|
Name |
Accession |
Description |
Interval |
E-value |
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
1-311 |
0e+00 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 616.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 1 MLNTTFANAKFANPFMNASGVHCMTIEDLEELKASQAGAYITKSSTLEKREGNPLPRYVDLELGSINSMGLPNLGFDYYL 80
Cdd:PRK02506 1 STSTQIAGFKFDNCLMNAAGVYCMTKEELEEVEASAAGAFVTKSATLEPRPGNPEPRYADTPLGSINSMGLPNLGFDYYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 81 DYVLKNQKENaQEGPIFFSIAGMSAAENIAMLKKIQESDFSGITELNLSCPNVPGKPQLAYDFEATEKLLKEVFTFFTKP 160
Cdd:PRK02506 81 DYVLELQKKG-PNKPHFLSVVGLSPEETHTILKKIQASDFNGLVELNLSCPNVPGKPQIAYDFETTEQILEEVFTYFTKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 161 LGVKLPPYFDLVHFDIMAEILNQFPLTYVNSVNSIGNGLFIDPEAESVVIKPKDGFGGIGGAYIKPTALANVRAFYTRLK 240
Cdd:PRK02506 160 LGVKLPPYFDIVHFDQAAAIFNKFPLAFVNCINSIGNGLVIDPEDETVVIKPKNGFGGIGGDYIKPTALANVRAFYQRLN 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2098351 241 PEIQIIGTGGIETGQDAFEHLLCGATMLQIGTALHKEGPAIFDRIIKELEEIMNQKGYQSIADFHGKLKSL 311
Cdd:PRK02506 240 PSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAIMAEKGYQSLEDFRGKLKYL 310
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
4-293 |
6.88e-173 |
|
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: 480.28 E-value: 6.88e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 4 TTFANAKFANPFMNASGVHCMTIEDLEELKASQAGAYITKSSTLEKREGNPLPRYVDLELGSINSMGLPNLGFDYYLDYV 83
Cdd:cd04741 1 VTPPGLTISPPLMNAAGPWCTTLEDLLELAASSTGAVTTRSSTLAGRPGNPEPRYYAFPLGSINSLGLPNLGLDYYLEYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 84 LKNQKEN-AQEGPIFFSIAGMsAAENIAMLKKIQESD--FSGITELNLSCPNVPGKPQLAYDFEATEKLLKEVFTFFTKP 160
Cdd:cd04741 81 RTISDGLpGSAKPFFISVTGS-AEDIAAMYKKIAAHQkqFPLAMELNLSCPNVPGKPPPAYDFDATLEYLTAVKAAYSIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 161 LGVKLPPYFDLVHFDIMAEILNQF--PLTYVNSVNSIGNGLFIDPEAESVVIKPKDGFGGIGGAYIKPTALANVRAFYTR 238
Cdd:cd04741 160 VGVKTPPYTDPAQFDTLAEALNAFacPISFITATNTLGNGLVLDPERETVVLKPKTGFGGLAGAYLHPLALGNVRTFRRL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2098351 239 LKPEIQIIGTGGIETGQDAFEHLLCGATMLQIGTALHKEGPAIFDRIIKELEEIM 293
Cdd:cd04741 240 LPSEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEKELEDIW 294
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
1-293 |
1.27e-142 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 403.65 E-value: 1.27e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 1 MLNTTFANAKFANPFMNASGVHCMTIEDLEELKASQAGAYITKSSTLEKREGNPLPRYVDLELGSINSMGLPNLGFDYYL 80
Cdd:pfam01180 1 MLATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVTPYPQPGNPTPRVFRLPEGVLNRMGLNNPGLDAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 81 DYVLKNQKENAQ-EGPIFFSIAGMSAAENIAMLKKIQEsdFSGITELNLSCPNVPGKPQLAYDFEATEKLLKEVFTFFTK 159
Cdd:pfam01180 81 AELLKRRKEYPRpDLGINLSKAGMTVDDYVEVARKIGP--FADYIELNVSCPNTPGLRALQTDPELAAILLKVVKEVSKV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 160 PLGVKLPP-YFDLVHFDIMAEILNQFPLTYVNSVNSIGNGLFIDPEAESVVIKPkdGFGGIGGAYIKPTALANVRAFYTR 238
