|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
1-336 |
0e+00 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 600.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 1 MLYRLARTGFFQLDAEKAHDLAIQNFKRFTGTPIDLLYRQQL----PHRPVECMGLTFKNPVGLAAGLDKNGECIDAFGA 76
Cdd:PRK05286 1 MYYPLARPLLFKLDPETAHELTIRALKRASRTPLLSLLRQRLtytdPRLPVTVMGLTFPNPVGLAAGFDKNGEAIDALGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 77 MGFGFVEVGTVTPRPQAGNDKPRLFRLVEAEGIINRMGFNNLGVDNLVENVKKSNYDGILGINIGKNKDTPIEKGAEDYL 156
Cdd:PRK05286 81 LGFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKAYRGIPLGINIGKNKDTPLEDAVDDYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 157 ICMEKVYQYAGYIAVNISSPNTPGLRSLQYGEALDDLLSELKTKQSELeekhGKYVPLALKIAPDLSDDEIRQICESLIK 236
Cdd:PRK05286 161 ICLEKLYPYADYFTVNISSPNTPGLRDLQYGEALDELLAALKEAQAEL----HGYVPLLVKIAPDLSDEELDDIADLALE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 237 NKIDGVIATNTTLDRSIVEGMKHCDEAGGLSGRPVQSRSTEVVRKLHEELGDKLPIIGVGGVDSYVAAKEKMMAGAKLVQ 316
Cdd:PRK05286 237 HGIDGVIATNTTLSRDGLKGLPNADEAGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGASLVQ 316
|
330 340
....*....|....*....|
gi 1515654850 317 VYSGFIYKGPGLVGDIVKNL 336
Cdd:PRK05286 317 IYSGLIYEGPGLVKEIVRGL 336
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
10-336 |
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: 527.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 10 FFQLDAEKAHDLAIQNFKRFTGTPIDLLYRQQLPHRPVECMGLTFKNPVGLAAGLDKNGECIDAFGAMGFGFVEVGTVTP 89
Cdd:cd04738 4 LFLLDPETAHRLAIRALKLGLGPPLLLLLVYDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFVEVGTVTP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 90 RPQAGNDKPRLFRLVEAEGIINRMGFNNLGVDNLVENVKKSNY-DGILGINIGKNKDTPIEKGAEDYLICMEKVYQYAGY 168
Cdd:cd04738 84 RPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRRPrGGPLGVNIGKNKDTPLEDAVEDYVIGVRKLGPYADY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 169 IAVNISSPNTPGLRSLQYGEALDDLLSELKTKQSELeekhGKYVPLALKIAPDLSDDEIRQICESLIKNKIDGVIATNTT 248
Cdd:cd04738 164 LVVNVSSPNTPGLRDLQGKEALRELLTAVKEERNKL----GKKVPLLVKIAPDLSDEELEDIADVALEHGVDGIIATNTT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 249 LDRSIVEGMKHCDEAGGLSGRPVQSRSTEVVRKLHEELGDKLPIIGVGGVDSYVAAKEKMMAGAKLVQVYSGFIYKGPGL 328
Cdd:cd04738 240 ISRPGLLRSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTGLVYEGPGL 319
|
....*...
gi 1515654850 329 VGDIVKNL 336
Cdd:cd04738 320 VKRIKREL 327
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
3-336 |
9.99e-177 |
|
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: 492.76 E-value: 9.99e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 3 YRLARTGFFQLDAEKAHDLAIQNFKRFTGTPIDLLYRQQLPHR---PVECMGLTFKNPVGLAAGLDKNGECIDAFGAMGF 79
Cdd:TIGR01036 1 YPLVRKLLFLLDPESAHELTFQFLRLGTGTPFLALLRSLFGASdplEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAMGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 80 GFVEVGTVTPRPQAGNDKPRLFRLVEAEGIINRMGFNNLGVDNLVENVKKSNYDGILGINIGKNKDTPIEKGAEDYLICM 159
Cdd:TIGR01036 81 GFLEIGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLKRARYKGPIGINIGKNKDTPSEDAKEDYAACL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 160 EKVYQYAGYIAVNISSPNTPGLRSLQYGEALDDLLSELKTKQSELEEKHgkYVPLALKIAPDLSDDEIRQICESLIKNKI 239
Cdd:TIGR01036 161 RKLGPLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAVKQEQDGLRRVH--RVPVLVKIAPDLTESDLEDIADSLVELGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 240 DGVIATNTTLDRSIVEGMKHCDEAGGLSGRPVQSRSTEVVRKLHEELGDKLPIIGVGGVDSYVAAKEKMMAGAKLVQVYS 319
Cdd:TIGR01036 239 DGVIATNTTVSRSLVQGPKNSDETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGASLLQIYS 318
|
330
....*....|....*..
