|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
4-342 |
0e+00 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 537.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 4 LFETLGRRALFTFDAEQAHGLSITGLKTG--------IVTCRTPEDPALSVKVAGLKFPNPLGMAAGYDKNAEVPDALLK 75
Cdd:PRK05286 1 MYYPLARPLLFKLDPETAHELTIRALKRAsrtpllslLRQRLTYTDPRLPVTVMGLTFPNPVGLAAGFDKNGEAIDALGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 76 LGFGFAEVGTLTPRPQSGNPRPRIFRLVDDKAVINRLGFNNEGHEAAFKRLsRRAGKSGIVGVNIGANKD--AEDRIADY 153
Cdd:PRK05286 81 LGFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERL-KKAYRGIPLGINIGKNKDtpLEDAVDDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 154 VAGIRRFYQLARYFTVNISSPNTPGLRNLQAREALHELLSRVLEARDEEGNmctlKRPVFLKIAPDLTDEELDDIAAEAD 233
Cdd:PRK05286 160 LICLEKLYPYADYFTVNISSPNTPGLRDLQYGEALDELLAALKEAQAELHG----YVPLLVKIAPDLSDEELDDIADLAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 234 AQKLDGIIVSNTTLSRSGLKNPENSNETGGLSGAPLFERSTVVLARMRERVGPDMPLIGVGGIDSAETALAKIKAGADLV 313
Cdd:PRK05286 236 EHGIDGVIATNTTLSRDGLKGLPNADEAGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGASLV 315
|
330 340
....*....|....*....|....*....
gi 81847184 314 QLYTGLIYRGPGLPGEILRGLSTAIKHEG 342
Cdd:PRK05286 316 QIYSGLIYEGPGLVKEIVRGLARLLRRDG 344
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
10-334 |
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: 525.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 10 RRALFTFDAEQAHGLSITGLKTGIVTC----RTPEDPALSVKVAGLKFPNPLGMAAGYDKNAEVPDALLKLGFGFAEVGT 85
Cdd:cd04738 1 RPLLFLLDPETAHRLAIRALKLGLGPPllllLVYDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFVEVGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 86 LTPRPQSGNPRPRIFRLVDDKAVINRLGFNNEGHEAAFKRLSRRAGKSGIVGVNIGANKD--AEDRIADYVAGIRRFYQL 163
Cdd:cd04738 81 VTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRRPRGGPLGVNIGKNKDtpLEDAVEDYVIGVRKLGPY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 164 ARYFTVNISSPNTPGLRNLQAREALHELLSRVLEARDEEGNmctlKRPVFLKIAPDLTDEELDDIAAEADAQKLDGIIVS 243
Cdd:cd04738 161 ADYLVVNVSSPNTPGLRDLQGKEALRELLTAVKEERNKLGK----KVPLLVKIAPDLSDEELEDIADVALEHGVDGIIAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 244 NTTLSRSGLKNPENSNETGGLSGAPLFERSTVVLARMRERVGPDMPLIGVGGIDSAETALAKIKAGADLVQLYTGLIYRG 323
Cdd:cd04738 237 NTTISRPGLLRSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTGLVYEG 316
|
330
....*....|.
