|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
25-370 |
1.65e-151 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 431.12 E-value: 1.65e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 25 YKHIIKPhFVFNQTPDVAHDQMIQFCKITKNiPPLMWACREMLNYSDPVLETSVMGVDFVNPFGLSAGLDKNCEMPVLLD 104
Cdd:PRK05286 2 YYPLARP-LLFKLDPETAHELTIRALKRASR-TPLLSLLRQRLTYTDPRLPVTVMGLTFPNPVGLAAGFDKNGEAIDALG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 105 NAGFGFETVGSTTSRPCPGNPKPWFHRLPEYDSMMVHVGLANEGSEIVVPRAEQAWtkaRDMQISVSIARTnddKTGDLD 184
Cdd:PRK05286 80 ALGFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKAY---RGIPLGINIGKN---KDTPLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 185 EGIEDYCISMRRTAGRTAMVEVNISCPNTMAGEPFnQSPEALDKLFTELDKI----ERPQPTLVKMPLNKSWEEFKDLLD 260
Cdd:PRK05286 154 DAVDDYLICLEKLYPYADYFTVNISSPNTPGLRDL-QYGEALDELLAALKEAqaelHGYVPLLVKIAPDLSDEELDDIAD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 261 VLAEHNVQGLSIANLQKDRAGME--IPRDWEGGLSGSPCYEASNERIKQVYREYGDRFAIAGIGGVFTPQQAYAKIRSGS 338
Cdd:PRK05286 233 LALEHGIDGVIATNTTLSRDGLKglPNADEAGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGA 312
|
330 340 350
....*....|....*....|....*....|..
gi 490331880 339 SLVMFISSLMYRGPQQITVLKRGLAELLKRDG 370
Cdd:PRK05286 313 SLVQIYSGLIYEGPGLVKEIVRGLARLLRRDG 344
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
33-362 |
2.10e-124 |
|
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: 361.82 E-value: 2.10e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 33 FVFNQTPDVAHDQMIQFCKITKNIPPlmwacREMLNYSDPVLETSVMGVDFVNPFGLSAGLDKNCEMPVLLDNAGFGFET 112
Cdd:cd04738 3 LLFLLDPETAHRLAIRALKLGLGPPL-----LLLLVYDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFVE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 113 VGSTTSRPCPGNPKPWFHRLPEYDSMMVHVGLANEGSEIVVPRAEQAWtkARDMQISVSIARTnddKTGDLDEGIEDYCI 192
Cdd:cd04738 78 VGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRR--PRGGPLGVNIGKN---KDTPLEDAVEDYVI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 193 SMRRTAGRTAMVEVNISCPNTMAGEPFnQSPEALDKLFT----ELDKIERPQPTLVKMPLNKSWEEFKDLLDVLAEHNVQ 268
Cdd:cd04738 153 GVRKLGPYADYLVVNVSSPNTPGLRDL-QGKEALRELLTavkeERNKLGKKVPLLVKIAPDLSDEELEDIADVALEHGVD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 269 GLSIANLQKDRAG--MEIPRDWEGGLSGSPCYEASNERIKQVYREYGDRFAIAGIGGVFTPQQAYAKIRSGSSLVMFISS 346
Cdd:cd04738 232 GIIATNTTISRPGllRSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTG 311
|
330
....*....|....*.
