|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07565 |
PRK07565 |
dihydroorotate dehydrogenase-like protein; |
2-335 |
0e+00 |
|
dihydroorotate dehydrogenase-like protein;
Pssm-ID: 236051 Cd Length: 334 Bit Score: 503.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 2 SDLHTKYMGLTLKSPLVASAGPIQQKVDGVKALADAGVGAIVMYSLFEEQVRHEEARQAEIELEYMDSFAESLSFFPTVA 81
Cdd:PRK07565 1 MDLSTTYLGLTLRNPLVASASPLSESVDNVKRLEDAGAGAVVLKSLFEEQIRHEAAELDRHLTHGTESFAEALDYFPEPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 82 SNEGGiTERYLAHLEASANAVDIPVIASLNGATNGGWVDTAKRMEGAGAAGIECNIYMVPGDLEQSAEEVEDRHVEIVQA 161
Cdd:PRK07565 81 KFYVG-PEEYLELIRRAKEAVDIPVIASLNGSSAGGWVDYARQIEQAGADALELNIYYLPTDPDISGAEVEQRYLDILRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 162 VKDAVSVPVAVKLSPFFSALGNMATRLDAAGADALVMFNRFLQPDINVETMQVEPGVWLSSPADARLPLTWIAALSGRIG 241
Cdd:PRK07565 160 VKSAVSIPVAVKLSPYFSNLANMAKRLDAAGADGLVLFNRFYQPDIDLETLEVVPGLVLSTPAELRLPLRWIAILSGRVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 242 ASLAASSGVESAADVVKYLLAGADVVMTTSALVRHGTGYATELQKGLESYLPRKEV-NLDTLRGMLAVPNDASTAEYERN 320
Cdd:PRK07565 240 ADLAATTGVHDAEDVIKMLLAGADVVMIASALLRHGPDYIGTILRGLEDWMERHGYeSLQQFRGSMSQKNVPDPAAFERA 319
|
330
....*....|....*
gi 365738569 321 GYVAALEKAKTTYGS 335
Cdd:PRK07565 320 QYMKALSSYSPEAGP 334
|
|
| DHOD_like |
cd04739 |
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
3-328 |
6.42e-175 |
|
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: 487.89 E-value: 6.42e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 3 DLHTKYMGLTLKSPLVASAGPIQQKVDGVKALADAGVGAIVMYSLFEEQVRHEeARQAEIELEYMDSFAESLSFFPTVAS 82
Cdd:cd04739 1 DLSTTYLGLSLKNPLVASASPLSRNLDNIRRLEDAGAGAIVLPSLFEEQIERE-AQELDRFLTYGSSFAEALSYFPEYGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 83 NEGGiTERYLAHLEASANAVDIPVIASLNGATNGGWVDTAKRMEGAGAAGIECNIYMVPGDLEQSAEEVEDRHVEIVQAV 162
Cdd:cd04739 80 YNLG-PEEYLELIRRAKRAVSIPVIASLNGVSAGGWVDYARQIEEAGADALELNIYALPTDPDISGAEVEQRYLDILRAV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 163 KDAVSVPVAVKLSPFFSALGNMATRLDAAGADALVMFNRFLQPDINVETMQVEPGVWLSSPADARLPLTWIAALSGRIGA 242
Cdd:cd04739 159 KSAVTIPVAVKLSPFFSALAHMAKQLDAAGADGLVLFNRFYQPDIDLETLEVVPNLLLSSPAEIRLPLRWIAILSGRVKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 243 SLAASSGVESAADVVKYLLAGADVVMTTSALVRHGTGYATELQKGLESYLPRKEV-NLDTLRGMLAVPNDASTAEYERNG 321
Cdd:cd04739 239 SLAASGGVHDAEDVVKYLLAGADVVMTTSALLRHGPDYIGTLLAGLEAWMEEHGYeSVQQLRGSMSQKNVPDPAAFERAQ 318
|
....*..
