|
Name |
Accession |
Description |
Interval |
E-value |
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
1-260 |
2.41e-46 |
|
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: 157.28 E-value: 2.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 1 MSAGFDKNVQLSPLMEDVGFGFASGGSVTMEPRKGNLRPWFHRLPNTKSVVVYAGMPNYGLEKISDYIElnRSKVKSMPT 80
Cdd:cd04738 54 LAAGFDKNAEAIDALLALGFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLK--KRRPRGGPL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 81 VVSVAviADKSTkdefgpvvPEEYIIRDVKKAVSYIVenSLASVIEINISCPN-AGKEPFIYADTLESLLS----ELDSV 155
Cdd:cd04738 132 GVNIG--KNKDT--------PLEDAVEDYVIGVRKLG--PYADYLVVNVSSPNtPGLRDLQGKEALRELLTavkeERNKL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 156 ERNVPFWIKM-PHLyDLKQFDSLLKVIVEHNIRGVTVANLIKDRGKVdLKDPLTDDiRGGLSGEPTRTHSLELIGYTYKN 234
Cdd:cd04738 200 GKKVPLLVKIaPDL-SDEELEDIADVALEHGVDGIIATNTTISRPGL-LRSPLANE-TGGLSGAPLKERSTEVLRELYKL 276
|
250 260
....*....|....*....|....*.
gi 2052594783 235 YGDKLTVIGVGGVFRPKTHTLRLRQG 260
Cdd:cd04738 277 TGGKIPIIGVGGISSGEDAYEKIRAG 302
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
1-248 |
3.87e-46 |
|
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: 156.00 E-value: 3.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 1 MSAGF-DKNVQLSPLMEDVGFGFASGGSVTMEPRKGNLRPWFHRLPNTKSVVVYAGMPNYGLEKISDyiELNRSKVKSMP 79
Cdd:COG0167 17 LASGFfDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDAFLE--RLLPAKRYDVP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 80 TVVSVAviadKSTKDEFgpvvpeEYIIRdvkkavsyIVENSLASVIEINISCPNA---GKEPFIYADTLESLLSELDSVe 156
Cdd:COG0167 95 VIVNIG----GNTVEDY------VELAR--------RLADAGADYLELNISCPNTpggGRALGQDPEALAELLAAVKAA- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 157 RNVPFWIKMPHlyDLKQFDSLLKVIVEHNIRGVTVANLIKDRGK-VDLKDPLTDDIRGGLSGEPTRTHSLELIGYTYKNY 235
Cdd:COG0167 156 TDKPVLVKLAP--DLTDIVEIARAAEEAGADGVIAINTTLGRAIdLETRRPVLANEAGGLSGPALKPIALRMVREVAQAV 233
|
250
....*....|...
gi 2052594783 236 GDKLTVIGVGGVF 248
Cdd:COG0167 234 GGDIPIIGVGGIS 246
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
1-262 |
1.82e-43 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 150.31 E-value: 1.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 1 MSAGFDKNVQLSPLMEDVGFGFASGGSVTMEPRKGNLRPWFHRLPNTKSVVVYAGMPNYGLEKISDYIELNRSKVksmpt 80
Cdd:PRK05286 64 LAAGFDKNGEAIDALGALGFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKAYRGI----- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 81 VVSVAVIADKSTKDEFGpvvPEEYII--RDVKKAVSYIVenslasvieINISCPN-AGKEPFIYADTLESLLSEL----D 153
Cdd:PRK05286 139 PLGINIGKNKDTPLEDA---VDDYLIclEKLYPYADYFT---------VNISSPNtPGLRDLQYGEALDELLAALkeaqA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 154 SVERNVPFWIKM-PHLyDLKQFDSLLKVIVEHNIRGVTVANLIKDRgkVDLKDPLTDDIRGGLSGEPTRTHSLELIGYTY 232
Cdd:PRK05286 207 ELHGYVPLLVKIaPDL-SDEELDDIADLALEHGIDGVIATNTTLSR--DGLKGLPNADEAGGLSGRPLFERSTEVIRRLY 283
|
250 260 270
....*....|....*....|....*....|..
