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Conserved domains on  [gi|589910890|pdb|3W7M|B]
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Chain B, Dihydroorotate dehydrogenase (fumarate)

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
 3-312 0e+00

dihydroorotate dehydrogenase 1A; Reviewed


:

Pssm-ID: 235045  Cd Length: 310  Bit Score: 501.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B         3 LKLNLLDHVFANPFMNAAGVLCSTEEDLRCMTASSSGALVSKSCTSAPRDGNPEPRYMAFPLGSINSMGLPNLGFDFYLK 82
Cdd:PRK02506   2 TSTQIAGFKFDNCLMNAAGVYCMTKEELEEVEASAAGAFVTKSATLEPRPGNPEPRYADTPLGSINSMGLPNLGFDYYLD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B        83 YASDLH-DYSKKPLFLSISGLSVEENVAMVRRLApvAQEKGVLLELNLSCPNVPGKPQVAYDFEAMRTYLQQVSLAYGLP 161
Cdd:PRK02506  82 YVLELQkKGPNKPHFLSVVGLSPEETHTILKKIQ--ASDFNGLVELNLSCPNVPGKPQIAYDFETTEQILEEVFTYFTKP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B       162 FGVKMPPYFDIAHFDTAAAVLNEFPLvKFVTCVNSVGNGLVIDAESESVVIKPKQGFGGLGGKYILPTALANVNAFYRR- 240
Cdd:PRK02506 160 LGVKLPPYFDIVHFDQAAAIFNKFPL-AFVNCINSIGNGLVIDPEDETVVIKPKNGFGGIGGDYIKPTALANVRAFYQRl 238

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
3W7M_B       241 CPDKLVFGCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDELLEIMARKGYRTLEEFRGRVKTI 312
Cdd:PRK02506 239 NPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAIMAEKGYQSLEDFRGKLKYL 310
 
Name Accession Description Interval E-value
PRK02506 PRK02506
dihydroorotate dehydrogenase 1A; Reviewed
 3-312 0e+00

dihydroorotate dehydrogenase 1A; Reviewed


Pssm-ID: 235045  Cd Length: 310  Bit Score: 501.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B         3 LKLNLLDHVFANPFMNAAGVLCSTEEDLRCMTASSSGALVSKSCTSAPRDGNPEPRYMAFPLGSINSMGLPNLGFDFYLK 82
Cdd:PRK02506   2 TSTQIAGFKFDNCLMNAAGVYCMTKEELEEVEASAAGAFVTKSATLEPRPGNPEPRYADTPLGSINSMGLPNLGFDYYLD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B        83 YASDLH-DYSKKPLFLSISGLSVEENVAMVRRLApvAQEKGVLLELNLSCPNVPGKPQVAYDFEAMRTYLQQVSLAYGLP 161
Cdd:PRK02506  82 YVLELQkKGPNKPHFLSVVGLSPEETHTILKKIQ--ASDFNGLVELNLSCPNVPGKPQIAYDFETTEQILEEVFTYFTKP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B       162 FGVKMPPYFDIAHFDTAAAVLNEFPLvKFVTCVNSVGNGLVIDAESESVVIKPKQGFGGLGGKYILPTALANVNAFYRR- 240
Cdd:PRK02506 160 LGVKLPPYFDIVHFDQAAAIFNKFPL-AFVNCINSIGNGLVIDPEDETVVIKPKNGFGGIGGDYIKPTALANVRAFYQRl 238

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
3W7M_B       241 CPDKLVFGCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDELLEIMARKGYRTLEEFRGRVKTI 312
Cdd:PRK02506 239 NPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAIMAEKGYQSLEDFRGKLKYL 310
DHOD_1A_like cd04741
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ...
 6-294 2.45e-160

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: 448.70  E-value: 2.45e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B        6 NLLDHVFANPFMNAAGVLCSTEEDLRCMTASSSGALVSKSCTSAPRDGNPEPRYMAFPLGSINSMGLPNLGFDFYLKYAS 85
Cdd:cd04741   2 TPPGLTISPPLMNAAGPWCTTLEDLLELAASSTGAVTTRSSTLAGRPGNPEPRYYAFPLGSINSLGLPNLGLDYYLEYIR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B       86 DLHDY---SKKPLFLSISGlSVEENVAMVRRLAPVAQEKGVLLELNLSCPNVPGKPQVAYDFEAMRTYLQQVSLAYGLPF 162
Cdd:cd04741  82 TISDGlpgSAKPFFISVTG-SAEDIAAMYKKIAAHQKQFPLAMELNLSCPNVPGKPPPAYDFDATLEYLTAVKAAYSIPV 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B      163 GVKMPPYFDIAHFDTAAAVLNEFP-LVKFVTCVNSVGNGLVIDAESESVVIKPKQGFGGLGGKYILPTALANVNAFYRRC 241
Cdd:cd04741 161 GVKTPPYTDPAQFDTLAEALNAFAcPISFITATNTLGNGLVLDPERETVVLKPKTGFGGLAGAYLHPLALGNVRTFRRLL 240

