|
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: 598.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 1 MYYPFVRKALFQLDPERAHEFTFQQLRRITGTPFEALVRQKV----PAKPVNCMGLTFKNPLGLAAGLDKDGECIDALGA 76
Cdd:PRK05286 1 MYYPLARPLLFKLDPETAHELTIRALKRASRTPLLSLLRQRLtytdPRLPVTVMGLTFPNPVGLAAGFDKNGEAIDALGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 77 MGFGSIEIGTVTPRPQPGNDKPRLFRLVDAEGLINRMGFNNLGVDNLVENVKKAHYDGVLGINIGKNKDTPVEQGKDDYL 156
Cdd:PRK05286 81 LGFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKAYRGIPLGINIGKNKDTPLEDAVDDYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 157 ICMEKIYAYAGYIAINISSPNTPGLRTLQYGEALDDLLTAIKNKQNDLqamhHKYVPIAVKIAPDLSEEELIQVADSLVR 236
Cdd:PRK05286 161 ICLEKLYPYADYFTVNISSPNTPGLRDLQYGEALDELLAALKEAQAEL----HGYVPLLVKIAPDLSDEELDDIADLALE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 237 HNIDGVIATNTTLDRSLVQGMKNCDQTGGLSGRPLQLKSTEIIRRLSLELNGRLPIIGVGGIDSVIAAREKIAAGASLVQ 316
Cdd:PRK05286 237 HGIDGVIATNTTLSRDGLKGLPNADEAGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGASLVQ 316
|
330 340
....*....|....*....|
gi 481023921 317 IYSGFIFKGPPLIKEIVTHI 336
Cdd:PRK05286 317 IYSGLIYEGPGLVKEIVRGL 336
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
3-336 |
0e+00 |
|
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: 586.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 3 YPFVRKALFQLDPERAHEFTFQQLRRITGTPFEALVRQKVPAK---PVNCMGLTFKNPLGLAAGLDKDGECIDALGAMGF 79
Cdd:TIGR01036 1 YPLVRKLLFLLDPESAHELTFQFLRLGTGTPFLALLRSLFGASdplEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAMGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 80 GSIEIGTVTPRPQPGNDKPRLFRLVDAEGLINRMGFNNLGVDNLVENVKKAHYDGVLGINIGKNKDTPVEQGKDDYLICM 159
Cdd:TIGR01036 81 GFLEIGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLKRARYKGPIGINIGKNKDTPSEDAKEDYAACL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 160 EKIYAYAGYIAINISSPNTPGLRTLQYGEALDDLLTAIKNKQNDLQAMHHkyVPIAVKIAPDLSEEELIQVADSLVRHNI 239
Cdd:TIGR01036 161 RKLGPLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAVKQEQDGLRRVHR--VPVLVKIAPDLTESDLEDIADSLVELGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 240 DGVIATNTTLDRSLVQGMKNCDQTGGLSGRPLQLKSTEIIRRLSLELNGRLPIIGVGGIDSVIAAREKIAAGASLVQIYS 319
Cdd:TIGR01036 239 DGVIATNTTVSRSLVQGPKNSDETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGASLLQIYS 318
|
330
....*....|....*..
gi 481023921 320 GFIFKGPPLIKEIVTHI 336
Cdd:TIGR01036 319 GFIYWGPPLVKEIVKEI 335
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
7-336 |
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: 526.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 7 RKALFQLDPERAHEFTFQQLRRITGTPFEALVRQKVPAKPVNCMGLTFKNPLGLAAGLDKDGECIDALGAMGFGSIEIGT 86
Cdd:cd04738 1 RPLLFLLDPETAHRLAIRALKLGLGPPLLLLLVYDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFVEVGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 87 VTPRPQPGNDKPRLFRLVDAEGLINRMGFNNLGVDNLVENVKKA-HYDGVLGINIGKNKDTPVEQGKDDYLICMEKIYAY 165
Cdd:cd04738 81 VTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRrPRGGPLGVNIGKNKDTPLEDAVEDYVIGVRKLGPY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 166 AGYIAINISSPNTPGLRTLQYGEALDDLLTAIKNKQNDLqamhHKYVPIAVKIAPDLSEEELIQVADSLVRHNIDGVIAT 245
Cdd:cd04738 161 ADYLVVNVSSPNTPGLRDLQGKEALRELLTAVKEERNKL----GKKVPLLVKIAPDLSDEELEDIADVALEHGVDGIIAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 246 NTTLDRSLVQGMKNCDQTGGLSGRPLQLKSTEIIRRLSLELNGRLPIIGVGGIDSVIAAREKIAAGASLVQIYSGFIFKG 325
Cdd:cd04738 237 NTTISRPGLLRSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTGLVYEG 316
|
330
....*....|.
