|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
7-306 |
4.49e-172 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 478.88 E-value: 4.49e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 7 DLRVRLGPLELKNPVIAASGTFGYGEEYASLVDLNQIGAIVVKGLSLKPKSGNPPPRIVETNGGMLNAIGLANVGVETFI 86
Cdd:PRK07259 1 RLSVELPGLKLKNPVMPASGTFGFGGEYARFYDLNGLGAIVTKSTTLEPREGNPTPRIAETPGGMLNAIGLQNPGVDAFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 87 REKLPVLRKYDTRIIANIYGHHIDEYGDLASMLKGVEGIAALEVNISCPNVECGGMVFGVDPDVSARVTERVLKNTDKPV 166
Cdd:PRK07259 81 EEELPWLEEFDTPIIANVAGSTEEEYAEVAEKLSKAPNVDAIELNISCPNVKHGGMAFGTDPELAYEVVKAVKEVVKVPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 167 IMKLTPNVTDIRVIARAVESAGAHAISLINTLTGMAIDVDSRTPKLANIYGGLSGPAIRPVAVFMVYQAASSVRIPVIGM 246
Cdd:PRK07259 161 IVKLTPNVTDIVEIAKAAEEAGADGLSLINTLKGMAIDIKTRKPILANVTGGLSGPAIKPIALRMVYQVYQAVDIPIIGM 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 247 GGIMDARDALEFIIAGASAVQVGTANFVDPAATLDVLDGIRGYCEKHGIGRIQEIVGTLK 306
Cdd:PRK07259 241 GGISSAEDAIEFIMAGASAVQVGTANFYDPYAFPKIIEGLEAYLDKYGIKSIEEIVGIAH 300
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
10-305 |
1.89e-159 |
|
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: 446.61 E-value: 1.89e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 10 VRLGPLELKNPVIAASGTFGYGEEYASLVDLNQIGAIVVKGLSLKPKSGNPPPRIVETNGGMLNAIGLANVGVETFIREK 89
Cdd:cd04740 2 VELAGLRLKNPVILASGTFGFGEELSRVADLGKLGAIVTKSITLEPREGNPPPRVVETPGGMLNAIGLQNPGVEAFLEEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 90 LPVLRKYDTRIIANIYGHHIDEYGDLASMLKGVeGIAALEVNISCPNVECGGMVFGVDPDVSARVTERVLKNTDKPVIMK 169
Cdd:cd04740 82 LPWLREFGTPVIASIAGSTVEEFVEVAEKLADA-GADAIELNISCPNVKGGGMAFGTDPEAVAEIVKAVKKATDVPVIVK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 170 LTPNVTDIRVIARAVESAGAHAISLINTLTGMAIDVDSRTPKLANIYGGLSGPAIRPVAVFMVYQAASSVRIPVIGMGGI 249
Cdd:cd04740 161 LTPNVTDIVEIARAAEEAGADGLTLINTLKGMAIDIETRKPILGNVTGGLSGPAIKPIALRMVYQVYKAVEIPIIGVGGI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1308832086 250 MDARDALEFIIAGASAVQVGTANFVDPAATLDVLDGIRGYCEKHGIGRIQEIVGTL 305
Cdd:cd04740 241 ASGEDALEFLMAGASAVQVGTANFVDPEAFKEIIEGLEAYLDEEGIKSIEELVGLA 296
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
7-298 |
4.87e-138 |
|
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: 392.51 E-value: 4.87e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 7 DLRVRLGPLELKNPVIAASGTFGYGEEYASLVDLNQIGAIVVKGLSLKPKSGNPPPRIVET--NGGMLNAIGLANVGVET 84
Cdd:COG0167 1 DLSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLpeDSGLINRMGLNNPGVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 85 FIREKLPvLRKYDTRIIANIYGHHIDEYGDLASMLKGVeGIAALEVNISCPNVECGGMVFGVDPDVSARVTERVLKNTDK 164
Cdd:COG0167 81 FLERLLP-AKRYDVPVIVNIGGNTVEDYVELARRLADA-GADYLELNISCPNTPGGGRALGQDPEALAELLAAVKAATDK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 165 PVIMKLTPNVTDIRVIARAVESAGAHAISLINTLTGMAIDVDSRTPKLANIYGGLSGPAIRPVAVFMVYQAASSV--RIP 242
Cdd:COG0167 159 PVLVKLAPDLTDIVEIARAAEEAGADGVIAINTTLGRAIDLETRRPVLANEAGGLSGPALKPIALRMVREVAQAVggDIP 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1308832086 243 VIGMGGIMDARDALEFIIAGASAVQVGTANFVD-PAATLDVLDGIRGYCEKHGIGRI 298
