|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
1-341 |
5.29e-176 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 491.98 E-value: 5.29e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 1 MYKLIKPFLFKIEPEKAHGLTIDALKTLQKFPVLfPVVDKLFTYKNPTLSQTIQGNTYDNPIGLAAGFDKSCEVPKALEH 80
Cdd:PRK05286 2 YYPLARPLLFKLDPETAHELTIRALKRASRTPLL-SLLRQRLTYTDPRLPVTVMGLTFPNPVGLAAGFDKNGEAIDALGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 81 LGFGALELGGITPKPQPGNPQPRMFRLLEDDALINRMGFNNIGMNKALSHLRKNAYQVPVGINVGVNKMTPYEARYQDYI 160
Cdd:PRK05286 81 LGFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKAYRGIPLGINIGKNKDTPLEDAVDDYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 161 KVIDTFKHDVSFFTVNISSPNTENLQNFHDKDEFSMLCQALTTFKKQHDVTVPIYLKLTSDMDFDGLKALLPAITET-FD 239
Cdd:PRK05286 161 ICLEKLYPYADYFTVNISSPNTPGLRDLQYGEALDELLAALKEAQAELHGYVPLLVKIAPDLSDEELDDIADLALEHgID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 240 GIILANTTRQRDGLTS-ANKVEEGGLSGRPLFERNLKLIKYAYQQTNGEFLIIGTGGVFSTEDAIKMMRHGASLIQIYSS 318
Cdd:PRK05286 241 GVIATNTTLSRDGLKGlPNADEAGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGASLVQIYSG 320
|
330 340
....*....|....*....|...
gi 21205681 319 LVIEGPGLTKKMNKGIARYLKDH 341
Cdd:PRK05286 321 LIYEGPGLVKEIVRGLARLLRRD 343
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
6-334 |
1.73e-150 |
|
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: 426.92 E-value: 1.73e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 6 KPFLFKIEPEKAHGLTIDALKTLQKFPVLFpvvdkLFTYKNPTLSQTIQGNTYDNPIGLAAGFDKSCEVPKALEHLGFGA 85
Cdd:cd04738 1 RPLLFLLDPETAHRLAIRALKLGLGPPLLL-----LLVYDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 86 LELGGITPKPQPGNPQPRMFRLLEDDALINRMGFNNIGMNKALSHLRK-NAYQVPVGINVGVNKMTPYEARYQDYIKVID 164
Cdd:cd04738 76 VEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKrRPRGGPLGVNIGKNKDTPLEDAVEDYVIGVR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 165 TFKHDVSFFTVNISSPNTENLQNFHDKDEFSMLCQALTTFKKQHDVTVPIYLKLTSDMDFDGLKALLPAITET-FDGIIL 243
Cdd:cd04738 156 KLGPYADYLVVNVSSPNTPGLRDLQGKEALRELLTAVKEERNKLGKKVPLLVKIAPDLSDEELEDIADVALEHgVDGIIA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 244 ANTTRQRDGLT-SANKVEEGGLSGRPLFERNLKLIKYAYQQTNGEFLIIGTGGVFSTEDAIKMMRHGASLIQIYSSLVIE 322
Cdd:cd04738 236 TNTTISRPGLLrSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTGLVYE 315
|
330
....*....|..