gi 481023921 326 PPLIKEIVTHI 336
Cdd:cd04738 317 PGLVKRIKREL 327
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
46-333 |
6.22e-114 |
|
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: 332.04 E-value: 6.22e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 46 PVNCMGLTFKNPLGLAAG-LDKDGECIDALGAMGFGSIEIGTVTPRPQPGNDKPRLFRLVDAEGLINRMGFNNLGVDNLV 124
Cdd:COG0167 3 SVELAGLKFPNPVGLASGfFDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDAFL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 125 ENVKKA-HYDGVLGINIGKNkdTPveqgkDDYLICMEKIYAY-AGYIAINISSPNTPG-LRTL-QYGEALDDLLTAIKNK 200
Cdd:COG0167 83 ERLLPAkRYDVPVIVNIGGN--TV-----EDYVELARRLADAgADYLELNISCPNTPGgGRALgQDPEALAELLAAVKAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 201 QNdlqamhhkyVPIAVKIAPDLseEELIQVADSLVRHNIDGVIATNTTLDRS--LVQGMKN-CDQTGGLSGRPLQLKSTE 277
Cdd:COG0167 156 TD---------KPVLVKLAPDL--TDIVEIARAAEEAGADGVIAINTTLGRAidLETRRPVlANEAGGLSGPALKPIALR 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 481023921 278 IIRRLSLELNGRLPIIGVGGIDSVIAAREKIAAGASLVQIYSGFIFKGPPLIKEIV 333
Cdd:COG0167 225 MVREVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRII 280
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
47-332 |
1.47e-93 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 280.00 E-value: 1.47e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 47 VNCMGLTFKNPLGLAAGLDKDGECIDALGAMG-FGSIEIGTVTPRPQPGNDKPRLFRLVdaEGLINRMGFNNLGVDNLVE 125
Cdd:pfam01180 4 TKIPGLDFKNPIGLASGFDKFGEEALKWLALGkFGAIEIKSVTPYPQPGNPTPRVFRLP--EGVLNRMGLNNPGLDAVLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 126 NVK---KAHYDGVLGINIGKNKDTpveqgKDDYLICMEKIYAYAGYIAINISSPNTPGLRTLQYGEALDDLLTAIKNKQN 202
Cdd:pfam01180 82 ELLkrrKEYPRPDLGINLSKAGMT-----VDDYVEVARKIGPFADYIELNVSCPNTPGLRALQTDPELAAILLKVVKEVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 203 DlqamhhkyVPIAVKIAPDLSEEELIQVADSLVR-HNIDGVIATNTTLDRSL--VQGMKNCDQ--TGGLSGRPLQLKSTE 277
Cdd:pfam01180 157 K--------VPVLVKLAPDLTDIVIIDIADVALGeDGLDGINATNTTVRGMRidLKTEKPILAngTGGLSGPPIKPIALK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 481023921 278 IIRRLSLELNGRLPIIGVGGIDSVIAAREKIAAGASLVQIYSGFIFKGPPLIKEI 332
Cdd:pfam01180 229 VIRELYQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKI 283
|
|
| |
|
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: 598.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 1 MYYPFVRKALFQLDPERAHEFTFQQLRRITGTPFEALVRQKV----PAKPVNCMGLTFKNPLGLAAGLDKDGECIDALGA 76
Cdd:PRK05286 1 MYYPLARPLLFKLDPETAHELTIRALKRASRTPLLSLLRQRLtytdPRLPVTVMGLTFPNPVGLAAGFDKNGEAIDALGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 77 MGFGSIEIGTVTPRPQPGNDKPRLFRLVDAEGLINRMGFNNLGVDNLVENVKKAHYDGVLGINIGKNKDTPVEQGKDDYL 156
Cdd:PRK05286 81 LGFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKAYRGIPLGINIGKNKDTPLEDAVDDYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 157 ICMEKIYAYAGYIAINISSPNTPGLRTLQYGEALDDLLTAIKNKQNDLqamhHKYVPIAVKIAPDLSEEELIQVADSLVR 236