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
3W7M_B      242 P-DKLVFGCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDELLEIM 294
Cdd:cd04741 241 PsEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEKELEDIW 294
DHO_dh pfam01180
Dihydroorotate dehydrogenase;
3-294 2.79e-93

Dihydroorotate dehydrogenase;


Pssm-ID: 426103  Cd Length: 291  Bit Score: 278.46  E-value: 2.79e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B          3 LKLNLLDHVFANPFMNAAGVLCSTEEDLRCMTASSSGALVSKSCTSAPRDGNPEPRYMAFPLGSINSMGLPNLGFDFYLK 82
Cdd:pfam01180   2 LATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVTPYPQPGNPTPRVFRLPEGVLNRMGLNNPGLDAVLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B         83 YASDLHDYSKK---PLFLSISGLSVEENVAMVRRLAPVAQekgvLLELNLSCPNVPGKPQVAYDFEAMRTYLQQVSLAYG 159
Cdd:pfam01180  82 ELLKRRKEYPRpdlGINLSKAGMTVDDYVEVARKIGPFAD----YIELNVSCPNTPGLRALQTDPELAAILLKVVKEVSK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B        160 LPFGVKMPP-YFDIAHFDTAAAVLNEFPLVkFVTCVNSVGNGLVIDAESESVVIKPkqGFGGLGGKYILPTALANVNAFY 238
Cdd:pfam01180 158 VPVLVKLAPdLTDIVIIDIADVALGEDGLD-GINATNTTVRGMRIDLKTEKPILAN--GTGGLSGPPIKPIALKVIRELY 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
3W7M_B        239 RRCPDKL-VFGCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDELLEIM 294
Cdd:pfam01180 235 QRTGPEIpIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 3-303 6.65e-86

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: 259.62  E-value: 6.65e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B        3 LKLNLLDHVFANPFMNAAGVLCSTEEDLRCMTASSSGALVSKSCTSAPRDGNPEPRY--MAFPLGSINSMGLPNLGFDFY 80
Cdd:COG0167   2 LSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLfrLPEDSGLINRMGLNNPGVDAF 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B       81 LKYASDLHDYsKKPLFLSISGLSVEENVAMVRRLAPVaqekGV-LLELNLSCPNVPGK-PQVAYDFEAMRTYLQQVSLAY 158
Cdd:COG0167  82 LERLLPAKRY-DVPVIVNIGGNTVEDYVELARRLADA----GAdYLELNISCPNTPGGgRALGQDPEALAELLAAVKAAT 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B      159 GLPFGVKMPPyfDIAHFDTAAAVLNEFPLvKFVTCVNSVgNGLVIDAESESVVIKPkqGFGGLGGKYILPTALANVNAFY 238
Cdd:COG0167 157 DKPVLVKLAP--DLTDIVEIARAAEEAGA-DGVIAINTT-LGRAIDLETRRPVLAN--EAGGLSGPALKPIALRMVREVA 230

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
3W7M_B      239 RRCPDKL-VFGCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDELLEIMARKGYRTLE 303
Cdd:COG0167 231 QAVGGDIpIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSIS 296
pyrD_sub1_fam TIGR01037
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ...
 3-308 3.38e-44

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: 152.97  E-value: 3.38e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B          3 LKLNLLDHVFANPFMNAAGVLCSTEEDLRCMTASSSGALVSKSCTSAPRDGNPEPRYMAFPLGSINSMGLPNLGFDFYLK 82
Cdd:TIGR01037   1 LEVELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTIVETPCGMLNAIGLQNPGVEAFLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B         83 YASDLHDYSKKPLFLSISGLSVEENVAMVRRLAPvAQEKGVLLELNLSCPNVPG-------KPQVAYDFeamrtyLQQVS 155
Cdd:TIGR01037  81 ELKPVREEFPTPLIASVYGSSVEEFAEVAEKLEK-APPYVDAYELNLSCPHVKGggiaigqDPELSADV------VKAVK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B        156 LAYGLPFGVKMPPYF-DIAHFDTAAavlnEFPLVKFVTCVNSVGnGLVIDAESESVVIKPKqgFGGLGGKYILPTALANV 234
Cdd:TIGR01037 154 DKTDVPVFAKLSPNVtDITEIAKAA----EEAGADGLTLINTLR-GMKIDIKTGKPILANK--TGGLSGPAIKPIALRMV 226

