|
Name |
Accession |
Description |
Interval |
E-value |
| DHOD_e_trans |
cd06218 |
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ... |
9-254 |
3.47e-100 |
|
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster.
Pssm-ID: 99814 [Multi-domain] Cd Length: 246 Bit Score: 292.14 E-value: 3.47e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 9 VVSQREVAYNIFEMVLKGTLVDEMDLPGQFLHLAVPNG-AMLLRRPISISSWDKRAKTCTILYRIGDEttGTYKLSKLES 87
Cdd:cd06218 1 VLSNREIADDIYRLVLEAPEIAAAAKPGQFVMLRVPDGsDPLLRRPISIHDVDPEEGTITLLYKVVGK--GTRLLSELKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 88 GAKVDVMGPLGNGFPVAEvtSTDKILIIGGGIGVPPLYELAKQLEKTGCQMTILLGFASENVKILENEFSNLKnVTLKIA 167
Cdd:cd06218 79 GDELDVLGPLGNGFDLPD--DDGKVLLVGGGIGIAPLLFLAKQLAERGIKVTVLLGFRSADDLFLVEEFEALG-AEVYVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 168 TDDGSYGTKGHVGMLMNEIDFE--VDALYTCGAPAMLKAVAKKYDQL-ERLYISMESRMACGIGACYACVEHDKEDESHA 244
Cdd:cd06218 156 TDDGSAGTKGFVTDLLKELLAEarPDVVYACGPEPMLKAVAELAAERgVPCQVSLEERMACGIGACLGCVVKTKDDEGGY 235
|
250
....*....|
1EP2_B 245 LKVCEDGPVF 254
Cdd:cd06218 236 KRVCKDGPVF 245
|
|
| PRK00054 |
PRK00054 |
dihydroorotate dehydrogenase electron transfer subunit; Reviewed |
3-261 |
2.01e-90 |
|
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
Pssm-ID: 234601 [Multi-domain] Cd Length: 250 Bit Score: 267.51 E-value: 2.01e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 3 LQEMMTVVSQREVAYNIFEMVLKGTlVDEMDLPGQFLHLAVPNGAMLLRRPISISswDKRAKTCTILYRIGDEttGTYKL 82
Cdd:PRK00054 3 KPENMKIVENKEIAPNIYTLVLDGE-KVFDMKPGQFVMVWVPGVEPLLERPISIS--DIDKNEITILYRKVGE--GTKKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 83 SKLESGAKVDVMGPLGNGFPVAEVTstDKILIIGGGIGVPPLYELAKQLEKTGCQMTILLGFASENVKILENEFSNLKNV 162
Cdd:PRK00054 78 SKLKEGDELDIRGPLGNGFDLEEIG--GKVLLVGGGIGVAPLYELAKELKKKGVEVTTVLGARTKDEVIFEEEFAKVGDV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 163 tlKIATDDGSYGTKGHVGMLMNEIDFEVDALYTCGAPAMLKAVAKKYDQLE-RLYISMESRMACGIGACYACVEHDKede 241
Cdd:PRK00054 156 --YVTTDDGSYGFKGFVTDVLDELDSEYDAIYSCGPEIMMKKVVEILKEKKvPAYVSLERRMKCGIGACGACVCDTE--- 230
|
250 260
....*....|....*....|
1EP2_B 242 SHALKVCEDGPVFLGKQLSL 261
Cdd:PRK00054 231 TGGKRVCKDGPVFSGGELVL 250
|
|
| Mcr1 |
COG0543 |
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ... |
8-261 |
9.11e-68 |
|
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];
Pssm-ID: 440309 [Multi-domain] Cd Length: 247 Bit Score: 209.72 E-value: 9.11e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 8 TVVSQREVAYNIFEMVLKGTLVDEMDLPGQFLHLAVPNGamLLRRPISISSWDKRAKTCTILYR-IGDettGTYKLSKLE 86
Cdd:COG0543 1 KVVSVERLAPDVYLLRLEAPLIALKFKPGQFVMLRVPGD--GLRRPFSIASAPREDGTIELHIRvVGK---GTRALAELK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 87 SGAKVDVMGPLGNGFPVAEVTSTdkiliigggigVPPLYELAKQLEKTGCQMTILLGFASENVKILENEFSNLKNVTLKI 166
Cdd:COG0543 76 PGDELDVRGPLGNGFPLEDSGRPvllva--ggtgLAPLRSLAEALLARGRRVTLYLGARTPEDLYLLDELEALADFRVVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 167 ATDDGSYGTKGHVGMLMNEI--DFEVDALYTCGAPAMLKAVAKKYDQL----ERLYISMESRMACGIGACYACVEHDKEd 240
Cdd:COG0543 154 TTDDGWYGRKGFVTDALKELlaEDSGDDVYACGPPPMMKAVAELLLERgvppERIYVSLERRMACGIGMCGGCVVPVGG- 232
|
250 260
....*....|....*....|.
