|
Name |
Accession |
Description |
Interval |
E-value |
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
4-313 |
0e+00 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 501.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 4 LKLNLLDHVFANPFMNAAGVLCSTEEDLRCMTASSSGALVSKSCTSAPRDGNPEPRYMAFPLGSINSMGLPNLGFDFYLK 83
Cdd:PRK02506 2 TSTQIAGFKFDNCLMNAAGVYCMTKEELEEVEASAAGAFVTKSATLEPRPGNPEPRYADTPLGSINSMGLPNLGFDYYLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 84 YASDLH-DYSKKPLFLSISGLSVEENVAMVRRLApvAQEKGVLLELNLSCPNVPGKPQVAYDFEAMRTYLQQVSLAYGLP 162
Cdd:PRK02506 82 YVLELQkKGPNKPHFLSVVGLSPEETHTILKKIQ--ASDFNGLVELNLSCPNVPGKPQIAYDFETTEQILEEVFTYFTKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 163 FGVKMPPYFDIAHFDTAAAVLNEFPLvKFVTCVNSVGNGLVIDAESESVVIKPKQGFGGLGGKYILPTALANVNAFYRR- 241
Cdd:PRK02506 160 LGVKLPPYFDIVHFDQAAAIFNKFPL-AFVNCINSIGNGLVIDPEDETVVIKPKNGFGGIGGDYIKPTALANVRAFYQRl 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
2E6F_A 242 CPDKLVFGCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDELLEIMARKGYRTLEEFRGRVKTI 313
Cdd:PRK02506 239 NPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAIMAEKGYQSLEDFRGKLKYL 310
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
7-295 |
2.23e-160 |
|
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: 448.70 E-value: 2.23e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 7 NLLDHVFANPFMNAAGVLCSTEEDLRCMTASSSGALVSKSCTSAPRDGNPEPRYMAFPLGSINSMGLPNLGFDFYLKYAS 86
Cdd:cd04741 2 TPPGLTISPPLMNAAGPWCTTLEDLLELAASSTGAVTTRSSTLAGRPGNPEPRYYAFPLGSINSLGLPNLGLDYYLEYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 87 DLHDY---SKKPLFLSISGlSVEENVAMVRRLAPVAQEKGVLLELNLSCPNVPGKPQVAYDFEAMRTYLQQVSLAYGLPF 163
Cdd:cd04741 82 TISDGlpgSAKPFFISVTG-SAEDIAAMYKKIAAHQKQFPLAMELNLSCPNVPGKPPPAYDFDATLEYLTAVKAAYSIPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 164 GVKMPPYFDIAHFDTAAAVLNEFP-LVKFVTCVNSVGNGLVIDAESESVVIKPKQGFGGLGGKYILPTALANVNAFYRRC 242
Cdd:cd04741 161 GVKTPPYTDPAQFDTLAEALNAFAcPISFITATNTLGNGLVLDPERETVVLKPKTGFGGLAGAYLHPLALGNVRTFRRLL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
2E6F_A 243 P-DKLVFGCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDELLEIM 295
Cdd:cd04741 241 PsEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEKELEDIW 294
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
4-295 |
2.43e-93 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 278.85 E-value: 2.43e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 4 LKLNLLDHVFANPFMNAAGVLCSTEEDLRCMTASSSGALVSKSCTSAPRDGNPEPRYMAFPLGSINSMGLPNLGFDFYLK 83
Cdd:pfam01180 2 LATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVTPYPQPGNPTPRVFRLPEGVLNRMGLNNPGLDAVLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 84 YASDLHDYSKK---PLFLSISGLSVEENVAMVRRLAPVAQekgvLLELNLSCPNVPGKPQVAYDFEAMRTYLQQVSLAYG 160
Cdd:pfam01180 82 ELLKRRKEYPRpdlGINLSKAGMTVDDYVEVARKIGPFAD----YIELNVSCPNTPGLRALQTDPELAAILLKVVKEVSK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 161 LPFGVKMPP-YFDIAHFDTAAAVLNEFPLVkFVTCVNSVGNGLVIDAESESVVIKPkqGFGGLGGKYILPTALANVNAFY 239