gi 2052594783 233 KNYGDKLTVIGVGGVFRPKTHTLRLRQG--LV 262
Cdd:PRK05286 284 KELGGRLPIIGVGGIDSAEDAYEKIRAGasLV 315
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
2-248 |
3.66e-30 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 113.98 E-value: 3.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 2 SAGFDKN-VQLSPLMEDVGFGFASGGSVTMEPRKGNLRPWFHRLPntKSVVVYAGMPNYGLEKISDYIELNRSKVKSMPt 80
Cdd:pfam01180 18 ASGFDKFgEEALKWLALGKFGAIEIKSVTPYPQPGNPTPRVFRLP--EGVLNRMGLNNPGLDAVLAELLKRRKEYPRPD- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 81 vvsVAVIADKSTKDEfgpvvpEEYIirdvkkAVSYIVENsLASVIEINISCPNA-GKEPFIYADTLESLLSELDSVERNV 159
Cdd:pfam01180 95 ---LGINLSKAGMTV------DDYV------EVARKIGP-FADYIELNVSCPNTpGLRALQTDPELAAILLKVVKEVSKV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 160 PFWIKM-PHLYDLKQFDSLLKVIVEHNIRGVTVANLIKDRGKVDLK--DPLTDDIRGGLSGEPTRTHSLELIGYTYKNYG 236
Cdd:pfam01180 159 PVLVKLaPDLTDIVIIDIADVALGEDGLDGINATNTTVRGMRIDLKteKPILANGTGGLSGPPIKPIALKVIRELYQRTG 238
|
250
....*....|..
gi 2052594783 237 DKLTVIGVGGVF 248
Cdd:pfam01180 239 PEIPIIGVGGIE 250
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
1-247 |
5.32e-25 |
|
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: 101.40 E-value: 5.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 1 MSAGFDKNVQ-LSPLMEdVGFGFASGGSVTMEPRKGNLRPWFHRLPNTKSVVVYAGMPNYGLekisDYIELNrskVKSMP 79
Cdd:TIGR01036 61 LAAGFDKDGEaIDALGA-MGFGFLEIGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGA----DVLVER---LKRAR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 80 --TVVSVAVIADKSTKDEFGpvvPEEYIIrDVKKAVSYivenslASVIEINISCPN-AGKEPFIYADTLESLLS----EL 152
Cdd:TIGR01036 133 ykGPIGINIGKNKDTPSEDA---KEDYAA-CLRKLGPL------ADYLVVNVSSPNtPGLRDLQYKAELRDLLTavkqEQ 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 153 DSVER--NVPFWIKM-PHLYDlKQFDSLLKVIVEHNIRGVTVANLIKDRGKVdlKDPLTDDIRGGLSGEPTRTHSLELIG 229
Cdd:TIGR01036 203 DGLRRvhRVPVLVKIaPDLTE-SDLEDIADSLVELGIDGVIATNTTVSRSLV--QGPKNSDETGGLSGKPLQDKSTEIIR 279
|
250
....*....|....*...
gi 2052594783 230 YTYKNYGDKLTVIGVGGV 247
Cdd:TIGR01036 280 RLYAELQGRLPIIGVGGI 297
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
1-260 |
2.41e-46 |
|
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: 157.28 E-value: 2.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 1 MSAGFDKNVQLSPLMEDVGFGFASGGSVTMEPRKGNLRPWFHRLPNTKSVVVYAGMPNYGLEKISDYIElnRSKVKSMPT 80
Cdd:cd04738 54 LAAGFDKNAEAIDALLALGFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLK--KRRPRGGPL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 81 VVSVAviADKSTkdefgpvvPEEYIIRDVKKAVSYIVenSLASVIEINISCPN-AGKEPFIYADTLESLLS----ELDSV 155
Cdd:cd04738 132 GVNIG--KNKDT--------PLEDAVEDYVIGVRKLG--PYADYLVVNVSSPNtPGLRDLQGKEALRELLTavkeERNKL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 156 ERNVPFWIKM-PHLyDLKQFDSLLKVIVEHNIRGVTVANLIKDRGKVdLKDPLTDDiRGGLSGEPTRTHSLELIGYTYKN 234
Cdd:cd04738 200 GKKVPLLVKIaPDL-SDEELEDIADVALEHGVDGIIATNTTISRPGL-LRSPLANE-TGGLSGAPLKERSTEVLRELYKL 276
|
250 260
....*....|....*....|....*.