Cdd:PRK05286 161 ICLEKLYPYADYFTVNISSPNTPGLRDLQYGEALDELLAALKEAQAEL----HGYVPLLVKIAPDLSDEELDDIADLALE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 237 HNIDGVIATNTTLDRSLVQGMKNCDQTGGLSGRPLQLKSTEIIRRLSLELNGRLPIIGVGGIDSVIAAREKIAAGASLVQ 316
Cdd:PRK05286 237 HGIDGVIATNTTLSRDGLKGLPNADEAGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGASLVQ 316
|
330 340
....*....|....*....|
gi 481023921 317 IYSGFIFKGPPLIKEIVTHI 336
Cdd:PRK05286 317 IYSGLIYEGPGLVKEIVRGL 336
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
3-336 |
0e+00 |
|
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: 586.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 3 YPFVRKALFQLDPERAHEFTFQQLRRITGTPFEALVRQKVPAK---PVNCMGLTFKNPLGLAAGLDKDGECIDALGAMGF 79
Cdd:TIGR01036 1 YPLVRKLLFLLDPESAHELTFQFLRLGTGTPFLALLRSLFGASdplEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAMGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 80 GSIEIGTVTPRPQPGNDKPRLFRLVDAEGLINRMGFNNLGVDNLVENVKKAHYDGVLGINIGKNKDTPVEQGKDDYLICM 159
Cdd:TIGR01036 81 GFLEIGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLKRARYKGPIGINIGKNKDTPSEDAKEDYAACL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 160 EKIYAYAGYIAINISSPNTPGLRTLQYGEALDDLLTAIKNKQNDLQAMHHkyVPIAVKIAPDLSEEELIQVADSLVRHNI 239
Cdd:TIGR01036 161 RKLGPLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAVKQEQDGLRRVHR--VPVLVKIAPDLTESDLEDIADSLVELGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 240 DGVIATNTTLDRSLVQGMKNCDQTGGLSGRPLQLKSTEIIRRLSLELNGRLPIIGVGGIDSVIAAREKIAAGASLVQIYS 319
Cdd:TIGR01036 239 DGVIATNTTVSRSLVQGPKNSDETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGASLLQIYS 318
|
330
....*....|....*..
gi 481023921 320 GFIFKGPPLIKEIVTHI 336
Cdd:TIGR01036 319 GFIYWGPPLVKEIVKEI 335
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
7-336 |
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: 526.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 7 RKALFQLDPERAHEFTFQQLRRITGTPFEALVRQKVPAKPVNCMGLTFKNPLGLAAGLDKDGECIDALGAMGFGSIEIGT 86
Cdd:cd04738 1 RPLLFLLDPETAHRLAIRALKLGLGPPLLLLLVYDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFVEVGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 87 VTPRPQPGNDKPRLFRLVDAEGLINRMGFNNLGVDNLVENVKKA-HYDGVLGINIGKNKDTPVEQGKDDYLICMEKIYAY 165
Cdd:cd04738 81 VTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRrPRGGPLGVNIGKNKDTPLEDAVEDYVIGVRKLGPY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 166 AGYIAINISSPNTPGLRTLQYGEALDDLLTAIKNKQNDLqamhHKYVPIAVKIAPDLSEEELIQVADSLVRHNIDGVIAT 245
Cdd:cd04738 161 ADYLVVNVSSPNTPGLRDLQGKEALRELLTAVKEERNKL----GKKVPLLVKIAPDLSDEELEDIADVALEHGVDGIIAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 246 NTTLDRSLVQGMKNCDQTGGLSGRPLQLKSTEIIRRLSLELNGRLPIIGVGGIDSVIAAREKIAAGASLVQIYSGFIFKG 325
Cdd:cd04738 237 NTTISRPGLLRSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTGLVYEG 316
|
330
....*....|.
