|
Name |
Accession |
Description |
Interval |
E-value |
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
4-314 |
0e+00 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 583.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 4 SLTTKFLNNTYENPFMNASGVHCMTTQELDELANSKAGAFITKSATTLEREGNPEPRYISVPLGSINSMGLPNEGIDYYL 83
Cdd:PRK02506 1 STSTQIAGFKFDNCLMNAAGVYCMTKEELEEVEASAAGAFVTKSATLEPRPGNPEPRYADTPLGSINSMGLPNLGFDYYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 84 SYVLNRQKNYPDAPaIFFSVAGMSIDENLNLLRKIQDSEFNGITELNLSCPNVPGKPQVAYDFDLTKETLEKVFAFFKKP 163
Cdd:PRK02506 81 DYVLELQKKGPNKP-HFLSVVGLSPEETHTILKKIQASDFNGLVELNLSCPNVPGKPQIAYDFETTEQILEEVFTYFTKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 164 LGVKLPPYFDFAHFDIMAKILNEFPLAYVNSINSIGNGLFIDVEKESVVVKPKNGFGGIGGEYVKPTALANVRAFYTRLR 243
Cdd:PRK02506 160 LGVKLPPYFDIVHFDQAAAIFNKFPLAFVNCINSIGNGLVIDPEDETVVIKPKNGFGGIGGDYIKPTALANVRAFYQRLN 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2480389716 244 PEIKVIGTGGIKSGKDAFEHLLCGASMLQIGTELQKEGVKIFERIEKELKDIMEAKGYTSIDQFRGKLNSI 314
Cdd:PRK02506 240 PSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAIMAEKGYQSLEDFRGKLKYL 310
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
7-296 |
6.94e-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: 480.67 E-value: 6.94e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 7 TKFLNNTYENPFMNASGVHCMTTQELDELANSKAGAFITKSATTLEREGNPEPRYISVPLGSINSMGLPNEGIDYYLSYV 86
Cdd:cd04741 1 VTPPGLTISPPLMNAAGPWCTTLEDLLELAASSTGAVTTRSSTLAGRPGNPEPRYYAFPLGSINSLGLPNLGLDYYLEYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 87 LNRQKNYP-DAPAIFFSVAGMsIDENLNLLRKIQDS--EFNGITELNLSCPNVPGKPQVAYDFDLTKETLEKVFAFFKKP 163
Cdd:cd04741 81 RTISDGLPgSAKPFFISVTGS-AEDIAAMYKKIAAHqkQFPLAMELNLSCPNVPGKPPPAYDFDATLEYLTAVKAAYSIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 164 LGVKLPPYFDFAHFDIMAKILNEF--PLAYVNSINSIGNGLFIDVEKESVVVKPKNGFGGIGGEYVKPTALANVRAFYTR 241
Cdd:cd04741 160 VGVKTPPYTDPAQFDTLAEALNAFacPISFITATNTLGNGLVLDPERETVVLKPKTGFGGLAGAYLHPLALGNVRTFRRL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2480389716 242 LRPEIKVIGTGGIKSGKDAFEHLLCGASMLQIGTELQKEGVKIFERIEKELKDIM 296
Cdd:cd04741 240 LPSEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEKELEDIW 294
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
4-296 |
6.25e-143 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 404.42 E-value: 6.25e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 4 SLTTKFLNNTYENPFMNASGVHCMTTQELDELANSKAGAFITKSATTLEREGNPEPRYISVPLGSINSMGLPNEGIDYYL 83
Cdd:pfam01180 1 MLATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVTPYPQPGNPTPRVFRLPEGVLNRMGLNNPGLDAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 84 SYVLNRQKNYPD-APAIFFSVAGMSIDENLNLLRKIQdsEFNGITELNLSCPNVPGKPQVAYDFDLTKETLEKVFAFFKK 162
Cdd:pfam01180 81 AELLKRRKEYPRpDLGINLSKAGMTVDDYVEVARKIG--PFADYIELNVSCPNTPGLRALQTDPELAAILLKVVKEVSKV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 163 PLGVKLPP-YFDFAHFDIMAKILNEFPLAYVNSINSIGNGLFIDVEKESVVVKPknGFGGIGGEYVKPTALANVRAFYTR 241
Cdd:pfam01180 159 PVLVKLAPdLTDIVIIDIADVALGEDGLDGINATNTTVRGMRIDLKTEKPILAN--GTGGLSGPPIKPIALKVIRELYQR 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2480389716 242 LRPEIKVIGTGGIKSGKDAFEHLLCGASMLQIGTELQKEGVKIFERIEKELKDIM 296
