|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
10-350 |
0e+00 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 532.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 10 YQLALKAMFQVPPEQIHEVISKSLKGLQKSeSLQRAVSKLLVVDDAVLRQTVFGVDFPRPLGLAAGFDKAAIAPDCWGPI 89
Cdd:PRK05286 3 YPLARPLLFKLDPETAHELTIRALKRASRT-PLLSLLRQRLTYTDPRLPVTVMGLTFPNPVGLAAGFDKNGEAIDALGAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 90 GFGYAELGTVTAKPQPGNDRPRLFRLKEDRAILNRMGFNNPGAAAVAENLRARRSDDVIGINIGKTKVTPLEEAVDDYRE 169
Cdd:PRK05286 82 GFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKAYRGIPLGINIGKNKDTPLEDAVDDYLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 170 SASQLGGLADYVVVNVSSPNTPGLRDLQAVESLRPILAAVTEETDS-----PVLVKIAPDLSDEDVIAVADLAVDLGLAG 244
Cdd:PRK05286 162 CLEKLYPYADYFTVNISSPNTPGLRDLQYGEALDELLAALKEAQAElhgyvPLLVKIAPDLSDEELDDIADLALEHGIDG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 245 IVATNTTISREGLRTP--ADEvaemgAGGVSGAPVAARSLEVLKLLHERVGGKLVLISVGGIETAEQAWERIANGASLLQ 322
Cdd:PRK05286 242 VIATNTTLSRDGLKGLpnADE-----AGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGASLVQ 316
|
330 340
....*....|....*....|....*...
gi 1093453903 323 GYTPLIYGGPDWIRDIHQGLARQIRAQG 350
Cdd:PRK05286 317 IYSGLIYEGPGLVKEIVRGLARLLRRDG 344
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
15-342 |
2.74e-162 |
|
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: 456.96 E-value: 2.74e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 15 KAMFQVPPEQIHEVISKSLKGLQKSESLQravskLLVVDDAVLRQTVFGVDFPRPLGLAAGFDKAAIAPDCWGPIGFGYA 94
Cdd:cd04738 2 PLLFLLDPETAHRLAIRALKLGLGPPLLL-----LLVYDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 95 ELGTVTAKPQPGNDRPRLFRLKEDRAILNRMGFNNPGAAAVAENLRARRSDD-VIGINIGKTKVTPLEEAVDDYRESASQ 173
Cdd:cd04738 77 EVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRRPRGgPLGVNIGKNKDTPLEDAVEDYVIGVRK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 174 LGGLADYVVVNVSSPNTPGLRDLQAVESLRPILAAVTEETDS-----PVLVKIAPDLSDEDVIAVADLAVDLGLAGIVAT 248
Cdd:cd04738 157 LGPYADYLVVNVSSPNTPGLRDLQGKEALRELLTAVKEERNKlgkkvPLLVKIAPDLSDEELEDIADVALEHGVDGIIAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 249 NTTISREGLRTPADEVaemGAGGVSGAPVAARSLEVLKLLHERVGGKLVLISVGGIETAEQAWERIANGASLLQGYTPLI 328
Cdd:cd04738 237 NTTISRPGLLRSPLAN---ETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTGLV 313
|
330
....*....|....