Cdd:pfam01180 159 PVLVKLAPdLTDIVIIDIADVALGEDGLDGINATNTTVRGMRIDLKTEKPILAN--GTGGLSGPPIKPIALKVIRELYQR 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2098351 239 LKPEIQIIGTGGIETGQDAFEHLLCGATMLQIGTALHKEGPAIFDRIIKELEEIM 293
Cdd:pfam01180 237 TGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
2-302 |
3.12e-103 |
|
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: 303.92 E-value: 3.12e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 2 LNTTFANAKFANPFMNASGVHCMTIEDLEELKASQAGAYITKSSTLEKREGNPLPRYVDL--ELGSINSMGLPNLGFDYY 79
Cdd:COG0167 2 LSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLpeDSGLINRMGLNNPGVDAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 80 LDYVLKNQKENaqeGPIFFSIAGMSAAENIAMLKKIQESDFSGItELNLSCPNVPGK-PQLAYDFEATEKLLKEVFTFFT 158
Cdd:COG0167 82 LERLLPAKRYD---VPVIVNIGGNTVEDYVELARRLADAGADYL-ELNISCPNTPGGgRALGQDPEALAELLAAVKAATD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 159 KPLGVKLPPyfDLVHFDIMAEILNQFPLTYVNSVNSIgNGLFIDPEAESVVIKpkDGFGGIGGAYIKPTALANVRAFYTR 238
Cdd:COG0167 158 KPVLVKLAP--DLTDIVEIARAAEEAGADGVIAINTT-LGRAIDLETRRPVLA--NEAGGLSGPALKPIALRMVREVAQA 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2098351 239 LKPEIQIIGTGGIETGQDAFEHLLCGATMLQIGTALHKEGPAIFDRIIKELEEIMNQKGYQSIA 302
Cdd:COG0167 233 VGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSIS 296
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
2-306 |
2.14e-50 |
|
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: 168.76 E-value: 2.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 2 LNTTFANAKFANPFMNASGVHCMTIEDLEELKASQAGAYITKSSTLEKREGNPLPRYVDLELGSINSMGLPNLGFDYYLD 81
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTIVETPCGMLNAIGLQNPGVEAFLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 82 YVLKNQKEnaQEGPIFFSIAGMSAAENIAMLKKIQESD-FSGITELNLSCPNVPG-------KPQLAYDfeatekLLKEV 153
Cdd:TIGR01037 81 ELKPVREE--FPTPLIASVYGSSVEEFAEVAEKLEKAPpYVDAYELNLSCPHVKGggiaigqDPELSAD------VVKAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 154 FTFFTKPLGVKLPPYF-DLVHFDIMAEILNQFPLTYVNSVnsigNGLFIDPEAESVVIKPKdgFGGIGGAYIKPTALANV 232
Cdd:TIGR01037 153 KDKTDVPVFAKLSPNVtDITEIAKAAEEAGADGLTLINTL----RGMKIDIKTGKPILANK--TGGLSGPAIKPIALRMV 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2098351 233 RAFYTRLkpEIQIIGTGGIETGQDAFEHLLCGATMLQIGTALHKEgPAIFDRIIKELEEIMNQKGYQSIADFHG 306
Cdd:TIGR01037 227 YDVYKMV--DIPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYR-GFAFKKIIEGLIAFLKAEGFTSIEELIG 297
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
1-311 |
0e+00 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 616.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 1 MLNTTFANAKFANPFMNASGVHCMTIEDLEELKASQAGAYITKSSTLEKREGNPLPRYVDLELGSINSMGLPNLGFDYYL 80
Cdd:PRK02506 1 STSTQIAGFKFDNCLMNAAGVYCMTKEELEEVEASAAGAFVTKSATLEPRPGNPEPRYADTPLGSINSMGLPNLGFDYYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 81 DYVLKNQKENaQEGPIFFSIAGMSAAENIAMLKKIQESDFSGITELNLSCPNVPGKPQLAYDFEATEKLLKEVFTFFTKP 160