1EP2_B 241 eshalkVCEDGPVFLGKQLSL 261
Cdd:COG0543 233 ------GCKDGPVFDAAEVDW 247
|
|
| DHODB_Fe-S_bind |
pfam10418 |
Iron-sulfur cluster binding domain of dihydroorotate dehydrogenase B; Lactococcus lactis is ... |
220-259 |
1.16e-15 |
|
Iron-sulfur cluster binding domain of dihydroorotate dehydrogenase B; Lactococcus lactis is one of the few organizms with two dihydroorotate dehydrogenases, DHODs, A and B. The B enzyme is a prototype for DHODs in Gram-positive bacteria that use NAD+ as the second substrate. DHODB is a hetero-tetramer composed of a central homodimer of PyrDB subunits resembling the DHODA structure and two PyrK subunits along with three different cofactors: FMN, FAD, and a [2Fe-2S] cluster. The [2Fe-2S] iron-sulfur cluster binds to this C-terminal domain of the PyrK subunit, which is at the interface between the flavin and NAD binding domains and contains three beta-strands. The four cysteine residues at the N-terminal part of this domain are the ones that bind, in pairs, to the iron-sulfur cluster. The conformation of the whole molecule means that the iron-sulfur cluster is localized in a well-ordered part of this domain close to the FAD binding site. The FAD and and NAD binding domains are FAD_binding_6, pfam00970 and NAD_binding_1, pfam00175.
Pssm-ID: 463084 [Multi-domain] Cd Length: 40 Bit Score: 68.78 E-value: 1.16e-15
10 20 30 40
....*....|....*....|....*....|....*....|
1EP2_B 220 ESRMACGIGACYACVEHDKEDESHALKVCEDGPVFLGKQL 259
Cdd:pfam10418 1 EERMACGVGACGGCVVKTKGGDGEYKRVCVDGPVFDADEV 40
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DHOD_e_trans |
cd06218 |
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ... |
9-254 |
3.47e-100 |
|
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster.
Pssm-ID: 99814 [Multi-domain] Cd Length: 246 Bit Score: 292.14 E-value: 3.47e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 9 VVSQREVAYNIFEMVLKGTLVDEMDLPGQFLHLAVPNG-AMLLRRPISISSWDKRAKTCTILYRIGDEttGTYKLSKLES 87
Cdd:cd06218 1 VLSNREIADDIYRLVLEAPEIAAAAKPGQFVMLRVPDGsDPLLRRPISIHDVDPEEGTITLLYKVVGK--GTRLLSELKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 88 GAKVDVMGPLGNGFPVAEvtSTDKILIIGGGIGVPPLYELAKQLEKTGCQMTILLGFASENVKILENEFSNLKnVTLKIA 167
Cdd:cd06218 79 GDELDVLGPLGNGFDLPD--DDGKVLLVGGGIGIAPLLFLAKQLAERGIKVTVLLGFRSADDLFLVEEFEALG-AEVYVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 168 TDDGSYGTKGHVGMLMNEIDFE--VDALYTCGAPAMLKAVAKKYDQL-ERLYISMESRMACGIGACYACVEHDKEDESHA 244
