|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
44-426 |
0e+00 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 852.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 44 SAAESEPDLSVTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGAVIAKTVSLDASKVINVTPRYARLRTGSNGSAKTD 123
Cdd:PLN02495 3 GLAASEPDLSVTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGGVIAKTVSLDASKVINVTPRYARLRAGANGSAKGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 124 VIGWQNIELISDRPLETMLKEFERLKKEYPDRILIASVMEEYNKTAWEELIDRVEQTGVDALEINFSCPHGMPERRMGAA 203
Cdd:PLN02495 83 VIGWQNIELISDRPFETMLAEFKQLKEEYPDRILIASIMEEYNKDAWEEIIERVEETGVDALEINFSCPHGMPERKMGAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 204 VGQDCALLDEVCGWINAKATVPVWAKMTPNITDITEPARVSLKSGCEGIAAINTIMSVMGIDMKTLRPEPCVEGYSTPGG 283
Cdd:PLN02495 163 VGQDCDLLEEVCGWINAKATVPVWAKMTPNITDITQPARVALKSGCEGVAAINTIMSVMGINLDTLRPEPCVEGYSTPGG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 284 YSYKAVRPIALAKVMNIAKMMKSEFSEDRSLSGIGGVETGYDAAEFILLGSNTVQVCTGVMMHGYGHVKTLCAELKDFMK 363
Cdd:PLN02495 243 YSSKAVRPIALAKVMAIAKMMKSEFPEDRSLSGIGGVETGGDAAEFILLGADTVQVCTGVMMHGYPLVKNLCAELQDFMK 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1901085933 364 QHNFSTIEEFRGHSLQYFTTHTDLVKRQKEAVEQRKAEKRGLKSDKDWTGDGFVKETESMVSN 426
Cdd:PLN02495 323 KHNFSSIEDFRGASLPYFTTHTDLVQRQKEAIRQRKAIRKGLASDKDWTGDGFVKETESMVSN 385
|
|
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
51-358 |
0e+00 |
|
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: 511.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 51 DLSVTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGAVIAKTVSLDASKVINVTPRYARLRTGSNGsaktdVIGWQNI 130
Cdd:cd02940 1 DLSVTFCGIKFPNPFGLASAPPTTSYPMIRRAFEAGWGGAVTKTLGLDKDIVTNVSPRIARLRTSGRG-----QIGFNNI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 131 ELISDRPLETMLKEFERLKKEYPDRILIASVMEEYNKTAWEELIDRVEQTGVDALEINFSCPHGMPERRMGAAVGQDCAL 210
Cdd:cd02940 76 ELISEKPLEYWLKEIRELKKDFPDKILIASIMCEYNKEDWTELAKLVEEAGADALELNFSCPHGMPERGMGAAVGQDPEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 211 LDEVCGWINAKATVPVWAKMTPNITDITEPARVSLKSGCEGIAAINTIMSVMGIDMKTLRPEPCVEGYSTPGGYSYKAVR 290
Cdd:cd02940 156 VEEICRWVREAVKIPVIAKLTPNITDIREIARAAKEGGADGVSAINTVNSLMGVDLDGTPPAPGVEGKTTYGGYSGPAVK 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1901085933 291 PIALAKVMNIAKMMKsefsEDRSLSGIGGVETGYDAAEFILLGSNTVQVCTGVMMHGYGHVKTLCAEL 358
Cdd:cd02940 236 PIALRAVSQIARAPE----PGLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
51-371 |
5.52e-92 |
|
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: 279.65 E-value: 5.52e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 51 DLSVTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGAVIAKTVSLDAsKVINVTPRYARLRTGSngsaktdviGWQNI 130
Cdd:COG0167 1 DLSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTPEP-QPGNPRPRLFRLPEDS---------GLINR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 131 ELISDRPLETMLKEFERLKKeyPDRILIASVM----EEYnktawEELIDRVEQTGVDALEINFSCPHGmpeRRMGAAVGQ 206
Cdd:COG0167 71 MGLNNPGVDAFLERLLPAKR--YDVPVIVNIGgntvEDY-----VELARRLADAGADYLELNISCPNT---PGGGRALGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 207 DCALLDEVCGWINAKATVPVWAKMTPNITDITEPARVSLKSGCEGIAAINTIMSvMGIDMKTLRPEPcVEGYstpGGYSY 286