gi 81847184 324 PGLPGEILRGL 334
Cdd:cd04738 317 PGLVKRIKREL 327
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
16-348 |
1.39e-133 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 387.56 E-value: 1.39e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 16 FDAEQAHGLSITGLKTGIVTCRT-PEDPALSVKVAGLKFPNPLGMAAGYDKNAEVPDALLKLGFGFAEVGTLTPRPQSGN 94
Cdd:PLN02826 45 LDPETAHSLAISAAARGLVPREKrPDPSVLGVEVWGRTFSNPIGLAAGFDKNAEAVEGLLGLGFGFVEIGSVTPLPQPGN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 95 PRPRIFRLVDDKAVINRLGFNNEGHEAAFKRLSRRAGK-----------------------SGIVGVNIGANKDAEDRIA 151
Cdd:PLN02826 125 PKPRVFRLREEGAIINRYGFNSEGIVAVAKRLGAQHGKrkldetssssfssddvkaggkagPGILGVNLGKNKTSEDAAA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 152 DYVAGIRRFYQLARYFTVNISSPNTPGLRNLQAREALHELLSRVLEARDEEGNMCTLKRPVFLKIAPDLTDEELDDIAAE 231
Cdd:PLN02826 205 DYVQGVRALSQYADYLVINVSSPNTPGLRKLQGRKQLKDLLKKVLAARDEMQWGEEGPPPLLVKIAPDLSKEDLEDIAAV 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 232 ADAQKLDGIIVSNTTLSRSG-LKNPENSNETGGLSGAPLFERSTVVLARMRERVGPDMPLIGVGGIDSAETALAKIKAGA 310
Cdd:PLN02826 285 ALALGIDGLIISNTTISRPDsVLGHPHADEAGGLSGKPLFDLSTEVLREMYRLTRGKIPLVGCGGVSSGEDAYKKIRAGA 364
|
330 340 350
....*....|....*....|....*....|....*...
gi 81847184 311 DLVQLYTGLIYRGPGLPGEILRGLSTAIKHEGVSSIAE 348
Cdd:PLN02826 365 SLVQLYTAFAYEGPALIPRIKAELAACLERDGFKSIQE 402
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
6-334 |
1.17e-127 |
|
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: 369.50 E-value: 1.17e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 6 ETLGRRALFTFDAEQAHGLSITGLKTG-------IVTCRTPEDPALSVKVAGLKFPNPLGMAAGYDKNAEVPDALLKLGF 78
Cdd:TIGR01036 1 YPLVRKLLFLLDPESAHELTFQFLRLGtgtpflaLLRSLFGASDPLEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAMGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 79 GFAEVGTLTPRPQSGNPRPRIFRLVDDKAVINRLGFNNEGHEAAFKRLsRRAGKSGIVGVNIGANKD--AEDRIADYVAG 156
Cdd:TIGR01036 81 GFLEIGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERL-KRARYKGPIGINIGKNKDtpSEDAKEDYAAC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 157 IRRFYQLARYFTVNISSPNTPGLRNLQAREALHELLSRVLEARDEEGNMctLKRPVFLKIAPDLTDEELDDIAAEADAQK 236
Cdd:TIGR01036 160 LRKLGPLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAVKQEQDGLRRV--HRVPVLVKIAPDLTESDLEDIADSLVELG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 237 LDGIIVSNTTLSRSGLKNPENSNETGGLSGAPLFERSTVVLARMRERVGPDMPLIGVGGIDSAETALAKIKAGADLVQLY 316
Cdd:TIGR01036 238 IDGVIATNTTVSRSLVQGPKNSDETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGASLLQIY 317
|
330
....*....|....*...
gi 81847184 317 TGLIYRGPGLPGEILRGL 334
Cdd:TIGR01036 318 SGFIYWGPPLVKEIVKEI 335
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
44-347 |
3.02e-126 |
|
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: 364.39 E-value: 3.02e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 44 LSVKVAGLKFPNPLGMAAG-YDKNAEVPDALLKLGFGFAEVGTLTPRPQSGNPRPRIFRLVDDKAVINRLGFNNEGHEAA 122
Cdd:COG0167 2 LSVELAGLKFPNPVGLASGfFDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 123 FKRLSRRAGKSGIVGVNIGANkdaedRIADYVAGIRRFYQL-ARYFTVNISSPNTPG-LRNL-QAREALHELLSRVLEAR 199