Cdd:PRK02506 81 DYVLELQKKG-PNKPHFLSVVGLSPEETHTILKKIQASDFNGLVELNLSCPNVPGKPQIAYDFETTEQILEEVFTYFTKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 161 LGVKLPPYFDLVHFDIMAEILNQFPLTYVNSVNSIGNGLFIDPEAESVVIKPKDGFGGIGGAYIKPTALANVRAFYTRLK 240
Cdd:PRK02506 160 LGVKLPPYFDIVHFDQAAAIFNKFPLAFVNCINSIGNGLVIDPEDETVVIKPKNGFGGIGGDYIKPTALANVRAFYQRLN 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2098351 241 PEIQIIGTGGIETGQDAFEHLLCGATMLQIGTALHKEGPAIFDRIIKELEEIMNQKGYQSIADFHGKLKSL 311
Cdd:PRK02506 240 PSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAIMAEKGYQSLEDFRGKLKYL 310
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
4-293 |
6.88e-173 |
|
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: 480.28 E-value: 6.88e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 4 TTFANAKFANPFMNASGVHCMTIEDLEELKASQAGAYITKSSTLEKREGNPLPRYVDLELGSINSMGLPNLGFDYYLDYV 83
Cdd:cd04741 1 VTPPGLTISPPLMNAAGPWCTTLEDLLELAASSTGAVTTRSSTLAGRPGNPEPRYYAFPLGSINSLGLPNLGLDYYLEYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 84 LKNQKEN-AQEGPIFFSIAGMsAAENIAMLKKIQESD--FSGITELNLSCPNVPGKPQLAYDFEATEKLLKEVFTFFTKP 160
Cdd:cd04741 81 RTISDGLpGSAKPFFISVTGS-AEDIAAMYKKIAAHQkqFPLAMELNLSCPNVPGKPPPAYDFDATLEYLTAVKAAYSIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 161 LGVKLPPYFDLVHFDIMAEILNQF--PLTYVNSVNSIGNGLFIDPEAESVVIKPKDGFGGIGGAYIKPTALANVRAFYTR 238
Cdd:cd04741 160 VGVKTPPYTDPAQFDTLAEALNAFacPISFITATNTLGNGLVLDPERETVVLKPKTGFGGLAGAYLHPLALGNVRTFRRL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2098351 239 LKPEIQIIGTGGIETGQDAFEHLLCGATMLQIGTALHKEGPAIFDRIIKELEEIM 293
Cdd:cd04741 240 LPSEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEKELEDIW 294
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
1-293 |
1.27e-142 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 403.65 E-value: 1.27e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 1 MLNTTFANAKFANPFMNASGVHCMTIEDLEELKASQAGAYITKSSTLEKREGNPLPRYVDLELGSINSMGLPNLGFDYYL 80
Cdd:pfam01180 1 MLATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVTPYPQPGNPTPRVFRLPEGVLNRMGLNNPGLDAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 81 DYVLKNQKENAQ-EGPIFFSIAGMSAAENIAMLKKIQEsdFSGITELNLSCPNVPGKPQLAYDFEATEKLLKEVFTFFTK 159
Cdd:pfam01180 81 AELLKRRKEYPRpDLGINLSKAGMTVDDYVEVARKIGP--FADYIELNVSCPNTPGLRALQTDPELAAILLKVVKEVSKV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 160 PLGVKLPP-YFDLVHFDIMAEILNQFPLTYVNSVNSIGNGLFIDPEAESVVIKPkdGFGGIGGAYIKPTALANVRAFYTR 238
Cdd:pfam01180 159 PVLVKLAPdLTDIVIIDIADVALGEDGLDGINATNTTVRGMRIDLKTEKPILAN--GTGGLSGPPIKPIALKVIRELYQR 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2098351 239 LKPEIQIIGTGGIETGQDAFEHLLCGATMLQIGTALHKEGPAIFDRIIKELEEIM 293
Cdd:pfam01180 237 TGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
4-288 |
4.63e-117 |
|
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: 338.94 E-value: 4.63e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 4 TTFANAKFANPFMNASGVHCMTIEDLEELKASQAGAYITKSSTLEKREGNPLPRYVDL---------ELGSINSMGLPNL 74