Cdd:COG0167 141 DPEALAELLAAVKAATDKPVLVKLAPDLTDIVEIARAAEEAGADGVIAINTTLG-RAIDLETRRPVL-ANEA---GGLSG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 287 KAVRPIALAKVMNIAKMMKSEFsedrSLSGIGGVETGYDAAEFILLGSNTVQVCTGVMMHGYGHVKTLCAELKDFMKQHN 366
Cdd:COG0167 216 PALKPIALRMVREVAQAVGGDI----PIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKG 291
|
....*
gi 1901085933 367 FSTIE 371
Cdd:COG0167 292 FSSIS 296
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
52-375 |
2.02e-53 |
|
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: 180.32 E-value: 2.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 52 LSVTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGAVIAKTVSLDASKViNVTPRYARLRTGSngsakTDVIGWQNie 131
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGLEPRPG-YRNPTIVETPCGM-----LNAIGLQN-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 132 lisdrP-LETMLKEFERLKKEYPdRILIASVmeeYNKTAWE--ELIDRVEQTG--VDALEINFSCPHGMperRMGAAVGQ 206
Cdd:TIGR01037 73 -----PgVEAFLEELKPVREEFP-TPLIASV---YGSSVEEfaEVAEKLEKAPpyVDAYELNLSCPHVK---GGGIAIGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 207 DCALLDEVCGWINAKATVPVWAKMTPNITDITEPARVSLKSGCEGIAAINTIMSvMGIDMKTLRPEPCvegySTPGGYSY 286
Cdd:TIGR01037 141 DPELSADVVKAVKDKTDVPVFAKLSPNVTDITEIAKAAEEAGADGLTLINTLRG-MKIDIKTGKPILA----NKTGGLSG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 287 KAVRPIALAKVMNIAKMMksefseDRSLSGIGGVETGYDAAEFILLGSNTVQVCTGVMMHGYGHVKtLCAELKDFMKQHN 366
Cdd:TIGR01037 216 PAIKPIALRMVYDVYKMV------DIPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYRGFAFKK-IIEGLIAFLKAEG 288
|
....*....
gi 1901085933 367 FSTIEEFRG 375
Cdd:TIGR01037 289 FTSIEELIG 297
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
52-362 |
7.20e-37 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 136.32 E-value: 7.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 52 LSVTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGAVIAKTVSLDAsKVINVTPRYARLRTGSNGSaktdvIGWQNIE 131
Cdd:pfam01180 2 LATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVTPYP-QPGNPTPRVFRLPEGVLNR-----MGLNNPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 132 LisdrplETMLKEFERLKKEYPDRIL--IASVmeeyNKTAWEELIDRVEQTG--VDALEINFSCPH--GmperrmGAAVG 205
Cdd:pfam01180 76 L------DAVLAELLKRRKEYPRPDLgiNLSK----AGMTVDDYVEVARKIGpfADYIELNVSCPNtpG------LRALQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 206 QDCALLDEVCGWINAKATVPVWAKMTPNITDITEPARVSL---KSGCEGIAAINTIMSVMGIDMKTLRPepcVEGYSTpG 282
Cdd:pfam01180 140 TDPELAAILLKVVKEVSKVPVLVKLAPDLTDIVIIDIADValgEDGLDGINATNTTVRGMRIDLKTEKP---ILANGT-G 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 283 GYSYKAVRPIALAKVMNIAKMMKSEFSedrsLSGIGGVETGYDAAEFILLGSNTVQVCTGVMMHGYGHVKTLCAELKDFM 362
Cdd:pfam01180 216 GLSGPPIKPIALKVIRELYQRTGPEIP----IIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
44-426 |
0e+00 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 852.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 44 SAAESEPDLSVTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGAVIAKTVSLDASKVINVTPRYARLRTGSNGSAKTD 123
