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Conserved domains on  [gi|515995497|ref|WP_017426080|]
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MULTISPECIES: dihydroorotate dehydrogenase [Paenibacillus]

Protein Classification

dihydroorotate dehydrogenase( domain architecture ID 10012903)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK07259 PRK07259
dihydroorotate dehydrogenase;
4-310 6.93e-159

dihydroorotate dehydrogenase;


:

Pssm-ID: 235982  Cd Length: 301  Bit Score: 444.98  E-value: 6.93e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497   4 MACNIAGVPFKNPIIMASGTFGFGREYAEFYSPELLGGIVGKGLTLHPKAGNTGQRIHETASGMLNSVGLENPGVAAFLK 83
Cdd:PRK07259   2 LSVELPGLKLKNPVMPASGTFGFGGEYARFYDLNGLGAIVTKSTTLEPREGNPTPRIAETPGGMLNAIGLQNPGVDAFIE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497  84 DELDDMTRWNTAVIANVGGSNLEEYVqAVAMITENAQkrrtmnrrGVDMLELNISCPNVKQGGMQFGIQTEVAREVVRQV 163
Cdd:PRK07259  82 EELPWLEEFDTPIIANVAGSTEEEYA-EVAEKLSKAP--------NVDAIELNISCPNVKHGGMAFGTDPELAYEVVKAV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 164 RNVTALPLIVKLSPNAENITQMAVMCEEEGADGVSLINTFSAMKIDIRRRRSVFANTYAGLSGPAIKPIALRMVHQVAQA 243
Cdd:PRK07259 153 KEVVKVPVIVKLTPNVTDIVEIAKAAEEAGADGLSLINTLKGMAIDIKTRKPILANVTGGLSGPAIKPIALRMVYQVYQA 232

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515995497 244 VSIPVIGMGGISSVEDIIEFTMAGAAAIQVGTYNFVHLHAGAELVYGLEQWMQQEKVQSLDEIRGIL 310
Cdd:PRK07259 233 VDIPIIGMGGISSAEDAIEFIMAGASAVQVGTANFYDPYAFPKIIEGLEAYLDKYGIKSIEEIVGIA 299
 
Name Accession Description Interval E-value
PRK07259 PRK07259
dihydroorotate dehydrogenase;
4-310 6.93e-159

dihydroorotate dehydrogenase;


Pssm-ID: 235982  Cd Length: 301  Bit Score: 444.98  E-value: 6.93e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497   4 MACNIAGVPFKNPIIMASGTFGFGREYAEFYSPELLGGIVGKGLTLHPKAGNTGQRIHETASGMLNSVGLENPGVAAFLK 83
Cdd:PRK07259   2 LSVELPGLKLKNPVMPASGTFGFGGEYARFYDLNGLGAIVTKSTTLEPREGNPTPRIAETPGGMLNAIGLQNPGVDAFIE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497  84 DELDDMTRWNTAVIANVGGSNLEEYVqAVAMITENAQkrrtmnrrGVDMLELNISCPNVKQGGMQFGIQTEVAREVVRQV 163
Cdd:PRK07259  82 EELPWLEEFDTPIIANVAGSTEEEYA-EVAEKLSKAP--------NVDAIELNISCPNVKHGGMAFGTDPELAYEVVKAV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 164 RNVTALPLIVKLSPNAENITQMAVMCEEEGADGVSLINTFSAMKIDIRRRRSVFANTYAGLSGPAIKPIALRMVHQVAQA 243
Cdd:PRK07259 153 KEVVKVPVIVKLTPNVTDIVEIAKAAEEAGADGLSLINTLKGMAIDIKTRKPILANVTGGLSGPAIKPIALRMVYQVYQA 232

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515995497 244 VSIPVIGMGGISSVEDIIEFTMAGAAAIQVGTYNFVHLHAGAELVYGLEQWMQQEKVQSLDEIRGIL 310
Cdd:PRK07259 233 VDIPIIGMGGISSAEDAIEFIMAGASAVQVGTANFYDPYAFPKIIEGLEAYLDKYGIKSIEEIVGIA 299
DHOD_1B_like cd04740
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ...
 7-310 1.23e-140

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: 398.85  E-value: 1.23e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497   7 NIAGVPFKNPIIMASGTFGFGREYAEFYSPELLGGIVGKGLTLHPKAGNTGQRIHETASGMLNSVGLENPGVAAFLKDEL 86
Cdd:cd04740    3 ELAGLRLKNPVILASGTFGFGEELSRVADLGKLGAIVTKSITLEPREGNPPPRVVETPGGMLNAIGLQNPGVEAFLEELL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497  87 DDMTRWNTAVIANVGGSNLEEYVQAVamitenaqkrRTMNRRGVDMLELNISCPNVKQGGMQFGIQTEVAREVVRQVRNV 166
Cdd:cd04740   83 PWLREFGTPVIASIAGSTVEEFVEVA----------EKLADAGADAIELNISCPNVKGGGMAFGTDPEAVAEIVKAVKKA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 167 TALPLIVKLSPNAENITQMAVMCEEEGADGVSLINTFSAMKIDIRRRRSVFANTYAGLSGPAIKPIALRMVHQVAQAVSI 246
Cdd:cd04740  153 TDVPVIVKLTPNVTDIVEIARAAEEAGADGLTLINTLKGMAIDIETRKPILGNVTGGLSGPAIKPIALRMVYQVYKAVEI 232

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515995497 247 PVIGMGGISSVEDIIEFTMAGAAAIQVGTYNFVHLHAGAELVYGLEQWMQQEKVQSLDEIRGIL 310
Cdd:cd04740  233 PIIGVGGIASGEDALEFLMAGASAVQVGTANFVDPEAFKEIIEGLEAYLDEEGIKSIEELVGLA 296
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 3-304 1.64e-126

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: 362.85  E-value: 1.64e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497   3 SMACNIAGVPFKNPIIMASGTFGFGREYAEFYSPELLGGIVGKGLTLHPKAGNTGQRIHET--ASGMLNSVGLENPGVAA 80
Cdd:COG0167    1 DLSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLpeDSGLINRMGLNNPGVDA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497  81 FLKdELDDMTRWNTAVIANVGGSNLEEYVQAVamitenaqkrRTMNRRGVDMLELNISCPNVKQGGMQFGIQTEVAREVV 160
Cdd:COG0167   81 FLE-RLLPAKRYDVPVIVNIGGNTVEDYVELA----------RRLADAGADYLELNISCPNTPGGGRALGQDPEALAELL 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 161 RQVRNVTALPLIVKLSPNAENITQMAVMCEEEGADGVSLINTFSAMKIDIRRRRSVFANTYAGLSGPAIKPIALRMVHQV 240
Cdd:COG0167  150 AAVKAATDKPVLVKLAPDLTDIVEIARAAEEAGADGVIAINTTLGRAIDLETRRPVLANEAGGLSGPALKPIALRMVREV 229

