|
Name |
Accession |
Description |
Interval |
E-value |
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
43-368 |
0e+00 |
|
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: 527.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 43 MPVVRCIDPERAHNVAVFATKFALVSSGP---YQDSARLKTTVWGLDFNNPIGMAAGFDKQGEAVNGLHKIGFGFVEVGS 119
Cdd:cd04738 1 RPLLFLLDPETAHRLAIRALKLGLGPPLLlllVYDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFVEVGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 120 VTPEPQDGNPKPRVFRLQEDKAVINRYGFNSDGHEVVYERLRNVKNGPefvGVVGVNLGKNKTT--SDHVQDYVEGVKKF 197
Cdd:cd04738 81 VTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRRPRG---GPLGVNIGKNKDTplEDAVEDYVIGVRKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 198 GEVADYFVINVSSPNTPGLRSLQAKENLEELITKVKAASENLPKKPPLLVKLAPDLSDQERQDVADVINSSKcrVDGLVI 277
Cdd:cd04738 158 GPYADYLVVNVSSPNTPGLRDLQGKEALRELLTAVKEERNKLGKKVPLLVKIAPDLSDEELEDIADVALEHG--VDGIIA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 278 SNTTIDRPNLMSSE-KEENGGLSGAPLANLSTAMIADMYRRTHGKIPIIGVGGIFSGADAYEKIKSGASLVQIYTSYIYH 356
Cdd:cd04738 236 TNTTISRPGLLRSPlANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTGLVYE 315
|
330
....*....|..
gi 2194834072 357 GPPIVTRIKKEL 368
Cdd:cd04738 316 GPGLVKRIKREL 327
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
37-376 |
9.61e-178 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 498.15 E-value: 9.61e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 37 FYEDFLMPVVRCIDPERAHNVAVFATKFA--------LVSSGPYQDSaRLKTTVWGLDFNNPIGMAAGFDKQGEAVNGLH 108
Cdd:PRK05286 1 MYYPLARPLLFKLDPETAHELTIRALKRAsrtpllslLRQRLTYTDP-RLPVTVMGLTFPNPVGLAAGFDKNGEAIDALG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 109 KIGFGFVEVGSVTPEPQDGNPKPRVFRLQEDKAVINRYGFNSDGHEVVYERLRNVKNGPefvgVVGVNLGKNKTTS--DH 186
Cdd:PRK05286 80 ALGFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKAYRGI----PLGINIGKNKDTPleDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 187 VQDYVEGVKKFGEVADYFVINVSSPNTPGLRSLQAKENLEELITKVKAASENLPKKPPLLVKLAPDLSDQERQDVADVIN 266
Cdd:PRK05286 156 VDDYLICLEKLYPYADYFTVNISSPNTPGLRDLQYGEALDELLAALKEAQAELHGYVPLLVKIAPDLSDEELDDIADLAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 267 SSKcrVDGLVISNTTIDRPNLMSSE-KEENGGLSGAPLANLSTAMIADMYRRTHGKIPIIGVGGIFSGADAYEKIKSGAS 345
Cdd:PRK05286 236 EHG--IDGVIATNTTLSRDGLKGLPnADEAGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGAS 313
|
330 340 350
....*....|....*....|....*....|.
gi 2194834072 346 LVQIYTSYIYHGPPIVTRIKKELDELLVKDG 376
Cdd:PRK05286 314 LVQIYSGLIYEGPGLVKEIVRGLARLLRRDG 344
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
49-368 |
3.94e-129 |
|
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: 374.51 E-value: 3.94e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 49 IDPERAHNVAVFATKfaLVSSGPY--------QDSARLKTTVWGLDFNNPIGMAAGFDKQGEAVNGLHKIGFGFVEVGSV 120
Cdd:TIGR01036 11 LDPESAHELTFQFLR--LGTGTPFlallrslfGASDPLEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAMGFGFLEIGTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 121 TPEPQDGNPKPRVFRLQEDKAVINRYGFNSDGHEVVYERLRNVKNGpefvGVVGVNLGKNKTTS--DHVQDYVEGVKKFG 198
Cdd:TIGR01036 89 TPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLKRARYK----GPIGINIGKNKDTPseDAKEDYAACLRKLG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 199 EVADYFVINVSSPNTPGLRSLQAKENLEELITKVKAASENLP--KKPPLLVKLAPDLSDQERQDVADVINSSKcrVDGLV 276
Cdd:TIGR01036 165 PLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAVKQEQDGLRrvHRVPVLVKIAPDLTESDLEDIADSLVELG--IDGVI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 277 ISNTTIDRPNLMSSEK-EENGGLSGAPLANLSTAMIADMYRRTHGKIPIIGVGGIFSGADAYEKIKSGASLVQIYTSYIY 355
Cdd:TIGR01036 243 ATNTTVSRSLVQGPKNsDETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGASLLQIYSGFIY 322
|
330
....*....|...
