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Conserved domains on  [gi|1517412261|gb|AYW48625|]
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dihydroorotate oxidase [Tetragenococcus osmophilus]

Protein Classification

dihydroorotate dehydrogenase( domain architecture ID 10011806)

dihydroorotate dehydrogenase 1A (fumarate) catalyzes the conversion of (S)-dihydroorotate and fumarate to orotate and succinate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK02506 PRK02506
dihydroorotate dehydrogenase 1A; Reviewed
 1-309 0e+00

dihydroorotate dehydrogenase 1A; Reviewed


:

Pssm-ID: 235045  Cd Length: 310  Bit Score: 579.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261   1 MLETAFQDYTFQSPLMNASGVHCMTTEELNELANSKAGTFVTKSVTKQKRQGNPEPRYYETDFGSINSMGLPNLGFDYYL 80
Cdd:PRK02506    1 STSTQIAGFKFDNCLMNAAGVYCMTKEELEEVEASAAGAFVTKSATLEPRPGNPEPRYADTPLGSINSMGLPNLGFDYYL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261  81 DYLKKHQKI-ASTPVFFSVASMNMQDNIETLKRLEDSEFRGFTELNLSCPNVPGKPQVAYDFETTEKILTEVFSFFTKPL 159
Cdd:PRK02506   81 DYVLELQKKgPNKPHFLSVVGLSPEETHTILKKIQASDFNGLVELNLSCPNVPGKPQIAYDFETTEQILEEVFTYFTKPL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 160 GVKLPPYFDLVHFDQMATILNKFPLAFVNSINSVGNGLIVDTEKEQVVIKPKEGFGGIGGQYIKPTALANVRAFYLRLNP 239
Cdd:PRK02506  161 GVKLPPYFDIVHFDQAAAIFNKFPLAFVNCINSIGNGLVIDPEDETVVIKPKNGFGGIGGDYIKPTALANVRAFYQRLNP 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 240 SIQIIGTGGITSGQDAFEHLLCGASMLQIGTQLYKEGTSVFSRVLSELEAIMDAKGYSRIEQFRGNLKTF 309
Cdd:PRK02506  241 SIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAIMAEKGYQSLEDFRGKLKYL 310
 
Name Accession Description Interval E-value
PRK02506 PRK02506
dihydroorotate dehydrogenase 1A; Reviewed
 1-309 0e+00

dihydroorotate dehydrogenase 1A; Reviewed


Pssm-ID: 235045  Cd Length: 310  Bit Score: 579.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261   1 MLETAFQDYTFQSPLMNASGVHCMTTEELNELANSKAGTFVTKSVTKQKRQGNPEPRYYETDFGSINSMGLPNLGFDYYL 80
Cdd:PRK02506    1 STSTQIAGFKFDNCLMNAAGVYCMTKEELEEVEASAAGAFVTKSATLEPRPGNPEPRYADTPLGSINSMGLPNLGFDYYL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261  81 DYLKKHQKI-ASTPVFFSVASMNMQDNIETLKRLEDSEFRGFTELNLSCPNVPGKPQVAYDFETTEKILTEVFSFFTKPL 159
Cdd:PRK02506   81 DYVLELQKKgPNKPHFLSVVGLSPEETHTILKKIQASDFNGLVELNLSCPNVPGKPQIAYDFETTEQILEEVFTYFTKPL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 160 GVKLPPYFDLVHFDQMATILNKFPLAFVNSINSVGNGLIVDTEKEQVVIKPKEGFGGIGGQYIKPTALANVRAFYLRLNP 239
Cdd:PRK02506  161 GVKLPPYFDIVHFDQAAAIFNKFPLAFVNCINSIGNGLVIDPEDETVVIKPKNGFGGIGGDYIKPTALANVRAFYQRLNP 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 240 SIQIIGTGGITSGQDAFEHLLCGASMLQIGTQLYKEGTSVFSRVLSELEAIMDAKGYSRIEQFRGNLKTF 309
Cdd:PRK02506  241 SIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAIMAEKGYQSLEDFRGKLKYL 310
DHOD_1A_like cd04741
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ...
 10-291 4.90e-151

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: 425.20  E-value: 4.90e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261  10 TFQSPLMNASGVHCMTTEELNELANSKAGTFVTKSVTKQKRQGNPEPRYYETDFGSINSMGLPNLGFDYYLDYLKKHQKI 89
Cdd:cd04741     7 TISPPLMNAAGPWCTTLEDLLELAASSTGAVTTRSSTLAGRPGNPEPRYYAFPLGSINSLGLPNLGLDYYLEYIRTISDG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261  90 A---STPVFFSVASMnMQDNIETLKRLEDS--EFRGFTELNLSCPNVPGKPQVAYDFETTEKILTEVFSFFTKPLGVKLP 164
Cdd:cd04741    87 LpgsAKPFFISVTGS-AEDIAAMYKKIAAHqkQFPLAMELNLSCPNVPGKPPPAYDFDATLEYLTAVKAAYSIPVGVKTP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 165 PYFDLVHFDQMATILNKF--PLAFVNSINSVGNGLIVDTEKEQVVIKPKEGFGGIGGQYIKPTALANVRAFYLRLNPSIQ 242
Cdd:cd04741   166 PYTDPAQFDTLAEALNAFacPISFITATNTLGNGLVLDPERETVVLKPKTGFGGLAGAYLHPLALGNVRTFRRLLPSEIQ 245

