|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06222 |
PRK06222 |
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein; |
4-275 |
5.14e-147 |
|
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein;
Pssm-ID: 235747 [Multi-domain] Cd Length: 281 Bit Score: 413.04 E-value: 5.14e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 4 FEIVNKRQLNDTINWYTIYAPLVARHAKPGQFIILRVDEYGERIPITMAGHDAEKGTVDIIVQSVGRTSILLSQLNVGDC 83
Cdd:PRK06222 2 YKILEKEELAPNVFLMEIEAPRVAKKAKPGQFVIVRIDEKGERIPLTIADYDREKGTITIVFQAVGKSTRKLAELKEGDS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 84 LADLVGPLGQPSHMEGLKKVAIVGGGVGNALAYPLAIGMHKAGIHVDMICGFKTKDIVILEDEFRAGVDRVFMMTDDGTY 163
Cdd:PRK06222 82 ILDVVGPLGKPSEIEKFGTVVCVGGGVGIAPVYPIAKALKEAGNKVITIIGARNKDLLILEDEMKAVSDELYVTTDDGSY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 164 GEKGFTTDKLKALLDSGEKYDEIVAVGPAIMMKFVCGIAQDYGIPSVASLATYMIDGTGMCGGCRAIIGGEPKFVCVDGP 243
Cdd:PRK06222 162 GRKGFVTDVLKELLESGKKVDRVVAIGPVIMMKFVAELTKPYGIKTIVSLNPIMVDGTGMCGACRVTVGGETKFACVDGP 241
|
250 260 270
....*....|....*....|....*....|..
gi 1222105945 244 DFDGSLIDWDLLIKRGKTFAEQEAHDREHICK 275
Cdd:PRK06222 242 EFDGHLVDFDELMRRLAMYKEEEKLALEKYEE 273
|
|
| DHOD_e_trans_like1 |
cd06219 |
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ... |
4-251 |
2.11e-135 |
|
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: 382.69 E-value: 2.11e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 4 FEIVNKRQLNDTINWYTIYAPLVARHAKPGQFIILRVDEYGERIPITMAGHDAEKGTVDIIVQSVGRTSILLSQLNVGDC 83
Cdd:cd06219 1 YKILEKEELAPNVKLFEIEAPLIAKKAKPGQFVIVRADEKGERIPLTIADWDPEKGTITIVVQVVGKSTRELATLEEGDK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 84 LADLVGPLGQPSHMEGLKKVAIVGGGVGNALAYPLAIGMHKAGIHVDMICGFKTKDIVILEDEFRAGVDRVFMMTDDGTY 163
Cdd:cd06219 81 IHDVVGPLGKPSEIENYGTVVFVGGGVGIAPIYPIAKALKEAGNRVITIIGARTKDLVILEDEFRAVSDELIITTDDGSY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 164 GEKGFTTDKLKALLDSGEKYDEIVAVGPAIMMKFVCGIAQDYGIPSVASLATYMIDGTGMCGGCRAIIGGEPKFVCVDGP 243
Cdd:cd06219 161 GEKGFVTDPLKELIESGEKVDLVIAIGPPIMMKAVSELTRPYGIPTVVSLNPIMVDGTGMCGACRVTVGGETKFACVDGP 240
|
....*...
gi 1222105945 244 DFDGSLID 251
Cdd:cd06219 241 EFDAHKVD 248
|
|
| Mcr1 |
COG0543 |
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ... |
5-252 |
1.07e-81 |
|
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];
Pssm-ID: 440309 [Multi-domain] Cd Length: 247 Bit Score: 246.31 E-value: 1.07e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 5 EIVNKRQLNDTINWYTIYAPLVARHAKPGQFIILRVDEYGERIPITMAGHDAEKGTVDIIVQSVGRTSILLSQLNVGDCL 84
Cdd:COG0543 1 KVVSVERLAPDVYLLRLEAPLIALKFKPGQFVMLRVPGDGLRRPFSIASAPREDGTIELHIRVVGKGTRALAELKPGDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 85 aDLVGPLGQPSHME-GLKKVAIVGGGVGNALAYPLAIGMHKAGIHVDMICGFKTKDIVILEDEFRA-GVDRVFMMTDDGT 162
Cdd:COG0543 81 -DVRGPLGNGFPLEdSGRPVLLVAGGTGLAPLRSLAEALLARGRRVTLYLGARTPEDLYLLDELEAlADFRVVVTTDDGW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 163 YGEKGFTTDKLKALLDsGEKYDEIVAVGPAIMMKFVCGIAQDYGIPS---VASLATYMIDGTGMCGGCRAiiggEPKFVC 239
Cdd:COG0543 160 YGRKGFVTDALKELLA-EDSGDDVYACGPPPMMKAVAELLLERGVPPeriYVSLERRMACGIGMCGGCVV----PVGGGC 234
|
250
....*....|...