gi 365738569 322 YVAALEK 328
Cdd:cd04739 319 YMKALSS 325
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
3-298 |
9.04e-41 |
|
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: 144.45 E-value: 9.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 3 DLHTKYMGLTLKSPLVASAGPIQQKVDGVKALADAGVGAIVMYSLF-EEQVRHEEARQAEieLEYMDSFAESLSFfptva 81
Cdd:COG0167 1 DLSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTpEPQPGNPRPRLFR--LPEDSGLINRMGL----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 82 SNEGgiTERYLAHLEASANAvDIPVIASLNGATNGGWVDTAKRMEGAGAAGIECNIy--mVPG---DLEQSAEEVEdrhv 156
Cdd:COG0167 74 NNPG--VDAFLERLLPAKRY-DVPVIVNIGGNTVEDYVELARRLADAGADYLELNIscpnTPGggrALGQDPEALA---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 157 EIVQAVKDAVSVPVAVKLSPFFSALGNMATRLDAAGADALVMFNRFLQPDINVETMQVEPGVW---LSSPADARLPLTWI 233
Cdd:COG0167 147 ELLAAVKAATDKPVLVKLAPDLTDIVEIARAAEEAGADGVIAINTTLGRAIDLETRRPVLANEaggLSGPALKPIALRMV 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 365738569 234 AALSGRIGASLA--ASSGVESAADVVKYLLAGADVVMTTSALVRHGTGYATELQKGLESYLPRKEVN 298
Cdd:COG0167 227 REVAQAVGGDIPiiGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFS 293
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
4-306 |
8.54e-20 |
|
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: 87.87 E-value: 8.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 4 LHTKYMGLTLKSPLVASAGPIQQKVDGVKALADAGVGAIVMYSL-FEEQVRHEEARQAEIELEYMDSFAeslsffptvAS 82
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIgLEPRPGYRNPTIVETPCGMLNAIG---------LQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 83 NEGgiTERYLAHLEASANAVDIPVIASLNGATNGGWVDTAKRMEGAG--AAGIECNI---------YMVPGDLEQSAEev 151
Cdd:TIGR01037 72 NPG--VEAFLEELKPVREEFPTPLIASVYGSSVEEFAEVAEKLEKAPpyVDAYELNLscphvkgggIAIGQDPELSAD-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 152 edrhveIVQAVKDAVSVPVAVKLSPFFSALGNMATRLDAAGADALVMFNRFLQPDINVET----MQVEPGvWLSSPADAR 227
Cdd:TIGR01037 148 ------VVKAVKDKTDVPVFAKLSPNVTDITEIAKAAEEAGADGLTLINTLRGMKIDIKTgkpiLANKTG-GLSGPAIKP 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 365738569 228 LPLTWIAALSGRIGASLAASSGVESAADVVKYLLAGADVVMTTSALVRHGTGYaTELQKGLESYLprKEVNLDTLRGML 306
Cdd:TIGR01037 221 IALRMVYDVYKMVDIPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYRGFAF-KKIIEGLIAFL--KAEGFTSIEELI 296
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
4-292 |
1.13e-14 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 73.15 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 4 LHTKYMGLTLKSPLVASAGPIQQKVDGVKALADAGVGAIVMYSL-FEEQVRHEEARQAEIELEYMDSFAeslsfFPtvas 82
Cdd:pfam01180 2 LATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVtPYPQPGNPTPRVFRLPEGVLNRMG-----LN---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 83 NEGgiTERYLAHLEA---SANAVDIPVIASLNGATNGGWVDTAKRMeGAGAAGIECNIYM--VPGdLEQSAEEVEDRHvE 157