gi 2052594783 235 YGDKLTVIGVGGVFRPKTHTLRLRQG 260
Cdd:cd04738 277 TGGKIPIIGVGGISSGEDAYEKIRAG 302
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
1-248 |
3.87e-46 |
|
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: 156.00 E-value: 3.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 1 MSAGF-DKNVQLSPLMEDVGFGFASGGSVTMEPRKGNLRPWFHRLPNTKSVVVYAGMPNYGLEKISDyiELNRSKVKSMP 79
Cdd:COG0167 17 LASGFfDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDAFLE--RLLPAKRYDVP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 80 TVVSVAviadKSTKDEFgpvvpeEYIIRdvkkavsyIVENSLASVIEINISCPNA---GKEPFIYADTLESLLSELDSVe 156
Cdd:COG0167 95 VIVNIG----GNTVEDY------VELAR--------RLADAGADYLELNISCPNTpggGRALGQDPEALAELLAAVKAA- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 157 RNVPFWIKMPHlyDLKQFDSLLKVIVEHNIRGVTVANLIKDRGK-VDLKDPLTDDIRGGLSGEPTRTHSLELIGYTYKNY 235
Cdd:COG0167 156 TDKPVLVKLAP--DLTDIVEIARAAEEAGADGVIAINTTLGRAIdLETRRPVLANEAGGLSGPALKPIALRMVREVAQAV 233
|
250
....*....|...
gi 2052594783 236 GDKLTVIGVGGVF 248
Cdd:COG0167 234 GGDIPIIGVGGIS 246
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
1-262 |
1.82e-43 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 150.31 E-value: 1.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 1 MSAGFDKNVQLSPLMEDVGFGFASGGSVTMEPRKGNLRPWFHRLPNTKSVVVYAGMPNYGLEKISDYIELNRSKVksmpt 80
Cdd:PRK05286 64 LAAGFDKNGEAIDALGALGFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKAYRGI----- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 81 VVSVAVIADKSTKDEFGpvvPEEYII--RDVKKAVSYIVenslasvieINISCPN-AGKEPFIYADTLESLLSEL----D 153
Cdd:PRK05286 139 PLGINIGKNKDTPLEDA---VDDYLIclEKLYPYADYFT---------VNISSPNtPGLRDLQYGEALDELLAALkeaqA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 154 SVERNVPFWIKM-PHLyDLKQFDSLLKVIVEHNIRGVTVANLIKDRgkVDLKDPLTDDIRGGLSGEPTRTHSLELIGYTY 232
Cdd:PRK05286 207 ELHGYVPLLVKIaPDL-SDEELDDIADLALEHGIDGVIATNTTLSR--DGLKGLPNADEAGGLSGRPLFERSTEVIRRLY 283
|
250 260 270
....*....|....*....|....*....|..