gi 490331880 347 LMYRGPQQITVLKRGL 362
Cdd:cd04738 312 LVYEGPGLVKRIKREL 327
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
74-375 |
3.16e-89 |
|
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: 270.79 E-value: 3.16e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 74 LETSVMGVDFVNPFGLSAG-LDKNCEMPVLLDNAGFGFETVGSTTSRPCPGNPKPWFHRLPEYDSMMVHVGLANEGSEIV 152
Cdd:COG0167 2 LSVELAGLKFPNPVGLASGfFDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 153 VPRAEQAwtKARDMQISVSIARTNddktgdldegIEDYCISMRRTAGRTA-MVEVNISCPNTMA-GEPFNQSPEALDKLF 230
Cdd:COG0167 82 LERLLPA--KRYDVPVIVNIGGNT----------VEDYVELARRLADAGAdYLELNISCPNTPGgGRALGQDPEALAELL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 231 TELDKiERPQPTLVKMPLNksWEEFKDLLDVLAEHNVQGLSIANLQKDRA-----GMEIPRDWEGGLSGSPCYEASNERI 305
Cdd:COG0167 150 AAVKA-ATDKPVLVKLAPD--LTDIVEIARAAEEAGADGVIAINTTLGRAidletRRPVLANEAGGLSGPALKPIALRMV 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 306 KQVYREYGDRFAIAGIGGVFTPQQAYAKIRSGSSLVMFISSLMYRGPQQITVLKRGLAELLKRDGFDHVS 375
Cdd:COG0167 227 REVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSIS 296
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
31-362 |
9.94e-58 |
|
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: 191.15 E-value: 9.94e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 31 PHFVFNQTPDVAHDQMIQFCKITKNIPPLMWAcREMLNYSDPvLETSVMGVDFVNPFGLSAGLDKNCEMPVLLDNAGFGF 110
Cdd:TIGR01036 5 RKLLFLLDPESAHELTFQFLRLGTGTPFLALL-RSLFGASDP-LEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAMGFGF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 111 ETVGSTTSRPCPGNPKPWFHRLPEYDSMMVHVGLANEGSEIVVPRAEQAwtkARDMQISVSIARTNDDKTGDldeGIEDY 190
Cdd:TIGR01036 83 LEIGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLKRA---RYKGPIGINIGKNKDTPSED---AKEDY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 191 CISMRRTAGRTAMVEVNISCPNTmAGEPFNQSPEALDKLFT-------ELDKIERPqPTLVKMPLNKSWEEFKDLLDVLA 263
Cdd:TIGR01036 157 AACLRKLGPLADYLVVNVSSPNT-PGLRDLQYKAELRDLLTavkqeqdGLRRVHRV-PVLVKIAPDLTESDLEDIADSLV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 264 EHNVQGLSIANLQKDRAGMEIPRDWE--GGLSGSPCYEASNERIKQVYREYGDRFAIAGIGGVFTPQQAYAKIRSGSSLV 341
Cdd:TIGR01036 235 ELGIDGVIATNTTVSRSLVQGPKNSDetGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGASLL 314
|
330 340
....*....|....*....|.
gi 490331880 342 MFISSLMYRGPQQITVLKRGL 362
Cdd:TIGR01036 315 QIYSGFIYWGPPLVKEIVKEI 335
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
73-366 |
4.76e-48 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 164.83 E-value: 4.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 73 VLETSVMGVDFVNPFGLSAGLDKNCE-MPVLLDNAGFGFETVGSTTSRPCPGNPKPWFHRLPEydSMMVHVGLANEGSEI 151
Cdd:pfam01180 1 MLATKIPGLDFKNPIGLASGFDKFGEeALKWLALGKFGAIEIKSVTPYPQPGNPTPRVFRLPE--GVLNRMGLNNPGLDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 152 VVPRAEQAWTKARDMQISVSIARTNDDktgdldegIEDYcISMRRTAGRTA-MVEVNISCPNTMAGEPFNQSPEALDKLF 230
Cdd:pfam01180 79 VLAELLKRRKEYPRPDLGINLSKAGMT--------VDDY-VEVARKIGPFAdYIELNVSCPNTPGLRALQTDPELAAILL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 231 TELDKIERPqPTLVKMPLNKSWEEFKDLLDVLA-EHNVQGLSIAN--LQKDRAGME----IPRDWEGGLSGSPCYEASNE 303
Cdd:pfam01180 150 KVVKEVSKV-PVLVKLAPDLTDIVIIDIADVALgEDGLDGINATNttVRGMRIDLKtekpILANGTGGLSGPPIKPIALK 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490331880 304 RIKQVYREYGDRFAIAGIGGVFTPQQAYAKIRSGSSLVMFISSLMYRGPQQITVLKRGLAELL 366
Cdd:pfam01180 229 VIRELYQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
25-370 |
1.65e-151 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 431.12 E-value: 1.65e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 25 YKHIIKPhFVFNQTPDVAHDQMIQFCKITKNiPPLMWACREMLNYSDPVLETSVMGVDFVNPFGLSAGLDKNCEMPVLLD 104
Cdd:PRK05286 2 YYPLARP-LLFKLDPETAHELTIRALKRASR-TPLLSLLRQRLTYTDPRLPVTVMGLTFPNPVGLAAGFDKNGEAIDALG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 105 NAGFGFETVGSTTSRPCPGNPKPWFHRLPEYDSMMVHVGLANEGSEIVVPRAEQAWtkaRDMQISVSIARTnddKTGDLD 184
Cdd:PRK05286 80 ALGFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKAY---RGIPLGINIGKN---KDTPLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 185 EGIEDYCISMRRTAGRTAMVEVNISCPNTMAGEPFnQSPEALDKLFTELDKI----ERPQPTLVKMPLNKSWEEFKDLLD 260
Cdd:PRK05286 154 DAVDDYLICLEKLYPYADYFTVNISSPNTPGLRDL-QYGEALDELLAALKEAqaelHGYVPLLVKIAPDLSDEELDDIAD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 261 VLAEHNVQGLSIANLQKDRAGME--IPRDWEGGLSGSPCYEASNERIKQVYREYGDRFAIAGIGGVFTPQQAYAKIRSGS 338
Cdd:PRK05286 233 LALEHGIDGVIATNTTLSRDGLKglPNADEAGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGA 312
|
330 340 350
....*....|....*....|....*....|..
