARHGLDGVIVSNTSILRP------ESLKSANmgEAGGLSGPPIFERSTQLVRLF 271
Cdd:pfam01180 156 SKVPVLVKLAPDLTDIViIDIADVALGEDGLDGINATNTTVRGMridlktEKPILAN--GTGGLSGPPIKPIALKVIREL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2787263404 272 REAAGPDLAIIGVGGVDSADAAYAKIRAGANAIQLYTGLVYHGPGLVQQIKDGLVERL 329
Cdd:pfam01180 234 YQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
45-324 |
9.67e-55 |
|
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: 181.01 E-value: 9.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 45 IRLAGIDLPNPIGLAAGFD-KNAEAPDALLAMGFGFVECGAVTPRPQDGKPRPRIFRL-------EDDEAVINRMGFPNQ 116
Cdd:cd02810 1 VNFLGLKLKNPFGVAAGPLlKTGELIARAAAAGFGAVVYKTVTLHPRPGNPLPRVARLppegesyPEQLGILNSFGLPNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 117 GLARFRSNL--ARRARRGGVVGVNIGANldsedRVADYVTCLEALQGL-AQFFTVNVSSPNTPGLRTL-QSSGALDTLLA 192
Cdd:cd02810 81 GLDVWLQDIakAKKEFPGQPLIASVGGS-----SKEDYVELARKIERAgAKALELNLSCPNVGGGRQLgQDPEAVANLLK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 193 AVAAIgSQVPVFLKIAPDIDDSEAGVMVEAVARHGLDGVIVSNTSILRPESLKSANMGE---AGGLSGPPIFERSTQLVR 269
Cdd:cd02810 156 AVKAA-VDIPLLVKLSPYFDLEDIVELAKAAERAGADGLTAINTISGRVVDLKTVGPGPkrgTGGLSGAPIRPLALRWVA 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2787263404 270 LFREAAGPDLAIIGVGGVDSADAAYAKIRAGANAIQLYTGLVYHGPGLVQQIKDG 324
Cdd:cd02810 235 RLAARLQLDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKIKKE 289
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
42-343 |
2.84e-34 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 127.57 E-value: 2.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 42 RLAIRLAGIDLPNPIGLAAG-FDKNAEAPDALLAMGFGFVECGAVTPRPQDGKPRPRIFRLEDdeAVINRMGFPNQGLAR 120
Cdd:PRK07259 1 RLSVELPGLKLKNPVMPASGtFGFGGEYARFYDLNGLGAIVTKSTTLEPREGNPTPRIAETPG--GMLNAIGLQNPGVDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 121 FRSNLARRARRGGV-VGVNIGANldSEDrvaDYVTCLEALQ--GLAQFFTVNVSSPNTP--GLRTLQSSGALDTLLAAVA 195
Cdd:PRK07259 79 FIEEELPWLEEFDTpIIANVAGS--TEE---EYAEVAEKLSkaPNVDAIELNISCPNVKhgGMAFGTDPELAYEVVKAVK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 196 AIgSQVPVFLKIAPDIDDseAGVMVEAVARHGLDGVIVSNTsiLR-----PESLKS--ANMgeAGGLSGPPIFERStqlV 268
Cdd:PRK07259 154 EV-VKVPVIVKLTPNVTD--IVEIAKAAEEAGADGLSLINT--LKgmaidIKTRKPilANV--TGGLSGPAIKPIA---L 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2787263404 269 RLFREAAGP-DLAIIGVGGVDSADAAYAKIRAGANAIQLYTGlVYHGPGLVQQIKDGLVERLQADGFASVSEAVGA 343
Cdd:PRK07259 224 RMVYQVYQAvDIPIIGMGGISSAEDAIEFIMAGASAVQVGTA-NFYDPYAFPKIIEGLEAYLDKYGIKSIEEIVGI 298
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
44-343 |
3.51e-34 |
|
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: 127.28 E-value: 3.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 44 AIRLAGIDLPNPIGLAAG-FDKNAEAPDALLAMGFGFVECGAVTPRPQDGKPRPRIFRLEDdeAVINRMGFPNQGLARFR 122
Cdd:cd04740 1 SVELAGLRLKNPVILASGtFGFGEELSRVADLGKLGAIVTKSITLEPREGNPPPRVVETPG--GMLNAIGLQNPGVEAFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 123 SN-LARRARRGGVVGVNIGAnldseDRVADYVTCLEALQGL-AQFFTVNVSSPNTPGLRTlqssgALDTLLAAVAAIGSQ 200