Cdd:pfam01180 73 NPG--LDAVLAELLKrrkEYPRPDLGINLSKAGMTVDDYVEVARKI-GPFADYIELNVSCpnTPG-LRALQTDPELAA-I 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 158 IVQAVKDAVSVPVAVKLSPFFSALGNMATRLDAAGADALVMFN------RFLQPDINVETMQVEPGV-WLSSPADARLPL 230
Cdd:pfam01180 148 LLKVVKEVSKVPVLVKLAPDLTDIVIIDIADVALGEDGLDGINatnttvRGMRIDLKTEKPILANGTgGLSGPPIKPIAL 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 365738569 231 TWIAALSGRIGASLA--ASSGVESAADVVKYLLAGADVVMTTSALVRHGTGYATELQKGLESYL 292
Cdd:pfam01180 228 KVIRELYQRTGPEIPiiGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07565 |
PRK07565 |
dihydroorotate dehydrogenase-like protein; |
2-335 |
0e+00 |
|
dihydroorotate dehydrogenase-like protein;
Pssm-ID: 236051 Cd Length: 334 Bit Score: 503.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 2 SDLHTKYMGLTLKSPLVASAGPIQQKVDGVKALADAGVGAIVMYSLFEEQVRHEEARQAEIELEYMDSFAESLSFFPTVA 81
Cdd:PRK07565 1 MDLSTTYLGLTLRNPLVASASPLSESVDNVKRLEDAGAGAVVLKSLFEEQIRHEAAELDRHLTHGTESFAEALDYFPEPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 82 SNEGGiTERYLAHLEASANAVDIPVIASLNGATNGGWVDTAKRMEGAGAAGIECNIYMVPGDLEQSAEEVEDRHVEIVQA 161
Cdd:PRK07565 81 KFYVG-PEEYLELIRRAKEAVDIPVIASLNGSSAGGWVDYARQIEQAGADALELNIYYLPTDPDISGAEVEQRYLDILRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 162 VKDAVSVPVAVKLSPFFSALGNMATRLDAAGADALVMFNRFLQPDINVETMQVEPGVWLSSPADARLPLTWIAALSGRIG 241
Cdd:PRK07565 160 VKSAVSIPVAVKLSPYFSNLANMAKRLDAAGADGLVLFNRFYQPDIDLETLEVVPGLVLSTPAELRLPLRWIAILSGRVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 242 ASLAASSGVESAADVVKYLLAGADVVMTTSALVRHGTGYATELQKGLESYLPRKEV-NLDTLRGMLAVPNDASTAEYERN 320
Cdd:PRK07565 240 ADLAATTGVHDAEDVIKMLLAGADVVMIASALLRHGPDYIGTILRGLEDWMERHGYeSLQQFRGSMSQKNVPDPAAFERA 319
|
330
....*....|....*
gi 365738569 321 GYVAALEKAKTTYGS 335
Cdd:PRK07565 320 QYMKALSSYSPEAGP 334
|
|
| DHOD_like |
cd04739 |
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
3-328 |
6.42e-175 |
|
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: 487.89 E-value: 6.42e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 3 DLHTKYMGLTLKSPLVASAGPIQQKVDGVKALADAGVGAIVMYSLFEEQVRHEeARQAEIELEYMDSFAESLSFFPTVAS 82
Cdd:cd04739 1 DLSTTYLGLSLKNPLVASASPLSRNLDNIRRLEDAGAGAIVLPSLFEEQIERE-AQELDRFLTYGSSFAEALSYFPEYGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 83 NEGGiTERYLAHLEASANAVDIPVIASLNGATNGGWVDTAKRMEGAGAAGIECNIYMVPGDLEQSAEEVEDRHVEIVQAV 162
Cdd:cd04739 80 YNLG-PEEYLELIRRAKRAVSIPVIASLNGVSAGGWVDYARQIEEAGADALELNIYALPTDPDISGAEVEQRYLDILRAV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 163 KDAVSVPVAVKLSPFFSALGNMATRLDAAGADALVMFNRFLQPDINVETMQVEPGVWLSSPADARLPLTWIAALSGRIGA 242
Cdd:cd04739 159 KSAVTIPVAVKLSPFFSALAHMAKQLDAAGADGLVLFNRFYQPDIDLETLEVVPNLLLSSPAEIRLPLRWIAILSGRVKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 243 SLAASSGVESAADVVKYLLAGADVVMTTSALVRHGTGYATELQKGLESYLPRKEV-NLDTLRGMLAVPNDASTAEYERNG 321
Cdd:cd04739 239 SLAASGGVHDAEDVVKYLLAGADVVMTTSALLRHGPDYIGTLLAGLEAWMEEHGYeSVQQLRGSMSQKNVPDPAAFERAQ 318
|
....*..