Cdd:cd06218 156 TDDGSAGTKGFVTDLLKELLAEarPDVVYACGPEPMLKAVAELAAERgVPCQVSLEERMACGIGACLGCVVKTKDDEGGY 235
|
250
....*....|
1EP2_B 245 LKVCEDGPVF 254
Cdd:cd06218 236 KRVCKDGPVF 245
|
|
| PRK00054 |
PRK00054 |
dihydroorotate dehydrogenase electron transfer subunit; Reviewed |
3-261 |
2.01e-90 |
|
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
Pssm-ID: 234601 [Multi-domain] Cd Length: 250 Bit Score: 267.51 E-value: 2.01e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 3 LQEMMTVVSQREVAYNIFEMVLKGTlVDEMDLPGQFLHLAVPNGAMLLRRPISISswDKRAKTCTILYRIGDEttGTYKL 82
Cdd:PRK00054 3 KPENMKIVENKEIAPNIYTLVLDGE-KVFDMKPGQFVMVWVPGVEPLLERPISIS--DIDKNEITILYRKVGE--GTKKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 83 SKLESGAKVDVMGPLGNGFPVAEVTstDKILIIGGGIGVPPLYELAKQLEKTGCQMTILLGFASENVKILENEFSNLKNV 162
Cdd:PRK00054 78 SKLKEGDELDIRGPLGNGFDLEEIG--GKVLLVGGGIGVAPLYELAKELKKKGVEVTTVLGARTKDEVIFEEEFAKVGDV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 163 tlKIATDDGSYGTKGHVGMLMNEIDFEVDALYTCGAPAMLKAVAKKYDQLE-RLYISMESRMACGIGACYACVEHDKede 241
Cdd:PRK00054 156 --YVTTDDGSYGFKGFVTDVLDELDSEYDAIYSCGPEIMMKKVVEILKEKKvPAYVSLERRMKCGIGACGACVCDTE--- 230
|
250 260
....*....|....*....|
1EP2_B 242 SHALKVCEDGPVFLGKQLSL 261
Cdd:PRK00054 231 TGGKRVCKDGPVFSGGELVL 250
|
|
| DHOD_e_trans_like |
cd06192 |
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ... |
9-255 |
2.46e-68 |
|
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as NAD binding. NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.
Pssm-ID: 99789 [Multi-domain] Cd Length: 243 Bit Score: 211.42 E-value: 2.46e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 9 VVSQREVAYNIFEMVLKGTLVDEMDLPGQFLHLAVPNGAMLLRRPISISSWDKRAKTCTILYRIGDETTGtyKLSKLESG 88
Cdd:cd06192 1 IVKKEQLEPNLVLLTIKAPLAARLFRPGQFVFLRNFESPGLERIPLSLAGVDPEEGTISLLVEIRGPKTK--LIAELKPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 89 AKVDVMGPLGNGFPVAEvtSTDKILIIGGGIGVPPLYELAKQLEKTGCQMTILLGFASENVKILENEFSnLKNVTLKIAT 168
Cdd:cd06192 79 EKLDVMGPLGNGFEGPK--KGGTVLLVAGGIGLAPLLPIAKKLAANGNKVTVLAGAKKAKEEFLDEYFE-LPADVEIWTT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 169 DDGSYGTKGHVGMLMNEI-DFEVDALYTCGAPAMLKAVAKKYD---QLERLYISMESRMACGIGACYACVEHDKEdesHA 244
Cdd:cd06192 156 DDGELGLEGKVTDSDKPIpLEDVDRIIVAGSDIMMKAVVEALDewlQLIKASVSNNSPMCCGIGICGACTIETKH---GV 232
|
250
....*....|.