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515995497 241 AQAV--SIPVIGMGGISSVEDIIEFTMAGAAAIQVGTYNFVH-LHAGAELVYGLEQWMQQEKVQSLD 304
Cdd:COG0167  230 AQAVggDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEgPGLVRRIIRGLEAYLEEKGFSSIS 296
pyrD_sub1_fam TIGR01037
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ...
 7-309 1.07e-109

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: 320.53  E-value: 1.07e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497    7 NIAGVPFKNPIIMASGTFGFGREYAEFYSPELLGGIVGKGLTLHPKAGNTGQRIHETASGMLNSVGLENPGVAAFLKDEL 86
Cdd:TIGR01037   4 ELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTIVETPCGMLNAIGLQNPGVEAFLEELK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497   87 DDMTRWNTAVIANVGGSNLEEYVQaVAMITENAQKRrtmnrrgVDMLELNISCPNVKQGGMQFGIQTEVAREVVRQVRNV 166
Cdd:TIGR01037  84 PVREEFPTPLIASVYGSSVEEFAE-VAEKLEKAPPY-------VDAYELNLSCPHVKGGGIAIGQDPELSADVVKAVKDK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497  167 TALPLIVKLSPNAENITQMAVMCEEEGADGVSLINTFSAMKIDIRRRRSVFANTYAGLSGPAIKPIALRMVHQVAQAVSI 246
Cdd:TIGR01037 156 TDVPVFAKLSPNVTDITEIAKAAEEAGADGLTLINTLRGMKIDIKTGKPILANKTGGLSGPAIKPIALRMVYDVYKMVDI 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515995497  247 PVIGMGGISSVEDIIEFTMAGAAAIQVGTYNFVHLHAGAELVYGLEQWMQQEKVQSLDEIRGI 309
Cdd:TIGR01037 236 PIIGVGGITSFEDALEFLMAGASAVQVGTAVYYRGFAFKKIIEGLIAFLKAEGFTSIEELIGI 298
DHO_dh pfam01180
Dihydroorotate dehydrogenase;
3-275 2.43e-72

Dihydroorotate dehydrogenase;


Pssm-ID: 426103  Cd Length: 291  Bit Score: 224.92  E-value: 2.43e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497    3 SMACNIAGVPFKNPIIMASGTFGFGREYAEFYSPELLGGIVGKGLTLHPKAGNTGQRIHETASGMLNSVGLENPG---VA 79
Cdd:pfam01180   1 MLATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVTPYPQPGNPTPRVFRLPEGVLNRMGLNNPGldaVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497   80 AFLKDELDDMTRWNTAVIANVGGSNLEEYVQAVAMITENAqkrrtmnrrgvDMLELNISCPNVKqGGMQFGIQTEVAREV 159
Cdd:pfam01180  81 AELLKRRKEYPRPDLGINLSKAGMTVDDYVEVARKIGPFA-----------DYIELNVSCPNTP-GLRALQTDPELAAIL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497  160 VRQVRNVTALPLIVKLSPNAENITQMAVMCEEEGADGVSLIN----TFSAMKIDIRRRRSVFANTYAGLSGPAIKPIALR 235
Cdd:pfam01180 149 LKVVKEVSKVPVLVKLAPDLTDIVIIDIADVALGEDGLDGINatntTVRGMRIDLKTEKPILANGTGGLSGPPIKPIALK 228

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 515995497  236 MVHQVAQAVS--IPVIGMGGISSVEDIIEFTMAGAAAIQVGT 275
Cdd:pfam01180 229 VIRELYQRTGpeIPIIGVGGIESGEDALEKILAGASAVQIGT 270
 
Name Accession Description Interval E-value
PRK07259 PRK07259
dihydroorotate dehydrogenase;
4-310 6.93e-159

dihydroorotate dehydrogenase;


Pssm-ID: 235982  Cd Length: 301  Bit Score: 444.98  E-value: 6.93e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497   4 MACNIAGVPFKNPIIMASGTFGFGREYAEFYSPELLGGIVGKGLTLHPKAGNTGQRIHETASGMLNSVGLENPGVAAFLK 83
Cdd:PRK07259   2 LSVELPGLKLKNPVMPASGTFGFGGEYARFYDLNGLGAIVTKSTTLEPREGNPTPRIAETPGGMLNAIGLQNPGVDAFIE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497  84 DELDDMTRWNTAVIANVGGSNLEEYVqAVAMITENAQkrrtmnrrGVDMLELNISCPNVKQGGMQFGIQTEVAREVVRQV 163
Cdd:PRK07259  82 EELPWLEEFDTPIIANVAGSTEEEYA-EVAEKLSKAP--------NVDAIELNISCPNVKHGGMAFGTDPELAYEVVKAV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 164 RNVTALPLIVKLSPNAENITQMAVMCEEEGADGVSLINTFSAMKIDIRRRRSVFANTYAGLSGPAIKPIALRMVHQVAQA 243
Cdd:PRK07259 153 KEVVKVPVIVKLTPNVTDIVEIAKAAEEAGADGLSLINTLKGMAIDIKTRKPILANVTGGLSGPAIKPIALRMVYQVYQA 232

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515995497 244 VSIPVIGMGGISSVEDIIEFTMAGAAAIQVGTYNFVHLHAGAELVYGLEQWMQQEKVQSLDEIRGIL 310
Cdd:PRK07259 233 VDIPIIGMGGISSAEDAIEFIMAGASAVQVGTANFYDPYAFPKIIEGLEAYLDKYGIKSIEEIVGIA 299
DHOD_1B_like cd04740
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ...
 7-310 1.23e-140

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: 398.85  E-value: 1.23e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497   7 NIAGVPFKNPIIMASGTFGFGREYAEFYSPELLGGIVGKGLTLHPKAGNTGQRIHETASGMLNSVGLENPGVAAFLKDEL 86
Cdd:cd04740    3 ELAGLRLKNPVILASGTFGFGEELSRVADLGKLGAIVTKSITLEPREGNPPPRVVETPGGMLNAIGLQNPGVEAFLEELL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497  87 DDMTRWNTAVIANVGGSNLEEYVQAVamitenaqkrRTMNRRGVDMLELNISCPNVKQGGMQFGIQTEVAREVVRQVRNV 166
Cdd:cd04740   83 PWLREFGTPVIASIAGSTVEEFVEVA----------EKLADAGADAIELNISCPNVKGGGMAFGTDPEAVAEIVKAVKKA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 167 TALPLIVKLSPNAENITQMAVMCEEEGADGVSLINTFSAMKIDIRRRRSVFANTYAGLSGPAIKPIALRMVHQVAQAVSI 246
Cdd:cd04740  153 TDVPVIVKLTPNVTDIVEIARAAEEAGADGLTLINTLKGMAIDIETRKPILGNVTGGLSGPAIKPIALRMVYQVYKAVEI 232