gi 1093453903 329 YGGPDWIRDIHQGL 342
Cdd:cd04738 314 YEGPGLVKRIKREL 327
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
10-342 |
4.10e-144 |
|
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: 411.49 E-value: 4.10e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 10 YQLALKAMFQVPPEQIHEVISKSLKGLqkSESLQRAVSKLLVVDDAVLRQTVFGVDFPRPLGLAAGFDKAAIAPDCWGPI 89
Cdd:TIGR01036 1 YPLVRKLLFLLDPESAHELTFQFLRLG--TGTPFLALLRSLFGASDPLEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 90 GFGYAELGTVTAKPQPGNDRPRLFRLKEDRAILNRMGFNNPGAAAVAENLRARRSDDVIGINIGKTKVTPLEEAVDDYRE 169
Cdd:TIGR01036 79 GFGFLEIGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLKRARYKGPIGINIGKNKDTPSEDAKEDYAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 170 SASQLGGLADYVVVNVSSPNTPGLRDLQAVESLRPILAAVTEETDS-------PVLVKIAPDLSDEDVIAVADLAVDLGL 242
Cdd:TIGR01036 159 CLRKLGPLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAVKQEQDGlrrvhrvPVLVKIAPDLTESDLEDIADSLVELGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 243 AGIVATNTTISREGLRTPADevaEMGAGGVSGAPVAARSLEVLKLLHERVGGKLVLISVGGIETAEQAWERIANGASLLQ 322
Cdd:TIGR01036 239 DGVIATNTTVSRSLVQGPKN---SDETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGASLLQ 315
|
330 340
....*....|....*....|
gi 1093453903 323 GYTPLIYGGPDWIRDIHQGL 342
Cdd:TIGR01036 316 IYSGFIYWGPPLVKEIVKEI 335
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
57-355 |
4.95e-117 |
|
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: 341.28 E-value: 4.95e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 57 LRQTVFGVDFPRPLGLAAGF-DKAAIAPDCWGPIGFGYAELGTVTAKPQPGNDRPRLFRLKEDRAILNRMGFNNPGAAAV 135
Cdd:COG0167 2 LSVELAGLKFPNPVGLASGFfDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 136 AENLRARRSDDV-IGINIGKTkvtpleeAVDDYRESASQLGGL-ADYVVVNVSSPNTPG-LRDL-QAVESLRPILAAVTE 211
Cdd:COG0167 82 LERLLPAKRYDVpVIVNIGGN-------TVEDYVELARRLADAgADYLELNISCPNTPGgGRALgQDPEALAELLAAVKA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 212 ETDSPVLVKIAPDLsdEDVIAVADLAVDLGLAGIVATNTTISRE-GLRTPaDEVAEMGAGGVSGAPVAARSLEVLKLLHE 290
Cdd:COG0167 155 ATDKPVLVKLAPDL--TDIVEIARAAEEAGADGVIAINTTLGRAiDLETR-RPVLANEAGGLSGPALKPIALRMVREVAQ 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1093453903 291 RVGGKLVLISVGGIETAEQAWERIANGASLLQGYTPLIYGGPDWIRDIHQGLARQIRAQGFYSIS 355
Cdd:COG0167 232 AVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSIS 296
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
56-344 |
2.48e-103 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 306.20 E-value: 2.48e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 56 VLRQTVFGVDFPRPLGLAAGFDKAAIAPDCWGPIG-FGYAELGTVTAKPQPGNDRPRLFRLKEDraILNRMGFNNPGAAA 134
Cdd:pfam01180 1 MLATKIPGLDFKNPIGLASGFDKFGEEALKWLALGkFGAIEIKSVTPYPQPGNPTPRVFRLPEG--VLNRMGLNNPGLDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 135 VAENLRARR---SDDVIGINIGKTKVTpleeaVDDYRESASQLGGLADYVVVNVSSPNTPGLRDLQAVESLRPILAAVTE 211
Cdd:pfam01180 79 VLAELLKRRkeyPRPDLGINLSKAGMT-----VDDYVEVARKIGPFADYIELNVSCPNTPGLRALQTDPELAAILLKVVK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 212 ETDS-PVLVKIAPDLSDEDVIAVADLAVD-LGLAGIVATNTTISREGLRTPADE-VAEMGAGGVSGAPVAARSLEVLKLL 288
Cdd:pfam01180 154 EVSKvPVLVKLAPDLTDIVIIDIADVALGeDGLDGINATNTTVRGMRIDLKTEKpILANGTGGLSGPPIKPIALKVIREL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1093453903 289 HERVGGKLVLISVGGIETAEQAWERIANGASLLQGYTPLIYGGPDWIRDIHQGLAR 344
Cdd:pfam01180 234 YQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPE 289
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
10-350 |
0e+00 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 532.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 10 YQLALKAMFQVPPEQIHEVISKSLKGLQKSeSLQRAVSKLLVVDDAVLRQTVFGVDFPRPLGLAAGFDKAAIAPDCWGPI 89
Cdd:PRK05286 3 YPLARPLLFKLDPETAHELTIRALKRASRT-PLLSLLRQRLTYTDPRLPVTVMGLTFPNPVGLAAGFDKNGEAIDALGAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 90 GFGYAELGTVTAKPQPGNDRPRLFRLKEDRAILNRMGFNNPGAAAVAENLRARRSDDVIGINIGKTKVTPLEEAVDDYRE 169
Cdd:PRK05286 82 GFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKAYRGIPLGINIGKNKDTPLEDAVDDYLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 170 SASQLGGLADYVVVNVSSPNTPGLRDLQAVESLRPILAAVTEETDS-----PVLVKIAPDLSDEDVIAVADLAVDLGLAG 244
Cdd:PRK05286 162 CLEKLYPYADYFTVNISSPNTPGLRDLQYGEALDELLAALKEAQAElhgyvPLLVKIAPDLSDEELDDIADLALEHGIDG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 245 IVATNTTISREGLRTP--ADEvaemgAGGVSGAPVAARSLEVLKLLHERVGGKLVLISVGGIETAEQAWERIANGASLLQ 322
Cdd:PRK05286 242 VIATNTTLSRDGLKGLpnADE-----AGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGASLVQ 316
|
330 340
....*....|....*....|....*...