gi 481023921 326 PPLIKEIVTHI 336
Cdd:cd04738 317 PGLVKRIKREL 327
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
46-333 |
6.22e-114 |
|
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: 332.04 E-value: 6.22e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 46 PVNCMGLTFKNPLGLAAG-LDKDGECIDALGAMGFGSIEIGTVTPRPQPGNDKPRLFRLVDAEGLINRMGFNNLGVDNLV 124
Cdd:COG0167 3 SVELAGLKFPNPVGLASGfFDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDAFL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 125 ENVKKA-HYDGVLGINIGKNkdTPveqgkDDYLICMEKIYAY-AGYIAINISSPNTPG-LRTL-QYGEALDDLLTAIKNK 200
Cdd:COG0167 83 ERLLPAkRYDVPVIVNIGGN--TV-----EDYVELARRLADAgADYLELNISCPNTPGgGRALgQDPEALAELLAAVKAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 201 QNdlqamhhkyVPIAVKIAPDLseEELIQVADSLVRHNIDGVIATNTTLDRS--LVQGMKN-CDQTGGLSGRPLQLKSTE 277
Cdd:COG0167 156 TD---------KPVLVKLAPDL--TDIVEIARAAEEAGADGVIAINTTLGRAidLETRRPVlANEAGGLSGPALKPIALR 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 481023921 278 IIRRLSLELNGRLPIIGVGGIDSVIAAREKIAAGASLVQIYSGFIFKGPPLIKEIV 333
Cdd:COG0167 225 MVREVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRII 280
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
2-332 |
1.68e-110 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 327.46 E-value: 1.68e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 2 YYPFVRKalfqLDPERAHEFTFQQLRRITGtPFEAlvRQKVPAKPVNCMGLTFKNPLGLAAGLDKDGECIDALGAMGFGS 81
Cdd:PLN02826 38 VNPLFRL----LDPETAHSLAISAAARGLV-PREK--RPDPSVLGVEVWGRTFSNPIGLAAGFDKNAEAVEGLLGLGFGF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 82 IEIGTVTPRPQPGNDKPRLFRLVDAEGLINRMGFNNLGVD----NLVENVKKAHYD--------------------GVLG 137
Cdd:PLN02826 111 VEIGSVTPLPQPGNPKPRVFRLREEGAIINRYGFNSEGIVavakRLGAQHGKRKLDetssssfssddvkaggkagpGILG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 138 INIGKNKDTpvEQGKDDYLICMEKIYAYAGYIAINISSPNTPGLRTLQYGEALDDLLTAIKNKQNDLQAMHHKYVPIAVK 217
Cdd:PLN02826 191 VNLGKNKTS--EDAAADYVQGVRALSQYADYLVINVSSPNTPGLRKLQGRKQLKDLLKKVLAARDEMQWGEEGPPPLLVK 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 218 IAPDLSEEELIQVADSLVRHNIDGVIATNTTLDR-SLVQGMKNCDQTGGLSGRPLQLKSTEIIRRLSLELNGRLPIIGVG 296
Cdd:PLN02826 269 IAPDLSKEDLEDIAAVALALGIDGLIISNTTISRpDSVLGHPHADEAGGLSGKPLFDLSTEVLREMYRLTRGKIPLVGCG 348
|
330 340 350
....*....|....*....|....*....|....*.