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515995497 247 PVIGMGGISSVEDIIEFTMAGAAAIQVGTYNFVHLHAGAELVYGLEQWMQQEKVQSLDEIRGIL 310
Cdd:cd04740  233 PIIGVGGIASGEDALEFLMAGASAVQVGTANFVDPEAFKEIIEGLEAYLDEEGIKSIEELVGLA 296
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 3-304 1.64e-126

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: 362.85  E-value: 1.64e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497   3 SMACNIAGVPFKNPIIMASGTFGFGREYAEFYSPELLGGIVGKGLTLHPKAGNTGQRIHET--ASGMLNSVGLENPGVAA 80
Cdd:COG0167    1 DLSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLpeDSGLINRMGLNNPGVDA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497  81 FLKdELDDMTRWNTAVIANVGGSNLEEYVQAVamitenaqkrRTMNRRGVDMLELNISCPNVKQGGMQFGIQTEVAREVV 160
Cdd:COG0167   81 FLE-RLLPAKRYDVPVIVNIGGNTVEDYVELA----------RRLADAGADYLELNISCPNTPGGGRALGQDPEALAELL 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 161 RQVRNVTALPLIVKLSPNAENITQMAVMCEEEGADGVSLINTFSAMKIDIRRRRSVFANTYAGLSGPAIKPIALRMVHQV 240
Cdd:COG0167  150 AAVKAATDKPVLVKLAPDLTDIVEIARAAEEAGADGVIAINTTLGRAIDLETRRPVLANEAGGLSGPALKPIALRMVREV 229

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515995497 241 AQAV--SIPVIGMGGISSVEDIIEFTMAGAAAIQVGTYNFVH-LHAGAELVYGLEQWMQQEKVQSLD 304
Cdd:COG0167  230 AQAVggDIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEgPGLVRRIIRGLEAYLEEKGFSSIS 296
pyrD_sub1_fam TIGR01037
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ...
 7-309 1.07e-109

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: 320.53  E-value: 1.07e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497    7 NIAGVPFKNPIIMASGTFGFGREYAEFYSPELLGGIVGKGLTLHPKAGNTGQRIHETASGMLNSVGLENPGVAAFLKDEL 86
Cdd:TIGR01037   4 ELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTIVETPCGMLNAIGLQNPGVEAFLEELK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497   87 DDMTRWNTAVIANVGGSNLEEYVQaVAMITENAQKRrtmnrrgVDMLELNISCPNVKQGGMQFGIQTEVAREVVRQVRNV 166
Cdd:TIGR01037  84 PVREEFPTPLIASVYGSSVEEFAE-VAEKLEKAPPY-------VDAYELNLSCPHVKGGGIAIGQDPELSADVVKAVKDK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497  167 TALPLIVKLSPNAENITQMAVMCEEEGADGVSLINTFSAMKIDIRRRRSVFANTYAGLSGPAIKPIALRMVHQVAQAVSI 246
Cdd:TIGR01037 156 TDVPVFAKLSPNVTDITEIAKAAEEAGADGLTLINTLRGMKIDIKTGKPILANKTGGLSGPAIKPIALRMVYDVYKMVDI 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515995497  247 PVIGMGGISSVEDIIEFTMAGAAAIQVGTYNFVHLHAGAELVYGLEQWMQQEKVQSLDEIRGI 309
Cdd:TIGR01037 236 PIIGVGGITSFEDALEFLMAGASAVQVGTAVYYRGFAFKKIIEGLIAFLKAEGFTSIEELIGI 298
DHO_dh pfam01180
Dihydroorotate dehydrogenase;
3-275 2.43e-72

Dihydroorotate dehydrogenase;


Pssm-ID: 426103  Cd Length: 291  Bit Score: 224.92  E-value: 2.43e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497    3 SMACNIAGVPFKNPIIMASGTFGFGREYAEFYSPELLGGIVGKGLTLHPKAGNTGQRIHETASGMLNSVGLENPG---VA 79
Cdd:pfam01180   1 MLATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVTPYPQPGNPTPRVFRLPEGVLNRMGLNNPGldaVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497   80 AFLKDELDDMTRWNTAVIANVGGSNLEEYVQAVAMITENAqkrrtmnrrgvDMLELNISCPNVKqGGMQFGIQTEVAREV 159
Cdd:pfam01180  81 AELLKRRKEYPRPDLGINLSKAGMTVDDYVEVARKIGPFA-----------DYIELNVSCPNTP-GLRALQTDPELAAIL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497  160 VRQVRNVTALPLIVKLSPNAENITQMAVMCEEEGADGVSLIN----TFSAMKIDIRRRRSVFANTYAGLSGPAIKPIALR 235
Cdd:pfam01180 149 LKVVKEVSKVPVLVKLAPDLTDIVIIDIADVALGEDGLDGINatntTVRGMRIDLKTEKPILANGTGGLSGPPIKPIALK 228

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 515995497  236 MVHQVAQAVS--IPVIGMGGISSVEDIIEFTMAGAAAIQVGT 275
Cdd:pfam01180 229 VIRELYQRTGpeIPIIGVGGIESGEDALEKILAGASAVQIGT 270
DHOD_DHPD_FMN cd02810
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ...
 7-275 1.57e-60

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: 194.49  E-value: 1.57e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497   7 NIAGVPFKNPIIMASGTFGFGREYAEFYSPELLGGIVGKGLTLHPKAGNTGQRIHET---------ASGMLNSVGLENPG 77
Cdd:cd02810    2 NFLGLKLKNPFGVAAGPLLKTGELIARAAAAGFGAVVYKTVTLHPRPGNPLPRVARLppegesypeQLGILNSFGLPNLG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497  78 VAAFLkdelDDMTRWNTA-----VIANVGGSNLEEYVQAVAMITenaqkrrtmnRRGVDMLELNISCPNVKqGGMQFGIQ 152
Cdd:cd02810   82 LDVWL----QDIAKAKKEfpgqpLIASVGGSSKEDYVELARKIE----------RAGAKALELNLSCPNVG-GGRQLGQD 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 153 TEVAREVVRQVRNVTALPLIVKLSPN--AENITQMAVMCEEEGADGVSLINTFSAMKIDIRRRRSVFANTYAGLSGPAIK 230
Cdd:cd02810  147 PEAVANLLKAVKAAVDIPLLVKLSPYfdLEDIVELAKAAERAGADGLTAINTISGRVVDLKTVGPGPKRGTGGLSGAPIR 226

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 515995497 231 PIALRMVHQVAQAVS--IPVIGMGGISSVEDIIEFTMAGAAAIQVGT 275
Cdd:cd02810  227 PLALRWVARLAARLQldIPIIGVGGIDSGEDVLEMLMAGASAVQVAT 273
DHPD_FMN cd02940
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ...
 6-276 2.13e-43