gi 365738569 322 YVAALEK 328
Cdd:cd04739 319 YMKALSS 325
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
6-277 |
2.56e-46 |
|
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: 158.67 E-value: 2.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 6 TKYMGLTLKSPLVASAGPIQQKVDGVKALADAGVGAIVMYSLF-EEQVRHEEARQAEIELEYmDSFAESLSFFptvasNE 84
Cdd:cd02810 1 VNFLGLKLKNPFGVAAGPLLKTGELIARAAAAGFGAVVYKTVTlHPRPGNPLPRVARLPPEG-ESYPEQLGIL-----NS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 85 GGITE---RYLAH--LEASANAVDIPVIASLNGATNGGWVDTAKRMEGAGAAGIECNIYMVPGDLEQSAEEVEDRHVEIV 159
Cdd:cd02810 75 FGLPNlglDVWLQdiAKAKKEFPGQPLIASVGGSSKEDYVELARKIERAGAKALELNLSCPNVGGGRQLGQDPEAVANLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 160 QAVKDAVSVPVAVKLSPFFSA--LGNMATRLDAAGADALVMFNRFLQPDINVETMQVEPG---VWLSSPADARLPLTWIA 234
Cdd:cd02810 155 KAVKAAVDIPLLVKLSPYFDLedIVELAKAAERAGADGLTAINTISGRVVDLKTVGPGPKrgtGGLSGAPIRPLALRWVA 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 365738569 235 ALSGRIGASLA--ASSGVESAADVVKYLLAGADVVMTTSALVRHG 277
Cdd:cd02810 235 RLAARLQLDIPiiGVGGIDSGEDVLEMLMAGASAVQVATALMWDG 279
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
3-298 |
9.04e-41 |
|
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: 144.45 E-value: 9.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 3 DLHTKYMGLTLKSPLVASAGPIQQKVDGVKALADAGVGAIVMYSLF-EEQVRHEEARQAEieLEYMDSFAESLSFfptva 81
Cdd:COG0167 1 DLSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTpEPQPGNPRPRLFR--LPEDSGLINRMGL----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 82 SNEGgiTERYLAHLEASANAvDIPVIASLNGATNGGWVDTAKRMEGAGAAGIECNIy--mVPG---DLEQSAEEVEdrhv 156
Cdd:COG0167 74 NNPG--VDAFLERLLPAKRY-DVPVIVNIGGNTVEDYVELARRLADAGADYLELNIscpnTPGggrALGQDPEALA---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 157 EIVQAVKDAVSVPVAVKLSPFFSALGNMATRLDAAGADALVMFNRFLQPDINVETMQVEPGVW---LSSPADARLPLTWI 233
Cdd:COG0167 147 ELLAAVKAATDKPVLVKLAPDLTDIVEIARAAEEAGADGVIAINTTLGRAIDLETRRPVLANEaggLSGPALKPIALRMV 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 365738569 234 AALSGRIGASLA--ASSGVESAADVVKYLLAGADVVMTTSALVRHGTGYATELQKGLESYLPRKEVN 298
Cdd:COG0167 227 REVAQAVGGDIPiiGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFS 293
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
10-306 |
3.20e-23 |
|
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: 97.23 E-value: 3.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 10 GLTLKSPLVASAGPIQQKVDGVKALADAGVGAIVMYSL-FEEQVRHEEARQAEIELEYMDSFAeslsffptvASNEGgiT 88
Cdd:cd04740 6 GLRLKNPVILASGTFGFGEELSRVADLGKLGAIVTKSItLEPREGNPPPRVVETPGGMLNAIG---------LQNPG--V 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 89 ERYLAHLEASANAVDIPVIASLNGATNGGWVDTAKRMEGAGAAGIECNIY--------MVPG-DLEQSAEevedrhveIV 159
