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Conserved domains on  [gi|478754275|gb|AGJ62847|]
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Dihydroorotate dehydrogenase [Sulfolobus islandicus LAL14/1]

Protein Classification

dihydroorotate dehydrogenase( domain architecture ID 10140816)

catalytic subunit of dihydroorotate dehydrogenase 1B (NAD(+)) catalyzes the conversion of (S)-dihydroorotate and NAD(+) to orotate and NADH

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
dihydoor_dh_Arch super family cl46146
dihydroorotate dehydrogenase PyrD;
2-289 1.93e-173

dihydroorotate dehydrogenase PyrD;


The actual alignment was detected with superfamily member NF041011:

Pssm-ID: 468940  Cd Length: 289  Bit Score: 480.59  E-value: 1.93e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275   2 IKIKDITFNDPLTIASGIIPDVPNYVTTVCEKYKPSAITTKTVTLNPLGPHKPPTVIKLHDGIYMNAIGLGNPGAKAINE 81
Cdd:NF041011   1 IRLAGLELEDPLIIASGILPDVPEYIERVCEKYGPSAITTKTLTLNPLEPHKPPTVVKLHDGCYLNAIGLGNPGIGLLEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275  82 MNVS-CPLIVSVGGASINEIKEVVKVIESKAKIIEINVSSPNRKGYGESLSTLIGDIVENVKSVTRLPVFVKLGPWDNVV 160
Cdd:NF041011  81 IRVKlCPLIVSIGGSSLEEIVEVAEIAEEKADAIELNLSSPNRKGYGASLASLVREIVKAVKSVVKKPVFVKLGPWDNVL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275 161 ELAGRALEKGADGFTLINTIRGLIVDIETFKPILYYGTGGVSGRCLYPVALRIIRDVYEEYGVDIIGVGGVYDWTDVIGM 240
Cdd:NF041011 161 EIAGKALEAGADGLTLINTVKGMAIDVESFKPVLSYGTGGISGKCIHPLAVRIIYDVYREYEAEIIGVGGVFSWRDAIEL 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 478754275 241 LAVGAKLVGLGTVLIEKGFSIIEEIRKGLQSYLFEKGLKFEDIIGISVR 289
Cdd:NF041011 241 MSVGAKAVGVGTAIIDKGLSVISEIRKGLEEYLEEKGLKLEDIIGIAVK 289
 
Name Accession Description Interval E-value
dihydoor_dh_Arch NF041011
dihydroorotate dehydrogenase PyrD;
2-289 1.93e-173

dihydroorotate dehydrogenase PyrD;


Pssm-ID: 468940  Cd Length: 289  Bit Score: 480.59  E-value: 1.93e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275   2 IKIKDITFNDPLTIASGIIPDVPNYVTTVCEKYKPSAITTKTVTLNPLGPHKPPTVIKLHDGIYMNAIGLGNPGAKAINE 81
Cdd:NF041011   1 IRLAGLELEDPLIIASGILPDVPEYIERVCEKYGPSAITTKTLTLNPLEPHKPPTVVKLHDGCYLNAIGLGNPGIGLLEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275  82 MNVS-CPLIVSVGGASINEIKEVVKVIESKAKIIEINVSSPNRKGYGESLSTLIGDIVENVKSVTRLPVFVKLGPWDNVV 160
Cdd:NF041011  81 IRVKlCPLIVSIGGSSLEEIVEVAEIAEEKADAIELNLSSPNRKGYGASLASLVREIVKAVKSVVKKPVFVKLGPWDNVL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275 161 ELAGRALEKGADGFTLINTIRGLIVDIETFKPILYYGTGGVSGRCLYPVALRIIRDVYEEYGVDIIGVGGVYDWTDVIGM 240
Cdd:NF041011 161 EIAGKALEAGADGLTLINTVKGMAIDVESFKPVLSYGTGGISGKCIHPLAVRIIYDVYREYEAEIIGVGGVFSWRDAIEL 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 478754275 241 LAVGAKLVGLGTVLIEKGFSIIEEIRKGLQSYLFEKGLKFEDIIGISVR 289
Cdd:NF041011 241 MSVGAKAVGVGTAIIDKGLSVISEIRKGLEEYLEEKGLKLEDIIGIAVK 289
DHOD_1B_like cd04740
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ...
 1-287 1.08e-107