Cdd:COG0167 239 IIGVGGISTAEDALEFILAGASAVQVGTALFYEgPGLVRRIIRGLEAYLEEKGFSSI 295
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
8-303 |
7.33e-120 |
|
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: 346.72 E-value: 7.33e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 8 LRVRLGPLELKNPVIAASGTFGYGEEYASLVDLNQIGAIVVKGLSLKPKSGNPPPRIVETNGGMLNAIGLANVGVETFIR 87
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTIVETPCGMLNAIGLQNPGVEAFLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 88 EKLPVLRKYDTRIIANIYGHHIDEYGDLA-SMLKGVEGIAALEVNISCPNVECGGMVFGVDPDVSARVTERVLKNTDKPV 166
Cdd:TIGR01037 81 ELKPVREEFPTPLIASVYGSSVEEFAEVAeKLEKAPPYVDAYELNLSCPHVKGGGIAIGQDPELSADVVKAVKDKTDVPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 167 IMKLTPNVTDIRVIARAVESAGAHAISLINTLTGMAIDVDSRTPKLANIYGGLSGPAIRPVAVFMVYQAASSVRIPVIGM 246
Cdd:TIGR01037 161 FAKLSPNVTDITEIAKAAEEAGADGLTLINTLRGMKIDIKTGKPILANKTGGLSGPAIKPIALRMVYDVYKMVDIPIIGV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1308832086 247 GGIMDARDALEFIIAGASAVQVGTANFVDPAATLDVLDGIRGYCEKHGIGRIQEIVG 303
Cdd:TIGR01037 241 GGITSFEDALEFLMAGASAVQVGTAVYYRGFAFKKIIEGLIAFLKAEGFTSIEELIG 297
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
8-286 |
7.16e-83 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 252.27 E-value: 7.16e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 8 LRVRLGPLELKNPVIAASGTFGYGEEYASLVDLNQIGAIVVKGLSLKPKSGNPPPRIVETNGGMLNAIGLANVGVETFIR 87
Cdd:pfam01180 2 LATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVTPYPQPGNPTPRVFRLPEGVLNRMGLNNPGLDAVLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 88 EKLPVLRKY---DTRIIANIYGHHIDEYGDLASMLKGVEGIaaLEVNISCPNVEcGGMVFGVDPDVSARVTERVLKNTDK 164
Cdd:pfam01180 82 ELLKRRKEYprpDLGINLSKAGMTVDDYVEVARKIGPFADY--IELNVSCPNTP-GLRALQTDPELAAILLKVVKEVSKV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 165 PVIMKLTPNVTDIRVIARAVESAGAHAISLIN----TLTGMAIDVDSRTPKLANIYGGLSGPAIRPVAVFMVYQAASSV- 239
Cdd:pfam01180 159 PVLVKLAPDLTDIVIIDIADVALGEDGLDGINatntTVRGMRIDLKTEKPILANGTGGLSGPPIKPIALKVIRELYQRTg 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1308832086 240 -RIPVIGMGGIMDARDALEFIIAGASAVQVGTAN-FVDPAATLDVLDGI 286
Cdd:pfam01180 239 pEIPIIGVGGIESGEDALEKILAGASAVQIGTALiFGGPFIFPKIIDEL 287
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
10-273 |
1.17e-61 |
|
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: 197.96 E-value: 1.17e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 10 VRLGPLELKNPVIAASGTFGYGEEYASLVDLNQIGAIVVKGLSLKPKSGNPPPRIVETNG---------GMLNAIGLANV 80
Cdd:cd02810 1 VNFLGLKLKNPFGVAAGPLLKTGELIARAAAAGFGAVVYKTVTLHPRPGNPLPRVARLPPegesypeqlGILNSFGLPNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 81 GVETFIREKLPVLRKYDTR-IIANIYGHHIDEYGDLASMLkGVEGIAALEVNISCPNVEcGGMVFGVDPDVSARVTERVL 159
Cdd:cd02810 81 GLDVWLQDIAKAKKEFPGQpLIASVGGSSKEDYVELARKI-ERAGAKALELNLSCPNVG-GGRQLGQDPEAVANLLKAVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 160 KNTDKPVIMKLTPNVTDIRV--IARAVESAGAHAISLINTLTGMAIDVDSRTPKLANIYGGLSGPAIRPVAVFMVYQAAS 237
Cdd:cd02810 159 AAVDIPLLVKLSPYFDLEDIveLAKAAERAGADGLTAINTISGRVVDLKTVGPGPKRGTGGLSGAPIRPLALRWVARLAA 238
|
250 260 270
....*....|....*....|....*....|....*...