Cdd:COG0167 82 LERLLPAKRYDVPVIVNIGGN-----TVEDYVELARRLADAgADYLELNISCPNTPGgGRALgQDPEALAELLAAVKAAT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 200 DeegnmctlkRPVFLKIAPDLTDeeLDDIAAEADAQKLDGIIVSNTTLSRS-GLKN--PENSNETGGLSGAPLFERSTVV 276
Cdd:COG0167 157 D---------KPVLVKLAPDLTD--IVEIARAAEEAGADGVIAINTTLGRAiDLETrrPVLANEAGGLSGPALKPIALRM 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81847184 277 LARMRERVGPDMPLIGVGGIDSAETALAKIKAGADLVQLYTGLIYRGPGLPGEILRGLSTAIKHEGVSSIA 347
Cdd:COG0167 226 VREVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSIS 296
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
44-334 |
2.85e-98 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 293.10 E-value: 2.85e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 44 LSVKVAGLKFPNPLGMAAGYDKNAEVPDALLKLG-FGFAEVGTLTPRPQSGNPRPRIFRLVDDkaVINRLGFNNEGHEA- 121
Cdd:pfam01180 2 LATKIPGLDFKNPIGLASGFDKFGEEALKWLALGkFGAIEIKSVTPYPQPGNPTPRVFRLPEG--VLNRMGLNNPGLDAv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 122 -AFKRLSRRAGKSGIVGVNIGANKDAEDriaDYVAGIRRFYQLARYFTVNISSPNTPGLRNLQAREALHELLSRVLEARD 200
Cdd:pfam01180 80 lAELLKRRKEYPRPDLGINLSKAGMTVD---DYVEVARKIGPFADYIELNVSCPNTPGLRALQTDPELAAILLKVVKEVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 201 eegnmctlKRPVFLKIAPDLTDEELDDIAAEA-DAQKLDGIIVSNTTLSRSGL----KNPENSNETGGLSGAPLFERSTV 275
Cdd:pfam01180 157 --------KVPVLVKLAPDLTDIVIIDIADVAlGEDGLDGINATNTTVRGMRIdlktEKPILANGTGGLSGPPIKPIALK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 81847184 276 VLARMRERVGPDMPLIGVGGIDSAETALAKIKAGADLVQLYTGLIYRGPGLPGEILRGL 334
Cdd:pfam01180 229 VIRELYQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDEL 287
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
46-330 |
1.74e-61 |
|
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: 198.73 E-value: 1.74e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 46 VKVAGLKFPNPLGMAAGYD-KNAEVPDALLKLGFGFAEVGTLTPRPQSGNPRPRIFRLVDDK-------AVINRLGFNNE 117
Cdd:cd02810 1 VNFLGLKLKNPFGVAAGPLlKTGELIARAAAAGFGAVVYKTVTLHPRPGNPLPRVARLPPEGesypeqlGILNSFGLPNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 118 GHEAAFK--RLSRRAGKSGIVGVNIGANKdaedrIADYVAGIRRFYQL-ARYFTVNISSPNTPGLRNL-QAREALHELLS 193
Cdd:cd02810 81 GLDVWLQdiAKAKKEFPGQPLIASVGGSS-----KEDYVELARKIERAgAKALELNLSCPNVGGGRQLgQDPEAVANLLK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 194 RVLEARDeegnmctlkRPVFLKIAPDLTDEELDDIAAEADAQKLDGIIVSNTTLSRSGLKN---PENSNETGGLSGAPLF 270
Cdd:cd02810 156 AVKAAVD---------IPLLVKLSPYFDLEDIVELAKAAERAGADGLTAINTISGRVVDLKtvgPGPKRGTGGLSGAPIR 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 271 ERSTVVLARMRERVGPDMPLIGVGGIDSAETALAKIKAGADLVQLYTGLIYRGPGLPGEI 330
Cdd:cd02810 227 PLALRWVARLAARLQLDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKI 286
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
45-350 |
4.61e-32 |
|
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: 121.89 E-value: 4.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 45 SVKVAGLKFPNPLGMAAG-YDKNAEVPDALLKLGFGFAEVGTLTPRPQSGNPRPRIFRLVDdkAVINRLGFNNEGHEAAF 123
Cdd:cd04740 1 SVELAGLRLKNPVILASGtFGFGEELSRVADLGKLGAIVTKSITLEPREGNPPPRVVETPG--GMLNAIGLQNPGVEAFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 124 KRLSRRAGKSGI-VGVNIGAnkdaeDRIADYVAGIRRFYQL-ARYFTVNISSPNTP-GLRNLQAR-EALHELLSRVLEAr 199