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: 150.51  E-value: 2.13e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497   6 CNIAGVPFKNPIIMASGTFG-----FGREYAEFYspellGGIVGKGLTL-HPKAGNTGQRIHETASGMLNSVGLEN---- 75
Cdd:cd02940    4 VTFCGIKFPNPFGLASAPPTtsypmIRRAFEAGW-----GGAVTKTLGLdKDIVTNVSPRIARLRTSGRGQIGFNNieli 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497  76 ---PgvaafLKDELDDMTRW-----NTAVIANV-GGSNLEEYVQAVAMITEnaqkrrtmnrRGVDMLELNISCPNV---K 143
Cdd:cd02940   79 sekP-----LEYWLKEIRELkkdfpDKILIASImCEYNKEDWTELAKLVEE----------AGADALELNFSCPHGmpeR 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 144 QGGMQFGIQTEVAREVVRQVRNVTALPLIVKLSPNAENITQMAVMCEEEGADGVSLINT-FSAMKIDIRRRRS-VFAN-- 219
Cdd:cd02940  144 GMGAAVGQDPELVEEICRWVREAVKIPVIAKLTPNITDIREIARAAKEGGADGVSAINTvNSLMGVDLDGTPPaPGVEgk 223

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 220 -TYAGLSGPAIKPIALRMVHQVAQAV--SIPVIGMGGISSVEDIIEFTMAGAAAIQVGTY 276
Cdd:cd02940  224 tTYGGYSGPAVKPIALRAVSQIARAPepGLPISGIGGIESWEDAAEFLLLGASVVQVCTA 283
PRK08318 PRK08318
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
1-309 5.42e-43

NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;


Pssm-ID: 236237 [Multi-domain]  Cd Length: 420  Bit Score: 152.41  E-value: 5.42e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497   1 MISMACNIAGVPFKNPIIMASG-----------TFGFGreyaefyspelLGGIVGKglTLHPKAGN-TGQRIHETASGML 68
Cdd:PRK08318   1 MADLSITFCGIKSPNPFWLASApptnkyynvarAFEAG-----------WGGVVWK--TLGPPIVNvSSPRFGALVKEDR 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497  69 NSVGLEN-------PgvaafLKDELDDMTR----W-NTAVIANV-GGSNLEEYVQAVAMITEnaqkrrtmnrRGVDMLEL 135
Cdd:PRK08318  68 RFIGFNNielitdrP-----LEVNLREIRRvkrdYpDRALIASImVECNEEEWKEIAPLVEE----------TGADGIEL 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 136 NISCPnvkQG----GM--QFGIQTEVAREVVRQVRNVTALPLIVKLSPNAENITQMAVMCEEEGADGVSLINTF-SAMKI 208
Cdd:PRK08318 133 NFGCP---HGmserGMgsAVGQVPELVEMYTRWVKRGSRLPVIVKLTPNITDIREPARAAKRGGADAVSLINTInSITGV 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 209 DIRRrrsvFA--------NTYAGLSGPAIKPIALRMVHQVA---QAVSIPVIGMGGISSVEDIIEFTMAGAAAIQVGTYN 277
Cdd:PRK08318 210 DLDR----MIpmpivngkSSHGGYCGPAVKPIALNMVAEIArdpETRGLPISGIGGIETWRDAAEFILLGAGTVQVCTAA 285

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 515995497 278 FVHlhaG----AELVYGLEQWMQQEKVQSLDEIRGI 309
Cdd:PRK08318 286 MQY---GfrivEDMISGLSHYMDEKGFASLEDMVGL 318
PRK02506 PRK02506
dihydroorotate dehydrogenase 1A; Reviewed
 3-310 1.92e-32

dihydroorotate dehydrogenase 1A; Reviewed


Pssm-ID: 235045  Cd Length: 310  Bit Score: 121.98  E-value: 1.92e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497   3 SMACNIAGVPFKNPIIMASGTFGFGREyaefyspELL-------GGIVGKGLTLHPKAGNTGQRIHETASGMLNSVGLEN 75
Cdd:PRK02506   1 STSTQIAGFKFDNCLMNAAGVYCMTKE-------ELEeveasaaGAFVTKSATLEPRPGNPEPRYADTPLGSINSMGLPN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497  76 PGVAAFLkDELDDMTR--WNTAVIANVGGSNLEEYVQAVAMITENAQKrrtmnrrgvDMLELNISCPNVKqGGMQFGIQT 153
Cdd:PRK02506  74 LGFDYYL-DYVLELQKkgPNKPHFLSVVGLSPEETHTILKKIQASDFN---------GLVELNLSCPNVP-GKPQIAYDF 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 154 EVAREVVRQVRNVTALPLIVKLSP--NAENITQMAVMCEEEGADGVSLINTF-SAMKIDIRRRRSVFA--NTYAGLSGPA 228
Cdd:PRK02506 143 ETTEQILEEVFTYFTKPLGVKLPPyfDIVHFDQAAAIFNKFPLAFVNCINSIgNGLVIDPEDETVVIKpkNGFGGIGGDY 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 229 IKPIALRMVHQVAQAV--SIPVIGMGGISSVEDIIEFTMAGAAAIQVGTynfvHLHAGAELVYG-----LEQWMQQEKVQ 301
Cdd:PRK02506 223 IKPTALANVRAFYQRLnpSIQIIGTGGVKTGRDAFEHILCGASMVQVGT----ALHKEGPAVFErltkeLKAIMAEKGYQ 298


                 ....*....
gi 515995497 302 SLDEIRGIL 310
Cdd:PRK02506 299 SLEDFRGKL 307
DHOD_2_like cd04738
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ...
 5-273 2.01e-29

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: 114.13  E-value: 2.01e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497   5 ACNIAGVPFKNPIIMASG------------TFGFGreYAEfyspelLGGIvgkglTLHPKAGNTGQRIH--ETASGMLNS 70
Cdd:cd04738   40 EVEVFGLTFPNPVGLAAGfdknaeaidallALGFG--FVE------VGTV-----TPRPQPGNPKPRLFrlPEDEALINR 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497  71 VGLENPGVAAF---LKDelddmTRWNTAVI-ANVGGSN-------LEEYVQAVAMItenaqkrrtmnRRGVDMLELNISC 139
Cdd:cd04738  107 MGFNNDGADAVakrLKK-----RRPRGGPLgVNIGKNKdtpledaVEDYVIGVRKL-----------GPYADYLVVNVSS 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 140 PNVKqGG--MQFGIQ-----TEVAREVVRQVRNVtalPLIVKLSPNAEN--ITQMAVMCEEEGADGVSLINTfsamkiDI 210
Cdd:cd04738  171 PNTP-GLrdLQGKEAlrellTAVKEERNKLGKKV---PLLVKIAPDLSDeeLEDIADVALEHGVDGIIATNT------TI 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515995497 211 RR---RRSVFANTYAGLSGPAIKPIALRMVHQVAQAV--SIPVIGMGGISSVEDIIEFTMAGAAAIQV 273
Cdd:cd04738  241 SRpglLRSPLANETGGLSGAPLKERSTEVLRELYKLTggKIPIIGVGGISSGEDAYEKIRAGASLVQL 308
DHOD_1A_like cd04741
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ...
 7-275 2.98e-28