gi 1093453903 323 GYTPLIYGGPDWIRDIHQGLARQIRAQG 350
Cdd:PRK05286 317 IYSGLIYEGPGLVKEIVRGLARLLRRDG 344
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
15-342 |
2.74e-162 |
|
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: 456.96 E-value: 2.74e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 15 KAMFQVPPEQIHEVISKSLKGLQKSESLQravskLLVVDDAVLRQTVFGVDFPRPLGLAAGFDKAAIAPDCWGPIGFGYA 94
Cdd:cd04738 2 PLLFLLDPETAHRLAIRALKLGLGPPLLL-----LLVYDDPRLEVEVFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 95 ELGTVTAKPQPGNDRPRLFRLKEDRAILNRMGFNNPGAAAVAENLRARRSDD-VIGINIGKTKVTPLEEAVDDYRESASQ 173
Cdd:cd04738 77 EVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLKKRRPRGgPLGVNIGKNKDTPLEDAVEDYVIGVRK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 174 LGGLADYVVVNVSSPNTPGLRDLQAVESLRPILAAVTEETDS-----PVLVKIAPDLSDEDVIAVADLAVDLGLAGIVAT 248
Cdd:cd04738 157 LGPYADYLVVNVSSPNTPGLRDLQGKEALRELLTAVKEERNKlgkkvPLLVKIAPDLSDEELEDIADVALEHGVDGIIAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 249 NTTISREGLRTPADEVaemGAGGVSGAPVAARSLEVLKLLHERVGGKLVLISVGGIETAEQAWERIANGASLLQGYTPLI 328
Cdd:cd04738 237 NTTISRPGLLRSPLAN---ETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTGLV 313
|
330
....*....|....
gi 1093453903 329 YGGPDWIRDIHQGL 342
Cdd:cd04738 314 YEGPGLVKRIKREL 327
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
10-342 |
4.10e-144 |
|
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: 411.49 E-value: 4.10e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 10 YQLALKAMFQVPPEQIHEVISKSLKGLqkSESLQRAVSKLLVVDDAVLRQTVFGVDFPRPLGLAAGFDKAAIAPDCWGPI 89
Cdd:TIGR01036 1 YPLVRKLLFLLDPESAHELTFQFLRLG--TGTPFLALLRSLFGASDPLEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 90 GFGYAELGTVTAKPQPGNDRPRLFRLKEDRAILNRMGFNNPGAAAVAENLRARRSDDVIGINIGKTKVTPLEEAVDDYRE 169
Cdd:TIGR01036 79 GFGFLEIGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGADVLVERLKRARYKGPIGINIGKNKDTPSEDAKEDYAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 170 SASQLGGLADYVVVNVSSPNTPGLRDLQAVESLRPILAAVTEETDS-------PVLVKIAPDLSDEDVIAVADLAVDLGL 242
Cdd:TIGR01036 159 CLRKLGPLADYLVVNVSSPNTPGLRDLQYKAELRDLLTAVKQEQDGlrrvhrvPVLVKIAPDLTESDLEDIADSLVELGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 243 AGIVATNTTISREGLRTPADevaEMGAGGVSGAPVAARSLEVLKLLHERVGGKLVLISVGGIETAEQAWERIANGASLLQ 322
Cdd:TIGR01036 239 DGVIATNTTVSRSLVQGPKN---SDETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAGASLLQ 315
|
330 340
....*....|....*....|
gi 1093453903 323 GYTPLIYGGPDWIRDIHQGL 342
Cdd:TIGR01036 316 IYSGFIYWGPPLVKEIVKEI 335
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
57-355 |
4.95e-117 |
|
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: 341.28 E-value: 4.95e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 57 LRQTVFGVDFPRPLGLAAGF-DKAAIAPDCWGPIGFGYAELGTVTAKPQPGNDRPRLFRLKEDRAILNRMGFNNPGAAAV 135
Cdd:COG0167 2 LSVELAGLKFPNPVGLASGFfDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 136 AENLRARRSDDV-IGINIGKTkvtpleeAVDDYRESASQLGGL-ADYVVVNVSSPNTPG-LRDL-QAVESLRPILAAVTE 211
Cdd:COG0167 82 LERLLPAKRYDVpVIVNIGGN-------TVEDYVELARRLADAgADYLELNISCPNTPGgGRALgQDPEALAELLAAVKA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 212 ETDSPVLVKIAPDLsdEDVIAVADLAVDLGLAGIVATNTTISRE-GLRTPaDEVAEMGAGGVSGAPVAARSLEVLKLLHE 290
