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Conserved domains on  [gi|353739663|gb|AER20670|]
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dihydroorotate dehydrogenase family protein [Streptococcus suis ST1]

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
 3-310 0e+00

dihydroorotate dehydrogenase 1A; Reviewed


:

Pssm-ID: 235045  Cd Length: 310  Bit Score: 637.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663   3 STATTLGGFTFDNCLMNAAGVWCMTKEELDAVKNSKAGTFVTKTATLDYRAGNPEPRYQNVPLGSINSMGLPNQGLAYYL 82
Cdd:PRK02506   1 STSTQIAGFKFDNCLMNAAGVYCMTKEELEEVEASAAGAFVTKSATLEPRPGNPEPRYADTPLGSINSMGLPNLGFDYYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663  83 DYLLELQETEPERIFVLSLVGMSPDETHEILKTVEASDFKGLIELNLSCPNVPGKPQIAYDFETTETILQEVFTYFTKPL 162
Cdd:PRK02506  81 DYVLELQKKGPNKPHFLSVVGLSPEETHTILKKIQASDFNGLVELNLSCPNVPGKPQIAYDFETTEQILEEVFTYFTKPL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 163 GIKLPPYFDIVHFDQVAAIFNQFPLKFVNCVNSIGNGLYI--KDESVVIKPKNGFGGIGGEYIKPTALANVHAFYQRLKP 240
Cdd:PRK02506 161 GVKLPPYFDIVHFDQAAAIFNKFPLAFVNCINSIGNGLVIdpEDETVVIKPKNGFGGIGGDYIKPTALANVRAFYQRLNP 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 241 EIQIVGTGGVLTGRDAFEHILCGASMVQVGTTLQKEGVAAFGRITAELQAIMAEKGYETIEDFRGKLQHL 310
Cdd:PRK02506 241 SIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAIMAEKGYQSLEDFRGKLKYL 310
 
Name Accession Description Interval E-value
PRK02506 PRK02506
dihydroorotate dehydrogenase 1A; Reviewed
 3-310 0e+00

dihydroorotate dehydrogenase 1A; Reviewed


Pssm-ID: 235045  Cd Length: 310  Bit Score: 637.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663   3 STATTLGGFTFDNCLMNAAGVWCMTKEELDAVKNSKAGTFVTKTATLDYRAGNPEPRYQNVPLGSINSMGLPNQGLAYYL 82
Cdd:PRK02506   1 STSTQIAGFKFDNCLMNAAGVYCMTKEELEEVEASAAGAFVTKSATLEPRPGNPEPRYADTPLGSINSMGLPNLGFDYYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663  83 DYLLELQETEPERIFVLSLVGMSPDETHEILKTVEASDFKGLIELNLSCPNVPGKPQIAYDFETTETILQEVFTYFTKPL 162
Cdd:PRK02506  81 DYVLELQKKGPNKPHFLSVVGLSPEETHTILKKIQASDFNGLVELNLSCPNVPGKPQIAYDFETTEQILEEVFTYFTKPL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 163 GIKLPPYFDIVHFDQVAAIFNQFPLKFVNCVNSIGNGLYI--KDESVVIKPKNGFGGIGGEYIKPTALANVHAFYQRLKP 240
Cdd:PRK02506 161 GVKLPPYFDIVHFDQAAAIFNKFPLAFVNCINSIGNGLVIdpEDETVVIKPKNGFGGIGGDYIKPTALANVRAFYQRLNP 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 241 EIQIVGTGGVLTGRDAFEHILCGASMVQVGTTLQKEGVAAFGRITAELQAIMAEKGYETIEDFRGKLQHL 310
Cdd:PRK02506 241 SIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAIMAEKGYQSLEDFRGKLKYL 310
DHOD_1A_like cd04741
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ...
 6-292 2.32e-146

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: 413.26  E-value: 2.32e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663   6 TTLGGFTFDNCLMNAAGVWCMTKEELDAVKNSKAGTFVTKTATLDYRAGNPEPRYQNVPLGSINSMGLPNQGLAYYLDYL 85
Cdd:cd04741    1 VTPPGLTISPPLMNAAGPWCTTLEDLLELAASSTGAVTTRSSTLAGRPGNPEPRYYAFPLGSINSLGLPNLGLDYYLEYI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663  86 LELQETEPER--IFVLSLVGMsPDETHEILKTVEASD--FKGLIELNLSCPNVPGKPQIAYDFETTETILQEVFTYFTKP 161
Cdd:cd04741   81 RTISDGLPGSakPFFISVTGS-AEDIAAMYKKIAAHQkqFPLAMELNLSCPNVPGKPPPAYDFDATLEYLTAVKAAYSIP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 162 LGIKLPPYFDIVHFDQVAAIFNQF--PLKFVNCVNSIGNGLYIKD--ESVVIKPKNGFGGIGGEYIKPTALANVHAFYQR 237
Cdd:cd04741  160 VGVKTPPYTDPAQFDTLAEALNAFacPISFITATNTLGNGLVLDPerETVVLKPKTGFGGLAGAYLHPLALGNVRTFRRL 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 353739663 238 LKPEIQIVGTGGVLTGRDAFEHILCGASMVQVGTTLQKEGVAAFGRITAELQAIM 292
Cdd:cd04741  240 LPSEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEKELEDIW 294
DHO_dh pfam01180
Dihydroorotate dehydrogenase;
5-292 6.49e-101