Cdd:PLN02495 3 GLAASEPDLSVTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGGVIAKTVSLDASKVINVTPRYARLRAGANGSAKGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 124 VIGWQNIELISDRPLETMLKEFERLKKEYPDRILIASVMEEYNKTAWEELIDRVEQTGVDALEINFSCPHGMPERRMGAA 203
Cdd:PLN02495 83 VIGWQNIELISDRPFETMLAEFKQLKEEYPDRILIASIMEEYNKDAWEEIIERVEETGVDALEINFSCPHGMPERKMGAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 204 VGQDCALLDEVCGWINAKATVPVWAKMTPNITDITEPARVSLKSGCEGIAAINTIMSVMGIDMKTLRPEPCVEGYSTPGG 283
Cdd:PLN02495 163 VGQDCDLLEEVCGWINAKATVPVWAKMTPNITDITQPARVALKSGCEGVAAINTIMSVMGINLDTLRPEPCVEGYSTPGG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 284 YSYKAVRPIALAKVMNIAKMMKSEFSEDRSLSGIGGVETGYDAAEFILLGSNTVQVCTGVMMHGYGHVKTLCAELKDFMK 363
Cdd:PLN02495 243 YSSKAVRPIALAKVMAIAKMMKSEFPEDRSLSGIGGVETGGDAAEFILLGADTVQVCTGVMMHGYPLVKNLCAELQDFMK 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1901085933 364 QHNFSTIEEFRGHSLQYFTTHTDLVKRQKEAVEQRKAEKRGLKSDKDWTGDGFVKETESMVSN 426
Cdd:PLN02495 323 KHNFSSIEDFRGASLPYFTTHTDLVQRQKEAIRQRKAIRKGLASDKDWTGDGFVKETESMVSN 385
|
|
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
51-358 |
0e+00 |
|
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: 511.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 51 DLSVTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGAVIAKTVSLDASKVINVTPRYARLRTGSNGsaktdVIGWQNI 130
Cdd:cd02940 1 DLSVTFCGIKFPNPFGLASAPPTTSYPMIRRAFEAGWGGAVTKTLGLDKDIVTNVSPRIARLRTSGRG-----QIGFNNI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 131 ELISDRPLETMLKEFERLKKEYPDRILIASVMEEYNKTAWEELIDRVEQTGVDALEINFSCPHGMPERRMGAAVGQDCAL 210
Cdd:cd02940 76 ELISEKPLEYWLKEIRELKKDFPDKILIASIMCEYNKEDWTELAKLVEEAGADALELNFSCPHGMPERGMGAAVGQDPEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 211 LDEVCGWINAKATVPVWAKMTPNITDITEPARVSLKSGCEGIAAINTIMSVMGIDMKTLRPEPCVEGYSTPGGYSYKAVR 290
Cdd:cd02940 156 VEEICRWVREAVKIPVIAKLTPNITDIREIARAAKEGGADGVSAINTVNSLMGVDLDGTPPAPGVEGKTTYGGYSGPAVK 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1901085933 291 PIALAKVMNIAKMMKsefsEDRSLSGIGGVETGYDAAEFILLGSNTVQVCTGVMMHGYGHVKTLCAEL 358
Cdd:cd02940 236 PIALRAVSQIARAPE----PGLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
51-387 |
7.79e-136 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 395.85 E-value: 7.79e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 51 DLSVTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGAVIAKTVSldaSKVINVT-PRYarlrtGSNGSAKTDVIGWQN 129
Cdd:PRK08318 3 DLSITFCGIKSPNPFWLASAPPTNKYYNVARAFEAGWGGVVWKTLG---PPIVNVSsPRF-----GALVKEDRRFIGFNN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 130 IELISDRPLETMLKEFERLKKEYPDRILIASVMEEYNKTAWEELIDRVEQTGVDALEINFSCPHGMPERRMGAAVGQDCA 209
Cdd:PRK08318 75 IELITDRPLEVNLREIRRVKRDYPDRALIASIMVECNEEEWKEIAPLVEETGADGIELNFGCPHGMSERGMGSAVGQVPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 210 LLDEVCGWINAKATVPVWAKMTPNITDITEPARVSLKSGCEGIAAINTIMSVMGIDMKTLRPEPCVEGYSTPGGYSYKAV 289
Cdd:PRK08318 155 LVEMYTRWVKRGSRLPVIVKLTPNITDIREPARAAKRGGADAVSLINTINSITGVDLDRMIPMPIVNGKSSHGGYCGPAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 290 RPIALAKVmniAKMMKSEFSEDRSLSGIGGVETGYDAAEFILLGSNTVQVCTGVMMHGYGHVKTLCAELKDFMKQHNFST 369
Cdd:PRK08318 235 KPIALNMV---AEIARDPETRGLPISGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISGLSHYMDEKGFAS 311
|
330
....*....|....*...