gi 1515654850 320 GFIYKGPGLVGDIVKNL 336
Cdd:TIGR01036 319 GFIYWGPPLVKEIVKEI 335
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
46-336 |
9.85e-124 |
|
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: 357.08 E-value: 9.85e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 46 PVECMGLTFKNPVGLAAG-LDKNGECIDAFGAMGFGFVEVGTVTPRPQAGNDKPRLFRLVEAEGIINRMGFNNLGVDNLV 124
Cdd:COG0167 3 SVELAGLKFPNPVGLASGfFDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDAFL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 125 ENVKKS-NYDGILGINIGKNkdtpiekGAEDYLICMEKVYQY-AGYIAVNISSPNTPG-LRSL-QYGEALDDLLSELKTK 200
Cdd:COG0167 83 ERLLPAkRYDVPVIVNIGGN-------TVEDYVELARRLADAgADYLELNISCPNTPGgGRALgQDPEALAELLAAVKAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 201 QSeleekhgkyVPLALKIAPDLSDdeIRQICESLIKNKIDGVIATNTTLDRSI-VEGMKH--CDEAGGLSGRPVQSRSTE 277
Cdd:COG0167 156 TD---------KPVLVKLAPDLTD--IVEIARAAEEAGADGVIAINTTLGRAIdLETRRPvlANEAGGLSGPALKPIALR 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1515654850 278 VVRKLHEELGDKLPIIGVGGVDSYVAAKEKMMAGAKLVQVYSGFIYKGPGLVGDIVKNL 336
Cdd:COG0167 225 MVREVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGL 283
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
47-336 |
7.37e-92 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 275.77 E-value: 7.37e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 47 VECMGLTFKNPVGLAAGLDKNGECIDAFGAMG-FGFVEVGTVTPRPQAGNDKPRLFRLVEaeGIINRMGFNNLGVDNLVE 125
Cdd:pfam01180 4 TKIPGLDFKNPIGLASGFDKFGEEALKWLALGkFGAIEIKSVTPYPQPGNPTPRVFRLPE--GVLNRMGLNNPGLDAVLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 126 NVK---KSNYDGILGINIGKNKDTpiekgAEDYLICMEKVYQYAGYIAVNISSPNTPGLRSLQYGEALDDLLSELKTKQS 202
Cdd:pfam01180 82 ELLkrrKEYPRPDLGINLSKAGMT-----VDDYVEVARKIGPFADYIELNVSCPNTPGLRALQTDPELAAILLKVVKEVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 203 EleekhgkyVPLALKIAPDLSD-DEIRQICESLIKNKIDGVIATNTTLDRSI--VEGMKHCDE--AGGLSGRPVQSRSTE 277
Cdd:pfam01180 157 K--------VPVLVKLAPDLTDiVIIDIADVALGEDGLDGINATNTTVRGMRidLKTEKPILAngTGGLSGPPIKPIALK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1515654850 278 VVRKLHEELGDKLPIIGVGGVDSYVAAKEKMMAGAKLVQVYSGFIYKGPGLVGDIVKNL 336
Cdd:pfam01180 229 VIRELYQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDEL 287
|
|
| dihydoor_dh_Arch |
NF041011 |
dihydroorotate dehydrogenase PyrD; |
47-336 |
6.40e-21 |
|
dihydroorotate dehydrogenase PyrD;
Pssm-ID: 468940 Cd Length: 289 Bit Score: 90.77 E-value: 6.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 47 VECMGLTFKNPVGLAAG-LDKNGECIDAF-GAMGFGFVEVGTVTPRPQAGNDKPRLFRLvEAEGIINRMGFNNLGVDnLV 124
Cdd:NF041011 1 IRLAGLELEDPLIIASGiLPDVPEYIERVcEKYGPSAITTKTLTLNPLEPHKPPTVVKL-HDGCYLNAIGLGNPGIG-LL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 125 ENVKKSNYDGILGINiGKNKDTPIEKGaedylicmEKVYQYAGYIAVNISSPNTPGlrslqYGEALDDLLSELkTKqsel 204