gi 21205681 323 GPGLTKKMNKGI 334
Cdd:cd04738 316 GPGLVKRIKREL 327
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
49-347 |
4.88e-102 |
|
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: 302.38 E-value: 4.88e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 49 LSQTIQGNTYDNPIGLAAGF-DKSCEVPKALEHLGFGALELGGITPKPQPGNPQPRMFRLLEDDALINRMGFNNIGMNKA 127
Cdd:COG0167 2 LSVELAGLKFPNPVGLASGFfDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 128 LSHLRKN-AYQVPVGINVGvnKMTPyearyQDYIKVIDTFK-HDVSFFTVNISSPNTEN-LQNF-HDKDEFSMLCQALtt 203
Cdd:COG0167 82 LERLLPAkRYDVPVIVNIG--GNTV-----EDYVELARRLAdAGADYLELNISCPNTPGgGRALgQDPEALAELLAAV-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 204 fkKQHdVTVPIYLKLTSDMDfdGLKALLPAITET-FDGIILANTTRQRD-GLTSANKV---EEGGLSGRPLFERNLKLIK 278
Cdd:COG0167 153 --KAA-TDKPVLVKLAPDLT--DIVEIARAAEEAgADGVIAINTTLGRAiDLETRRPVlanEAGGLSGPALKPIALRMVR 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21205681 279 YAYQQTNGEFLIIGTGGVFSTEDAIKMMRHGASLIQIYSSLVIEGPGLTKKMNKGIARYLKDHHFDNVS 347
Cdd:COG0167 228 EVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSIS 296
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
2-334 |
1.02e-92 |
|
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: 280.13 E-value: 1.02e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 2 YKLIKPFLFKIEPEKAHGLTIDALKTLQKFPVLfPVVDKLFTYKNPtLSQTIQGNTYDNPIGLAAGFDKSCEVPKALEHL 81
Cdd:TIGR01036 1 YPLVRKLLFLLDPESAHELTFQFLRLGTGTPFL-ALLRSLFGASDP-LEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 82 GFGALELGGITPKPQPGNPQPRMFRLLEDDALINRMGFNNIGMNKALSHLRKNAYQVPVGINVGVNKMTPYEARYQDYIK 161
Cdd:TIGR01036 79 GFGFLEIGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLKRARYKGPIGINIGKNKDTPSEDAKEDYAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 162 VIDTFKHDVSFFTVNISSPNTENLQNFHDKDEF-SMLCQALT-TFKKQHDVTVPIYLKLTSDMDFDGLKALLPAITE-TF 238
Cdd:TIGR01036 159 CLRKLGPLADYLVVNVSSPNTPGLRDLQYKAELrDLLTAVKQeQDGLRRVHRVPVLVKIAPDLTESDLEDIADSLVElGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 239 DGIILANTTRQRDGLTSA-NKVEEGGLSGRPLFERNLKLIKYAYQQTNGEFLIIGTGGVFSTEDAIKMMRHGASLIQIYS 317
Cdd:TIGR01036 239 DGVIATNTTVSRSLVQGPkNSDETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGASLLQIYS 318
|
330
....*....|....*..
gi 21205681 318 SLVIEGPGLTKKMNKGI 334
Cdd:TIGR01036 319 GFIYWGPPLVKEIVKEI 335
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
49-338 |
2.44e-70 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 221.45 E-value: 2.44e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 49 LSQTIQGNTYDNPIGLAAGFDKSCEVPKALEHLG-FGALELGGITPKPQPGNPQPRMFRLLEDdaLINRMGFNNIGMNKA 127
Cdd:pfam01180 2 LATKIPGLDFKNPIGLASGFDKFGEEALKWLALGkFGAIEIKSVTPYPQPGNPTPRVFRLPEG--VLNRMGLNNPGLDAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 128 LSHL---RKNAYQVPVGINVGVNKMTpyearYQDYIKVIDTFKHDVSFFTVNISSPNTENLQNFHDKDEFS-MLCQALTT 203
Cdd:pfam01180 80 LAELlkrRKEYPRPDLGINLSKAGMT-----VDDYVEVARKIGPFADYIELNVSCPNTPGLRALQTDPELAaILLKVVKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 204 FKKqhdvtVPIYLKLTSDMdFDGLK---ALLPAITETFDGIILANTTRQRDGL---TSANKVEE--GGLSGRPLFERNLK 275
Cdd:pfam01180 155 VSK-----VPVLVKLAPDL-TDIVIidiADVALGEDGLDGINATNTTVRGMRIdlkTEKPILANgtGGLSGPPIKPIALK 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21205681 276 LIKYAYQQTNGEFLIIGTGGVFSTEDAIKMMRHGASLIQIYSSLVIEGPGLTKKMNKGIARYL 338
Cdd:pfam01180 229 VIRELYQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| dihydoor_dh_Arch |
NF041011 |