Cdd:pfam01180 158 VPVLVKLAPdLTDIVIIDIADVALGEDGLD-GINATNTTVRGMRIDLKTEKPILAN--GTGGLSGPPIKPIALKVIRELY 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
2E6F_A 240 RRCPDKL-VFGCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDELLEIM 295
Cdd:pfam01180 235 QRTGPEIpIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
4-304 |
6.59e-86 |
|
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: 260.01 E-value: 6.59e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 4 LKLNLLDHVFANPFMNAAGVLCSTEEDLRCMTASSSGALVSKSCTSAPRDGNPEPRY--MAFPLGSINSMGLPNLGFDFY 81
Cdd:COG0167 2 LSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLfrLPEDSGLINRMGLNNPGVDAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 82 LKYASDLHDYsKKPLFLSISGLSVEENVAMVRRLAPVaqekGV-LLELNLSCPNVPGK-PQVAYDFEAMRTYLQQVSLAY 159
Cdd:COG0167 82 LERLLPAKRY-DVPVIVNIGGNTVEDYVELARRLADA----GAdYLELNISCPNTPGGgRALGQDPEALAELLAAVKAAT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 160 GLPFGVKMPPyfDIAHFDTAAAVLNEFPLvKFVTCVNSVgNGLVIDAESESVVIKPkqGFGGLGGKYILPTALANVNAFY 239
Cdd:COG0167 157 DKPVLVKLAP--DLTDIVEIARAAEEAGA-DGVIAINTT-LGRAIDLETRRPVLAN--EAGGLSGPALKPIALRMVREVA 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
2E6F_A 240 RRCPDKL-VFGCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDELLEIMARKGYRTLE 304
Cdd:COG0167 231 QAVGGDIpIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSIS 296
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
4-309 |
3.70e-44 |
|
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: 152.58 E-value: 3.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 4 LKLNLLDHVFANPFMNAAGVLCSTEEDLRCMTASSSGALVSKSCTSAPRDGNPEPRYMAFPLGSINSMGLPNLGFDFYLK 83
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTIVETPCGMLNAIGLQNPGVEAFLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 84 YASDLHDYSKKPLFLSISGLSVEENVAMVRRLAPvAQEKGVLLELNLSCPNVPG-------KPQVAYDFeamrtyLQQVS 156
Cdd:TIGR01037 81 ELKPVREEFPTPLIASVYGSSVEEFAEVAEKLEK-APPYVDAYELNLSCPHVKGggiaigqDPELSADV------VKAVK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 157 LAYGLPFGVKMPPYF-DIAHFDTAAavlnEFPLVKFVTCVNSVGnGLVIDAESESVVIKPKqgFGGLGGKYILPTALANV 235
Cdd:TIGR01037 154 DKTDVPVFAKLSPNVtDITEIAKAA----EEAGADGLTLINTLR-GMKIDIKTGKPILANK--TGGLSGPAIKPIALRMV 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
2E6F_A 236 NAFYRRCpDKLVFGCGGVYSGEDAFLHILAGASMVQVGTALQEEgPGIFTRLEDELLEIMARKGYRTLEEFRGR 309
Cdd:TIGR01037 227 YDVYKMV-DIPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYR-GFAFKKIIEGLIAFLKAEGFTSIEELIGI 298
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
4-313 |
0e+00 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 501.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 4 LKLNLLDHVFANPFMNAAGVLCSTEEDLRCMTASSSGALVSKSCTSAPRDGNPEPRYMAFPLGSINSMGLPNLGFDFYLK 83
Cdd:PRK02506 2 TSTQIAGFKFDNCLMNAAGVYCMTKEELEEVEASAAGAFVTKSATLEPRPGNPEPRYADTPLGSINSMGLPNLGFDYYLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 84 YASDLH-DYSKKPLFLSISGLSVEENVAMVRRLApvAQEKGVLLELNLSCPNVPGKPQVAYDFEAMRTYLQQVSLAYGLP 162