Cdd:NF041011 79 EEIRVKLCPLIVSIG-GSSLEEIVEVA--------EIAEEKADAIELNLSSPNRKG-----YGASLASLVREI-VK---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 205 EEKHGKYVPLALKIAPDlsdDEIRQICESLIKNKIDGVIATNTtldrsiVEGMKHCDEA---------GGLSGRPVQSRS 275
Cdd:NF041011 140 AVKSVVKKPVFVKLGPW---DNVLEIAGKALEAGADGLTLINT------VKGMAIDVESfkpvlsygtGGISGKCIHPLA 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1515654850 276 TEVVRKLHEELgdKLPIIGVGGVDSYVAAKEKMMAGAKLVQVYSGFIYKGPGLVGDIVKNL 336
Cdd:NF041011 211 VRIIYDVYREY--EAEIIGVGGVFSWRDAIELMSVGAKAVGVGTAIIDKGLSVISEIRKGL 269
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
1-336 |
0e+00 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 600.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 1 MLYRLARTGFFQLDAEKAHDLAIQNFKRFTGTPIDLLYRQQL----PHRPVECMGLTFKNPVGLAAGLDKNGECIDAFGA 76
Cdd:PRK05286 1 MYYPLARPLLFKLDPETAHELTIRALKRASRTPLLSLLRQRLtytdPRLPVTVMGLTFPNPVGLAAGFDKNGEAIDALGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 77 MGFGFVEVGTVTPRPQAGNDKPRLFRLVEAEGIINRMGFNNLGVDNLVENVKKSNYDGILGINIGKNKDTPIEKGAEDYL 156
Cdd:PRK05286 81 LGFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKAYRGIPLGINIGKNKDTPLEDAVDDYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 157 ICMEKVYQYAGYIAVNISSPNTPGLRSLQYGEALDDLLSELKTKQSELeekhGKYVPLALKIAPDLSDDEIRQICESLIK 236
Cdd:PRK05286 161 ICLEKLYPYADYFTVNISSPNTPGLRDLQYGEALDELLAALKEAQAEL----HGYVPLLVKIAPDLSDEELDDIADLALE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 237 NKIDGVIATNTTLDRSIVEGMKHCDEAGGLSGRPVQSRSTEVVRKLHEELGDKLPIIGVGGVDSYVAAKEKMMAGAKLVQ 316
Cdd:PRK05286 237 HGIDGVIATNTTLSRDGLKGLPNADEAGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGASLVQ 316
|
330 340
....*....|....*....|
gi 1515654850 317 VYSGFIYKGPGLVGDIVKNL 336
Cdd:PRK05286 317 IYSGLIYEGPGLVKEIVRGL 336
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
10-336 |
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: 527.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 10 FFQLDAEKAHDLAIQNFKRFTGTPIDLLYRQQLPHRPVECMGLTFKNPVGLAAGLDKNGECIDAFGAMGFGFVEVGTVTP 89
Cdd:cd04738 4 LFLLDPETAHRLAIRALKLGLGPPLLLLLVYDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFVEVGTVTP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 90 RPQAGNDKPRLFRLVEAEGIINRMGFNNLGVDNLVENVKKSNY-DGILGINIGKNKDTPIEKGAEDYLICMEKVYQYAGY 168
Cdd:cd04738 84 RPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRRPrGGPLGVNIGKNKDTPLEDAVEDYVIGVRKLGPYADY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 169 IAVNISSPNTPGLRSLQYGEALDDLLSELKTKQSELeekhGKYVPLALKIAPDLSDDEIRQICESLIKNKIDGVIATNTT 248
Cdd:cd04738 164 LVVNVSSPNTPGLRDLQGKEALRELLTAVKEERNKL----GKKVPLLVKIAPDLSDEELEDIADVALEHGVDGIIATNTT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 249 LDRSIVEGMKHCDEAGGLSGRPVQSRSTEVVRKLHEELGDKLPIIGVGGVDSYVAAKEKMMAGAKLVQVYSGFIYKGPGL 328
Cdd:cd04738 240 ISRPGLLRSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTGLVYEGPGL 319
|
....*...