Dihydroorotate dehydrogenase;


Pssm-ID: 426103  Cd Length: 291  Bit Score: 297.72  E-value: 6.49e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663    5 ATTLGGFTFDNCLMNAAGVWCMTKEELDAVKNSKAGTFVTKTATLDYRAGNPEPRYQNVPLGSINSMGLPNQGLAYYLDY 84
Cdd:pfam01180   3 ATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVTPYPQPGNPTPRVFRLPEGVLNRMGLNNPGLDAVLAE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663   85 LLELQETEPE---RIFvLSLVGMSPDETHEILKTVEasDFKGLIELNLSCPNVPGKPQIAYDFETTETILQEVFTYFTKP 161
Cdd:pfam01180  83 LLKRRKEYPRpdlGIN-LSKAGMTVDDYVEVARKIG--PFADYIELNVSCPNTPGLRALQTDPELAAILLKVVKEVSKVP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663  162 LGIKLPP-YFDIVHFDQVAAIFNQFPLKFVNCVNSIGNGLYIKDESVVIKPKNGFGGIGGEYIKPTALANVHAFYQRLKP 240
Cdd:pfam01180 160 VLVKLAPdLTDIVIIDIADVALGEDGLDGINATNTTVRGMRIDLKTEKPILANGTGGLSGPPIKPIALKVIRELYQRTGP 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 353739663  241 EIQIVGTGGVLTGRDAFEHILCGASMVQVGTTLQKEGVAAFGRITAELQAIM 292
Cdd:pfam01180 240 EIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 5-301 2.89e-91

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: 273.49  E-value: 2.89e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663   5 ATTLGGFTFDNCLMNAAGVWCMTKEELDAVKNSKAGTFVTKTATLDYRAGNPEPRYQNVPL--GSINSMGLPNQGLAYYL 82
Cdd:COG0167    3 SVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEdsGLINRMGLNNPGVDAFL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663  83 DYLLELQEtePERIFVLSLVGMSPDETHEILKTVEASDFKGlIELNLSCPNVPGK-PQIAYDFETTETILQEVFTYFTKP 161
Cdd:COG0167   83 ERLLPAKR--YDVPVIVNIGGNTVEDYVELARRLADAGADY-LELNISCPNTPGGgRALGQDPEALAELLAAVKAATDKP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 162 LGIKLPPyfDIVHFDQVAAIFNQFPLKFVNCVNSIgNGLYIKDESVVIKPKNGFGGIGGEYIKPTALANVHAFYQRLKPE 241
Cdd:COG0167  160 VLVKLAP--DLTDIVEIARAAEEAGADGVIAINTT-LGRAIDLETRRPVLANEAGGLSGPALKPIALRMVREVAQAVGGD 236

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 242 IQIVGTGGVLTGRDAFEHILCGASMVQVGTTLQKEGVAAFGRITAELQAIMAEKGYETIE 301
Cdd:COG0167  237 IPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSIS 296
pyrD_sub1_fam TIGR01037
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ...
 6-305 2.38e-50

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: 168.76  E-value: 2.38e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663    6 TTLGGFTFDNCLMNAAGVWCMTKEELDAVKNSKAGTFVTKTATLDYRAGNPEPRYQNVPLGSINSMGLPNQGLAYYLDYL 85
Cdd:TIGR01037   3 VELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTIVETPCGMLNAIGLQNPGVEAFLEEL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663   86 LELQETEPeRIFVLSLVGMSPDETHEILKTVEASD-FKGLIELNLSCPNVPG-KPQIAYDFETTETILQEVFTYFTKPLG 163
Cdd:TIGR01037  83 KPVREEFP-TPLIASVYGSSVEEFAEVAEKLEKAPpYVDAYELNLSCPHVKGgGIAIGQDPELSADVVKAVKDKTDVPVF 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663  164 IKLPPYF-DIVHFDQVAAIFNQFPLKFVNCVNSIGNGLYIKdesvviKP--KNGFGGIGGEYIKPTALANVHAFYQRLkp 240
Cdd:TIGR01037 162 AKLSPNVtDITEIAKAAEEAGADGLTLINTLRGMKIDIKTG------KPilANKTGGLSGPAIKPIALRMVYDVYKMV-- 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 353739663  241 EIQIVGTGGVLTGRDAFEHILCGASMVQVGTTLQKEGVaAFGRITAELQAIMAEKGYETIEDFRG 305
Cdd:TIGR01037 234 DIPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYRGF-AFKKIIEGLIAFLKAEGFTSIEELIG 297
 