Cdd:PRK02506 82 YVLELQkKGPNKPHFLSVVGLSPEETHTILKKIQ--ASDFNGLVELNLSCPNVPGKPQIAYDFETTEQILEEVFTYFTKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 163 FGVKMPPYFDIAHFDTAAAVLNEFPLvKFVTCVNSVGNGLVIDAESESVVIKPKQGFGGLGGKYILPTALANVNAFYRR- 241
Cdd:PRK02506 160 LGVKLPPYFDIVHFDQAAAIFNKFPL-AFVNCINSIGNGLVIDPEDETVVIKPKNGFGGIGGDYIKPTALANVRAFYQRl 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
2E6F_A 242 CPDKLVFGCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDELLEIMARKGYRTLEEFRGRVKTI 313
Cdd:PRK02506 239 NPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAIMAEKGYQSLEDFRGKLKYL 310
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
7-295 |
2.23e-160 |
|
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: 448.70 E-value: 2.23e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 7 NLLDHVFANPFMNAAGVLCSTEEDLRCMTASSSGALVSKSCTSAPRDGNPEPRYMAFPLGSINSMGLPNLGFDFYLKYAS 86
Cdd:cd04741 2 TPPGLTISPPLMNAAGPWCTTLEDLLELAASSTGAVTTRSSTLAGRPGNPEPRYYAFPLGSINSLGLPNLGLDYYLEYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 87 DLHDY---SKKPLFLSISGlSVEENVAMVRRLAPVAQEKGVLLELNLSCPNVPGKPQVAYDFEAMRTYLQQVSLAYGLPF 163
Cdd:cd04741 82 TISDGlpgSAKPFFISVTG-SAEDIAAMYKKIAAHQKQFPLAMELNLSCPNVPGKPPPAYDFDATLEYLTAVKAAYSIPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 164 GVKMPPYFDIAHFDTAAAVLNEFP-LVKFVTCVNSVGNGLVIDAESESVVIKPKQGFGGLGGKYILPTALANVNAFYRRC 242
Cdd:cd04741 161 GVKTPPYTDPAQFDTLAEALNAFAcPISFITATNTLGNGLVLDPERETVVLKPKTGFGGLAGAYLHPLALGNVRTFRRLL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
2E6F_A 243 P-DKLVFGCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDELLEIM 295
Cdd:cd04741 241 PsEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEKELEDIW 294
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
7-290 |
1.68e-97 |
|
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: 289.25 E-value: 1.68e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 7 NLLDHVFANPFMNAAGVLCSTEEDLRCMTASSSGALVSKSCTSAPRDGNPEPRYMAFP---------LGSINSMGLPNLG 77
Cdd:cd02810 2 NFLGLKLKNPFGVAAGPLLKTGELIARAAAAGFGAVVYKTVTLHPRPGNPLPRVARLPpegesypeqLGILNSFGLPNLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 78 FDFYLKYASDLHDY-SKKPLFLSISGLSVEENVAMVRRLAPVaqeKGVLLELNLSCPNVPGKPQVAYDFEAMRTYLQQVS 156
Cdd:cd02810 82 LDVWLQDIAKAKKEfPGQPLIASVGGSSKEDYVELARKIERA---GAKALELNLSCPNVGGGRQLGQDPEAVANLLKAVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 157 LAYGLPFGVKMPPYFDIAHFDTAAAVLNEFPlVKFVTCVNSVGNGLVIDAEsesVVIKPKQGFGGLGGKYILPTALANVN 236
Cdd:cd02810 159 AAVDIPLLVKLSPYFDLEDIVELAKAAERAG-ADGLTAINTISGRVVDLKT---VGPGPKRGTGGLSGAPIRPLALRWVA 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
2E6F_A 237 AFYRRCP-DKLVFGCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDE 290
Cdd:cd02810 235 RLAARLQlDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKIKKE 289
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
4-295 |
2.43e-93 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 278.85 E-value: 2.43e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 4 LKLNLLDHVFANPFMNAAGVLCSTEEDLRCMTASSSGALVSKSCTSAPRDGNPEPRYMAFPLGSINSMGLPNLGFDFYLK 83