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: 314.49  E-value: 1.08e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275   1 MIKIKDITFNDPLTIASGIIPdVPNYVTTVCEKYKPSAITTKTVTLNPLGPHKPPTVIKLHDGiYMNAIGLGNPGA-KAI 79
Cdd:cd04740    1 SVELAGLRLKNPVILASGTFG-FGEELSRVADLGKLGAIVTKSITLEPREGNPPPRVVETPGG-MLNAIGLQNPGVeAFL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275  80 NEM-----NVSCPLIVSVGGASINEIKEVVKVIE-SKAKIIEINVSSPNRKGYGESLST---LIGDIVENVKSVTRLPVF 150
Cdd:cd04740   79 EELlpwlrEFGTPVIASIAGSTVEEFVEVAEKLAdAGADAIELNISCPNVKGGGMAFGTdpeAVAEIVKAVKKATDVPVI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275 151 VKLGPW-DNVVELAGRALEKGADGFTLINTIRGLIVDIETFKPILYYGTGGVSGRCLYPVALRIIRDVYEEYGVDIIGVG 229
Cdd:cd04740  159 VKLTPNvTDIVEIARAAEEAGADGLTLINTLKGMAIDIETRKPILGNVTGGLSGPAIKPIALRMVYQVYKAVEIPIIGVG 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 478754275 230 GVYDWTDVIGMLAVGAKLVGLGTVLIEkGFSIIEEIRKGLQSYLFEKGLK-FEDIIGIS 287
Cdd:cd04740  239 GIASGEDALEFLMAGASAVQVGTANFV-DPEAFKEIIEGLEAYLDEEGIKsIEELVGLA 296
PRK07259 PRK07259
dihydroorotate dehydrogenase;
2-289 1.85e-76

dihydroorotate dehydrogenase;


Pssm-ID: 235982  Cd Length: 301  Bit Score: 235.04  E-value: 1.85e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275   2 IKIKDITFNDPLTIASGII---PDVPNYVttvcEKYKPSAITTKTVTLNPLGPHKPPTVIKLHDGIyMNAIGLGNPGAKA 78
Cdd:PRK07259   4 VELPGLKLKNPVMPASGTFgfgGEYARFY----DLNGLGAIVTKSTTLEPREGNPTPRIAETPGGM-LNAIGLQNPGVDA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275  79 --------INEMNVscPLIVSVGGASINEIKEVVKVIES--KAKIIEINVSSPNRKGYGESLST---LIGDIVENVKSVT 145
Cdd:PRK07259  79 fieeelpwLEEFDT--PIIANVAGSTEEEYAEVAEKLSKapNVDAIELNISCPNVKHGGMAFGTdpeLAYEVVKAVKEVV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275 146 RLPVFVKLGP-WDNVVELAGRALEKGADGFTLINTIRGLIVDIETFKPILYYGTGGVSGRCLYPVALRIIRDVYEEYGVD 224
Cdd:PRK07259 157 KVPVIVKLTPnVTDIVEIAKAAEEAGADGLSLINTLKGMAIDIKTRKPILANVTGGLSGPAIKPIALRMVYQVYQAVDIP 236

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 478754275 225 IIGVGGVYDWTDVIGMLAVGAKLVGLGTVLIeKGFSIIEEIRKGLQSYLFEKGLK-FEDIIGISVR 289
Cdd:PRK07259 237 IIGMGGISSAEDAIEFIMAGASAVQVGTANF-YDPYAFPKIIEGLEAYLDKYGIKsIEEIVGIAHK 301
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 2-279 9.47e-72

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: 222.64  E-value: 9.47e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275   2 IKIKDITFNDPLTIASGIiPDVPNYVTTVCEKYKPSAITTKTVTLNPLGPHKPPTVIKL--HDGIyMNAIGLGNPGAKA- 78
Cdd:COG0167    4 VELAGLKFPNPVGLASGF-FDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLpeDSGL-INRMGLNNPGVDAf 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275  79 INEM----NVSCPLIVSVGGASINEIKEVVKVI-ESKAKIIEINVSSPNRKGYGESLST---LIGDIVENVKSVTRLPVF 150
Cdd:COG0167   82 LERLlpakRYDVPVIVNIGGNTVEDYVELARRLaDAGADYLELNISCPNTPGGGRALGQdpeALAELLAAVKAATDKPVL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275 151 VKLGPW-DNVVELAGRALEKGADGFTLINTIRGLIVDIETFKPILYYGTGGVSGRCLYPVALRIIRDVYEEYGVD--IIG 227
Cdd:COG0167  162 VKLAPDlTDIVEIARAAEEAGADGVIAINTTLGRAIDLETRRPVLANEAGGLSGPALKPIALRMVREVAQAVGGDipIIG 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 478754275 228 VGGVYDWTDVIGMLAVGAKLVGLGTVLIEKGFSIIEEIRKGLQSYLFEKGLK 279
Cdd:COG0167  242 VGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFS 293
pyrD_sub1_fam TIGR01037
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ...
 2-287 1.39e-64

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: 204.58  E-value: 1.39e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275    2 IKIKDITFNDPLTIASGIIPDVPNYVTTVcEKYKPSAITTKTVTLNPLGPHKPPTVIKLHDGIyMNAIGLGNPGAKAINE 81
Cdd:TIGR01037   3 VELFGIRFKNPLILASGIMGSGVESLRRI-DRSGAGAVVTKSIGLEPRPGYRNPTIVETPCGM-LNAIGLQNPGVEAFLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275   82 ------MNVSCPLIVSVGGASINEIKEVVKVIESKAK---IIEINVSSPNRKGYGESLST---LIGDIVENVKSVTRLPV 149
Cdd:TIGR01037  81 elkpvrEEFPTPLIASVYGSSVEEFAEVAEKLEKAPPyvdAYELNLSCPHVKGGGIAIGQdpeLSADVVKAVKDKTDVPV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275  150 FVKLGP-WDNVVELAGRALEKGADGFTLINTIRGLIVDIETFKPILYYGTGGVSGRCLYPVALRIIRDVYEEYGVDIIGV 228
Cdd:TIGR01037 161 FAKLSPnVTDITEIAKAAEEAGADGLTLINTLRGMKIDIKTGKPILANKTGGLSGPAIKPIALRMVYDVYKMVDIPIIGV 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275  229 GGVYDWTDVIGMLAVGAKLVGLGTVLIEKGFsIIEEIRKGLQSYLFEKGLK-FEDIIGIS 287
Cdd:TIGR01037 241 GGITSFEDALEFLMAGASAVQVGTAVYYRGF-AFKKIIEGLIAFLKAEGFTsIEELIGIA 299
DHO_dh pfam01180
Dihydroorotate dehydrogenase;
3-273 1.61e-45