Cdd:pfam01180 237 TGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
4-305 |
4.64e-95 |
|
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: 283.12 E-value: 4.64e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 4 SLTTKFLNNTYENPFMNASGVHCMTTQELDELANSKAGAFITKSATTLEREGNPEPRYISVPL--GSINSMGLPNEGIDY 81
Cdd:COG0167 1 DLSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEdsGLINRMGLNNPGVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 82 YLSYVLNRQKnyPDAPaIFFSVAGMSIDENLNLLRKIQDSEFNGItELNLSCPNVPGK-PQVAYDFDLTKETLEKVFAFF 160
Cdd:COG0167 81 FLERLLPAKR--YDVP-VIVNIGGNTVEDYVELARRLADAGADYL-ELNISCPNTPGGgRALGQDPEALAELLAAVKAAT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 161 KKPLGVKLPPyfDFAHFDIMAKILNEFPLAYVNSINSIgNGLFIDVEKESVVVKpkNGFGGIGGEYVKPTALANVRAFYT 240
Cdd:COG0167 157 DKPVLVKLAP--DLTDIVEIARAAEEAGADGVIAINTT-LGRAIDLETRRPVLA--NEAGGLSGPALKPIALRMVREVAQ 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2480389716 241 RLRPEIKVIGTGGIKSGKDAFEHLLCGASMLQIGTELQKEGVKIFERIEKELKDIMEAKGYTSID 305
Cdd:COG0167 232 AVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSIS 296
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
5-309 |
1.99e-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: 169.15 E-value: 1.99e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 5 LTTKFLNNTYENPFMNASGVHCMTTQELDELANSKAGAFITKSATTLEREGNPEPRYISVPLGSINSMGLPNEGIDYYLS 84
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTIVETPCGMLNAIGLQNPGVEAFLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 85 YVLNRQKNYPdaPAIFFSVAGMSIDENLNLLRKIQDS-EFNGITELNLSCPNVPG-------KPQVAYdfDLTKETLEKV 156
Cdd:TIGR01037 81 ELKPVREEFP--TPLIASVYGSSVEEFAEVAEKLEKApPYVDAYELNLSCPHVKGggiaigqDPELSA--DVVKAVKDKT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 157 faffKKPLGVKLPPyfdfAHFDI--MAKILNEFPLAYVNSINSIGnGLFIDVEKEsvvvKP--KNGFGGIGGEYVKPTAL 232
Cdd:TIGR01037 157 ----DVPVFAKLSP----NVTDIteIAKAAEEAGADGLTLINTLR-GMKIDIKTG----KPilANKTGGLSGPAIKPIAL 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2480389716 233 ANVRAFYTRLrpEIKVIGTGGIKSGKDAFEHLLCGASMLQIGTELQKEGvKIFERIEKELKDIMEAKGYTSIDQFRG 309
Cdd:TIGR01037 224 RMVYDVYKMV--DIPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYRG-FAFKKIIEGLIAFLKAEGFTSIEELIG 297
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
4-314 |
0e+00 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 583.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 4 SLTTKFLNNTYENPFMNASGVHCMTTQELDELANSKAGAFITKSATTLEREGNPEPRYISVPLGSINSMGLPNEGIDYYL 83
Cdd:PRK02506 1 STSTQIAGFKFDNCLMNAAGVYCMTKEELEEVEASAAGAFVTKSATLEPRPGNPEPRYADTPLGSINSMGLPNLGFDYYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 84 SYVLNRQKNYPDAPaIFFSVAGMSIDENLNLLRKIQDSEFNGITELNLSCPNVPGKPQVAYDFDLTKETLEKVFAFFKKP 163
Cdd:PRK02506 81 DYVLELQKKGPNKP-HFLSVVGLSPEETHTILKKIQASDFNGLVELNLSCPNVPGKPQIAYDFETTEQILEEVFTYFTKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 164 LGVKLPPYFDFAHFDIMAKILNEFPLAYVNSINSIGNGLFIDVEKESVVVKPKNGFGGIGGEYVKPTALANVRAFYTRLR 243
Cdd:PRK02506 160 LGVKLPPYFDIVHFDQAAAIFNKFPLAFVNCINSIGNGLVIDPEDETVVIKPKNGFGGIGGDYIKPTALANVRAFYQRLN 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2480389716 244 PEIKVIGTGGIKSGKDAFEHLLCGASMLQIGTELQKEGVKIFERIEKELKDIMEAKGYTSIDQFRGKLNSI 314
Cdd:PRK02506 240 PSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAIMAEKGYQSLEDFRGKLKYL 310