Cdd:pfam01180 2 LATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVTPYPQPGNPTPRVFRLPEGVLNRMGLNNPGLDAVLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 84 YASDLHDYSKK---PLFLSISGLSVEENVAMVRRLAPVAQekgvLLELNLSCPNVPGKPQVAYDFEAMRTYLQQVSLAYG 160
Cdd:pfam01180 82 ELLKRRKEYPRpdlGINLSKAGMTVDDYVEVARKIGPFAD----YIELNVSCPNTPGLRALQTDPELAAILLKVVKEVSK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 161 LPFGVKMPP-YFDIAHFDTAAAVLNEFPLVkFVTCVNSVGNGLVIDAESESVVIKPkqGFGGLGGKYILPTALANVNAFY 239
Cdd:pfam01180 158 VPVLVKLAPdLTDIVIIDIADVALGEDGLD-GINATNTTVRGMRIDLKTEKPILAN--GTGGLSGPPIKPIALKVIRELY 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
2E6F_A 240 RRCPDKL-VFGCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDELLEIM 295
Cdd:pfam01180 235 QRTGPEIpIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
4-304 |
6.59e-86 |
|
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: 260.01 E-value: 6.59e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 4 LKLNLLDHVFANPFMNAAGVLCSTEEDLRCMTASSSGALVSKSCTSAPRDGNPEPRY--MAFPLGSINSMGLPNLGFDFY 81
Cdd:COG0167 2 LSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLfrLPEDSGLINRMGLNNPGVDAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 82 LKYASDLHDYsKKPLFLSISGLSVEENVAMVRRLAPVaqekGV-LLELNLSCPNVPGK-PQVAYDFEAMRTYLQQVSLAY 159
Cdd:COG0167 82 LERLLPAKRY-DVPVIVNIGGNTVEDYVELARRLADA----GAdYLELNISCPNTPGGgRALGQDPEALAELLAAVKAAT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 160 GLPFGVKMPPyfDIAHFDTAAAVLNEFPLvKFVTCVNSVgNGLVIDAESESVVIKPkqGFGGLGGKYILPTALANVNAFY 239
Cdd:COG0167 157 DKPVLVKLAP--DLTDIVEIARAAEEAGA-DGVIAINTT-LGRAIDLETRRPVLAN--EAGGLSGPALKPIALRMVREVA 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
2E6F_A 240 RRCPDKL-VFGCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDELLEIMARKGYRTLE 304
Cdd:COG0167 231 QAVGGDIpIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSIS 296
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
13-308 |
2.65e-56 |
|
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: 183.90 E-value: 2.65e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 13 FANPFMNAAGVLCSTEEDLRCMTASSSGALVSKSCTSAPRDGNPEPRYMAFPLGSINSMGLPNLGFDFYLKYASDLHDYS 92
Cdd:cd04740 9 LKNPVILASGTFGFGEELSRVADLGKLGAIVTKSITLEPREGNPPPRVVETPGGMLNAIGLQNPGVEAFLEELLPWLREF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 93 KKPLFLSISGLSVEENVAMVRRLAPVaqeKGVLLELNLSCPNVPGK-------PQVAYDF-EAMRTylqqvslAYGLPFG 164
Cdd:cd04740 89 GTPVIASIAGSTVEEFVEVAEKLADA---GADAIELNISCPNVKGGgmafgtdPEAVAEIvKAVKK-------ATDVPVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 165 VKMPPYF-DIAhfDTAAAVLNEFplVKFVTCVNSVGnGLVIDAESESVVIkpKQGFGGLGGKYILPTALANVNAFYRRCp 243
Cdd:cd04740 159 VKLTPNVtDIV--EIARAAEEAG--ADGLTLINTLK-GMAIDIETRKPIL--GNVTGGLSGPAIKPIALRMVYQVYKAV- 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
2E6F_A 244 DKLVFGCGGVYSGEDAFLHILAGASMVQVGTALQeEGPGIFTRLEDELLEIMARKGYRTLEEFRG 308
Cdd:cd04740 231 EIPIIGVGGIASGEDALEFLMAGASAVQVGTANF-VDPEAFKEIIEGLEAYLDEEGIKSIEELVG 294
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
4-311 |