Name Accession Description Interval E-value
PRK02506 PRK02506
dihydroorotate dehydrogenase 1A; Reviewed
 3-310 0e+00

dihydroorotate dehydrogenase 1A; Reviewed


Pssm-ID: 235045  Cd Length: 310  Bit Score: 637.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663   3 STATTLGGFTFDNCLMNAAGVWCMTKEELDAVKNSKAGTFVTKTATLDYRAGNPEPRYQNVPLGSINSMGLPNQGLAYYL 82
Cdd:PRK02506   1 STSTQIAGFKFDNCLMNAAGVYCMTKEELEEVEASAAGAFVTKSATLEPRPGNPEPRYADTPLGSINSMGLPNLGFDYYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663  83 DYLLELQETEPERIFVLSLVGMSPDETHEILKTVEASDFKGLIELNLSCPNVPGKPQIAYDFETTETILQEVFTYFTKPL 162
Cdd:PRK02506  81 DYVLELQKKGPNKPHFLSVVGLSPEETHTILKKIQASDFNGLVELNLSCPNVPGKPQIAYDFETTEQILEEVFTYFTKPL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 163 GIKLPPYFDIVHFDQVAAIFNQFPLKFVNCVNSIGNGLYI--KDESVVIKPKNGFGGIGGEYIKPTALANVHAFYQRLKP 240
Cdd:PRK02506 161 GVKLPPYFDIVHFDQAAAIFNKFPLAFVNCINSIGNGLVIdpEDETVVIKPKNGFGGIGGDYIKPTALANVRAFYQRLNP 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 241 EIQIVGTGGVLTGRDAFEHILCGASMVQVGTTLQKEGVAAFGRITAELQAIMAEKGYETIEDFRGKLQHL 310
Cdd:PRK02506 241 SIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAIMAEKGYQSLEDFRGKLKYL 310
DHOD_1A_like cd04741
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ...
 6-292 2.32e-146

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: 413.26  E-value: 2.32e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663   6 TTLGGFTFDNCLMNAAGVWCMTKEELDAVKNSKAGTFVTKTATLDYRAGNPEPRYQNVPLGSINSMGLPNQGLAYYLDYL 85
Cdd:cd04741    1 VTPPGLTISPPLMNAAGPWCTTLEDLLELAASSTGAVTTRSSTLAGRPGNPEPRYYAFPLGSINSLGLPNLGLDYYLEYI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663  86 LELQETEPER--IFVLSLVGMsPDETHEILKTVEASD--FKGLIELNLSCPNVPGKPQIAYDFETTETILQEVFTYFTKP 161
Cdd:cd04741   81 RTISDGLPGSakPFFISVTGS-AEDIAAMYKKIAAHQkqFPLAMELNLSCPNVPGKPPPAYDFDATLEYLTAVKAAYSIP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 162 LGIKLPPYFDIVHFDQVAAIFNQF--PLKFVNCVNSIGNGLYIKD--ESVVIKPKNGFGGIGGEYIKPTALANVHAFYQR 237
Cdd:cd04741  160 VGVKTPPYTDPAQFDTLAEALNAFacPISFITATNTLGNGLVLDPerETVVLKPKTGFGGLAGAYLHPLALGNVRTFRRL 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 353739663 238 LKPEIQIVGTGGVLTGRDAFEHILCGASMVQVGTTLQKEGVAAFGRITAELQAIM 292
Cdd:cd04741  240 LPSEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEKELEDIW 294
DHO_dh pfam01180
Dihydroorotate dehydrogenase;
5-292 6.49e-101

Dihydroorotate dehydrogenase;