Cdd:cd04740 79 EELLPWLREFGTpVIASIAG-----STVEEFVEVAEKLADAgADAIELNISCPNVKgGGMAFGTDpEAVAEIVKAVKKA- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 200 deegnmctLKRPVFLKIAPDLTD-EELDDIAAEADAqklDGIIVSNTTLsrsGLK-NPEN-----SNETGGLSGAPLFER 272
Cdd:cd04740 153 --------TDVPVIVKLTPNVTDiVEIARAAEEAGA---DGLTLINTLK---GMAiDIETrkpilGNVTGGLSGPAIKPI 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81847184 273 STVVLARMRERVgpDMPLIGVGGIDSAETALAKIKAGADLVQLYTGLIYrGPGLPGEILRGLSTAIKHEGVSSIAELR 350
Cdd:cd04740 219 ALRMVYQVYKAV--EIPIIGVGGIASGEDALEFLMAGASAVQVGTANFV-DPEAFKEIIEGLEAYLDEEGIKSIEELV 293
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
44-350 |
1.55e-28 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 112.55 E-value: 1.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 44 LSVKVAGLKFPNPLGMAAG-YDKNAEVPDALLKLGFGFAEVGTLTPRPQSGNPRPRIFRLvdDKAVINRLGFNNEGHEAA 122
Cdd:PRK07259 2 LSVELPGLKLKNPVMPASGtFGFGGEYARFYDLNGLGAIVTKSTTLEPREGNPTPRIAET--PGGMLNAIGLQNPGVDAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 123 FKRLSRRAGKSGI-VGVNIGAnKDAEDriadYVAGIRRF--YQLARYFTVNISSPNTP--GLRNLQAREALHELLSRVLE 197
Cdd:PRK07259 80 IEEELPWLEEFDTpIIANVAG-STEEE----YAEVAEKLskAPNVDAIELNISCPNVKhgGMAFGTDPELAYEVVKAVKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 198 ArdeegnmctLKRPVFLKIAPDLTDeeLDDIAAEADAQKLDGIIVSNTTLsrsGLK------NPENSNETGGLSGAPLFE 271
Cdd:PRK07259 155 V---------VKVPVIVKLTPNVTD--IVEIAKAAEEAGADGLSLINTLK---GMAidiktrKPILANVTGGLSGPAIKP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 272 rstvVLARM----RERVgpDMPLIGVGGIDSAETALAKIKAGADLVQLYTGlIYRGPGLPGEILRGLSTAIKHEGVSSIA 347
Cdd:PRK07259 221 ----IALRMvyqvYQAV--DIPIIGMGGISSAEDAIEFIMAGASAVQVGTA-NFYDPYAFPKIIEGLEAYLDKYGIKSIE 293
|
...
gi 81847184 348 ELR 350
Cdd:PRK07259 294 EIV 296
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
44-349 |
1.13e-25 |
|
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 dihydroorotate dehydrogenases while excluding the closely related subfamily 2 (TIGR01036). This family also includes a number of uncharacterized proteins and a domain of dihydropyrimidine dehydrogenase. The uncharacterized proteins might all be dihydroorotate dehydrogenase.
Pssm-ID: 130109 [Multi-domain] Cd Length: 300 Bit Score: 104.82 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 44 LSVKVAGLKFPNPLGMAAG-YDKNAEVPDALLKLGFGFAEVGTLTPRPQSGNPRPRIfrlVDDKA-VINRLGFNNEGHEA 121
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGiMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTI---VETPCgMLNAIGLQNPGVEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 122 AFKRLS--RRAGKSGIVGVNIGANkdaEDRIADYVAGIRRFYQLARYFTVNISSPN--TPGLRNLQAREALHELLSRVLE 197
Cdd:TIGR01037 78 FLEELKpvREEFPTPLIASVYGSS---VEEFAEVAEKLEKAPPYVDAYELNLSCPHvkGGGIAIGQDPELSADVVKAVKD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 198 ArdeegnmctLKRPVFLKIAPDLTD-EELDDIAAEADAqklDGIIVSNTTLsrsGLK------NPENSNETGGLSGA--- 267
Cdd:TIGR01037 155 K---------TDVPVFAKLSPNVTDiTEIAKAAEEAGA---DGLTLINTLR---GMKidiktgKPILANKTGGLSGPaik 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 268 PLFERSTVVLARMRervgpDMPLIGVGGIDSAETALAKIKAGADLVQLYTGLIYRgPGLPGEILRGLSTAIKHEGVSSIA 347
Cdd:TIGR01037 220 PIALRMVYDVYKMV-----DIPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYR-GFAFKKIIEGLIAFLKAEGFTSIE 293
|
..