gi 2194834072 356 HGPPIVTRIKKEL 368
Cdd:TIGR01036 323 WGPPLVKEIVKEI 335
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
78-380 |
3.13e-118 |
|
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: 345.13 E-value: 3.13e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 78 LKTTVWGLDFNNPIGMAAGF-DKQGEAVNGLHKIGFGFVEVGSVTPEPQDGNPKPRVFRLQEDKAVINRYGFNSDGHEVV 156
Cdd:COG0167 2 LSVELAGLKFPNPVGLASGFfDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 157 YERLRNVKNGPefvGVVGVNLGKNkttsdHVQDYVEGVKKFGEV-ADYFVINVSSPNTPG-LRSL-QAKENLEELITKVK 233
Cdd:COG0167 82 LERLLPAKRYD---VPVIVNIGGN-----TVEDYVELARRLADAgADYLELNISCPNTPGgGRALgQDPEALAELLAAVK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 234 AASenlpkKPPLLVKLAPDLSDQErqDVADVINSSKcrVDGLVISNTTIDRPNLMSSEK----EENGGLSGAPLANLSTA 309
Cdd:COG0167 154 AAT-----DKPVLVKLAPDLTDIV--EIARAAEEAG--ADGVIAINTTLGRAIDLETRRpvlaNEAGGLSGPALKPIALR 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2194834072 310 MIADMYRRTHGKIPIIGVGGIFSGADAYEKIKSGASLVQIYTSYIYHGPPIVTRIKKELDELLVKDGHTSI 380
Cdd:COG0167 225 MVREVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSI 295
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
77-372 |
4.78e-110 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 324.30 E-value: 4.78e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 77 RLKTTVWGLDFNNPIGMAAGFDKQGEAVNGLHKIG-FGFVEVGSVTPEPQDGNPKPRVFRLQEDkaVINRYGFNSDGHEV 155
Cdd:pfam01180 1 MLATKIPGLDFKNPIGLASGFDKFGEEALKWLALGkFGAIEIKSVTPYPQPGNPTPRVFRLPEG--VLNRMGLNNPGLDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 156 VYERLRNVKNgPEFVGVVGVNLGKNKTTSDhvqDYVEGVKKFGEVADYFVINVSSPNTPGLRSLQAKENLEELITKVKAA 235
Cdd:pfam01180 79 VLAELLKRRK-EYPRPDLGINLSKAGMTVD---DYVEVARKIGPFADYIELNVSCPNTPGLRALQTDPELAAILLKVVKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 236 SEnlpkKPPLLVKLAPDLSDQERQDVADVInSSKCRVDGLVISNTTIDRPNLMSS-----EKEENGGLSGAPLANLSTAM 310
Cdd:pfam01180 155 VS----KVPVLVKLAPDLTDIVIIDIADVA-LGEDGLDGINATNTTVRGMRIDLKtekpiLANGTGGLSGPPIKPIALKV 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2194834072 311 IADMYRRTHGKIPIIGVGGIFSGADAYEKIKSGASLVQIYTSYIYHGPPIVTRIKKELDELL 372
Cdd:pfam01180 230 IRELYQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
43-368 |
0e+00 |
|
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: 527.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 43 MPVVRCIDPERAHNVAVFATKFALVSSGP---YQDSARLKTTVWGLDFNNPIGMAAGFDKQGEAVNGLHKIGFGFVEVGS 119
Cdd:cd04738 1 RPLLFLLDPETAHRLAIRALKLGLGPPLLlllVYDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFVEVGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 120 VTPEPQDGNPKPRVFRLQEDKAVINRYGFNSDGHEVVYERLRNVKNGPefvGVVGVNLGKNKTT--SDHVQDYVEGVKKF 197
Cdd:cd04738 81 VTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRRPRG---GPLGVNIGKNKDTplEDAVEDYVIGVRKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 198 GEVADYFVINVSSPNTPGLRSLQAKENLEELITKVKAASENLPKKPPLLVKLAPDLSDQERQDVADVINSSKcrVDGLVI 277
Cdd:cd04738 158 GPYADYLVVNVSSPNTPGLRDLQGKEALRELLTAVKEERNKLGKKVPLLVKIAPDLSDEELEDIADVALEHG--VDGIIA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 278 SNTTIDRPNLMSSE-KEENGGLSGAPLANLSTAMIADMYRRTHGKIPIIGVGGIFSGADAYEKIKSGASLVQIYTSYIYH 356
Cdd:cd04738 236 TNTTISRPGLLRSPlANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTGLVYE 315
|
330
....*....|..