Pssm-ID: 426103  Cd Length: 291  Bit Score: 297.72  E-value: 6.49e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663    5 ATTLGGFTFDNCLMNAAGVWCMTKEELDAVKNSKAGTFVTKTATLDYRAGNPEPRYQNVPLGSINSMGLPNQGLAYYLDY 84
Cdd:pfam01180   3 ATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVTPYPQPGNPTPRVFRLPEGVLNRMGLNNPGLDAVLAE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663   85 LLELQETEPE---RIFvLSLVGMSPDETHEILKTVEasDFKGLIELNLSCPNVPGKPQIAYDFETTETILQEVFTYFTKP 161
Cdd:pfam01180  83 LLKRRKEYPRpdlGIN-LSKAGMTVDDYVEVARKIG--PFADYIELNVSCPNTPGLRALQTDPELAAILLKVVKEVSKVP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663  162 LGIKLPP-YFDIVHFDQVAAIFNQFPLKFVNCVNSIGNGLYIKDESVVIKPKNGFGGIGGEYIKPTALANVHAFYQRLKP 240
Cdd:pfam01180 160 VLVKLAPdLTDIVIIDIADVALGEDGLDGINATNTTVRGMRIDLKTEKPILANGTGGLSGPPIKPIALKVIRELYQRTGP 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 353739663  241 EIQIVGTGGVLTGRDAFEHILCGASMVQVGTTLQKEGVAAFGRITAELQAIM 292
Cdd:pfam01180 240 EIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 5-301 2.89e-91

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: 273.49  E-value: 2.89e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663   5 ATTLGGFTFDNCLMNAAGVWCMTKEELDAVKNSKAGTFVTKTATLDYRAGNPEPRYQNVPL--GSINSMGLPNQGLAYYL 82
Cdd:COG0167    3 SVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEdsGLINRMGLNNPGVDAFL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663  83 DYLLELQEtePERIFVLSLVGMSPDETHEILKTVEASDFKGlIELNLSCPNVPGK-PQIAYDFETTETILQEVFTYFTKP 161
Cdd:COG0167   83 ERLLPAKR--YDVPVIVNIGGNTVEDYVELARRLADAGADY-LELNISCPNTPGGgRALGQDPEALAELLAAVKAATDKP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 162 LGIKLPPyfDIVHFDQVAAIFNQFPLKFVNCVNSIgNGLYIKDESVVIKPKNGFGGIGGEYIKPTALANVHAFYQRLKPE 241
Cdd:COG0167  160 VLVKLAP--DLTDIVEIARAAEEAGADGVIAINTT-LGRAIDLETRRPVLANEAGGLSGPALKPIALRMVREVAQAVGGD 236

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 242 IQIVGTGGVLTGRDAFEHILCGASMVQVGTTLQKEGVAAFGRITAELQAIMAEKGYETIE 301
Cdd:COG0167  237 IPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSIS 296
DHOD_DHPD_FMN cd02810
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ...
 6-287 3.21e-90

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: 270.76  E-value: 3.21e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663   6 TTLGGFTFDNCLMNAAGVWCMTKEELDAVKNSKAGTFVTKTATLDYRAGNPEPRY---------QNVPLGSINSMGLPNQ 76
Cdd:cd02810    1 VNFLGLKLKNPFGVAAGPLLKTGELIARAAAAGFGAVVYKTVTLHPRPGNPLPRVarlppegesYPEQLGILNSFGLPNL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663  77 GLAYYLDYLLELQETEPERIFVLSLVGMSPDETHEILKTVEASdFKGLIELNLSCPNVPGKPQIAYDFETTETILQEVFT 156
Cdd:cd02810   81 GLDVWLQDIAKAKKEFPGQPLIASVGGSSKEDYVELARKIERA-GAKALELNLSCPNVGGGRQLGQDPEAVANLLKAVKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 157 YFTKPLGIKLPPYFDIVHFDQVAAIFNQFPLKFVNCVNSIGNGLYIKDEsVVIKPKNGFGGIGGEYIKPTALANVHAFYQ 236
Cdd:cd02810  160 AVDIPLLVKLSPYFDLEDIVELAKAAERAGADGLTAINTISGRVVDLKT-VGPGPKRGTGGLSGAPIRPLALRWVARLAA 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 353739663 237 RLKPEIQIVGTGGVLTGRDAFEHILCGASMVQVGTTLQKEGVAAFGRITAE 287
Cdd:cd02810  239 RLQLDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKIKKE 289
DHOD_1B_like cd04740
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ...
 5-307 5.53e-57