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1517412261 243 IIGTGGITSGQDAFEHLLCGASMLQIGTQLYKEGTSVFSRVLSELEAIM 291
Cdd:cd04741   246 IIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEKELEDIW 294
DHO_dh pfam01180
Dihydroorotate dehydrogenase;
1-291 1.66e-120

Dihydroorotate dehydrogenase;


Pssm-ID: 426103  Cd Length: 291  Bit Score: 347.41  E-value: 1.66e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261   1 MLETAFQDYTFQSPLMNASGVHCMTTEELNELANSKAGTFVTKSVTKQKRQGNPEPRYYETDFGSINSMGLPNLGFDYYL 80
Cdd:pfam01180   1 MLATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVTPYPQPGNPTPRVFRLPEGVLNRMGLNNPGLDAVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261  81 DYLKKHQK---IASTPVFFSVASMNMQDNIETLKRLEdsEFRGFTELNLSCPNVPGKPQVAYDFETTEKILTEVFSFFTK 157
Cdd:pfam01180  81 AELLKRRKeypRPDLGINLSKAGMTVDDYVEVARKIG--PFADYIELNVSCPNTPGLRALQTDPELAAILLKVVKEVSKV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 158 PLGVKLPP-YFDLVHFDQMATILNKFPLAFVNSINSVGNGLIVDTEKEQVVIKPkeGFGGIGGQYIKPTALANVRAFYLR 236
Cdd:pfam01180 159 PVLVKLAPdLTDIVIIDIADVALGEDGLDGINATNTTVRGMRIDLKTEKPILAN--GTGGLSGPPIKPIALKVIRELYQR 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1517412261 237 LNPSIQIIGTGGITSGQDAFEHLLCGASMLQIGTQLYKEGTSVFSRVLSELEAIM 291
Cdd:pfam01180 237 TGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 2-300 1.75e-98

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: 291.59  E-value: 1.75e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261   2 LETAFQDYTFQSPLMNASGVHCMTTEELNELANSKAGTFVTKSVTKQKRQGNPEPRYYET--DFGSINSMGLPNLGFDYY 79
Cdd:COG0167     2 LSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLpeDSGLINRMGLNNPGVDAF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261  80 LDYLKKHQKIaSTPVFFSVASMNMQDNIETLKRLEDSEFRGFtELNLSCPNVPGK-PQVAYDFETTEKILTEVFSFFTKP 158
Cdd:COG0167    82 LERLLPAKRY-DVPVIVNIGGNTVEDYVELARRLADAGADYL-ELNISCPNTPGGgRALGQDPEALAELLAAVKAATDKP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 159 LGVKLPPyfDLVHFDQMATILNKFPLAFVNSINSVgNGLIVDTEKEQVVIKpkEGFGGIGGQYIKPTALANVRAFYLRLN 238
Cdd:COG0167   160 VLVKLAP--DLTDIVEIARAAEEAGADGVIAINTT-LGRAIDLETRRPVLA--NEAGGLSGPALKPIALRMVREVAQAVG 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1517412261 239 PSIQIIGTGGITSGQDAFEHLLCGASMLQIGTQLYKEGTSVFSRVLSELEAIMDAKGYSRIE 300
Cdd:COG0167   235 GDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSIS 296
pyrD_sub1_fam TIGR01037
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ...
 2-304 8.89e-54

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: 177.62  E-value: 8.89e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261   2 LETAFQDYTFQSPLMNASGVHCMTTEELNELANSKAGTFVTKSVTKQKRQGNPEPRYYETDFGSINSMGLPNLGFDYYLD 81
Cdd:TIGR01037   1 LEVELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTIVETPCGMLNAIGLQNPGVEAFLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261  82 YLKKHQKIASTPVFFSVASMNMQDNIETLKRLEDS-EFRGFTELNLSCPNVPG-KPQVAYDFETTEKILTEVFSFFTKPL 159
Cdd:TIGR01037  81 ELKPVREEFPTPLIASVYGSSVEEFAEVAEKLEKApPYVDAYELNLSCPHVKGgGIAIGQDPELSADVVKAVKDKTDVPV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 160 GVKLPPyfdlvhfdQMATILnKFPLAFVNS-------INSVGnGLIVDTEKEQVVIKPKegFGGIGGQYIKPTALANVRA 232
Cdd:TIGR01037 161 FAKLSP--------NVTDIT-EIAKAAEEAgadgltlINTLR-GMKIDIKTGKPILANK--TGGLSGPAIKPIALRMVYD 228