Dihydroorotate dehydrogenase;


Pssm-ID: 426103  Cd Length: 291  Bit Score: 155.20  E-value: 1.61e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275    3 KIKDITFNDPLTIASGIIPDvpnyvTTVCEKY----KPSAITTKTVTLNPLGPHKPPTVIKLHDGIyMNAIGLGNPGAKA 78
Cdd:pfam01180   5 KIPGLDFKNPIGLASGFDKF-----GEEALKWlalgKFGAIEIKSVTPYPQPGNPTPRVFRLPEGV-LNRMGLNNPGLDA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275   79 I-----------NEMNVscPLIVSVGGASINEIKEVVKVIESKAKIIEINVSSPNRKGyGESLST---LIGDIVENVKSV 144
Cdd:pfam01180  79 VlaellkrrkeyPRPDL--GINLSKAGMTVDDYVEVARKIGPFADYIELNVSCPNTPG-LRALQTdpeLAAILLKVVKEV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275  145 TRLPVFVKLGP-WDNVVELAGRALEKGADGFTLIN----TIRGLIVDIETFKPILYYGTGGVSGRCLYPVALRIIRDVYE 219
Cdd:pfam01180 156 SKVPVLVKLAPdLTDIVIIDIADVALGEDGLDGINatntTVRGMRIDLKTEKPILANGTGGLSGPPIKPIALKVIRELYQ 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 478754275  220 EYGVD--IIGVGGVYDWTDVIGMLAVGAKLVGLGTVLIEKGFSIIEEIRKGLQSYL 273
Cdd:pfam01180 236 RTGPEipIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
 
Name Accession Description Interval E-value
dihydoor_dh_Arch NF041011
dihydroorotate dehydrogenase PyrD;
2-289 1.93e-173

dihydroorotate dehydrogenase PyrD;


Pssm-ID: 468940  Cd Length: 289  Bit Score: 480.59  E-value: 1.93e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275   2 IKIKDITFNDPLTIASGIIPDVPNYVTTVCEKYKPSAITTKTVTLNPLGPHKPPTVIKLHDGIYMNAIGLGNPGAKAINE 81
Cdd:NF041011   1 IRLAGLELEDPLIIASGILPDVPEYIERVCEKYGPSAITTKTLTLNPLEPHKPPTVVKLHDGCYLNAIGLGNPGIGLLEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275  82 MNVS-CPLIVSVGGASINEIKEVVKVIESKAKIIEINVSSPNRKGYGESLSTLIGDIVENVKSVTRLPVFVKLGPWDNVV 160
Cdd:NF041011  81 IRVKlCPLIVSIGGSSLEEIVEVAEIAEEKADAIELNLSSPNRKGYGASLASLVREIVKAVKSVVKKPVFVKLGPWDNVL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275 161 ELAGRALEKGADGFTLINTIRGLIVDIETFKPILYYGTGGVSGRCLYPVALRIIRDVYEEYGVDIIGVGGVYDWTDVIGM 240
Cdd:NF041011 161 EIAGKALEAGADGLTLINTVKGMAIDVESFKPVLSYGTGGISGKCIHPLAVRIIYDVYREYEAEIIGVGGVFSWRDAIEL 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 478754275 241 LAVGAKLVGLGTVLIEKGFSIIEEIRKGLQSYLFEKGLKFEDIIGISVR 289
Cdd:NF041011 241 MSVGAKAVGVGTAIIDKGLSVISEIRKGLEEYLEEKGLKLEDIIGIAVK 289
DHOD_1B_like cd04740
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ...
 1-287 1.08e-107