Cdd:cd04740 79 EElLPWLREFGTPVIASIAG-----STVEEFVEVAEKLADAgADAIELNISCPNVKGGGM-----AFGTDPEAVAEIVKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 201 V------PVFLKIAPDIDDSEAgvMVEAVARHGLDGVIVSNTSI---LRPESLKSANMGEAGGLSGPPIFERSTQLVRLF 271
Cdd:cd04740 149 VkkatdvPVIVKLTPNVTDIVE--IARAAEEAGADGLTLINTLKgmaIDIETRKPILGNVTGGLSGPAIKPIALRMVYQV 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2787263404 272 REAAGPDlaIIGVGGVDSADAAYAKIRAGANAIQLYTGlVYHGPGLVQQIKDGLVERLQADGFASVSEAVGA 343
Cdd:cd04740 227 YKAVEIP--IIGVGGIASGEDALEFLMAGASAVQVGTA-NFVDPEAFKEIIEGLEAYLDEEGIKSIEELVGL 295
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
43-342 |
5.80e-27 |
|
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: 107.90 E-value: 5.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 43 LAIRLAGIDLPNPIGLAAG-FDKNAEAPDALLAMGFGFVECGAVTPRPQDGKPRPRIfrLEDDEAVINRMGFPNQGLARF 121
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGiMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTI--VETPCGMLNAIGLQNPGVEAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 122 RSNLARRARRggvVGVNIGANL--DSEDRVADYVTCLEALQGLAQFFTVNVSSPN--TPGLRTLQSSGALDTLLAAVAAI 197
Cdd:TIGR01037 79 LEELKPVREE---FPTPLIASVygSSVEEFAEVAEKLEKAPPYVDAYELNLSCPHvkGGGIAIGQDPELSADVVKAVKDK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 198 gSQVPVFLKIAPDIDD--SEAGVMVEAvarhGLDGVIVSNTSILRPESLKSAN---MGEAGGLSGPPIFERSTQLV-RLF 271
Cdd:TIGR01037 156 -TDVPVFAKLSPNVTDitEIAKAAEEA----GADGLTLINTLRGMKIDIKTGKpilANKTGGLSGPAIKPIALRMVyDVY 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2787263404 272 REAagpDLAIIGVGGVDSADAAYAKIRAGANAIQLYTGlVYHGPGLVQQIKDGLVERLQADGFASVSEAVG 342
Cdd:TIGR01037 231 KMV---DIPIIGVGGITSFEDALEFLMAGASAVQVGTA-VYYRGFAFKKIIEGLIAFLKAEGFTSIEELIG 297
|
|
| dihydoor_dh_Arch |
NF041011 |
dihydroorotate dehydrogenase PyrD; |
45-344 |
1.73e-21 |
|
dihydroorotate dehydrogenase PyrD;
Pssm-ID: 468940 Cd Length: 289 Bit Score: 92.69 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 45 IRLAGIDLPNPIGLAAGFdknaeAPDALLAM-------GFGFVECGAVTPRPQDGKPRPRIFRLEDDeAVINRMGFPNQG 117
Cdd:NF041011 1 IRLAGLELEDPLIIASGI-----LPDVPEYIervcekyGPSAITTKTLTLNPLEPHKPPTVVKLHDG-CYLNAIGLGNPG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 118 LarfrsNLARRARRGGV-VGVNIGANldSEDrvaDYVTCLEALQGLAQFFTVNVSSPNTPGLrTLQSSGALDTLLAAVAA 196
Cdd:NF041011 75 I-----GLLEEIRVKLCpLIVSIGGS--SLE---EIVEVAEIAEEKADAIELNLSSPNRKGY-GASLASLVREIVKAVKS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 197 IgSQVPVFLKIAP--DIDDSeAGVMVEAvarhGLDGVIVSNT---SILRPESLKSANMGEAGGLSGPPIFERSTQLVR-L 270
Cdd:NF041011 144 V-VKKPVFVKLGPwdNVLEI-AGKALEA----GADGLTLINTvkgMAIDVESFKPVLSYGTGGISGKCIHPLAVRIIYdV 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2787263404 271 FREAAGPdlaIIGVGGVDSADAAYAKIRAGANAIQLYTGLVYHGPGLVQQIKDGLVERLQADGFAsVSEAVGAG 344
Cdd:NF041011 218 YREYEAE---IIGVGGVFSWRDAIELMSVGAKAVGVGTAIIDKGLSVISEIRKGLEEYLEEKGLK-LEDIIGIA 287