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
7-296 |
6.94e-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: 480.67 E-value: 6.94e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 7 TKFLNNTYENPFMNASGVHCMTTQELDELANSKAGAFITKSATTLEREGNPEPRYISVPLGSINSMGLPNEGIDYYLSYV 86
Cdd:cd04741 1 VTPPGLTISPPLMNAAGPWCTTLEDLLELAASSTGAVTTRSSTLAGRPGNPEPRYYAFPLGSINSLGLPNLGLDYYLEYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 87 LNRQKNYP-DAPAIFFSVAGMsIDENLNLLRKIQDS--EFNGITELNLSCPNVPGKPQVAYDFDLTKETLEKVFAFFKKP 163
Cdd:cd04741 81 RTISDGLPgSAKPFFISVTGS-AEDIAAMYKKIAAHqkQFPLAMELNLSCPNVPGKPPPAYDFDATLEYLTAVKAAYSIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 164 LGVKLPPYFDFAHFDIMAKILNEF--PLAYVNSINSIGNGLFIDVEKESVVVKPKNGFGGIGGEYVKPTALANVRAFYTR 241
Cdd:cd04741 160 VGVKTPPYTDPAQFDTLAEALNAFacPISFITATNTLGNGLVLDPERETVVLKPKTGFGGLAGAYLHPLALGNVRTFRRL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2480389716 242 LRPEIKVIGTGGIKSGKDAFEHLLCGASMLQIGTELQKEGVKIFERIEKELKDIM 296
Cdd:cd04741 240 LPSEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEKELEDIW 294
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
4-296 |
6.25e-143 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 404.42 E-value: 6.25e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 4 SLTTKFLNNTYENPFMNASGVHCMTTQELDELANSKAGAFITKSATTLEREGNPEPRYISVPLGSINSMGLPNEGIDYYL 83
Cdd:pfam01180 1 MLATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVTPYPQPGNPTPRVFRLPEGVLNRMGLNNPGLDAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 84 SYVLNRQKNYPD-APAIFFSVAGMSIDENLNLLRKIQdsEFNGITELNLSCPNVPGKPQVAYDFDLTKETLEKVFAFFKK 162
Cdd:pfam01180 81 AELLKRRKEYPRpDLGINLSKAGMTVDDYVEVARKIG--PFADYIELNVSCPNTPGLRALQTDPELAAILLKVVKEVSKV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 163 PLGVKLPP-YFDFAHFDIMAKILNEFPLAYVNSINSIGNGLFIDVEKESVVVKPknGFGGIGGEYVKPTALANVRAFYTR 241
Cdd:pfam01180 159 PVLVKLAPdLTDIVIIDIADVALGEDGLDGINATNTTVRGMRIDLKTEKPILAN--GTGGLSGPPIKPIALKVIRELYQR 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2480389716 242 LRPEIKVIGTGGIKSGKDAFEHLLCGASMLQIGTELQKEGVKIFERIEKELKDIM 296
Cdd:pfam01180 237 TGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
7-291 |
7.42e-98 |
|
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: 290.02 E-value: 7.42e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 7 TKFLNNTYENPFMNASGVHCMTTQELDELANSKAGAFITKSATTLEREGNPEPRY---------ISVPLGSINSMGLPNE 77
Cdd:cd02810 1 VNFLGLKLKNPFGVAAGPLLKTGELIARAAAAGFGAVVYKTVTLHPRPGNPLPRVarlppegesYPEQLGILNSFGLPNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 78 GIDYYLSYVLNRQKNYPDAPaIFFSVAGMSIDENLNLLRKIQDSeFNGITELNLSCPNVPGKPQVAYDFDLTKETLEKVF 157
Cdd:cd02810 81 GLDVWLQDIAKAKKEFPGQP-LIASVGGSSKEDYVELARKIERA-GAKALELNLSCPNVGGGRQLGQDPEAVANLLKAVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 158 AFFKKPLGVKLPPYFDFAHFDIMAKILNEFPLAYVNSINSIGNGLFIDVEkesVVVKPKNGFGGIGGEYVKPTALANVRA 237
Cdd:cd02810 159 AAVDIPLLVKLSPYFDLEDIVELAKAAERAGADGLTAINTISGRVVDLKT---VGPGPKRGTGGLSGAPIRPLALRWVAR 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2480389716 238 FYTRLRPEIKVIGTGGIKSGKDAFEHLLCGASMLQIGTELQKEGVKIFERIEKE 291
Cdd:cd02810 236 LAARLQLDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKIKKE 289
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