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: 314.49  E-value: 1.08e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275   1 MIKIKDITFNDPLTIASGIIPdVPNYVTTVCEKYKPSAITTKTVTLNPLGPHKPPTVIKLHDGiYMNAIGLGNPGA-KAI 79
Cdd:cd04740    1 SVELAGLRLKNPVILASGTFG-FGEELSRVADLGKLGAIVTKSITLEPREGNPPPRVVETPGG-MLNAIGLQNPGVeAFL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275  80 NEM-----NVSCPLIVSVGGASINEIKEVVKVIE-SKAKIIEINVSSPNRKGYGESLST---LIGDIVENVKSVTRLPVF 150
Cdd:cd04740   79 EELlpwlrEFGTPVIASIAGSTVEEFVEVAEKLAdAGADAIELNISCPNVKGGGMAFGTdpeAVAEIVKAVKKATDVPVI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275 151 VKLGPW-DNVVELAGRALEKGADGFTLINTIRGLIVDIETFKPILYYGTGGVSGRCLYPVALRIIRDVYEEYGVDIIGVG 229
Cdd:cd04740  159 VKLTPNvTDIVEIARAAEEAGADGLTLINTLKGMAIDIETRKPILGNVTGGLSGPAIKPIALRMVYQVYKAVEIPIIGVG 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 478754275 230 GVYDWTDVIGMLAVGAKLVGLGTVLIEkGFSIIEEIRKGLQSYLFEKGLK-FEDIIGIS 287
Cdd:cd04740  239 GIASGEDALEFLMAGASAVQVGTANFV-DPEAFKEIIEGLEAYLDEEGIKsIEELVGLA 296
PRK07259 PRK07259
dihydroorotate dehydrogenase;
2-289 1.85e-76

dihydroorotate dehydrogenase;


Pssm-ID: 235982  Cd Length: 301  Bit Score: 235.04  E-value: 1.85e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275   2 IKIKDITFNDPLTIASGII---PDVPNYVttvcEKYKPSAITTKTVTLNPLGPHKPPTVIKLHDGIyMNAIGLGNPGAKA 78
Cdd:PRK07259   4 VELPGLKLKNPVMPASGTFgfgGEYARFY----DLNGLGAIVTKSTTLEPREGNPTPRIAETPGGM-LNAIGLQNPGVDA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275  79 --------INEMNVscPLIVSVGGASINEIKEVVKVIES--KAKIIEINVSSPNRKGYGESLST---LIGDIVENVKSVT 145
Cdd:PRK07259  79 fieeelpwLEEFDT--PIIANVAGSTEEEYAEVAEKLSKapNVDAIELNISCPNVKHGGMAFGTdpeLAYEVVKAVKEVV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275 146 RLPVFVKLGP-WDNVVELAGRALEKGADGFTLINTIRGLIVDIETFKPILYYGTGGVSGRCLYPVALRIIRDVYEEYGVD 224
Cdd:PRK07259 157 KVPVIVKLTPnVTDIVEIAKAAEEAGADGLSLINTLKGMAIDIKTRKPILANVTGGLSGPAIKPIALRMVYQVYQAVDIP 236

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 478754275 225 IIGVGGVYDWTDVIGMLAVGAKLVGLGTVLIeKGFSIIEEIRKGLQSYLFEKGLK-FEDIIGISVR 289
Cdd:PRK07259 237 IIGMGGISSAEDAIEFIMAGASAVQVGTANF-YDPYAFPKIIEGLEAYLDKYGIKsIEEIVGIAHK 301
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 2-279 9.47e-72

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: 222.64  E-value: 9.47e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275   2 IKIKDITFNDPLTIASGIiPDVPNYVTTVCEKYKPSAITTKTVTLNPLGPHKPPTVIKL--HDGIyMNAIGLGNPGAKA- 78
Cdd:COG0167    4 VELAGLKFPNPVGLASGF-FDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLpeDSGL-INRMGLNNPGVDAf 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275  79 INEM----NVSCPLIVSVGGASINEIKEVVKVI-ESKAKIIEINVSSPNRKGYGESLST---LIGDIVENVKSVTRLPVF 150
Cdd:COG0167   82 LERLlpakRYDVPVIVNIGGNTVEDYVELARRLaDAGADYLELNISCPNTPGGGRALGQdpeALAELLAAVKAATDKPVL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275 151 VKLGPW-DNVVELAGRALEKGADGFTLINTIRGLIVDIETFKPILYYGTGGVSGRCLYPVALRIIRDVYEEYGVD--IIG 227
Cdd:COG0167  162 VKLAPDlTDIVEIARAAEEAGADGVIAINTTLGRAIDLETRRPVLANEAGGLSGPALKPIALRMVREVAQAVGGDipIIG 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 478754275 228 VGGVYDWTDVIGMLAVGAKLVGLGTVLIEKGFSIIEEIRKGLQSYLFEKGLK 279
Cdd:COG0167  242 VGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFS 293
pyrD_sub1_fam TIGR01037
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ...
 2-287 1.39e-64