1EP2_B 245 LKVCEDGPVFL 255
Cdd:cd06192 233 KRLCKDGPVFR 243
|
|
| Mcr1 |
COG0543 |
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ... |
8-261 |
9.11e-68 |
|
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];
Pssm-ID: 440309 [Multi-domain] Cd Length: 247 Bit Score: 209.72 E-value: 9.11e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 8 TVVSQREVAYNIFEMVLKGTLVDEMDLPGQFLHLAVPNGamLLRRPISISSWDKRAKTCTILYR-IGDettGTYKLSKLE 86
Cdd:COG0543 1 KVVSVERLAPDVYLLRLEAPLIALKFKPGQFVMLRVPGD--GLRRPFSIASAPREDGTIELHIRvVGK---GTRALAELK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 87 SGAKVDVMGPLGNGFPVAEVTSTdkiliigggigVPPLYELAKQLEKTGCQMTILLGFASENVKILENEFSNLKNVTLKI 166
Cdd:COG0543 76 PGDELDVRGPLGNGFPLEDSGRPvllva--ggtgLAPLRSLAEALLARGRRVTLYLGARTPEDLYLLDELEALADFRVVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 167 ATDDGSYGTKGHVGMLMNEI--DFEVDALYTCGAPAMLKAVAKKYDQL----ERLYISMESRMACGIGACYACVEHDKEd 240
Cdd:COG0543 154 TTDDGWYGRKGFVTDALKELlaEDSGDDVYACGPPPMMKAVAELLLERgvppERIYVSLERRMACGIGMCGGCVVPVGG- 232
|
250 260
....*....|....*....|.
1EP2_B 241 eshalkVCEDGPVFLGKQLSL 261
Cdd:COG0543 233 ------GCKDGPVFDAAEVDW 247
|
|
| DHOD_e_trans_like1 |
cd06219 |
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ... |
8-254 |
6.03e-32 |
|
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as NAD binding. NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group, as in flavoenzymes, or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD, forming FADH2 via a semiquinone intermediate, and then transfers a hydride ion to convert NADP+ to NADPH.
Pssm-ID: 99815 [Multi-domain] Cd Length: 248 Bit Score: 117.68 E-value: 6.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 8 TVVSQREVAYNIFEMVLKGTLVDEMDLPGQFLHLAV-PNGAmllRRPISISSWDKRAKTCTILYRIGDETTgtYKLSKLE 86
Cdd:cd06219 2 KILEKEELAPNVKLFEIEAPLIAKKAKPGQFVIVRAdEKGE---RIPLTIADWDPEKGTITIVVQVVGKST--RELATLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 87 SGAKV-DVMGPLGNGFPVAEVtstDKILIIGGGIGVPPLYELAKQLEKTGCQMTILLGFASENVKILENEFSNLKNvTLK 165
Cdd:cd06219 77 EGDKIhDVVGPLGKPSEIENY---GTVVFVGGGVGIAPIYPIAKALKEAGNRVITIIGARTKDLVILEDEFRAVSD-ELI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 166 IATDDGSYGTKGHVGMLMNEIDFE---VDALYTCGAPAMLKAVA---KKYDQleRLYISMESRMACGIGACYAC-VEHDK 238
Cdd:cd06219 153 ITTDDGSYGEKGFVTDPLKELIESgekVDLVIAIGPPIMMKAVSeltRPYGI--PTVVSLNPIMVDGTGMCGACrVTVGG 230
|
250
....*....|....*..
1EP2_B 239 EdeshaLK-VCEDGPVF 254
Cdd:cd06219 231 E-----TKfACVDGPEF 242
|
|
| PRK06222 |
PRK06222 |
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein; |
6-254 |
1.00e-30 |
|
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein;
Pssm-ID: 235747 [Multi-domain] Cd Length: 281 Bit Score: 115.28 E-value: 1.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 6 MMTVVSQREVAYNIFEMVLKGTLVDEMDLPGQFLHLAV-PNGAmllRRPISISSWDKRAKTCTILYR-IGdetTGTYKLS 83
Cdd:PRK06222 1 MYKILEKEELAPNVFLMEIEAPRVAKKAKPGQFVIVRIdEKGE---RIPLTIADYDREKGTITIVFQaVG---KSTRKLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 84 KLESGAKV-DVMGPLGNgfPvAEVTSTDKILIIGGGIGVPPLYELAKQLEKTGCQMTILLGFASENVKILENEFsnlKNV 162
Cdd:PRK06222 75 ELKEGDSIlDVVGPLGK--P-SEIEKFGTVVCVGGGVGIAPVYPIAKALKEAGNKVITIIGARNKDLLILEDEM---KAV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 163 T--LKIATDDGSYGTKGHVGMLMNEI---DFEVDALYTCGAPAMLKAVA---KKYDQleRLYISMESRMACGIGACYAC- 233
Cdd:PRK06222 149 SdeLYVTTDDGSYGRKGFVTDVLKELlesGKKVDRVVAIGPVIMMKFVAeltKPYGI--KTIVSLNPIMVDGTGMCGACr 226
|
250 260
....*....|....*....|..