Cdd:cd02810 1 VNFLGLKLKNPFGVAAGPLLKTGELIARAAAAGFGAVVYKTVTLHPRPGNPLPRVARLppegesypeQLGILNSFGLPNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 75 GFDYYLDYVLKNQKEnAQEGPIFFSIAGMSAAENIAMLKKIQESdFSGITELNLSCPNVPGKPQLAYDFEATEKLLKEVF 154
Cdd:cd02810 81 GLDVWLQDIAKAKKE-FPGQPLIASVGGSSKEDYVELARKIERA-GAKALELNLSCPNVGGGRQLGQDPEAVANLLKAVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 155 TFFTKPLGVKLPPYFDLVHFDIMAEILNQFPLTYVNSVNSIGNGLFIDPEaesVVIKPKDGFGGIGGAYIKPTALANVRA 234
Cdd:cd02810 159 AAVDIPLLVKLSPYFDLEDIVELAKAAERAGADGLTAINTISGRVVDLKT---VGPGPKRGTGGLSGAPIRPLALRWVAR 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2098351 235 FYTRLKPEIQIIGTGGIETGQDAFEHLLCGATMLQIGTALHKEGPAIFDRIIKE 288
Cdd:cd02810 236 LAARLQLDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKIKKE 289
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
2-302 |
3.12e-103 |
|
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: 303.92 E-value: 3.12e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 2 LNTTFANAKFANPFMNASGVHCMTIEDLEELKASQAGAYITKSSTLEKREGNPLPRYVDL--ELGSINSMGLPNLGFDYY 79
Cdd:COG0167 2 LSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLpeDSGLINRMGLNNPGVDAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 80 LDYVLKNQKENaqeGPIFFSIAGMSAAENIAMLKKIQESDFSGItELNLSCPNVPGK-PQLAYDFEATEKLLKEVFTFFT 158
Cdd:COG0167 82 LERLLPAKRYD---VPVIVNIGGNTVEDYVELARRLADAGADYL-ELNISCPNTPGGgRALGQDPEALAELLAAVKAATD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 159 KPLGVKLPPyfDLVHFDIMAEILNQFPLTYVNSVNSIgNGLFIDPEAESVVIKpkDGFGGIGGAYIKPTALANVRAFYTR 238
Cdd:COG0167 158 KPVLVKLAP--DLTDIVEIARAAEEAGADGVIAINTT-LGRAIDLETRRPVLA--NEAGGLSGPALKPIALRMVREVAQA 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2098351 239 LKPEIQIIGTGGIETGQDAFEHLLCGATMLQIGTALHKEGPAIFDRIIKELEEIMNQKGYQSIA 302
Cdd:COG0167 233 VGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSIS 296
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
1-309 |
1.46e-62 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 200.38 E-value: 1.46e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 1 MLNTTFANAKFANPFMNASGVHCMTIEDLEELKASQAGAYITKSSTLEKREGNPLPRYVDLELGSINSMGLPNLGFDYYL 80
Cdd:PRK07259 1 RLSVELPGLKLKNPVMPASGTFGFGGEYARFYDLNGLGAIVTKSTTLEPREGNPTPRIAETPGGMLNAIGLQNPGVDAFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 81 DYVLKNQKEnaQEGPIFFSIAGMSAAENIAMLKKIQESDFSGITELNLSCPNVPG-------KPQLAYDfeatekLLKEV 153
Cdd:PRK07259 81 EEELPWLEE--FDTPIIANVAGSTEEEYAEVAEKLSKAPNVDAIELNISCPNVKHggmafgtDPELAYE------VVKAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 154 FTFFTKPLGVKLPPYF-DLVHFDIMAEILNQFPLTYVNSVnsigNGLFIDPEAEsvviKP--KDGFGGIGGAYIKPTALA 230
Cdd:PRK07259 153 KEVVKVPVIVKLTPNVtDIVEIAKAAEEAGADGLSLINTL----KGMAIDIKTR----KPilANVTGGLSGPAIKPIALR 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2098351 231 NVRAFYTRLKpeIQIIGTGGIETGQDAFEHLLCGATMLQIGTALHKeGPAIFDRIIKELEEIMNQKGYQSIADFHGKLK 309
Cdd:PRK07259 225 MVYQVYQAVD--IPIIGMGGISSAEDAIEFIMAGASAVQVGTANFY-DPYAFPKIIEGLEAYLDKYGIKSIEEIVGIAH 300
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
4-308 |
1.32e-58 |
|