gi 1515654850 329 VGDIVKNL 336
Cdd:cd04738 320 VKRIKREL 327
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
3-336 |
9.99e-177 |
|
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: 492.76 E-value: 9.99e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 3 YRLARTGFFQLDAEKAHDLAIQNFKRFTGTPIDLLYRQQLPHR---PVECMGLTFKNPVGLAAGLDKNGECIDAFGAMGF 79
Cdd:TIGR01036 1 YPLVRKLLFLLDPESAHELTFQFLRLGTGTPFLALLRSLFGASdplEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAMGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 80 GFVEVGTVTPRPQAGNDKPRLFRLVEAEGIINRMGFNNLGVDNLVENVKKSNYDGILGINIGKNKDTPIEKGAEDYLICM 159
Cdd:TIGR01036 81 GFLEIGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLKRARYKGPIGINIGKNKDTPSEDAKEDYAACL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 160 EKVYQYAGYIAVNISSPNTPGLRSLQYGEALDDLLSELKTKQSELEEKHgkYVPLALKIAPDLSDDEIRQICESLIKNKI 239
Cdd:TIGR01036 161 RKLGPLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAVKQEQDGLRRVH--RVPVLVKIAPDLTESDLEDIADSLVELGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 240 DGVIATNTTLDRSIVEGMKHCDEAGGLSGRPVQSRSTEVVRKLHEELGDKLPIIGVGGVDSYVAAKEKMMAGAKLVQVYS 319
Cdd:TIGR01036 239 DGVIATNTTVSRSLVQGPKNSDETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGASLLQIYS 318
|
330
....*....|....*..
gi 1515654850 320 GFIYKGPGLVGDIVKNL 336
Cdd:TIGR01036 319 GFIYWGPPLVKEIVKEI 335
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
46-336 |
9.85e-124 |
|
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: 357.08 E-value: 9.85e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 46 PVECMGLTFKNPVGLAAG-LDKNGECIDAFGAMGFGFVEVGTVTPRPQAGNDKPRLFRLVEAEGIINRMGFNNLGVDNLV 124
Cdd:COG0167 3 SVELAGLKFPNPVGLASGfFDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDAFL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 125 ENVKKS-NYDGILGINIGKNkdtpiekGAEDYLICMEKVYQY-AGYIAVNISSPNTPG-LRSL-QYGEALDDLLSELKTK 200
Cdd:COG0167 83 ERLLPAkRYDVPVIVNIGGN-------TVEDYVELARRLADAgADYLELNISCPNTPGgGRALgQDPEALAELLAAVKAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 201 QSeleekhgkyVPLALKIAPDLSDdeIRQICESLIKNKIDGVIATNTTLDRSI-VEGMKH--CDEAGGLSGRPVQSRSTE 277
Cdd:COG0167 156 TD---------KPVLVKLAPDLTD--IVEIARAAEEAGADGVIAINTTLGRAIdLETRRPvlANEAGGLSGPALKPIALR 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1515654850 278 VVRKLHEELGDKLPIIGVGGVDSYVAAKEKMMAGAKLVQVYSGFIYKGPGLVGDIVKNL 336
Cdd:COG0167 225 MVREVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGL 283
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
13-336 |
1.66e-115 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 340.18 E-value: 1.66e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 13 LDAEKAHDLAIQNFKRftgtpiDLLYRQQLPHRP---VECMGLTFKNPVGLAAGLDKNGECIDAFGAMGFGFVEVGTVTP 89
Cdd:PLN02826 45 LDPETAHSLAISAAAR------GLVPREKRPDPSvlgVEVWGRTFSNPIGLAAGFDKNAEAVEGLLGLGFGFVEIGSVTP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 90 RPQAGNDKPRLFRLVEAEGIINRMGFNNLGVD----NLVENVKKSNYD--------------------GILGINIGKNKD 145
Cdd:PLN02826 119 LPQPGNPKPRVFRLREEGAIINRYGFNSEGIVavakRLGAQHGKRKLDetssssfssddvkaggkagpGILGVNLGKNKT 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 146 TpiEKGAEDYLICMEKVYQYAGYIAVNISSPNTPGLRSLQYGEALDDLLSELKTKQSELEEKHGKYVPLALKIAPDLSDD 225
Cdd:PLN02826 199 S--EDAAADYVQGVRALSQYADYLVINVSSPNTPGLRKLQGRKQLKDLLKKVLAARDEMQWGEEGPPPLLVKIAPDLSKE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 226 EIRQICESLIKNKIDGVIATNTTLDR-SIVEGMKHCDEAGGLSGRPVQSRSTEVVRKLHEELGDKLPIIGVGGVDSYVAA 304
Cdd:PLN02826 277 DLEDIAAVALALGIDGLIISNTTISRpDSVLGHPHADEAGGLSGKPLFDLSTEVLREMYRLTRGKIPLVGCGGVSSGEDA 356
|
330 340 350
....*....|....*....|....*....|..