gi 1222105945 240 VDGPDFDGSLIDW 252
Cdd:COG0543 235 KDGPVFDAAEVDW 247
|
|
| sulfite_red_B |
TIGR02911 |
sulfite reductase, subunit B; Members of this protein family include the B subunit, one of ... |
30-246 |
2.28e-18 |
|
sulfite reductase, subunit B; Members of this protein family include the B subunit, one of three subunits, of the anaerobic sulfite reductase of Salmonella, and close homologs from various Clostridum species, where the three-gene neighborhood is preserved. Two such gene clusters are found in Clostridium perfringens, but it may be that these sets of genes correspond to the distinct assimilatory and dissimilatory forms as seen in Clostridium pasteurianum. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 131957 [Multi-domain] Cd Length: 261 Bit Score: 82.15 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 30 AKPGQFIILRVDEYGERiPITMAGHDaeKGTVDIIVQSVGRTSILLSQLNVGDCLAdLVGPLGQPSHMEGL--KKVAIVG 107
Cdd:TIGR02911 31 VKPGQFFEVSLPKYGEA-PISVSGIG--EGYIDLTIRRVGKVTDEVFTLKEGDNLF-LRGPYGNGFDVDNYkhKELVVVA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 108 GGVGNA----LAYPLAIGMHKAGiHVDMICGFKTKDIVILEDEFRAGVDRV-FMMT----DDGTYGEKGFTTDKLKALLD 178
Cdd:TIGR02911 107 GGTGVApvkgVVEYFVKNPKEIK-SLNLILGFKTPDDILFKEDIAEWKGNInLTLTldeaEEDYKGNIGLVTKYIPELTL 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1222105945 179 SGEKYDEIVAVGPAIMMKFVCGIAQDYGIPSVASLATY---MIDGTGMCGGCRAiiggEPKFVCVDGPDFD 246
Cdd:TIGR02911 186 KDIEEVQAIVVGPPIMMKFTVQELLKKGIKEENIWVSYerkMCCGVGKCGHCKI----DDVYVCLDGPVFN 252
|
|
| DHODB_Fe-S_bind |
pfam10418 |
Iron-sulfur cluster binding domain of dihydroorotate dehydrogenase B; Lactococcus lactis is ... |
215-250 |
2.44e-08 |
|
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: 49.14 E-value: 2.44e-08
10 20 30
....*....|....*....|....*....|....*....
gi 1222105945 215 TYMIDGTGMCGGCR---AIIGGEPKFVCVDGPDFDGSLI 250
Cdd:pfam10418 2 ERMACGVGACGGCVvktKGGDGEYKRVCVDGPVFDADEV 40
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06222 |
PRK06222 |
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein; |
4-275 |
5.14e-147 |
|
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein;
Pssm-ID: 235747 [Multi-domain] Cd Length: 281 Bit Score: 413.04 E-value: 5.14e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 4 FEIVNKRQLNDTINWYTIYAPLVARHAKPGQFIILRVDEYGERIPITMAGHDAEKGTVDIIVQSVGRTSILLSQLNVGDC 83
Cdd:PRK06222 2 YKILEKEELAPNVFLMEIEAPRVAKKAKPGQFVIVRIDEKGERIPLTIADYDREKGTITIVFQAVGKSTRKLAELKEGDS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 84 LADLVGPLGQPSHMEGLKKVAIVGGGVGNALAYPLAIGMHKAGIHVDMICGFKTKDIVILEDEFRAGVDRVFMMTDDGTY 163
Cdd:PRK06222 82 ILDVVGPLGKPSEIEKFGTVVCVGGGVGIAPVYPIAKALKEAGNKVITIIGARNKDLLILEDEMKAVSDELYVTTDDGSY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 164 GEKGFTTDKLKALLDSGEKYDEIVAVGPAIMMKFVCGIAQDYGIPSVASLATYMIDGTGMCGGCRAIIGGEPKFVCVDGP 243
Cdd:PRK06222 162 GRKGFVTDVLKELLESGKKVDRVVAIGPVIMMKFVAELTKPYGIKTIVSLNPIMVDGTGMCGACRVTVGGETKFACVDGP 241
|
250 260 270
....*....|....*....|....*....|..
gi 1222105945 244 DFDGSLIDWDLLIKRGKTFAEQEAHDREHICK 275
Cdd:PRK06222 242 EFDGHLVDFDELMRRLAMYKEEEKLALEKYEE 273
|
|
| DHOD_e_trans_like1 |
cd06219 |
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ... |
4-251 |
2.11e-135 |
|
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: 382.69 E-value: 2.11e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 4 FEIVNKRQLNDTINWYTIYAPLVARHAKPGQFIILRVDEYGERIPITMAGHDAEKGTVDIIVQSVGRTSILLSQLNVGDC 83
Cdd:cd06219 1 YKILEKEELAPNVKLFEIEAPLIAKKAKPGQFVIVRADEKGERIPLTIADWDPEKGTITIVVQVVGKSTRELATLEEGDK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 84 LADLVGPLGQPSHMEGLKKVAIVGGGVGNALAYPLAIGMHKAGIHVDMICGFKTKDIVILEDEFRAGVDRVFMMTDDGTY 163
Cdd:cd06219 81 IHDVVGPLGKPSEIENYGTVVFVGGGVGIAPIYPIAKALKEAGNRVITIIGARTKDLVILEDEFRAVSDELIITTDDGSY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 164 GEKGFTTDKLKALLDSGEKYDEIVAVGPAIMMKFVCGIAQDYGIPSVASLATYMIDGTGMCGGCRAIIGGEPKFVCVDGP 243
Cdd:cd06219 161 GEKGFVTDPLKELIESGEKVDLVIAIGPPIMMKAVSELTRPYGIPTVVSLNPIMVDGTGMCGACRVTVGGETKFACVDGP 240
|
....*...