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3W7M_B        235 NAFYRRCpDKLVFGCGGVYSGEDAFLHILAGASMVQVGTALQEEgPGIFTRLEDELLEIMARKGYRTLEEFRGR 308
Cdd:TIGR01037 227 YDVYKMV-DIPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYR-GFAFKKIIEGLIAFLKAEGFTSIEELIGI 298
 
Name Accession Description Interval E-value
PRK02506 PRK02506
dihydroorotate dehydrogenase 1A; Reviewed
 3-312 0e+00

dihydroorotate dehydrogenase 1A; Reviewed


Pssm-ID: 235045  Cd Length: 310  Bit Score: 501.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B         3 LKLNLLDHVFANPFMNAAGVLCSTEEDLRCMTASSSGALVSKSCTSAPRDGNPEPRYMAFPLGSINSMGLPNLGFDFYLK 82
Cdd:PRK02506   2 TSTQIAGFKFDNCLMNAAGVYCMTKEELEEVEASAAGAFVTKSATLEPRPGNPEPRYADTPLGSINSMGLPNLGFDYYLD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B        83 YASDLH-DYSKKPLFLSISGLSVEENVAMVRRLApvAQEKGVLLELNLSCPNVPGKPQVAYDFEAMRTYLQQVSLAYGLP 161
Cdd:PRK02506  82 YVLELQkKGPNKPHFLSVVGLSPEETHTILKKIQ--ASDFNGLVELNLSCPNVPGKPQIAYDFETTEQILEEVFTYFTKP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B       162 FGVKMPPYFDIAHFDTAAAVLNEFPLvKFVTCVNSVGNGLVIDAESESVVIKPKQGFGGLGGKYILPTALANVNAFYRR- 240
Cdd:PRK02506 160 LGVKLPPYFDIVHFDQAAAIFNKFPL-AFVNCINSIGNGLVIDPEDETVVIKPKNGFGGIGGDYIKPTALANVRAFYQRl 238

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
3W7M_B       241 CPDKLVFGCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDELLEIMARKGYRTLEEFRGRVKTI 312
Cdd:PRK02506 239 NPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAIMAEKGYQSLEDFRGKLKYL 310
DHOD_1A_like cd04741
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ...
 6-294 2.45e-160

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: 448.70  E-value: 2.45e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B        6 NLLDHVFANPFMNAAGVLCSTEEDLRCMTASSSGALVSKSCTSAPRDGNPEPRYMAFPLGSINSMGLPNLGFDFYLKYAS 85
Cdd:cd04741   2 TPPGLTISPPLMNAAGPWCTTLEDLLELAASSTGAVTTRSSTLAGRPGNPEPRYYAFPLGSINSLGLPNLGLDYYLEYIR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B       86 DLHDY---SKKPLFLSISGlSVEENVAMVRRLAPVAQEKGVLLELNLSCPNVPGKPQVAYDFEAMRTYLQQVSLAYGLPF 162
Cdd:cd04741  82 TISDGlpgSAKPFFISVTG-SAEDIAAMYKKIAAHQKQFPLAMELNLSCPNVPGKPPPAYDFDATLEYLTAVKAAYSIPV 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B      163 GVKMPPYFDIAHFDTAAAVLNEFP-LVKFVTCVNSVGNGLVIDAESESVVIKPKQGFGGLGGKYILPTALANVNAFYRRC 241
Cdd:cd04741 161 GVKTPPYTDPAQFDTLAEALNAFAcPISFITATNTLGNGLVLDPERETVVLKPKTGFGGLAGAYLHPLALGNVRTFRRLL 240

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
3W7M_B      242 P-DKLVFGCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDELLEIM 294
Cdd:cd04741 241 PsEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEKELEDIW 294
DHOD_DHPD_FMN cd02810
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ...
 6-289 1.45e-97

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: 289.25  E-value: 1.45e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B        6 NLLDHVFANPFMNAAGVLCSTEEDLRCMTASSSGALVSKSCTSAPRDGNPEPRYMAFP---------LGSINSMGLPNLG 76
Cdd:cd02810   2 NFLGLKLKNPFGVAAGPLLKTGELIARAAAAGFGAVVYKTVTLHPRPGNPLPRVARLPpegesypeqLGILNSFGLPNLG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B       77 FDFYLKYASDLHDY-SKKPLFLSISGLSVEENVAMVRRLAPVaqeKGVLLELNLSCPNVPGKPQVAYDFEAMRTYLQQVS 155
Cdd:cd02810  82 LDVWLQDIAKAKKEfPGQPLIASVGGSSKEDYVELARKIERA---GAKALELNLSCPNVGGGRQLGQDPEAVANLLKAVK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B      156 LAYGLPFGVKMPPYFDIAHFDTAAAVLNEFPlVKFVTCVNSVGNGLVIDAEsesVVIKPKQGFGGLGGKYILPTALANVN 235
Cdd:cd02810 159 AAVDIPLLVKLSPYFDLEDIVELAKAAERAG-ADGLTAINTISGRVVDLKT---VGPGPKRGTGGLSGAPIRPLALRWVA 234