9.30e-56 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 182.66 E-value: 9.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 4 LKLNLLDHVFANPFMNAAGVLCSTEEDLRCMTASSSGALVSKSCTSAPRDGNPEPRYMAFPLGSINSMGLPNLGFDFYLK 83
Cdd:PRK07259 2 LSVELPGLKLKNPVMPASGTFGFGGEYARFYDLNGLGAIVTKSTTLEPREGNPTPRIAETPGGMLNAIGLQNPGVDAFIE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 84 YASDLHDYSKKPLFLSISGLSVEENVAMVRRLAPVAQEKGvlLELNLSCPNVPG-------KPQVAYDF-EAMRTylqqv 155
Cdd:PRK07259 82 EELPWLEEFDTPIIANVAGSTEEEYAEVAEKLSKAPNVDA--IELNISCPNVKHggmafgtDPELAYEVvKAVKE----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 156 slAYGLPFGVKMPPYF-DIAhfDTAAAVLNEFplVKFVTCVNSVgNGLVIDAESEsvviKP--KQGFGGLGGKYILPTAL 232
Cdd:PRK07259 155 --VVKVPVIVKLTPNVtDIV--EIAKAAEEAG--ADGLSLINTL-KGMAIDIKTR----KPilANVTGGLSGPAIKPIAL 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
2E6F_A 233 ANVNAFYRRCpDKLVFGCGGVYSGEDAFLHILAGASMVQVGTALQeEGPGIFTRLEDELLEIMARKGYRTLEEFRGRVK 311
Cdd:PRK07259 224 RMVYQVYQAV-DIPIIGMGGISSAEDAIEFIMAGASAVQVGTANF-YDPYAFPKIIEGLEAYLDKYGIKSIEEIVGIAH 300
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
4-309 |
3.70e-44 |
|
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: 152.58 E-value: 3.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 4 LKLNLLDHVFANPFMNAAGVLCSTEEDLRCMTASSSGALVSKSCTSAPRDGNPEPRYMAFPLGSINSMGLPNLGFDFYLK 83
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTIVETPCGMLNAIGLQNPGVEAFLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 84 YASDLHDYSKKPLFLSISGLSVEENVAMVRRLAPvAQEKGVLLELNLSCPNVPG-------KPQVAYDFeamrtyLQQVS 156
Cdd:TIGR01037 81 ELKPVREEFPTPLIASVYGSSVEEFAEVAEKLEK-APPYVDAYELNLSCPHVKGggiaigqDPELSADV------VKAVK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 157 LAYGLPFGVKMPPYF-DIAHFDTAAavlnEFPLVKFVTCVNSVGnGLVIDAESESVVIKPKqgFGGLGGKYILPTALANV 235
Cdd:TIGR01037 154 DKTDVPVFAKLSPNVtDITEIAKAA----EEAGADGLTLINTLR-GMKIDIKTGKPILANK--TGGLSGPAIKPIALRMV 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
2E6F_A 236 NAFYRRCpDKLVFGCGGVYSGEDAFLHILAGASMVQVGTALQEEgPGIFTRLEDELLEIMARKGYRTLEEFRGR 309
Cdd:TIGR01037 227 YDVYKMV-DIPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYR-GFAFKKIIEGLIAFLKAEGFTSIEELIGI 298
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
46-291 |
2.21e-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: 2.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 46 SCTSAPRDGNPEPRymAFPL----GSINSMGLPNLGFDFYLKYASDLHdYSKKPLFLSI-----SGLS--VEENVAMVRR 114
Cdd:cd04738 80 TVTPRPQPGNPKPR--LFRLpedeALINRMGFNNDGADAVAKRLKKRR-PRGGPLGVNIgknkdTPLEdaVEDYVIGVRK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 115 LAPVAQekgvLLELNLSCPNVPG--KPQVAYDFEAMRTYLQ--QVSLAYGLPFGVKMPPYFDIAHFDTAAAVLNEFPLvk 190
Cdd:cd04738 157 LGPYAD----YLVVNVSSPNTPGlrDLQGKEALRELLTAVKeeRNKLGKKVPLLVKIAPDLSDEELEDIADVALEHGV-- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 191 fvtcvnsvgNGLVID----AESESVVIKPKQGFGGLGGKYILPTALANVNAFYRRCPDKL-VFGCGGVYSGEDAFLHILA 265
Cdd:cd04738 231 ---------DGIIATnttiSRPGLLRSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIpIIGVGGISSGEDAYEKIRA 301
|
250 260
....*....|....*....|....*.