gi 490331880 339 SLVMFISSLMYRGPQQITVLKRGLAELLKRDG 370
Cdd:PRK05286 313 SLVQIYSGLIYEGPGLVKEIVRGLARLLRRDG 344
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
33-362 |
2.10e-124 |
|
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: 361.82 E-value: 2.10e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 33 FVFNQTPDVAHDQMIQFCKITKNIPPlmwacREMLNYSDPVLETSVMGVDFVNPFGLSAGLDKNCEMPVLLDNAGFGFET 112
Cdd:cd04738 3 LLFLLDPETAHRLAIRALKLGLGPPL-----LLLLVYDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFVE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 113 VGSTTSRPCPGNPKPWFHRLPEYDSMMVHVGLANEGSEIVVPRAEQAWtkARDMQISVSIARTnddKTGDLDEGIEDYCI 192
Cdd:cd04738 78 VGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRR--PRGGPLGVNIGKN---KDTPLEDAVEDYVI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 193 SMRRTAGRTAMVEVNISCPNTMAGEPFnQSPEALDKLFT----ELDKIERPQPTLVKMPLNKSWEEFKDLLDVLAEHNVQ 268
Cdd:cd04738 153 GVRKLGPYADYLVVNVSSPNTPGLRDL-QGKEALRELLTavkeERNKLGKKVPLLVKIAPDLSDEELEDIADVALEHGVD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 269 GLSIANLQKDRAG--MEIPRDWEGGLSGSPCYEASNERIKQVYREYGDRFAIAGIGGVFTPQQAYAKIRSGSSLVMFISS 346
Cdd:cd04738 232 GIIATNTTISRPGllRSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTG 311
|
330
....*....|....*.
gi 490331880 347 LMYRGPQQITVLKRGL 362
Cdd:cd04738 312 LVYEGPGLVKRIKREL 327
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
74-375 |
3.16e-89 |
|
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: 270.79 E-value: 3.16e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 74 LETSVMGVDFVNPFGLSAG-LDKNCEMPVLLDNAGFGFETVGSTTSRPCPGNPKPWFHRLPEYDSMMVHVGLANEGSEIV 152
Cdd:COG0167 2 LSVELAGLKFPNPVGLASGfFDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 153 VPRAEQAwtKARDMQISVSIARTNddktgdldegIEDYCISMRRTAGRTA-MVEVNISCPNTMA-GEPFNQSPEALDKLF 230
Cdd:COG0167 82 LERLLPA--KRYDVPVIVNIGGNT----------VEDYVELARRLADAGAdYLELNISCPNTPGgGRALGQDPEALAELL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 231 TELDKiERPQPTLVKMPLNksWEEFKDLLDVLAEHNVQGLSIANLQKDRA-----GMEIPRDWEGGLSGSPCYEASNERI 305
Cdd:COG0167 150 AAVKA-ATDKPVLVKLAPD--LTDIVEIARAAEEAGADGVIAINTTLGRAidletRRPVLANEAGGLSGPALKPIALRMV 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 306 KQVYREYGDRFAIAGIGGVFTPQQAYAKIRSGSSLVMFISSLMYRGPQQITVLKRGLAELLKRDGFDHVS 375
Cdd:COG0167 227 REVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSIS 296
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
39-381 |