gi 1515654850 305 KEKMMAGAKLVQVYSGFIYKGPGLVGDIVKNL 336
Cdd:PLN02826 357 YKKIRAGASLVQLYTAFAYEGPALIPRIKAEL 388
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
47-336 |
7.37e-92 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 275.77 E-value: 7.37e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 47 VECMGLTFKNPVGLAAGLDKNGECIDAFGAMG-FGFVEVGTVTPRPQAGNDKPRLFRLVEaeGIINRMGFNNLGVDNLVE 125
Cdd:pfam01180 4 TKIPGLDFKNPIGLASGFDKFGEEALKWLALGkFGAIEIKSVTPYPQPGNPTPRVFRLPE--GVLNRMGLNNPGLDAVLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 126 NVK---KSNYDGILGINIGKNKDTpiekgAEDYLICMEKVYQYAGYIAVNISSPNTPGLRSLQYGEALDDLLSELKTKQS 202
Cdd:pfam01180 82 ELLkrrKEYPRPDLGINLSKAGMT-----VDDYVEVARKIGPFADYIELNVSCPNTPGLRALQTDPELAAILLKVVKEVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 203 EleekhgkyVPLALKIAPDLSD-DEIRQICESLIKNKIDGVIATNTTLDRSI--VEGMKHCDE--AGGLSGRPVQSRSTE 277
Cdd:pfam01180 157 K--------VPVLVKLAPDLTDiVIIDIADVALGEDGLDGINATNTTVRGMRidLKTEKPILAngTGGLSGPPIKPIALK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1515654850 278 VVRKLHEELGDKLPIIGVGGVDSYVAAKEKMMAGAKLVQVYSGFIYKGPGLVGDIVKNL 336
Cdd:pfam01180 229 VIRELYQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDEL 287
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
47-335 |
4.83e-78 |
|
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: 240.33 E-value: 4.83e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 47 VECMGLTFKNPVGLAAGLD-KNGECIDAFGAMGFGFVEVGTVTPRPQAGNDKPRLFRLV-------EAEGIINRMGFNNL 118
Cdd:cd02810 1 VNFLGLKLKNPFGVAAGPLlKTGELIARAAAAGFGAVVYKTVTLHPRPGNPLPRVARLPpegesypEQLGILNSFGLPNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 119 GVDNLVENVKKSNY---DGILGINIGKNkdtpiekGAEDYLICMEKVYQY-AGYIAVNISSPNTPGLRSL-QYGEALDDL 193
Cdd:cd02810 81 GLDVWLQDIAKAKKefpGQPLIASVGGS-------SKEDYVELARKIERAgAKALELNLSCPNVGGGRQLgQDPEAVANL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 194 LSELKTKQseleekhgkYVPLALKIAPDLSDDEIRQICESLIKNKIDGVIATNTTLDRSIVE---GMKHCDEAGGLSGRP 270
Cdd:cd02810 154 LKAVKAAV---------DIPLLVKLSPYFDLEDIVELAKAAERAGADGLTAINTISGRVVDLktvGPGPKRGTGGLSGAP 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1515654850 271 VQSRSTEVVRKLHEELGDKLPIIGVGGVDSYVAAKEKMMAGAKLVQVYSGFIYKGPGLVGDIVKN 335
Cdd:cd02810 225 IRPLALRWVARLAARLQLDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKIKKE 289
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
46-336 |
7.64e-28 |
|
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: 109.95 E-value: 7.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 46 PVECMGLTFKNPVGLAAGLDKNGECI-DAFGAMGFGFVEVGTVTPRPQAGNDKPRLFRLveAEGIINRMGFNNLGVDNLV 124
Cdd:cd04740 1 SVELAGLRLKNPVILASGTFGFGEELsRVADLGKLGAIVTKSITLEPREGNPPPRVVET--PGGMLNAIGLQNPGVEAFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 125 ENVK--KSNYDGILGINIGKnkDTPiekgaEDYLICMEKVYQY-AGYIAVNISSPNTPGlRSLQYG---EALDDLLSELK 198