2E6F_A 266 GASMVQVGTALQEEGPGIFTRLEDEL 291
Cdd:cd04738 302 GASLVQLYTGLVYEGPGLVKRIKREL 327
|
|
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
13-291 |
2.19e-22 |
|
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: 94.66 E-value: 2.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 13 FANPFMNAAG-VLCSTEEDLRCMTASSSGALVSKSCTSAPRDGNPEPRYMAFPLGSINSMGLPNL------GFDFYLKYA 85
Cdd:cd02940 11 FPNPFGLASApPTTSYPMIRRAFEAGWGGAVTKTLGLDKDIVTNVSPRIARLRTSGRGQIGFNNIelisekPLEYWLKEI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 86 SDLH-DYSKKPLFLSISGlsvEENVAMVRRLAPVAQEKGV-LLELNLSCPNvpGKPQ------VAYDFEAMRTYLQQVSL 157
Cdd:cd02940 91 RELKkDFPDKILIASIMC---EYNKEDWTELAKLVEEAGAdALELNFSCPH--GMPErgmgaaVGQDPELVEEICRWVRE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 158 AYGLPFGVKMPP-YFDIAhfDTAAAVLNEFplVKFVTCVNSVgNGLV-IDAESES--VVIKPKQGFGGLGGKYILPTALA 233
Cdd:cd02940 166 AVKIPVIAKLTPnITDIR--EIARAAKEGG--ADGVSAINTV-NSLMgVDLDGTPpaPGVEGKTTYGGYSGPAVKPIALR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
2E6F_A 234 NVNAFYRRCPDKL-VFGCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDEL 291
Cdd:cd02940 241 AVSQIARAPEPGLpISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
46-305 |
2.87e-20 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 90.18 E-value: 2.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 46 SCTSAPRDGNPEPRYMAFP--LGSINSMGLPNLGFDFYLKYASDLHDYSKKPLFLSIS-----------------GLSVE 106
Cdd:PLN02826 115 SVTPLPQPGNPKPRVFRLReeGAIINRYGFNSEGIVAVAKRLGAQHGKRKLDETSSSSfssddvkaggkagpgilGVNLG 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 107 EN----------VAMVRRLAPVAQekgvLLELNLSCPNVPG--KPQVAYDFEAMRTYLQ------QVSLAYGLPFGVKMP 168
Cdd:PLN02826 195 KNktsedaaadyVQGVRALSQYAD----YLVINVSSPNTPGlrKLQGRKQLKDLLKKVLaardemQWGEEGPPPLLVKIA 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 169 PyfDIAHFDT---AAAVLnefplvkfvtcvnSVG-NGLVI----DAESESVVIKPKQG-FGGLGGKYILPTALANVNAFY 239
Cdd:PLN02826 271 P--DLSKEDLediAAVAL-------------ALGiDGLIIsnttISRPDSVLGHPHADeAGGLSGKPLFDLSTEVLREMY 335
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
2E6F_A 240 RRCPDKL-VFGCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDELLEIMARKGYRTLEE 305
Cdd:PLN02826 336 RLTRGKIpLVGCGGVSSGEDAYKKIRAGASLVQLYTAFAYEGPALIPRIKAELAACLERDGFKSIQE 402
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
48-299 |
3.13e-20 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 89.45 E-value: 3.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 48 TSAPRDGNPEPRYmaFPL----GSINSMGLPNLGFDFYLKYASDLHDYSkkPLFLSI--SGLSVEEN-----VAMVRRLA 116
Cdd:PRK05286 92 TPRPQPGNPKPRL--FRLpedeALINRMGFNNDGADALAERLKKAYRGI--PLGINIgkNKDTPLEDavddyLICLEKLY 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 117 PVAQekgvLLELNLSCPNVPGKPQVAYDfEAMRTYLQQV-----SLAYGLPFGVKMPPYFDIAHFDTAAAVLNEFPLvkf 191
Cdd:PRK05286 168 PYAD----YFTVNISSPNTPGLRDLQYG-EALDELLAALkeaqaELHGYVPLLVKIAPDLSDEELDDIADLALEHGI--- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 192 vtcvnsvgNGLVID----AESESVVIKPKQGFGGLGGKYILPTALANVNAFYRRCPDKL-VFGCGGVYSGEDAFLHILAG 266
Cdd:PRK05286 240 --------DGVIATnttlSRDGLKGLPNADEAGGLSGRPLFERSTEVIRRLYKELGGRLpIIGVGGIDSAEDAYEKIRAG 311
|
250 260 270
....*....|....*....|....*....|...