2.48e-60 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 200.35 E-value: 2.48e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 39 PDVAHDQMIQFCKitknippLMWACREMlNYSDPVLETSVMGVDFVNPFGLSAGLDKNCE-MPVLLDnAGFGFETVGSTT 117
Cdd:PLN02826 47 PETAHSLAISAAA-------RGLVPREK-RPDPSVLGVEVWGRTFSNPIGLAAGFDKNAEaVEGLLG-LGFGFVEIGSVT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 118 SRPCPGNPKPWFHRLPEYDSMMVHVGLANEGSEIVVPRAEQAWTKARDMQISVSIARTNDDKTGDL-------------- 183
Cdd:PLN02826 118 PLPQPGNPKPRVFRLREEGAIINRYGFNSEGIVAVAKRLGAQHGKRKLDETSSSSFSSDDVKAGGKagpgilgvnlgknk 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 184 --DEGIEDYCISMRrTAGRTA--MVeVNISCPNTmAG----EPFNQSPEALDKLFTELDKIERPQ----PTLVKMPLNKS 251
Cdd:PLN02826 198 tsEDAAADYVQGVR-ALSQYAdyLV-INVSSPNT-PGlrklQGRKQLKDLLKKVLAARDEMQWGEegppPLLVKIAPDLS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 252 WEEFKDLLDVLAEHNVQGLSIANLQKDRAGMEIP---RDWEGGLSGSPCYEASNERIKQVYREYGDRFAIAGIGGVFTPQ 328
Cdd:PLN02826 275 KEDLEDIAAVALALGIDGLIISNTTISRPDSVLGhphADEAGGLSGKPLFDLSTEVLREMYRLTRGKIPLVGCGGVSSGE 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 490331880 329 QAYAKIRSGSSLVMFISSLMYRGPQQITVLKRGLAELLKRDGFDHVSQAVGID 381
Cdd:PLN02826 355 DAYKKIRAGASLVQLYTAFAYEGPALIPRIKAELAACLERDGFKSIQEAVGAD 407
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
31-362 |
9.94e-58 |
|
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: 191.15 E-value: 9.94e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 31 PHFVFNQTPDVAHDQMIQFCKITKNIPPLMWAcREMLNYSDPvLETSVMGVDFVNPFGLSAGLDKNCEMPVLLDNAGFGF 110
Cdd:TIGR01036 5 RKLLFLLDPESAHELTFQFLRLGTGTPFLALL-RSLFGASDP-LEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAMGFGF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 111 ETVGSTTSRPCPGNPKPWFHRLPEYDSMMVHVGLANEGSEIVVPRAEQAwtkARDMQISVSIARTNDDKTGDldeGIEDY 190
Cdd:TIGR01036 83 LEIGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLKRA---RYKGPIGINIGKNKDTPSED---AKEDY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 191 CISMRRTAGRTAMVEVNISCPNTmAGEPFNQSPEALDKLFT-------ELDKIERPqPTLVKMPLNKSWEEFKDLLDVLA 263
Cdd:TIGR01036 157 AACLRKLGPLADYLVVNVSSPNT-PGLRDLQYKAELRDLLTavkqeqdGLRRVHRV-PVLVKIAPDLTESDLEDIADSLV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 264 EHNVQGLSIANLQKDRAGMEIPRDWE--GGLSGSPCYEASNERIKQVYREYGDRFAIAGIGGVFTPQQAYAKIRSGSSLV 341
Cdd:TIGR01036 235 ELGIDGVIATNTTVSRSLVQGPKNSDetGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGASLL 314
|
330 340
....*....|....*....|.