4-305 |
4.64e-95 |
|
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: 283.12 E-value: 4.64e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 4 SLTTKFLNNTYENPFMNASGVHCMTTQELDELANSKAGAFITKSATTLEREGNPEPRYISVPL--GSINSMGLPNEGIDY 81
Cdd:COG0167 1 DLSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEdsGLINRMGLNNPGVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 82 YLSYVLNRQKnyPDAPaIFFSVAGMSIDENLNLLRKIQDSEFNGItELNLSCPNVPGK-PQVAYDFDLTKETLEKVFAFF 160
Cdd:COG0167 81 FLERLLPAKR--YDVP-VIVNIGGNTVEDYVELARRLADAGADYL-ELNISCPNTPGGgRALGQDPEALAELLAAVKAAT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 161 KKPLGVKLPPyfDFAHFDIMAKILNEFPLAYVNSINSIgNGLFIDVEKESVVVKpkNGFGGIGGEYVKPTALANVRAFYT 240
Cdd:COG0167 157 DKPVLVKLAP--DLTDIVEIARAAEEAGADGVIAINTT-LGRAIDLETRRPVLA--NEAGGLSGPALKPIALRMVREVAQ 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2480389716 241 RLRPEIKVIGTGGIKSGKDAFEHLLCGASMLQIGTELQKEGVKIFERIEKELKDIMEAKGYTSID 305
Cdd:COG0167 232 AVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSIS 296
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
7-311 |
4.20e-61 |
|
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: 196.23 E-value: 4.20e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 7 TKFLNNTYENPFMNASGVhCMTTQELDELAN-SKAGAFITKSATTLEREGNPEPRYISVPLGSINSMGLPNEGIDYYLSY 85
Cdd:cd04740 2 VELAGLRLKNPVILASGT-FGFGEELSRVADlGKLGAIVTKSITLEPREGNPPPRVVETPGGMLNAIGLQNPGVEAFLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 86 VLNrQKNYPDAPAIfFSVAGMSIDENLNLLRKIQDSEFNGItELNLSCPNVP-GKPQVAYDFDLTKETLEKVFAFFKKPL 164
Cdd:cd04740 81 LLP-WLREFGTPVI-ASIAGSTVEEFVEVAEKLADAGADAI-ELNISCPNVKgGGMAFGTDPEAVAEIVKAVKKATDVPV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 165 GVKLPPYFDfahfDI--MAKILNEfplAYVNS---INSIGnGLFIDVEKEsvvvKP--KNGFGGIGGEYVKPTALANVRA 237
Cdd:cd04740 158 IVKLTPNVT----DIveIARAAEE---AGADGltlINTLK-GMAIDIETR----KPilGNVTGGLSGPAIKPIALRMVYQ 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2480389716 238 FYTRLrpEIKVIGTGGIKSGKDAFEHLLCGASMLQIGTELqKEGVKIFERIEKELKDIMEAKGYTSIDQFRGKL 311
Cdd:cd04740 226 VYKAV--EIPIIGVGGIASGEDALEFLMAGASAVQVGTAN-FVDPEAFKEIIEGLEAYLDEEGIKSIEELVGLA 296
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
5-311 |
3.05e-57 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 186.51 E-value: 3.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 5 LTTKFLNNTYENPFMNASGVHCMTTQELDELANSKAGAFITKSATTLEREGNPEPRYISVPLGSINSMGLPNEGIDYYLS 84
Cdd:PRK07259 2 LSVELPGLKLKNPVMPASGTFGFGGEYARFYDLNGLGAIVTKSTTLEPREGNPTPRIAETPGGMLNAIGLQNPGVDAFIE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 85 YVLNRQKNYpDAPAIfFSVAGMSIDENLNLLRKIQDSEFNGITELNLSCPNVPG-------KPQVAYdfDLTKETLEKVf 157
Cdd:PRK07259 82 EELPWLEEF-DTPII-ANVAGSTEEEYAEVAEKLSKAPNVDAIELNISCPNVKHggmafgtDPELAY--EVVKAVKEVV- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 158 affKKPLGVKLPPYFDfahfDI--MAKILNEFPLAYVNSINSIgNGLFIDVEKEsvvvKP--KNGFGGIGGEYVKPTALA 233
Cdd:PRK07259 157 ---KVPVIVKLTPNVT----DIveIAKAAEEAGADGLSLINTL-KGMAIDIKTR----KPilANVTGGLSGPAIKPIALR 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2480389716 234 NVRAFYTRLRpeIKVIGTGGIKSGKDAFEHLLCGASMLQIGTELQKeGVKIFERIEKELKDIMEAKGYTSIDQFRGKL 311
Cdd:PRK07259 225 MVYQVYQAVD--IPIIGMGGISSAEDAIEFIMAGASAVQVGTANFY-DPYAFPKIIEGLEAYLDKYGIKSIEEIVGIA 299