gi 481023921 297 GIDSVIAAREKIAAGASLVQIYSGFIFKGPPLIKEI 332
Cdd:PLN02826 349 GVSSGEDAYKKIRAGASLVQLYTAFAYEGPALIPRI 384
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
47-335 |
6.40e-94 |
|
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: 280.78 E-value: 6.40e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 47 VNCMGLTFKNPLGLAAGLD-KDGECIDALGAMGFGSIEIGTVTPRPQPGNDKPRLFRLV-------DAEGLINRMGFNNL 118
Cdd:cd02810 1 VNFLGLKLKNPFGVAAGPLlKTGELIARAAAAGFGAVVYKTVTLHPRPGNPLPRVARLPpegesypEQLGILNSFGLPNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 119 GVDNLVENVKKAHY---DGVLGINIGKNkdtpveqGKDDYLICMEKIYAY-AGYIAINISSPNTPGLRTL-QYGEALDDL 193
Cdd:cd02810 81 GLDVWLQDIAKAKKefpGQPLIASVGGS-------SKEDYVELARKIERAgAKALELNLSCPNVGGGRQLgQDPEAVANL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 194 LTAIKNKQndlqamhhkYVPIAVKIAPDLSEEELIQVADSLVRHNIDGVIATNTTLDRSLVQ---GMKNCDQTGGLSGRP 270
Cdd:cd02810 154 LKAVKAAV---------DIPLLVKLSPYFDLEDIVELAKAAERAGADGLTAINTISGRVVDLktvGPGPKRGTGGLSGAP 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 481023921 271 LQLKSTEIIRRLSLELNGRLPIIGVGGIDSVIAAREKIAAGASLVQIYSGFIFKGPPLIKEIVTH 335
Cdd:cd02810 225 IRPLALRWVARLAARLQLDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKIKKE 289
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
47-332 |
1.47e-93 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 280.00 E-value: 1.47e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 47 VNCMGLTFKNPLGLAAGLDKDGECIDALGAMG-FGSIEIGTVTPRPQPGNDKPRLFRLVdaEGLINRMGFNNLGVDNLVE 125
Cdd:pfam01180 4 TKIPGLDFKNPIGLASGFDKFGEEALKWLALGkFGAIEIKSVTPYPQPGNPTPRVFRLP--EGVLNRMGLNNPGLDAVLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 126 NVK---KAHYDGVLGINIGKNKDTpveqgKDDYLICMEKIYAYAGYIAINISSPNTPGLRTLQYGEALDDLLTAIKNKQN 202
Cdd:pfam01180 82 ELLkrrKEYPRPDLGINLSKAGMT-----VDDYVEVARKIGPFADYIELNVSCPNTPGLRALQTDPELAAILLKVVKEVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 203 DlqamhhkyVPIAVKIAPDLSEEELIQVADSLVR-HNIDGVIATNTTLDRSL--VQGMKNCDQ--TGGLSGRPLQLKSTE 277
Cdd:pfam01180 157 K--------VPVLVKLAPDLTDIVIIDIADVALGeDGLDGINATNTTVRGMRidLKTEKPILAngTGGLSGPPIKPIALK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 481023921 278 IIRRLSLELNGRLPIIGVGGIDSVIAAREKIAAGASLVQIYSGFIFKGPPLIKEI 332
Cdd:pfam01180 229 VIRELYQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKI 283
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
46-336 |
5.74e-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: 110.33 E-value: 5.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 46 PVNCMGLTFKNPLGLAAG-LDKDGECIDALGAMGFGSIEIGTVTPRPQPGNDKPRLFRLVDaeGLINRMGFNNLGVDNLV 124
Cdd:cd04740 1 SVELAGLRLKNPVILASGtFGFGEELSRVADLGKLGAIVTKSITLEPREGNPPPRVVETPG--GMLNAIGLQNPGVEAFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 125 ENVKKAHydgvlginigKNKDTPV-----EQGKDDYLICMEKIYAY-AGYIAINISSPNTPGlRTLQYG---EALDDLLT 195
Cdd:cd04740 79 EELLPWL----------REFGTPViasiaGSTVEEFVEVAEKLADAgADAIELNISCPNVKG-GGMAFGtdpEAVAEIVK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 196 AIKNKQNdlqamhhkyVPIAVKIAPDLSEeeLIQVADSLVRHNIDGVIATNTtldrslVQGMK-----------NcdQTG 264
Cdd:cd04740 148 AVKKATD---------VPVIVKLTPNVTD--IVEIARAAEEAGADGLTLINT------LKGMAidietrkpilgN--VTG 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 481023921 265 GLSG---RPLQLKsteIIRRLSLELNgrLPIIGVGGIDSVIAAREKIAAGASLVQIYSGfIFKGPPLIKEIVTHI 336