Cdd:COG0167 155 ATDKPVLVKLAPDL--TDIVEIARAAEEAGADGVIAINTTLGRAiDLETR-RPVLANEAGGLSGPALKPIALRMVREVAQ 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1093453903 291 RVGGKLVLISVGGIETAEQAWERIANGASLLQGYTPLIYGGPDWIRDIHQGLARQIRAQGFYSIS 355
Cdd:COG0167 232 AVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSIS 296
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
56-344 |
2.48e-103 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 306.20 E-value: 2.48e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 56 VLRQTVFGVDFPRPLGLAAGFDKAAIAPDCWGPIG-FGYAELGTVTAKPQPGNDRPRLFRLKEDraILNRMGFNNPGAAA 134
Cdd:pfam01180 1 MLATKIPGLDFKNPIGLASGFDKFGEEALKWLALGkFGAIEIKSVTPYPQPGNPTPRVFRLPEG--VLNRMGLNNPGLDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 135 VAENLRARR---SDDVIGINIGKTKVTpleeaVDDYRESASQLGGLADYVVVNVSSPNTPGLRDLQAVESLRPILAAVTE 211
Cdd:pfam01180 79 VLAELLKRRkeyPRPDLGINLSKAGMT-----VDDYVEVARKIGPFADYIELNVSCPNTPGLRALQTDPELAAILLKVVK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 212 ETDS-PVLVKIAPDLSDEDVIAVADLAVD-LGLAGIVATNTTISREGLRTPADE-VAEMGAGGVSGAPVAARSLEVLKLL 288
Cdd:pfam01180 154 EVSKvPVLVKLAPDLTDIVIIDIADVALGeDGLDGINATNTTVRGMRIDLKTEKpILANGTGGLSGPPIKPIALKVIREL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1093453903 289 HERVGGKLVLISVGGIETAEQAWERIANGASLLQGYTPLIYGGPDWIRDIHQGLAR 344
Cdd:pfam01180 234 YQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPE 289
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
53-359 |
4.94e-96 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 291.64 E-value: 4.94e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 53 DDAVLRQTVFGVDFPRPLGLAAGFDKAAIAPDCWGPIGFGYAELGTVTAKPQPGNDRPRLFRLKEDRAILNRMGFNNPGA 132
Cdd:PLN02826 70 DPSVLGVEVWGRTFSNPIGLAAGFDKNAEAVEGLLGLGFGFVEIGSVTPLPQPGNPKPRVFRLREEGAIINRYGFNSEGI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 133 AAVAENLRARRSDD------------------------VIGINIGKTKVTplEEAVDDYRESASQLGGLADYVVVNVSSP 188
Cdd:PLN02826 150 VAVAKRLGAQHGKRkldetssssfssddvkaggkagpgILGVNLGKNKTS--EDAAADYVQGVRALSQYADYLVINVSSP 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 189 NTPGLRDLQAVESLRPILAAVTEETDS---------PVLVKIAPDLSDEDVIAVADLAVDLGLAGIVATNTTISREGlrT 259
Cdd:PLN02826 228 NTPGLRKLQGRKQLKDLLKKVLAARDEmqwgeegppPLLVKIAPDLSKEDLEDIAAVALALGIDGLIISNTTISRPD--S 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 260 PADEVAEMGAGGVSGAPVAARSLEVLKLLHERVGGKLVLISVGGIETAEQAWERIANGASLLQGYTPLIYGGPDWIRDIH 339
Cdd:PLN02826 306 VLGHPHADEAGGLSGKPLFDLSTEVLREMYRLTRGKIPLVGCGGVSSGEDAYKKIRAGASLVQLYTAFAYEGPALIPRIK 385
|
330 340
....*....|....*....|
gi 1093453903 340 QGLARQIRAQGFYSISEAVG 359
Cdd:PLN02826 386 AELAACLERDGFKSIQEAVG 405
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
60-341 |
2.66e-51 |
|
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: 172.54 E-value: 2.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 60 TVFGVDFPRPLGLAAGFD-KAAIAPDCWGPIGFGYAELGTVTAKPQPGNDRPRLFRLKEDR-------AILNRMGFNNPG 131
Cdd:cd02810 2 NFLGLKLKNPFGVAAGPLlKTGELIARAAAAGFGAVVYKTVTLHPRPGNPLPRVARLPPEGesypeqlGILNSFGLPNLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 132 AAAVAENLRARRS---DDVIGINIGKTKvtpLEEAVDDYReSASQLGglADYVVVNVSSPNTPGLRDL-QAVESLRPILA 207