gi 1222105945 244 DFDGSLID 251
Cdd:cd06219 241 EFDAHKVD 248
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
4-279 |
1.52e-112 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 341.34 E-value: 1.52e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 4 FEIVNKRQLNDTINWYTIYAPLVARHAKPGQFIILRVDEYGERIPITMAGHDAEKGTVDIIVQSVGRTSILLSQLNVGDC 83
Cdd:PRK12778 2 NKIVEKEIFSEKVFLLEIEAPLIAKSRKPGQFVIVRVGEKGERIPLTIADADPEKGTITLVIQEVGLSTTKLCELNEGDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 84 LADLVGPLGQPSHMEGLKKVAIVGGGVGNALAYPLAIGMHKAGIHVDMICGFKTKDIVILEDEFRAGVDRVFMMTDDGTY 163
Cdd:PRK12778 82 ITDVVGPLGNPSEIENYGTVVCAGGGVGVAPMLPIVKALKAAGNRVITILGGRSKELIILEDEMRESSDEVIIMTDDGSY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 164 GEKGFTTDKLKALLDSGEKYDEIVAVGPAIMMKFVCGIAQDYGIPSVASLATYMIDGTGMCGGCRAIIGGEPKFVCVDGP 243
Cdd:PRK12778 162 GRKGLVTDGLEEVIKRETKVDKVFAIGPAIMMKFVCLLTKKYGIPTIVSLNTIMVDGTGMCGACRVTVGGKTKFACVDGP 241
|
250 260 270
....*....|....*....|....*....|....*.
gi 1222105945 244 DFDGSLIDWDLLIKRGKTFaeqEAHDREHICKLTGG 279
Cdd:PRK12778 242 EFDGHLVDFDEMLKRMGAY---KTIEGEELLKLEER 274
|
|
| Mcr1 |
COG0543 |
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ... |
5-252 |
1.07e-81 |
|
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];
Pssm-ID: 440309 [Multi-domain] Cd Length: 247 Bit Score: 246.31 E-value: 1.07e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 5 EIVNKRQLNDTINWYTIYAPLVARHAKPGQFIILRVDEYGERIPITMAGHDAEKGTVDIIVQSVGRTSILLSQLNVGDCL 84
Cdd:COG0543 1 KVVSVERLAPDVYLLRLEAPLIALKFKPGQFVMLRVPGDGLRRPFSIASAPREDGTIELHIRVVGKGTRALAELKPGDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 85 aDLVGPLGQPSHME-GLKKVAIVGGGVGNALAYPLAIGMHKAGIHVDMICGFKTKDIVILEDEFRA-GVDRVFMMTDDGT 162
Cdd:COG0543 81 -DVRGPLGNGFPLEdSGRPVLLVAGGTGLAPLRSLAEALLARGRRVTLYLGARTPEDLYLLDELEAlADFRVVVTTDDGW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 163 YGEKGFTTDKLKALLDsGEKYDEIVAVGPAIMMKFVCGIAQDYGIPS---VASLATYMIDGTGMCGGCRAiiggEPKFVC 239
Cdd:COG0543 160 YGRKGFVTDALKELLA-EDSGDDVYACGPPPMMKAVAELLLERGVPPeriYVSLERRMACGIGMCGGCVV----PVGGGC 234
|
250
....*....|...
gi 1222105945 240 VDGPDFDGSLIDW 252
Cdd:COG0543 235 KDGPVFDAAEVDW 247
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
4-276 |
1.86e-78 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 256.41 E-value: 1.86e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 4 FEIVNKRQLNDTINWYTIYAPLVARHAKPGQFIILRVDEYGERIPITMAGHDAEKGTVDIIVQSVGRTSI-LLSQLNVGD 82
Cdd:PRK12775 2 YSIVRREAFSDTTFLWEVEAPDVAASAEPGHFVMLRLYEGAERIPLTVADFDRKKGTITMVVQALGKTTReMMTKFKAGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 83 CLADLVGPLGQPSHMEGLKKVAIVGGGVGNALAYPLAIGMHKAGIHVDMICGFKTKDIVILEDEFRAGVDRVFMMTDDGT 162
Cdd:PRK12775 82 TFEDFVGPLGLPQHIDKAGHVVLVGGGLGVAPVYPQLRAFKEAGARTTGIIGFRNKDLVFWEDKFGKYCDDLIVCTDDGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 163 YGEKGFTTDKLKALLDSgEKYDEIVAVGPAIMMKFVCGIAQDYGIPSVASLATYMIDGTGMCGGCRAIIGGEPKFVCVDG 242
Cdd:PRK12775 162 YGKPGFVTAALKEVCEK-DKPDLVVAIGPLPMMNACVETTRPFGVKTMVSLNAIMVDGTGMCGSCRVTVGGEVKFACVDG 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 1222105945 243 PDFDGSLIDWDLLIKRGKTFAEQEAHDRE---HICKL 276