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1517412261 233 FYLRLNpsIQIIGTGGITSGQDAFEHLLCGASMLQIGTQLYKEGtSVFSRVLSELEAIMDAKGYSRIEQFRG 304
Cdd:TIGR01037 229 VYKMVD--IPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYRG-FAFKKIIEGLIAFLKAEGFTSIEELIG 297
 
Name Accession Description Interval E-value
PRK02506 PRK02506
dihydroorotate dehydrogenase 1A; Reviewed
 1-309 0e+00

dihydroorotate dehydrogenase 1A; Reviewed


Pssm-ID: 235045  Cd Length: 310  Bit Score: 579.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261   1 MLETAFQDYTFQSPLMNASGVHCMTTEELNELANSKAGTFVTKSVTKQKRQGNPEPRYYETDFGSINSMGLPNLGFDYYL 80
Cdd:PRK02506    1 STSTQIAGFKFDNCLMNAAGVYCMTKEELEEVEASAAGAFVTKSATLEPRPGNPEPRYADTPLGSINSMGLPNLGFDYYL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261  81 DYLKKHQKI-ASTPVFFSVASMNMQDNIETLKRLEDSEFRGFTELNLSCPNVPGKPQVAYDFETTEKILTEVFSFFTKPL 159
Cdd:PRK02506   81 DYVLELQKKgPNKPHFLSVVGLSPEETHTILKKIQASDFNGLVELNLSCPNVPGKPQIAYDFETTEQILEEVFTYFTKPL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 160 GVKLPPYFDLVHFDQMATILNKFPLAFVNSINSVGNGLIVDTEKEQVVIKPKEGFGGIGGQYIKPTALANVRAFYLRLNP 239
Cdd:PRK02506  161 GVKLPPYFDIVHFDQAAAIFNKFPLAFVNCINSIGNGLVIDPEDETVVIKPKNGFGGIGGDYIKPTALANVRAFYQRLNP 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 240 SIQIIGTGGITSGQDAFEHLLCGASMLQIGTQLYKEGTSVFSRVLSELEAIMDAKGYSRIEQFRGNLKTF 309
Cdd:PRK02506  241 SIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAIMAEKGYQSLEDFRGKLKYL 310
DHOD_1A_like cd04741
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ...
 10-291 4.90e-151

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: 425.20  E-value: 4.90e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261  10 TFQSPLMNASGVHCMTTEELNELANSKAGTFVTKSVTKQKRQGNPEPRYYETDFGSINSMGLPNLGFDYYLDYLKKHQKI 89
Cdd:cd04741     7 TISPPLMNAAGPWCTTLEDLLELAASSTGAVTTRSSTLAGRPGNPEPRYYAFPLGSINSLGLPNLGLDYYLEYIRTISDG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261  90 A---STPVFFSVASMnMQDNIETLKRLEDS--EFRGFTELNLSCPNVPGKPQVAYDFETTEKILTEVFSFFTKPLGVKLP 164
Cdd:cd04741    87 LpgsAKPFFISVTGS-AEDIAAMYKKIAAHqkQFPLAMELNLSCPNVPGKPPPAYDFDATLEYLTAVKAAYSIPVGVKTP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 165 PYFDLVHFDQMATILNKF--PLAFVNSINSVGNGLIVDTEKEQVVIKPKEGFGGIGGQYIKPTALANVRAFYLRLNPSIQ 242
Cdd:cd04741   166 PYTDPAQFDTLAEALNAFacPISFITATNTLGNGLVLDPERETVVLKPKTGFGGLAGAYLHPLALGNVRTFRRLLPSEIQ 245

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1517412261 243 IIGTGGITSGQDAFEHLLCGASMLQIGTQLYKEGTSVFSRVLSELEAIM 291
Cdd:cd04741   246 IIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEKELEDIW 294
DHO_dh pfam01180
Dihydroorotate dehydrogenase;
1-291 1.66e-120

Dihydroorotate dehydrogenase;