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
3W7M_B      236 AFYRRCP-DKLVFGCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDE 289
Cdd:cd02810 235 RLAARLQlDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKIKKE 289
DHO_dh pfam01180
Dihydroorotate dehydrogenase;
3-294 2.79e-93

Dihydroorotate dehydrogenase;


Pssm-ID: 426103  Cd Length: 291  Bit Score: 278.46  E-value: 2.79e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B          3 LKLNLLDHVFANPFMNAAGVLCSTEEDLRCMTASSSGALVSKSCTSAPRDGNPEPRYMAFPLGSINSMGLPNLGFDFYLK 82
Cdd:pfam01180   2 LATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVTPYPQPGNPTPRVFRLPEGVLNRMGLNNPGLDAVLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B         83 YASDLHDYSKK---PLFLSISGLSVEENVAMVRRLAPVAQekgvLLELNLSCPNVPGKPQVAYDFEAMRTYLQQVSLAYG 159
Cdd:pfam01180  82 ELLKRRKEYPRpdlGINLSKAGMTVDDYVEVARKIGPFAD----YIELNVSCPNTPGLRALQTDPELAAILLKVVKEVSK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B        160 LPFGVKMPP-YFDIAHFDTAAAVLNEFPLVkFVTCVNSVGNGLVIDAESESVVIKPkqGFGGLGGKYILPTALANVNAFY 238
Cdd:pfam01180 158 VPVLVKLAPdLTDIVIIDIADVALGEDGLD-GINATNTTVRGMRIDLKTEKPILAN--GTGGLSGPPIKPIALKVIRELY 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
3W7M_B        239 RRCPDKL-VFGCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDELLEIM 294
Cdd:pfam01180 235 QRTGPEIpIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 3-303 6.65e-86

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: 259.62  E-value: 6.65e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B        3 LKLNLLDHVFANPFMNAAGVLCSTEEDLRCMTASSSGALVSKSCTSAPRDGNPEPRY--MAFPLGSINSMGLPNLGFDFY 80
Cdd:COG0167   2 LSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLfrLPEDSGLINRMGLNNPGVDAF 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B       81 LKYASDLHDYsKKPLFLSISGLSVEENVAMVRRLAPVaqekGV-LLELNLSCPNVPGK-PQVAYDFEAMRTYLQQVSLAY 158
Cdd:COG0167  82 LERLLPAKRY-DVPVIVNIGGNTVEDYVELARRLADA----GAdYLELNISCPNTPGGgRALGQDPEALAELLAAVKAAT 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B      159 GLPFGVKMPPyfDIAHFDTAAAVLNEFPLvKFVTCVNSVgNGLVIDAESESVVIKPkqGFGGLGGKYILPTALANVNAFY 238
Cdd:COG0167 157 DKPVLVKLAP--DLTDIVEIARAAEEAGA-DGVIAINTT-LGRAIDLETRRPVLAN--EAGGLSGPALKPIALRMVREVA 230

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
3W7M_B      239 RRCPDKL-VFGCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDELLEIMARKGYRTLE 303
Cdd:COG0167 231 QAVGGDIpIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSIS 296
DHOD_1B_like cd04740
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ...
 12-307 2.60e-56

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: 183.90  E-value: 2.60e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B       12 FANPFMNAAGVLCSTEEDLRCMTASSSGALVSKSCTSAPRDGNPEPRYMAFPLGSINSMGLPNLGFDFYLKYASDLHDYS 91
Cdd:cd04740   9 LKNPVILASGTFGFGEELSRVADLGKLGAIVTKSITLEPREGNPPPRVVETPGGMLNAIGLQNPGVEAFLEELLPWLREF 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B       92 KKPLFLSISGLSVEENVAMVRRLAPVaqeKGVLLELNLSCPNVPGK-------PQVAYDF-EAMRTylqqvslAYGLPFG 163
Cdd:cd04740  89 GTPVIASIAGSTVEEFVEVAEKLADA---GADAIELNISCPNVKGGgmafgtdPEAVAEIvKAVKK-------ATDVPVI 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B      164 VKMPPYF-DIAhfDTAAAVLNEFplVKFVTCVNSVGnGLVIDAESESVVIkpKQGFGGLGGKYILPTALANVNAFYRRCp 242
Cdd:cd04740 159 VKLTPNVtDIV--EIARAAEEAG--ADGLTLINTLK-GMAIDIETRKPIL--GNVTGGLSGPAIKPIALRMVYQVYKAV- 230