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: 185.83  E-value: 5.53e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663   5 ATTLGGFTFDNCLMNAAGVWCMTKEELDAVKNSKAGTFVTKTATLDYRAGNPEPRYQNVPLGSINSMGLPNQGLAYYLDY 84
Cdd:cd04740    1 SVELAGLRLKNPVILASGTFGFGEELSRVADLGKLGAIVTKSITLEPREGNPPPRVVETPGGMLNAIGLQNPGVEAFLEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663  85 LLELQETEPERIFVlSLVGMSPDETHEILKTVEASDFKGlIELNLSCPNVP-GKPQIAYDFETTETILQEVFTYFTKPLG 163
Cdd:cd04740   81 LLPWLREFGTPVIA-SIAGSTVEEFVEVAEKLADAGADA-IELNISCPNVKgGGMAFGTDPEAVAEIVKAVKKATDVPVI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 164 IKLPPYF-DIVHFDQVA------AIfnqfplkfvNCVNSIGnGLYIKDESVviKP--KNGFGGIGGEYIKPTALANVHAF 234
Cdd:cd04740  159 VKLTPNVtDIVEIARAAeeagadGL---------TLINTLK-GMAIDIETR--KPilGNVTGGLSGPAIKPIALRMVYQV 226

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 353739663 235 YQRLkpEIQIVGTGGVLTGRDAFEHILCGASMVQVGTTLqKEGVAAFGRITAELQAIMAEKGYETIEDFRGKL 307
Cdd:cd04740  227 YKAV--EIPIIGVGGIASGEDALEFLMAGASAVQVGTAN-FVDPEAFKEIIEGLEAYLDEEGIKSIEELVGLA 296
PRK07259 PRK07259
dihydroorotate dehydrogenase;
4-308 8.30e-53

dihydroorotate dehydrogenase;


Pssm-ID: 235982  Cd Length: 301  Bit Score: 174.95  E-value: 8.30e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663   4 TATTLGGFTFDNCLMNAAGVWCMTKEELDAVKNSKAGTFVTKTATLDYRAGNPEPRYQNVPLGSINSMGLPNQGLAYYLD 83
Cdd:PRK07259   2 LSVELPGLKLKNPVMPASGTFGFGGEYARFYDLNGLGAIVTKSTTLEPREGNPTPRIAETPGGMLNAIGLQNPGVDAFIE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663  84 YLLELQETEPERIFVlSLVGMSPDETHEILKTVEASDFKGLIELNLSCPNVP-GKPQIAYDFETTETILQEVFTYFTKPL 162
Cdd:PRK07259  82 EELPWLEEFDTPIIA-NVAGSTEEEYAEVAEKLSKAPNVDAIELNISCPNVKhGGMAFGTDPELAYEVVKAVKEVVKVPV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 163 GIKLPPYF-DIVHF---------DQVAAIfNQFPlkfvncvnsignGLYIKDESVviKP--KNGFGGIGGEYIKPTALAN 230
Cdd:PRK07259 161 IVKLTPNVtDIVEIakaaeeagaDGLSLI-NTLK------------GMAIDIKTR--KPilANVTGGLSGPAIKPIALRM 225

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 353739663 231 VHAFYQRLKpeIQIVGTGGVLTGRDAFEHILCGASMVQVGTTLQKeGVAAFGRITAELQAIMAEKGYETIEDFRGKLQ 308
Cdd:PRK07259 226 VYQVYQAVD--IPIIGMGGISSAEDAIEFIMAGASAVQVGTANFY-DPYAFPKIIEGLEAYLDKYGIKSIEEIVGIAH 300
pyrD_sub1_fam TIGR01037
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ...
 6-305 2.38e-50

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: 168.76  E-value: 2.38e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663    6 TTLGGFTFDNCLMNAAGVWCMTKEELDAVKNSKAGTFVTKTATLDYRAGNPEPRYQNVPLGSINSMGLPNQGLAYYLDYL 85
Cdd:TIGR01037   3 VELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTIVETPCGMLNAIGLQNPGVEAFLEEL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663   86 LELQETEPeRIFVLSLVGMSPDETHEILKTVEASD-FKGLIELNLSCPNVPG-KPQIAYDFETTETILQEVFTYFTKPLG 163
Cdd:TIGR01037  83 KPVREEFP-TPLIASVYGSSVEEFAEVAEKLEKAPpYVDAYELNLSCPHVKGgGIAIGQDPELSADVVKAVKDKTDVPVF 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663  164 IKLPPYF-DIVHFDQVAAIFNQFPLKFVNCVNSIGNGLYIKdesvviKP--KNGFGGIGGEYIKPTALANVHAFYQRLkp 240
Cdd:TIGR01037 162 AKLSPNVtDITEIAKAAEEAGADGLTLINTLRGMKIDIKTG------KPilANKTGGLSGPAIKPIALRMVYDVYKMV-- 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 353739663  241 EIQIVGTGGVLTGRDAFEHILCGASMVQVGTTLQKEGVaAFGRITAELQAIMAEKGYETIEDFRG 305
Cdd:TIGR01037 234 DIPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYRGF-AFKKIIEGLIAFLKAEGFTSIEELIG 297
DHPD_FMN cd02940
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ...
 40-288 5.95e-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: 5.95e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663  40 GTFVTKTATLDYR-AGNPEPRYQNVPLGSINSMGLPN------QGLAYYLDYLLELQETEPERIFVLSLVGM-SPDETHE 111
Cdd:cd02940   38 GGAVTKTLGLDKDiVTNVSPRIARLRTSGRGQIGFNNieliseKPLEYWLKEIRELKKDFPDKILIASIMCEyNKEDWTE 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 112 ILKTVEASDFKGlIELNLSCPNvpGKPQ------IAYDFETTETILQEVFTYFTKPLGIKLPP-YFDIVHF--------- 175
Cdd:cd02940  118 LAKLVEEAGADA-LELNFSCPH--GMPErgmgaaVGQDPELVEEICRWVREAVKIPVIAKLTPnITDIREIaraakegga 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 176 DQVAAIfnqfplkfvNCVNSIgNGLYIKDES--VVIKPKNGFGGIGGEYIKPTALANVHAFYQRLKPEIQIVGTGGVLTG 253
Cdd:cd02940  195 DGVSAI---------NTVNSL-MGVDLDGTPpaPGVEGKTTYGGYSGPAVKPIALRAVSQIARAPEPGLPISGIGGIESW 264