1EP2_B 234 VEHDKEdeshaLK-VCEDGPVF 254
Cdd:PRK06222 227 VTVGGE-----TKfACVDGPEF 243
|
|
| DHOD_e_trans_like2 |
cd06220 |
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ... |
27-260 |
1.67e-29 |
|
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster.
Pssm-ID: 99816 [Multi-domain] Cd Length: 233 Bit Score: 110.80 E-value: 1.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 27 TLVDEMDL---PGQFLHLAVPNgamLLRRPISISSWDKRaKTCTILyRIGDETTgtyKLSKLESGAKVDVMGPLGNGFPV 103
Cdd:cd06220 15 TFVFDWDFdfkPGQFVMVWVPG---VDEIPMSLSYIDGP-NSITVK-KVGEATS---ALHDLKEGDKLGIRGPYGNGFEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 104 AEvtstDKILIIGGGIGVPPLYELAKQLEKTGcQMTILLGFASENVKILENEFSnlKNVTLKIATDDGSYGTKGHVGMLM 183
Cdd:cd06220 87 VG----GKVLLIGGGIGIAPLAPLAERLKKAA-DVTVLLGARTKEELLFLDRLR--KSDELIVTTDDGSYGFKGFVTDLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 184 NEIDFEV-DALYTCGAPAMLKAV---AKKYDQleRLYISMESRMACGIGACYACVEhdkedESHALKVCEDGPVFLGKQL 259
Cdd:cd06220 160 KELDLEEyDAIYVCGPEIMMYKVleiLDERGV--RAQFSLERYMKCGIGICGSCCI-----DPTGLRVCRDGPVFDGEQL 232
|
.
1EP2_B 260 S 260
Cdd:cd06220 233 K 233
|
|
| sulfite_reductase_like |
cd06221 |
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ... |
35-254 |
1.80e-26 |
|
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural similarity to ferredoxin reductase and sequence similarity to dihydroorotate dehydrogenases. Clostridium pasteurianum inducible dissimilatory type sulfite reductase is linked to ferredoxin and reduces NH2OH and SeO3 at a lesser rate than it's normal substate SO3(2-). Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+.
Pssm-ID: 99817 [Multi-domain] Cd Length: 253 Bit Score: 103.46 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 35 PGQFLHLAVPnGAMllRRPISISSWDKRAKT--CTILyRIGDETTGtykLSKLESGAKVDVMGPLGNGFPVAEVTSTDki 112
Cdd:cd06221 30 PGQFVMLSLP-GVG--EAPISISSDPTRRGPleLTIR-RVGRVTEA---LHELKPGDTVGLRGPFGNGFPVEEMKGKD-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 113 liigggigV---------PPLYELAKQL----EKTGcQMTILLGFASENVKILENEF---SNLKNVTLKIATDDGSYGTK 176
Cdd:cd06221 101 --------LllvagglglAPLRSLINYIldnrEDYG-KVTLLYGARTPEDLLFKEELkewAKRSDVEVILTVDRAEEGWT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 177 GHVGM---LMNEIDFEVD--ALYTCGAPAMLKAVAKKYDQL----ERLYISMESRMACGIGACYACVehdkedeSHALKV 247
Cdd:cd06221 172 GNVGLvtdLLPELTLDPDntVAIVCGPPIMMRFVAKELLKLgvpeEQIWVSLERRMKCGVGKCGHCQ-------IGPKYV 244
|
....*..