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
3W7M_B      243 DKLVFGCGGVYSGEDAFLHILAGASMVQVGTALQeEGPGIFTRLEDELLEIMARKGYRTLEEFRG 307
Cdd:cd04740 231 EIPIIGVGGIASGEDALEFLMAGASAVQVGTANF-VDPEAFKEIIEGLEAYLDEEGIKSIEELVG 294
PRK07259 PRK07259
dihydroorotate dehydrogenase;
3-310 8.01e-56

dihydroorotate dehydrogenase;


Pssm-ID: 235982  Cd Length: 301  Bit Score: 183.04  E-value: 8.01e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B         3 LKLNLLDHVFANPFMNAAGVLCSTEEDLRCMTASSSGALVSKSCTSAPRDGNPEPRYMAFPLGSINSMGLPNLGFDFYLK 82
Cdd:PRK07259   2 LSVELPGLKLKNPVMPASGTFGFGGEYARFYDLNGLGAIVTKSTTLEPREGNPTPRIAETPGGMLNAIGLQNPGVDAFIE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B        83 YASDLHDYSKKPLFLSISGLSVEENVAMVRRLAPVAQEKGvlLELNLSCPNVPG-------KPQVAYDF-EAMRTylqqv 154
Cdd:PRK07259  82 EELPWLEEFDTPIIANVAGSTEEEYAEVAEKLSKAPNVDA--IELNISCPNVKHggmafgtDPELAYEVvKAVKE----- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B       155 slAYGLPFGVKMPPYF-DIAhfDTAAAVLNEFplVKFVTCVNSVgNGLVIDAESEsvviKP--KQGFGGLGGKYILPTAL 231
Cdd:PRK07259 155 --VVKVPVIVKLTPNVtDIV--EIAKAAEEAG--ADGLSLINTL-KGMAIDIKTR----KPilANVTGGLSGPAIKPIAL 223

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
3W7M_B       232 ANVNAFYRRCpDKLVFGCGGVYSGEDAFLHILAGASMVQVGTALQeEGPGIFTRLEDELLEIMARKGYRTLEEFRGRVK 310
Cdd:PRK07259 224 RMVYQVYQAV-DIPIIGMGGISSAEDAIEFIMAGASAVQVGTANF-YDPYAFPKIIEGLEAYLDKYGIKSIEEIVGIAH 300
pyrD_sub1_fam TIGR01037
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ...
 3-308 3.38e-44

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: 152.97  E-value: 3.38e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B          3 LKLNLLDHVFANPFMNAAGVLCSTEEDLRCMTASSSGALVSKSCTSAPRDGNPEPRYMAFPLGSINSMGLPNLGFDFYLK 82
Cdd:TIGR01037   1 LEVELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTIVETPCGMLNAIGLQNPGVEAFLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B         83 YASDLHDYSKKPLFLSISGLSVEENVAMVRRLAPvAQEKGVLLELNLSCPNVPG-------KPQVAYDFeamrtyLQQVS 155
Cdd:TIGR01037  81 ELKPVREEFPTPLIASVYGSSVEEFAEVAEKLEK-APPYVDAYELNLSCPHVKGggiaigqDPELSADV------VKAVK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B        156 LAYGLPFGVKMPPYF-DIAHFDTAAavlnEFPLVKFVTCVNSVGnGLVIDAESESVVIKPKqgFGGLGGKYILPTALANV 234
Cdd:TIGR01037 154 DKTDVPVFAKLSPNVtDITEIAKAA----EEAGADGLTLINTLR-GMKIDIKTGKPILANK--TGGLSGPAIKPIALRMV 226

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3W7M_B        235 NAFYRRCpDKLVFGCGGVYSGEDAFLHILAGASMVQVGTALQEEgPGIFTRLEDELLEIMARKGYRTLEEFRGR 308
Cdd:TIGR01037 227 YDVYKMV-DIPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYR-GFAFKKIIEGLIAFLKAEGFTSIEELIGI 298
DHOD_2_like cd04738
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ...
 45-290 2.60e-27

Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences, their cellular location and their natural electron acceptor used to reoxidize the flavin group. Members of class 1 are cytosolic enzymes and multimers, while class 2 enzymes are membrane associated, monomeric and use respiratory quinones as their physiological electron acceptors.