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: 189.68 E-value: 1.32e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 4 TTFANAKFANPFMNASGVHCMTIEDLEELKASQAGAYITKSSTLEKREGNPLPRYVDLELGSINSMGLPNLGFDYYLDYV 83
Cdd:cd04740 2 VELAGLRLKNPVILASGTFGFGEELSRVADLGKLGAIVTKSITLEPREGNPPPRVVETPGGMLNAIGLQNPGVEAFLEEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 84 LKnqKENAQEGPIFFSIAGMSAAENIAMLKKIQESDFSGItELNLSCPNVP-GKPQLAYDFEATEKLLKEVFTFFTKPLG 162
Cdd:cd04740 82 LP--WLREFGTPVIASIAGSTVEEFVEVAEKLADAGADAI-ELNISCPNVKgGGMAFGTDPEAVAEIVKAVKKATDVPVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 163 VKLPPYF-DLVHFDIMAEILNQFPLTYVNSVnsigNGLFIDPEAESVVIkpKDGFGGIGGAYIKPTALANVRAFYTRLkp 241
Cdd:cd04740 159 VKLTPNVtDIVEIARAAEEAGADGLTLINTL----KGMAIDIETRKPIL--GNVTGGLSGPAIKPIALRMVYQVYKAV-- 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2098351 242 EIQIIGTGGIETGQDAFEHLLCGATMLQIGTALhKEGPAIFDRIIKELEEIMNQKGYQSIADFHGKL 308
Cdd:cd04740 231 EIPIIGVGGIASGEDALEFLMAGASAVQVGTAN-FVDPEAFKEIIEGLEAYLDEEGIKSIEELVGLA 296
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
2-306 |
2.14e-50 |
|
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: 168.76 E-value: 2.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 2 LNTTFANAKFANPFMNASGVHCMTIEDLEELKASQAGAYITKSSTLEKREGNPLPRYVDLELGSINSMGLPNLGFDYYLD 81
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTIVETPCGMLNAIGLQNPGVEAFLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 82 YVLKNQKEnaQEGPIFFSIAGMSAAENIAMLKKIQESD-FSGITELNLSCPNVPG-------KPQLAYDfeatekLLKEV 153
Cdd:TIGR01037 81 ELKPVREE--FPTPLIASVYGSSVEEFAEVAEKLEKAPpYVDAYELNLSCPHVKGggiaigqDPELSAD------VVKAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 154 FTFFTKPLGVKLPPYF-DLVHFDIMAEILNQFPLTYVNSVnsigNGLFIDPEAESVVIKPKdgFGGIGGAYIKPTALANV 232
Cdd:TIGR01037 153 KDKTDVPVFAKLSPNVtDITEIAKAAEEAGADGLTLINTL----RGMKIDIKTGKPILANK--TGGLSGPAIKPIALRMV 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2098351 233 RAFYTRLkpEIQIIGTGGIETGQDAFEHLLCGATMLQIGTALHKEgPAIFDRIIKELEEIMNQKGYQSIADFHG 306
Cdd:TIGR01037 227 YDVYKMV--DIPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYR-GFAFKKIIEGLIAFLKAEGFTSIEELIG 297
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
46-289 |
1.95e-27 |
|
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: 108.74 E-value: 1.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 46 TLEKREGNPLPRYVDL--ELGSINSMGLPNLGfdyyLDYVLKN-QKENAQEGPIFFSIA------GMSAAEN-IAMLKKI 115
Cdd:cd04738 82 TPRPQPGNPKPRLFRLpeDEALINRMGFNNDG----ADAVAKRlKKRRPRGGPLGVNIGknkdtpLEDAVEDyVIGVRKL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 116 qeSDFSGITELNLSCPNVPGKPQLAYDfEATEKLLKEVFTFFT-----KPLGVKLPPyfDLVHFDI--MAEILNQFPLty 188
Cdd:cd04738 158 --GPYADYLVVNVSSPNTPGLRDLQGK-EALRELLTAVKEERNklgkkVPLLVKIAP--DLSDEELedIADVALEHGV-- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 189 vnsvnsigNGLF-----IDPEaESVVIKPKDGFGGIGGAYIKPTALANVRAFYTRLKPEIQIIGTGGIETGQDAFEHLLC 263
Cdd:cd04738 231 --------DGIIatnttISRP-GLLRSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRA 301
|
250 260
....*....|....*....|....*.