1EP2_B 248 CEDGPVF 254
Cdd:cd06221 245 CKDGPVF 251
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
6-258 |
2.97e-25 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 104.44 E-value: 2.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 6 MMTVVSQREVAYNIFEMVLKGTLVDEMDLPGQFLHLAVPNGAMllRRPISISSWDKRAKTCTILYR-IGDETTgtyKLSK 84
Cdd:PRK12778 1 MNKIVEKEIFSEKVFLLEIEAPLIAKSRKPGQFVIVRVGEKGE--RIPLTIADADPEKGTITLVIQeVGLSTT---KLCE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 85 LESGAKV-DVMGPLGNGfpvAEVTSTDKILIIGGGIGVPPLYELAKQLEKTGCQMTILLGFASENVKILENEFSNLKNvT 163
Cdd:PRK12778 76 LNEGDYItDVVGPLGNP---SEIENYGTVVCAGGGVGVAPMLPIVKALKAAGNRVITILGGRSKELIILEDEMRESSD-E 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 164 LKIATDDGSYGTKGHVGMLMNEI---DFEVDALYTCGAPAMLKAV---AKKYDQLerLYISMESRMACGIGACYACvehd 237
Cdd:PRK12778 152 VIIMTDDGSYGRKGLVTDGLEEVikrETKVDKVFAIGPAIMMKFVcllTKKYGIP--TIVSLNTIMVDGTGMCGAC---- 225
|
250 260
....*....|....*....|..
1EP2_B 238 KEDESHALK-VCEDGPVFLGKQ 258
Cdd:PRK12778 226 RVTVGGKTKfACVDGPEFDGHL 247
|
|
| FNR_like |
cd00322 |
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ... |
10-212 |
4.37e-24 |
|
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in many organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).
Pssm-ID: 99778 [Multi-domain] Cd Length: 223 Bit Score: 96.36 E-value: 4.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 10 VSQREVAYNIFEMVLKGTLVDEMdLPGQFLHLAVPNGAMLLRRPISISSWDKRAKTCTILYRIGDETTGTYKLSKLESGA 89
Cdd:cd00322 1 VATEDVTDDVRLFRLQLPNGFSF-KPGQYVDLHLPGDGRGLRRAYSIASSPDEEGELELTVKIVPGGPFSAWLHDLKPGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 90 KVDVMGPLGNGFPVAEVTSTdkiliigggiGV--------PPLYELAKQL--EKTGCQMTILLGFASENVKILENEFSNL 159
Cdd:cd00322 80 EVEVSGPGGDFFLPLEESGP----------VVliaggigiTPFRSMLRHLaaDKPGGEITLLYGARTPADLLFLDELEEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
1EP2_B 160 ----KNVTLKIATDDGSYGTKGHVGMLMNE-------IDFEVDALYTCGAPAMLKAVAKKYDQL 212
Cdd:cd00322 150 akegPNFRLVLALSRESEAKLGPGGRIDREaeilallPDDSGALVYICGPPAMAKAVREALVSL 213
|
|
| PRK08345 |
PRK08345 |
cytochrome-c3 hydrogenase subunit gamma; Provisional |
35-254 |
1.33e-16 |
|
cytochrome-c3 hydrogenase subunit gamma; Provisional
Pssm-ID: 236247 [Multi-domain] Cd Length: 289 Bit Score: 77.54 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 35 PGQFLHLAVPNGAMLlrrPISI-SSWDKRAKTCTILYRIGDETTGTYKLSKlesGAKVDVMGPLGNGFPVAEVTSTDKIL 113
Cdd:PRK08345 40 PGQFVQVTIPGVGEV---PISIcSSPTRKGFFELCIRRAGRVTTVIHRLKE---GDIVGVRGPYGNGFPVDEMEGMDLLL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 114 IIGGGIGVPP----LYELAKQlEKTGcQMTILLG--------FASENVKILENEfSNLKnVTLKIATDDGSYG------- 174
Cdd:PRK08345 114 IAGGLGMAPLrsvlLYAMDNR-WKYG-NITLIYGakyyedllFYDELIKDLAEA-ENVK-IIQSVTRDPEWPGchglpqg 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 175 -----TKGHVGMLMNEIDFEVDALYT--CGAPAMLKAVAKKYDQL----ERLYISMESRMACGIGACYACVehdkEDESH 243
Cdd:PRK08345 190 fiervCKGVVTDLFREANTDPKNTYAaiCGPPVMYKFVFKELINRgyrpERIYVTLERRMRCGIGKCGHCI----VGTST 265
|
250
....*....|..