Pssm-ID: 240089  Cd Length: 327  Bit Score: 108.74  E-value: 2.60e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B       45 SCTSAPRDGNPEPRymAFPL----GSINSMGLPNLGFDFYLKYASDLHdYSKKPLFLSI-----SGLS--VEENVAMVRR 113
Cdd:cd04738  80 TVTPRPQPGNPKPR--LFRLpedeALINRMGFNNDGADAVAKRLKKRR-PRGGPLGVNIgknkdTPLEdaVEDYVIGVRK 156

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B      114 LAPVAQekgvLLELNLSCPNVPG--KPQVAYDFEAMRTYLQ--QVSLAYGLPFGVKMPPYFDIAHFDTAAAVLNEFPLvk 189
Cdd:cd04738 157 LGPYAD----YLVVNVSSPNTPGlrDLQGKEALRELLTAVKeeRNKLGKKVPLLVKIAPDLSDEELEDIADVALEHGV-- 230

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B      190 fvtcvnsvgNGLVID----AESESVVIKPKQGFGGLGGKYILPTALANVNAFYRRCPDKL-VFGCGGVYSGEDAFLHILA 264
Cdd:cd04738 231 ---------DGIIATnttiSRPGLLRSPLANETGGLSGAPLKERSTEVLRELYKLTGGKIpIIGVGGISSGEDAYEKIRA 301

                       250       260
                ....*....|....*....|....*.
3W7M_B      265 GASMVQVGTALQEEGPGIFTRLEDEL 290
Cdd:cd04738 302 GASLVQLYTGLVYEGPGLVKRIKREL 327
DHPD_FMN cd02940
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ...
 12-290 2.15e-22

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: 94.66  E-value: 2.15e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B       12 FANPFMNAAG-VLCSTEEDLRCMTASSSGALVSKSCTSAPRDGNPEPRYMAFPLGSINSMGLPNL------GFDFYLKYA 84
Cdd:cd02940  11 FPNPFGLASApPTTSYPMIRRAFEAGWGGAVTKTLGLDKDIVTNVSPRIARLRTSGRGQIGFNNIelisekPLEYWLKEI 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B       85 SDLH-DYSKKPLFLSISGlsvEENVAMVRRLAPVAQEKGV-LLELNLSCPNvpGKPQ------VAYDFEAMRTYLQQVSL 156
Cdd:cd02940  91 RELKkDFPDKILIASIMC---EYNKEDWTELAKLVEEAGAdALELNFSCPH--GMPErgmgaaVGQDPELVEEICRWVRE 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B      157 AYGLPFGVKMPP-YFDIAhfDTAAAVLNEFplVKFVTCVNSVgNGLV-IDAESES--VVIKPKQGFGGLGGKYILPTALA 232
Cdd:cd02940 166 AVKIPVIAKLTPnITDIR--EIARAAKEGG--ADGVSAINTV-NSLMgVDLDGTPpaPGVEGKTTYGGYSGPAVKPIALR 240

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
3W7M_B      233 NVNAFYRRCPDKL-VFGCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDEL 290
Cdd:cd02940 241 AVSQIARAPEPGLpISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
PLN02826 PLN02826
dihydroorotate dehydrogenase
 45-304 3.11e-20

dihydroorotate dehydrogenase


Pssm-ID: 178421  Cd Length: 409  Bit Score: 90.18  E-value: 3.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B        45 SCTSAPRDGNPEPRYMAFP--LGSINSMGLPNLGFDFYLKYASDLHDYSKKPLFLSIS-----------------GLSVE 105
Cdd:PLN02826 115 SVTPLPQPGNPKPRVFRLReeGAIINRYGFNSEGIVAVAKRLGAQHGKRKLDETSSSSfssddvkaggkagpgilGVNLG 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B       106 EN----------VAMVRRLAPVAQekgvLLELNLSCPNVPG--KPQVAYDFEAMRTYLQ------QVSLAYGLPFGVKMP 167
Cdd:PLN02826 195 KNktsedaaadyVQGVRALSQYAD----YLVINVSSPNTPGlrKLQGRKQLKDLLKKVLaardemQWGEEGPPPLLVKIA 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B       168 PyfDIAHFDT---AAAVLnefplvkfvtcvnSVG-NGLVI----DAESESVVIKPKQG-FGGLGGKYILPTALANVNAFY 238
Cdd:PLN02826 271 P--DLSKEDLediAAVAL-------------ALGiDGLIIsnttISRPDSVLGHPHADeAGGLSGKPLFDLSTEVLREMY 335

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
3W7M_B       239 RRCPDKL-VFGCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDELLEIMARKGYRTLEE 304
Cdd:PLN02826 336 RLTRGKIpLVGCGGVSSGEDAYKKIRAGASLVQLYTAFAYEGPALIPRIKAELAACLERDGFKSIQE 402
PRK05286 PRK05286
quinone-dependent dihydroorotate dehydrogenase;
47-298 3.43e-20

quinone-dependent dihydroorotate dehydrogenase;