gi 2052594783 233 KNYGDKLTVIGVGGVFRPKTHTLRLRQG--LV 262
Cdd:PRK05286 284 KELGGRLPIIGVGGIDSAEDAYEKIRAGasLV 315
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
2-247 |
3.49e-32 |
|
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: 119.38 E-value: 3.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 2 SAGFD-KNVQLSPLMEDVGFGFASGGSVTMEPRKGNLRPWFHRLPNTKSVVVYA-------GMPNYGLEKISDYIELNRS 73
Cdd:cd02810 15 AAGPLlKTGELIARAAAAGFGAVVYKTVTLHPRPGNPLPRVARLPPEGESYPEQlgilnsfGLPNLGLDVWLQDIAKAKK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 74 KVKSMPTVVSVAviadKSTKDEfgpvvpeeyIIRDVKKavsyiVENSLASVIEINISCPNAGKEPFIY--ADTLESLLSE 151
Cdd:cd02810 95 EFPGQPLIASVG----GSSKED---------YVELARK-----IERAGAKALELNLSCPNVGGGRQLGqdPEAVANLLKA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 152 LDSvERNVPFWIKMPHLYDLKQFDSLLKVIVEHNIRGVTVANLIKDRgKVDLKDPLT--DDIRGGLSGEPTRTHSLELIG 229
Cdd:cd02810 157 VKA-AVDIPLLVKLSPYFDLEDIVELAKAAERAGADGLTAINTISGR-VVDLKTVGPgpKRGTGGLSGAPIRPLALRWVA 234
|
250
....*....|....*...
gi 2052594783 230 YTYKNYGDKLTVIGVGGV 247
Cdd:cd02810 235 RLAARLQLDIPIIGVGGI 252
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
2-248 |
3.66e-30 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 113.98 E-value: 3.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 2 SAGFDKN-VQLSPLMEDVGFGFASGGSVTMEPRKGNLRPWFHRLPntKSVVVYAGMPNYGLEKISDYIELNRSKVKSMPt 80
Cdd:pfam01180 18 ASGFDKFgEEALKWLALGKFGAIEIKSVTPYPQPGNPTPRVFRLP--EGVLNRMGLNNPGLDAVLAELLKRRKEYPRPD- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 81 vvsVAVIADKSTKDEfgpvvpEEYIirdvkkAVSYIVENsLASVIEINISCPNA-GKEPFIYADTLESLLSELDSVERNV 159
Cdd:pfam01180 95 ---LGINLSKAGMTV------DDYV------EVARKIGP-FADYIELNVSCPNTpGLRALQTDPELAAILLKVVKEVSKV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 160 PFWIKM-PHLYDLKQFDSLLKVIVEHNIRGVTVANLIKDRGKVDLK--DPLTDDIRGGLSGEPTRTHSLELIGYTYKNYG 236
Cdd:pfam01180 159 PVLVKLaPDLTDIVIIDIADVALGEDGLDGINATNTTVRGMRIDLKteKPILANGTGGLSGPPIKPIALKVIRELYQRTG 238
|
250
....*....|..
gi 2052594783 237 DKLTVIGVGGVF 248
Cdd:pfam01180 239 PEIPIIGVGGIE 250
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
1-247 |
5.32e-25 |
|
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: 101.40 E-value: 5.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 1 MSAGFDKNVQ-LSPLMEdVGFGFASGGSVTMEPRKGNLRPWFHRLPNTKSVVVYAGMPNYGLekisDYIELNrskVKSMP 79
Cdd:TIGR01036 61 LAAGFDKDGEaIDALGA-MGFGFLEIGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGA----DVLVER---LKRAR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 80 --TVVSVAVIADKSTKDEFGpvvPEEYIIrDVKKAVSYivenslASVIEINISCPN-AGKEPFIYADTLESLLS----EL 152
Cdd:TIGR01036 133 ykGPIGINIGKNKDTPSEDA---KEDYAA-CLRKLGPL------ADYLVVNVSSPNtPGLRDLQYKAELRDLLTavkqEQ 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 153 DSVER--NVPFWIKM-PHLYDlKQFDSLLKVIVEHNIRGVTVANLIKDRGKVdlKDPLTDDIRGGLSGEPTRTHSLELIG 229
Cdd:TIGR01036 203 DGLRRvhRVPVLVKIaPDLTE-SDLEDIADSLVELGIDGVIATNTTVSRSLV--QGPKNSDETGGLSGKPLQDKSTEIIR 279
|
250
....*....|....*...