dihydroorotate dehydrogenase PyrD; |
53-352 |
1.33e-20 |
|
dihydroorotate dehydrogenase PyrD;
Pssm-ID: 468940 Cd Length: 289 Bit Score: 90.38 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 53 IQGNTYDNPIGLAAGFDKSceVPKALEHL----GFGALELGGITPKPQPGNPQPRMFRLlEDDALINRMGFNNIGMnKAL 128
Cdd:NF041011 3 LAGLELEDPLIIASGILPD--VPEYIERVcekyGPSAITTKTLTLNPLEPHKPPTVVKL-HDGCYLNAIGLGNPGI-GLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 129 SHLRKNAYQVPVGINvGVNKmtpyearyQDYIKVIDTFKHDVSFFTVNISSPNTENLqnfhdKDEFSMLCQALTTFKKQH 208
Cdd:NF041011 79 EEIRVKLCPLIVSIG-GSSL--------EEIVEVAEIAEEKADAIELNLSSPNRKGY-----GASLASLVREIVKAVKSV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 209 dVTVPIYLKL-TSD--MDFDGlKALLPAItetfDGIILANTTRqrdGLtsANKVEE---------GGLSGRPLFERNLKL 276
Cdd:NF041011 145 -VKKPVFVKLgPWDnvLEIAG-KALEAGA----DGLTLINTVK---GM--AIDVESfkpvlsygtGGISGKCIHPLAVRI 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21205681 277 IKYAYQQTNGEflIIGTGGVFSTEDAIKMMRHGASLIQIYSSLVIEGPGLTKKMNKGIARYLKDHHFdNVSDIIGL 352
Cdd:NF041011 214 IYDVYREYEAE--IIGVGGVFSWRDAIELMSVGAKAVGVGTAIIDKGLSVISEIRKGLEEYLEEKGL-KLEDIIGI 286
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
1-341 |
5.29e-176 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 491.98 E-value: 5.29e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 1 MYKLIKPFLFKIEPEKAHGLTIDALKTLQKFPVLfPVVDKLFTYKNPTLSQTIQGNTYDNPIGLAAGFDKSCEVPKALEH 80
Cdd:PRK05286 2 YYPLARPLLFKLDPETAHELTIRALKRASRTPLL-SLLRQRLTYTDPRLPVTVMGLTFPNPVGLAAGFDKNGEAIDALGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 81 LGFGALELGGITPKPQPGNPQPRMFRLLEDDALINRMGFNNIGMNKALSHLRKNAYQVPVGINVGVNKMTPYEARYQDYI 160
Cdd:PRK05286 81 LGFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKAYRGIPLGINIGKNKDTPLEDAVDDYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 161 KVIDTFKHDVSFFTVNISSPNTENLQNFHDKDEFSMLCQALTTFKKQHDVTVPIYLKLTSDMDFDGLKALLPAITET-FD 239
Cdd:PRK05286 161 ICLEKLYPYADYFTVNISSPNTPGLRDLQYGEALDELLAALKEAQAELHGYVPLLVKIAPDLSDEELDDIADLALEHgID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 240 GIILANTTRQRDGLTS-ANKVEEGGLSGRPLFERNLKLIKYAYQQTNGEFLIIGTGGVFSTEDAIKMMRHGASLIQIYSS 318
Cdd:PRK05286 241 GVIATNTTLSRDGLKGlPNADEAGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGASLVQIYSG 320
|
330 340
....*....|....*....|...
gi 21205681 319 LVIEGPGLTKKMNKGIARYLKDH 341
Cdd:PRK05286 321 LIYEGPGLVKEIVRGLARLLRRD 343
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
6-334 |
1.73e-150 |
|
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: 426.92 E-value: 1.73e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 6 KPFLFKIEPEKAHGLTIDALKTLQKFPVLFpvvdkLFTYKNPTLSQTIQGNTYDNPIGLAAGFDKSCEVPKALEHLGFGA 85
Cdd:cd04738 1 RPLLFLLDPETAHRLAIRALKLGLGPPLLL-----LLVYDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 86 LELGGITPKPQPGNPQPRMFRLLEDDALINRMGFNNIGMNKALSHLRK-NAYQVPVGINVGVNKMTPYEARYQDYIKVID 164
Cdd:cd04738 76 VEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKrRPRGGPLGVNIGKNKDTPLEDAVEDYVIGVR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 165 TFKHDVSFFTVNISSPNTENLQNFHDKDEFSMLCQALTTFKKQHDVTVPIYLKLTSDMDFDGLKALLPAITET-FDGIIL 243
Cdd:cd04738 156 KLGPYADYLVVNVSSPNTPGLRDLQGKEALRELLTAVKEERNKLGKKVPLLVKIAPDLSDEELEDIADVALEHgVDGIIA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 244 ANTTRQRDGLT-SANKVEEGGLSGRPLFERNLKLIKYAYQQTNGEFLIIGTGGVFSTEDAIKMMRHGASLIQIYSSLVIE 322
Cdd:cd04738 236 TNTTISRPGLLrSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTGLVYE 315
|
330
....*....|..