2E6F_A 267 ASMVQVGTALQEEGPGIFTRLEDELLEIMARKG 299
Cdd:PRK05286 312 ASLVQIYSGLIYEGPGLVKEIVRGLARLLRRDG 344
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
90-313 |
2.66e-15 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 75.75 E-value: 2.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 90 DYSKKPLFLSISGLSVEENVamvRRLAPVAQEKGV-LLELNLSCPNvpGKP---------QVAydfEAMRTYLQQVSLAY 159
Cdd:PRK08318 96 DYPDRALIASIMVECNEEEW---KEIAPLVEETGAdGIELNFGCPH--GMSergmgsavgQVP---ELVEMYTRWVKRGS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 160 GLPFGVKMPPYF-DI------AHFDTAAAV--LNEfplVKFVTCVNsvgnglvIDAESESVVIKPKQGFGGLGGKYILPT 230
Cdd:PRK08318 168 RLPVIVKLTPNItDIreparaAKRGGADAVslINT---INSITGVD-------LDRMIPMPIVNGKSSHGGYCGPAVKPI 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 231 ALANVNAFYRrcpDKLVF-----GCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDELLEIMARKGYRTLEE 305
Cdd:PRK08318 238 ALNMVAEIAR---DPETRglpisGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISGLSHYMDEKGFASLED 314
|
....*....
2E6F_A 306 FRGR-VKTI 313
Cdd:PRK08318 315 MVGLaVPNV 323
|
|
| DHOD_like |
cd04739 |
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
15-309 |
8.24e-13 |
|
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: 68.03 E-value: 8.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 15 NPFMNAAGVLCSTEEDLRCMTASSSGALVSKSC--TSAPRDGNPEPRYMAFPLGSINSMGLpnlgFDFYLKYASDLHDY- 91
Cdd:cd04739 13 NPLVASASPLSRNLDNIRRLEDAGAGAIVLPSLfeEQIEREAQELDRFLTYGSSFAEALSY----FPEYGRYNLGPEEYl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 92 -----SKK----PLFLSISGLSVEENVAMVRRLapvaQEKGV-LLELNLScpNVPGKPQVAY-DFEAMrtY---LQQVSL 157
Cdd:cd04739 89 elirrAKRavsiPVIASLNGVSAGGWVDYARQI----EEAGAdALELNIY--ALPTDPDISGaEVEQR--YldiLRAVKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 158 AYGLPFGVKMPPYFdiahfdTAaavlnefpLVKFVTCVNSVG-NGLV---------IDAESESVVIKPKQGFGGLGGKYI 227
Cdd:cd04739 161 AVTIPVAVKLSPFF------SA--------LAHMAKQLDAAGaDGLVlfnrfyqpdIDLETLEVVPNLLLSSPAEIRLPL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 228 LPTALAnvnafYRRCPDKLVfGCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDELLEIMARKGYRTLEEFR 307
Cdd:cd04739 227 RWIAIL-----SGRVKASLA-ASGGVHDAEDVVKYLLAGADVVMTTSALLRHGPDYIGTLLAGLEAWMEEHGYESVQQLR 300
|
..