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 353739663 254 RDAFEHILCGASMVQVGTTLQKEGVAAFGRITAEL 288
Cdd:cd02940  265 EDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
PRK08318 PRK08318
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
58-306 8.64e-22

NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;


Pssm-ID: 236237 [Multi-domain]  Cd Length: 420  Bit Score: 94.63  E-value: 8.64e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663  58 PRYQNVPLGSINSMGLPN------QGLAYYLDYLLELQETEPERIFVLSL-VGMSPDETHEILKTVEASDFKGlIELNLS 130
Cdd:PRK08318  57 PRFGALVKEDRRFIGFNNielitdRPLEVNLREIRRVKRDYPDRALIASImVECNEEEWKEIAPLVEETGADG-IELNFG 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 131 CP-------------NVPgkpqiaydfETTETILQEVFTYFTKPLGIKLPPYF-DIVH---------FDQVAAIfnqfpl 187
Cdd:PRK08318 136 CPhgmsergmgsavgQVP---------ELVEMYTRWVKRGSRLPVIVKLTPNItDIREparaakrggADAVSLI------ 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 188 kfvNCVNSIGNglyIKDESVVIKP----KNGFGGIGGEYIKPTALANVHAFYQRLK-PEIQIVGTGGVLTGRDAFEHILC 262
Cdd:PRK08318 201 ---NTINSITG---VDLDRMIPMPivngKSSHGGYCGPAVKPIALNMVAEIARDPEtRGLPISGIGGIETWRDAAEFILL 274

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 353739663 263 GASMVQVGTTLQKEGVAAFGRITAELQAIMAEKGYETIEDFRGK 306
Cdd:PRK08318 275 GAGTVQVCTAAMQYGFRIVEDMISGLSHYMDEKGFASLEDMVGL 318
PLN02495 PLN02495
oxidoreductase, acting on the CH-CH group of donors
 40-306 8.28e-21

oxidoreductase, acting on the CH-CH group of donors


Pssm-ID: 215273 [Multi-domain]  Cd Length: 385  Bit Score: 91.44  E-value: 8.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663  40 GTFVTKTATLDY-RAGNPEPRYQNVPLGSINSMG-----------LPNQGLAYYLDYLLELQETEPERIFVLSLVG-MSP 106
Cdd:PLN02495  47 GGVIAKTVSLDAsKVINVTPRYARLRAGANGSAKgrvigwqnielISDRPFETMLAEFKQLKEEYPDRILIASIMEeYNK 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 107 DETHEILKTVEASDFKGLiELNLSCPNvpGKPQ------IAYDFETTETILQEVFTYFTKPLGIKLPPyfDIVHFDQVAA 180
Cdd:PLN02495 127 DAWEEIIERVEETGVDAL-EINFSCPH--GMPErkmgaaVGQDCDLLEEVCGWINAKATVPVWAKMTP--NITDITQPAR 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 181 IFNQFPLKFVNCVNSIGNGLYIKDESVVIKPK-NGFGGIGG---EYIKPTALANVHAFYQRLKPE----IQIVGTGGVLT 252
Cdd:PLN02495 202 VALKSGCEGVAAINTIMSVMGINLDTLRPEPCvEGYSTPGGyssKAVRPIALAKVMAIAKMMKSEfpedRSLSGIGGVET 281