gi 2098351 264 GATMLQIGTALHKEGPAIFDRIIKEL 289
Cdd:cd04738 302 GASLVQLYTGLVYEGPGLVKRIKREL 327
|
|
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
2-289 |
7.87e-27 |
|
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: 106.60 E-value: 7.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 2 LNTTFANAKFANPFMNASGVHCMTIEDLEelKASQAG--AYITKSSTLEKRE-GNPLPRYVDLELGSINSMGLPNLGF-- 76
Cdd:cd02940 2 LSVTFCGIKFPNPFGLASAPPTTSYPMIR--RAFEAGwgGAVTKTLGLDKDIvTNVSPRIARLRTSGRGQIGFNNIELis 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 77 DYYLDYVLKNQKENAQEGP---IFFSIAGM-SAAENIAMLKKIQESDFSGItELNLSCPNvpGKPQLAY------DFEAT 146
Cdd:cd02940 80 EKPLEYWLKEIRELKKDFPdkiLIASIMCEyNKEDWTELAKLVEEAGADAL-ELNFSCPH--GMPERGMgaavgqDPELV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 147 EKLLKEVFTFFTKPLGVKLPP-YFDLVHFDIMAEILNQFPLTYVNSVNSIgNGLFIDPEAESVVIKPKDGFGGIGGAYIK 225
Cdd:cd02940 157 EEICRWVREAVKIPVIAKLTPnITDIREIARAAKEGGADGVSAINTVNSL-MGVDLDGTPPAPGVEGKTTYGGYSGPAVK 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2098351 226 PTALANVRAFYTRLKPEIQIIGTGGIETGQDAFEHLLCGATMLQIGTALHKEGPAIFDRIIKEL 289
Cdd:cd02940 236 PIALRAVSQIARAPEPGLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
52-297 |
1.90e-22 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 95.61 E-value: 1.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 52 GNPLP---RYVDLElGSINSMGLPNLGfdyyLDYVLKNQKENAQEGPIFFSIaGMS-------AAEN-IAMLKKIqeSDF 120
Cdd:PRK05286 98 GNPKPrlfRLPEDE-ALINRMGFNNDG----ADALAERLKKAYRGIPLGINI-GKNkdtpledAVDDyLICLEKL--YPY 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 121 SGITELNLSCPNVPGKPQLAYDfEATEKLLKEV-----FTFFTKPLGVKLPPYFDLVHFDIMAEILNQFPLtyvnsvnsi 195
Cdd:PRK05286 170 ADYFTVNISSPNTPGLRDLQYG-EALDELLAALkeaqaELHGYVPLLVKIAPDLSDEELDDIADLALEHGI--------- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 196 gNGLF-----ID-PEAESvvIKPKDGFGGIGGAYIKPTALANVRAFYTRLKPEIQIIGTGGIETGQDAFEHLLCGATMLQ 269
Cdd:PRK05286 240 -DGVIatnttLSrDGLKG--LPNADEAGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGASLVQ 316
|
250 260
....*....|....*....|....*...
gi 2098351 270 IGTALHKEGPAIFDRIIKELEEIMNQKG 297
Cdd:PRK05286 317 IYSGLIYEGPGLVKEIVRGLARLLRRDG 344
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
2-307 |
6.20e-20 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 89.23 E-value: 6.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 2 LNTTFANAKFANPFMNASGVHCMTIEDLEelKASQAG--AYITKssTLekreGNPLPRYVDLELGSINSMGLPNLGF--- 76
Cdd:PRK08318 4 LSITFCGIKSPNPFWLASAPPTNKYYNVA--RAFEAGwgGVVWK--TL----GPPIVNVSSPRFGALVKEDRRFIGFnni 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 77 ----DYYLDYVLKNQKENAQEGP---IFFSIAGMSAAEN-IAMLKKIQESDFSGItELNLSCP-------------NVPg 135
Cdd:PRK08318 76 elitDRPLEVNLREIRRVKRDYPdraLIASIMVECNEEEwKEIAPLVEETGADGI-ELNFGCPhgmsergmgsavgQVP- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 136 kpqlaydfEATEKLLKEVFTFFTKPLGVKLPPYF-DLVHFDIMAEILNQFPLTYVNSVNSIgNGLFIDPEAESVVIKPKD 214
Cdd:PRK08318 154 --------ELVEMYTRWVKRGSRLPVIVKLTPNItDIREPARAAKRGGADAVSLINTINSI-TGVDLDRMIPMPIVNGKS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 215 GFGGIGGAYIKPTALANVRAFYTRLK-PEIQIIGTGGIETGQDAFEHLLCGATMLQIGTALHKEGPAIFDRIIKELEEIM 293
Cdd:PRK08318 225 SHGGYCGPAVKPIALNMVAEIARDPEtRGLPISGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISGLSHYM 304
|
330
....*....|....