Pssm-ID: 235388  Cd Length: 344  Bit Score: 89.45  E-value: 3.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B        47 TSAPRDGNPEPRYmaFPL----GSINSMGLPNLGFDFYLKYASDLHDYSkkPLFLSI--SGLSVEEN-----VAMVRRLA 115
Cdd:PRK05286  92 TPRPQPGNPKPRL--FRLpedeALINRMGFNNDGADALAERLKKAYRGI--PLGINIgkNKDTPLEDavddyLICLEKLY 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B       116 PVAQekgvLLELNLSCPNVPGKPQVAYDfEAMRTYLQQV-----SLAYGLPFGVKMPPYFDIAHFDTAAAVLNEFPLvkf 190
Cdd:PRK05286 168 PYAD----YFTVNISSPNTPGLRDLQYG-EALDELLAALkeaqaELHGYVPLLVKIAPDLSDEELDDIADLALEHGI--- 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B       191 vtcvnsvgNGLVID----AESESVVIKPKQGFGGLGGKYILPTALANVNAFYRRCPDKL-VFGCGGVYSGEDAFLHILAG 265
Cdd:PRK05286 240 --------DGVIATnttlSRDGLKGLPNADEAGGLSGRPLFERSTEVIRRLYKELGGRLpIIGVGGIDSAEDAYEKIRAG 311

                        250       260       270
                 ....*....|....*....|....*....|...
3W7M_B       266 ASMVQVGTALQEEGPGIFTRLEDELLEIMARKG 298
Cdd:PRK05286 312 ASLVQIYSGLIYEGPGLVKEIVRGLARLLRRDG 344
PRK08318 PRK08318
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
89-312 2.62e-15

NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;


Pssm-ID: 236237 [Multi-domain]  Cd Length: 420  Bit Score: 75.75  E-value: 2.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B        89 DYSKKPLFLSISGLSVEENVamvRRLAPVAQEKGV-LLELNLSCPNvpGKP---------QVAydfEAMRTYLQQVSLAY 158
Cdd:PRK08318  96 DYPDRALIASIMVECNEEEW---KEIAPLVEETGAdGIELNFGCPH--GMSergmgsavgQVP---ELVEMYTRWVKRGS 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B       159 GLPFGVKMPPYF-DI------AHFDTAAAV--LNEfplVKFVTCVNsvgnglvIDAESESVVIKPKQGFGGLGGKYILPT 229
Cdd:PRK08318 168 RLPVIVKLTPNItDIreparaAKRGGADAVslINT---INSITGVD-------LDRMIPMPIVNGKSSHGGYCGPAVKPI 237

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B       230 ALANVNAFYRrcpDKLVF-----GCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDELLEIMARKGYRTLEE 304
Cdd:PRK08318 238 ALNMVAEIAR---DPETRglpisGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISGLSHYMDEKGFASLED 314


                 ....*....
3W7M_B       305 FRGR-VKTI 312
Cdd:PRK08318 315 MVGLaVPNV 323
DHOD_like cd04739
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ...
 14-308 7.49e-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: 7.49e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B       14 NPFMNAAGVLCSTEEDLRCMTASSSGALVSKSC--TSAPRDGNPEPRYMAFPLGSINSMGLpnlgFDFYLKYASDLHDY- 90
Cdd:cd04739  13 NPLVASASPLSRNLDNIRRLEDAGAGAIVLPSLfeEQIEREAQELDRFLTYGSSFAEALSY----FPEYGRYNLGPEEYl 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B       91 -----SKK----PLFLSISGLSVEENVAMVRRLapvaQEKGV-LLELNLScpNVPGKPQVAY-DFEAMrtY---LQQVSL 156
Cdd:cd04739  89 elirrAKRavsiPVIASLNGVSAGGWVDYARQI----EEAGAdALELNIY--ALPTDPDISGaEVEQR--YldiLRAVKS 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B      157 AYGLPFGVKMPPYFdiahfdTAaavlnefpLVKFVTCVNSVG-NGLV---------IDAESESVVIKPKQGFGGLGGKYI 226
Cdd:cd04739 161 AVTIPVAVKLSPFF------SA--------LAHMAKQLDAAGaDGLVlfnrfyqpdIDLETLEVVPNLLLSSPAEIRLPL 226

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B      227 LPTALAnvnafYRRCPDKLVfGCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDELLEIMARKGYRTLEEFR 306
Cdd:cd04739 227 RWIAIL-----SGRVKASLA-ASGGVHDAEDVVKYLLAGADVVMTTSALLRHGPDYIGTLLAGLEAWMEEHGYESVQQLR 300


                ..
3W7M_B      307 GR 308
Cdd:cd04739 301 GS 302
PRK07565 PRK07565
dihydroorotate dehydrogenase-like protein;
14-308 2.35e-12

dihydroorotate dehydrogenase-like protein;