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 353739663 253 GRDAFEHILCGASMVQVGTTLQKEGVAAFGRITAELQAIMAEKGYETIEDFRGK 306
Cdd:PLN02495 282 GGDAAEFILLGADTVQVCTGVMMHGYPLVKNLCAELQDFMKKHNFSSIEDFRGA 335
DHOD_2_like cd04738
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ...
 5-288 3.55e-17

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: 80.62  E-value: 3.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663   5 ATTLGGFTFDNCLMNAAGvwcmtkeeLDavKN-------SKAG-TFVT-KTATLDYRAGNPEPR------YQNVplgsIN 69
Cdd:cd04738   40 EVEVFGLTFPNPVGLAAG--------FD--KNaeaidalLALGfGFVEvGTVTPRPQPGNPKPRlfrlpeDEAL----IN 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663  70 SMGLPNQGLAYYLDYLLELQeteperiFVLSLVGM-------SPDETheilktvEASDF-KGL---------IELNLSCP 132
Cdd:cd04738  106 RMGFNNDGADAVAKRLKKRR-------PRGGPLGVnigknkdTPLED-------AVEDYvIGVrklgpyadyLVVNVSSP 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 133 NVPGKPQIAYDfETTETILQEVFTYFT-----KPLGIKLPPyfDIVHfDQVAAIfnqfplkfVNCVNSIG-NGLYI---- 202
Cdd:cd04738  172 NTPGLRDLQGK-EALRELLTAVKEERNklgkkVPLLVKIAP--DLSD-EELEDI--------ADVALEHGvDGIIAtntt 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 203 --KDESVVIKPKNGFGGIGGEYIKPTALANVHAFYQRLKPEIQIVGTGGVLTGRDAFEHILCGASMVQVGTTLQKEGVAA 280
Cdd:cd04738  240 isRPGLLRSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTGLVYEGPGL 319


                 ....*...
gi 353739663 281 FGRITAEL 288
Cdd:cd04738  320 VKRIKREL 327
PLN02826 PLN02826
dihydroorotate dehydrogenase
 127-302 2.34e-15

dihydroorotate dehydrogenase


Pssm-ID: 178421  Cd Length: 409  Bit Score: 75.93  E-value: 2.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 127 LNLSCPNVPG------KPQIAYDFETTETILQEVFTYFTK--PLGIKLPPYFDIVHFDQVAAIFNQFPLKFVncvnSIGN 198
Cdd:PLN02826 222 INVSSPNTPGlrklqgRKQLKDLLKKVLAARDEMQWGEEGppPLLVKIAPDLSKEDLEDIAAVALALGIDGL----IISN 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 199 GLYIKDESVVIKPKNG-FGGIGGEYIKPTALANVHAFYQRLKPEIQIVGTGGVLTGRDAFEHILCGASMVQVGTTLQKEG 277
Cdd:PLN02826 298 TTISRPDSVLGHPHADeAGGLSGKPLFDLSTEVLREMYRLTRGKIPLVGCGGVSSGEDAYKKIRAGASLVQLYTAFAYEG 377

                        170       180
                 ....*....|....*....|....*
gi 353739663 278 VAAFGRITAELQAIMAEKGYETIED 302
Cdd:PLN02826 378 PALIPRIKAELAACLERDGFKSIQE 402
PRK05286 PRK05286
quinone-dependent dihydroorotate dehydrogenase;
5-296 3.08e-15

quinone-dependent dihydroorotate dehydrogenase;


Pssm-ID: 235388  Cd Length: 344  Bit Score: 75.20  E-value: 3.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663   5 ATTLGGFTFDNCLMNAAGvwcmtkeeLDavKNSKA---------GtFVT-KTATLDYRAGNPEPR------YQNVplgsI 68
Cdd:PRK05286  50 PVTVMGLTFPNPVGLAAG--------FD--KNGEAidalgalgfG-FVEvGTVTPRPQPGNPKPRlfrlpeDEAL----I 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663  69 NSMGLPNQGLayylDYLLE-LQETEPERIFVLSLvGMSPDETHE-----ILKTVEA----SDFkglIELNLSCPNVPG-- 136
Cdd:PRK05286 115 NRMGFNNDGA----DALAErLKKAYRGIPLGINI-GKNKDTPLEdavddYLICLEKlypyADY---FTVNISSPNTPGlr 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 137 ----KPQIAYDFETTETILQEVFTYftKPLGIKLPPYFDIVHFDQVAAIFNQFPLKFVNCVN-SIGnglyiKDESVVIKP 211
Cdd:PRK05286 187 dlqyGEALDELLAALKEAQAELHGY--VPLLVKIAPDLSDEELDDIADLALEHGIDGVIATNtTLS-----RDGLKGLPN 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 212 KNGFGGIGGEYIKPTALANVHAFYQRLKPEIQIVGTGGVLTGRDAFEHILCGASMVQVGTTLQKEGVAAFGRITAELQAI 291
Cdd:PRK05286 260 ADEAGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGASLVQIYSGLIYEGPGLVKEIVRGLARL 339