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: 110.49  E-value: 2.98e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497   7 NIAGVPFKNPIIMASGTFGFG-REYAEFYSPELlGGIVGKGLTLHPKAGNTGQRIHETASGMLNSVGLENPGV---AAFL 82
Cdd:cd04741    2 TPPGLTISPPLMNAAGPWCTTlEDLLELAASST-GAVTTRSSTLAGRPGNPEPRYYAFPLGSINSLGLPNLGLdyyLEYI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497  83 KDELDDMTRWNTAVIANVGGSnLEEYVQAVAMITENAQKrrtmnrrGVDMLELNISCPNVkqGGM-QFGIQTEVAREVVR 161
Cdd:cd04741   81 RTISDGLPGSAKPFFISVTGS-AEDIAAMYKKIAAHQKQ-------FPLAMELNLSCPNV--PGKpPPAYDFDATLEYLT 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 162 QVRNVTALPLIVKLSPNAEnITQMAVMCE--EEGADGVSLI---NTF-SAMKIDIRRRRSVF--ANTYAGLSGPAIKPIA 233
Cdd:cd04741  151 AVKAAYSIPVGVKTPPYTD-PAQFDTLAEalNAFACPISFItatNTLgNGLVLDPERETVVLkpKTGFGGLAGAYLHPLA 229

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 515995497 234 LRMVHQVAQAV--SIPVIGMGGISSVEDIIEFTMAGAAAIQVGT 275
Cdd:cd04741  230 LGNVRTFRRLLpsEIQIIGVGGVLDGRGAFRMRLAGASAVQVGT 273
PRK05286 PRK05286
quinone-dependent dihydroorotate dehydrogenase;
7-273 1.54e-25

quinone-dependent dihydroorotate dehydrogenase;


Pssm-ID: 235388  Cd Length: 344  Bit Score: 104.09  E-value: 1.54e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497   7 NIAGVPFKNPIIMASG------------TFGFGreYAEfyspellggiVGkGLTLHPKAGNTGQRIH--ETASGMLNSVG 72
Cdd:PRK05286  52 TVMGLTFPNPVGLAAGfdkngeaidalgALGFG--FVE----------VG-TVTPRPQPGNPKPRLFrlPEDEALINRMG 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497  73 LENPGVAAFLKdELDdMTRWNTAVIANVGGSNLEEYVQAVAmitenaQKRRTMNR--RGVDMLELNISCPNVK-----QG 145
Cdd:PRK05286 119 FNNDGADALAE-RLK-KAYRGIPLGINIGKNKDTPLEDAVD------DYLICLEKlyPYADYFTVNISSPNTPglrdlQY 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 146 GMQFG-IQTEVAREVVRQVRNVtalPLIVKLSPN--AENITQMAVMCEEEGADGVSLINTfsamkiDIRR---RRSVFAN 219
Cdd:PRK05286 191 GEALDeLLAALKEAQAELHGYV---PLLVKIAPDlsDEELDDIADLALEHGIDGVIATNT------TLSRdglKGLPNAD 261

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515995497 220 TYAGLSGPAIKPIALRMVHQVAQAV--SIPVIGMGGISSVEDIIEFTMAGAAAIQV 273
Cdd:PRK05286 262 EAGGLSGRPLFERSTEVIRRLYKELggRLPIIGVGGIDSAEDAYEKIRAGASLVQI 317
PLN02495 PLN02495
oxidoreductase, acting on the CH-CH group of donors
 129-308 5.74e-22

oxidoreductase, acting on the CH-CH group of donors


Pssm-ID: 215273 [Multi-domain]  Cd Length: 385  Bit Score: 94.90  E-value: 5.74e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 129 GVDMLELNISCPN---VKQGGMQFGIQTEVAREVVRQVRNVTALPLIVKLSPNAENITQMAVMCEEEGADGVSLINTF-S 204
Cdd:PLN02495 140 GVDALEINFSCPHgmpERKMGAAVGQDCDLLEEVCGWINAKATVPVWAKMTPNITDITQPARVALKSGCEGVAAINTImS 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 205 AMKIDIRRRR---SVFA-NTYAGLSGPAIKPIALRMVHQVAQAV------SIPVIGMGGISSVEDIIEFTMAGAAAIQVG 274
Cdd:PLN02495 220 VMGINLDTLRpepCVEGySTPGGYSSKAVRPIALAKVMAIAKMMksefpeDRSLSGIGGVETGGDAAEFILLGADTVQVC 299

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 515995497 275 TYNFVHLHAGAE-LVYGLEQWMQQEKVQSLDEIRG 308
Cdd:PLN02495 300 TGVMMHGYPLVKnLCAELQDFMKKHNFSSIEDFRG 334
DHOD_like cd04739
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ...
 64-310 1.08e-19

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: 87.67  E-value: 1.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497  64 ASGMLNSVGLENPGVAAFL------KDELDdmtrwnTAVIANVGGSNLEEYVQAVAMItENAqkrrtmnrrGVDMLELNI 137
Cdd:cd04739   70 ALSYFPEYGRYNLGPEEYLelirraKRAVS------IPVIASLNGVSAGGWVDYARQI-EEA---------GADALELNI 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 138 ----SCPNVKQGGMQfgiQTEVarEVVRQVRNVTALPLIVKLSPNAENITQMAVMCEEEGADGVSLINTFSAMKIDIRRR 213
Cdd:cd04739  134 yalpTDPDISGAEVE---QRYL--DILRAVKSAVTIPVAVKLSPFFSALAHMAKQLDAAGADGLVLFNRFYQPDIDLETL 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 214 RSVFANTyagLSGPAIKPIALRMVHQVAQAVSIPVIGMGGISSVEDIIEFTMAGAAAIQVGTynfVHLHAGA----ELVY 289
Cdd:cd04739  209 EVVPNLL---LSSPAEIRLPLRWIAILSGRVKASLAASGGVHDAEDVVKYLLAGADVVMTTS---ALLRHGPdyigTLLA 282

                        250       260
                 ....*....|....*....|.
gi 515995497 290 GLEQWMQQEKVQSLDEIRGIL 310
Cdd:cd04739  283 GLEAWMEEHGYESVQQLRGSM 303
PRK07565 PRK07565
dihydroorotate dehydrogenase-like protein;
96-310 2.15e-19

dihydroorotate dehydrogenase-like protein;


Pssm-ID: 236051  Cd Length: 334  Bit Score: 86.84  E-value: 2.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497  96 VIANVGGSNLEEYVQ-AvamitenaqkrRTMNRRGVDMLELNIscpnvkqggmqFGIQTEVAR----------EVVRQVR 164
Cdd:PRK07565 104 VIASLNGSSAGGWVDyA-----------RQIEQAGADALELNI-----------YYLPTDPDIsgaeveqrylDILRAVK 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 165 NVTALPLIVKLSPNAENITQMAVMCEEEGADGVSLINTFSAMKIDIRRRRSVFANTyagLSGPAIKPIALRMVHQVAQAV 244
Cdd:PRK07565 162 SAVSIPVAVKLSPYFSNLANMAKRLDAAGADGLVLFNRFYQPDIDLETLEVVPGLV---LSTPAELRLPLRWIAILSGRV 238