Cdd:PRK12775 241 PDFDGHKVDFKELHARQKRFKSQEDRANEdyaHVCNL 277
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
6-266 |
6.59e-74 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 243.20 E-value: 6.59e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 6 IVNKRQLNDTINWYTIYAPLVARHAKPGQFIILRVDEYGERIPITMAGHDAEKGTVDIIVQSVGRTSILLSQLNVGDCLA 85
Cdd:PRK12779 653 IVGKVQLAGGIVEFTVRAPMVARSAQAGQFVRVLPWEKGELIPLTLADWDAEKGTIDLVVQGMGTSSLEINRMAIGDAFS 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 86 DLVGPLGQPSHM---EGLKKVAIVGGGVGNALAYPLAIGMHKAGIHVDMICGFKTKDIVILEDE-FRAGVDR-------- 153
Cdd:PRK12779 733 GIAGPLGRASELhryEGNQTVVFCAGGVGLPPVYPIMRAHLRLGNHVTLISGFRAKEFLFWTGDdERVGKLKaefgdqld 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 154 VFMMTDDGTYGEKGFTTDKLKALLDS-----GEKYDEIVAVGPAIMMKFVCGIAQDYGIPSVASLATYMIDGTGMCGGCR 228
Cdd:PRK12779 813 VIYTTNDGSFGVKGFVTGPLEEMLKAnqqgkGRTIAEVIAIGPPLMMRAVSDLTKPYGVKTVASLNSIMVDATGMCGACM 892
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1222105945 229 AIIGGEPKFV----CVDGPDFDGSLIDWDLLIKRGKTFAEQE 266
Cdd:PRK12779 893 VPVTIDGKMVrkhaCIDGPEIDAHIIDWDKFLPRFNQFKAQE 934
|
|
| DHOD_e_trans_like |
cd06192 |
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ... |
6-246 |
5.54e-56 |
|
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: 180.60 E-value: 5.54e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 6 IVNKRQLNDTINWYTIYAPLVARHAKPGQFIILRVDEYG--ERIPITMAGHDAEKGTVDIIVQSVGRTSILLSQLNVGDC 83
Cdd:cd06192 1 IVKKEQLEPNLVLLTIKAPLAARLFRPGQFVFLRNFESPglERIPLSLAGVDPEEGTISLLVEIRGPKTKLIAELKPGEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 84 LaDLVGPLGQPshMEGLKK---VAIVGGGVGNALAYPLAIGMHKAGIHVDMICGFKTKDIVILEDEFRAGVDRVFMMTDD 160
Cdd:cd06192 81 L-DVMGPLGNG--FEGPKKggtVLLVAGGIGLAPLLPIAKKLAANGNKVTVLAGAKKAKEEFLDEYFELPADVEIWTTDD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 161 GTYGEKGFTTDKLKALLDsgEKYDEIVAVGPAIMMKFVCGIAQDYG--IPSVASLATYMIDGTGMCGGCRAIIGGEPKFV 238
Cdd:cd06192 158 GELGLEGKVTDSDKPIPL--EDVDRIIVAGSDIMMKAVVEALDEWLqlIKASVSNNSPMCCGIGICGACTIETKHGVKRL 235
|
....*...
gi 1222105945 239 CVDGPDFD 246
Cdd:cd06192 236 CKDGPVFR 243
|
|
| DHOD_e_trans |
cd06218 |
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ... |
6-246 |
7.99e-56 |
|
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: 180.05 E-value: 7.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 6 IVNKRQLNDTINWYTIYAPLVARHAKPGQFIILRVDEYGE---RIPITMAGHDAEKGTVDIIVQSVGRTSILLSQLNVGD 82
Cdd:cd06218 1 VLSNREIADDIYRLVLEAPEIAAAAKPGQFVMLRVPDGSDpllRRPISIHDVDPEEGTITLLYKVVGKGTRLLSELKAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 83 CLaDLVGPLGQP-SHMEGLKKVAIVGGGVGNALAYPLAIGMHKAGIHVDMICGFKTKDIVILEDEFRAGVDRVFMMTDDG 161
Cdd:cd06218 81 EL-DVLGPLGNGfDLPDDDGKVLLVGGGIGIAPLLFLAKQLAERGIKVTVLLGFRSADDLFLVEEFEALGAEVYVATDDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 162 TYGEKGFTTDKLKALLDSGeKYDEIVAVGPAIMMKFVCGIAQDYGIPSVASLATYMIDGTGMCGGC---RAIIGGEPKFV 238
Cdd:cd06218 160 SAGTKGFVTDLLKELLAEA-RPDVVYACGPEPMLKAVAELAAERGVPCQVSLEERMACGIGACLGCvvkTKDDEGGYKRV 238
|
....*...