gi 490331880 342 MFISSLMYRGPQQITVLKRGL 362
Cdd:TIGR01036 315 QIYSGFIYWGPPLVKEIVKEI 335
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
73-366 |
4.76e-48 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 164.83 E-value: 4.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 73 VLETSVMGVDFVNPFGLSAGLDKNCE-MPVLLDNAGFGFETVGSTTSRPCPGNPKPWFHRLPEydSMMVHVGLANEGSEI 151
Cdd:pfam01180 1 MLATKIPGLDFKNPIGLASGFDKFGEeALKWLALGKFGAIEIKSVTPYPQPGNPTPRVFRLPE--GVLNRMGLNNPGLDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 152 VVPRAEQAWTKARDMQISVSIARTNDDktgdldegIEDYcISMRRTAGRTA-MVEVNISCPNTMAGEPFNQSPEALDKLF 230
Cdd:pfam01180 79 VLAELLKRRKEYPRPDLGINLSKAGMT--------VDDY-VEVARKIGPFAdYIELNVSCPNTPGLRALQTDPELAAILL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 231 TELDKIERPqPTLVKMPLNKSWEEFKDLLDVLA-EHNVQGLSIAN--LQKDRAGME----IPRDWEGGLSGSPCYEASNE 303
Cdd:pfam01180 150 KVVKEVSKV-PVLVKLAPDLTDIVIIDIADVALgEDGLDGINATNttVRGMRIDLKtekpILANGTGGLSGPPIKPIALK 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490331880 304 RIKQVYREYGDRFAIAGIGGVFTPQQAYAKIRSGSSLVMFISSLMYRGPQQITVLKRGLAELL 366
Cdd:pfam01180 229 VIRELYQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
76-352 |
7.90e-43 |
|
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: 150.97 E-value: 7.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 76 TSVMGVDFVNPFGLSAGLD-KNCEMPVLLDNAGFGFETVGSTTSRPCPGNPKPWFHRLPEYD-------SMMVHVGLANE 147
Cdd:cd02810 1 VNFLGLKLKNPFGVAAGPLlKTGELIARAAAAGFGAVVYKTVTLHPRPGNPLPRVARLPPEGesypeqlGILNSFGLPNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 148 GSEIVVPRAEQAWTKARDMQISVSIARTnddktgdldeGIEDYcISMRRTAGR--TAMVEVNISCPNTMAGEPFNQSPEA 225
Cdd:cd02810 81 GLDVWLQDIAKAKKEFPGQPLIASVGGS----------SKEDY-VELARKIERagAKALELNLSCPNVGGGRQLGQDPEA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 226 LDKLFTELdKIERPQPTLVKMPLNKSWEEFKDLLDVLAEHNVQGLSIAN-----LQKDRAGMEIPRDWEGGLSGSPCYEA 300
Cdd:cd02810 150 VANLLKAV-KAAVDIPLLVKLSPYFDLEDIVELAKAAERAGADGLTAINtisgrVVDLKTVGPGPKRGTGGLSGAPIRPL 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 490331880 301 SNERIKQVYREYGDRFAIAGIGGVFTPQQAYAKIRSGSSLVMFISSLMYRGP 352
Cdd:cd02810 229 ALRWVARLAARLQLDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGP 280
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
75-380 |
1.75e-26 |
|
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: 107.25 E-value: 1.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 75 ETSVMGVDFVNPFGLSAG-LDKNCEMPVLLDNAGFGFETVGSTTSRPCPGNPKPwfhRLPEYDS-MMVHVGLANEGSEIV 152
Cdd:cd04740 1 SVELAGLRLKNPVILASGtFGFGEELSRVADLGKLGAIVTKSITLEPREGNPPP---RVVETPGgMLNAIGLQNPGVEAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 153 VpRAEQAWTKARDMQISVSIARTNDDKTGDLDEGIEDYCIsmrrtagrtAMVEVNISCPNTMA-GEPFNQSPEALDKLFT 231
Cdd:cd04740 78 L-EELLPWLREFGTPVIASIAGSTVEEFVEVAEKLADAGA---------DAIELNISCPNVKGgGMAFGTDPEAVAEIVK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 232 ELDKIERpQPTLVKMPLNKSweefkDLLDV---LAEHNVQGLSIANLQKdraGMEIprDWE----------GGLSGsPCy 298
Cdd:cd04740 148 AVKKATD-VPVIVKLTPNVT-----DIVEIaraAEEAGADGLTLINTLK---GMAI--DIEtrkpilgnvtGGLSG-PA- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 299 easnerIK--------QVYREYGdrFAIAGIGGVFTPQQAYAKIRSGSSLVMfISSLMYRGPQQITVLKRGLAELLKRDG 370
Cdd:cd04740 215 ------IKpialrmvyQVYKAVE--IPIIGVGGIASGEDALEFLMAGASAVQ-VGTANFVDPEAFKEIIEGLEAYLDEEG 285
|
330
....*....|
gi 490331880 371 FDHVSQAVGI 380
Cdd:cd04740 286 IKSIEELVGL 295
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