gi 21205681 323 GPGLTKKMNKGI 334
Cdd:cd04738 316 GPGLVKRIKREL 327
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
49-347 |
4.88e-102 |
|
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: 302.38 E-value: 4.88e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 49 LSQTIQGNTYDNPIGLAAGF-DKSCEVPKALEHLGFGALELGGITPKPQPGNPQPRMFRLLEDDALINRMGFNNIGMNKA 127
Cdd:COG0167 2 LSVELAGLKFPNPVGLASGFfDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 128 LSHLRKN-AYQVPVGINVGvnKMTPyearyQDYIKVIDTFK-HDVSFFTVNISSPNTEN-LQNF-HDKDEFSMLCQALtt 203
Cdd:COG0167 82 LERLLPAkRYDVPVIVNIG--GNTV-----EDYVELARRLAdAGADYLELNISCPNTPGgGRALgQDPEALAELLAAV-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 204 fkKQHdVTVPIYLKLTSDMDfdGLKALLPAITET-FDGIILANTTRQRD-GLTSANKV---EEGGLSGRPLFERNLKLIK 278
Cdd:COG0167 153 --KAA-TDKPVLVKLAPDLT--DIVEIARAAEEAgADGVIAINTTLGRAiDLETRRPVlanEAGGLSGPALKPIALRMVR 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21205681 279 YAYQQTNGEFLIIGTGGVFSTEDAIKMMRHGASLIQIYSSLVIEGPGLTKKMNKGIARYLKDHHFDNVS 347
Cdd:COG0167 228 EVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSIS 296
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
2-334 |
1.02e-92 |
|
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: 280.13 E-value: 1.02e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 2 YKLIKPFLFKIEPEKAHGLTIDALKTLQKFPVLfPVVDKLFTYKNPtLSQTIQGNTYDNPIGLAAGFDKSCEVPKALEHL 81
Cdd:TIGR01036 1 YPLVRKLLFLLDPESAHELTFQFLRLGTGTPFL-ALLRSLFGASDP-LEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 82 GFGALELGGITPKPQPGNPQPRMFRLLEDDALINRMGFNNIGMNKALSHLRKNAYQVPVGINVGVNKMTPYEARYQDYIK 161
Cdd:TIGR01036 79 GFGFLEIGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLKRARYKGPIGINIGKNKDTPSEDAKEDYAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 162 VIDTFKHDVSFFTVNISSPNTENLQNFHDKDEF-SMLCQALT-TFKKQHDVTVPIYLKLTSDMDFDGLKALLPAITE-TF 238
Cdd:TIGR01036 159 CLRKLGPLADYLVVNVSSPNTPGLRDLQYKAELrDLLTAVKQeQDGLRRVHRVPVLVKIAPDLTESDLEDIADSLVElGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 239 DGIILANTTRQRDGLTSA-NKVEEGGLSGRPLFERNLKLIKYAYQQTNGEFLIIGTGGVFSTEDAIKMMRHGASLIQIYS 317
Cdd:TIGR01036 239 DGVIATNTTVSRSLVQGPkNSDETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGASLLQIYS 318
|
330
....*....|....*..