1EP2_B 244 ALK-VCEDGPVF 254
Cdd:PRK08345 266 SIKyVCKDGPVF 277
|
|
| DHODB_Fe-S_bind |
pfam10418 |
Iron-sulfur cluster binding domain of dihydroorotate dehydrogenase B; Lactococcus lactis is ... |
220-259 |
1.16e-15 |
|
Iron-sulfur cluster binding domain of dihydroorotate dehydrogenase B; Lactococcus lactis is one of the few organizms with two dihydroorotate dehydrogenases, DHODs, A and B. The B enzyme is a prototype for DHODs in Gram-positive bacteria that use NAD+ as the second substrate. DHODB is a hetero-tetramer composed of a central homodimer of PyrDB subunits resembling the DHODA structure and two PyrK subunits along with three different cofactors: FMN, FAD, and a [2Fe-2S] cluster. The [2Fe-2S] iron-sulfur cluster binds to this C-terminal domain of the PyrK subunit, which is at the interface between the flavin and NAD binding domains and contains three beta-strands. The four cysteine residues at the N-terminal part of this domain are the ones that bind, in pairs, to the iron-sulfur cluster. The conformation of the whole molecule means that the iron-sulfur cluster is localized in a well-ordered part of this domain close to the FAD binding site. The FAD and and NAD binding domains are FAD_binding_6, pfam00970 and NAD_binding_1, pfam00175.
Pssm-ID: 463084 [Multi-domain] Cd Length: 40 Bit Score: 68.78 E-value: 1.16e-15
10 20 30 40
....*....|....*....|....*....|....*....|
1EP2_B 220 ESRMACGIGACYACVEHDKEDESHALKVCEDGPVFLGKQL 259
Cdd:pfam10418 1 EERMACGVGACGGCVVKTKGGDGEYKRVCVDGPVFDADEV 40
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
8-252 |
1.87e-15 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 75.64 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 8 TVVSQREVAYNIFEMVLKGTLVDEMDLPGQFLH-LAVPNGAMLlrrPISISSWDKRAKT-CTILYRIGdetTGTYKLSKL 85
Cdd:PRK12779 652 TIVGKVQLAGGIVEFTVRAPMVARSAQAGQFVRvLPWEKGELI---PLTLADWDAEKGTiDLVVQGMG---TSSLEINRM 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 86 ESG-AKVDVMGPLGNGFPVAEVTSTDKILIIGGGIGVPPLYELAKQLEKTGCQMTILLGF----------ASENVKILEN 154
Cdd:PRK12779 726 AIGdAFSGIAGPLGRASELHRYEGNQTVVFCAGGVGLPPVYPIMRAHLRLGNHVTLISGFrakeflfwtgDDERVGKLKA 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 155 EFSNLKNVTLkiATDDGSYGTKGHV-----GMLMNEIDFE---VDALYTCGAPAMLKAVA---KKYDQleRLYISMESRM 223
Cdd:PRK12779 806 EFGDQLDVIY--TTNDGSFGVKGFVtgpleEMLKANQQGKgrtIAEVIAIGPPLMMRAVSdltKPYGV--KTVASLNSIM 881
|
250 260 270
....*....|....*....|....*....|...