gi 1222105945 239 CVDGPDFD 246
Cdd:cd06218 239 CKDGPVFD 246
|
|
| PRK00054 |
PRK00054 |
dihydroorotate dehydrogenase electron transfer subunit; Reviewed |
1-247 |
2.13e-55 |
|
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
Pssm-ID: 234601 [Multi-domain] Cd Length: 250 Bit Score: 179.30 E-value: 2.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 1 MKRFEIVNKRQLNDTInwYTIY-APLVARHAKPGQFIILRVDEYGERIPITMAGHDAEKGTVDIIVQSVGRTSILLSQLN 79
Cdd:PRK00054 4 PENMKIVENKEIAPNI--YTLVlDGEKVFDMKPGQFVMVWVPGVEPLLERPISISDIDKNEITILYRKVGEGTKKLSKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 80 VGDCLaDLVGPLGQ--PSHMEGlKKVAIVGGGVGNALAYPLAIGMHKAGIHVDMICGFKTKDIVILEDEFRAgVDRVFMM 157
Cdd:PRK00054 82 EGDEL-DIRGPLGNgfDLEEIG-GKVLLVGGGIGVAPLYELAKELKKKGVEVTTVLGARTKDEVIFEEEFAK-VGDVYVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 158 TDDGTYGEKGFTTDKLKALLdsgEKYDEIVAVGPAIMMKFVCGIAQDYGIPSVASLATYMIDGTGMCGGCRAIIGGEPKF 237
Cdd:PRK00054 159 TDDGSYGFKGFVTDVLDELD---SEYDAIYSCGPEIMMKKVVEILKEKKVPAYVSLERRMKCGIGACGACVCDTETGGKR 235
|
250
....*....|
gi 1222105945 238 VCVDGPDFDG 247
Cdd:PRK00054 236 VCKDGPVFSG 245
|
|
| DHOD_e_trans_like2 |
cd06220 |
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ... |
29-247 |
1.36e-43 |
|
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: 148.16 E-value: 1.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 29 HAKPGQFIILRVDEYGErIPITMAGHDAEKGtvdIIVQSVGRTSILLSQLNVGDCLAdLVGPLGQPSHMEGlKKVAIVGG 108
Cdd:cd06220 23 DFKPGQFVMVWVPGVDE-IPMSLSYIDGPNS---ITVKKVGEATSALHDLKEGDKLG-IRGPYGNGFELVG-GKVLLIGG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 109 GVGNALAYPLAiGMHKAGIHVDMICGFKTKDIVILEDEFRAgVDRVFMMTDDGTYGEKGFTTDKLKALLDsgEKYDEIVA 188
Cdd:cd06220 97 GIGIAPLAPLA-ERLKKAADVTVLLGARTKEELLFLDRLRK-SDELIVTTDDGSYGFKGFVTDLLKELDL--EEYDAIYV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1222105945 189 VGPAIMMKFVCGIAQDYGIPSVASLATYMIDGTGMCGGCraIIGGEPKFVCVDGPDFDG 247
Cdd:cd06220 173 CGPEIMMYKVLEILDERGVRAQFSLERYMKCGIGICGSC--CIDPTGLRVCRDGPVFDG 229
|
|
| sulfite_reductase_like |
cd06221 |
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ... |
6-246 |
3.40e-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: 3.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 6 IVNKRQLNDTINWYTI---YAPLVARHAKPGQFIILRVDEYGErIPITMAGHDAEKGTVDIIVQSVGRTSILLSQLNVGD 82
Cdd:cd06221 1 IVEVVDETEDIKTFTLrleDDDEELFTFKPGQFVMLSLPGVGE-APISISSDPTRRGPLELTIRRVGRVTEALHELKPGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 83 CLAdLVGPLGQP---SHMEGlKKVAIVGGGVGNALAYPLAIGMHKAGIH---VDMICGFKTKDIVILEDEF---RAGVD- 152
Cdd:cd06221 80 TVG-LRGPFGNGfpvEEMKG-KDLLLVAGGLGLAPLRSLINYILDNREDygkVTLLYGARTPEDLLFKEELkewAKRSDv 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 153 RVFMMTDDGTYGEKGFT---TDKLKALLDSGEKYDEIVaVGPAIMMKFVCGIAQDYGIPS---VASLATYMIDGTGMCGG 226
Cdd:cd06221 158 EVILTVDRAEEGWTGNVglvTDLLPELTLDPDNTVAIV-CGPPIMMRFVAKELLKLGVPEeqiWVSLERRMKCGVGKCGH 236
|
250 260
....*....|....*....|
gi 1222105945 227 CRaiIGgePKFVCVDGPDFD 246
Cdd:cd06221 237 CQ--IG--PKYVCKDGPVFS 252
|
|
| sulfite_red_B |
TIGR02911 |
sulfite reductase, subunit B; Members of this protein family include the B subunit, one of ... |
30-246 |
2.28e-18 |
|
sulfite reductase, subunit B; Members of this protein family include the B subunit, one of three subunits, of the anaerobic sulfite reductase of Salmonella, and close homologs from various Clostridum species, where the three-gene neighborhood is preserved. Two such gene clusters are found in Clostridium perfringens, but it may be that these sets of genes correspond to the distinct assimilatory and dissimilatory forms as seen in Clostridium pasteurianum. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 131957 [Multi-domain] Cd Length: 261 Bit Score: 82.15 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 30 AKPGQFIILRVDEYGERiPITMAGHDaeKGTVDIIVQSVGRTSILLSQLNVGDCLAdLVGPLGQPSHMEGL--KKVAIVG 107