Cdd:cd02810 82 LDVWLQDIAKAKKefpGQPLIASVGGSS---KEDYVELAR-KIERAG--AKALELNLSCPNVGGGRQLgQDPEAVANLLK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 208 AVTEETDSPVLVKIAPDLSDEDVIAVADLAVDLGLAGIVATNTTISREGLRTPADEVAEMGAGGVSGAPVAARSLEVLKL 287
Cdd:cd02810 156 AVKAAVDIPLLVKLSPYFDLEDIVELAKAAERAGADGLTAINTISGRVVDLKTVGPGPKRGTGGLSGAPIRPLALRWVAR 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1093453903 288 LHERVGGKLVLISVGGIETAEQAWERIANGASLLQGYTPLIYGGPDWIRDIHQG 341
Cdd:cd02810 236 LAARLQLDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKIKKE 289
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
60-360 |
2.22e-29 |
|
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: 114.95 E-value: 2.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 60 TVFGVDFPRPLGLAAG-FDKAAIAPDCWGPIGFGYAELGTVTAKPQPGNDRPRLFRLkeDRAILNRMGFNNPGA-AAVAE 137
Cdd:cd04740 3 ELAGLRLKNPVILASGtFGFGEELSRVADLGKLGAIVTKSITLEPREGNPPPRVVET--PGGMLNAIGLQNPGVeAFLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 138 NLRARRSDDVIGI-NIGKtkvtpleEAVDDYRESASQLGGL-ADYVVVNVSSPNTPGL-----RDLQAVESlrpILAAVT 210
Cdd:cd04740 81 LLPWLREFGTPVIaSIAG-------STVEEFVEVAEKLADAgADAIELNISCPNVKGGgmafgTDPEAVAE---IVKAVK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 211 EETDSPVLVKIAPDlsDEDVIAVADLAVDLGLAGIVATNTTIsreGL------RTPadeVAEMGAGGVSGA---PVAars 281
Cdd:cd04740 151 KATDVPVIVKLTPN--VTDIVEIARAAEEAGADGLTLINTLK---GMaidietRKP---ILGNVTGGLSGPaikPIA--- 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093453903 282 LEVLKLLHERVggKLVLISVGGIETAEQAWERIANGASLLQGYTpLIYGGPDWIRDIHQGLARQIRAQGFYSISEAVGC 360
Cdd:cd04740 220 LRMVYQVYKAV--EIPIIGVGGIASGEDALEFLMAGASAVQVGT-ANFVDPEAFKEIIEGLEAYLDEEGIKSIEELVGL 295
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
57-359 |
1.29e-24 |
|
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: 101.74 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 57 LRQTVFGVDFPRPLGLAAG-FDKAAIAPDCWGPIGFGYAELGTVTAKPQPGNDRPRLFRLKEdrAILNRMGFNNPGAAAV 135
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGiMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTIVETPC--GMLNAIGLQNPGVEAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 136 AENLRARRSD---DVIGINIGKTkvtpleeaVDDYRESASQLGGLADYVV---VNVSSPN--TPGLRDLQAVESLRPILA 207
Cdd:TIGR01037 79 LEELKPVREEfptPLIASVYGSS--------VEEFAEVAEKLEKAPPYVDayeLNLSCPHvkGGGIAIGQDPELSADVVK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 208 AVTEETDSPVLVKIAPDLSDedVIAVADLAVDLGLAGIVATNTTIS-REGLRTPADEVAEMgAGGVSGAPVAARSLEVLK 286
Cdd:TIGR01037 151 AVKDKTDVPVFAKLSPNVTD--ITEIAKAAEEAGADGLTLINTLRGmKIDIKTGKPILANK-TGGLSGPAIKPIALRMVY 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1093453903 287 LLHERVGgkLVLISVGGIETAEQAWERIANGASLLQGYTPLIYgGPDWIRDIHQGLARQIRAQGFYSISEAVG 359
Cdd:TIGR01037 228 DVYKMVD--IPIIGVGGITSFEDALEFLMAGASAVQVGTAVYY-RGFAFKKIIEGLIAFLKAEGFTSIEELIG 297
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
57-360 |
5.87e-23 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 97.14 E-value: 5.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 57 LRQTVFGVDFPRPLGLAAG-FdkaaiapdcwgpiGFG--YAE------LG-----TVTAKPQPGNDRPRLFRLkeDRAIL 122
Cdd:PRK07259 2 LSVELPGLKLKNPVMPASGtF-------------GFGgeYARfydlngLGaivtkSTTLEPREGNPTPRIAET--PGGML 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 123 NRMGFNNPGA-AAVAENLRARRSDD--VIGiNI-GKTkvtpleeaVDDYRESASQLG--GLADYVVVNVSSPNTPGL--- 193