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: 204.58  E-value: 1.39e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275    2 IKIKDITFNDPLTIASGIIPDVPNYVTTVcEKYKPSAITTKTVTLNPLGPHKPPTVIKLHDGIyMNAIGLGNPGAKAINE 81
Cdd:TIGR01037   3 VELFGIRFKNPLILASGIMGSGVESLRRI-DRSGAGAVVTKSIGLEPRPGYRNPTIVETPCGM-LNAIGLQNPGVEAFLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275   82 ------MNVSCPLIVSVGGASINEIKEVVKVIESKAK---IIEINVSSPNRKGYGESLST---LIGDIVENVKSVTRLPV 149
Cdd:TIGR01037  81 elkpvrEEFPTPLIASVYGSSVEEFAEVAEKLEKAPPyvdAYELNLSCPHVKGGGIAIGQdpeLSADVVKAVKDKTDVPV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275  150 FVKLGP-WDNVVELAGRALEKGADGFTLINTIRGLIVDIETFKPILYYGTGGVSGRCLYPVALRIIRDVYEEYGVDIIGV 228
Cdd:TIGR01037 161 FAKLSPnVTDITEIAKAAEEAGADGLTLINTLRGMKIDIKTGKPILANKTGGLSGPAIKPIALRMVYDVYKMVDIPIIGV 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275  229 GGVYDWTDVIGMLAVGAKLVGLGTVLIEKGFsIIEEIRKGLQSYLFEKGLK-FEDIIGIS 287
Cdd:TIGR01037 241 GGITSFEDALEFLMAGASAVQVGTAVYYRGF-AFKKIIEGLIAFLKAEGFTsIEELIGIA 299
DHOD_DHPD_FMN cd02810
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ...
 38-268 8.36e-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: 155.98  E-value: 8.36e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275  38 AITTKTVTLNPLGPHKPPTVIKLHDGI--------YMNAIGLGNPG--------AKAINEMnVSCPLIVSVGGASINEIK 101
Cdd:cd02810   36 AVVYKTVTLHPRPGNPLPRVARLPPEGesypeqlgILNSFGLPNLGldvwlqdiAKAKKEF-PGQPLIASVGGSSKEDYV 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275 102 EVV-KVIESKAKIIEINVSSPNRKGYGESLST--LIGDIVENVKSVTRLPVFVKLGP---WDNVVELAGRALEKGADGFT 175
Cdd:cd02810  115 ELArKIERAGAKALELNLSCPNVGGGRQLGQDpeAVANLLKAVKAAVDIPLLVKLSPyfdLEDIVELAKAAERAGADGLT 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275 176 LINTIRGLIVDIETFKPILYYGTGGVSGRCLYPVALRIIRDVYEEYGVD--IIGVGGVYDWTDVIGMLAVGAKLVGLGTV 253
Cdd:cd02810  195 AINTISGRVVDLKTVGPGPKRGTGGLSGAPIRPLALRWVARLAARLQLDipIIGVGGIDSGEDVLEMLMAGASAVQVATA 274

                        250
                 ....*....|....*
gi 478754275 254 LIEKGFSIIEEIRKG 268
Cdd:cd02810  275 LMWDGPDVIRKIKKE 289
DHO_dh pfam01180
Dihydroorotate dehydrogenase;
3-273 1.61e-45

Dihydroorotate dehydrogenase;


Pssm-ID: 426103  Cd Length: 291  Bit Score: 155.20  E-value: 1.61e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275    3 KIKDITFNDPLTIASGIIPDvpnyvTTVCEKY----KPSAITTKTVTLNPLGPHKPPTVIKLHDGIyMNAIGLGNPGAKA 78
Cdd:pfam01180   5 KIPGLDFKNPIGLASGFDKF-----GEEALKWlalgKFGAIEIKSVTPYPQPGNPTPRVFRLPEGV-LNRMGLNNPGLDA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275   79 I-----------NEMNVscPLIVSVGGASINEIKEVVKVIESKAKIIEINVSSPNRKGyGESLST---LIGDIVENVKSV 144
Cdd:pfam01180  79 VlaellkrrkeyPRPDL--GINLSKAGMTVDDYVEVARKIGPFADYIELNVSCPNTPG-LRALQTdpeLAAILLKVVKEV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275  145 TRLPVFVKLGP-WDNVVELAGRALEKGADGFTLIN----TIRGLIVDIETFKPILYYGTGGVSGRCLYPVALRIIRDVYE 219
Cdd:pfam01180 156 SKVPVLVKLAPdLTDIVIIDIADVALGEDGLDGINatntTVRGMRIDLKTEKPILANGTGGLSGPPIKPIALKVIRELYQ 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 478754275  220 EYGVD--IIGVGGVYDWTDVIGMLAVGAKLVGLGTVLIEKGFSIIEEIRKGLQSYL 273
Cdd:pfam01180 236 RTGPEipIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
PRK08318 PRK08318
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
88-290 7.94e-31

NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;


Pssm-ID: 236237 [Multi-domain]  Cd Length: 420  Bit Score: 119.28  E-value: 7.94e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275  88 LIVSV-GGASINEIKEVVKVIESK-AKIIEINVSSPN---RKGYGESLST---LIGDIVENVKSVTRLPVFVKLGP-WDN 158
Cdd:PRK08318 102 LIASImVECNEEEWKEIAPLVEETgADGIELNFGCPHgmsERGMGSAVGQvpeLVEMYTRWVKRGSRLPVIVKLTPnITD 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275 159 VVELAGRALEKGADGFTLINTIRGLI-VDIETFKP---ILYYGT-GGVSGRCLYPVALRIIRDVY---EEYGVDIIGVGG 230
Cdd:PRK08318 182 IREPARAAKRGGADAVSLINTINSITgVDLDRMIPmpiVNGKSShGGYCGPAVKPIALNMVAEIArdpETRGLPISGIGG 261