Cdd:TIGR02911 31 VKPGQFFEVSLPKYGEA-PISVSGIG--EGYIDLTIRRVGKVTDEVFTLKEGDNLF-LRGPYGNGFDVDNYkhKELVVVA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 108 GGVGNA----LAYPLAIGMHKAGiHVDMICGFKTKDIVILEDEFRAGVDRV-FMMT----DDGTYGEKGFTTDKLKALLD 178
Cdd:TIGR02911 107 GGTGVApvkgVVEYFVKNPKEIK-SLNLILGFKTPDDILFKEDIAEWKGNInLTLTldeaEEDYKGNIGLVTKYIPELTL 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1222105945 179 SGEKYDEIVAVGPAIMMKFVCGIAQDYGIPSVASLATY---MIDGTGMCGGCRAiiggEPKFVCVDGPDFD 246
Cdd:TIGR02911 186 KDIEEVQAIVVGPPIMMKFTVQELLKKGIKEENIWVSYerkMCCGVGKCGHCKI----DDVYVCLDGPVFN 252
|
|
| PRK08345 |
PRK08345 |
cytochrome-c3 hydrogenase subunit gamma; Provisional |
31-259 |
8.69e-15 |
|
cytochrome-c3 hydrogenase subunit gamma; Provisional
Pssm-ID: 236247 [Multi-domain] Cd Length: 289 Bit Score: 72.92 E-value: 8.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 31 KPGQFIILRVDEYGErIPITMAGHDAEKGTVDIIVQSVGRTSILLSQLNVGDCLAdLVGPLGQ--P-SHMEGLkKVAIVG 107
Cdd:PRK08345 39 KPGQFVQVTIPGVGE-VPISICSSPTRKGFFELCIRRAGRVTTVIHRLKEGDIVG-VRGPYGNgfPvDEMEGM-DLLLIA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 108 GGVGNA-----LAYPLAIGMhKAGiHVDMICGFKTKDIVILEDE----FRAGVD---RVFMMTDDGT----YGEKGFTTD 171
Cdd:PRK08345 116 GGLGMAplrsvLLYAMDNRW-KYG-NITLIYGAKYYEDLLFYDElikdLAEAENvkiIQSVTRDPEWpgchGLPQGFIER 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 172 KLKAL---LDSGEKYD----EIVAVGPAIMMKFVCGIAQDYGIPS---VASLATYMIDGTGMCGGCraIIGGEP--KFVC 239
Cdd:PRK08345 194 VCKGVvtdLFREANTDpkntYAAICGPPVMYKFVFKELINRGYRPeriYVTLERRMRCGIGKCGHC--IVGTSTsiKYVC 271
|
250 260
....*....|....*....|
gi 1222105945 240 VDGPDFDGslidWDLLIKRG 259
Cdd:PRK08345 272 KDGPVFTY----FDILSTRG 287
|
|
| FNR_like |
cd00322 |
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ... |
29-208 |
9.26e-13 |
|
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: 65.93 E-value: 9.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 29 HAKPGQFIILRVDEYGERI--PITMAGHDAEKGTVDIIVQSV--GRTSILLSQLNVGDcLADLVGPLGQP-SHMEGLKKV 103
Cdd:cd00322 22 SFKPGQYVDLHLPGDGRGLrrAYSIASSPDEEGELELTVKIVpgGPFSAWLHDLKPGD-EVEVSGPGGDFfLPLEESGPV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 104 AIVGGGVGnaLAYPLAIGMH----KAGIHVDMICGFKTKDIVILEDEFRA------GVDRVFMMTDD---GTYGEKGFTT 170
Cdd:cd00322 101 VLIAGGIG--ITPFRSMLRHlaadKPGGEITLLYGARTPADLLFLDELEElakegpNFRLVLALSREseaKLGPGGRIDR 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 1222105945 171 DKLKALLDSGEKYDEIVAVGPAIMMKFVCGIAQDYGIP 208
Cdd:cd00322 179 EAEILALLPDDSGALVYICGPPAMAKAVREALVSLGVP 216
|
|
| DHODB_Fe-S_bind |
pfam10418 |
Iron-sulfur cluster binding domain of dihydroorotate dehydrogenase B; Lactococcus lactis is ... |
215-250 |
2.44e-08 |
|
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: 49.14 E-value: 2.44e-08
10 20 30
....*....|....*....|....*....|....*....
gi 1222105945 215 TYMIDGTGMCGGCR---AIIGGEPKFVCVDGPDFDGSLI 250
Cdd:pfam10418 2 ERMACGVGACGGCVvktKGGDGEYKRVCVDGPVFDADEV 40
|
|
| PRK06567 |
PRK06567 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Validated |
12-200 |
3.55e-08 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Validated
Pssm-ID: 235832 [Multi-domain] Cd Length: 1028 Bit Score: 54.53 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 12 LNDTINWYTIYAPLVARHAKPGQFiiLRVDEYGERI-----PITM--AGHDAEKGTVDIIVQSVGRTSILLSQLNVGDCL 84
Cdd:PRK06567 801 LDDKTFELIIHSPLAAKNFKFGQF--FRLQNYSEDAakliePVALspIDIDVEKGLISFIVFEVGKSTSLCKTLSENEKV 878
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 85 AdLVGPLGQPSHMEGLKKVAIVGGGVGNalayplaIGMHKA-GIHVDMICGFKTKDIVILEdefRAGVDRVFMMTDDGTY 163
Cdd:PRK06567 879 V-LMGPTGSPLEIPQNKKIVIVDFEVGN-------IGLLKVlKENNNEVIFVTYPDIKIRK---LVSVDIVIINASPEII 947
|
170 180 190
....*....|....*....|....*....|....*....