Pssm-ID: 426103  Cd Length: 291  Bit Score: 347.41  E-value: 1.66e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261   1 MLETAFQDYTFQSPLMNASGVHCMTTEELNELANSKAGTFVTKSVTKQKRQGNPEPRYYETDFGSINSMGLPNLGFDYYL 80
Cdd:pfam01180   1 MLATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVTPYPQPGNPTPRVFRLPEGVLNRMGLNNPGLDAVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261  81 DYLKKHQK---IASTPVFFSVASMNMQDNIETLKRLEdsEFRGFTELNLSCPNVPGKPQVAYDFETTEKILTEVFSFFTK 157
Cdd:pfam01180  81 AELLKRRKeypRPDLGINLSKAGMTVDDYVEVARKIG--PFADYIELNVSCPNTPGLRALQTDPELAAILLKVVKEVSKV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 158 PLGVKLPP-YFDLVHFDQMATILNKFPLAFVNSINSVGNGLIVDTEKEQVVIKPkeGFGGIGGQYIKPTALANVRAFYLR 236
Cdd:pfam01180 159 PVLVKLAPdLTDIVIIDIADVALGEDGLDGINATNTTVRGMRIDLKTEKPILAN--GTGGLSGPPIKPIALKVIRELYQR 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1517412261 237 LNPSIQIIGTGGITSGQDAFEHLLCGASMLQIGTQLYKEGTSVFSRVLSELEAIM 291
Cdd:pfam01180 237 TGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 2-300 1.75e-98

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: 291.59  E-value: 1.75e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261   2 LETAFQDYTFQSPLMNASGVHCMTTEELNELANSKAGTFVTKSVTKQKRQGNPEPRYYET--DFGSINSMGLPNLGFDYY 79
Cdd:COG0167     2 LSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLpeDSGLINRMGLNNPGVDAF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261  80 LDYLKKHQKIaSTPVFFSVASMNMQDNIETLKRLEDSEFRGFtELNLSCPNVPGK-PQVAYDFETTEKILTEVFSFFTKP 158
Cdd:COG0167    82 LERLLPAKRY-DVPVIVNIGGNTVEDYVELARRLADAGADYL-ELNISCPNTPGGgRALGQDPEALAELLAAVKAATDKP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 159 LGVKLPPyfDLVHFDQMATILNKFPLAFVNSINSVgNGLIVDTEKEQVVIKpkEGFGGIGGQYIKPTALANVRAFYLRLN 238
Cdd:COG0167   160 VLVKLAP--DLTDIVEIARAAEEAGADGVIAINTT-LGRAIDLETRRPVLA--NEAGGLSGPALKPIALRMVREVAQAVG 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1517412261 239 PSIQIIGTGGITSGQDAFEHLLCGASMLQIGTQLYKEGTSVFSRVLSELEAIMDAKGYSRIE 300
Cdd:COG0167   235 GDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSIS 296
DHOD_DHPD_FMN cd02810
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ...
 9-286 3.75e-93

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: 278.08  E-value: 3.75e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261   9 YTFQSPLMNASGVHCMTTEELNELANSKAGTFVTKSVTKQKRQGNPEPRY---------YETDFGSINSMGLPNLGFDYY 79
Cdd:cd02810     6 LKLKNPFGVAAGPLLKTGELIARAAAAGFGAVVYKTVTLHPRPGNPLPRVarlppegesYPEQLGILNSFGLPNLGLDVW 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261  80 LDY-LKKHQKIASTPVFFSVASMNMQDNIETLKRLEDSeFRGFTELNLSCPNVPGKPQVAYDFETTEKILTEVFSFFTKP 158
Cdd:cd02810    86 LQDiAKAKKEFPGQPLIASVGGSSKEDYVELARKIERA-GAKALELNLSCPNVGGGRQLGQDPEAVANLLKAVKAAVDIP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 159 LGVKLPPYFDLVHFDQMATILNKFPLAFVNSINSVGNGLIVDtekEQVVIKPKEGFGGIGGQYIKPTALANVRAFYLRLN 238
Cdd:cd02810   165 LLVKLSPYFDLEDIVELAKAAERAGADGLTAINTISGRVVDL---KTVGPGPKRGTGGLSGAPIRPLALRWVARLAARLQ 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1517412261 239 PSIQIIGTGGITSGQDAFEHLLCGASMLQIGTQLYKEGTSVFSRVLSE 286
Cdd:cd02810   242 LDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKIKKE 289
DHOD_1B_like cd04740
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ...
 10-306 2.17e-62

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: 199.70  E-value: 2.17e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261  10 TFQSPLMNASGVhCMTTEELNELAN-SKAGTFVTKSVTKQKRQGNPEPRYYETDFGSINSMGLPNLGFDYYLDYLKKHQK 88
Cdd:cd04740     8 RLKNPVILASGT-FGFGEELSRVADlGKLGAIVTKSITLEPREGNPPPRVVETPGGMLNAIGLQNPGVEAFLEELLPWLR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261  89 IASTPVFFSVASMNMQDNIETLKRLEDSEFRGFtELNLSCPNVP-GKPQVAYDFETTEKILTEVFSFFTKPLGVKLPPyf 167
Cdd:cd04740    87 EFGTPVIASIAGSTVEEFVEVAEKLADAGADAI-ELNISCPNVKgGGMAFGTDPEAVAEIVKAVKKATDVPVIVKLTP-- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 168 dlvhfdqMATILNKFPLAFVNS-------INSVGnGLIVDTEKEQVVIkpKEGFGGIGGQYIKPTALANVRAFYLRLnpS 240
Cdd:cd04740   164 -------NVTDIVEIARAAEEAgadgltlINTLK-GMAIDIETRKPIL--GNVTGGLSGPAIKPIALRMVYQVYKAV--E 231