gi 2194834072 357 GPPIVTRIKKEL 368
Cdd:cd04738 316 GPGLVKRIKREL 327
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
37-376 |
9.61e-178 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 498.15 E-value: 9.61e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 37 FYEDFLMPVVRCIDPERAHNVAVFATKFA--------LVSSGPYQDSaRLKTTVWGLDFNNPIGMAAGFDKQGEAVNGLH 108
Cdd:PRK05286 1 MYYPLARPLLFKLDPETAHELTIRALKRAsrtpllslLRQRLTYTDP-RLPVTVMGLTFPNPVGLAAGFDKNGEAIDALG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 109 KIGFGFVEVGSVTPEPQDGNPKPRVFRLQEDKAVINRYGFNSDGHEVVYERLRNVKNGPefvgVVGVNLGKNKTTS--DH 186
Cdd:PRK05286 80 ALGFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKAYRGI----PLGINIGKNKDTPleDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 187 VQDYVEGVKKFGEVADYFVINVSSPNTPGLRSLQAKENLEELITKVKAASENLPKKPPLLVKLAPDLSDQERQDVADVIN 266
Cdd:PRK05286 156 VDDYLICLEKLYPYADYFTVNISSPNTPGLRDLQYGEALDELLAALKEAQAELHGYVPLLVKIAPDLSDEELDDIADLAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 267 SSKcrVDGLVISNTTIDRPNLMSSE-KEENGGLSGAPLANLSTAMIADMYRRTHGKIPIIGVGGIFSGADAYEKIKSGAS 345
Cdd:PRK05286 236 EHG--IDGVIATNTTLSRDGLKGLPnADEAGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGAS 313
|
330 340 350
....*....|....*....|....*....|.
gi 2194834072 346 LVQIYTSYIYHGPPIVTRIKKELDELLVKDG 376
Cdd:PRK05286 314 LVQIYSGLIYEGPGLVKEIVRGLARLLRRDG 344
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
41-387 |
5.35e-168 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 476.15 E-value: 5.35e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 41 FLMPVVRCIDPERAHNVAVFATKFALVSSGPYQDSARLKTTVWGLDFNNPIGMAAGFDKQGEAVNGLHKIGFGFVEVGSV 120
Cdd:PLN02826 37 LVNPLFRLLDPETAHSLAISAAARGLVPREKRPDPSVLGVEVWGRTFSNPIGLAAGFDKNAEAVEGLLGLGFGFVEIGSV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 121 TPEPQDGNPKPRVFRLQEDKAVINRYGFNSDGHEVVYERL-------------------RNVKNGP-EFVGVVGVNLGKN 180
Cdd:PLN02826 117 TPLPQPGNPKPRVFRLREEGAIINRYGFNSEGIVAVAKRLgaqhgkrkldetssssfssDDVKAGGkAGPGILGVNLGKN 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 181 KTTSDHVQDYVEGVKKFGEVADYFVINVSSPNTPGLRSLQAKENLEELITKVKAASENLPK----KPPLLVKLAPDLSDQ 256
Cdd:PLN02826 197 KTSEDAAADYVQGVRALSQYADYLVINVSSPNTPGLRKLQGRKQLKDLLKKVLAARDEMQWgeegPPPLLVKIAPDLSKE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 257 ERQDVADVinSSKCRVDGLVISNTTIDRPNLMSSEK--EENGGLSGAPLANLSTAMIADMYRRTHGKIPIIGVGGIFSGA 334
Cdd:PLN02826 277 DLEDIAAV--ALALGIDGLIISNTTISRPDSVLGHPhaDEAGGLSGKPLFDLSTEVLREMYRLTRGKIPLVGCGGVSSGE 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2194834072 335 DAYEKIKSGASLVQIYTSYIYHGPPIVTRIKKELDELLVKDGHTSIQEAIGKD 387
Cdd:PLN02826 355 DAYKKIRAGASLVQLYTAFAYEGPALIPRIKAELAACLERDGFKSIQEAVGAD 407
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
49-368 |
3.94e-129 |
|