gi 1222105945 164 GEkgftTDKLKALLdSGEKYDEIVAVGPAI--MMKFVCG 200
Cdd:PRK06567 948 EE----LQSLKNEI-FGENTEIIVSVNSSMqcMMKGICG 981
|
|
| Fpr |
COG1018 |
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; |
3-208 |
7.47e-08 |
|
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
Pssm-ID: 440641 [Multi-domain] Cd Length: 231 Bit Score: 52.10 E-value: 7.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 3 RFEIVNKRQLNDTInwYTIY----APLVARHAKPGQFIILRVDEYGERIP----ITMAGHDaekGTVDIIVQSV--GR-T 71
Cdd:COG1018 5 PLRVVEVRRETPDV--VSFTleppDGAPLPRFRPGQFVTLRLPIDGKPLRraysLSSAPGD---GRLEITVKRVpgGGgS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 72 SILLSQLNVGDCLaDLVGPLGQ-PSHMEGLKKVAIVGGGVGNA-----LAYPLAIGMHKagiHVDMICGFKTKDIVILED 145
Cdd:COG1018 80 NWLHDHLKVGDTL-EVSGPRGDfVLDPEPARPLLLIAGGIGITpflsmLRTLLARGPFR---PVTLVYGARSPADLAFRD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1222105945 146 EFRAGVD-----RVFMMTDDGTYGEKGF-TTDKLKALLDSGEKyDEIVAVGPAIMMKFVCGIAQDYGIP 208
Cdd:COG1018 156 ELEALAArhprlRLHPVLSREPAGLQGRlDAELLAALLPDPAD-AHVYLCGPPPMMEAVRAALAELGVP 223
|
|
| FNR_iron_sulfur_binding |
cd06191 |
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
23-208 |
1.79e-06 |
|
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with a C-terminal iron-sulfur binding cluster domain. FNR 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 methnae assimilation in a variety of 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: 99788 [Multi-domain] Cd Length: 231 Bit Score: 47.91 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 23 APLVARHaKPGQFIILRVDEYGERI----PITMAGhdaEKGTVDIIVQSV--GRTS-ILLSQLNVGDCLaDLVGPLGQ-- 93
Cdd:cd06191 22 GPLQYGF-RPGQHVTLKLDFDGEELrrcySLCSSP---APDEISITVKRVpgGRVSnYLREHIQPGMTV-EVMGPQGHfv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 94 -PSHMEGlkKVAIVGGGVGnalAYPLaIGMHKA------GIHVDMICGFKTKDIVILEDEFR------AGVDRVFMMTDD 160
Cdd:cd06191 97 yQPQPPG--RYLLVAAGSG---ITPL-MAMIRAtlqtapESDFTLIHSARTPADMIFAQELReladkpQRLRLLCIFTRE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1222105945 161 G----TYGEKGFTTDKLKALLDSGEKYDEIVAVGPAIMMKFVCGIAQDYGIP 208
Cdd:cd06191 171 TldsdLLHGRIDGEQSLGAALIPDRLEREAFICGPAGMMDAVETALKELGMP 222
|
|
| phenol_2-monooxygenase_like |
cd06211 |
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ... |
5-194 |
8.54e-06 |
|
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use molecular oxygen as a substrate in the microbial degredation of phenol. This protein is encoded by a single gene and uses a tightly bound FAD cofactor in the NAD(P)H dependent conversion of phenol and O2 to catechol and H2O. This group is related to the NAD binding ferredoxin reductases.
Pssm-ID: 99807 Cd Length: 238 Bit Score: 45.78 E-value: 8.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 5 EIVNKRQLNDTIN--WYTIYAPLVARHaKPGQFIILRVDEYGERIPITMAGHDAEKGTVDIIVQSV--GR-TSILLSQLN 79
Cdd:cd06211 10 TVVEIEDLTPTIKgvRLKLDEPEEIEF-QAGQYVNLQAPGYEGTRAFSIASSPSDAGEIELHIRLVpgGIaTTYVHKQLK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 80 VGDCLaDLVGPLGQPSHMEGLKKVAIVGGGvGNALAYPLAI--GMHKAGI--HVDMICGFKTKDIVILEDEFRAGVDRVF 155
Cdd:cd06211 89 EGDEL-EISGPYGDFFVRDSDQRPIIFIAG-GSGLSSPRSMilDLLERGDtrKITLFFGARTRAELYYLDEFEALEKDHP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1222105945 156 MMT----------DDGTYGEKGFTTDKLKALLDSGEKYDEIVAVGPAIM 194
Cdd:cd06211 167 NFKyvpalsreppESNWKGFTGFVHDAAKKHFKNDFRGHKAYLCGPPPM 215
|
|
| FNR_iron_sulfur_binding_1 |
cd06215 |
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
31-208 |
1.74e-05 |
|
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: 44.89 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 31 KPGQFIILRVDEYGERI--PITMAGHDAEKGTVDIIVQSV--GRTS-ILLSQLNVGDCLaDLVGPLGQ---PSHMEglKK 102
Cdd:cd06215 29 KPGQFLTLELEIDGETVyrAYTLSSSPSRPDSLSITVKRVpgGLVSnWLHDNLKVGDEL-WASGPAGEftlIDHPA--DK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 103 VAIVGGGVG-----NALAYPLAIGMhKAGIHVDMICgfKTKDIVILEDEFR------AGVDRVFMMTDDGT---YGEKGF 168