gi 2052594783 230 YTYKNYGDKLTVIGVGGV 247
Cdd:TIGR01036 280 RLYAELQGRLPIIGVGGI 297
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
1-260 |
1.74e-22 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 95.19 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 1 MSAGFDKNVQLSPLMEDVGFGFASGGSVTMEPRKGNLRPWFHRLPNTKSVVVYAGMPNYGLEKISDYIELNRSKVKSMPT 80
Cdd:PLN02826 89 LAAGFDKNAEAVEGLLGLGFGFVEIGSVTPLPQPGNPKPRVFRLREEGAIINRYGFNSEGIVAVAKRLGAQHGKRKLDET 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 81 VVSVAVIADKSTKDEFGPVV--------------PEEYI--IRDVKKAVSYIVenslasvieINISCPNA-------GKE 137
Cdd:PLN02826 169 SSSSFSSDDVKAGGKAGPGIlgvnlgknktsedaAADYVqgVRALSQYADYLV---------INVSSPNTpglrklqGRK 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 138 PFiyADTLESLLSELDSVERN----VPFWIKM-PHLY--DLKQfdsLLKVIVEHNIRGVTVANLIKDRGKVDLKDPLTDD 210
Cdd:PLN02826 240 QL--KDLLKKVLAARDEMQWGeegpPPLLVKIaPDLSkeDLED---IAAVALALGIDGLIISNTTISRPDSVLGHPHADE 314
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2052594783 211 IrGGLSGEPTRTHSLELIGYTYKNYGDKLTVIGVGGVFRPKTHTLRLRQG 260
Cdd:PLN02826 315 A-GGLSGKPLFDLSTEVLREMYRLTRGKIPLVGCGGVSSGEDAYKKIRAG 363
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
25-247 |
1.98e-14 |
|
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: 71.20 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 25 GGSVTMEPRKGNLRPWFHRLPNtkSVVVYAGMPNYGLEKISDYIELNRSKVK--SMPTVVSVAVIADKstkdefgpvvpe 102
Cdd:cd04741 39 TRSSTLAGRPGNPEPRYYAFPL--GSINSLGLPNLGLDYYLEYIRTISDGLPgsAKPFFISVTGSAED------------ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 103 eyIIRDVKKAVSyiVENSLASVIEINISCPN-AGKEPFIYA-DTLESLLSELDSVERnVPFWIKMPHLYDLKQFDSLLKV 180
Cdd:cd04741 105 --IAAMYKKIAA--HQKQFPLAMELNLSCPNvPGKPPPAYDfDATLEYLTAVKAAYS-IPVGVKTPPYTDPAQFDTLAEA 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2052594783 181 IVEHN--IRGVTVANLI-------KDRGKVDLKdplTDDIRGGLSGEPTRTHSLELIGYTYKNYGDKLTVIGVGGV 247
Cdd:cd04741 180 LNAFAcpISFITATNTLgnglvldPERETVVLK---PKTGFGGLAGAYLHPLALGNVRTFRRLLPSEIQIIGVGGV 252
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
27-247 |
7.93e-12 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 64.20 E-value: 7.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 27 SVTMEPRKGNLRPWFHRLP----NTksvvvyAGMPNYGLEKISDYIELNRSKVKSMPTVVSVAVIAdkstkdefgpvvPE 102
Cdd:PRK02506 44 SATLEPRPGNPEPRYADTPlgsiNS------MGLPNLGFDYYLDYVLELQKKGPNKPHFLSVVGLS------------PE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 103 EyIIRDVKKavsyIVENSLASVIEINISCPN-AGKEPFIYA-DTLESLLSELDSVeRNVPFWIKMPHLYDLKQFDSLLKV 180
Cdd:PRK02506 106 E-THTILKK----IQASDFNGLVELNLSCPNvPGKPQIAYDfETTEQILEEVFTY-FTKPLGVKLPPYFDIVHFDQAAAI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2052594783 181 IVEHNIRGVTVANLIKDRGKVDLKDPlTDDIR-----GGLSGEPTRTHSLELIGYTYKNYGDKLTVIGVGGV 247