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: 374.51 E-value: 3.94e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 49 IDPERAHNVAVFATKfaLVSSGPY--------QDSARLKTTVWGLDFNNPIGMAAGFDKQGEAVNGLHKIGFGFVEVGSV 120
Cdd:TIGR01036 11 LDPESAHELTFQFLR--LGTGTPFlallrslfGASDPLEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAMGFGFLEIGTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 121 TPEPQDGNPKPRVFRLQEDKAVINRYGFNSDGHEVVYERLRNVKNGpefvGVVGVNLGKNKTTS--DHVQDYVEGVKKFG 198
Cdd:TIGR01036 89 TPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLKRARYK----GPIGINIGKNKDTPseDAKEDYAACLRKLG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 199 EVADYFVINVSSPNTPGLRSLQAKENLEELITKVKAASENLP--KKPPLLVKLAPDLSDQERQDVADVINSSKcrVDGLV 276
Cdd:TIGR01036 165 PLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAVKQEQDGLRrvHRVPVLVKIAPDLTESDLEDIADSLVELG--IDGVI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 277 ISNTTIDRPNLMSSEK-EENGGLSGAPLANLSTAMIADMYRRTHGKIPIIGVGGIFSGADAYEKIKSGASLVQIYTSYIY 355
Cdd:TIGR01036 243 ATNTTVSRSLVQGPKNsDETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGASLLQIYSGFIY 322
|
330
....*....|...
gi 2194834072 356 HGPPIVTRIKKEL 368
Cdd:TIGR01036 323 WGPPLVKEIVKEI 335
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
78-380 |
3.13e-118 |
|
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: 345.13 E-value: 3.13e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 78 LKTTVWGLDFNNPIGMAAGF-DKQGEAVNGLHKIGFGFVEVGSVTPEPQDGNPKPRVFRLQEDKAVINRYGFNSDGHEVV 156
Cdd:COG0167 2 LSVELAGLKFPNPVGLASGFfDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 157 YERLRNVKNGPefvGVVGVNLGKNkttsdHVQDYVEGVKKFGEV-ADYFVINVSSPNTPG-LRSL-QAKENLEELITKVK 233
Cdd:COG0167 82 LERLLPAKRYD---VPVIVNIGGN-----TVEDYVELARRLADAgADYLELNISCPNTPGgGRALgQDPEALAELLAAVK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 234 AASenlpkKPPLLVKLAPDLSDQErqDVADVINSSKcrVDGLVISNTTIDRPNLMSSEK----EENGGLSGAPLANLSTA 309
Cdd:COG0167 154 AAT-----DKPVLVKLAPDLTDIV--EIARAAEEAG--ADGVIAINTTLGRAIDLETRRpvlaNEAGGLSGPALKPIALR 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2194834072 310 MIADMYRRTHGKIPIIGVGGIFSGADAYEKIKSGASLVQIYTSYIYHGPPIVTRIKKELDELLVKDGHTSI 380
Cdd:COG0167 225 MVREVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSI 295
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
77-372 |
4.78e-110 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 324.30 E-value: 4.78e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 77 RLKTTVWGLDFNNPIGMAAGFDKQGEAVNGLHKIG-FGFVEVGSVTPEPQDGNPKPRVFRLQEDkaVINRYGFNSDGHEV 155
Cdd:pfam01180 1 MLATKIPGLDFKNPIGLASGFDKFGEEALKWLALGkFGAIEIKSVTPYPQPGNPTPRVFRLPEG--VLNRMGLNNPGLDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 156 VYERLRNVKNgPEFVGVVGVNLGKNKTTSDhvqDYVEGVKKFGEVADYFVINVSSPNTPGLRSLQAKENLEELITKVKAA 235