gi 1308832086 238 SV--RIPVIGMGGIMDARDALEFIIAGASAVQVGTANF 273
Cdd:cd02810 239 RLqlDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALM 276
|
|
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
44-271 |
3.42e-47 |
|
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: 160.53 E-value: 3.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 44 GAIVVKGLSL-KPKSGNPPPRIVETNGGMLNAIGLANV------GVETFIREKLPVLRKYDTRI-IANIYGHHIDEygDL 115
Cdd:cd02940 38 GGAVTKTLGLdKDIVTNVSPRIARLRTSGRGQIGFNNIelisekPLEYWLKEIRELKKDFPDKIlIASIMCEYNKE--DW 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 116 ASMLKGVE--GIAALEVNISCPNvECG----GMVFGVDPDVSARVTERVLKNTDKPVIMKLTPNVTDIRVIARAVESAGA 189
Cdd:cd02940 116 TELAKLVEeaGADALELNFSCPH-GMPergmGAAVGQDPELVEEICRWVREAVKIPVIAKLTPNITDIREIARAAKEGGA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 190 HAISLINTLTG-MAIDVDSRTPKLA----NIYGGLSGPAIRPVAVFMVYQAASSV--RIPVIGMGGIMDARDALEFIIAG 262
Cdd:cd02940 195 DGVSAINTVNSlMGVDLDGTPPAPGvegkTTYGGYSGPAVKPIALRAVSQIARAPepGLPISGIGGIESWEDAAEFLLLG 274
|
....*....
gi 1308832086 263 ASAVQVGTA 271
Cdd:cd02940 275 ASVVQVCTA 283
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
83-317 |
1.62e-44 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 156.64 E-value: 1.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 83 ETFIREKLPVLRKYDTR-IIANIYGHHIDEygDLASMLKGVE--GIAALEVNISCPNVEC-GGM--VFGVDPDVSARVTE 156
Cdd:PRK08318 84 EVNLREIRRVKRDYPDRaLIASIMVECNEE--EWKEIAPLVEetGADGIELNFGCPHGMSeRGMgsAVGQVPELVEMYTR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 157 RVLKNTDKPVIMKLTPNVTDIRVIARAVESAGAHAISLINTLTG-MAIDVDSRTPkLANI-----YGGLSGPAIRPVAVF 230
Cdd:PRK08318 162 WVKRGSRLPVIVKLTPNITDIREPARAAKRGGADAVSLINTINSiTGVDLDRMIP-MPIVngkssHGGYCGPAVKPIALN 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 231 MVYQAASS---VRIPVIGMGGIMDARDALEFIIAGASAVQVGTA------NFVDpaatlDVLDGIRGYCEKHGIGRIQEI 301
Cdd:PRK08318 241 MVAEIARDpetRGLPISGIGGIETWRDAAEFILLGAGTVQVCTAamqygfRIVE-----DMISGLSHYMDEKGFASLEDM 315
|
250
....*....|....*.
gi 1308832086 302 VGtlkskTSLPQISDP 317
Cdd:PRK08318 316 VG-----LAVPNVTDW 326
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
7-271 |
3.94e-37 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 134.70 E-value: 3.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 7 DLRVRLGPLELKNPVIAASGTFGYGEEYASLVDLNQIGAIVVKGLSLKPKSGNPPPRIVETNGGMLNAIGLANVGvetfI 86
Cdd:PRK02506 1 STSTQIAGFKFDNCLMNAAGVYCMTKEELEEVEASAAGAFVTKSATLEPRPGNPEPRYADTPLGSINSMGLPNLG----F 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 87 REKLPVLRKYDT-----RIIANIYGHHIDEYGDLASMLKGVEGIAALEVNISCPNVEcGGMVFGVDPDVSARVTERVLKN 161
Cdd:PRK02506 77 DYYLDYVLELQKkgpnkPHFLSVVGLSPEETHTILKKIQASDFNGLVELNLSCPNVP-GKPQIAYDFETTEQILEEVFTY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 162 TDKPVIMKLTPNVtDIRVIARAVESAGAHAISLINTL----TGMAIDVDSRT----PKlaNIYGGLSGPAIRPVAVFMV- 232
Cdd:PRK02506 156 FTKPLGVKLPPYF-DIVHFDQAAAIFNKFPLAFVNCInsigNGLVIDPEDETvvikPK--NGFGGIGGDYIKPTALANVr 232
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1308832086 233 --YQAASSvRIPVIGMGGIMDARDALEFIIAGASAVQVGTA 271
Cdd:PRK02506 233 afYQRLNP-SIQIIGTGGVKTGRDAFEHILCGASMVQVGTA 272
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
10-271 |
1.06e-29 |
|