Cdd:cd04740 75 EAFLEELLPWLREFGTPVIASIAGSTVEEFVEVAEKLADAGADAIELNIScpnvkgggMAFGtDPEAVAE--------IV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 160 QAVKDAVSVPVAVKLSPFFSALGNMATRLDAAGADALVMFNRFLQPDINVETMQ-----VEPGvwLSSPADARLPLTWIA 234
Cdd:cd04740 147 KAVKKATDVPVIVKLTPNVTDIVEIARAAEEAGADGLTLINTLKGMAIDIETRKpilgnVTGG--LSGPAIKPIALRMVY 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 365738569 235 ALSGRIGASLAASSGVESAADVVKYLLAGADVVMTTSALVrHGTGYATELQKGLESYLPRKEV-NLDTLRGML 306
Cdd:cd04740 225 QVYKAVEIPIIGVGGIASGEDALEFLMAGASAVQVGTANF-VDPEAFKEIIEGLEAYLDEEGIkSIEELVGLA 296
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
4-306 |
8.54e-20 |
|
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: 87.87 E-value: 8.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 4 LHTKYMGLTLKSPLVASAGPIQQKVDGVKALADAGVGAIVMYSL-FEEQVRHEEARQAEIELEYMDSFAeslsffptvAS 82
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIgLEPRPGYRNPTIVETPCGMLNAIG---------LQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 83 NEGgiTERYLAHLEASANAVDIPVIASLNGATNGGWVDTAKRMEGAG--AAGIECNI---------YMVPGDLEQSAEev 151
Cdd:TIGR01037 72 NPG--VEAFLEELKPVREEFPTPLIASVYGSSVEEFAEVAEKLEKAPpyVDAYELNLscphvkgggIAIGQDPELSAD-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 152 edrhveIVQAVKDAVSVPVAVKLSPFFSALGNMATRLDAAGADALVMFNRFLQPDINVET----MQVEPGvWLSSPADAR 227
Cdd:TIGR01037 148 ------VVKAVKDKTDVPVFAKLSPNVTDITEIAKAAEEAGADGLTLINTLRGMKIDIKTgkpiLANKTG-GLSGPAIKP 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 365738569 228 LPLTWIAALSGRIGASLAASSGVESAADVVKYLLAGADVVMTTSALVRHGTGYaTELQKGLESYLprKEVNLDTLRGML 306
Cdd:TIGR01037 221 IALRMVYDVYKMVDIPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYRGFAF-KKIIEGLIAFL--KAEGFTSIEELI 296
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
78-306 |
1.11e-18 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 84.82 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 78 PTVASNEGGI----------TERYLAHLEASANAVDIPVIASLNGATNGGWVDTAKRMEGAG-AAGIECNIY-------- 138
Cdd:PRK07259 56 PRIAETPGGMlnaiglqnpgVDAFIEEELPWLEEFDTPIIANVAGSTEEEYAEVAEKLSKAPnVDAIELNIScpnvkhgg 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 139 MVPGdleQSAEEVEdrhvEIVQAVKDAVSVPVAVKLSPFFSALGNMATRLDAAGADALVMFNRFLQPDINVETMQveP-- 216
Cdd:PRK07259 136 MAFG---TDPELAY----EVVKAVKEVVKVPVIVKLTPNVTDIVEIAKAAEEAGADGLSLINTLKGMAIDIKTRK--Pil 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 217 -----GvwLSSPA--------------DARLPLtwiaalsgrIGAslaasSGVESAADVVKYLLAGADVVMTTSALVrHG 277
Cdd:PRK07259 207 anvtgG--LSGPAikpialrmvyqvyqAVDIPI---------IGM-----GGISSAEDAIEFIMAGASAVQVGTANF-YD 269
|
250 260 270
....*....|....*....|....*....|
gi 365738569 278 TGYATELQKGLESYLPRKEV-NLDTLRGML 306
Cdd:PRK07259 270 PYAFPKIIEGLEAYLDKYGIkSIEEIVGIA 299
|
|
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
3-288 |
2.88e-18 |
|