Cdd:pfam01180 79 VLAELLKRRK-EYPRPDLGINLSKAGMTVD---DYVEVARKIGPFADYIELNVSCPNTPGLRALQTDPELAAILLKVVKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 236 SEnlpkKPPLLVKLAPDLSDQERQDVADVInSSKCRVDGLVISNTTIDRPNLMSS-----EKEENGGLSGAPLANLSTAM 310
Cdd:pfam01180 155 VS----KVPVLVKLAPDLTDIVIIDIADVA-LGEDGLDGINATNTTVRGMRIDLKtekpiLANGTGGLSGPPIKPIALKV 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2194834072 311 IADMYRRTHGKIPIIGVGGIFSGADAYEKIKSGASLVQIYTSYIYHGPPIVTRIKKELDELL 372
Cdd:pfam01180 230 IRELYQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
80-367 |
1.05e-71 |
|
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: 226.08 E-value: 1.05e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 80 TTVWGLDFNNPIGMAAGFD-KQGEAVNGLHKIGFGFVEVGSVTPEPQDGNPKPRVFRLQEDK-------AVINRYGFNSD 151
Cdd:cd02810 1 VNFLGLKLKNPFGVAAGPLlKTGELIARAAAAGFGAVVYKTVTLHPRPGNPLPRVARLPPEGesypeqlGILNSFGLPNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 152 GHEVVYERLR-NVKNGPEfvGVVGVNLGKNKttsdhVQDYVEGVKKFGEV-ADYFVINVSSPNTPGLRSL-QAKENLEEL 228
Cdd:cd02810 81 GLDVWLQDIAkAKKEFPG--QPLIASVGGSS-----KEDYVELARKIERAgAKALELNLSCPNVGGGRQLgQDPEAVANL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 229 ITKVKAASenlpkKPPLLVKLAPDLSDQERQDVADVINSSKcrVDGLVISNTT----IDRPNLMSSEKEENGGLSGAPLA 304
Cdd:cd02810 154 LKAVKAAV-----DIPLLVKLSPYFDLEDIVELAKAAERAG--ADGLTAINTIsgrvVDLKTVGPGPKRGTGGLSGAPIR 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2194834072 305 NLSTAMIADMYRRTHGKIPIIGVGGIFSGADAYEKIKSGASLVQIYTSYIYHGPPIVTRIKKE 367
Cdd:cd02810 227 PLALRWVARLAARLQLDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKIKKE 289
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
78-385 |
6.06e-36 |
|
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: 133.32 E-value: 6.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 78 LKTTVWGLDFNNPIGMAAG-FDKQGEAVNGLHKIGFGFVEVGSVTPEPQDGNPKPRVFRLQedKAVINRYGFNSDGHEVV 156
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGiMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTIVETP--CGMLNAIGLQNPGVEAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 157 YERLRNVKNgpEFVGVVGVNL-GKNkttsdhVQDYVEGVKKF---GEVADYFVINVSSPN--TPGLRSLQAKENLEELIT 230
Cdd:TIGR01037 79 LEELKPVRE--EFPTPLIASVyGSS------VEEFAEVAEKLekaPPYVDAYELNLSCPHvkGGGIAIGQDPELSADVVK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 231 KVKAASENlpkkpPLLVKLAPDLSDQerQDVADVINSSKcrVDGLVISNT----TID----RPNLMSsekeENGGLSGAP 302
Cdd:TIGR01037 151 AVKDKTDV-----PVFAKLSPNVTDI--TEIAKAAEEAG--ADGLTLINTlrgmKIDiktgKPILAN----KTGGLSGPA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 303 LANLSTAMIADMYRRThgKIPIIGVGGIFSGADAYEKIKSGASLVQIYTSyIYHGPPIVTRIKKELDELLVKDGHTSIQE 382
Cdd:TIGR01037 218 IKPIALRMVYDVYKMV--DIPIIGVGGITSFEDALEFLMAGASAVQVGTA-VYYRGFAFKKIIEGLIAFLKAEGFTSIEE 294
|
...