2E6F_A 308 GR 309
Cdd:cd04739 301 GS 302
|
|
| PRK07565 |
PRK07565 |
dihydroorotate dehydrogenase-like protein; |
15-309 |
2.40e-12 |
|
dihydroorotate dehydrogenase-like protein;
Pssm-ID: 236051 Cd Length: 334 Bit Score: 66.43 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 15 NPFMNAAGVLCSTEEDLRCMTASSSGALVSKS---------------CTSAPRDGNPEPRyMAFPLGSINSMGLpnlgfD 79
Cdd:PRK07565 14 NPLVASASPLSESVDNVKRLEDAGAGAVVLKSlfeeqirheaaeldrHLTHGTESFAEAL-DYFPEPAKFYVGP-----E 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 80 FYLKYASDLHDYSKKPLFLSISGLSVEENVAMVRRLapvaQEKGV-LLELNLScpNVPGKPQVAY-DFEAMrtY---LQQ 154
Cdd:PRK07565 88 EYLELIRRAKEAVDIPVIASLNGSSAGGWVDYARQI----EQAGAdALELNIY--YLPTDPDISGaEVEQR--YldiLRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 155 VSLAYGLPFGVKMPPYF-DIAHFdtaaavlnefplvkfVTCVNSVG-NGLV---------IDAESESVVIK-----PKQG 218
Cdd:PRK07565 160 VKSAVSIPVAVKLSPYFsNLANM---------------AKRLDAAGaDGLVlfnrfyqpdIDLETLEVVPGlvlstPAEL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 219 FGGLGGKYILptalanvnafYRRCPDKLVfGCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDELLEIMARK 298
Cdd:PRK07565 225 RLPLRWIAIL----------SGRVGADLA-ATTGVHDAEDVIKMLLAGADVVMIASALLRHGPDYIGTILRGLEDWMERH 293
|
330
....*....|.
2E6F_A 299 GYRTLEEFRGR 309
Cdd:PRK07565 294 GYESLQQFRGS 304
|
|
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
40-308 |
2.47e-11 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 63.70 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 40 GALVSKSCT-SAPRDGNPEPRYMAFPLGSINSMGLPNLG-----------FDFYLKYASDL-HDYSKKPLFLSIsglsVE 106
Cdd:PLN02495 47 GGVIAKTVSlDASKVINVTPRYARLRAGANGSAKGRVIGwqnielisdrpFETMLAEFKQLkEEYPDRILIASI----ME 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 107 E-NVAMVRRLAPVAQEKGV-LLELNLSCPNvpGKPQ------VAYDFEAMRTYLQQVSLAYGLPFGVKMPPYF-DIAHfd 177
Cdd:PLN02495 123 EyNKDAWEEIIERVEETGVdALEINFSCPH--GMPErkmgaaVGQDCDLLEEVCGWINAKATVPVWAKMTPNItDITQ-- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 178 TAAAVLNEFplVKFVTCVNSVGNGLVIDAESesvvIKPK---QGF---GGLGGKYILPTALANVNAFYRRC-----PDKL 246
Cdd:PLN02495 199 PARVALKSG--CEGVAAINTIMSVMGINLDT----LRPEpcvEGYstpGGYSSKAVRPIALAKVMAIAKMMksefpEDRS 272
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
2E6F_A 247 VFGCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDELLEIMARKGYRTLEEFRG 308
Cdd:PLN02495 273 LSGIGGVETGGDAAEFILLGADTVQVCTGVMMHGYPLVKNLCAELQDFMKKHNFSSIEDFRG 334
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
90-274 |
1.22e-05 |
|
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: 45.27 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 90 DYSKKPLFLSISGLSVEENVAMVRRLAPVAQEKGVllELNLSCPnvpgkpqvaYDFEAMRTYLQQVSLAY-GLPFGVKMP 168
Cdd:cd04722 54 AETDLPLGVQLAINDAAAAVDIAAAAARAAGADGV--EIHGAVG---------YLAREDLELIRELREAVpDVKVVVKLS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E6F_A 169 PYFDIAHFDTAAAvlnefpLVKFVTCVNSVGNGLVIDAESESVVIKpkqgfgglggkyilptalanvnAFYRRCPDKLVF 248
Cdd:cd04722 123 PTGELAAAAAEEA------GVDEVGLGNGGGGGGGRDAVPIADLLL----------------------ILAKRGSKVPVI 174
|
170 180
....*....|....*....|....*.
2E6F_A 249 GCGGVYSGEDAFLHILAGASMVQVGT 274
Cdd:cd04722 175 AGGGINDPEDAAEALALGADGVIVGS 200
|
|
| |