Pssm-ID: 236051  Cd Length: 334  Bit Score: 66.43  E-value: 2.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B        14 NPFMNAAGVLCSTEEDLRCMTASSSGALVSKS---------------CTSAPRDGNPEPRyMAFPLGSINSMGLpnlgfD 78
Cdd:PRK07565  14 NPLVASASPLSESVDNVKRLEDAGAGAVVLKSlfeeqirheaaeldrHLTHGTESFAEAL-DYFPEPAKFYVGP-----E 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B        79 FYLKYASDLHDYSKKPLFLSISGLSVEENVAMVRRLapvaQEKGV-LLELNLScpNVPGKPQVAY-DFEAMrtY---LQQ 153
Cdd:PRK07565  88 EYLELIRRAKEAVDIPVIASLNGSSAGGWVDYARQI----EQAGAdALELNIY--YLPTDPDISGaEVEQR--YldiLRA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B       154 VSLAYGLPFGVKMPPYF-DIAHFdtaaavlnefplvkfVTCVNSVG-NGLV---------IDAESESVVIK-----PKQG 217
Cdd:PRK07565 160 VKSAVSIPVAVKLSPYFsNLANM---------------AKRLDAAGaDGLVlfnrfyqpdIDLETLEVVPGlvlstPAEL 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B       218 FGGLGGKYILptalanvnafYRRCPDKLVfGCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDELLEIMARK 297
Cdd:PRK07565 225 RLPLRWIAIL----------SGRVGADLA-ATTGVHDAEDVIKMLLAGADVVMIASALLRHGPDYIGTILRGLEDWMERH 293

                        330
                 ....*....|.
3W7M_B       298 GYRTLEEFRGR 308
Cdd:PRK07565 294 GYESLQQFRGS 304
PLN02495 PLN02495
oxidoreductase, acting on the CH-CH group of donors
 39-307 2.44e-11

oxidoreductase, acting on the CH-CH group of donors


Pssm-ID: 215273 [Multi-domain]  Cd Length: 385  Bit Score: 63.70  E-value: 2.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B        39 GALVSKSCT-SAPRDGNPEPRYMAFPLGSINSMGLPNLG-----------FDFYLKYASDL-HDYSKKPLFLSIsglsVE 105
Cdd:PLN02495  47 GGVIAKTVSlDASKVINVTPRYARLRAGANGSAKGRVIGwqnielisdrpFETMLAEFKQLkEEYPDRILIASI----ME 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B       106 E-NVAMVRRLAPVAQEKGV-LLELNLSCPNvpGKPQ------VAYDFEAMRTYLQQVSLAYGLPFGVKMPPYF-DIAHfd 176
Cdd:PLN02495 123 EyNKDAWEEIIERVEETGVdALEINFSCPH--GMPErkmgaaVGQDCDLLEEVCGWINAKATVPVWAKMTPNItDITQ-- 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B       177 TAAAVLNEFplVKFVTCVNSVGNGLVIDAESesvvIKPK---QGF---GGLGGKYILPTALANVNAFYRRC-----PDKL 245
Cdd:PLN02495 199 PARVALKSG--CEGVAAINTIMSVMGINLDT----LRPEpcvEGYstpGGYSSKAVRPIALAKVMAIAKMMksefpEDRS 272

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
3W7M_B       246 VFGCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDELLEIMARKGYRTLEEFRG 307
Cdd:PLN02495 273 LSGIGGVETGGDAAEFILLGADTVQVCTGVMMHGYPLVKNLCAELQDFMKKHNFSSIEDFRG 334
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 89-273 1.31e-05

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


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 45.27  E-value: 1.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B       89 DYSKKPLFLSISGLSVEENVAMVRRLAPVAQEKGVllELNLSCPnvpgkpqvaYDFEAMRTYLQQVSLAY-GLPFGVKMP 167
Cdd:cd04722  54 AETDLPLGVQLAINDAAAAVDIAAAAARAAGADGV--EIHGAVG---------YLAREDLELIRELREAVpDVKVVVKLS 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W7M_B      168 PYFDIAHFDTAAAvlnefpLVKFVTCVNSVGNGLVIDAESESVVIKpkqgfgglggkyilptalanvnAFYRRCPDKLVF 247
Cdd:cd04722 123 PTGELAAAAAEEA------GVDEVGLGNGGGGGGGRDAVPIADLLL----------------------ILAKRGSKVPVI 174

                       170       180
                ....*....|....*....|....*.
3W7M_B      248 GCGGVYSGEDAFLHILAGASMVQVGT 273
Cdd:cd04722 175 AGGGINDPEDAAEALALGADGVIVGS 200
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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