gi 2194834072 383 AIG 385
Cdd:TIGR01037 295 LIG 297
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
79-386 |
2.72e-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: 131.13 E-value: 2.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 79 KTTVWGLDFNNPIGMAAGFDKQGEAVNGLHKIG-FGFVEVGSVTPEPQDGNPKPRVFRLqeDKAVINRYGFNSDGHEVVY 157
Cdd:cd04740 1 SVELAGLRLKNPVILASGTFGFGEELSRVADLGkLGAIVTKSITLEPREGNPPPRVVET--PGGMLNAIGLQNPGVEAFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 158 ERLRNVKNGPE---FVGVVGvnlgknkttsDHVQDYVEGVKKFGEV-ADYFVINVSSPNTPGLRSL--QAKENLEELITK 231
Cdd:cd04740 79 EELLPWLREFGtpvIASIAG----------STVEEFVEVAEKLADAgADAIELNISCPNVKGGGMAfgTDPEAVAEIVKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 232 VKAASenlpkKPPLLVKLAPDlsdqerqdVADVINSSKCRV----DGLVISNT----TID----RP---NLMssekeenG 296
Cdd:cd04740 149 VKKAT-----DVPVIVKLTPN--------VTDIVEIARAAEeagaDGLTLINTlkgmAIDietrKPilgNVT-------G 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 297 GLSGA---PLAnlsTAMIADMYRRThgKIPIIGVGGIFSGADAYEKIKSGASLVQIYTSyIYHGPPIVTRIKKELDELLV 373
Cdd:cd04740 209 GLSGPaikPIA---LRMVYQVYKAV--EIPIIGVGGIASGEDALEFLMAGASAVQVGTA-NFVDPEAFKEIIEGLEAYLD 282
|
330
....*....|...
gi 2194834072 374 KDGHTSIQEAIGK 386
Cdd:cd04740 283 EEGIKSIEELVGL 295
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
77-385 |
8.39e-35 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 130.27 E-value: 8.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 77 RLKTTVWGLDFNNPIGMAAG-FDKQGEAVNGLHKIGFGFVEVGSVTPEPQDGNPKPRVFRLqeDKAVINRYGFNSDGHEV 155
Cdd:PRK07259 1 RLSVELPGLKLKNPVMPASGtFGFGGEYARFYDLNGLGAIVTKSTTLEPREGNPTPRIAET--PGGMLNAIGLQNPGVDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 156 VYERLRNVKNGPEFVGVVGVnLGKNkttsdhVQDYVEGVKKFGEV--ADYFVINVSSPNTP--GLRSLQAKENLEELITK 231
Cdd:PRK07259 79 FIEEELPWLEEFDTPIIANV-AGST------EEEYAEVAEKLSKApnVDAIELNISCPNVKhgGMAFGTDPELAYEVVKA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 232 VKAASenlpkKPPLLVKLAPDlsdqerqdVADVINSSKCRV----DGLVISNT----TID----RPNLmssekeEN--GG 297
Cdd:PRK07259 152 VKEVV-----KVPVIVKLTPN--------VTDIVEIAKAAEeagaDGLSLINTlkgmAIDiktrKPIL------ANvtGG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 298 LSGAPLANLSTAMIADMYRRThgKIPIIGVGGIFSGADAYEKIKSGASLVQIYTsYIYHGPPIVTRIKKELDELLVKDGH 377
Cdd:PRK07259 213 LSGPAIKPIALRMVYQVYQAV--DIPIIGMGGISSAEDAIEFIMAGASAVQVGT-ANFYDPYAFPKIIEGLEAYLDKYGI 289
|
....*...
gi 2194834072 378 TSIQEAIG 385
Cdd:PRK07259 290 KSIEEIVG 297
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
77-386 |
4.45e-29 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 115.05 E-value: 4.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 77 RLKTTVWGLDFNNPIGMAAG-FDKQGEAVNGLHKIGFGFVEVGSVTPEPQDGNPKPRVFRLqeDKAVINRYGFNSDGH-- 153
Cdd:PRK02506 1 STSTQIAGFKFDNCLMNAAGvYCMTKEELEEVEASAAGAFVTKSATLEPRPGNPEPRYADT--PLGSINSMGLPNLGFdy 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 154 --EVVYERLRNVKNGPEFVGVVGVNLGKNKTTSDHVQDyvegvkkfGEVADYFVINVSSPNTPGlrslqaK-------EN 224
Cdd:PRK02506 79 ylDYVLELQKKGPNKPHFLSVVGLSPEETHTILKKIQA--------SDFNGLVELNLSCPNVPG------KpqiaydfET 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 225 LEELITKVKAASENlpkkpPLLVKLAP--DLS--DQerqdVADVINssKCRVD----------GLVI---SNTTIDRPnl 287
Cdd:PRK02506 145 TEQILEEVFTYFTK-----PLGVKLPPyfDIVhfDQ----AAAIFN--KFPLAfvncinsignGLVIdpeDETVVIKP-- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 288 msseKEENGGLSGA-----PLANlstamIADMYRRTHGKIPIIGVGGIFSGADAYEKIKSGASLVQIYTSYIYHGPPIVT 362
Cdd:PRK02506 212 ----KNGFGGIGGDyikptALAN-----VRAFYQRLNPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFE 282
|
330 340
....*....|....*....|....