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1517412261 241 IQIIGTGGITSGQDAFEHLLCGASMLQIGTQLYkEGTSVFSRVLSELEAIMDAKGYSRIEQFRGNL 306
Cdd:cd04740   232 IPIIGVGGIASGEDALEFLMAGASAVQVGTANF-VDPEAFKEIIEGLEAYLDEEGIKSIEELVGLA 296
PRK07259 PRK07259
dihydroorotate dehydrogenase;
1-304 1.06e-59

dihydroorotate dehydrogenase;


Pssm-ID: 235982  Cd Length: 301  Bit Score: 192.67  E-value: 1.06e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261   1 MLETAFQDYTFQSPLMNASGVHCMTTEELNELANSKAGTFVTKSVTKQKRQGNPEPRYYETDFGSINSMGLPNLGFDYYL 80
Cdd:PRK07259    1 RLSVELPGLKLKNPVMPASGTFGFGGEYARFYDLNGLGAIVTKSTTLEPREGNPTPRIAETPGGMLNAIGLQNPGVDAFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261  81 DYLKKHQKIASTPVFFSVASMNMQDNIETLKRLEDSEFRGFTELNLSCPNVPG-------KPQVAYDfettekILTEVFS 153
Cdd:PRK07259   81 EEELPWLEEFDTPIIANVAGSTEEEYAEVAEKLSKAPNVDAIELNISCPNVKHggmafgtDPELAYE------VVKAVKE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 154 FFTKPLGVKLPPYF-DLVhfdQMAtilnkfpLAFVNS-------INSVgNGLIVDTEKEQVVIKPKegFGGIGGQYIKPT 225
Cdd:PRK07259  155 VVKVPVIVKLTPNVtDIV---EIA-------KAAEEAgadglslINTL-KGMAIDIKTRKPILANV--TGGLSGPAIKPI 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 226 AlanVRAFY-LRLNPSIQIIGTGGITSGQDAFEHLLCGASMLQIGTQLYKeGTSVFSRVLSELEAIMDAKGYSRIEQFRG 304
Cdd:PRK07259  222 A---LRMVYqVYQAVDIPIIGMGGISSAEDAIEFIMAGASAVQVGTANFY-DPYAFPKIIEGLEAYLDKYGIKSIEEIVG 297
pyrD_sub1_fam TIGR01037
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ...
 2-304 8.89e-54

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: 177.62  E-value: 8.89e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261   2 LETAFQDYTFQSPLMNASGVHCMTTEELNELANSKAGTFVTKSVTKQKRQGNPEPRYYETDFGSINSMGLPNLGFDYYLD 81
Cdd:TIGR01037   1 LEVELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTIVETPCGMLNAIGLQNPGVEAFLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261  82 YLKKHQKIASTPVFFSVASMNMQDNIETLKRLEDS-EFRGFTELNLSCPNVPG-KPQVAYDFETTEKILTEVFSFFTKPL 159
Cdd:TIGR01037  81 ELKPVREEFPTPLIASVYGSSVEEFAEVAEKLEKApPYVDAYELNLSCPHVKGgGIAIGQDPELSADVVKAVKDKTDVPV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 160 GVKLPPyfdlvhfdQMATILnKFPLAFVNS-------INSVGnGLIVDTEKEQVVIKPKegFGGIGGQYIKPTALANVRA 232
Cdd:TIGR01037 161 FAKLSP--------NVTDIT-EIAKAAEEAgadgltlINTLR-GMKIDIKTGKPILANK--TGGLSGPAIKPIALRMVYD 228

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1517412261 233 FYLRLNpsIQIIGTGGITSGQDAFEHLLCGASMLQIGTQLYKEGtSVFSRVLSELEAIMDAKGYSRIEQFRG 304
Cdd:TIGR01037 229 VYKMVD--IPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYRG-FAFKKIIEGLIAFLKAEGFTSIEELIG 297
DHOD_2_like cd04738
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ...
 44-287 3.02e-25

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: 102.96  E-value: 3.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261  44 SVTKQKRQGNPEPRYY--ETDFGSINSMGLPNLGFDYYLDYLKKHQKiASTPVFFSVASmNMQDNIEtlKRLED-----S 116
Cdd:cd04738    80 TVTPRPQPGNPKPRLFrlPEDEALINRMGFNNDGADAVAKRLKKRRP-RGGPLGVNIGK-NKDTPLE--DAVEDyvigvR 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 117 EFRGFT---ELNLSCPNVPG--KPQVAydfETTEKILTEVFSFFT-----KPLGVKLPPyfDLVHfDQMATIlnkfplaf 186
Cdd:cd04738   156 KLGPYAdylVVNVSSPNTPGlrDLQGK---EALRELLTAVKEERNklgkkVPLLVKIAP--DLSD-EELEDI-------- 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 187 VNSINSVG-NGLIV--------DTEKEqvviKPKEGFGGIGGQYIKPTALANVRAFYLRLNPSIQIIGTGGITSGQDAFE 257
Cdd:cd04738   222 ADVALEHGvDGIIAtnttisrpGLLRS----PLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYE 297