gi 21205681 318 SLVIEGPGLTKKMNKGI 334
Cdd:TIGR01036 319 GFIYWGPPLVKEIVKEI 335
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
1-353 |
4.83e-83 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 258.13 E-value: 4.83e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 1 MYKLIKPFLFKIEPEKAHGLTIDALKtlqkfpvlfpvVDKLFTYKNPT---LSQTIQGNTYDNPIGLAAGFDKSCEVPKA 77
Cdd:PLN02826 34 ATKLVNPLFRLLDPETAHSLAISAAA-----------RGLVPREKRPDpsvLGVEVWGRTFSNPIGLAAGFDKNAEAVEG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 78 LEHLGFGALELGGITPKPQPGNPQPRMFRLLEDDALINRMGFNNIGMNKALSHL------------------------RK 133
Cdd:PLN02826 103 LLGLGFGFVEIGSVTPLPQPGNPKPRVFRLREEGAIINRYGFNSEGIVAVAKRLgaqhgkrkldetssssfssddvkaGG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 134 NAYQVPVGINVGVNKMTpyEARYQDYIKVIDTFKHDVSFFTVNISSPNTENLQNFHDKDEFSMLCQALTTFK----KQHD 209
Cdd:PLN02826 183 KAGPGILGVNLGKNKTS--EDAAADYVQGVRALSQYADYLVINVSSPNTPGLRKLQGRKQLKDLLKKVLAARdemqWGEE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 210 VTVPIYLKLTSDMDFDGLKALLPAITET-FDGIILANTTRQRDGLTSANKV--EEGGLSGRPLFERNLKLIKYAYQQTNG 286
Cdd:PLN02826 261 GPPPLLVKIAPDLSKEDLEDIAAVALALgIDGLIISNTTISRPDSVLGHPHadEAGGLSGKPLFDLSTEVLREMYRLTRG 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21205681 287 EFLIIGTGGVFSTEDAIKMMRHGASLIQIYSSLVIEGPGLTKKMNKGIARYLKDHHFDNVSDIIGLD 353
Cdd:PLN02826 341 KIPLVGCGGVSSGEDAYKKIRAGASLVQLYTAFAYEGPALIPRIKAELAACLERDGFKSIQEAVGAD 407
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
49-338 |
2.44e-70 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 221.45 E-value: 2.44e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 49 LSQTIQGNTYDNPIGLAAGFDKSCEVPKALEHLG-FGALELGGITPKPQPGNPQPRMFRLLEDdaLINRMGFNNIGMNKA 127
Cdd:pfam01180 2 LATKIPGLDFKNPIGLASGFDKFGEEALKWLALGkFGAIEIKSVTPYPQPGNPTPRVFRLPEG--VLNRMGLNNPGLDAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 128 LSHL---RKNAYQVPVGINVGVNKMTpyearYQDYIKVIDTFKHDVSFFTVNISSPNTENLQNFHDKDEFS-MLCQALTT 203
Cdd:pfam01180 80 LAELlkrRKEYPRPDLGINLSKAGMT-----VDDYVEVARKIGPFADYIELNVSCPNTPGLRALQTDPELAaILLKVVKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 204 FKKqhdvtVPIYLKLTSDMdFDGLK---ALLPAITETFDGIILANTTRQRDGL---TSANKVEE--GGLSGRPLFERNLK 275
Cdd:pfam01180 155 VSK-----VPVLVKLAPDL-TDIVIidiADVALGEDGLDGINATNTTVRGMRIdlkTEKPILANgtGGLSGPPIKPIALK 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21205681 276 LIKYAYQQTNGEFLIIGTGGVFSTEDAIKMMRHGASLIQIYSSLVIEGPGLTKKMNKGIARYL 338
Cdd:pfam01180 229 VIRELYQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
55-333 |
8.28e-41 |
|
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: 144.80 E-value: 8.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 55 GNTYDNPIGLAAGFD-KSCEVPKALEHLGFGALELGGITPKPQPGNPQPRMFRL-------LEDDALINRMGFNNIGMNK 126
Cdd:cd02810 5 GLKLKNPFGVAAGPLlKTGELIARAAAAGFGAVVYKTVTLHPRPGNPLPRVARLppegesyPEQLGILNSFGLPNLGLDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 127 ALSHLRKNAYQV---PVGINVGvnkMTPYEARYQDYIKVIDTFkhdVSFFTVNISSPNT-ENLQNFHDKDEFSMLCQALT 202