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 478754275 231 VYDWTDVIGMLAVGAKLVGLGTVLIEKGFSIIEEIRKGLQSYLFEKGL-KFEDIIGISVRR 290
Cdd:PRK08318 262 IETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISGLSHYMDEKGFaSLEDMVGLAVPN 322
DHOD_1A_like cd04741
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ...
 38-271 8.37e-31

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: 116.66  E-value: 8.37e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275  38 AITTKTVTLNPLgPHKPPTVIKLHDGIYMNAIGLGNPG---------AKAINEMNVSCPLIVSVGGaSINEIKEVVKVIE 108
Cdd:cd04741   36 AVTTRSSTLAGR-PGNPEPRYYAFPLGSINSLGLPNLGldyyleyirTISDGLPGSAKPFFISVTG-SAEDIAAMYKKIA 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275 109 SKAK----IIEINVSSPN-----RKGY-GESLSTLIgdivENVKSVTRLPVFVKLGPWDNVVELAG--RALEKGADGFTL 176
Cdd:cd04741  114 AHQKqfplAMELNLSCPNvpgkpPPAYdFDATLEYL----TAVKAAYSIPVGVKTPPYTDPAQFDTlaEALNAFACPISF 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275 177 INTIR----GLIVDIETFKPIL--YYGTGGVSGRCLYPVALRIIRDVYE--EYGVDIIGVGGVYDWTDVIGMLAVGAKLV 248
Cdd:cd04741  190 ITATNtlgnGLVLDPERETVVLkpKTGFGGLAGAYLHPLALGNVRTFRRllPSEIQIIGVGGVLDGRGAFRMRLAGASAV 269

                        250       260
                 ....*....|....*....|...
gi 478754275 249 GLGTVLIEKGFSIIEEIRKGLQS 271
Cdd:cd04741  270 QVGTALGKEGPKVFARIEKELED 292
DHPD_FMN cd02940
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ...
 85-269 3.29e-30

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: 115.07  E-value: 3.29e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275  85 SCPLIVSV-GGASINEIKEVVK-VIESKAKIIEINVSSPN---RKGYGESLST---LIGDIVENVKSVTRLPVFVKLGP- 155
Cdd:cd02940   99 DKILIASImCEYNKEDWTELAKlVEEAGADALELNFSCPHgmpERGMGAAVGQdpeLVEEICRWVREAVKIPVIAKLTPn 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275 156 WDNVVELAGRALEKGADGFTLINTIRGLI-VDIETFKPIL----YYGTGGVSGRCLYPVALRIIRDVY--EEYGVDIIGV 228
Cdd:cd02940  179 ITDIREIARAAKEGGADGVSAINTVNSLMgVDLDGTPPAPgvegKTTYGGYSGPAVKPIALRAVSQIAraPEPGLPISGI 258

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 478754275 229 GGVYDWTDVIGMLAVGAKLVGLGTVLIEKGFSIIEEIRKGL 269
Cdd:cd02940  259 GGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
DHOD_2_like cd04738
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ...
 66-269 2.05e-27

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: 108.36  E-value: 2.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275  66 MNAIGLGNPGAKAI-----NEMNVSCPLIVSVGG-------ASINEIKEVVKVIESKAKIIEINVSSPNRKG-----YGE 128
Cdd:cd04738  104 INRMGFNNDGADAVakrlkKRRPRGGPLGVNIGKnkdtpleDAVEDYVIGVRKLGPYADYLVVNVSSPNTPGlrdlqGKE 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275 129 SLSTLIGDIV-ENVKSVTRLPVFVKLGP---WDNVVELAGRALEKGADGFTLINTirgLIVDIETFKPILYYGTGGVSGR 204
Cdd:cd04738  184 ALRELLTAVKeERNKLGKKVPLLVKIAPdlsDEELEDIADVALEHGVDGIIATNT---TISRPGLLRSPLANETGGLSGA 260

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 478754275 205 CLYPVALRIIRDVYEEYG--VDIIGVGGVYDWTDVIGMLAVGAKLVGLGTVLIEKGFSIIEEIRKGL 269
Cdd:cd04738  261 PLKERSTEVLRELYKLTGgkIPIIGVGGISSGEDAYEKIRAGASLVQLYTGLVYEGPGLVKRIKREL 327
PRK05286 PRK05286
quinone-dependent dihydroorotate dehydrogenase;
114-273 7.20e-25

quinone-dependent dihydroorotate dehydrogenase;


Pssm-ID: 235388  Cd Length: 344  Bit Score: 101.78  E-value: 7.20e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275 114 IEINVSSPNRKG-----YGESLSTLIGDIVENVKSVT-RLPVFVKLGP---WDNVVELAGRALEKGADGFTLINT----- 179
Cdd:PRK05286 173 FTVNISSPNTPGlrdlqYGEALDELLAALKEAQAELHgYVPLLVKIAPdlsDEELDDIADLALEHGIDGVIATNTtlsrd 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275 180 -IRGLIVDIETfkpilyygtGGVSGRCLYPVALRIIRDVYEEYG--VDIIGVGGVYDWTDVIGMLAVGAKLVGLGTVLIE 256
Cdd:PRK05286 253 gLKGLPNADEA---------GGLSGRPLFERSTEVIRRLYKELGgrLPIIGVGGIDSAEDAYEKIRAGASLVQIYSGLIY 323