Cdd:cd04740 79 EELLpwLREFGTPVIASIAG--STV-----EEFVEVAEKLADAgADAIELNISCPNVKG-GGMAFGtdpEAVAEIVKAVK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 199 TKQSeleekhgkyVPLALKIAPDLSDdeIRQICESLIKNKIDGVIATNTTLDRSI-------VEGMKHcdeaGGLSGRPV 271
Cdd:cd04740 151 KATD---------VPVIVKLTPNVTD--IVEIARAAEEAGADGLTLINTLKGMAIdietrkpILGNVT----GGLSGPAI 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1515654850 272 QSRSTEVVRKLHEELgdKLPIIGVGGVDSYVAAKEKMMAGAKLVQVYSGfIYKGPGLVGDIVKNL 336
Cdd:cd04740 216 KPIALRMVYQVYKAV--EIPIIGVGGIASGEDALEFLMAGASAVQVGTA-NFVDPEAFKEIIEGL 277
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
47-336 |
5.00e-27 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 107.93 E-value: 5.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 47 VECMGLTFKNPVGLAAG-LDKNGECIDAFGAMGFGFVEVGTVTPRPQAGNDKPRLfrlVEAE-GIINRMGFNNLGVDNLV 124
Cdd:PRK07259 4 VELPGLKLKNPVMPASGtFGFGGEYARFYDLNGLGAIVTKSTTLEPREGNPTPRI---AETPgGMLNAIGLQNPGVDAFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 125 ENVKKSNydgilginigKNKDTPI-----EKGAEDYLICMEKVYQYAGY--IAVNISSPNTPGlrslqYG-------EAL 190
Cdd:PRK07259 81 EEELPWL----------EEFDTPIianvaGSTEEEYAEVAEKLSKAPNVdaIELNISCPNVKH-----GGmafgtdpELA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 191 DDLLSELKTKQSeleekhgkyVPLALKIAPDLSDdeIRQICESLIKNKIDGVIATNTtldrsiVEGMKHCDEA------- 263
Cdd:PRK07259 146 YEVVKAVKEVVK---------VPVIVKLTPNVTD--IVEIAKAAEEAGADGLSLINT------LKGMAIDIKTrkpilan 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1515654850 264 --GGLSGRPVQSRSTEVVRKLHEELgdKLPIIGVGGVDSYVAAKEKMMAGAKLVQVYSGfIYKGPGLVGDIVKNL 336
Cdd:PRK07259 209 vtGGLSGPAIKPIALRMVYQVYQAV--DIPIIGMGGISSAEDAIEFIMAGASAVQVGTA-NFYDPYAFPKIIEGL 280
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
47-325 |
1.70e-26 |
|
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: 106.36 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 47 VECMGLTFKNPVGLAAG-LDKNGECIDAFGAMGFGFVEVGTVTPRPQAGNDKPRLfrlVEAE-GIINRMGFNNLGVDNLV 124
Cdd:TIGR01037 3 VELFGIRFKNPLILASGiMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTI---VETPcGMLNAIGLQNPGVEAFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 125 ENVKK--SNYDGILGINI-GKNKDTPIEKGAEdylicMEKVYQYAGYIAVNISSPN--TPGLRSLQYGEALDDLLSELKT 199
Cdd:TIGR01037 80 EELKPvrEEFPTPLIASVyGSSVEEFAEVAEK-----LEKAPPYVDAYELNLSCPHvkGGGIAIGQDPELSADVVKAVKD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 200 KQSeleekhgkyVPLALKIAPDLSDdeIRQICESLIKNKIDGVIATNTtldrsiVEGMK---------HCDEAGGLSGRP 270
Cdd:TIGR01037 155 KTD---------VPVFAKLSPNVTD--ITEIAKAAEEAGADGLTLINT------LRGMKidiktgkpiLANKTGGLSGPA 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1515654850 271 VQSRSTEVVRKLHEELGdkLPIIGVGGVDSYVAAKEKMMAGAKLVQVYSGFIYKG 325
Cdd:TIGR01037 218 IKPIALRMVYDVYKMVD--IPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYRG 270