Cdd:cd02810 85 WLQDIAKAKKEFpgqPLIASVG---GSSKEDYVELARKIERAG---AKALELNLSCPNVgGGRQLGQDPEAVANLLKAVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 203 TFkkqhdVTVPIYLKLTSDMDFDGLKALLPAITE-TFDGIILANTTRQRDGLTSA----NKVEEGGLSGRPLFERNLKLI 277
Cdd:cd02810 159 AA-----VDIPLLVKLSPYFDLEDIVELAKAAERaGADGLTAINTISGRVVDLKTvgpgPKRGTGGLSGAPIRPLALRWV 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 21205681 278 KYAYQQTNGEFLIIGTGGVFSTEDAIKMMRHGASLIQIYSSLVIEGPGLTKKMNKG 333
Cdd:cd02810 234 ARLAARLQLDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKIKKE 289
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
60-352 |
3.71e-35 |
|
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: 129.98 E-value: 3.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 60 NPIGLAAG-FDKSCEVPKALEHLGFGALELGGITPKPQPGNPQPRMFRLleDDALINRMGFNNIGMNKALSHLR--KNAY 136
Cdd:cd04740 11 NPVILASGtFGFGEELSRVADLGKLGAIVTKSITLEPREGNPPPRVVET--PGGMLNAIGLQNPGVEAFLEELLpwLREF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 137 QVPVGINVGVNkmTPyearyQDYIKVIDTF-KHDVSFFTVNISSPNTENL-QNF-HDKDefsmLCQALT-TFKKQhdVTV 212
Cdd:cd04740 89 GTPVIASIAGS--TV-----EEFVEVAEKLaDAGADAIELNISCPNVKGGgMAFgTDPE----AVAEIVkAVKKA--TDV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 213 PIYLKLTSDMDfDGLKALLPAITETFDGIILANT---------TRQRDgLtsANKVeeGGLSGRPLFERNLKLIKYAYQQ 283
Cdd:cd04740 156 PVIVKLTPNVT-DIVEIARAAEEAGADGLTLINTlkgmaidieTRKPI-L--GNVT--GGLSGPAIKPIALRMVYQVYKA 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21205681 284 TNGEflIIGTGGVFSTEDAIKMMRHGASLIQIySSLVIEGPGLTKKMNKGIARYLKDHHFDNVSDIIGL 352
Cdd:cd04740 230 VEIP--IIGVGGIASGEDALEFLMAGASAVQV-GTANFVDPEAFKEIIEGLEAYLDEEGIKSIEELVGL 295
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
49-352 |
1.05e-30 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 118.33 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 49 LSQTIQGNTYDNPIGLAAG-FDKSCEVPKALEHLGFGALELGGITPKPQPGNPQPRMFRLleDDALINRMGFNNIGMNKA 127
Cdd:PRK07259 2 LSVELPGLKLKNPVMPASGtFGFGGEYARFYDLNGLGAIVTKSTTLEPREGNPTPRIAET--PGGMLNAIGLQNPGVDAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 128 LSHLR--KNAYQVPVGINVGVNkmTPyearyQDYIKV---IDTFKHdVSFFTVNISSPNTEnlqnfhdkdEFSM------ 196
Cdd:PRK07259 80 IEEELpwLEEFDTPIIANVAGS--TE-----EEYAEVaekLSKAPN-VDAIELNISCPNVK---------HGGMafgtdp 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 197 -LCQALTTFKKQHdVTVPIYLKLT---SDmdfdglkallpaITET--------FDGIILANT---------TRqRDGLts 255
Cdd:PRK07259 143 eLAYEVVKAVKEV-VKVPVIVKLTpnvTD------------IVEIakaaeeagADGLSLINTlkgmaidikTR-KPIL-- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 256 ANKVeeGGLSGRPLFERNLKLIKYAYQQTNGEflIIGTGGVFSTEDAIKMMRHGASLIQIYSSLVIeGPGLTKKMNKGIA 335
Cdd:PRK07259 207 ANVT--GGLSGPAIKPIALRMVYQVYQAVDIP--IIGMGGISSAEDAIEFIMAGASAVQVGTANFY-DPYAFPKIIEGLE 281
|
330
....*....|....*..