gi 2194834072 363 RIKKELDELLVKDGHTSIQEAIGK 386
Cdd:PRK02506 283 RLTKELKAIMAEKGYQSLEDFRGK 306
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
80-372 |
1.94e-24 |
|
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: 101.63 E-value: 1.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 80 TTVWGLDFNNPIGMAAG-FDKQGEAVNGLHKIGFGFVEVGSVTPEPQDGNPKPRVFRLQedKAVINRYGFNSDGHEVVYE 158
Cdd:cd04741 1 VTPPGLTISPPLMNAAGpWCTTLEDLLELAASSTGAVTTRSSTLAGRPGNPEPRYYAFP--LGSINSLGLPNLGLDYYLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 159 RLRNVKNG------PEFVGVVGVnlgknkttsdhVQDYVEGVKKFGEVADYFV----INVSSPNTPGLRSLQAK-ENLEE 227
Cdd:cd04741 79 YIRTISDGlpgsakPFFISVTGS-----------AEDIAAMYKKIAAHQKQFPlameLNLSCPNVPGKPPPAYDfDATLE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 228 LITKVKAASenlpkKPPLLVKLAPDLSDQERQDVADVINSSKCRVDGLVISNTTidrPN--LMSSEKEEN--------GG 297
Cdd:cd04741 148 YLTAVKAAY-----SIPVGVKTPPYTDPAQFDTLAEALNAFACPISFITATNTL---GNglVLDPERETVvlkpktgfGG 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2194834072 298 LSGAPLANLSTAMIADMYRRTHGKIPIIGVGGIFSGADAYEKIKSGASLVQIYTSYIYHGPPIVTRIKKELDELL 372
Cdd:cd04741 220 LAGAYLHPLALGNVRTFRRLLPSEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEKELEDIW 294
|
|
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
78-368 |
1.78e-13 |
|
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: 70.39 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 78 LKTTVWGLDFNNPIGMAAG-FDKQGEAVNGLHKIGFGFVEVGSVTPE-PQDGNPKPRVFRLQ-EDKAVInryGFNS---- 150
Cdd:cd02940 2 LSVTFCGIKFPNPFGLASApPTTSYPMIRRAFEAGWGGAVTKTLGLDkDIVTNVSPRIARLRtSGRGQI---GFNNieli 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 151 --DGHEVVYERLRNVK-NGPEFVGVVGVNLGKNKttsdhvQDYVEGVKKFGEV-ADYFVINVSSPNTPGLRSL-----QA 221
Cdd:cd02940 79 seKPLEYWLKEIRELKkDFPDKILIASIMCEYNK------EDWTELAKLVEEAgADALELNFSCPHGMPERGMgaavgQD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 222 KENLEELITKVKAASenlpkKPPLLVKLAPDLSDQERQDVAdvinSSKCRVDGLVISNT-------TID--RPNLMSSEK 292
Cdd:cd02940 153 PELVEEICRWVREAV-----KIPVIAKLTPNITDIREIARA----AKEGGADGVSAINTvnslmgvDLDgtPPAPGVEGK 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2194834072 293 EENGGLSGAPLANLSTAMIADMYRRTHGKIPIIGVGGIFSGADAYEKIKSGASLVQIYTSYIYHGPPIVTRIKKEL 368
Cdd:cd02940 224 TTYGGYSGPAVKPIALRAVSQIARAPEPGLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
244-388 |
5.32e-11 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 63.81 E-value: 5.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 244 PLLVKLAPDLSD---------QERQDVADVINSSKCrvdglvISNTTIDR--PNLMSSEKEENGGLSGAPLANLSTAMIA 312
Cdd:PRK08318 170 PVIVKLTPNITDireparaakRGGADAVSLINTINS------ITGVDLDRmiPMPIVNGKSSHGGYCGPAVKPIALNMVA 243
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2194834072 313 DMYR--RTHGkIPIIGVGGIFSGADAYEKIKSGASLVQIYTSYIYHGPPIVTRIKKELDELLVKDGHTSIQEAIGKDV 388
Cdd:PRK08318 244 EIARdpETRG-LPISGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISGLSHYMDEKGFASLEDMVGLAV 320
|
|