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515995497 245 SIPVIGMGGISSVEDIIEFTMAGAAAIQVGTYNFVH-LHAGAELVYGLEQWMQQEKVQSLDEIRGIL 310
Cdd:PRK07565 239 GADLAATTGVHDAEDVIKMLLAGADVVMIASALLRHgPDYIGTILRGLEDWMERHGYESLQQFRGSM 305
pyrD_sub2 TIGR01036
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ...
 7-275 3.44e-15

dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate dehydrogenase exclusively for subfamily 2. It includes members from bacteria, yeast, plants etc. The subfamilies 1 and 2 share extensive homology, particularly toward the C-terminus. This subfamily has a longer N-terminal region. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273408  Cd Length: 335  Bit Score: 74.82  E-value: 3.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497    7 NIAGVPFKNPIIMASG------------TFGFGreYAEFYSpellggivgkgLTLHPKAGNTGQRI--HETASGMLNSVG 72
Cdd:TIGR01036  49 TVLGLKFPNPLGLAAGfdkdgeaidalgAMGFG--FLEIGT-----------VTPKPQPGNPRPRLfrLIEDEALINRMG 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497   73 LENPGVAAFLkdELDDMTRWNTAVIANVGGSNLEEYVQAVAMITENAQKRRTMnrrgVDMLELNISCPNVK-----QGGM 147
Cdd:TIGR01036 116 FNNHGADVLV--ERLKRARYKGPIGINIGKNKDTPSEDAKEDYAACLRKLGPL----ADYLVVNVSSPNTPglrdlQYKA 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497  148 QFGIQTEVAREVVRQVRNVTALPLIVKLSPN--AENITQMAVMCEEEGADGVSLINTfsamKIDirrRRSVFANTYA--- 222
Cdd:TIGR01036 190 ELRDLLTAVKQEQDGLRRVHRVPVLVKIAPDltESDLEDIADSLVELGIDGVIATNT----TVS---RSLVQGPKNSdet 262

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 515995497  223 -GLSGPAIKPIALRMVHQVAQAVS--IPVIGMGGISSVEDIIEFTMAGAAAIQVGT 275
Cdd:TIGR01036 263 gGLSGKPLQDKSTEIIRRLYAELQgrLPIIGVGGISSAQDALEKIRAGASLLQIYS 318
PLN02826 PLN02826
dihydroorotate dehydrogenase
 10-275 3.89e-15

dihydroorotate dehydrogenase


Pssm-ID: 178421  Cd Length: 409  Bit Score: 75.16  E-value: 3.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497  10 GVPFKNPIIMASGtfgFGREyAEFYsPELLG---GIVGKG-LTLHPKAGNTGQRIHETAS--GMLNSVGLENPG---VAA 80
Cdd:PLN02826  80 GRTFSNPIGLAAG---FDKN-AEAV-EGLLGlgfGFVEIGsVTPLPQPGNPKPRVFRLREegAIINRYGFNSEGivaVAK 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497  81 FL-----KDELDDMTRWNTAVIANVGGSNLEEYVQAV---------AMITENAQKRRTMNRRGvDMLELNISCPNVKqgG 146
Cdd:PLN02826 155 RLgaqhgKRKLDETSSSSFSSDDVKAGGKAGPGILGVnlgknktseDAAADYVQGVRALSQYA-DYLVINVSSPNTP--G 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 147 MQFGIQTEVAREVVRQV---RNVTA------LPLIVKLSP--NAENITQMAVMCEEEGADGVSLINTfsamkiDIRRRRS 215
Cdd:PLN02826 232 LRKLQGRKQLKDLLKKVlaaRDEMQwgeegpPPLLVKIAPdlSKEDLEDIAAVALALGIDGLIISNT------TISRPDS 305

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515995497 216 VFANTYA----GLSGPAIKPIALRMVHQVAQ--AVSIPVIGMGGISSVEDIIEFTMAGAAAIQVGT 275
Cdd:PLN02826 306 VLGHPHAdeagGLSGKPLFDLSTEVLREMYRltRGKIPLVGCGGVSSGEDAYKKIRAGASLVQLYT 371
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
 96-263 2.79e-09

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


Pssm-ID: 239200 [Multi-domain]  Cd Length: 231  Bit Score: 56.35  E-value: 2.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497  96 VIANVGGSNLEEYVQAVAMItenaqkrrtmNRRGVDMLELNISCP--NVKQGGMQFGI--QTEVAREVVRQVRNVTALPL 171
Cdd:cd02801   57 LIVQLGGSDPETLAEAAKIV----------EELGADGIDLNMGCPspKVTKGGAGAALlkDPELVAEIVRAVREAVPIPV 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 172 IVK---LSPNAENITQMAVMCEEEGADGVSlintfsamkIDIRRRRSvfantyaGLSGPAIkpiaLRMVHQVAQAVSIPV 248
Cdd:cd02801  127 TVKirlGWDDEEETLELAKALEDAGASALT---------VHGRTREQ-------RYSGPAD----WDYIAEIKEAVSIPV 186

                        170
                 ....*....|....*
gi 515995497 249 IGMGGISSVEDIIEF 263
Cdd:cd02801  187 IANGDIFSLEDALRC 201
DusA COG0042
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ...
 101-274 8.48e-08

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


Pssm-ID: 439812 [Multi-domain]  Cd Length: 310  Bit Score: 52.79  E-value: 8.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 101 GGSNLEEYVQAVAMITEnaqkrrtmnrRGVDMLELNISCP--NVKQGG-----MQfgiQTEVAREVVRQVRNVTALPLIV 173
Cdd:COG0042   69 FGSDPEELAEAARIAEE----------LGADEIDINMGCPvkKVTKGGagaalLR---DPELVAEIVKAVVEAVDVPVTV 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 174 K----LSPNAENITQMAVMCEEEGADGVSlintfsamkidI--RRRrsvfANTYaglSGPAikpiALRMVHQVAQAVSIP 247
Cdd:COG0042  136 KirlgWDDDDENALEFARIAEDAGAAALT-----------VhgRTR----EQRY---KGPA----DWDAIARVKEAVSIP 193

                        170       180
                 ....*....|....*....|....*...
gi 515995497 248 VIGMGGISSVEDIIE-FTMAGAAAIQVG 274
Cdd:COG0042  194 VIGNGDIFSPEDAKRmLEETGCDGVMIG 221
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
 237-275 2.24e-06

2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.