                        170
                 ....*....|....*..
gi 478754275 257 KGFSIIEEIRKGLQSYL 273
Cdd:PRK05286 324 EGPGLVKEIVRGLARLL 340
PRK07565 PRK07565
dihydroorotate dehydrogenase-like protein;
84-283 6.90e-20

dihydroorotate dehydrogenase-like protein;


Pssm-ID: 236051  Cd Length: 334  Bit Score: 87.61  E-value: 6.90e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275  84 VSCPLIVSVGGASINEIKEVVKVIESK-AKIIEINV-SSPNRKGY-GESLSTLIGDIVENVKSVTRLPVFVKLGP-WDNV 159
Cdd:PRK07565 100 VDIPVIASLNGSSAGGWVDYARQIEQAgADALELNIyYLPTDPDIsGAEVEQRYLDILRAVKSAVSIPVAVKLSPyFSNL 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275 160 VELAGRALEKGADGFTLINTIRGLIVDIETF--KPILYYGTGGvSGRclypVALRIIRDVYEEYGVDIIGVGGVYDWTDV 237
Cdd:PRK07565 180 ANMAKRLDAAGADGLVLFNRFYQPDIDLETLevVPGLVLSTPA-ELR----LPLRWIAILSGRVGADLAATTGVHDAEDV 254

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 478754275 238 IGMLAVGAKLVGLGTVLIEKGFSIIEEIRKGLQSYLFEKGlkFEDI 283
Cdd:PRK07565 255 IKMLLAGADVVMIASALLRHGPDYIGTILRGLEDWMERHG--YESL 298
pyrD_sub2 TIGR01036
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ...
 43-269 1.49e-19

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: 86.76  E-value: 1.49e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275   43 TVTLNPLGPHKPPTVIKLHD--GIyMNAIGLGNPGAKAINEmNVS-----CPLIVSVG-------GASINEIKEVVKVIE 108
Cdd:TIGR01036  87 TVTPKPQPGNPRPRLFRLIEdeAL-INRMGFNNHGADVLVE-RLKrarykGPIGINIGknkdtpsEDAKEDYAACLRKLG 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275  109 SKAKIIEINVSSPNRKG-----YGESLSTLIGDIVE---NVKSVTRLPVFVKLGP---WDNVVELAGRALEKGADGFTLI 177
Cdd:TIGR01036 165 PLADYLVVNVSSPNTPGlrdlqYKAELRDLLTAVKQeqdGLRRVHRVPVLVKIAPdltESDLEDIADSLVELGIDGVIAT 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275  178 NTI--RGLIvdietFKPILYYGTGGVSGRCLYPVALRIIRDVYEEYG--VDIIGVGGVYDWTDVIGMLAVGAKLVGLGTV 253
Cdd:TIGR01036 245 NTTvsRSLV-----QGPKNSDETGGLSGKPLQDKSTEIIRRLYAELQgrLPIIGVGGISSAQDALEKIRAGASLLQIYSG 319

                         250
                  ....*....|....*.
gi 478754275  254 LIEKGFSIIEEIRKGL 269
Cdd:TIGR01036 320 FIYWGPPLVKEIVKEI 335
PRK02506 PRK02506
dihydroorotate dehydrogenase 1A; Reviewed
 3-277 1.79e-19

dihydroorotate dehydrogenase 1A; Reviewed


Pssm-ID: 235045  Cd Length: 310  Bit Score: 86.16  E-value: 1.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275   3 KIKDITFNDPLTIASGIipdvpnYVTTVCE-----KYKPSAITTKTVTLNPLGPHKPPTVIKLHDGiYMNAIGLGNPGAK 77
Cdd:PRK02506   5 QIAGFKFDNCLMNAAGV------YCMTKEEleeveASAAGAFVTKSATLEPRPGNPEPRYADTPLG-SINSMGLPNLGFD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275  78 A-------INEMNVSCPLIVSVGGASINEIKEVVKVIE--SKAKIIEINVSSPNRKG---YGESLSTlIGDIVENVKSVT 145
Cdd:PRK02506  78 YyldyvleLQKKGPNKPHFLSVVGLSPEETHTILKKIQasDFNGLVELNLSCPNVPGkpqIAYDFET-TEQILEEVFTYF 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275 146 RLPVFVKLGPWDNVVELAGRA--LEKGADGF-TLINTI-RGLIVDIET----FKPilYYGTGGVSGRCLYPVALRIIRDV 217
Cdd:PRK02506 157 TKPLGVKLPPYFDIVHFDQAAaiFNKFPLAFvNCINSIgNGLVIDPEDetvvIKP--KNGFGGIGGDYIKPTALANVRAF 234

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 478754275 218 YE--EYGVDIIGVGGVYDWTDVIGMLAVGAKLVGLGTVLIEKGFSIIEEIRKGLQSYLFEKG 277
Cdd:PRK02506 235 YQrlNPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAIMAEKG 296
DHOD_like cd04739
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ...
 84-277 1.07e-17