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
5-309 |
1.99e-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: 169.15 E-value: 1.99e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 5 LTTKFLNNTYENPFMNASGVHCMTTQELDELANSKAGAFITKSATTLEREGNPEPRYISVPLGSINSMGLPNEGIDYYLS 84
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTIVETPCGMLNAIGLQNPGVEAFLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 85 YVLNRQKNYPdaPAIFFSVAGMSIDENLNLLRKIQDS-EFNGITELNLSCPNVPG-------KPQVAYdfDLTKETLEKV 156
Cdd:TIGR01037 81 ELKPVREEFP--TPLIASVYGSSVEEFAEVAEKLEKApPYVDAYELNLSCPHVKGggiaigqDPELSA--DVVKAVKDKT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 157 faffKKPLGVKLPPyfdfAHFDI--MAKILNEFPLAYVNSINSIGnGLFIDVEKEsvvvKP--KNGFGGIGGEYVKPTAL 232
Cdd:TIGR01037 157 ----DVPVFAKLSP----NVTDIteIAKAAEEAGADGLTLINTLR-GMKIDIKTG----KPilANKTGGLSGPAIKPIAL 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2480389716 233 ANVRAFYTRLrpEIKVIGTGGIKSGKDAFEHLLCGASMLQIGTELQKEGvKIFERIEKELKDIMEAKGYTSIDQFRG 309
Cdd:TIGR01037 224 RMVYDVYKMV--DIPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYRG-FAFKKIIEGLIAFLKAEGFTSIEELIG 297
|
|
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
5-292 |
3.81e-26 |
|
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: 105.06 E-value: 3.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 5 LTTKFLNNTYENPFMNASGVhcmTTQELDELANS-KAG--AFITKsatTLEREG----NPEPRYISVPLGSINSMGLPN- 76
Cdd:cd02940 2 LSVTFCGIKFPNPFGLASAP---PTTSYPMIRRAfEAGwgGAVTK---TLGLDKdivtNVSPRIARLRTSGRGQIGFNNi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 77 EGI-----DYYLSYVLNRQKNYPDAPAIFFSVAGMSIDENLNLLRKIQDSEFNGItELNLSCPNvpGKPQ------VAYD 145
Cdd:cd02940 76 ELIsekplEYWLKEIRELKKDFPDKILIASIMCEYNKEDWTELAKLVEEAGADAL-ELNFSCPH--GMPErgmgaaVGQD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 146 FDLTKETLEKVFAFFKKPLGVKLPPyfDFAHFDIMAKILNEFPLAYVNSINSIgNGLF-IDVEKES--VVVKPKNGFGGI 222
Cdd:cd02940 153 PELVEEICRWVREAVKIPVIAKLTP--NITDIREIARAAKEGGADGVSAINTV-NSLMgVDLDGTPpaPGVEGKTTYGGY 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 223 GGEYVKPTALANVRAFYTRLRPEIKVIGTGGIKSGKDAFEHLLCGASMLQIGTELQKEGVKIFERIEKEL 292
Cdd:cd02940 230 SGPAVKPIALRAVSQIARAPEPGLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
47-292 |
6.75e-20 |
|
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: 88.32 E-value: 6.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 47 SATTLEREGNPEPRYISVP--LGSINSMGLPNEGIDYylsyVLNRQKNYPDAPAIFfsvaGMSIDEN------------L 112
Cdd:cd04738 80 TVTPRPQPGNPKPRLFRLPedEALINRMGFNNDGADA----VAKRLKKRRPRGGPL----GVNIGKNkdtpledavedyV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 113 NLLRKIQDseFNGITELNLSCPNVPG--KPQvaydfdlTKETLEKVFA---------FFKKPLGVKLPPYFDFAHFDIMA 181
Cdd:cd04738 152 IGVRKLGP--YADYLVVNVSSPNTPGlrDLQ-------GKEALRELLTavkeernklGKKVPLLVKIAPDLSDEELEDIA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 182 KILNEFPLAyvnsinsignGLFID---VEKESVVVKP-KNGFGGIGGEYVKPTALANVRAFYTRLRPEIKVIGTGGIKSG 257
Cdd:cd04738 223 DVALEHGVD----------GIIATnttISRPGLLRSPlANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSG 292
|
250 260 270
....*....|....*....|....*....|....*
gi 2480389716 258 KDAFEHLLCGASMLQIGTELQKEGVKIFERIEKEL 292
Cdd:cd04738 293 EDAYEKIRAGASLVQLYTGLVYEGPGLVKRIKREL 327