gi 1901085933 370 IEEFRGHSLQYFTTHTDL 387
Cdd:PRK08318 312 LEDMVGLAVPNVTDWEDL 329
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
51-371 |
5.52e-92 |
|
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: 279.65 E-value: 5.52e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 51 DLSVTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGAVIAKTVSLDAsKVINVTPRYARLRTGSngsaktdviGWQNI 130
Cdd:COG0167 1 DLSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTPEP-QPGNPRPRLFRLPEDS---------GLINR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 131 ELISDRPLETMLKEFERLKKeyPDRILIASVM----EEYnktawEELIDRVEQTGVDALEINFSCPHGmpeRRMGAAVGQ 206
Cdd:COG0167 71 MGLNNPGVDAFLERLLPAKR--YDVPVIVNIGgntvEDY-----VELARRLADAGADYLELNISCPNT---PGGGRALGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 207 DCALLDEVCGWINAKATVPVWAKMTPNITDITEPARVSLKSGCEGIAAINTIMSvMGIDMKTLRPEPcVEGYstpGGYSY 286
Cdd:COG0167 141 DPEALAELLAAVKAATDKPVLVKLAPDLTDIVEIARAAEEAGADGVIAINTTLG-RAIDLETRRPVL-ANEA---GGLSG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 287 KAVRPIALAKVMNIAKMMKSEFsedrSLSGIGGVETGYDAAEFILLGSNTVQVCTGVMMHGYGHVKTLCAELKDFMKQHN 366
Cdd:COG0167 216 PALKPIALRMVREVAQAVGGDI----PIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKG 291
|
....*
gi 1901085933 367 FSTIE 371
Cdd:COG0167 292 FSSIS 296
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
53-375 |
1.19e-64 |
|
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: 209.33 E-value: 1.19e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 53 SVTVNGLKMPNPFVIGSGPPGTnYTVMKRAFDEGW-GAVIAKTVSLDASKViNVTPRYARLrTGSNGSAktdvIGWQNie 131
Cdd:cd04740 1 SVELAGLRLKNPVILASGTFGF-GEELSRVADLGKlGAIVTKSITLEPREG-NPPPRVVET-PGGMLNA----IGLQN-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 132 lisdrP-LETMLKEFERLKKEYpDRILIASV----MEEYnktawEELIDRVEQTGVDALEINFSCPHgmpERRMGAAVGQ 206
Cdd:cd04740 72 -----PgVEAFLEELLPWLREF-GTPVIASIagstVEEF-----VEVAEKLADAGADAIELNISCPN---VKGGGMAFGT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 207 DCALLDEVCGWINAKATVPVWAKMTPNITDITEPARVSLKSGCEGIAAINTIMsVMGIDMKTLRPepcVEGYSTpGGYSY 286
Cdd:cd04740 138 DPEAVAEIVKAVKKATDVPVIVKLTPNVTDIVEIARAAEEAGADGLTLINTLK-GMAIDIETRKP---ILGNVT-GGLSG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 287 KAVRPIALAKVMNIAKMMKSEfsedrsLSGIGGVETGYDAAEFILLGSNTVQVCTGVMMhGYGHVKTLCAELKDFMKQHN 366
Cdd:cd04740 213 PAIKPIALRMVYQVYKAVEIP------IIGVGGIASGEDALEFLMAGASAVQVGTANFV-DPEAFKEIIEGLEAYLDEEG 285
|
....*....