gi 81847184 348 EL 349
Cdd:TIGR01037 294 EL 295
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
46-334 |
8.42e-19 |
|
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: 85.45 E-value: 8.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 46 VKVAGLKFPNPLGMAAG-YDKNAEVPDALLKLGFGFAEVGTLTPRPQSGNPRPRIFRLvdDKAVINRLGFNNEGHEAAFK 124
Cdd:cd04741 1 VTPPGLTISPPLMNAAGpWCTTLEDLLELAASSTGAVTTRSSTLAGRPGNPEPRYYAF--PLGSINSLGLPNLGLDYYLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 125 RLSRRA------GKSGIVGVNiGAnkdAEDRIADY--VAGIRRFYQLAryFTVNISSPNTPGLRNLQA-REALHELLSRV 195
Cdd:cd04741 79 YIRTISdglpgsAKPFFISVT-GS---AEDIAAMYkkIAAHQKQFPLA--MELNLSCPNVPGKPPPAYdFDATLEYLTAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 196 LEArdeegnmctLKRPVFLKIAPdLTDEELDDIAAEADAQKLDGI--IVSNTTLSRSGLKNPENS-------NETGGLSG 266
Cdd:cd04741 153 KAA---------YSIPVGVKTPP-YTDPAQFDTLAEALNAFACPIsfITATNTLGNGLVLDPEREtvvlkpkTGFGGLAG 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81847184 267 APLFERSTVVLARMRERVGPDMPLIGVGGIDSAETALAKIKAGADLVQLYTGLIYRGPGLPGEILRGL 334
Cdd:cd04741 223 AYLHPLALGNVRTFRRLLPSEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEKEL 290
|
|
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
44-334 |
1.78e-16 |
|
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: 78.87 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 44 LSVKVAGLKFPNPLGMAAG-----YDKNAEVPDAllklGFGFAEVGTLTP-RPQSGNPRPRIFRLVDDKAVInrLGFNN- 116
Cdd:cd02940 2 LSVTFCGIKFPNPFGLASAppttsYPMIRRAFEA----GWGGAVTKTLGLdKDIVTNVSPRIARLRTSGRGQ--IGFNNi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 117 --------EGHEAAFKRLSRRAGKSGIVGVNIGA-NKDAEDRIADYV--AGirrfyqlARYFTVNISSPNTPGLRNL--- 182
Cdd:cd02940 76 elisekplEYWLKEIRELKKDFPDKILIASIMCEyNKEDWTELAKLVeeAG-------ADALELNFSCPHGMPERGMgaa 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 183 --QAREALHELLSRVLEArdeegnmCTLkrPVFLKIAPDLTDEEldDIAAEADAQKLDGIIVSNTTLSRSGLK----NPE 256
Cdd:cd02940 149 vgQDPELVEEICRWVREA-------VKI--PVIAKLTPNITDIR--EIARAAKEGGADGVSAINTVNSLMGVDldgtPPA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 257 ---NSNET-GGLSGA---PLFERSTVVLARMrerVGPDMPLIGVGGIDSAETALAKIKAGADLVQLYTGLIYRGPGLPGE 329
Cdd:cd02940 218 pgvEGKTTyGGYSGPavkPIALRAVSQIARA---PEPGLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDD 294
|
....*
gi 81847184 330 ILRGL 334
Cdd:cd02940 295 MCTGL 299
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