74-380 |
3.18e-21 |
|
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: 92.88 E-value: 3.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 74 LETSVMGVDFVNPFGLSAG-LDKNCEMPVLLDNAGFGFETVGSTTSRPCPGNPKPwfhRLPE-YDSMMVHVGLANEGSEI 151
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGiMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNP---TIVEtPCGMLNAIGLQNPGVEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 152 VVpRAEQAWTKARDMQISVSIARTNDDKTGDLDEGIEDycismrrtAGRTA-MVEVNISCPNTM-AGEPFNQSPEALDKL 229
Cdd:TIGR01037 78 FL-EELKPVREEFPTPLIASVYGSSVEEFAEVAEKLEK--------APPYVdAYELNLSCPHVKgGGIAIGQDPELSADV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 230 FTEL-DKIERpqPTLVKMPLNKSweEFKDLLDVLAEHNVQGLSIANLQKD-----RAGMEIPRDWEGGLSGSPCYEASNE 303
Cdd:TIGR01037 149 VKAVkDKTDV--PVFAKLSPNVT--DITEIAKAAEEAGADGLTLINTLRGmkidiKTGKPILANKTGGLSGPAIKPIALR 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490331880 304 RIKQVYREYGdrFAIAGIGGVFTPQQAYAKIRSGSSLVMFISSLMYRG--PQQItvlKRGLAELLKRDGFDHVSQAVGI 380
Cdd:TIGR01037 225 MVYDVYKMVD--IPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYRGfaFKKI---IEGLIAFLKAEGFTSIEELIGI 298
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
74-380 |
1.19e-20 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 90.98 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 74 LETSVMGVDFVNPFGLSAG-LDKNCEMPVLLDNAGFGFETVGSTTSRPCPGNPKPWFHRLPeyDSMMVHVGLANEGSEIV 152
Cdd:PRK07259 2 LSVELPGLKLKNPVMPASGtFGFGGEYARFYDLNGLGAIVTKSTTLEPREGNPTPRIAETP--GGMLNAIGLQNPGVDAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 153 VPRaEQAWTKARDMQISVSIARTNDDKTGDLDEGIEDycismrrtAGRTAMVEVNISCPNTMA-GEPFNQSPEALDKLFT 231
Cdd:PRK07259 80 IEE-ELPWLEEFDTPIIANVAGSTEEEYAEVAEKLSK--------APNVDAIELNISCPNVKHgGMAFGTDPELAYEVVK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 232 ELDKIERpQPTLVKMPLNKSweefkDLLDV---LAEHNVQGLSIANLQKdraGMEIprDWE----------GGLSGsPCy 298
Cdd:PRK07259 151 AVKEVVK-VPVIVKLTPNVT-----DIVEIakaAEEAGADGLSLINTLK---GMAI--DIKtrkpilanvtGGLSG-PA- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 299 easnerIK--------QVYREYgdRFAIAGIGGVFTPQQAYAKIRSGSSLVMfISSLMYRGPQQITVLKRGLAELLKRDG 370
Cdd:PRK07259 218 ------IKpialrmvyQVYQAV--DIPIIGMGGISSAEDAIEFIMAGASAVQ-VGTANFYDPYAFPKIIEGLEAYLDKYG 288
|
330
....*....|
gi 490331880 371 FDHVSQAVGI 380
Cdd:PRK07259 289 IKSIEEIVGI 298
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
74-379 |
1.06e-11 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 64.98 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 74 LETSVMGVDFVNPFGLSAGLdkNC----EMPVLLDNAGFGFETvGSTTSRPCPGNPKPWFHRLP--EYDSMmvhvGLANE 147
Cdd:PRK02506 2 TSTQIAGFKFDNCLMNAAGV--YCmtkeELEEVEASAAGAFVT-KSATLEPRPGNPEPRYADTPlgSINSM----GLPNL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 148 GSEIVVPRAEQAWTKARDMQISVSIARTNDDKTGDLDEGIEDycismrrtAGRTAMVEVNISCPNtMAGEP-----FNQS 222
Cdd:PRK02506 75 GFDYYLDYVLELQKKGPNKPHFLSVVGLSPEETHTILKKIQA--------SDFNGLVELNLSCPN-VPGKPqiaydFETT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 223 PEALDKLFTELDKierpqPTLVKMPLNKSWEEFKDLLDVLAEHNVQGL----SIAN----LQKDRAGMEIPRDWEGGLSG 294
Cdd:PRK02506 146 EQILEEVFTYFTK-----PLGVKLPPYFDIVHFDQAAAIFNKFPLAFVncinSIGNglviDPEDETVVIKPKNGFGGIGG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 295 S---PCYEASnerIKQVYREYGDRFAIAGIGGVFTPQQAYAKIRSGSSLVMFISSLMYRGPQQITVLKRGLAELLKRDGF 371
Cdd:PRK02506 221 DyikPTALAN---VRAFYQRLNPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAIMAEKGY 297
|
....*...