gi 1901085933 367 FSTIEEFRG 375
Cdd:cd04740 286 IKSIEELVG 294
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
51-375 |
2.02e-57 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 190.75 E-value: 2.02e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 51 DLSVTVNGLKMPNPFVIGSGPPGTNYTvMKRAFD-EGWGAVIAKTVSLDAsKVINVTPRYARLRTGSNGSaktdvIGWQN 129
Cdd:PRK07259 1 RLSVELPGLKLKNPVMPASGTFGFGGE-YARFYDlNGLGAIVTKSTTLEP-REGNPTPRIAETPGGMLNA-----IGLQN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 130 ielisdrP-LETMLKEFERLKKEYPDRIlIASV----MEEYNKTAweELIDRVEqtGVDALEINFSCPHGMperRMGAAV 204
Cdd:PRK07259 74 -------PgVDAFIEEELPWLEEFDTPI-IANVagstEEEYAEVA--EKLSKAP--NVDAIELNISCPNVK---HGGMAF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 205 GQDCALLDEVCGWINAKATVPVWAKMTPNITDITEPARVSLKSGCEGIAAINTIMSvMGIDMKTLRPepcVEGYSTpGGY 284
Cdd:PRK07259 139 GTDPELAYEVVKAVKEVVKVPVIVKLTPNVTDIVEIAKAAEEAGADGLSLINTLKG-MAIDIKTRKP---ILANVT-GGL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 285 SYKAVRPIALAKVMNIAKMMKSEfsedrsLSGIGGVETGYDAAEFILLGSNTVQVCTGVMMhGYGHVKTLCAELKDFMKQ 364
Cdd:PRK07259 214 SGPAIKPIALRMVYQVYQAVDIP------IIGMGGISSAEDAIEFIMAGASAVQVGTANFY-DPYAFPKIIEGLEAYLDK 286
|
330
....*....|.
gi 1901085933 365 HNFSTIEEFRG 375
Cdd:PRK07259 287 YGIKSIEEIVG 297
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
54-357 |
5.55e-56 |
|
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: 186.41 E-value: 5.55e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 54 VTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGAVIAKTVSLDAsKVINVTPRYARLRTGSNGSakTDVIGWQNIELI 133
Cdd:cd02810 1 VNFLGLKLKNPFGVAAGPLLKTGELIARAAAAGFGAVVYKTVTLHP-RPGNPLPRVARLPPEGESY--PEQLGILNSFGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 134 SDRPLETMLKEFERLKKEYPDRILIASVMEEyNKTAWEELIDRVEQTGVDALEINFSCPHGMPERRmgaaVGQDCALLDE 213
Cdd:cd02810 78 PNLGLDVWLQDIAKAKKEFPGQPLIASVGGS-SKEDYVELARKIERAGAKALELNLSCPNVGGGRQ----LGQDPEAVAN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 214 VCGWINAKATVPVWAKMTPNIT--DITEPARVSLKSGCEGIAAINTIMSVMGIDMKTlrPEPCVEGYstpGGYSYKAVRP 291
Cdd:cd02810 153 LLKAVKAAVDIPLLVKLSPYFDleDIVELAKAAERAGADGLTAINTISGRVVDLKTV--GPGPKRGT---GGLSGAPIRP 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1901085933 292 IALAKVmniaKMMKSEFSEDRSLSGIGGVETGYDAAEFILLGSNTVQVCTGVMMHGYGHVKTLCAE 357
Cdd:cd02810 228 LALRWV----ARLAARLQLDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKIKKE 289
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
52-375 |
2.02e-53 |
|
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: 180.32 E-value: 2.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 52 LSVTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGAVIAKTVSLDASKViNVTPRYARLRTGSngsakTDVIGWQNie 131
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGLEPRPG-YRNPTIVETPCGM-----LNAIGLQN-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 132 lisdrP-LETMLKEFERLKKEYPdRILIASVmeeYNKTAWE--ELIDRVEQTG--VDALEINFSCPHGMperRMGAAVGQ 206
Cdd:TIGR01037 73 -----PgVEAFLEELKPVREEFP-TPLIASV---YGSSVEEfaEVAEKLEKAPpyVDAYELNLSCPHVK---GGGIAIGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 207 DCALLDEVCGWINAKATVPVWAKMTPNITDITEPARVSLKSGCEGIAAINTIMSvMGIDMKTLRPEPCvegySTPGGYSY 286
Cdd:TIGR01037 141 DPELSADVVKAVKDKTDVPVFAKLSPNVTDITEIAKAAEEAGADGLTLINTLRG-MKIDIKTGKPILA----NKTGGLSG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 287 KAVRPIALAKVMNIAKMMksefseDRSLSGIGGVETGYDAAEFILLGSNTVQVCTGVMMHGYGHVKtLCAELKDFMKQHN 366
Cdd:TIGR01037 216 PAIKPIALRMVYDVYKMV------DIPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYRGFAFKK-IIEGLIAFLKAEG 288
|
....*....