|
|
| dihydoor_dh_Arch |
NF041011 |
dihydroorotate dehydrogenase PyrD; |
47-336 |
6.40e-21 |
|
dihydroorotate dehydrogenase PyrD;
Pssm-ID: 468940 Cd Length: 289 Bit Score: 90.77 E-value: 6.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 47 VECMGLTFKNPVGLAAG-LDKNGECIDAF-GAMGFGFVEVGTVTPRPQAGNDKPRLFRLvEAEGIINRMGFNNLGVDnLV 124
Cdd:NF041011 1 IRLAGLELEDPLIIASGiLPDVPEYIERVcEKYGPSAITTKTLTLNPLEPHKPPTVVKL-HDGCYLNAIGLGNPGIG-LL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 125 ENVKKSNYDGILGINiGKNKDTPIEKGaedylicmEKVYQYAGYIAVNISSPNTPGlrslqYGEALDDLLSELkTKqsel 204
Cdd:NF041011 79 EEIRVKLCPLIVSIG-GSSLEEIVEVA--------EIAEEKADAIELNLSSPNRKG-----YGASLASLVREI-VK---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 205 EEKHGKYVPLALKIAPDlsdDEIRQICESLIKNKIDGVIATNTtldrsiVEGMKHCDEA---------GGLSGRPVQSRS 275
Cdd:NF041011 140 AVKSVVKKPVFVKLGPW---DNVLEIAGKALEAGADGLTLINT------VKGMAIDVESfkpvlsygtGGISGKCIHPLA 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1515654850 276 TEVVRKLHEELgdKLPIIGVGGVDSYVAAKEKMMAGAKLVQVYSGFIYKGPGLVGDIVKNL 336
Cdd:NF041011 211 VRIIYDVYREY--EAEIIGVGGVFSWRDAIELMSVGAKAVGVGTAIIDKGLSVISEIRKGL 269
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
51-336 |
2.43e-18 |
|
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: 83.91 E-value: 2.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 51 GLTFKNPVGLAAG-LDKNGECIDAFGAMGFGFVEVGTVTPRPQAGNDKPRLFRLveAEGIINRMGFNNLGVDNLVENVKK 129
Cdd:cd04741 5 GLTISPPLMNAAGpWCTTLEDLLELAASSTGAVTTRSSTLAGRPGNPEPRYYAF--PLGSINSLGLPNLGLDYYLEYIRT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 130 snydgILGINIGKNKdtPI----EKGAEDYLICMEKV----YQYAGYIAVNISSPNTPGLRSLQY-GEALDDLLSELKTK 200
Cdd:cd04741 83 -----ISDGLPGSAK--PFfisvTGSAEDIAAMYKKIaahqKQFPLAMELNLSCPNVPGKPPPAYdFDATLEYLTAVKAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 201 QSeleekhgkyVPLALKIAPDLSDDEIRQICESLIK--NKIDGVIATNT-----TLD---RSIVegMKHCDEAGGLSGRP 270
Cdd:cd04741 156 YS---------IPVGVKTPPYTDPAQFDTLAEALNAfaCPISFITATNTlgnglVLDperETVV--LKPKTGFGGLAGAY 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1515654850 271 VQSRSTEVVRKLHEELGDKLPIIGVGGVDSYVAAKEKMMAGAKLVQVYSGFIYKGPGLVGDIVKNL 336
Cdd:cd04741 225 LHPLALGNVRTFRRLLPSEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEKEL 290
|
|
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
47-336 |
4.79e-15 |
|
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: 74.24 E-value: 4.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 47 VECMGLTFKNPVGLAAG--LDKNGECIDAFGAmGFGFVEVGTVTP-RPQAGNDKPRLFRLV-EAEGIInrmGFNNLGV-- 120
Cdd:cd02940 4 VTFCGIKFPNPFGLASAppTTSYPMIRRAFEA-GWGGAVTKTLGLdKDIVTNVSPRIARLRtSGRGQI---GFNNIELis 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 121 -DNLVENVK-----KSNY-DGIL--GINIGKNKD--TPIEKGAEDylicmekvyqyAGY--IAVNISSPNTPGLRSL--- 184