Cdd:PRK07259 67 NAIGLQNPGVdAFIEEELPWLEEFDtpIIA-NVaGST--------EEEYAEVAEKLSkaPNVDAIELNISCPNVKHGgma 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 194 --RDLQAVESlrpILAAVTEETDSPVLVKIAPDLSDEDVIAVAdlAVDLGLAGIVATNT----TISREgLRTPadeVAEM 267
Cdd:PRK07259 138 fgTDPELAYE---VVKAVKEVVKVPVIVKLTPNVTDIVEIAKA--AEEAGADGLSLINTlkgmAIDIK-TRKP---ILAN 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 268 GAGGVSGA---PVAARSL-EVLKLLhervggKLVLISVGGIETAEQAWERIANGASLLQGYTPlIYGGPDWIRDIHQGLA 343
Cdd:PRK07259 209 VTGGLSGPaikPIALRMVyQVYQAV------DIPIIGMGGISSAEDAIEFIMAGASAVQVGTA-NFYDPYAFPKIIEGLE 281
|
330
....*....|....*..
gi 1093453903 344 RQIRAQGFYSISEAVGC 360
Cdd:PRK07259 282 AYLDKYGIKSIEEIVGI 298
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
97-344 |
8.63e-17 |
|
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: 79.68 E-value: 8.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 97 GTVTAKPQPGNDRPRLFRLKEdrAILNRMGFNNPGAAAVAENLRARRSddvIGINIGKT---KVTPL-EEAVDDYRESAS 172
Cdd:cd04741 40 RSSTLAGRPGNPEPRYYAFPL--GSINSLGLPNLGLDYYLEYIRTISD---GLPGSAKPffiSVTGSaEDIAAMYKKIAA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 173 QLGGLADYVVVNVSSPNTPGLRDLQA-VESLRPILAAVTEETDSPVLVKIAP--DLSDEDVIAVADLAVDLGLAGIVATN 249
Cdd:cd04741 115 HQKQFPLAMELNLSCPNVPGKPPPAYdFDATLEYLTAVKAAYSIPVGVKTPPytDPAQFDTLAEALNAFACPISFITATN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 250 TTISREGLRTPADEVA---EMGAGGVSGAPVAARSLEVLKLLHERVGGKLVLISVGGIETAEQAWERIANGASLLQGYTP 326
Cdd:cd04741 195 TLGNGLVLDPERETVVlkpKTGFGGLAGAYLHPLALGNVRTFRRLLPSEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTA 274
|
250
....*....|....*...
gi 1093453903 327 LIYGGPDWIRDIHQGLAR 344
Cdd:cd04741 275 LGKEGPKVFARIEKELED 292
|
|
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
57-342 |
3.75e-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: 57.29 E-value: 3.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 57 LRQTVFGVDFPRPLGLAAG-----FDKAAIAPDcwgpIGFGYAELGTVT-AKPQPGNDRPRLFRL-KEDRAILnrmGFNN 129
Cdd:cd02940 2 LSVTFCGIKFPNPFGLASAppttsYPMIRRAFE----AGWGGAVTKTLGlDKDIVTNVSPRIARLrTSGRGQI---GFNN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 130 P---GAAAVAENLRARRS------DDVIginIGKTKVTPLEEAVDDYRESASQLGglADYVVVNVSSPNTPGLRDL---- 196
Cdd:cd02940 75 IeliSEKPLEYWLKEIRElkkdfpDKIL---IASIMCEYNKEDWTELAKLVEEAG--ADALELNFSCPHGMPERGMgaav 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 197 -QAVESLRPILAAVTEETDSPVLVKIAPDLSDEDVIAVAdlAVDLGLAGIVATNTTISREGLR----TPADEVAEMGA-G 270
Cdd:cd02940 150 gQDPELVEEICRWVREAVKIPVIAKLTPNITDIREIARA--AKEGGADGVSAINTVNSLMGVDldgtPPAPGVEGKTTyG 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1093453903 271 GVSGA---PVAARSL-EVLKLLHERvggkLVLISVGGIETAEQAWERIANGASLLQGYTPLIYGGPDWIRDIHQGL 342
Cdd:cd02940 228 GYSGPavkPIALRAVsQIARAPEPG----LPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
277-363 |
9.89e-08 |
|
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: 52.98 E-value: 9.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 277 VAARSLEVLKLLHERVGGKLVLISVGGIETAEQAWERIANGASLLQGYTPLIYgGPDWIRDIHQGLARQIRAqgFYSISE 356
Cdd:cd04735 266 GRDDNQTIMELVKERIAGRLPLIAVGSINTPDDALEALETGADLVAIGRGLLV-DPDWVEKIKEGREDEINL--EIDPDD 342
|
....*..