gi 490331880 372 DHVSQAVG 379
Cdd:PRK02506 298 QSLEDFRG 305
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
112-365 |
2.68e-11 |
|
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: 63.88 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 112 TVGSTTSRPCPGNPKPWFHRLPEY--DSMmvhvGLANEG----SEIVVPRAEQAWTKARDMQISVsiartnddkTGDLDE 185
Cdd:cd04741 38 TTRSSTLAGRPGNPEPRYYAFPLGsiNSL----GLPNLGldyyLEYIRTISDGLPGSAKPFFISV---------TGSAED 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 186 GIEDYCISMRRTAGRTAMVEVNISCPNTMAGEPFNQSPEALDKLFTELDKIERPqPTLVKMPLNKSWEEFKDLLDVLAEH 265
Cdd:cd04741 105 IAAMYKKIAAHQKQFPLAMELNLSCPNVPGKPPPAYDFDATLEYLTAVKAAYSI-PVGVKTPPYTDPAQFDTLAEALNAF 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 266 ----------NvqglSIAN-LQKDRAGMEI---PRDWEGGLSGSPCYEASNERIKQVYREYGDRFAIAGIGGVFTPQQAY 331
Cdd:cd04741 184 acpisfitatN----TLGNgLVLDPERETVvlkPKTGFGGLAGAYLHPLALGNVRTFRRLLPSEIQIIGVGGVLDGRGAF 259
|
250 260 270
....*....|....*....|....*....|....
gi 490331880 332 AKIRSGSSLVMFISSLMYRGPqqiTVLKRGLAEL 365
Cdd:cd04741 260 RMRLAGASAVQVGTALGKEGP---KVFARIEKEL 290
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
253-341 |
1.06e-04 |
|
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 240086 [Multi-domain] Cd Length: 353 Bit Score: 43.74 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490331880 253 EEFKDLLDVLAEHNVQGLSIANLQKDRAGMEIPrdwegglsgspcyEASNERIKQVYREYGDRFAIAGIGGVFTPQQAYA 332
Cdd:cd04735 235 EDTLALVDKLADKGLDYLHISLWDFDRKSRRGR-------------DDNQTIMELVKERIAGRLPLIAVGSINTPDDALE 301
|
....*....
gi 490331880 333 KIRSGSSLV 341
Cdd:cd04735 302 ALETGADLV 310
|
|
| PRK07565 |
PRK07565 |
dihydroorotate dehydrogenase-like protein; |
318-376 |
1.55e-03 |
|
dihydroorotate dehydrogenase-like protein;
Pssm-ID: 236051 Cd Length: 334 Bit Score: 40.24 E-value: 1.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 490331880 318 IAGIGGVFTPQQAYAKIRSGSSLVMFISSLMYRGPQQITVLKRGLAELLKRDGFDHVSQ 376
Cdd:PRK07565 242 LAATTGVHDAEDVIKMLLAGADVVMIASALLRHGPDYIGTILRGLEDWMERHGYESLQQ 300
|
|
| DHOD_like |
cd04739 |
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
318-376 |
1.64e-03 |
|
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: 39.91 E-value: 1.64e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 490331880 318 IAGIGGVFTPQQAYAKIRSGSSLVMFISSLMYRGPQQITVLKRGLAELLKRDGFDHVSQ 376
Cdd:cd04739 240 LAASGGVHDAEDVVKYLLAGADVVMTTSALLRHGPDYIGTLLAGLEAWMEEHGYESVQQ 298
|
|
| |