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: 114.34 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 10 VRLGPLELKNPVIAASGTFGYGEEyaslvDLNQI-----GAIVVKGLSLKPKSGNPPPRIVETNGGMLNAIGLANVGVET 84
Cdd:cd04741 1 VTPPGLTISPPLMNAAGPWCTTLE-----DLLELaasstGAVTTRSSTLAGRPGNPEPRYYAFPLGSINSLGLPNLGLDY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 85 ---FIREKLPVLRKYDTRIIANIYGHHIDE---YGDLASMLKGVEGiaALEVNISCPNVecGGM-VFGVDPDVSARVTER 157
Cdd:cd04741 76 yleYIRTISDGLPGSAKPFFISVTGSAEDIaamYKKIAAHQKQFPL--AMELNLSCPNV--PGKpPPAYDFDATLEYLTA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 158 VLKNTDKPVIMKLTPnVTDIRVIARAVESAGAHAISL-----INTL-TGMAIDVDSRTP--KLANIYGGLSGPAIRPVAV 229
Cdd:cd04741 152 VKAAYSIPVGVKTPP-YTDPAQFDTLAEALNAFACPIsfitaTNTLgNGLVLDPERETVvlKPKTGFGGLAGAYLHPLAL 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1308832086 230 FMVYQ--AASSVRIPVIGMGGIMDARDALEFIIAGASAVQVGTA 271
Cdd:cd04741 231 GNVRTfrRLLPSEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTA 274
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
1-271 |
1.09e-28 |
|
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: 112.59 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 1 MDHQQPDLRVRLGPLELKNPV-IAAsgtfGY---GEEYASLVDLNqIGAIVVKGLSLKPKSGNPPPRI---VEtNGGMLN 73
Cdd:cd04738 32 LVYDDPRLEVEVFGLTFPNPVgLAA----GFdknAEAIDALLALG-FGFVEVGTVTPRPQPGNPKPRLfrlPE-DEALIN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 74 AIGLANVGVETFIReKLPVLRKYDTRIIANI----YGHHIDEYGDLASMLKGVEGIA-ALEVNISCPNVEcggmvfG--- 145
Cdd:cd04738 106 RMGFNNDGADAVAK-RLKKRRPRGGPLGVNIgknkDTPLEDAVEDYVIGVRKLGPYAdYLVVNVSSPNTP------Glrd 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 146 ------VDPDVSARVTERVLKNTDKPVIMKLTPNVTD--IRVIARAVESAGAHAISLINTLTgmaidvdSRTP----KLA 213
Cdd:cd04738 179 lqgkeaLRELLTAVKEERNKLGKKVPLLVKIAPDLSDeeLEDIADVALEHGVDGIIATNTTI-------SRPGllrsPLA 251
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1308832086 214 NIYGGLSGPAIRPVA---VFMVYQAASSvRIPVIGMGGIMDARDALEFIIAGASAVQVGTA 271
Cdd:cd04738 252 NETGGLSGAPLKERStevLRELYKLTGG-KIPIIGVGGISSGEDAYEKIRAGASLVQLYTG 311
|
|
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
6-304 |
2.00e-28 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 113.01 E-value: 2.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 6 PDLRVRLGPLELKNPVIAASGTFGYGEEYASLVDLNQIGAIVVKGLSL-KPKSGNPPPRIVETNGGMLNA-----IGLAN 79
Cdd:PLN02495 9 PDLSVTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGGVIAKTVSLdASKVINVTPRYARLRAGANGSakgrvIGWQN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 80 VGV------ETFIREKLPVLRKYDTRI-IANIyghhIDEYGDLA--SMLKGVE--GIAALEVNISCPNvecG------GM 142
Cdd:PLN02495 89 IELisdrpfETMLAEFKQLKEEYPDRIlIASI----MEEYNKDAweEIIERVEetGVDALEINFSCPH---GmperkmGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 143 VFGVDPDVSARVTERVLKNTDKPVIMKLTPNVTDIRVIARAVESAGAHAISLINTLTG-MAIDVDSRTPKLA----NIYG 217
Cdd:PLN02495 162 AVGQDCDLLEEVCGWINAKATVPVWAKMTPNITDITQPARVALKSGCEGVAAINTIMSvMGINLDTLRPEPCvegySTPG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 218 GLSGPAIRPVAVFMVYQAASSVR------IPVIGMGGIMDARDALEFIIAGASAVQVGTANFVDPAATLDVL-DGIRGYC 290
Cdd:PLN02495 242 GYSSKAVRPIALAKVMAIAKMMKsefpedRSLSGIGGVETGGDAAEFILLGADTVQVCTGVMMHGYPLVKNLcAELQDFM 321
|
330
....*....|....