Cdd:cd02940 80 eKPLEYWLKeirelKKDFpDKILiaSIMCEYNKEdwTELAKLVEE-----------AGAdaLELNFSCPHGMPERGMgaa 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 185 --QYGEALDDLLSELKTkqseleekhGKYVPLALKIAPDLSDdeIRQICESLIKNKIDGVIATNT-------TLDRS--- 252
Cdd:cd02940 149 vgQDPELVEEICRWVRE---------AVKIPVIAKLTPNITD--IREIARAAKEGGADGVSAINTvnslmgvDLDGTppa 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 253 -IVEGMKhcdEAGGLSGRPVQSRSTEVVRKLHEELGDKLPIIGVGGVDSYVAAKEKMMAGAKLVQVYSGFIYKGPGLVGD 331
Cdd:cd02940 218 pGVEGKT---TYGGYSGPAVKPIALRAVSQIARAPEPGLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDD 294
|
....*
gi 1515654850 332 IVKNL 336
Cdd:cd02940 295 MCTGL 299
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
51-336 |
5.62e-14 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 71.52 E-value: 5.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 51 GLTFKNPVGLAAG-LDKNGECIDAFGAMGFGFVEVGTVTPRPQAGNDKPRLFRLveAEGIINRMGFNNLGVD---NLVEN 126
Cdd:PRK02506 8 GFKFDNCLMNAAGvYCMTKEELEEVEASAAGAFVTKSATLEPRPGNPEPRYADT--PLGSINSMGLPNLGFDyylDYVLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 127 VKKSNYDG-----ILGINIgknkdtpiekgaEDYLICMEKVYQ--YAGYIAVNISSPNTPGLRSLQYG-EALDDLLSELK 198
Cdd:PRK02506 86 LQKKGPNKphflsVVGLSP------------EETHTILKKIQAsdFNGLVELNLSCPNVPGKPQIAYDfETTEQILEEVF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 199 TKQSeleekhgkyVPLALKIAPDLSDDEIRQICESLIKNKIDGVIATNttldrSIVEGM-----------KHCDEAGGLS 267
Cdd:PRK02506 154 TYFT---------KPLGVKLPPYFDIVHFDQAAAIFNKFPLAFVNCIN-----SIGNGLvidpedetvviKPKNGFGGIG 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1515654850 268 GRPVQSRSTEVVRKLHEELGDKLPIIGVGGVDSYVAAKEKMMAGAKLVQVYSGFIYKGPGLVGDIVKNL 336
Cdd:PRK02506 220 GDYIKPTALANVRAFYQRLNPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKEL 288
|
|
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
212-336 |
2.45e-05 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 45.60 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654850 212 VPLALKIAPDLSDdeIRQICESLIKNKIDGVIATNTTLdrSI-------------VEGMKhcdEAGGLSGRPVQ----SR 274
Cdd:PLN02495 183 VPVWAKMTPNITD--ITQPARVALKSGCEGVAAINTIM--SVmginldtlrpepcVEGYS---TPGGYSSKAVRpialAK 255
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1515654850 275 STEVVRKLHEELGDKLPIIGVGGVDSYVAAKEKMMAGAKLVQVYSGFIYKGPGLVGDIVKNL 336
Cdd:PLN02495 256 VMAIAKMMKSEFPEDRSLSGIGGVETGGDAAEFILLGADTVQVCTGVMMHGYPLVKNLCAEL 317
|
|
| PRK04169 |
PRK04169 |
heptaprenylglyceryl phosphate synthase; |
262-317 |
1.48e-04 |
|
heptaprenylglyceryl phosphate synthase;
Pssm-ID: 235237 Cd Length: 232 Bit Score: 42.49 E-value: 1.48e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1515654850 262 EAGGLSGRPVqsrSTEVVRKLHEELGDKLPIIGvGGVDSYVAAKEKMMAGAKLVQV 317
Cdd:PRK04169 161 EYGGGAGDPV---PPEMVKAVKKALDITPLIYG-GGIRSPEQARELMAAGADTIVV 212
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