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
3-310 |
3.44e-17 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 81.53 E-value: 3.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 3 ASLTTKFLNNTYENPFMNASGVhcmTTQELDELANS-KAG--AFITKsatTLereGNP-----EPRYISVPLGSINSMGL 74
Cdd:PRK08318 2 ADLSITFCGIKSPNPFWLASAP---PTNKYYNVARAfEAGwgGVVWK---TL---GPPivnvsSPRFGALVKEDRRFIGF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 75 PN-EGI-----DYYLSYVLNRQKNYPDApAIFFSVAGMSIDEN-LNLLRKIQDSEFNGItELNLSCPNvpGKP------- 140
Cdd:PRK08318 73 NNiELItdrplEVNLREIRRVKRDYPDR-ALIASIMVECNEEEwKEIAPLVEETGADGI-ELNFGCPH--GMSergmgsa 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 141 --QVAydfDLTKETLEKVFAFFKKPLGVKLPPYF-DFAHFDIMAKILNEFPLAYVNSINSIgnglfIDVEKESVVVKP-- 215
Cdd:PRK08318 149 vgQVP---ELVEMYTRWVKRGSRLPVIVKLTPNItDIREPARAAKRGGADAVSLINTINSI-----TGVDLDRMIPMPiv 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 216 --KNGFGGIGGEYVKPTALANVRAFYTRlrPEIKVI---GTGGIKSGKDAFEHLLCGASMLQIGTELQKEGVKIFERIEK 290
Cdd:PRK08318 221 ngKSSHGGYCGPAVKPIALNMVAEIARD--PETRGLpisGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMIS 298
|
330 340
....*....|....*....|
gi 2480389716 291 ELKDIMEAKGYTSIDQFRGK 310
Cdd:PRK08318 299 GLSHYMDEKGFASLEDMVGL 318
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
47-306 |
8.97e-17 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 80.17 E-value: 8.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 47 SATTLEREGNPEPRYISVP--LGSINSMGLPNEGID-------------------YYLSYVLNRQKNYPDAPAIFfsvaG 105
Cdd:PLN02826 115 SVTPLPQPGNPKPRVFRLReeGAIINRYGFNSEGIVavakrlgaqhgkrkldetsSSSFSSDDVKAGGKAGPGIL----G 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 106 MSIDENLNLLRKIQD--------SEFNGITELNLSCPNVPG--KPQVAYDF-DLTKETL----EKVFAF-FKKPLGVKLP 169
Cdd:PLN02826 191 VNLGKNKTSEDAAADyvqgvralSQYADYLVINVSSPNTPGlrKLQGRKQLkDLLKKVLaardEMQWGEeGPPPLLVKIA 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 170 PyfDFAHFDI-----MAKILNEFPLAYVNSINSIGNGLFIDVEKESVvvkpkngfGGIGGEYVKPTALANVRAFYTRLRP 244
Cdd:PLN02826 271 P--DLSKEDLediaaVALALGIDGLIISNTTISRPDSVLGHPHADEA--------GGLSGKPLFDLSTEVLREMYRLTRG 340
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2480389716 245 EIKVIGTGGIKSGKDAFEHLLCGASMLQIGTELQKEGVKIFERIEKELKDIMEAKGYTSIDQ 306
Cdd:PLN02826 341 KIPLVGCGGVSSGEDAYKKIRAGASLVQLYTAFAYEGPALIPRIKAELAACLERDGFKSIQE 402
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
55-300 |
6.67e-16 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 77.12 E-value: 6.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 55 GNPEPRYISVPL--GSINSMGLPNEGIDYylsyVLNRQKNYPDAPAIffsvaGMSIDEN------------LNLLRKIqd 120
Cdd:PRK05286 98 GNPKPRLFRLPEdeALINRMGFNNDGADA----LAERLKKAYRGIPL-----GINIGKNkdtpledavddyLICLEKL-- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 121 SEFNGITELNLSCPNVPGKpqvaydFDL-TKETLEKVFA---------FFKKPLGVKLPPYFDFAHFDIMAKILNEFPLA 190
Cdd:PRK05286 167 YPYADYFTVNISSPNTPGL------RDLqYGEALDELLAalkeaqaelHGYVPLLVKIAPDLSDEELDDIADLALEHGID 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 191 yvnsinsignGLFI---DVEKESVV-VKPKNGFGGIGGEYVKPTALANVRAFYTRLRPEIKVIGTGGIKSGKDAFEHLLC 266
Cdd:PRK05286 241 ----------GVIAtntTLSRDGLKgLPNADEAGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRA 310
|
250 260 270
....*....|....*....|....*....|....