gi 1308832086 291 EKHGIGRIQEIVGT 304
Cdd:PLN02495 322 KKHNFSSIEDFRGA 335
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
6-294 |
1.32e-23 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 99.08 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 6 PDLRVRLGPLELKNPV-IAAsgtfGY---GEEYASLVDLNqIGAIVVKGLSLKPKSGNPPPRI---VETNGgMLNAIGLA 78
Cdd:PRK05286 47 PRLPVTVMGLTFPNPVgLAA----GFdknGEAIDALGALG-FGFVEVGTVTPRPQPGNPKPRLfrlPEDEA-LINRMGFN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 79 NVGVETFIREklpvLRKYDTRII--ANI-------YGHHIDEYgdLASMlKGVEGIAA-LEVNISCPNVEcggmvfG--- 145
Cdd:PRK05286 121 NDGADALAER----LKKAYRGIPlgINIgknkdtpLEDAVDDY--LICL-EKLYPYADyFTVNISSPNTP------Glrd 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 146 ------VDPDVSARVTERVLKNTDKPVIMKLTPNVTD--IRVIARAVESAGAHAISLINTlTgmaIDVDS-RTPKLANIY 216
Cdd:PRK05286 188 lqygeaLDELLAALKEAQAELHGYVPLLVKIAPDLSDeeLDDIADLALEHGIDGVIATNT-T---LSRDGlKGLPNADEA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 217 GGLSGPAIRPVAVFMVYQAASSV--RIPVIGMGGIMDARDALEFIIAGASAVQVGTAnFV--DPAATLDVLDGIRGYCEK 292
Cdd:PRK05286 264 GGLSGRPLFERSTEVIRRLYKELggRLPIIGVGGIDSAEDAYEKIRAGASLVQIYSG-LIyeGPGLVKEIVRGLARLLRR 342
|
..
gi 1308832086 293 HG 294
Cdd:PRK05286 343 DG 344
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
3-271 |
6.43e-17 |
|
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate dehydrogenase exclusively for subfamily 2. It includes members from bacteria, yeast, plants etc. The subfamilies 1 and 2 share extensive homology, particularly toward the C-terminus. This subfamily has a longer N-terminal region. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273408 Cd Length: 335 Bit Score: 79.83 E-value: 6.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 3 HQQPDLRVRLGPLELKNPVIAASGTFGYGEEYASLVDLNqIGAIVVKGLSLKPKSGNPPPRI---VETNGgMLNAIGLAN 79
Cdd:TIGR01036 41 GASDPLEVTVLGLKFPNPLGLAAGFDKDGEAIDALGAMG-FGFLEIGTVTPKPQPGNPRPRLfrlIEDEA-LINRMGFNN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 80 VGVETFIREklpvLRK--YDTRIIANI-------YGHHIDEYGDLASMLKGVEGIaaLEVNISCPNVEcgGM-----VFG 145
Cdd:TIGR01036 119 HGADVLVER----LKRarYKGPIGINIgknkdtpSEDAKEDYAACLRKLGPLADY--LVVNVSSPNTP--GLrdlqyKAE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 146 VDPDVSARVTERVLKNTDK--PVIMKLTPNVT--DIRVIARAVESAGAHAISLINTltgmAIDVDS-RTPKLANIYGGLS 220
Cdd:TIGR01036 191 LRDLLTAVKQEQDGLRRVHrvPVLVKIAPDLTesDLEDIADSLVELGIDGVIATNT----TVSRSLvQGPKNSDETGGLS 266
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1308832086 221 GPAIRPVAVFMVYQAASSV--RIPVIGMGGIMDARDALEFIIAGASAVQVGTA 271
Cdd:TIGR01036 267 GKPLQDKSTEIIRRLYAELqgRLPIIGVGGISSAQDALEKIRAGASLLQIYSG 319
|
|
| DHOD_like |
cd04739 |
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
7-305 |
1.35e-16 |
|
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: 78.81 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 7 DLRVRLGPLELKNPVIAASGTFGYGEEYASLVDLNQIGAIVVKGL--------------SLKPKSGNPPPRivetngGML 72
Cdd:cd04739 1 DLSTTYLGLSLKNPLVASASPLSRNLDNIRRLEDAGAGAIVLPSLfeeqiereaqeldrFLTYGSSFAEAL------SYF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 73 NAIGLANVGVETFIREKLPVLRKYDTRIIANIYGHHIDEYGDLASMLKGVeGIAALEVNIscpnvecggMVFGVDPDVSA 152
Cdd:cd04739 75 PEYGRYNLGPEEYLELIRRAKRAVSIPVIASLNGVSAGGWVDYARQIEEA-GADALELNI---------YALPTDPDISG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 153 RVTE-------RVLKNTDK-PVIMKLTPNVTDIRVIARAVESAGAHAISLINTLTGMAIDVDSRTPKLANIyggLSGPA- 223
Cdd:cd04739 145 AEVEqryldilRAVKSAVTiPVAVKLSPFFSALAHMAKQLDAAGADGLVLFNRFYQPDIDLETLEVVPNLL---LSSPAe 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 224 ----IRPVAvfmvyQAASSVRIPVIGMGGIMDARDALEFIIAGASAVQVGTA---NFVDPAATLdvLDGIRGYCEKHGIG 296
Cdd:cd04739 222 irlpLRWIA-----ILSGRVKASLAASGGVHDAEDVVKYLLAGADVVMTTSAllrHGPDYIGTL--LAGLEAWMEEHGYE 294
|
....*....