gi 1901085933 367 FSTIEEFRG 375
Cdd:TIGR01037 289 FTSIEELIG 297
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
52-362 |
7.20e-37 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 136.32 E-value: 7.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 52 LSVTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGAVIAKTVSLDAsKVINVTPRYARLRTGSNGSaktdvIGWQNIE 131
Cdd:pfam01180 2 LATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVTPYP-QPGNPTPRVFRLPEGVLNR-----MGLNNPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 132 LisdrplETMLKEFERLKKEYPDRIL--IASVmeeyNKTAWEELIDRVEQTG--VDALEINFSCPH--GmperrmGAAVG 205
Cdd:pfam01180 76 L------DAVLAELLKRRKEYPRPDLgiNLSK----AGMTVDDYVEVARKIGpfADYIELNVSCPNtpG------LRALQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 206 QDCALLDEVCGWINAKATVPVWAKMTPNITDITEPARVSL---KSGCEGIAAINTIMSVMGIDMKTLRPepcVEGYSTpG 282
Cdd:pfam01180 140 TDPELAAILLKVVKEVSKVPVLVKLAPDLTDIVIIDIADValgEDGLDGINATNTTVRGMRIDLKTEKP---ILANGT-G 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 283 GYSYKAVRPIALAKVMNIAKMMKSEFSedrsLSGIGGVETGYDAAEFILLGSNTVQVCTGVMMHGYGHVKTLCAELKDFM 362
Cdd:pfam01180 216 GLSGPPIKPIALKVIRELYQRTGPEIP----IIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| DHOD_like |
cd04739 |
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
51-375 |
1.36e-23 |
|
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: 100.38 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 51 DLSVTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGAVIAKtvSLDASKVINVTPRYARLRTGSNGSAktdvigwqni 130
Cdd:cd04739 1 DLSTTYLGLSLKNPLVASASPLSRNLDNIRRLEDAGAGAIVLP--SLFEEQIEREAQELDRFLTYGSSFA---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 131 ELISDRP--------LETMLKEFERLKKEYpDRILIASvMEEYNKTAWEELIDRVEQTGVDALEINFscpHGMP--ERRM 200
Cdd:cd04739 69 EALSYFPeygrynlgPEEYLELIRRAKRAV-SIPVIAS-LNGVSAGGWVDYARQIEEAGADALELNI---YALPtdPDIS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 201 GAAVGQD-CALLDEVCgwinAKATVPVWAKMTPNITDITEPARVSLKSGCEGIAAINTIMSVmGIDMKTLRPEPCVEgYS 279
Cdd:cd04739 144 GAEVEQRyLDILRAVK----SAVTIPVAVKLSPFFSALAHMAKQLDAAGADGLVLFNRFYQP-DIDLETLEVVPNLL-LS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 280 TPGGYsYKAVRPIAL--AKVmniakmmksefseDRSLSGIGGVETGYDAAEFILLGSNTVQVCTGVMMHGYGHVKTLCAE 357
Cdd:cd04739 218 SPAEI-RLPLRWIAIlsGRV-------------KASLAASGGVHDAEDVVKYLLAGADVVMTTSALLRHGPDYIGTLLAG 283
|
330
....*....|....*...
gi 1901085933 358 LKDFMKQHNFSTIEEFRG 375
Cdd:cd04739 284 LEAWMEEHGYESVQQLRG 301
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
54-362 |
9.27e-21 |
|
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: 92.00 E-value: 9.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 54 VTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGAVIAKTVSLDAsKVINVTPRYARLRTGSNGSaktdvIGWQNieli 133
Cdd:cd04741 1 VTPPGLTISPPLMNAAGPWCTTLEDLLELAASSTGAVTTRSSTLAG-RPGNPEPRYYAFPLGSINS-----LGLPN---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 134 sdRPLETMLKEFERLKKEYPDR--ILIASV--MEEYNkTAWEELIDRVEQTGVDALEINFSCPH--GMPERrmgaavGQD 207
Cdd:cd04741 71 --LGLDYYLEYIRTISDGLPGSakPFFISVtgSAEDI-AAMYKKIAAHQKQFPLAMELNLSCPNvpGKPPP------AYD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 208 CALLDEVCGWINAKATVPVWAKMTPnITDITE-----------PARVSLksgcegIAAINTIMSVMGIDmkTLRPEPCVE 276
Cdd:cd04741 142 FDATLEYLTAVKAAYSIPVGVKTPP-YTDPAQfdtlaealnafACPISF------ITATNTLGNGLVLD--PERETVVLK 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 277 GYSTPGGYSYKAVRPIALAKVMNIAKMMKSEfsedRSLSGIGGVETGYDAAEFILLGSNTVQVCTGVMMHGYGHVKTLCA 356
Cdd:cd04741 213 PKTGFGGLAGAYLHPLALGNVRTFRRLLPSE----IQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEK 288
|
....*.