1EP2_B 224 ACGIGACYAC----VEHDKEDESHAlkvCEDGP 252
Cdd:PRK12779 882 VDATGMCGACmvpvTIDGKMVRKHA---CIDGP 911
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
35-259 |
5.64e-13 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 68.43 E-value: 5.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 35 PGQFLHLAVPNGAMllRRPISISSWDKRAKTCTILYRIGDETTGTYKLSKLESGAKVDVMGPLGngFPvAEVTSTDKILI 114
Cdd:PRK12775 30 PGHFVMLRLYEGAE--RIPLTVADFDRKKGTITMVVQALGKTTREMMTKFKAGDTFEDFVGPLG--LP-QHIDKAGHVVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 115 IGGGIGVPPLYELAKQLEKTGCQMTILLGFASENVKILENEFSNLKNvTLKIATDDGSYGTKGHVGMLMNEI--DFEVDA 192
Cdd:PRK12775 105 VGGGLGVAPVYPQLRAFKEAGARTTGIIGFRNKDLVFWEDKFGKYCD-DLIVCTDDGSYGKPGFVTAALKEVceKDKPDL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1EP2_B 193 LYTCGAPAMLKAVAKKYDQLE-RLYISMESRMACGIGACYACVEHDKEDESHAlkvCEDGPVFLGKQL 259
Cdd:PRK12775 184 VVAIGPLPMMNACVETTRPFGvKTMVSLNAIMVDGTGMCGSCRVTVGGEVKFA---CVDGPDFDGHKV 248
|
|
| Fpr |
COG1018 |
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; |
7-220 |
1.50e-07 |
|
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
Pssm-ID: 440641 [Multi-domain] Cd Length: 231 Bit Score: 50.94 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 7 MTVVSQREVAYNIFEMVLkgTLVDEMDL----PGQFLHLAVPNGAMLLRRPISISS--WDKRaktctilYRIG----DET 76
Cdd:COG1018 6 LRVVEVRRETPDVVSFTL--EPPDGAPLprfrPGQFVTLRLPIDGKPLRRAYSLSSapGDGR-------LEITvkrvPGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 77 TGTYKL-SKLESGAKVDVMGPLGNgFPVAE--------------VTstdkiliigggigvpPLYELAKQLEKTGC--QMT 139
Cdd:COG1018 77 GGSNWLhDHLKVGDTLEVSGPRGD-FVLDPeparpllliaggigIT---------------PFLSMLRTLLARGPfrPVT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 140 ILLGFASENVKILENEFSNLK----NVTLKIATDDGSYGTKGHV--GMLMNEI-DFEVDALYTCGAPAMLKAVAkkyDQL 212
Cdd:COG1018 141 LVYGARSPADLAFRDELEALAarhpRLRLHPVLSREPAGLQGRLdaELLAALLpDPADAHVYLCGPPPMMEAVR---AAL 217
|
....*...
1EP2_B 213 ERLYISME 220
Cdd:COG1018 218 AELGVPEE 225
|
|
| FNR_iron_sulfur_binding_1 |
cd06215 |
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
34-205 |
4.26e-04 |
|
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal portion of the FAD/NAD binding domain contains most of the NADP(H) binding residues and the N-terminal sub-domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. In this ferredoxin like sub-group, the FAD/NAD sub-domains is typically fused to a C-terminal iron-sulfur binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins which act as electron carriers in photosynthesis and ferredoxins which participate in redox chains from bacteria to mammals. Ferredoxin reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99811 [Multi-domain] Cd Length: 231 Bit Score: 40.65 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 34 LPGQFLHLAVPNGAMLLRRPISISSWDKRAKTCTI-LYRIGDETTGTYKLSKLESGAKVDVMGPLGnGFpVAEVTSTDKI 112
Cdd:cd06215 29 KPGQFLTLELEIDGETVYRAYTLSSSPSRPDSLSItVKRVPGGLVSNWLHDNLKVGDELWASGPAG-EF-TLIDHPADKL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EP2_B 113 LIIGGGIGVPPLYELAKQLEKTGCQMTILLGFASENVK--ILENEFSNLK----NVTLK-IATDDGSYGTKGHVGMLMNE 185
Cdd:cd06215 107 LLLSAGSGITPMMSMARWLLDTRPDADIVFIHSARSPAdiIFADELEELArrhpNFRLHlILEQPAPGAWGGYRGRLNAE 186
|
170 180
....*....|....*....|....*.
1EP2_B 186 I------DFEVDALYTCGAPAMLKAV 205
Cdd:cd06215 187 LlallvpDLKERTVFVCGPAGFMKAV 212
|
|
| |