gi 21205681 336 RYLKDHHFDNVSDIIGL 352
Cdd:PRK07259 282 AYLDKYGIKSIEEIVGI 298
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
49-352 |
1.04e-25 |
|
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: 104.82 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 49 LSQTIQGNTYDNPIGLAAG-FDKSCEVPKALEHLGFGALELGGITPKPQPGNPQPRMFRLleDDALINRMGFNNIGMNKA 127
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGiMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTIVET--PCGMLNAIGLQNPGVEAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 128 LSHLRKNAYQVPVGINVGVNKMTPYEarYQDYIKVIDTFKHDVSFFTVNISSPN--TENLQNFHDKDEFSMLCQALttfK 205
Cdd:TIGR01037 79 LEELKPVREEFPTPLIASVYGSSVEE--FAEVAEKLEKAPPYVDAYELNLSCPHvkGGGIAIGQDPELSADVVKAV---K 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 206 KQHDVtvPIYLKLTSDMDfDGLKALLPAITETFDGIILANTTR--QRDGLTS----ANKVeeGGLSGRPLFERNLKLIKY 279
Cdd:TIGR01037 154 DKTDV--PVFAKLSPNVT-DITEIAKAAEEAGADGLTLINTLRgmKIDIKTGkpilANKT--GGLSGPAIKPIALRMVYD 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21205681 280 AYQQTNgeFLIIGTGGVFSTEDAIKMMRHGASLIQIYSSLVIEgPGLTKKMNKGIARYLKDHHFDNVSDIIGL 352
Cdd:TIGR01037 229 VYKMVD--IPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYR-GFAFKKIIEGLIAFLKAEGFTSIEELIGI 298
|
|
| dihydoor_dh_Arch |
NF041011 |
dihydroorotate dehydrogenase PyrD; |
53-352 |
1.33e-20 |
|
dihydroorotate dehydrogenase PyrD;
Pssm-ID: 468940 Cd Length: 289 Bit Score: 90.38 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 53 IQGNTYDNPIGLAAGFDKSceVPKALEHL----GFGALELGGITPKPQPGNPQPRMFRLlEDDALINRMGFNNIGMnKAL 128
Cdd:NF041011 3 LAGLELEDPLIIASGILPD--VPEYIERVcekyGPSAITTKTLTLNPLEPHKPPTVVKL-HDGCYLNAIGLGNPGI-GLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 129 SHLRKNAYQVPVGINvGVNKmtpyearyQDYIKVIDTFKHDVSFFTVNISSPNTENLqnfhdKDEFSMLCQALTTFKKQH 208
Cdd:NF041011 79 EEIRVKLCPLIVSIG-GSSL--------EEIVEVAEIAEEKADAIELNLSSPNRKGY-----GASLASLVREIVKAVKSV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 209 dVTVPIYLKL-TSD--MDFDGlKALLPAItetfDGIILANTTRqrdGLtsANKVEE---------GGLSGRPLFERNLKL 276
Cdd:NF041011 145 -VKKPVFVKLgPWDnvLEIAG-KALEAGA----DGLTLINTVK---GM--AIDVESfkpvlsygtGGISGKCIHPLAVRI 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21205681 277 IKYAYQQTNGEflIIGTGGVFSTEDAIKMMRHGASLIQIYSSLVIEGPGLTKKMNKGIARYLKDHHFdNVSDIIGL 352
Cdd:NF041011 214 IYDVYREYEAE--IIGVGGVFSWRDAIELMSVGAKAVGVGTAIIDKGLSVISEIRKGLEEYLEEKGL-KLEDIIGI 286
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
52-336 |
2.17e-16 |
|
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: 78.52 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 52 TIQGNTYDNPIGLAAGfdKSCEVPKALEHL---GFGALELGGITPKPQPGNPQPRMFRLleDDALINRMGFNNIGMNKAL 128
Cdd:cd04741 2 TPPGLTISPPLMNAAG--PWCTTLEDLLELaasSTGAVTTRSSTLAGRPGNPEPRYYAF--PLGSINSLGLPNLGLDYYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 129 SHLRKNAYQVPV---GINVGVNKMTpyEARYQDYIKVIDTFKHDVSFFTVNISSPNTENL-QNFHDKDEFSMLCQALTTF 204
Cdd:cd04741 78 EYIRTISDGLPGsakPFFISVTGSA--EDIAAMYKKIAAHQKQFPLAMELNLSCPNVPGKpPPAYDFDATLEYLTAVKAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 205 kkqhdVTVPIYLKLT--SDMD-FDGLKALLPAI---------TETFDGIILANTTRQRDGLTSANKVeeGGLSGRPLFER 272
Cdd:cd04741 156 -----YSIPVGVKTPpyTDPAqFDTLAEALNAFacpisfitaTNTLGNGLVLDPERETVVLKPKTGF--GGLAGAYLHPL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21205681 273 NLKLIKYAYQQTNGEFLIIGTGGVFSTEDAIKMMRHGASLIQIYSSLVIEGPGLTKKMNKGIAR 336
Cdd:cd04741 229 ALGNVRTFRRLLPSEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEKELED 292
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
49-351 |
3.89e-11 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 63.05 E-value: 3.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 49 LSQTIQGNTYDNPIGLAAGFdkSCEVPKALEHLG---FGALELGGITPKPQPGNPQPRMFRLleddAL--INRMGFNNIG 123
Cdd:PRK02506 2 TSTQIAGFKFDNCLMNAAGV--YCMTKEELEEVEasaAGAFVTKSATLEPRPGNPEPRYADT----PLgsINSMGLPNLG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 124 MNKALSHLRKNAYQVPVG-INVGVNKMTPYE-------ARYQDYIKVIDtfkhdvsfftVNISSPNTENLQ----NFHDK 191
Cdd:PRK02506 76 FDYYLDYVLELQKKGPNKpHFLSVVGLSPEEthtilkkIQASDFNGLVE----------LNLSCPNVPGKPqiayDFETT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 192 DEFsmLCQALTTFKKQHDVTVPIYLKLTSdmdFDGLKALL---P-----AITETFDGIILANTTRQ-----RDGLtsank 258
Cdd:PRK02506 146 EQI--LEEVFTYFTKPLGVKLPPYFDIVH---FDQAAAIFnkfPlafvnCINSIGNGLVIDPEDETvvikpKNGF----- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 259 veeGGLSGRPLFERNLKLIKYAYQQTNGEFLIIGTGGVFSTEDAIKMMRHGASLIQIYSSLVIEGPGLTKKMNKGIARYL 338
Cdd:PRK02506 216 ---GGIGGDYIKPTALANVRAFYQRLNPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAIM 292
|
330
....*....|...