44-350 |
3.75e-12 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 66.13 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 44 LSVKVAGLKFPNPLGMAAG-YDKNAEVPDALLKLGFG--FAEVGTLTPRPqsGNPRPRIFRLvdDKAVINRLGFNNEGHE 120
Cdd:PRK02506 2 TSTQIAGFKFDNCLMNAAGvYCMTKEELEEVEASAAGafVTKSATLEPRP--GNPEPRYADT--PLGSINSMGLPNLGFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 121 AAFKRLSRRAGKSG-------IVGVNIgankdaEDRIAdyvagIRRFYQLARYFT---VNISSPNTPGLRNLQAR-EALH 189
Cdd:PRK02506 78 YYLDYVLELQKKGPnkphflsVVGLSP------EETHT-----ILKKIQASDFNGlveLNLSCPNVPGKPQIAYDfETTE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 190 ELLSRVLEArdeegnmctLKRPVFLKIAPDLTDEELDDIAAeadaqkldgiivsntTLSRSGLK--NPENS--------- 258
Cdd:PRK02506 147 QILEEVFTY---------FTKPLGVKLPPYFDIVHFDQAAA---------------IFNKFPLAfvNCINSignglvidp 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 259 -NET---------GGLSGA---PlferstVVLARMRE---RVGPDMPLIGVGGIDSAETALAKIKAGADLVQLYTGLIYR 322
Cdd:PRK02506 203 eDETvvikpkngfGGIGGDyikP------TALANVRAfyqRLNPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKE 276
|
330 340
....*....|....*....|....*...
gi 81847184 323 GPGLPGEILRGLSTAIKHEGVSSIAELR 350
Cdd:PRK02506 277 GPAVFERLTKELKAIMAEKGYQSLEDFR 304
|
|
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
40-350 |
5.22e-12 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 66.40 E-value: 5.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 40 EDPALSVKVAGLKFPNPLGMAAGY-DKNAEVPDALLKLGFG----------FAEVGTLTPR------PQSGNPRPRIF-- 100
Cdd:PLN02495 7 SEPDLSVTVNGLKMPNPFVIGSGPpGTNYTVMKRAFDEGWGgviaktvsldASKVINVTPRyarlraGANGSAKGRVIgw 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 101 ---RLVDDKAVINRLgfnnegheAAFKRLSRR-AGKSGIVGVNIGANKDAEDRIADYVAGIRrfyqlARYFTVNISSPNT 176
Cdd:PLN02495 87 qniELISDRPFETML--------AEFKQLKEEyPDRILIASIMEEYNKDAWEEIIERVEETG-----VDALEINFSCPHG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 177 PGLRNL-----QAREALHELLSRVLEArdeegnmCTLkrPVFLKIAPDLTDeeLDDIAAEADAQKLDGIIVSNTTLSRSG 251
Cdd:PLN02495 154 MPERKMgaavgQDCDLLEEVCGWINAK-------ATV--PVWAKMTPNITD--ITQPARVALKSGCEGVAAINTIMSVMG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 252 LK----NPENSNE----TGGLSGA---PLFERSTVVLARMRERVGP-DMPLIGVGGIDSAETALAKIKAGADLVQLYTGL 319
Cdd:PLN02495 223 INldtlRPEPCVEgystPGGYSSKavrPIALAKVMAIAKMMKSEFPeDRSLSGIGGVETGGDAAEFILLGADTVQVCTGV 302
|
330 340 350
....*....|....*....|....*....|.