                 ....*
gi 353739663 292 MAEKG 296
Cdd:PRK05286 340 LRRDG 344
DHOD_like cd04739
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ...
 125-307 1.62e-12

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: 66.87  E-value: 1.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 125 IELNLScpNVPGKPQIAY-DFETTET-ILQEVFTYFTKPLGIKLPPYFD-----IVHFDQVAA----IFNQFPLKFVNcv 193
Cdd:cd04739  129 LELNIY--ALPTDPDISGaEVEQRYLdILRAVKSAVTIPVAVKLSPFFSalahmAKQLDAAGAdglvLFNRFYQPDID-- 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 194 nsIGNgLYIKDESVVIKPkngfggigGEYIKP-TALANVHAfyqrlKPEIQIVGTGGVLTGRDAFEHILCGASMVQVGTT 272
Cdd:cd04739  205 --LET-LEVVPNLLLSSP--------AEIRLPlRWIAILSG-----RVKASLAASGGVHDAEDVVKYLLAGADVVMTTSA 268

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 353739663 273 LQKEGVAAFGRITAELQAIMAEKGYETIEDFRGKL 307
Cdd:cd04739  269 LLRHGPDYIGTLLAGLEAWMEEHGYESVQQLRGSM 303
PRK07565 PRK07565
dihydroorotate dehydrogenase-like protein;
125-307 7.75e-11

dihydroorotate dehydrogenase-like protein;


Pssm-ID: 236051  Cd Length: 334  Bit Score: 62.19  E-value: 7.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 125 IELNLScpNVPGKPQIAY-DFETTET-ILQEVFTYFTKPLGIKLPPYFD-----IVHFDQVAA----IFNQFplkfvncv 193
Cdd:PRK07565 131 LELNIY--YLPTDPDISGaEVEQRYLdILRAVKSAVSIPVAVKLSPYFSnlanmAKRLDAAGAdglvLFNRF-------- 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 194 nsignglYIKD---ESVVIKPKNGFGGIGGEYIKPTALANVHAfyqRLKpeIQIVGTGGVLTGRDAFEHILCGASMVQVG 270
Cdd:PRK07565 201 -------YQPDidlETLEVVPGLVLSTPAELRLPLRWIAILSG---RVG--ADLAATTGVHDAEDVIKMLLAGADVVMIA 268

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 353739663 271 TTLQKEGVAAFGRITAELQAIMAEKGYETIEDFRGKL 307
Cdd:PRK07565 269 SALLRHGPDYIGTILRGLEDWMERHGYESLQQFRGSM 305
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 76-271 7.89e-08

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: 51.82  E-value: 7.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663  76 QGLAYYLDYLLELQETEPERIFVLSLVGMSPDETHEILKTVEASDFKGLIELNLSCPnvpgkpqiaYDFETTETILQEVF 155
Cdd:cd04722   39 EEAETDDKEVLKEVAAETDLPLGVQLAINDAAAAVDIAAAAARAAGADGVEIHGAVG---------YLAREDLELIRELR 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 156 T-YFTKPLGIKLPPYFDIVHFDQVAAifnqfPLKFVNCVNSIGNGlyikdesvvikpknGFGGIGGEYIKPTALAnvhaf 234
Cdd:cd04722  110 EaVPDVKVVVKLSPTGELAAAAAEEA-----GVDEVGLGNGGGGG--------------GGRDAVPIADLLLILA----- 165

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 353739663 235 yqRLKPEIQIVGTGGVLTGRDAFEHILCGASMVQVGT 271
Cdd:cd04722  166 --KRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
IDI-2_FMN cd02811
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ...
 225-304 5.98e-04

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: 40.94  E-value: 5.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353739663 225 PTALANVHAfyQRLKPEIQIVGTGGVLTGRDAFEHILCGASMVQV-GTTLQ-----KEGV-AAFGRITAELQAIMAEKGY 297
Cdd:cd02811  241 PTAASLLEV--RSALPDLPLIASGGIRNGLDIAKALALGADLVGMaGPFLKaalegEEAViETIEQIIEELRTAMFLTGA 318


                 ....*..
gi 353739663 298 ETIEDFR 304
Cdd:cd02811  319 KNLAELK 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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