Cdd:cd04740 209 GLSGpaiKPIALR---MVYQVYKAVE--IPIIGVGGIASGEDALEFLMAGASAVQVGTA-NFVDPEAFKEIIEGL 277
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
47-324 |
1.73e-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: 1.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 47 VNCMGLTFKNPLGLAAG-LDKDGECIDALGAMGFGSIEIGTVTPRPQPGNDKPRLFRLvdAEGLINRMGFNNLGVDNLVE 125
Cdd:TIGR01037 3 VELFGIRFKNPLILASGiMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTIVET--PCGMLNAIGLQNPGVEAFLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 126 NVKKA--HYDGVLGINI-GKNKDTPVEQGKDdylicMEKIYAYAGYIAINISSPN--TPGLRTLQYGEALDDLLTAIKNK 200
Cdd:TIGR01037 81 ELKPVreEFPTPLIASVyGSSVEEFAEVAEK-----LEKAPPYVDAYELNLSCPHvkGGGIAIGQDPELSADVVKAVKDK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 201 QNdlqamhhkyVPIAVKIAPDLSEeeLIQVADSLVRHNIDGVIATNTtldrslVQGMKN---------CDQTGGLSGRPL 271
Cdd:TIGR01037 156 TD---------VPVFAKLSPNVTD--ITEIAKAAEEAGADGLTLINT------LRGMKIdiktgkpilANKTGGLSGPAI 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 481023921 272 QLKSTEIIRRLSLELNgrLPIIGVGGIDSVIAAREKIAAGASLVQI-----YSGFIFK 324
Cdd:TIGR01037 219 KPIALRMVYDVYKMVD--IPIIGVGGITSFEDALEFLMAGASAVQVgtavyYRGFAFK 274
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
47-333 |
2.77e-26 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 106.00 E-value: 2.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 47 VNCMGLTFKNPLGLAAG-LDKDGECIDALGAMGFGSIEIGTVTPRPQPGNDKPRLFRLVDaeGLINRMGFNNLGVDNLVE 125
Cdd:PRK07259 4 VELPGLKLKNPVMPASGtFGFGGEYARFYDLNGLGAIVTKSTTLEPREGNPTPRIAETPG--GMLNAIGLQNPGVDAFIE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 126 N--VKKAHYDGVLGINIGKNkdTPveqgkDDYLICMEKIYAYAGYIAI--NISSPNTPGlrtlqYG-------EALDDLL 194
Cdd:PRK07259 82 EelPWLEEFDTPIIANVAGS--TE-----EEYAEVAEKLSKAPNVDAIelNISCPNVKH-----GGmafgtdpELAYEVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 195 TAIKNKQNdlqamhhkyVPIAVKIAPDLSEeeLIQVADSLVRHNIDGVIATNTtldrslVQGMK-----------NcdQT 263
Cdd:PRK07259 150 KAVKEVVK---------VPVIVKLTPNVTD--IVEIAKAAEEAGADGLSLINT------LKGMAidiktrkpilaN--VT 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 481023921 264 GGLSG---RPLQLKsteIIRRLSLELNgrLPIIGVGGIDSVIAAREKIAAGASLVQIYSGfIFKGPPLIKEIV 333
Cdd:PRK07259 211 GGLSGpaiKPIALR---MVYQVYQAVD--IPIIGMGGISSAEDAIEFIMAGASAVQVGTA-NFYDPYAFPKII 277
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
47-332 |
8.99e-25 |
|
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: 8.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 47 VNCMGLTFKNPLGLAAG-LDKDGECIDALGAMGFGSIEIGTVTPRPQPGNDKPRLFRLvdAEGLINRMGFNNLGVDNLVE 125
Cdd:cd04741 1 VTPPGLTISPPLMNAAGpWCTTLEDLLELAASSTGAVTTRSSTLAGRPGNPEPRYYAF--PLGSINSLGLPNLGLDYYLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 126 NVKKAHYdgvlgINIGKNKD--TPVEQGKDDYLICMEKIYA----YAGYIAINISSPNTPGLRTLQY-GEALDDLLTAIK 198
Cdd:cd04741 79 YIRTISD-----GLPGSAKPffISVTGSAEDIAAMYKKIAAhqkqFPLAMELNLSCPNVPGKPPPAYdFDATLEYLTAVK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 199 nkqndlQAMHhkyVPIAVKIAPDLSEEELIQVADSLVRHN--IDGVIATNT-------TLDRSLVQgMKNCDQTGGLSG- 268
Cdd:cd04741 154 ------AAYS---IPVGVKTPPYTDPAQFDTLAEALNAFAcpISFITATNTlgnglvlDPERETVV-LKPKTGFGGLAGa 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 481023921 269 --RPLQLKSTEIIRRLsleLNGRLPIIGVGGIDSVIAAREKIAAGASLVQIYSGFIFKGPPLIKEI 332