                         250       260       270
                  ....*....|....*....|....*....|
gi 1517412261 258 HLLCGASMLQIGTQLYKEGTSVFSRVLSEL 287
Cdd:cd04738   298 KIRAGASLVQLYTGLVYEGPGLVKRIKREL 327
PRK05286 PRK05286
quinone-dependent dihydroorotate dehydrogenase;
44-295 5.11e-20

quinone-dependent dihydroorotate dehydrogenase;


Pssm-ID: 235388  Cd Length: 344  Bit Score: 88.68  E-value: 5.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261  44 SVTKQKRQGNPEPRYY--ETDFGSINSMGLPNLGFDYYLDYLKKHQKiaSTPVFFSVASMNM-------QDNIETLKRLe 114
Cdd:PRK05286   90 TVTPRPQPGNPKPRLFrlPEDEALINRMGFNNDGADALAERLKKAYR--GIPLGINIGKNKDtpledavDDYLICLEKL- 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 115 dSEFRGFTELNLSCPNVPGKPQVAYDfETTEKILTEV-----FSFFTKPLGVKLPPYFDLVHFDQMATILNKFPLAfvns 189
Cdd:PRK05286  167 -YPYADYFTVNISSPNTPGLRDLQYG-EALDELLAALkeaqaELHGYVPLLVKIAPDLSDEELDDIADLALEHGID---- 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 190 insvgnGLIV---DTEKEQVV-IKPKEGFGGIGGQYIKPTALANVRAFYLRLNPSIQIIGTGGITSGQDAFEHLLCGASM 265
Cdd:PRK05286  241 ------GVIAtntTLSRDGLKgLPNADEAGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGASL 314

                         250       260       270
                  ....*....|....*....|....*....|
gi 1517412261 266 LQIGTQLYKEGTSVFSRVLSELEAIMDAKG 295
Cdd:PRK05286  315 VQIYSGLIYEGPGLVKEIVRGLARLLRRDG 344
DHPD_FMN cd02940
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ...
 38-287 7.54e-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: 81.95  E-value: 7.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261  38 GTFVTKSVTKQKR-QGNPEPRYYETDFGSINSMGLPNL------GFDYYLDYLKKHQK-------IASTpvffsVASMNM 103
Cdd:cd02940    38 GGAVTKTLGLDKDiVTNVSPRIARLRTSGRGQIGFNNIelisekPLEYWLKEIRELKKdfpdkilIASI-----MCEYNK 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 104 QDNIETLKRLEDSEFRGFtELNLSCPNvpGKPQ------VAYDFETTEKILTEVFSFFTKPLGVKLPPyfDLVHFDQMAT 177
Cdd:cd02940   113 EDWTELAKLVEEAGADAL-ELNFSCPH--GMPErgmgaaVGQDPELVEEICRWVREAVKIPVIAKLTP--NITDIREIAR 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 178 ILNKFPLAFVNSINSVgNGLI---VDTEKEQVVIKPKEGFGGIGGQYIKPTALANVRAFYLRLNPSIQIIGTGGITSGQD 254
Cdd:cd02940   188 AAKEGGADGVSAINTV-NSLMgvdLDGTPPAPGVEGKTTYGGYSGPAVKPIALRAVSQIARAPEPGLPISGIGGIESWED 266

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1517412261 255 AFEHLLCGASMLQIGTQLYKEGTSVFSRVLSEL 287
Cdd:cd02940   267 AAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
pyrD_sub2 TIGR01036
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ...
 44-287 1.03e-16

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: 79.44  E-value: 1.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261  44 SVTKQKRQGNPEPRYYE--TDFGSINSMGLPNLGFDYYLDYLKKHQ----------KIASTPVFFSVasmnmQDNIETLK 111
Cdd:TIGR01036  87 TVTPKPQPGNPRPRLFRliEDEALINRMGFNNHGADVLVERLKRARykgpiginigKNKDTPSEDAK-----EDYAACLR 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 112 RLedSEFRGFTELNLSCPNVPGKPQVAYDfETTEKILTEV-------FSFFTKPLGVKLPPYFDLVHFDQMATILNKFPL 184
Cdd:TIGR01036 162 KL--GPLADYLVVNVSSPNTPGLRDLQYK-AELRDLLTAVkqeqdglRRVHRVPVLVKIAPDLTESDLEDIADSLVELGI 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 185 AFVNSINSvgnglivdTEKEQVVIKPK--EGFGGIGGQYIKPTALANVRAFYLRLNPSIQIIGTGGITSGQDAFEHLLCG 262
Cdd:TIGR01036 239 DGVIATNT--------TVSRSLVQGPKnsDETGGLSGKPLQDKSTEIIRRLYAELQGRLPIIGVGGISSAQDALEKIRAG 310