gi 1901085933 357 ELKDFM 362
Cdd:cd04741 289 ELEDIW 294
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
51-381 |
2.62e-20 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 90.78 E-value: 2.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 51 DLSVTVNGLKMPNPFVIGSGppgtnytVMKRAFDE-------GWGAVIAKTVSLDAsKVINVTPRYARLRTGSNGSaktd 123
Cdd:PRK02506 1 STSTQIAGFKFDNCLMNAAG-------VYCMTKEEleeveasAAGAFVTKSATLEP-RPGNPEPRYADTPLGSINS---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 124 vIGWQNIELisDRPLEtMLKEFERLKKEYPDRILIASVMEEYNKTaweeLIDRVEQTGVDAL-EINFSCPH--GMPErrm 200
Cdd:PRK02506 69 -MGLPNLGF--DYYLD-YVLELQKKGPNKPHFLSVVGLSPEETHT----ILKKIQASDFNGLvELNLSCPNvpGKPQ--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 201 gaaVGQDCALLDEVCGWINAKATVPVWAKMTP--NITDITEPARVSLKSGCEGIAAINTIMSVMGIDMKT----LRPEpc 274
Cdd:PRK02506 138 ---IAYDFETTEQILEEVFTYFTKPLGVKLPPyfDIVHFDQAAAIFNKFPLAFVNCINSIGNGLVIDPEDetvvIKPK-- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 275 vEGYSTPGGySYkaVRPIALAKVMNIAKMMKSEFSedrsLSGIGGVETGYDAAEFILLGSNTVQVCTGVMMHGYGHVKTL 354
Cdd:PRK02506 213 -NGFGGIGG-DY--IKPTALANVRAFYQRLNPSIQ----IIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERL 284
|
330 340
....*....|....*....|....*..
gi 1901085933 355 CAELKDFMKQHNFSTIEEFRGhSLQYF 381
Cdd:PRK02506 285 TKELKAIMAEKGYQSLEDFRG-KLKYL 310
|
|
| PRK07565 |
PRK07565 |
dihydroorotate dehydrogenase-like protein; |
51-375 |
2.31e-18 |
|
dihydroorotate dehydrogenase-like protein;
Pssm-ID: 236051 Cd Length: 334 Bit Score: 85.69 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 51 DLSVTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGAVIAKtvSLDASKVINVTPRYARLRT-GSNGSAK-TDVIGWQ 128
Cdd:PRK07565 2 DLSTTYLGLTLRNPLVASASPLSESVDNVKRLEDAGAGAVVLK--SLFEEQIRHEAAELDRHLThGTESFAEaLDYFPEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 129 NIELISdrpLETMLKEFERLKK--EYPdriLIASvMEEYNKTAWEELIDRVEQTGVDALEINFSCPHGMPERRmGAAVGQ 206
Cdd:PRK07565 80 AKFYVG---PEEYLELIRRAKEavDIP---VIAS-LNGSSAGGWVDYARQIEQAGADALELNIYYLPTDPDIS-GAEVEQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 207 D-CALLDEVCGWInakaTVPVWAKMTPNITDITEPARVSLKSGCEGIAAINTIMSVmGIDMKTLRPEPCVEgYSTPGGYs 285
Cdd:PRK07565 152 RyLDILRAVKSAV----SIPVAVKLSPYFSNLANMAKRLDAAGADGLVLFNRFYQP-DIDLETLEVVPGLV-LSTPAEL- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 286 YKAVRPIAL--AKVmniakmmksefseDRSLSGIGGVETGYDAAEFILLGSNTVQVCTGVMMHGYGHVKTLCAELKDFMK 363
Cdd:PRK07565 225 RLPLRWIAIlsGRV-------------GADLAATTGVHDAEDVIKMLLAGADVVMIASALLRHGPDYIGTILRGLEDWME 291
|
330
....*....|..