gi 81847184 320 IYRGPGLPGEILRGLSTAIKHEGVSSIAELR 350
Cdd:PLN02495 303 MMHGYPLVKNLCAELQDFMKKHNFSSIEDFR 333
|
|
| DHOD_like |
cd04739 |
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
277-350 |
7.75e-06 |
|
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: 47.22 E-value: 7.75e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81847184 277 LARMRERVGpdMPLIGVGGIDSAETALAKIKAGADLVQLYTGLIYRGPGLPGEILRGLSTAIKHEGVSSIAELR 350
Cdd:cd04739 229 IAILSGRVK--ASLAASGGVHDAEDVVKYLLAGADVVMTTSALLRHGPDYIGTLLAGLEAWMEEHGYESVQQLR 300
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
282-321 |
2.16e-04 |
|
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: 42.58 E-value: 2.16e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 81847184 282 ERVGPDMPLIGVGGIDSAETALAKIKAGADLVQLYTGLIY 321
Cdd:cd04735 279 ERIAGRLPLIAVGSINTPDDALEALETGADLVAIGRGLLV 318
|
|
| PRK07565 |
PRK07565 |
dihydroorotate dehydrogenase-like protein; |
277-350 |
2.41e-04 |
|
dihydroorotate dehydrogenase-like protein;
Pssm-ID: 236051 Cd Length: 334 Bit Score: 42.55 E-value: 2.41e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81847184 277 LARMRERVGpdMPLIGVGGIDSAETALAKIKAGADLVQLYTGLIYRGPGLPGEILRGLSTAIKHEGVSSIAELR 350
Cdd:PRK07565 231 IAILSGRVG--ADLAATTGVHDAEDVIKMLLAGADVVMIASALLRHGPDYIGTILRGLEDWMERHGYESLQQFR 302
|
|
| FadH |
COG1902 |
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ... |
211-313 |
3.46e-04 |
|
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family [Energy production and conversion];
Pssm-ID: 441506 [Multi-domain] Cd Length: 365 Bit Score: 42.08 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 211 PVFLKIAPD------LTDEELDDIAAEADAQKLDGIIVSnttlsrsglknpenSNETGGLSGAPLFERS---TVVLARMR 281
Cdd:COG1902 218 PVGVRLSPTdfveggLTLEESVELAKALEEAGVDYLHVS--------------SGGYEPDAMIPTIVPEgyqLPFAARIR 283
|
90 100 110
....*....|....*....|....*....|...
gi 81847184 282 ERVGpdMPLIGVGGIDSAETALAKIKAG-ADLV 313
Cdd:COG1902 284 KAVG--IPVIAVGGITTPEQAEAALASGdADLV 314
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
211-320 |
1.51e-03 |
|
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. 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. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 239201 [Multi-domain] Cd Length: 327 Bit Score: 40.25 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 211 PVFLKIAPD------LTDEELDDIAAEADAQKLDGIIVSnttlsrSGLKNPENSNETGGLSGAPLFERSTvvlARMRERV 284
Cdd:cd02803 210 PVGVRLSADdfvpggLTLEEAIEIAKALEEAGVDALHVS------GGSYESPPPIIPPPYVPEGYFLELA---EKIKKAV 280
|
90 100 110
....*....|....*....|....*....|....*..
gi 81847184 285 gpDMPLIGVGGIDSAETALAKIKAG-ADLVQLYTGLI 320
Cdd:cd02803 281 --KIPVIAVGGIRDPEVAEEILAEGkADLVALGRALL 315
|
|
| Eda |
COG0800 |
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; ... |
276-313 |
2.33e-03 |
|
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; 2-keto-3-deoxy-6-phosphogluconate aldolase is part of the Pathway/BioSystem: Entner-Doudoroff pathway
Pssm-ID: 440563 Cd Length: 213 Bit Score: 38.91 E-value: 2.33e-03
10 20 30
....*....|....*....|....*....|....*...