gi 1308832086 297 RIQEIVGTL 305
Cdd:cd04739 295 SVQQLRGSM 303
|
|
| PRK07565 |
PRK07565 |
dihydroorotate dehydrogenase-like protein; |
100-317 |
1.86e-14 |
|
dihydroorotate dehydrogenase-like protein;
Pssm-ID: 236051 Cd Length: 334 Bit Score: 72.98 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 100 IIANIYGHHIDEYGDLASMLKGVeGIAALEVNIscpnvecggMVFGVDPDVSAR--------VTERVLKNTDKPVIMKLT 171
Cdd:PRK07565 104 VIASLNGSSAGGWVDYARQIEQA-GADALELNI---------YYLPTDPDISGAeveqryldILRAVKSAVSIPVAVKLS 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 172 PNVTDIRVIARAVESAGAHAISLINTLTGMAIDVDSRTPKLANIyggLSGPA-----IRPVAvfMVYqaaSSVRIPVIGM 246
Cdd:PRK07565 174 PYFSNLANMAKRLDAAGADGLVLFNRFYQPDIDLETLEVVPGLV---LSTPAelrlpLRWIA--ILS---GRVGADLAAT 245
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308832086 247 GGIMDARDALEFIIAGASAVQVGTA---NFVDPAATLdvLDGIRGYCEKHGIGRIQEIVGTLksktSLPQISDP 317
Cdd:PRK07565 246 TGVHDAEDVIKMLLAGADVVMIASAllrHGPDYIGTI--LRGLEDWMERHGYESLQQFRGSM----SQKNVPDP 313
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
6-271 |
1.39e-11 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 64.76 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 6 PDLRVRLGPLELKNPVIAASGTFGYGEEYASLVDLNqIGAIVVKGLSLKPKSGNPPPRI--VETNGGMLNAIGLANVGVE 83
Cdd:PLN02826 72 SVLGVEVWGRTFSNPIGLAAGFDKNAEAVEGLLGLG-FGFVEIGSVTPLPQPGNPKPRVfrLREEGAIINRYGFNSEGIV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 84 TfIREKLPVL---RKYDTRIIANIYGHHIDEYGDLASMLKGV----------------EGIAALE-------VNISCPNV 137
Cdd:PLN02826 151 A-VAKRLGAQhgkRKLDETSSSSFSSDDVKAGGKAGPGILGVnlgknktsedaaadyvQGVRALSqyadylvINVSSPNT 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 138 ecggmvfgvdPD--------VSARVTERVLKNTDK---------PVIMKLTPNVT--DIRVIARAVESAGAHAISLINTL 198
Cdd:PLN02826 230 ----------PGlrklqgrkQLKDLLKKVLAARDEmqwgeegppPLLVKIAPDLSkeDLEDIAAVALALGIDGLIISNTT 299
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308832086 199 TGMAIDVDSRtpKLANIYGGLSGPAIRPVAVFMVYQ--AASSVRIPVIGMGGIMDARDALEFIIAGASAVQVGTA 271
Cdd:PLN02826 300 ISRPDSVLGH--PHADEAGGLSGKPLFDLSTEVLREmyRLTRGKIPLVGCGGVSSGEDAYKKIRAGASLVQLYTA 372
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
217-271 |
1.86e-07 |
|
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: 50.94 E-value: 1.86e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1308832086 217 GGLSGPAIRPVAVFmVYQAASSVRIPVIGMGGIMDARDALEFIIAGASAVQVGTA 271
Cdd:cd04730 134 GGHRGTFDIGTFAL-VPEVRDAVDIPVIAAGGIADGRGIAAALALGADGVQMGTR 187
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
81-270 |
2.22e-07 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 50.66 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 81 GVETFIREKLP-VLRKYDTRIIANIYGHHIDEYGDLASMLKGVEGIAALEVNISCPNVecggmvFGVDPDVSARVTERVL 159
Cdd:cd04722 40 EAETDDKEVLKeVAAETDLPLGVQLAINDAAAAVDIAAAAARAAGADGVEIHGAVGYL------AREDLELIRELREAVP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 160 kntDKPVIMKLTPNVTDIRviaRAVESAGAHAIslintltgmaidvdsrtpKLANIYGGLSGPAIRPVAVFMVYQAASSV 239
Cdd:cd04722 114 ---DVKVVVKLSPTGELAA---AAAEEAGVDEV------------------GLGNGGGGGGGRDAVPIADLLLILAKRGS 169
|
170 180 190
....*....|....*....|....*....|.