                         250       260
                  ....*....|....*....|....*
gi 1517412261 263 ASMLQIGTQLYKEGTSVFSRVLSEL 287
Cdd:TIGR01036 311 ASLLQIYSGFIYWGPPLVKEIVKEI 335
PRK08318 PRK08318
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
56-304 1.57e-15

NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;


Pssm-ID: 236237 [Multi-domain]  Cd Length: 420  Bit Score: 76.52  E-value: 1.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261  56 PRYYETDFGSINSMGLPNL------GFDYYLDYLKKHQK-------IASTPVffsvaSMNMQDNIETLKRLEDSEFRGFt 122
Cdd:PRK08318   57 PRFGALVKEDRRFIGFNNIelitdrPLEVNLREIRRVKRdypdralIASIMV-----ECNEEEWKEIAPLVEETGADGI- 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 123 ELNLSCPNvpGKP---------QVAydfETTEKILTEVFSFFTKPLGVKLPPYFDLVHFDQMATILNKF-PLAFVNSINS 192
Cdd:PRK08318  131 ELNFGCPH--GMSergmgsavgQVP---ELVEMYTRWVKRGSRLPVIVKLTPNITDIREPARAAKRGGAdAVSLINTINS 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 193 VGNgliVDTEKEQV--VIKPKEGFGGIGGQYIKPTALANVRAfyLRLNP---SIQIIGTGGITSGQDAFEHLLCGASMLQ 267
Cdd:PRK08318  206 ITG---VDLDRMIPmpIVNGKSSHGGYCGPAVKPIALNMVAE--IARDPetrGLPISGIGGIETWRDAAEFILLGAGTVQ 280

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1517412261 268 IGTQLYKEGTSVFSRVLSELEAIMDAKGYSRIEQFRG 304
Cdd:PRK08318  281 VCTAAMQYGFRIVEDMISGLSHYMDEKGFASLEDMVG 317
PLN02826 PLN02826
dihydroorotate dehydrogenase
 44-301 2.46e-14

dihydroorotate dehydrogenase


Pssm-ID: 178421  Cd Length: 409  Bit Score: 72.85  E-value: 2.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261  44 SVTKQKRQGNPEPRYYE--TDFGSINSMGLPNLGFDYYLDYLKKH---QKIAST-PVFFSVASMNMQD---------NIE 108
Cdd:PLN02826  115 SVTPLPQPGNPKPRVFRlrEEGAIINRYGFNSEGIVAVAKRLGAQhgkRKLDETsSSSFSSDDVKAGGkagpgilgvNLG 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 109 TLKRLED------------SEFRGFTELNLSCPNVPG--KPQVAYDFE-TTEKILT---EVFSFFTK--PLGVKLPPyfD 168
Cdd:PLN02826  195 KNKTSEDaaadyvqgvralSQYADYLVINVSSPNTPGlrKLQGRKQLKdLLKKVLAardEMQWGEEGppPLLVKIAP--D 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 169 LVHFD-----QMATILNKFPLAFVNSINSVGNGLIVDTEKEQVvikpkegfGGIGGQYIKPTALANVRAFYLRLNPSIQI 243
Cdd:PLN02826  273 LSKEDlediaAVALALGIDGLIISNTTISRPDSVLGHPHADEA--------GGLSGKPLFDLSTEVLREMYRLTRGKIPL 344

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1517412261 244 IGTGGITSGQDAFEHLLCGASMLQIGTQLYKEGTSVFSRVLSELEAIMDAKGYSRIEQ 301
Cdd:PLN02826  345 VGCGGVSSGEDAYKKIRAGASLVQLYTAFAYEGPALIPRIKAELAACLERDGFKSIQE 402
DHOD_like cd04739
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ...
 13-306 6.67e-13