gi 21205681 339 KDHHFDNVSDIIG 351
Cdd:PRK02506 293 AEKGYQSLEDFRG 305
|
|
| PRK07565 |
PRK07565 |
dihydroorotate dehydrogenase-like protein; |
293-351 |
2.49e-09 |
|
dihydroorotate dehydrogenase-like protein;
Pssm-ID: 236051 Cd Length: 334 Bit Score: 57.95 E-value: 2.49e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 21205681 293 TGGVFSTEDAIKMMRHGASLIQIYSSLVIEGPGLTKKMNKGIARYLKDHHFDNVSDIIG 351
Cdd:PRK07565 245 TTGVHDAEDVIKMLLAGADVVMIASALLRHGPDYIGTILRGLEDWMERHGYESLQQFRG 303
|
|
| DHOD_like |
cd04739 |
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
293-351 |
2.86e-08 |
|
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: 54.54 E-value: 2.86e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 21205681 293 TGGVFSTEDAIKMMRHGASLIQIYSSLVIEGPGLTKKMNKGIARYLKDHHFDNVSDIIG 351
Cdd:cd04739 243 SGGVHDAEDVVKYLLAGADVVMTTSALLRHGPDYIGTLLAGLEAWMEEHGYESVQQLRG 301
|
|
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
210-333 |
4.02e-05 |
|
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: 44.97 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 210 VTVPIYLKLT---SDMDF----------DGLKAllpaiTETFDGIILANTTRQRDGLTSANKVEEGGLSG---RPLferN 273
Cdd:cd02940 167 VKIPVIAKLTpniTDIREiaraakeggaDGVSA-----INTVNSLMGVDLDGTPPAPGVEGKTTYGGYSGpavKPI---A 238
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21205681 274 LKLIKYAYQQTNGEFLIIGTGGVFSTEDAIKMMRHGASLIQIYSSLVIEGPGLTKKMNKG 333
Cdd:cd02940 239 LRAVSQIARAPEPGLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTG 298
|
|
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
292-352 |
1.92e-04 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 42.90 E-value: 1.92e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21205681 292 GTGGVFSTEDAIKMMRHGASLIQIYSSLVIEGPGLTKKMNKGIARYLKDHHFDNVSDIIGL 352
Cdd:PLN02495 275 GIGGVETGGDAAEFILLGADTVQVCTGVMMHGYPLVKNLCAELQDFMKKHNFSSIEDFRGA 335
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| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
290-352 |
4.53e-04 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 41.85 E-value: 4.53e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21205681 290 IIGTGGVFSTEDAIKMMRHGASLIQIYSSLVIEGPGLTKKMNKGIARYLKDHHFDNVSDIIGL 352
Cdd:PRK08318 256 ISGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISGLSHYMDEKGFASLEDMVGL 318
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| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
271-333 |
1.56e-03 |
|
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 240086 [Multi-domain] Cd Length: 353 Bit Score: 39.89 E-value: 1.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21205681 271 ERNLKLIKYAYQQTNGEFLIIGTGGVFSTEDAIKMMRHGASLIQIYSSLVIEgPGLTKKMNKG 333
Cdd:cd04735 268 DDNQTIMELVKERIAGRLPLIAVGSINTPDDALEALETGADLVAIGRGLLVD-PDWVEKIKEG 329
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