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: 81.51  E-value: 1.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275  84 VSCPLIVSVGGASINEIKEVVKVIESK-AKIIEINVS-SP-NRKGYGESLSTLIGDIVENVKSVTRLPVFVKLGP-WDNV 159
Cdd:cd04739   98 VSIPVIASLNGVSAGGWVDYARQIEEAgADALELNIYaLPtDPDISGAEVEQRYLDILRAVKSAVTIPVAVKLSPfFSAL 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275 160 VELAGRALEKGADGFTLINTIRGLIVDIETFKPilyygtggVSGRCLYPVA-----LRIIRDVYEEYGVDIIGVGGVYDW 234
Cdd:cd04739  178 AHMAKQLDAAGADGLVLFNRFYQPDIDLETLEV--------VPNLLLSSPAeirlpLRWIAILSGRVKASLAASGGVHDA 249

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 478754275 235 TDVIGMLAVGAKLVGLGTVLIEKGFSIIEEIRKGLQSYLFEKG 277
Cdd:cd04739  250 EDVVKYLLAGADVVMTTSALLRHGPDYIGTLLAGLEAWMEEHG 292
PLN02826 PLN02826
dihydroorotate dehydrogenase
 116-289 5.56e-13

dihydroorotate dehydrogenase


Pssm-ID: 178421  Cd Length: 409  Bit Score: 68.61  E-value: 5.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275 116 INVSSPNRKGygesLSTLIG-----DIVENVKSVT---------RLPVFVKLGP---WDNVVELAGRALEKGADGFTLIN 178
Cdd:PLN02826 222 INVSSPNTPG----LRKLQGrkqlkDLLKKVLAARdemqwgeegPPPLLVKIAPdlsKEDLEDIAAVALALGIDGLIISN 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275 179 TIRGLIVDIETFKpiLYYGTGGVSGRCLYPVALRIIRDVYEEYG--VDIIGVGGVYDWTDVIGMLAVGAKLVGLGTVLIE 256
Cdd:PLN02826 298 TTISRPDSVLGHP--HADEAGGLSGKPLFDLSTEVLREMYRLTRgkIPLVGCGGVSSGEDAYKKIRAGASLVQLYTAFAY 375

                        170       180       190
                 ....*....|....*....|....*....|....
gi 478754275 257 KGFSIIEEIRKGLQSYLFEKGLKF-EDIIGISVR 289
Cdd:PLN02826 376 EGPALIPRIKAELAACLERDGFKSiQEAVGADHR 409
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
 87-242 1.88e-09

Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present.


Pssm-ID: 239200 [Multi-domain]  Cd Length: 231  Bit Score: 56.73  E-value: 1.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275  87 PLIVSVGGASINEIKEVVKVIESK-AKIIEINVSSP----NRKGYGESL---STLIGDIVENVKSVTRLPVFVK--LGpW 156
Cdd:cd02801   56 PLIVQLGGSDPETLAEAAKIVEELgADGIDLNMGCPspkvTKGGAGAALlkdPELVAEIVRAVREAVPIPVTVKirLG-W 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275 157 D---NVVELAGRALEKGADGFTlintirglivdietfkpilyygtggVSGR---CLY--PVALRIIRDVYEEYGVDIIGV 228
Cdd:cd02801  135 DdeeETLELAKALEDAGASALT-------------------------VHGRtreQRYsgPADWDYIAEIKEAVSIPVIAN 189

                        170
                 ....*....|....
gi 478754275 229 GGVYDWTDVIGMLA 242
Cdd:cd02801  190 GDIFSLEDALRCLE 203
DusA COG0042
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ...
 87-176 5.96e-08

tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; tRNA-dihydrouridine synthase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439812 [Multi-domain]  Cd Length: 310  Bit Score: 52.79  E-value: 5.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275  87 PLIVSVGGASINEIKEVVKVIES-KAKIIEINV--SSP--NRKGYGESL---STLIGDIVENVKSVTRLPVFVK--LGpW 156
Cdd:COG0042   63 PVAVQLFGSDPEELAEAARIAEElGADEIDINMgcPVKkvTKGGAGAALlrdPELVAEIVKAVVEAVDVPVTVKirLG-W 141

                         90       100
                 ....*....|....*....|....
gi 478754275 157 D----NVVELAGRALEKGADGFTL 176
Cdd:COG0042  142 DdddeNALEFARIAEDAGAAALTV 165
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 87-252 1.83e-05

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 44.50  E-value: 1.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275  87 PLIVSVGGASINEI--KEVVKVIESKAKIIEINVSSPNRKGYGESLSTLIGDIVENVksvtrlPVFVKLGPwdNVVELAG 164
Cdd:cd04722   59 PLGVQLAINDAAAAvdIAAAAARAAGADGVEIHGAVGYLAREDLELIRELREAVPDV------KVVVKLSP--TGELAAA 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 478754275 165 RALEKGADGFTLINtirglivdietfkpilyyGTGGVSGRCLYPVALRIIRDVYEEYGVDIIGVGGVYDWTDVIGMLAVG 244
Cdd:cd04722  131 AAEEAGVDEVGLGN------------------GGGGGGGRDAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALG 192


                 ....*...
gi 478754275 245 AKLVGLGT 252
Cdd:cd04722  193 ADGVIVGS 200
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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