gi 1093453903 357 AVGCGLP 363
Cdd:cd04735 343 LEELKIP 349
|
|
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
179-364 |
1.87e-07 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 52.53 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 179 DYVVVNVSSPNTPGLRDL-----QAVESLRPILAAVTEETDSPVLVKIAPDLSDedVIAVADLAVDLGLAGIVATNTTIS 253
Cdd:PLN02495 142 DALEINFSCPHGMPERKMgaavgQDCDLLEEVCGWINAKATVPVWAKMTPNITD--ITQPARVALKSGCEGVAAINTIMS 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 254 REG--LRTPADEVAEMG---AGGVSGA---PVA-ARSLEVLKLLHERVGGKLVLISVGGIETAEQAWERIANGASLLQGY 324
Cdd:PLN02495 220 VMGinLDTLRPEPCVEGystPGGYSSKavrPIAlAKVMAIAKMMKSEFPEDRSLSGIGGVETGGDAAEFILLGADTVQVC 299
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1093453903 325 TPLIYGGPDWIRDIHQGLARQIRAQGFYSISEAVGCGLPW 364
Cdd:PLN02495 300 TGVMMHGYPLVKNLCAELQDFMKKHNFSSIEDFRGASLPY 339
|
|
| DHOD_like |
cd04739 |
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
205-360 |
1.12e-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: 49.92 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 205 ILAAVTEETDSPVLVKIAPDLSdedviAVADLAVDL---GLAGIVATN------------TTISREGLRTPADevaemga 269
Cdd:cd04739 154 ILRAVKSAVTIPVAVKLSPFFS-----ALAHMAKQLdaaGADGLVLFNrfyqpdidletlEVVPNLLLSSPAE------- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 270 ggvsgapvAARSLEVLKLLHERVGGKLVliSVGGIETAEQAWERIANGASLLQGYTPLIYGGPDWIRDIHQGLARQIRAQ 349
Cdd:cd04739 222 --------IRLPLRWIAILSGRVKASLA--ASGGVHDAEDVVKYLLAGADVVMTTSALLRHGPDYIGTLLAGLEAWMEEH 291
|
170
....*....|.
gi 1093453903 350 GFYSISEAVGC 360
Cdd:cd04739 292 GYESVQQLRGS 302
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
208-363 |
4.10e-06 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 48.40 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 208 AVTEETDSPVLVKIAPDLSDedVIAVADLAVDLGLAGIVATNTTISREGL----RTPADEVAEMGA-GGVSGA---PVAA 279
Cdd:PRK08318 162 WVKRGSRLPVIVKLTPNITD--IREPARAAKRGGADAVSLINTINSITGVdldrMIPMPIVNGKSShGGYCGPavkPIAL 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 280 RSL-EVLKllHERVGGklVLIS-VGGIETAEQAWERIANGASLLQGYTPLIYGGPDWIRDIHQGLARQIRAQGFYSISEA 357
Cdd:PRK08318 240 NMVaEIAR--DPETRG--LPISgIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISGLSHYMDEKGFASLEDM 315
|
....*.