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: 68.03  E-value: 6.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261  13 SPLMNASGVHCMTTEELNELANSKAGTFVTKSV-TKQKRQGNPEPRYYETDFGS-------INSMGLPNLGFDYYLDYLK 84
Cdd:cd04739    13 NPLVASASPLSRNLDNIRRLEDAGAGAIVLPSLfEEQIEREAQELDRFLTYGSSfaealsyFPEYGRYNLGPEEYLELIR 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261  85 KHQKIASTPVffsVASMN-MQDN--IETLKRLEDSEFRGFtELNLScpNVPGKPQVAYdfETTEK----ILTEVFSFFTK 157
Cdd:cd04739    93 RAKRAVSIPV---IASLNgVSAGgwVDYARQIEEAGADAL-ELNIY--ALPTDPDISG--AEVEQryldILRAVKSAVTI 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 158 PLGVKLPPYF-DLVHfdqMATILNkfplafvnsinSVG-NGLI---------VDTEKEQVVIKPKegFGGIGGQYIKPTA 226
Cdd:cd04739   165 PVAVKLSPFFsALAH---MAKQLD-----------AAGaDGLVlfnrfyqpdIDLETLEVVPNLL--LSSPAEIRLPLRW 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 227 LANVRAfylRLNPSIQIigTGGITSGQDAFEHLLCGASMLQIGTQLYKEGTSVFSRVLSELEAIMDAKGYSRIEQFRGNL 306
Cdd:cd04739   229 IAILSG---RVKASLAA--SGGVHDAEDVVKYLLAGADVVMTTSALLRHGPDYIGTLLAGLEAWMEEHGYESVQQLRGSM 303
PRK07565 PRK07565
dihydroorotate dehydrogenase-like protein;
2-306 2.63e-12

dihydroorotate dehydrogenase-like protein;


Pssm-ID: 236051  Cd Length: 334  Bit Score: 66.43  E-value: 2.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261   2 LETAFQDYTFQSPLMNASGVHCMTTEELNELANSKAGTFVTKSV---------------TKQKRQGNPEPRYYetdfgsI 66
Cdd:PRK07565    3 LSTTYLGLTLRNPLVASASPLSESVDNVKRLEDAGAGAVVLKSLfeeqirheaaeldrhLTHGTESFAEALDY------F 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261  67 NSMGLPNLGFDYYLDYLKKHQKIASTPVffsVASMNMQDN---IETLKRLEDSEFRGFtELNLScpNVPGKPQvaYDFET 143
Cdd:PRK07565   77 PEPAKFYVGPEEYLELIRRAKEAVDIPV---IASLNGSSAggwVDYARQIEQAGADAL-ELNIY--YLPTDPD--ISGAE 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 144 TEK----ILTEVFSFFTKPLGVKLPPYFDlvhfdQMATILNKFPLAFVNsinsvgnGLI---------VDTEKEQVVIKP 210
Cdd:PRK07565  149 VEQryldILRAVKSAVSIPVAVKLSPYFS-----NLANMAKRLDAAGAD-------GLVlfnrfyqpdIDLETLEVVPGL 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 211 KEGFGGIGGQYIKPTALAnvrafYLRLNPSIQIigTGGITSGQDAFEHLLCGASMLQIGTQLYKEGTSVFSRVLSELEAI 290
Cdd:PRK07565  217 VLSTPAELRLPLRWIAIL-----SGRVGADLAA--TTGVHDAEDVIKMLLAGADVVMIASALLRHGPDYIGTILRGLEDW 289

                         330
                  ....*....|....*.
gi 1517412261 291 MDAKGYSRIEQFRGNL 306
Cdd:PRK07565  290 MERHGYESLQQFRGSM 305
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 93-270 1.74e-07

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: 50.66  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261  93 PVFFSVASMNMQDNIETLKRLEDSEFRGFTELNLSCPnvpgkpqvaYDFETTEKILTEVFS-FFTKPLGVKLPPYFDLVH 171
Cdd:cd04722    59 PLGVQLAINDAAAAVDIAAAAARAAGADGVEIHGAVG---------YLAREDLELIRELREaVPDVKVVVKLSPTGELAA 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 172 FDqmatiLNKFPLAFVNSINSVGNGLIVDtekeqvvikpkegfggiggqyikPTALANVRAFYLRLNPSIQIIGTGGITS 251
Cdd:cd04722   130 AA-----AEEAGVDEVGLGNGGGGGGGRD-----------------------AVPIADLLLILAKRGSKVPVIAGGGIND 181

                         170
                  ....*....|....*....
gi 1517412261 252 GQDAFEHLLCGASMLQIGT 270
Cdd:cd04722   182 PEDAAEALALGADGVIVGS 200
IDI-2_FMN cd02811
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ...
 224-303 3.40e-03

Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. Two types of IDIs have been characterized at present. The long known IDI-1 is only dependent on divalent metals for activity, whereas IDI-2 requires a metal, FMN and NADPH. IDI-2 catalyzes the interconversion of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) in the mevalonate pathway.


Pssm-ID: 239205 [Multi-domain]  Cd Length: 326  Bit Score: 38.63  E-value: 3.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517412261 224 PTA--LANVRAfylrLNPSIQIIGTGGITSGQDAFEHLLCGASM-------LQIGTQLYKEGTSVFSRVLSELEAIMDAK 294
Cdd:cd02811   241 PTAasLLEVRS----ALPDLPLIASGGIRNGLDIAKALALGADLvgmagpfLKAALEGEEAVIETIEQIIEELRTAMFLT 316


                  ....*....
gi 1517412261 295 GYSRIEQFR 303
Cdd:cd02811   317 GAKNLAELK 325
 
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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