Cdd:PRK02506 180 FNKFPLAFVNCINSIGNGLVIDPEDE-TVVIKpkngfGGIGGDYIKPTALANVRAFYQRLNPSIQIIGTGGV 250
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
27-247 |
1.10e-11 |
|
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: 63.60 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 27 SVTMEPRKGNLRPwfhRLPNTKSVVVYA-GMPNYGLEKISDYIELNRSKVKSmPTVVSVAviadKSTKDEFGPVVpeeyi 105
Cdd:TIGR01037 43 SIGLEPRPGYRNP---TIVETPCGMLNAiGLQNPGVEAFLEELKPVREEFPT-PLIASVY----GSSVEEFAEVA----- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 106 iRDVKKAVSYIVenslasVIEINISCPNA-------GKEPFIYADTLESLLSELDsvernVPFWIKM-PHLYDLKQFDsl 177
Cdd:TIGR01037 110 -EKLEKAPPYVD------AYELNLSCPHVkgggiaiGQDPELSADVVKAVKDKTD-----VPVFAKLsPNVTDITEIA-- 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2052594783 178 lKVIVEHNIRGVTVANLIkdRG-KVDLK--DPLTDDIRGGLSGEPTRTHSLELIGYTYKNYGdkLTVIGVGGV 247
Cdd:TIGR01037 176 -KAAEEAGADGLTLINTL--RGmKIDIKtgKPILANKTGGLSGPAIKPIALRMVYDVYKMVD--IPIIGVGGI 243
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
27-248 |
5.17e-11 |
|
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: 61.41 E-value: 5.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 27 SVTMEPRKGNLRPwfhRLPNTKSVVVYA-GMPNYGLEK-ISDYIELNRSKVKsmPTVVSVAviadKSTKDEFgpvvpeey 104
Cdd:cd04740 42 SITLEPREGNPPP---RVVETPGGMLNAiGLQNPGVEAfLEELLPWLREFGT--PVIASIA----GSTVEEF-------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 105 iirdvkKAVSYIVENSLASVIEINISCPNAGKEPFIYADTLESLLSELDSVER--NVPFWIKM-PHLYDLKQfdsLLKVI 181
Cdd:cd04740 105 ------VEVAEKLADAGADAIELNISCPNVKGGGMAFGTDPEAVAEIVKAVKKatDVPVIVKLtPNVTDIVE---IARAA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2052594783 182 VEHNIRGVTVANLIKDrGKVDLKD--PLTDDIRGGLSGEPTRTHSLELIGYTYKNYgdKLTVIGVGGVF 248
Cdd:cd04740 176 EEAGADGLTLINTLKG-MAIDIETrkPILGNVTGGLSGPAIKPIALRMVYQVYKAV--EIPIIGVGGIA 241
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
27-247 |
1.10e-10 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 60.55 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 27 SVTMEPRKGNlrpwfhrlPNTKSVVVYAGM------PNYGLEKISDYIElnrSKVKSMPTVVsVAVIADKStkdefgpvv 100
Cdd:PRK07259 44 STTLEPREGN--------PTPRIAETPGGMlnaiglQNPGVDAFIEEEL---PWLEEFDTPI-IANVAGST--------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 101 PEEYIirdvkKAVSYIVENSLASVIEINISCPNA-------GKEPfiyaDTLESLLSELDSVErNVPFWIKM-PHLYDLK 172
Cdd:PRK07259 103 EEEYA-----EVAEKLSKAPNVDAIELNISCPNVkhggmafGTDP----ELAYEVVKAVKEVV-KVPVIVKLtPNVTDIV 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2052594783 173 QfdsLLKVIVEHNIRGVTVANLIKdrG-KVDLK--DPLTDDIRGGLSGEPTRTHSLELIGYTYKNYgdKLTVIGVGGV 247
Cdd:PRK07259 173 E---IAKAAEEAGADGLSLINTLK--GmAIDIKtrKPILANVTGGLSGPAIKPIALRMVYQVYQAV--DIPIIGMGGI 243
|
|
|