Cdd:cd04741 224 ylHPLALGNVRTFRRL---LPSEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARI 286
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
51-326 |
6.44e-17 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 80.00 E-value: 6.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 51 GLTFKNPLGLAAG-LDKDGECIDALGAMGFGSIEIGTVTPRPQPGNDKPRLFRLvdAEGLINRMGFNNLGVD---NLVEN 126
Cdd:PRK02506 8 GFKFDNCLMNAAGvYCMTKEELEEVEASAAGAFVTKSATLEPRPGNPEPRYADT--PLGSINSMGLPNLGFDyylDYVLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 127 VKKAHYDGVLGINIgknkdtpVEQGKDDYLICMEKIYA--YAGYIAINISSPNTPGLRTLQYG-EALDDLLTAIknkqnd 203
Cdd:PRK02506 86 LQKKGPNKPHFLSV-------VGLSPEETHTILKKIQAsdFNGLVELNLSCPNVPGKPQIAYDfETTEQILEEV------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 204 lqamhHKY--VPIAVKIAPDLSEEELIQVADSLVRHNIDGVIATNT---TL-----DRSLVQGMKNcdQTGGLSGRplQL 273
Cdd:PRK02506 153 -----FTYftKPLGVKLPPYFDIVHFDQAAAIFNKFPLAFVNCINSignGLvidpeDETVVIKPKN--GFGGIGGD--YI 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 481023921 274 KSTEI--IRRLSLELNGRLPIIGVGGIDSVIAAREKIAAGASLVQIYSGFIFKGP 326
Cdd:PRK02506 224 KPTALanVRAFYQRLNPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGP 278
|
|
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
47-334 |
1.26e-09 |
|
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: 58.45 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 47 VNCMGLTFKNPLGLAAG--LDKDGECIDALGAmGFGSIEIGTVTP-RPQPGNDKPRLFRLVDaeGLINRMGFNNLGV--- 120
Cdd:cd02940 4 VTFCGIKFPNPFGLASAppTTSYPMIRRAFEA-GWGGAVTKTLGLdKDIVTNVSPRIARLRT--SGRGQIGFNNIELise 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 121 ------DNLVENVKKAHYDGVLGINIgknkdtPVEQGKDDYLICMEKIY-AYAGYIAINISSPNTPGLRTL-----QYGE 188
Cdd:cd02940 81 kpleywLKEIRELKKDFPDKILIASI------MCEYNKEDWTELAKLVEeAGADALELNFSCPHGMPERGMgaavgQDPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 189 ALDDLLTAIKNKqndlqamhhKYVPIAVKIAPDLSEEEliQVADSLVRHNIDGVIATNT-------TLDRSLVQGMKNCD 261
Cdd:cd02940 155 LVEEICRWVREA---------VKIPVIAKLTPNITDIR--EIARAAKEGGADGVSAINTvnslmgvDLDGTPPAPGVEGK 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 481023921 262 QT-GGLSG---RPLQLKSTEIIRRlslELNGRLPIIGVGGIDSVIAAREKIAAGASLVQIYSGFIFKGPPLIKEIVT 334
Cdd:cd02940 224 TTyGGYSGpavKPIALRAVSQIAR---APEPGLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCT 297
|
|
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
212-334 |
6.75e-05 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 44.44 E-value: 6.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481023921 212 VPIAVKIAPDLSEeeLIQVADSLVRHNIDGVIATNTTLD------RSL-----VQGMKNcdqTGGLSG---RPLQL-KST 276
Cdd:PLN02495 183 VPVWAKMTPNITD--ITQPARVALKSGCEGVAAINTIMSvmginlDTLrpepcVEGYST---PGGYSSkavRPIALaKVM 257
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 481023921 277 EIIRRLSLELNGRLPIIGVGGIDSVIAAREKIAAGASLVQIYSGFIFKGPPLIKEIVT 334
Cdd:PLN02495 258 AIAKMMKSEFPEDRSLSGIGGVETGGDAAEFILLGADTVQVCTGVMMHGYPLVKNLCA 315
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
278-322 |
1.47e-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: 1.47e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 481023921 278 IIRRLSLELNGRLPIIGVGGIDSVIAAREKIAAGASLVQIYSGFI 322
Cdd:cd04735 273 IMELVKERIAGRLPLIAVGSINTPDDALEALETGADLVAIGRGLL 317
|
|
| |