gi 2480389716 267 GASMLQIGTELQKEGVKIFERIEKELKDIMEAKG 300
Cdd:PRK05286 311 GASLVQIYSGLIYEGPGLVKEIVRGLARLLRRDG 344
|
|
| DHOD_like |
cd04739 |
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
5-312 |
2.50e-14 |
|
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: 72.26 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 5 LTTKFLNNTYENPFMNASGVHCMTTQELDELANSKAGAFITKS--ATTLEREGNPEPRYISVPLGSINSMGLPNEGIDY- 81
Cdd:cd04739 2 LSTTYLGLSLKNPLVASASPLSRNLDNIRRLEDAGAGAIVLPSlfEEQIEREAQELDRFLTYGSSFAEALSYFPEYGRYn 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 82 -----YLSYVlNRQKNYPDAPAIFfSVAGMSIDENLNLLRKIQDSEFNGItELNLScpnvpgkpQVAYDFDLTKETLEK- 155
Cdd:cd04739 82 lgpeeYLELI-RRAKRAVSIPVIA-SLNGVSAGGWVDYARQIEEAGADAL-ELNIY--------ALPTDPDISGAEVEQr 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 156 -------VFAFFKKPLGVKLPPYF-DFAHfdiMAKILNEfplAYVNSINsigngLF-------IDVEKESVVvkpkngfg 220
Cdd:cd04739 151 yldilraVKSAVTIPVAVKLSPFFsALAH---MAKQLDA---AGADGLV-----LFnrfyqpdIDLETLEVV-------- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 221 gIGGEYVKPTALANVRAFYTRLRPEIKV--IGTGGIKSGKDAFEHLLCGASMLQIGTELQKEGVKIFERIEKELKDIMEA 298
Cdd:cd04739 212 -PNLLLSSPAEIRLPLRWIAILSGRVKAslAASGGVHDAEDVVKYLLAGADVVMTTSALLRHGPDYIGTLLAGLEAWMEE 290
|
330
....*....|....
gi 2480389716 299 KGYTSIDQFRGKLN 312
Cdd:cd04739 291 HGYESVQQLRGSMS 304
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
77-275 |
4.05e-14 |
|
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: 69.92 E-value: 4.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 77 EGIDYYLSYVLNRQKNYPDAPaIFFSVAGMSIDENLNLLRKIQDSEFNGITELNLSCPnvpgkpqvaYDFDLTKETLEKV 156
Cdd:cd04722 39 EEAETDDKEVLKEVAAETDLP-LGVQLAINDAAAAVDIAAAAARAAGADGVEIHGAVG---------YLAREDLELIREL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 157 F-AFFKKPLGVKLPPYFDFAHFDimakiLNEFPLAYVNSINSIGNGLFIDVEKESVVVKPKNgfggiggeyvkptalanv 235
Cdd:cd04722 109 ReAVPDVKVVVKLSPTGELAAAA-----AEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILA------------------ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2480389716 236 rafytRLRPEIKVIGTGGIKSGKDAFEHLLCGASMLQIGT 275
Cdd:cd04722 166 -----KRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
47-292 |
9.35e-14 |
|
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: 70.58 E-value: 9.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 47 SATTLEREGNPEPRYISVP--LGSINSMGLPNEGIDYylsyVLNRQKNYPDAPAI-------FFSVAGMSIDENLNLLRK 117
Cdd:TIGR01036 87 TVTPKPQPGNPRPRLFRLIedEALINRMGFNNHGADV----LVERLKRARYKGPIginigknKDTPSEDAKEDYAACLRK 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 118 IQDseFNGITELNLSCPNVPGKPQVAYD------FDLTKETLEKVFAFFKKPLGVKLPPYFDFAHFDIMAKILNEFPLAY 191
Cdd:TIGR01036 163 LGP--LADYLVVNVSSPNTPGLRDLQYKaelrdlLTAVKQEQDGLRRVHRVPVLVKIAPDLTESDLEDIADSLVELGIDG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 192 VNSINSIgnglfIDvekESVVVKPKN--GFGGIGGEYVKPTALANVRAFYTRLRPEIKVIGTGGIKSGKDAFEHLLCGAS 269
Cdd:TIGR01036 241 VIATNTT-----VS---RSLVQGPKNsdETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGAS 312
|
250 260
....*....|....*....|...