gi 81847184 276 VLARMRERVGPDMpLIGVGGIDSAETALAKIKAGADLV 313
Cdd:COG0800 53 AIRALAKEVGPDA-LVGAGTVLTPEQARAAIAAGARFI 89
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
228-350 |
2.88e-03 |
|
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only]; FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440915 [Multi-domain] Cd Length: 357 Bit Score: 39.35 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 228 IAAEADAQKL-----DGIIVSNttlsrsglknpensneTGG--LSGAPlferSTV-VLARMRERVGPDMPLIGVGGIDSA 299
Cdd:COG1304 233 VLSPEDARRAvdagvDGIDVSN----------------HGGrqLDGGP----PTIdALPEIRAAVGGRIPVIADGGIRRG 292
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81847184 300 ETALAKIKAGADLV-----QLYtGLIYRGPglPG-----EILRG-LSTAIKHEGVSSIAELR 350
Cdd:COG1304 293 LDVAKALALGADAVglgrpFLY-GLAAGGE--AGvarvlELLRAeLRRAMALTGCRSLAELR 351
|
|
| PcrB |
COG1646 |
Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism]; |
265-333 |
3.18e-03 |
|
Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];
Pssm-ID: 441252 Cd Length: 241 Bit Score: 38.60 E-value: 3.18e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 265 SGAPLFERSTVVlARMRERVGpDMPLIGVGGIDSAETALAKIKAGADLVQlyTG-LIYRGPGLPGEILRG 333
Cdd:COG1646 176 SGAGEPVDPEMV-KAVKKALE-DTPLIYGGGIRSPEKAREMAEAGADTIV--VGnAIEEDPDLALETVEA 241
|
|
| PRK04169 |
PRK04169 |
heptaprenylglyceryl phosphate synthase; |
265-339 |
4.11e-03 |
|
heptaprenylglyceryl phosphate synthase;
Pssm-ID: 235237 Cd Length: 232 Bit Score: 38.25 E-value: 4.11e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81847184 265 SGAPLFERSTVVlARMRERVGpDMPLIGVGGIDSAETALAKIKAGADLVQlyTG-LIYRGpglPGEILRGLSTAIK 339
Cdd:PRK04169 164 GGAGDPVPPEMV-KAVKKALD-ITPLIYGGGIRSPEQARELMAAGADTIV--VGnIIEED---PKKTVKAIKKAIK 232
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
232-351 |
6.67e-03 |
|
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO). In green plants, glycolate oxidase is one of the key enzymes in photorespiration where it oxidizes glycolate to glyoxylate. LMO catalyzes the oxidation of L-lactate to acetate and carbon dioxide. MDH oxidizes (S)-mandelate to phenylglyoxalate. It is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate.
Pssm-ID: 239203 [Multi-domain] Cd Length: 299 Bit Score: 37.81 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 232 ADAQKL-----DGIIVSNttlsrsglknpensneTGG--LSGAPlferSTV-VLARMRERVGPDMPLIGVGGIDSAETAL 303
Cdd:cd02809 184 EDALRAvdagaDGIVVSN----------------HGGrqLDGAP----ATIdALPEIVAAVGGRIEVLLDGGIRRGTDVL 243
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 81847184 304 AKIKAGADLV-----QLYtGLIYRGPglPG-----EILRG-LSTAIKHEGVSSIAELRD 351
Cdd:cd02809 244 KALALGADAVligrpFLY-GLAAGGE--AGvahvlEILRDeLERAMALLGCASLADLDP 299
|
|
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
154-349 |
7.24e-03 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 37.90 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 154 VAGIRRfyqlaRYFTVNISSPNTPGLRNLQAREALHELLSRVLEARDEEGNMctlkRPVFLKIAPDLTDEELDDIAAE-- 231
Cdd:pfam01070 148 VLGRRE-----RDLRNGFTLPPRLTPRNLLDLALHPRWALGVLRRGGAGGAA----AFVGSQFDPALTWDDLAWLRERwk 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81847184 232 -----------ADAQKL-----DGIIVSNttlsrsglknpensneTGG--LSGAPlferSTV-VLARMRERVGPDMPLIG 292
Cdd:pfam01070 219 gplvvkgilspEDAKRAveagvDGIVVSN----------------HGGrqLDGAP----ATIdALPEIVAAVGGRIPVLV 278
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81847184 293 VGGIDSAETALAKIKAGADLV-----QLYtGLIYRGPglPG-----EILRG-LSTAIKHEGVSSIAEL 349
Cdd:pfam01070 279 DGGIRRGTDVLKALALGADAVllgrpFLY-GLAAGGE--AGvahalEILRDeLERTMALLGCKSIADL 343
|
|
| DeoC |
COG0274 |
Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism]; |
280-311 |
7.37e-03 |
|
Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];
Pssm-ID: 440043 Cd Length: 219 Bit Score: 37.35 E-value: 7.37e-03
10 20 30
....*....|....*....|....*....|....*
gi 81847184 280 MRERVGPDmplIGV---GGIDSAETALAKIKAGAD 311
Cdd:COG0274 169 MRETVGGR---VGVkasGGIRTLEDALAMIEAGAT 200
|
|
| |