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
42-342 |
1.33e-17 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 81.92 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 42 RLAIRLAGIDLPNPIGLAAG-FDKNAEAPDALLAMGFGFVECGAVTPRPQDGKPRPRIFRLEddEAVINRMGFPNQGLaR 120
Cdd:PRK02506 1 STSTQIAGFKFDNCLMNAAGvYCMTKEELEEVEASAAGAFVTKSATLEPRPGNPEPRYADTP--LGSINSMGLPNLGF-D 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 121 FRSNLARRARRGG--------VVGVNIGANLDSEDRVADyvtclEALQGLAQFftvNVSSPNTPGL-RTLQSSGALDTLL 191
Cdd:PRK02506 78 YYLDYVLELQKKGpnkphflsVVGLSPEETHTILKKIQA-----SDFNGLVEL---NLSCPNVPGKpQIAYDFETTEQIL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 192 AAVAAIGSqVPVFLKIAPDIDDSEAGVMVEAVARHGLD----------GVIV---SNTSILRPEslksanmGEAGGLSGP 258
Cdd:PRK02506 150 EEVFTYFT-KPLGVKLPPYFDIVHFDQAAAIFNKFPLAfvncinsignGLVIdpeDETVVIKPK-------NGFGGIGGD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 259 PIfeRSTQL--VRLFREAAGPDLAIIGVGGVDSADAAYAKIRAGANAIQLYTGLVYHGPGLVQQIKDGLVERLQADGFAS 336
Cdd:PRK02506 222 YI--KPTALanVRAFYQRLNPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAIMAEKGYQS 299
|
....*.
gi 2787263404 337 VSEAVG 342
Cdd:PRK02506 300 LEDFRG 305
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
46-325 |
1.85e-17 |
|
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: 81.22 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 46 RLAGIDLPNPIGLAAG-FDKNAEAPDALLAMGFGFVECGAVTPRPQDGKPRPRIFRLEDdeAVINRMGFPNQGLARFRSN 124
Cdd:cd04741 2 TPPGLTISPPLMNAAGpWCTTLEDLLELAASSTGAVTTRSSTLAGRPGNPEPRYYAFPL--GSINSLGLPNLGLDYYLEY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 125 LARRARRGGVVGVNIGANLDSEdrVADYVTCLEALQGLAQFFT----VNVSSPNTPGLRTLQSSG-ALDTLLAAVAAIGS 199
Cdd:cd04741 80 IRTISDGLPGSAKPFFISVTGS--AEDIAAMYKKIAAHQKQFPlameLNLSCPNVPGKPPPAYDFdATLEYLTAVKAAYS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 200 qVPVFLKIAPDIDDSEAGVMVEAVARH--GLDGVIVSNTS----ILRPES----LKSANmgEAGGLSGPPIFERSTQLVR 269
Cdd:cd04741 158 -IPVGVKTPPYTDPAQFDTLAEALNAFacPISFITATNTLgnglVLDPERetvvLKPKT--GFGGLAGAYLHPLALGNVR 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2787263404 270 LFREAAGPDLAIIGVGGVDSADAAYAKIRAGANAIQLYTGLVYHGPGLVQQIKDGL 325
Cdd:cd04741 235 TFRRLLPSEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEKEL 290
|
|
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
166-343 |
4.95e-12 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 66.40 E-value: 4.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 166 FTVNVSSPN-TP----GLRTLQSSGALDTLLAAVAAIGSqVPVFLKIAPDIDD--SEAGVMVEAvarhGLDGVIVSNT-- 236
Cdd:PLN02495 144 LEINFSCPHgMPerkmGAAVGQDCDLLEEVCGWINAKAT-VPVWAKMTPNITDitQPARVALKS----GCEGVAAINTim 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 237 SI-------LRPESLKSANMGeAGGLSG---PPI-FERSTQLVRLFREAAGPDLAIIGVGGVDSADAAYAKIRAGANAIQ 305
Cdd:PLN02495 219 SVmginldtLRPEPCVEGYST-PGGYSSkavRPIaLAKVMAIAKMMKSEFPEDRSLSGIGGVETGGDAAEFILLGADTVQ 297
|
170 180 190
....*....|....*....|....*....|....*...