gi 1308832086 240 RIPVIGMGGIMDARDALEFIIAGASAVQVGT 270
Cdd:cd04722 170 KVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
147-277 |
3.72e-07 |
|
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: 50.19 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 147 DPDVSARVTERVLKNTDKPVIMKltpnvtdIRV----------IARAVESAGAHAISlintltgmaidVDSRTPKLaniy 216
Cdd:cd02801 107 DPELVAEIVRAVREAVPIPVTVK-------IRLgwddeeetleLAKALEDAGASALT-----------VHGRTREQ---- 164
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1308832086 217 gGLSGPAIRPVavfmVYQAASSVRIPVIGMGGIMDARDALEFI-IAGASAVQVGTANFVDPA 277
Cdd:cd02801 165 -RYSGPADWDY----IAEIKEAVSIPVIANGDIFSLEDALRCLeQTGVDGVMIGRGALGNPW 221
|
|
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
232-271 |
9.08e-07 |
|
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];
Pssm-ID: 441673 [Multi-domain] Cd Length: 302 Bit Score: 49.72 E-value: 9.08e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1308832086 232 VYQAASSVRIPVIGMGGIMDARDALEFIIAGASAVQVGTA 271
Cdd:COG2070 150 VPEVRDAVDIPVIAAGGIADGRGIAAALALGADGVQMGTR 189
|
|
| NMO |
pfam03060 |
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ... |
134-271 |
2.53e-06 |
|
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: 48.28 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 134 CPNVECGGMVFGVDPDVsaRVTERVLKNTDKPVIMKLTPNVTDirVIARaVESAGAHAISLINTLTGMAIdVDSRTPKLA 213
Cdd:pfam03060 87 LGNNALGYNIEEGVPDY--GKVLVDLDEGVNVVSFGFGLPPND--VVFR-LHFAGVALIPTISSAKEARI-AEARGADAL 160
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308832086 214 NIYGGLSG-----PAIRPVAVF-MVYQAASSVRIPVIGMGGIMDARDALEFIIAGASAVQVGTA 271
Cdd:pfam03060 161 IVQGPEAGghqgtPEYGDKGLFrLVPQVPDAVDIPVIAAGGIWDRRGVAAALALGASGVQMGTR 224
|
|
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
104-269 |
9.03e-06 |
|
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: 46.63 E-value: 9.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 104 IYGHHIDeygDLASMLKGVEGIAALEVNISC----PNVECGGmvFGV----DPDVSARVTERVLKNTDKPVIMKL----- 170
Cdd:COG0042 68 LFGSDPE---ELAEAARIAEELGADEIDINMgcpvKKVTKGG--AGAallrDPELVAEIVKAVVEAVDVPVTVKIrlgwd 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 171 --TPNVTDIrviARAVESAGAHAIslinTLTGmaidvdsRTPklANIYgglSGPAIRPVavfmVYQAASSVRIPVIGMGG 248
Cdd:COG0042 143 ddDENALEF---ARIAEDAGAAAL----TVHG-------RTR--EQRY---KGPADWDA----IARVKEAVSIPVIGNGD 199
|
170 180
....*....|....*....|..
gi 1308832086 249 IMDARDALEFI-IAGASAVQVG 269
Cdd:COG0042 200 IFSPEDAKRMLeETGCDGVMIG 221
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
121-277 |
6.61e-05 |
|
Dihydrouridine synthase (Dus); 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 archae. 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. Dus 1 from Saccharomyces cerevisiae acts on pre-tRNA-Phe, while Dus 2 acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD. Some family members may be targeted to the mitochondria and even have a role in mitochondria.