gi 1093453903 358 VGCGLP 363
Cdd:PRK08318 316 VGLAVP 321
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
98-359 |
1.19e-05 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 46.49 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 98 TVTAKPQPGNDRPRLFRLkeDRAILNRMGFNNPGAAAVAENLRARRSDD--------VIGINIgktkvtplEEAVDDYRe 169
Cdd:PRK02506 44 SATLEPRPGNPEPRYADT--PLGSINSMGLPNLGFDYYLDYVLELQKKGpnkphflsVVGLSP--------EETHTILK- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 170 sASQLGGLADYVVVNVSSPNTPG----LRDLQAVESlrpILAAVTEETDSPVLVKIAP--DLSDEDVIAvadlAV--DLG 241
Cdd:PRK02506 113 -KIQASDFNGLVELNLSCPNVPGkpqiAYDFETTEQ---ILEEVFTYFTKPLGVKLPPyfDIVHFDQAA----AIfnKFP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 242 LAGIVATNTTisREGLR-TPADEVA----EMGAGGVSGAPVAARSLEVLKLLHERVGGKLVLISVGGIETAEQAWERIAN 316
Cdd:PRK02506 185 LAFVNCINSI--GNGLViDPEDETVvikpKNGFGGIGGDYIKPTALANVRAFYQRLNPSIQIIGTGGVKTGRDAFEHILC 262
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1093453903 317 GASLLQGYTPLIYGGPDWIRDIHQGLARQIRAQGFYSISEAVG 359
Cdd:PRK02506 263 GASMVQVGTALHKEGPAVFERLTKELKAIMAEKGYQSLEDFRG 305
|
|
| Aldolase_Class_I |
cd00945 |
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ... |
154-321 |
4.47e-05 |
|
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which stabilizes a reaction intermediates via Schiff base formation, and have TIM beta/alpha barrel fold. The members of this family include 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-4-hydroxyglutarate (KHG) aldolases, transaldolase, dihydrodipicolinate synthase sub-family, Type I 3-dehydroquinate dehydratase, DeoC and DhnA proteins, and metal-independent fructose-1,6-bisphosphate aldolase. Although structurally similar, the class II aldolases use a different mechanism and are believed to have an independent evolutionary origin.
Pssm-ID: 188634 [Multi-domain] Cd Length: 201 Bit Score: 43.86 E-value: 4.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 154 KTKVTPLEEAVDDYresasqlgglADYV--VVNVSSPNTpGLRDLQAVEslrpiLAAVTEETDSPVLVKI---APDLSDE 228
Cdd:cd00945 65 EVKVAEVEEAIDLG----------ADEIdvVINIGSLKE-GDWEEVLEE-----IAAVVEAADGGLPLKVileTRGLKTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 229 DVIA-VADLAVDLGlAGIVATNTTISREGLrtpadevaemgaggvsgapvaarSLEVLKLLHERVGGKLVLISVGGIETA 307
Cdd:cd00945 129 DEIAkAARIAAEAG-ADFIKTSTGFGGGGA-----------------------TVEDVKLMKEAVGGRVGVKAAGGIKTL 184
|
170
....*....|....
gi 1093453903 308 EQAWERIANGASLL 321
Cdd:cd00945 185 EDALAAIEAGADGI 198
|
|
| LOX_like_FMN |
cd04737 |
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ... |
206-330 |
1.62e-03 |
|
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing alpha-hydroxyacid oxidases and catalyzes the oxidation of l-lactate using molecular oxygen to generate pyruvate and H2O2. 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).
Pssm-ID: 240088 [Multi-domain] Cd Length: 351 Bit Score: 40.12 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 206 LAAVTEETDSPVLVKIApdLSDEDviavADLAVDLGLAGIVATNttisreglrtpadevaeMGAGGVSGAPVaarSLEVL 285
Cdd:cd04737 213 IEFIAKISGLPVIVKGI--QSPED----ADVAINAGADGIWVSN-----------------HGGRQLDGGPA---SFDSL 266
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1093453903 286 KLLHERVGGKLVLISVGGIETAEQAWERIANGASLLQGYTPLIYG 330
Cdd:cd04737 267 PEIAEAVNHRVPIIFDSGVRRGEHVFKALASGADAVAVGRPVLYG 311
|
|
| DeoC |
COG0274 |
Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism]; |
195-321 |
5.96e-03 |
|
Deoxyribose-phosphate aldolase [Nucleotide transport and metabolism];
Pssm-ID: 440043 Cd Length: 219 Bit Score: 37.73 E-value: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093453903 195 DLQAVESLrpiLAAVTEETDsPVLVKI---APDLSDEDVIAVADLAVDLGlAGIVATNTtisreglrtpadevaemgaGG 271
Cdd:COG0274 101 DYDAVEEE---IAAVVEAAG-GAVLKVileTGLLTDEEIRKACELAIEAG-ADFVKTST-------------------GF 156
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1093453903 272 VSGAPvaarSLEVLKLLHERVGGKL-VLISvGGIETAEQAWERIANGASLL 321
Cdd:COG0274 157 GPGGA----TVEDVRLMRETVGGRVgVKAS-GGIRTLEDALAMIEAGATRI 202
|
|
| |