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: 83.49 E-value: 2.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 3 DLHTKYMGLTLKSPLVASAGPIQQKVDGVKALADAGVGAIVM--YSLFEEQVRHEEARQAEIEleymDSFAESLSFfptv 80
Cdd:cd02940 1 DLSVTFCGIKFPNPFGLASAPPTTSYPMIRRAFEAGWGGAVTktLGLDKDIVTNVSPRIARLR----TSGRGQIGF---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 81 aSNEGGITERYLAHLEASANAV--DIP---VIASLNGATN-GGWVDTAKRMEGAGAAGIECNI---YMVP-----GDLEQ 146
Cdd:cd02940 73 -NNIELISEKPLEYWLKEIRELkkDFPdkiLIASIMCEYNkEDWTELAKLVEEAGADALELNFscpHGMPergmgAAVGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 147 SAEEVEdrhvEIVQAVKDAVSVPVAVKLSPFFSALGNMATRLDAAGADALVMFNR-FLQPDINVETMQVEPGV------- 218
Cdd:cd02940 152 DPELVE----EICRWVREAVKIPVIAKLTPNITDIREIARAAKEGGADGVSAINTvNSLMGVDLDGTPPAPGVegkttyg 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 365738569 219 WLSSPADARLPLTWIAAL--SGRIGASLAASSGVESAADVVKYLLAGADVVMTTSALVRHGTGYATELQKGL 288
Cdd:cd02940 228 GYSGPAVKPIALRAVSQIarAPEPGLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
4-292 |
1.13e-14 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 73.15 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 4 LHTKYMGLTLKSPLVASAGPIQQKVDGVKALADAGVGAIVMYSL-FEEQVRHEEARQAEIELEYMDSFAeslsfFPtvas 82
Cdd:pfam01180 2 LATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVtPYPQPGNPTPRVFRLPEGVLNRMG-----LN---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 83 NEGgiTERYLAHLEA---SANAVDIPVIASLNGATNGGWVDTAKRMeGAGAAGIECNIYM--VPGdLEQSAEEVEDRHvE 157
Cdd:pfam01180 73 NPG--LDAVLAELLKrrkEYPRPDLGINLSKAGMTVDDYVEVARKI-GPFADYIELNVSCpnTPG-LRALQTDPELAA-I 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 158 IVQAVKDAVSVPVAVKLSPFFSALGNMATRLDAAGADALVMFN------RFLQPDINVETMQVEPGV-WLSSPADARLPL 230
Cdd:pfam01180 148 LLKVVKEVSKVPVLVKLAPDLTDIVIIDIADVALGEDGLDGINatnttvRGMRIDLKTEKPILANGTgGLSGPPIKPIAL 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 365738569 231 TWIAALSGRIGASLA--ASSGVESAADVVKYLLAGADVVMTTSALVRHGTGYATELQKGLESYL 292
Cdd:pfam01180 228 KVIRELYQRTGPEIPiiGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
106-320 |
5.01e-14 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 72.28 E-value: 5.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 106 VIASLNGATN-GGWVDTAKRMEGAGAAGIECNiYMVP---------GDLEQSAEEVEdrhvEIVQAVKDAVSVPVAVKLS 175
Cdd:PRK08318 102 LIASIMVECNeEEWKEIAPLVEETGADGIELN-FGCPhgmsergmgSAVGQVPELVE----MYTRWVKRGSRLPVIVKLT 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 176 PffsALGNMATRLDAA---GADALVMFNrflqpDIN------VETMQVEPGV-------WLSSPAD-----------ARL 228
Cdd:PRK08318 177 P---NITDIREPARAAkrgGADAVSLIN-----TINsitgvdLDRMIPMPIVngksshgGYCGPAVkpialnmvaeiARD 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 229 PLTWIAALSGrIGaslaassGVESAADVVKYLLAGADVVMTTSALVRHGTGYATELQKGLESYLPRKEV-NLDTLRGmLA 307
Cdd:PRK08318 249 PETRGLPISG-IG-------GIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISGLSHYMDEKGFaSLEDMVG-LA 319
|
250
....*....|...