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
78-386 |
2.33e-10 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 61.78 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 78 LKTTVWGLDFNNP--IG----------MAAGFDKQGEAVNGlHKIGFGFVEVGSVTPE------PQDGNPKPRVFRLQED 139
Cdd:PLN02495 11 LSVTVNGLKMPNPfvIGsgppgtnytvMKRAFDEGWGGVIA-KTVSLDASKVINVTPRyarlraGANGSAKGRVIGWQNI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 140 KAVINRygfnsdGHEVVYERLRNVKNG-PEFVGVVGVNLGKNKTTSDHVQDYVEGVKkfgevADYFVINVSSPNTPGLRS 218
Cdd:PLN02495 90 ELISDR------PFETMLAEFKQLKEEyPDRILIASIMEEYNKDAWEEIIERVEETG-----VDALEINFSCPHGMPERK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 219 L-----QAKENLEELITKVKAASenlpkKPPLLVKLAPDLSDQERQdvADVINSSKCrvDGLVISNTTID---------R 284
Cdd:PLN02495 159 MgaavgQDCDLLEEVCGWINAKA-----TVPVWAKMTPNITDITQP--ARVALKSGC--EGVAAINTIMSvmginldtlR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 285 PNLMSSEKEENGGLSGA---PLANLSTAMIADMYRRTHGK-IPIIGVGGIFSGADAYEKIKSGASLVQIYTSYIYHGPPI 360
Cdd:PLN02495 230 PEPCVEGYSTPGGYSSKavrPIALAKVMAIAKMMKSEFPEdRSLSGIGGVETGGDAAEFILLGADTVQVCTGVMMHGYPL 309
|
330 340
....*....|....*....|....*.
gi 2194834072 361 VTRIKKELDELLVKDGHTSIQEAIGK 386
Cdd:PLN02495 310 VKNLCAELQDFMKKHNFSSIEDFRGA 335
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
315-366 |
3.68e-05 |
|
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: 45.28 E-value: 3.68e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2194834072 315 YRRTHGKIPIIGVGGIFSGADAYEKIKSGASLVQIYTSYIYHgPPIVTRIKK 366
Cdd:cd04735 278 KERIAGRLPLIAVGSINTPDDALEALETGADLVAIGRGLLVD-PDWVEKIKE 328
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| DHOD_like |
cd04739 |
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
227-386 |
2.53e-03 |
|
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: 39.52 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 227 ELITKVKAASenlpkKPPLLVKLAPDLS------DQERQDVADvinsskcrvdGLVISN------TTIDRPNLMSSEKee 294
Cdd:cd04739 153 DILRAVKSAV-----TIPVAVKLSPFFSalahmaKQLDAAGAD----------GLVLFNrfyqpdIDLETLEVVPNLL-- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2194834072 295 nggLSGAPLANLSTAMIADMYRRThgKIPIIGVGGIFSGADAYEKIKSGASLVQIyTSYIY-HGPPIVTRIKKELDELLV 373
Cdd:cd04739 216 ---LSSPAEIRLPLRWIAILSGRV--KASLAASGGVHDAEDVVKYLLAGADVVMT-TSALLrHGPDYIGTLLAGLEAWME 289
|
170
....*....|...
gi 2194834072 374 KDGHTSIQEAIGK 386
Cdd:cd04739 290 EHGYESVQQLRGS 302
|
|
| PRK07565 |
PRK07565 |
dihydroorotate dehydrogenase-like protein; |
319-386 |
3.04e-03 |
|
dihydroorotate dehydrogenase-like protein;
Pssm-ID: 236051 Cd Length: 334 Bit Score: 39.46 E-value: 3.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2194834072 319 HGKIP--IIGVGGIFSGADAYEKIKSGASLVQIyTSYIY-HGPPIVTRIKKELDELLVKDGHTSIQEAIGK 386
Cdd:PRK07565 235 SGRVGadLAATTGVHDAEDVIKMLLAGADVVMI-ASALLrHGPDYIGTILRGLEDWMERHGYESLQQFRGS 304
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|
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