gi 1901085933 364 QHNFSTIEEFRG 375
Cdd:PRK07565 292 RHGYESLQQFRG 303
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
50-358 |
2.84e-12 |
|
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: 67.14 E-value: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 50 PDLSVTVNGLKMPNPFVIGSGppgtnytvmkraFDE-----------GWGAVIAKTVSLDASKViNVTPRYARL------ 112
Cdd:cd04738 37 PRLEVEVFGLTFPNPVGLAAG------------FDKnaeaidallalGFGFVEVGTVTPRPQPG-NPKPRLFRLpedeal 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 113 --RTG--SNGsaktdvigwqnielisdrpLETMLKefeRLKKEYPDRIL----IAsvmeeYNKTAWEEliDRVE--QTGV 182
Cdd:cd04738 104 inRMGfnNDG-------------------ADAVAK---RLKKRRPRGGPlgvnIG-----KNKDTPLE--DAVEdyVIGV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 183 -------DALEINFSCP--HGMpeRRMgaavgQDCALLDEVCGWINA-----KATVPVWAKMTPNITD--ITEPARVSLK 246
Cdd:cd04738 155 rklgpyaDYLVVNVSSPntPGL--RDL-----QGKEALRELLTAVKEernklGKKVPLLVKIAPDLSDeeLEDIADVALE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 247 SGCEGIAAINTIMSVMGIDMKTLRPEPcvegystpGGYSYKAVRPIALAKVMNIAKMMKSEFSedrsLSGIGGVETGYDA 326
Cdd:cd04738 228 HGVDGIIATNTTISRPGLLRSPLANET--------GGLSGAPLKERSTEVLRELYKLTGGKIP----IIGVGGISSGEDA 295
|
330 340 350
....*....|....*....|....*....|..
gi 1901085933 327 AEFILLGSNTVQVCTGVMMHGYGHVKTLCAEL 358
Cdd:cd04738 296 YEKIRAGASLVQLYTGLVYEGPGLVKRIKREL 327
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
182-365 |
1.07e-08 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 56.32 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 182 VDALEINFSCP--HGMpeRRMgaavgQDCALLDEVCGWINAK-----ATVPVWAKMTPNITD--ITEPARVSLKSGCEGI 252
Cdd:PRK05286 170 ADYFTVNISSPntPGL--RDL-----QYGEALDELLAALKEAqaelhGYVPLLVKIAPDLSDeeLDDIADLALEHGIDGV 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 253 AAINTIMSVMGIDMKTLRPEPcvegystpGGYSYKAVRPIALAKVMNIAKMMKSEFSedrsLSGIGGVETGYDAAEFILL 332
Cdd:PRK05286 243 IATNTTLSRDGLKGLPNADEA--------GGLSGRPLFERSTEVIRRLYKELGGRLP----IIGVGGIDSAEDAYEKIRA 310
|
170 180 190
....*....|....*....|....*....|...
gi 1901085933 333 GSNTVQVCTGVMMHGYGHVKTLCAELKDFMKQH 365
Cdd:PRK05286 311 GASLVQIYSGLIYEGPGLVKEIVRGLARLLRRD 343
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
166-372 |
1.14e-05 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 47.42 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 166 NKTAWEELIDRVeqTGV-------DALEINFSCPHGmPERRM--GAAVGQDcaLLDEVCG------WINAkATVPVWAKM 230
Cdd:PLN02826 196 NKTSEDAAADYV--QGVralsqyaDYLVINVSSPNT-PGLRKlqGRKQLKD--LLKKVLAardemqWGEE-GPPPLLVKI 269
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901085933 231 TPNIT--DITEPARVSLKSGCEGIAAINTIMSvmgidmktlRPEPcVEGYSTP---GGYSYKAVRPIALAKVMNIAKMMK 305
Cdd:PLN02826 270 APDLSkeDLEDIAAVALALGIDGLIISNTTIS---------RPDS-VLGHPHAdeaGGLSGKPLFDLSTEVLREMYRLTR 339
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170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1901085933 306 SEFSedrsLSGIGGVETGYDAAEFILLGSNTVQVCTGVMMHGYGHVKTLCAELKDFMKQHNFSTIEE 372
Cdd:PLN02826 340 GKIP----LVGCGGVSSGEDAYKKIRAGASLVQLYTAFAYEGPALIPRIKAELAACLERDGFKSIQE 402
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