gi 365738569 308 VPNDASTAEYERN 320
Cdd:PRK08318 320 VPNVTDWEDLDLN 332
|
|
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
3-292 |
1.97e-06 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 49.07 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 3 DLHTKYMGLTLKSPLVASAGPIQQKVDGVKALADAGVGAIV--MYSLFEEQVRHEEARQAEIELEYMDSFAESLSFFptv 80
Cdd:PLN02495 10 DLSVTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGGVIakTVSLDASKVINVTPRYARLRAGANGSAKGRVIGW--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 81 aSNEGGITERYLAHLEASANAV-----DIPVIASLNGATN-GGWVDTAKRMEGAGAAGIECNIYMVPGDLEQ--SAEEVE 152
Cdd:PLN02495 87 -QNIELISDRPFETMLAEFKQLkeeypDRILIASIMEEYNkDAWEEIIERVEETGVDALEINFSCPHGMPERkmGAAVGQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 153 DRHV--EIVQAVKDAVSVPVAVKLSPFFSALGNMATRLDAAGADALVMFNRFLQ-PDINVETMQVEPGV-------WLSS 222
Cdd:PLN02495 166 DCDLleEVCGWINAKATVPVWAKMTPNITDITQPARVALKSGCEGVAAINTIMSvMGINLDTLRPEPCVegystpgGYSS 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 365738569 223 PADARLPLTWIAALSGRI------GASLAASSGVESAADVVKYLLAGADVVMTTSALVRHGTGYATELQKGLESYL 292
Cdd:PLN02495 246 KAVRPIALAKVMAIAKMMksefpeDRSLSGIGGVETGGDAAEFILLGADTVQVCTGVMMHGYPLVKNLCAELQDFM 321
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
146-288 |
1.18e-05 |
|
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: 46.34 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 146 QSAEEVEdrhvEIVQAVKDAVS-----VPVAVKLSPFFS--ALGNMATRLDAAGADALVMFNRFLQ-PDINVETMQVEPG 217
Cdd:cd04738 180 QGKEALR----ELLTAVKEERNklgkkVPLLVKIAPDLSdeELEDIADVALEHGVDGIIATNTTISrPGLLRSPLANETG 255
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 365738569 218 vWLSSPADARLPLTWIAALSGRIGASLA--ASSGVESAADVVKYLLAGADVVMTTSALVRHGTGYATELQKGL 288
Cdd:cd04738 256 -GLSGAPLKERSTEVLRELYKLTGGKIPiiGVGGISSGEDAYEKIRAGASLVQLYTGLVYEGPGLVKRIKREL 327
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
159-268 |
1.54e-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: 39.73 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 159 VQAVKDAVSVPVAVK--LSPffsalgNMATRLDAAGADALVMFN---RflqpdinvetmQVEPGVwlsSPADArlpLTWI 233
Cdd:COG1304 217 IAWLRERWPGPLIVKgvLSP------EDARRAVDAGVDGIDVSNhggR-----------QLDGGP---PTIDA---LPEI 273
|
90 100 110
....*....|....*....|....*....|....*
gi 365738569 234 AALSGRiGASLAASSGVESAADVVKYLLAGADVVM 268
Cdd:COG1304 274 RAAVGG-RIPVIADGGIRRGLDVAKALALGADAVG 307
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
119-240 |
1.83e-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: 39.48 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365738569 119 VDTAKRMEGAGAAGIE---CNIYMV-----P----------GDLEQSAeevedR-HVEIVQAVKDAV--SVPVAVKLSP- 176
Cdd:cd02803 144 AAAARRAKEAGFDGVEihgAHGYLLsqflsPytnkrtdeygGSLENRA-----RfLLEIVAAVREAVgpDFPVGVRLSAd 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 365738569 177 -FFSALGNM------ATRLDAAGADAL-VMFNRFLQPDINVETMQVEPGVWLSSPADAR----LPLtwIAAlsGRI 240
Cdd:cd02803 219 dFVPGGLTLeeaieiAKALEEAGVDALhVSGGSYESPPPIIPPPYVPEGYFLELAEKIKkavkIPV--IAV--GGI 290
|
|
| |