gi 2098351 294 NQKGYQSIADFHGK 307
Cdd:PRK08318 305 DEKGFASLEDMVGL 318
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
15-272 |
4.13e-19 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 83.40 E-value: 4.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 15 FMNASGVHC---MTIEDLEELKASQAGAYITKSSTLEKREGNPLPRyvdlelgsinsmglpnlgfdyyldyVLKNQKENA 91
Cdd:cd04722 1 VILALLAGGpsgDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDK-------------------------EVLKEVAAE 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 92 QEGPIFFSIAGMSAAENIAMLKKIQESDFSGITELNLSCPnvpgkpqlaYDFEATEKLLKEVFT-FFTKPLGVKLPPYFD 170
Cdd:cd04722 56 TDLPLGVQLAINDAAAAVDIAAAAARAAGADGVEIHGAVG---------YLAREDLELIRELREaVPDVKVVVKLSPTGE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 171 LVhfdimAEILNQFPLTYVNSVNSIGNGLFIDPEAESVVIKPKdgfggiggayikptalanvrafyTRLKPEIQIIGTGG 250
Cdd:cd04722 127 LA-----AAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLIL-----------------------AKRGSKVPVIAGGG 178
|
250 260
....*....|....*....|..
gi 2098351 251 IETGQDAFEHLLCGATMLQIGT 272
Cdd:cd04722 179 INDPEDAAEALALGADGVIVGS 200
|
|
| DHOD_like |
cd04739 |
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
2-308 |
1.57e-18 |
|
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: 84.20 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 2 LNTTFANAKFANPFMNASGVHCMTIEDLEELKASQAGAYITKSSTLEK--REGNPLPRYVDLELGSINSMG-LP-----N 73
Cdd:cd04739 2 LSTTYLGLSLKNPLVASASPLSRNLDNIRRLEDAGAGAIVLPSLFEEQieREAQELDRFLTYGSSFAEALSyFPeygryN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 74 LGFDYYLDYVLKNQKEnaQEGPIFFSIAGMSAAENIAMLKKIQESDFSGItELNLScpNVPGKPQLAY-DFEATE-KLLK 151
Cdd:cd04739 82 LGPEEYLELIRRAKRA--VSIPVIASLNGVSAGGWVDYARQIEEAGADAL-ELNIY--ALPTDPDISGaEVEQRYlDILR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 152 EVFTFFTKPLGVKLPPYFDlvhfdIMAEILNQFPLTYVNSVNsigngLF-------IDPEAESVVikPKDGFGGIGGAYI 224
Cdd:cd04739 157 AVKSAVTIPVAVKLSPFFS-----ALAHMAKQLDAAGADGLV-----LFnrfyqpdIDLETLEVV--PNLLLSSPAEIRL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 225 KPTALANVRAfytrlKPEIQIIGTGGIETGQDAFEHLLCGATMLQIGTALHKEGPAIFDRIIKELEEIMNQKGYQSIADF 304
Cdd:cd04739 225 PLRWIAILSG-----RVKASLAASGGVHDAEDVVKYLLAGADVVMTTSALLRHGPDYIGTLLAGLEAWMEEHGYESVQQL 299
|
....
gi 2098351 305 HGKL 308
Cdd:cd04739 300 RGSM 303
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
44-303 |
2.39e-18 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 84.79 E-value: 2.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 44 SSTLEKREGNPLPRYVDL--ELGSINSMGLPNLGFD----YYLDYVLKNQKENAQEGPIFFSIAGMSAAE-------NIA 110
Cdd:PLN02826 115 SVTPLPQPGNPKPRVFRLreEGAIINRYGFNSEGIVavakRLGAQHGKRKLDETSSSSFSSDDVKAGGKAgpgilgvNLG 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 111 MLKKIQES--DF-SGITEL---------NLSCPNVPG------KPQLAYDFEATEKLLKEVFTFFTK--PLGVKLPPyfD 170
Cdd:PLN02826 195 KNKTSEDAaaDYvQGVRALsqyadylviNVSSPNTPGlrklqgRKQLKDLLKKVLAARDEMQWGEEGppPLLVKIAP--D 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 171 LVHFDI-----MAEILNQFPLTYVNSVNSIGNGLFIDPEAESVvikpkdgfGGIGGAYIKPTALANVRAFYTRLKPEIQI 245
Cdd:PLN02826 273 LSKEDLediaaVALALGIDGLIISNTTISRPDSVLGHPHADEA--------GGLSGKPLFDLSTEVLREMYRLTRGKIPL 344