Pssm-ID: 240081 [Multi-domain]  Cd Length: 236  Bit Score: 47.86  E-value: 2.24e-06
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 515995497 237 VHQVAQAVSIPVIGMGGISSVEDIIEFTMAGAAAIQVGT 275
Cdd:cd04730  148 VPEVRDAVDIPVIAAGGIADGRGIAAALALGADGVQMGT 186
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 224-275 4.16e-06

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;


Pssm-ID: 184165  Cd Length: 241  Bit Score: 47.21  E-value: 4.16e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 515995497 224 LSGPAIKPialrmVHQVAQAVSIPVIGMGGISSVEDIIEFTMAGAAAIQVGT 275
Cdd:PRK13585 177 LEGVNTEP-----VKELVDSVDIPVIASGGVTTLDDLRALKEAGAAGVVVGS 223
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
 186-275 1.58e-05

NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];


Pssm-ID: 441673 [Multi-domain]  Cd Length: 302  Bit Score: 45.87  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 186 AVMCEEEGADGVslintfsamkidirrrrsVFANTYAG--LSGPAIKPIALrmVHQVAQAVSIPVIGMGGISSVEDIIEF 263
Cdd:COG2070  117 ARKAEKAGADAV------------------VAEGAEAGghRGADEVSTFAL--VPEVRDAVDIPVIAAGGIADGRGIAAA 176

                         90
                 ....*....|..
gi 515995497 264 TMAGAAAIQVGT 275
Cdd:COG2070  177 LALGADGVQMGT 188
OYE_like_FMN_family cd02803
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ...
 156-262 2.13e-05

Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 239201 [Multi-domain]  Cd Length: 327  Bit Score: 45.26  E-value: 2.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 156 AREVVRQVRNVTA--LPLIVKLSPN--------AENITQMAVMCEEEGADGvslintfsamkIDIRRRRSVFANTYAGlS 225
Cdd:cd02803  194 LLEIVAAVREAVGpdFPVGVRLSADdfvpggltLEEAIEIAKALEEAGVDA-----------LHVSGGSYESPPPIIP-P 261

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 515995497 226 GPAIKPIALRMVHQVAQAVSIPVIGMGGISSVEDIIE 262
Cdd:cd02803  262 PYVPEGYFLELAEKIKKAVKIPVIAVGGIRDPEVAEE 298
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 224-275 2.82e-05

Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.


Pssm-ID: 425971  Cd Length: 228  Bit Score: 44.39  E-value: 2.82e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 515995497  224 LSGPAIKpialrMVHQVAQAVSIPVIGMGGISSVEDIIEFTMAGAAAIQVGT 275
Cdd:pfam00977 174 LSGPDLE-----LTRELAEAVNIPVIASGGVGSLEDLKELFTEGVDGVIAGS 220
PRK10415 PRK10415
tRNA-dihydrouridine synthase B; Provisional
 63-274 3.80e-05

tRNA-dihydrouridine synthase B; Provisional


Pssm-ID: 182440  Cd Length: 321  Bit Score: 44.58  E-value: 3.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497  63 TASGMLNSvgleNPGVAAFLKDELDdMTRWNTAVIANV--GGSNLEEYVQAVAMITENaqkrrtmnrrGVDMLELNISCP 140
Cdd:PRK10415  37 TVSEMMSS----NPQVWESDKSRLR-MVHIDEPGIRTVqiAGSDPKEMADAARINVES----------GAQIIDINMGCP 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 141 ----NVKQGGMQFGIQTEVAREVVRQVRNVTALPLIVKL----SPNAENITQMAVMCEEEGadgvslintFSAMKIDIRR 212
Cdd:PRK10415 102 akkvNRKLAGSALLQYPDLVKSILTEVVNAVDVPVTLKIrtgwAPEHRNCVEIAQLAEDCG---------IQALTIHGRT 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515995497 213 RRSVFantyaglSGPAikpiALRMVHQVAQAVSIPVIGMGGISS---VEDIIEFTmaGAAAIQVG 274
Cdd:PRK10415 173 RACLF-------NGEA----EYDSIRAVKQKVSIPVIANGDITDplkARAVLDYT--GADALMIG 224
PRK07695 PRK07695
thiazole tautomerase TenI;
186-273 4.56e-05

thiazole tautomerase TenI;


Pssm-ID: 181086 [Multi-domain]  Cd Length: 201  Bit Score: 43.47  E-value: 4.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 186 AVMCEEEGADGVslintfsamkidirrrrsVFANTYAGLSGPAIKPIALRMVHQVAQAVSIPVIGMGGISSvEDIIEFTM 265
Cdd:PRK07695 108 AIQAEKNGADYV------------------VYGHVFPTDCKKGVPARGLEELSDIARALSIPVIAIGGITP-ENTRDVLA 168


                 ....*...
gi 515995497 266 AGAAAIQV 273
Cdd:PRK07695 169 AGVSGIAV 176
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 129-275 4.68e-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: 43.73  E-value: 4.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 129 GVDMLELNISCPNVkqggmqfgiqTEVAREVVRQVRNVTA-LPLIVKLSPNAEnitQMAVMCEEEGADGVSLintfsamk 207
Cdd:cd04722   84 GADGVEIHGAVGYL----------AREDLELIRELREAVPdVKVVVKLSPTGE---LAAAAAEEAGVDEVGL-------- 142

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515995497 208 idirrrrsvfANTYAGLSGPAIKPIALRMVHQVAQAVSIPVIGMGGISSVEDIIEFTMAGAAAIQVGT 275
Cdd:cd04722  143 ----------GNGGGGGGGRDAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
HisA COG0106
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ...
 224-274 1.85e-04

Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino acid transport and metabolism]; Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439876  Cd Length: 236  Bit Score: 41.95  E-value: 1.85e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515995497 224 LSGPAIKPIAlrmvhQVAQAVSIPVIGMGGISSVEDIIEFTMAGAAAIQVG 274
Cdd:COG0106  173 LQGPNLELYR-----ELAAATGIPVIASGGVSSLDDLRALKELGVEGAIVG 218
FadH COG1902
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ...
 156-269 3.85e-04

2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family [Energy production and conversion];


Pssm-ID: 441506 [Multi-domain]  Cd Length: 365  Bit Score: 41.69  E-value: 3.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 156 AREVVRQVRNVT--ALPLIVKLSPN--------AENITQMAVMCEEEGADGVSLI--NTFSAMKIDIRRRRSVFANtyag 223
Cdd:COG1902  202 LLEVVEAVRAAVgpDFPVGVRLSPTdfveggltLEESVELAKALEEAGVDYLHVSsgGYEPDAMIPTIVPEGYQLP---- 277

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 515995497 224 lsgpaikpialrMVHQVAQAVSIPVIGMGGISSVEDIIEFTMAGAA 269
Cdd:COG1902  278 ------------FAARIRKAVGIPVIAVGGITTPEQAEAALASGDA 311
NMO pfam03060
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ...
 234-275 3.93e-04

Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane dioxygenase (NPD) (EC:1.13.11.32), is an FMN-dependent enzyme that uses molecular oxygen to oxidize (anionic) alkyl nitronates and, in the case of the enzyme from Neurospora crassa, (neutral) nitroalkanes to the corresponding carbonyl compounds and nitrite. Previously classified as 2-nitropropane dioxygenase, but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms. The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor. Active towards linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, towards propyl-2-nitronate. The enzyme from N. crassa can also utilize neutral nitroalkanes, but with lower activity. One atom of oxygen is incorporated into the carbonyl group of the aldehyde product. The reaction appears to involve the formation of an enzyme-bound nitronate radical and an a-peroxynitroethane species, which then decomposes, either in the active site of the enzyme or after release, to acetaldehyde and nitrite.