gi 2787263404 306 LYTGLVYHGPGLVQQIKDGLVERLQADGFASVSEAVGA 343
Cdd:PLN02495 298 VCTGVMMHGYPLVKNLCAELQDFMKKHNFSSIEDFRGA 335
|
|
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
198-325 |
1.51e-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: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 198 GSQVPVFLKIAPDIDDSEagVMVEAVARHGLDGVIVSNT--SILRPESLKSANM------GEAGGLSGP---PIFERSTQ 266
Cdd:cd02940 166 AVKIPVIAKLTPNITDIR--EIARAAKEGGADGVSAINTvnSLMGVDLDGTPPApgvegkTTYGGYSGPavkPIALRAVS 243
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2787263404 267 LVRlfrEAAGPDLAIIGVGGVDSADAAYAKIRAGANAIQLYTGLVYHGPGLVQQIKDGL 325
Cdd:cd02940 244 QIA---RAPEPGLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
198-342 |
6.22e-07 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 50.71 E-value: 6.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787263404 198 GSQVPVFLKIAPDIDDSEAGVmvEAVARHGLDGVIVSNT--SILRPEsLKSANM-------GEAGGLSGP---PIFERST 265
Cdd:PRK08318 166 GSRLPVIVKLTPNITDIREPA--RAAKRGGADAVSLINTinSITGVD-LDRMIPmpivngkSSHGGYCGPavkPIALNMV 242
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2787263404 266 QlvRLFREAAGPDLAIIGVGGVDSADAAYAKIRAGANAIQLYTGLVYHGPGLVQQIKDGLVERLQADGFASVSEAVG 342
Cdd:PRK08318 243 A--EIARDPETRGLPISGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISGLSHYMDEKGFASLEDMVG 317
|
|
| DHOD_like |
cd04739 |
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
285-339 |
1.00e-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: 1.00e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2787263404 285 GGVDSADAAYAKIRAGANAIQLYTGLVYHGPGLVQQIKDGLVERLQADGFASVSE 339
Cdd:cd04739 244 GGVHDAEDVVKYLLAGADVVMTTSALLRHGPDYIGTLLAGLEAWMEEHGYESVQQ 298
|
|
| PRK07565 |
PRK07565 |
dihydroorotate dehydrogenase-like protein; |
278-339 |
2.39e-04 |
|
dihydroorotate dehydrogenase-like protein;
Pssm-ID: 236051 Cd Length: 334 Bit Score: 42.55 E-value: 2.39e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2787263404 278 DLAIigVGGVDSADAAYAKIRAGANAIQLYTGLVYHGPGLVQQIKDGLVERLQADGFASVSE 339
Cdd:PRK07565 241 DLAA--TTGVHDAEDVIKMLLAGADVVMIASALLRHGPDYIGTILRGLEDWMERHGYESLQQ 300
|
|
| PRK04169 |
PRK04169 |
heptaprenylglyceryl phosphate synthase; |
251-326 |
5.34e-03 |
|
heptaprenylglyceryl phosphate synthase;
Pssm-ID: 235237 Cd Length: 232 Bit Score: 37.87 E-value: 5.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2787263404 251 EAGGLSGPPIferSTQLVRLFREAAGPDLAIIGvGGVDSADAAYAKIRAGANAIQlyTG-LVYHGP-GLVQQIKDGLV 326
Cdd:PRK04169 161 EYGGGAGDPV---PPEMVKAVKKALDITPLIYG-GGIRSPEQARELMAAGADTIV--VGnIIEEDPkKTVKAIKKAIK 232
|
|
| |