Pssm-ID: 426126 Cd Length: 309 Bit Score: 43.85 E-value: 6.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 121 GVEGIaalEVNISCP----NVECGGMVFGVDPDVSARVTERVLKNTDKPVIMKltpnvtdIRV-----------IARAVE 185
Cdd:pfam01207 79 GADGI---DINMGCPskkvTRGGGGAALLRNPDLVAQIVKAVVKAVGIPVTVK-------IRIgwddshenaveIAKIVE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 186 SAGAHAIslinTLTGmaidvdsRTPKlaniyGGLSGPAIRPVavfmVYQAASSVRIPVIGMGGIMDARDA---LEFIiaG 262
Cdd:pfam01207 149 DAGAQAL----TVHG-------RTRA-----QNYEGTADWDA----IKQVKQAVSIPVIANGDITDPEDAqrcLAYT--G 206
|
170
....*....|....*
gi 1308832086 263 ASAVQVGTANFVDPA 277
Cdd:pfam01207 207 ADGVMIGRGALGNPW 221
|
|
| arch_FMN |
cd02911 |
Archeal FMN-binding domain. This family of archaeal proteins are part of the NAD(P)H-dependent ... |
85-271 |
1.31e-03 |
|
Archeal FMN-binding domain. This family of archaeal proteins are part of the NAD(P)H-dependent flavin oxidoreductase (oxidored) FMN-binding 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. The specific function of this group is unknown.
Pssm-ID: 239237 [Multi-domain] Cd Length: 233 Bit Score: 39.62 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 85 FIREKLPVLRKYDTRIIANIYGHHIDEYGDLASMLKGVEGIaaLEVNISC---PNVECG-GMVFGVDPDVSARVTERvLK 160
Cdd:cd02911 60 FIEGEIKALKDSNVLVGVNVRSSSLEPLLNAAALVAKNAAI--LEINAHCrqpEMVEAGaGEALLKDPERLSEFIKA-LK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 161 NTDKPVIMKLTPNVT-DIRVIARAVESAGAHAISLINTLTGMAIDVDsrtpKLANIygglsgpairpvavfmvyqaasSV 239
Cdd:cd02911 137 ETGVPVSVKIRAGVDvDDEELARLIEKAGADIIHVDAMDPGNHADLK----KIRDI----------------------ST 190
|
170 180 190
....*....|....*....|....*....|..
gi 1308832086 240 RIPVIGMGGIMDARDALEFIIAGASAVQVGTA 271
Cdd:cd02911 191 ELFIIGNNSVTTIESAKEMFSYGADMVSVARA 222
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
149-276 |
1.45e-03 |
|
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: 39.86 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 149 DVSARVTERVLKntDKPVIMKLTPN--------VTDIRVIARAVESAGAHAIslintltgmaiDVDSRTPKLANIYgglS 220
Cdd:cd02803 196 EIVAAVREAVGP--DFPVGVRLSADdfvpggltLEEAIEIAKALEEAGVDAL-----------HVSGGSYESPPPI---I 259
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1308832086 221 GPAIRPVAVF--MVYQAASSVRIPVIGMGGIMDARDALEFIIAG-ASAVQVGTANFVDP 276
Cdd:cd02803 260 PPPYVPEGYFleLAEKIKKAVKIPVIAVGGIRDPEVAEEILAEGkADLVALGRALLADP 318
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
151-287 |
6.98e-03 |
|
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only]; FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440915 [Multi-domain] Cd Length: 357 Bit Score: 37.80 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 151 SARVT--ERVLKNTDKPVIMKL--TPNVTDIRVIARAVESAGAHAISL-INTLTGMAIDVDSRT-------PKLANIYGG 218
Cdd:COG1304 108 TQSTTslEEVAAAAPAPLWFQLyvPKDRGFTDDLLRRAEAAGADALVLtVDTPVLGRRERDLREgfsqpprLTPRNLLEA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832086 219 LSGPA----IRPVAVFMVYQAASSV------------RIPVIgMGGIMDARDALEFIIAGASAVQV----GTAnfVDPA- 277
Cdd:COG1304 188 ATHPRwalgLASLAAWLDTNFDPSLtwddiawlrerwPGPLI-VKGVLSPEDARRAVDAGVDGIDVsnhgGRQ--LDGGp 264
|
170
....*....|
gi 1308832086 278 ATLDVLDGIR 287
Cdd:COG1304 265 PTIDALPEIR 274
|
|
| |