gi 2480389716 270 MLQIGTELQKEGVKIFERIEKEL 292
Cdd:TIGR01036 313 LLQIYSGFIYWGPPLVKEIVKEI 335
|
|
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
16-310 |
4.76e-13 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 69.10 E-value: 4.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 16 NPFMNASGVHCMTTQELDELANSKAGAFITKSAT-TLEREGNPEPRYISVPLGSINS-----MGLPN-EGI-DYYLSYVL 87
Cdd:PLN02495 22 NPFVIGSGPPGTNYTVMKRAFDEGWGGVIAKTVSlDASKVINVTPRYARLRAGANGSakgrvIGWQNiELIsDRPFETML 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 88 NRQKN----YPDAPAIffsvagMSIDENLN------LLRKIQDSEFNGItELNLSCPNvpGKPQ------VAYDFDLTKE 151
Cdd:PLN02495 102 AEFKQlkeeYPDRILI------ASIMEEYNkdaweeIIERVEETGVDAL-EINFSCPH--GMPErkmgaaVGQDCDLLEE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 152 TLEKVFAFFKKPLGVKLPPYFDfahfDIM--AKILNEFPLAYVNSINSIGN--GLFIDVEKESVVVKPKNGFGGIGGEYV 227
Cdd:PLN02495 173 VCGWINAKATVPVWAKMTPNIT----DITqpARVALKSGCEGVAAINTIMSvmGINLDTLRPEPCVEGYSTPGGYSSKAV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 228 KPTALANVRAFYTRLRPE----IKVIGTGGIKSGKDAFEHLLCGASMLQIGTELQKEGVKIFERIEKELKDIMEAKGYTS 303
Cdd:PLN02495 249 RPIALAKVMAIAKMMKSEfpedRSLSGIGGVETGGDAAEFILLGADTVQVCTGVMMHGYPLVKNLCAELQDFMKKHNFSS 328
|
....*..
gi 2480389716 304 IDQFRGK 310
Cdd:PLN02495 329 IEDFRGA 335
|
|
| PRK07565 |
PRK07565 |
dihydroorotate dehydrogenase-like protein; |
5-312 |
1.14e-12 |
|
dihydroorotate dehydrogenase-like protein;
Pssm-ID: 236051 Cd Length: 334 Bit Score: 67.58 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 5 LTTKFLNNTYENPFMNASGVHCMTTQELDELANSKAGAFITKS---------------ATTLEREGNPEPR-YISVPLGS 68
Cdd:PRK07565 3 LSTTYLGLTLRNPLVASASPLSESVDNVKRLEDAGAGAVVLKSlfeeqirheaaeldrHLTHGTESFAEALdYFPEPAKF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 69 insmglpNEGIDYYLSyVLNRQKNYPDAPAIFfSVAGMSIDENLNLLRKIQDSEFNGItELNLScpNVPGKPQVAYD--- 145
Cdd:PRK07565 83 -------YVGPEEYLE-LIRRAKEAVDIPVIA-SLNGSSAGGWVDYARQIEQAGADAL-ELNIY--YLPTDPDISGAeve 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 146 ---FDLtketLEKVFAFFKKPLGVKLPPYF-DFAHfdiMAKILnefplaYVNSINSIGngLF-------IDVEKESVVvk 214
Cdd:PRK07565 151 qryLDI----LRAVKSAVSIPVAVKLSPYFsNLAN---MAKRL------DAAGADGLV--LFnrfyqpdIDLETLEVV-- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 215 pkngfggIGGEYVKPTALANVRAFYTRLRPEIKV--IGTGGIKSGKDAFEHLLCGASMLQIGTELQKEGVKIFERIEKEL 292
Cdd:PRK07565 214 -------PGLVLSTPAELRLPLRWIAILSGRVGAdlAATTGVHDAEDVIKMLLAGADVVMIASALLRHGPDYIGTILRGL 286
|
330 340
....*....|....*....|
gi 2480389716 293 KDIMEAKGYTSIDQFRGKLN 312
Cdd:PRK07565 287 EDWMERHGYESLQQFRGSMS 306
|
|
| IDI-2_FMN |
cd02811 |
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ... |
229-308 |
1.68e-05 |
|
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. Two types of IDIs have been characterized at present. The long known IDI-1 is only dependent on divalent metals for activity, whereas IDI-2 requires a metal, FMN and NADPH. IDI-2 catalyzes the interconversion of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) in the mevalonate pathway.
Pssm-ID: 239205 [Multi-domain] Cd Length: 326 Bit Score: 45.57 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 229 PTA--LANVRAfytrLRPEIKVIGTGGIKSGKDAFEHLLCGASM-------LQIGTELQKEGVKIFERIEKELKDIMEAK 299
Cdd:cd02811 241 PTAasLLEVRS----ALPDLPLIASGGIRNGLDIAKALALGADLvgmagpfLKAALEGEEAVIETIEQIIEELRTAMFLT 316
|
....*....
gi 2480389716 300 GYTSIDQFR 308
Cdd:cd02811 317 GAKNLAELK 325
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
231-308 |
3.54e-03 |
|
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: 38.58 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2480389716 231 ALANVRAfytRLRPEIKVIGTGGIKSGKDAFEHLLCGASMLQIG-------TELQKEGV-KIFERIEKELKDIMEAKGYT 302
Cdd:COG1304 269 ALPEIRA---AVGGRIPVIADGGIRRGLDVAKALALGADAVGLGrpflyglAAGGEAGVaRVLELLRAELRRAMALTGCR 345
|
....*.
gi 2480389716 303 SIDQFR 308
Cdd:COG1304 346 SLAELR 351
|
|
| |