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2098351 246 IGTGGIETGQDAFEHLLCGATMLQIGTALHKEGPAIFDRIIKELEEIMNQKGYQSIAD 303
Cdd:PLN02826 345 VGCGGVSSGEDAYKKIRAGASLVQLYTAFAYEGPALIPRIKAELAACLERDGFKSIQE 402
|
|
| PRK07565 |
PRK07565 |
dihydroorotate dehydrogenase-like protein; |
2-308 |
4.80e-17 |
|
dihydroorotate dehydrogenase-like protein;
Pssm-ID: 236051 Cd Length: 334 Bit Score: 80.30 E-value: 4.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 2 LNTTFANAKFANPFMNASGVHCMTIEDLEELKASQAGAYITKS-----STLEKRE-GNPLPRYVDL---ELGSINSMGLP 72
Cdd:PRK07565 3 LSTTYLGLTLRNPLVASASPLSESVDNVKRLEDAGAGAVVLKSlfeeqIRHEAAElDRHLTHGTESfaeALDYFPEPAKF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 73 NLGFDYYLDYVlkNQKENAQEGPIFFSIAGMSAAENIAMLKKIQESDFSGItELNLScpNVPGKPQLAY-DFEATE-KLL 150
Cdd:PRK07565 83 YVGPEEYLELI--RRAKEAVDIPVIASLNGSSAGGWVDYARQIEQAGADAL-ELNIY--YLPTDPDISGaEVEQRYlDIL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 151 KEVFTFFTKPLGVKLPPYFDlvhfdIMAEILNQFPLTYVNSVNsigngLF-------IDPEAESVVikPKDGFGGIGGAY 223
Cdd:PRK07565 158 RAVKSAVSIPVAVKLSPYFS-----NLANMAKRLDAAGADGLV-----LFnrfyqpdIDLETLEVV--PGLVLSTPAELR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 224 IKPTALANVRAfytRLKpeIQIIGTGGIETGQDAFEHLLCGATMLQIGTALHKEGPAIFDRIIKELEEIMNQKGYQSIAD 303
Cdd:PRK07565 226 LPLRWIAILSG---RVG--ADLAATTGVHDAEDVIKMLLAGADVVMIASALLRHGPDYIGTILRGLEDWMERHGYESLQQ 300
|
....*
gi 2098351 304 FHGKL 308
Cdd:PRK07565 301 FRGSM 305
|
|
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
2-307 |
7.27e-16 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 77.19 E-value: 7.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 2 LNTTFANAKFANPFMNASGVHCMTIEDLEELKASQAGAYITKSSTLEKREG-NPLPRYVDLELGSINSMGLPNLGF---- 76
Cdd:PLN02495 11 LSVTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGGVIAKTVSLDASKViNVTPRYARLRAGANGSAKGRVIGWqnie 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 77 ---DYYLDYVLKNQKENAQEGPIFFSIAG-MSAAENIAMLKKIQESDFSGIT--ELNLSCPNvpGKPQ------LAYDFE 144
Cdd:PLN02495 91 lisDRPFETMLAEFKQLKEEYPDRILIASiMEEYNKDAWEEIIERVEETGVDalEINFSCPH--GMPErkmgaaVGQDCD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 145 ATEKLLKEVFTFFTKPLGVKLPPYFDlvhfDIM--AEILNQFPLTYVNSVNSIGNGLFID-----PEAesvvikPKDGFG 217
Cdd:PLN02495 169 LLEEVCGWINAKATVPVWAKMTPNIT----DITqpARVALKSGCEGVAAINTIMSVMGINldtlrPEP------CVEGYS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 218 GIGG---AYIKPTALANVRAFYTRLKPE----IQIIGTGGIETGQDAFEHLLCGATMLQIGTALHKEGPAIFDRIIKELE 290
Cdd:PLN02495 239 TPGGyssKAVRPIALAKVMAIAKMMKSEfpedRSLSGIGGVETGGDAAEFILLGADTVQVCTGVMMHGYPLVKNLCAELQ 318
|
330
....*....|....*..
gi 2098351 291 EIMNQKGYQSIADFHGK 307
Cdd:PLN02495 319 DFMKKHNFSSIEDFRGA 335
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
228-303 |
2.65e-04 |
|
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only]; FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440915 [Multi-domain] Cd Length: 357 Bit Score: 42.04 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098351 228 ALANVRAfytRLKPEIQIIGTGGIETGQDAFEHLLCGATMLQIG----TALHKEGPA----IFDRIIKELEEIMNQKGYQ 299
Cdd:COG1304 269 ALPEIRA---AVGGRIPVIADGGIRRGLDVAKALALGADAVGLGrpflYGLAAGGEAgvarVLELLRAELRRAMALTGCR 345
|
....
gi 2098351 300 SIAD 303
Cdd:COG1304 346 SLAE 349
|
|
| |