Pssm-ID: 367316 [Multi-domain]  Cd Length: 331  Bit Score: 41.73  E-value: 3.93e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 515995497  234 LRMVHQVAQAVSIPVIGMGGISSVEDIIEFTMAGAAAIQVGT 275
Cdd:pfam03060 182 FRLVPQVPDAVDIPVIAAGGIWDRRGVAAALALGASGVQMGT 223
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 224-275 5.03e-04

phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family consists of HisA, phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, the enzyme catalyzing the fourth step in histidine biosynthesis. It is closely related to the enzyme HisF for the sixth step. Examples of this enzyme in Actinobacteria have been found to be bifunctional, also possessing phosphoribosylanthranilate isomerase activity; the trusted cutoff here has now been raised to 275.0 to exclude the bifunctional group, now represented by model TIGR01919. HisA from Lactococcus lactis was reported to be inactive (MEDLINE:93322317). [Amino acid biosynthesis, Histidine family]


Pssm-ID: 272850 [Multi-domain]  Cd Length: 230  Bit Score: 40.65  E-value: 5.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 515995497  224 LSGPAIKPIAlrmvhQVAQAVSIPVIGMGGISSVEDIIEFTMAGAAAIQVGT 275
Cdd:TIGR00007 173 LSGPNFELTK-----ELVKAVNVPVIASGGVSSIDDLIALKKLGVYGVIVGK 219
Aldolase_Class_I cd00945
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ...
 75-271 5.99e-04

Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which stabilizes a reaction intermediates via Schiff base formation, and have TIM beta/alpha barrel fold. The members of this family include 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-4-hydroxyglutarate (KHG) aldolases, transaldolase, dihydrodipicolinate synthase sub-family, Type I 3-dehydroquinate dehydratase, DeoC and DhnA proteins, and metal-independent fructose-1,6-bisphosphate aldolase. Although structurally similar, the class II aldolases use a different mechanism and are believed to have an independent evolutionary origin.


Pssm-ID: 188634 [Multi-domain]  Cd Length: 201  Bit Score: 40.39  E-value: 5.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497  75 NPGVAAFLKDELDDMtrwNTAVIANVGGSNLEEYVQAVAMITENAqkrrtmNRRGVDMLELNISCPNVKQGgmqfgiQTE 154
Cdd:cd00945   33 NPGYVRLAADALAGS---DVPVIVVVGFPTGLTTTEVKVAEVEEA------IDLGADEIDVVINIGSLKEG------DWE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515995497 155 VAREVVRQVRNVTALPLIVK------LSPNAENITQMAVMCEEEGADGVSlintfsamkidirrrrsvfanTYAGLSGPA 228
Cdd:cd00945   98 EVLEEIAAVVEAADGGLPLKviletrGLKTADEIAKAARIAAEAGADFIK---------------------TSTGFGGGG 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 515995497 229 IKPIALRMVHQVAQAVsIPVIGMGGISSVEDIIEFTMAGAAAI 271
Cdd:cd00945  157 ATVEDVKLMKEAVGGR-VGVKAAGGIKTLEDALAAIEAGADGI 198
HisA_HisF cd04723
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ...
 230-285 9.58e-04

Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) and the cyclase subunit of imidazoleglycerol phosphate synthase (HisF). The ProFAR isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene. The Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.


Pssm-ID: 240074 [Multi-domain]  Cd Length: 233  Bit Score: 39.95  E-value: 9.58e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515995497 230 KPIALRMVHQVAQAVSIPVIGMGGISSVEDIIEFTMAGAAAIQVGTynfvHLHAGA 285
Cdd:cd04723  174 QGPDLELLERLAARADIPVIAAGGVRSVEDLELLKKLGASGALVAS----ALHDGG 225
HisF COG0107
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ...
 234-270 1.29e-03

Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; Imidazole glycerol phosphate synthase subunit HisF is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439877  Cd Length: 251  Bit Score: 39.62  E-value: 1.29e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 515995497 234 LRMVHQVAQAVSIPVIGMGGISSVEDIIE-FTMAGAAA 270
Cdd:COG0107  184 LELTRAVSEAVSIPVIASGGAGTLEHFVEvFTEGGADA 221
HisF cd04731
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ...
 234-270 1.68e-03

The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.


Pssm-ID: 240082  Cd Length: 243  Bit Score: 39.37  E-value: 1.68e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 515995497 234 LRMVHQVAQAVSIPVIGMGGISSVEDIIE-FTMAGAAA 270
Cdd:cd04731  182 LELIRAVSSAVNIPVIASGGAGKPEHFVEaFEEGGADA 219
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 224-274 1.93e-03

HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene.


Pssm-ID: 240083  Cd Length: 234  Bit Score: 39.00  E-value: 1.93e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515995497 224 LSGPAIKPIAlrmvhQVAQAVSIPVIGMGGISSVEDIIEFTMAGAAAIQVG 274
Cdd:cd04732  174 LSGPNFELYK-----ELAAATGIPVIASGGVSSLDDIKALKELGVAGVIVG 219
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 230-275 4.63e-03

Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.


Pssm-ID: 425971  Cd Length: 228  Bit Score: 37.84  E-value: 4.63e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 515995497  230 KPIALRMVHQVAQAVSIPV-IGmGGISSVEDIIEFTMAGAAAIQVGT 275
Cdd:pfam00977  58 RPVNLDVVEEIAEEVFIPVqVG-GGIRSLEDVERLLSAGADRVIIGT 103
PcrB COG1646
Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];
225-275 8.32e-03

Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];


Pssm-ID: 441252  Cd Length: 241  Bit Score: 37.06  E-value: 8.32e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 515995497 225 SGPAIKPIALRMVHQVAQAVS-IPVIGMGGISSVEDIIEFTMAGAAAIQVGT 275
Cdd:COG1646  175 GSGAGEPVDPEMVKAVKKALEdTPLIYGGGIRSPEKAREMAEAGADTIVVGN 226
PRK00748 PRK00748
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 224-260 9.14e-03

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated


Pssm-ID: 179108  Cd Length: 233  Bit Score: 36.97  E-value: 9.14e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 515995497 224 LSGPAIKpiALRmvhQVAQAVSIPVIGMGGISSVEDI 260
Cdd:PRK00748 174 LSGPNVE--ATR---ELAAAVPIPVIASGGVSSLDDI 205
 
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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