Cdd:cd06215 106 LLLLSAGSGitpmmSMARWLLDTRP-DADIVFIHSA--RSPADIIFADELEelarrhPNFRLHLILEQPAPgawGGYRGR 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1222105945 169 TTDKLKALLDSGEKYDEIVAVGPAIMMKFVCGIAQDYGIP 208
Cdd:cd06215 183 LNAELLALLVPDLKERTVFVCGPAGFMKAVKSLLAELGFP 222
|
|
| PRK05802 |
PRK05802 |
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein; |
5-234 |
1.76e-05 |
|
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein;
Pssm-ID: 235613 [Multi-domain] Cd Length: 320 Bit Score: 45.35 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 5 EIVNKRQLNDTINWYTIYAP--LVARHAKPGQFIILRVDEYGE--RIPITMAGHDAEKGTVDIIVQSVGRTSILLSQLNV 80
Cdd:PRK05802 68 KIIKKENIEDNLIILTLKVPhkLARDLVYPGSFVFLRNKNSSSffDVPISIMEADTEENIIKVAIEIRGVKTKKIAKLNK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 81 GDCLAdLVGP-----LGQpSHMEGLK--KVAIVGGGVGNALAYPLAIGMHKAGIHVDMICG-FKTKDIVILE--DEFRAG 150
Cdd:PRK05802 148 GDEIL-LRGPywngiLGL-KNIKSTKngKSLVIARGIGQAPGVPVIKKLYSNGNKIIVIIDkGPFKNNFIKEylELYNIE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 151 VdRVFMMTDDGTYGEKGftTDKLKALLDSgEKYDEIVAVGPAIMMKFVCGIAQDYG--IPSVASLATYMIDGTGMCGGCR 228
Cdd:PRK05802 226 I-IELNLLDDGELSEEG--KDILKEIIKK-EDINLIHCGGSDILHYKIIEYLDKLNekIKLSCSNNAKMCCGEGICGACT 301
|
....*.
gi 1222105945 229 AIIGGE 234
Cdd:PRK05802 302 VRYGGH 307
|
|
| FNR_like_3 |
cd06198 |
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ... |
27-208 |
5.14e-05 |
|
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) domain, which varies 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: 99795 [Multi-domain] Cd Length: 216 Bit Score: 43.40 E-value: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 27 ARHAKPGQFIILRVDEYG-ERI-PITMAGHDAEKGTVDIIVQSVGR-TSILLSQLNVGDcLADLVGPLGQPSHMEGLKKV 103
Cdd:cd06198 20 ALGHRAGQFAFLRFDASGwEEPhPFTISSAPDPDGRLRFTIKALGDyTRRLAERLKPGT-RVTVEGPYGRFTFDDRRARQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 104 AIVGGGVG----NALAYPLAIgmHKAGIHVDMICGFKTKDIVILEDEFRAGVDR---VFMMTDDGTyGEKGFTTDKLKAL 176
Cdd:cd06198 99 IWIAGGIGitpfLALLEALAA--RGDARPVTLFYCVRDPEDAVFLDELRALAAAagvVLHVIDSPS-DGRLTLEQLVRAL 175
|
170 180 190
....*....|....*....|....*....|...
gi 1222105945 177 LDSGEKYDeiVAV-GPAIMMKFVCGIAQDYGIP 208
Cdd:cd06198 176 VPDLADAD--VWFcGPPGMADALEKGLRALGVP 206
|
|
| T4MO_e_transfer_like |
cd06190 |
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ... |
31-194 |
1.19e-04 |
|
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates toluene and forms p-cresol as part of a three component toluene-4-monoxygenase system. Electron transfer is from NADH to an NADH:ferredoxin oxidoreductase (TmoF in P. mendocina) to ferredoxin to an iron-containing oxygenase. TmoF is homologous to other mono- and dioxygenase systems within the ferredoxin reductase family.
Pssm-ID: 99787 Cd Length: 232 Bit Score: 42.24 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 31 KPGQFIILRVDEYGERIPITMAGHDAEKGTVDIIVQSV--GRTS-ILLSQLNVGDCLaDLVGPLG----QPShmEGLKKV 103
Cdd:cd06190 25 LPGQYALLALPGVEGARAYSMANLANASGEWEFIIKRKpgGAASnALFDNLEPGDEL-ELDGPYGlaylRPD--EDRDIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 104 AIVGggvGNALAYPLAI------GMHKAGIHVDMICGFKT-KDIVILeDEFRAGVD-----RVFMMTDDGT-------YG 164
Cdd:cd06190 102 CIAG---GSGLAPMLSIlrgaarSPYLSDRPVDLFYGGRTpSDLCAL-DELSALVAlgarlRVTPAVSDAGsgsaagwDG 177
|
170 180 190
....*....|....*....|....*....|
gi 1222105945 165 EKGFTTDKLKALLDSGEKYDEIVAVGPAIM 194
Cdd:cd06190 178 PTGFVHEVVEATLGDRLAEFEFYFAGPPPM 207
|
|
| MMO_FAD_NAD_binding |
cd06210 |
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ... |
32-208 |
1.08e-03 |
|
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent hydroxylation of methane to methanol. This multicomponent enzyme mediates electron transfer via a hydroxylase (MMOH), a coupling protein, and a reductase which is comprised of an N-terminal [2Fe-2S] ferredoxin domain, an FAD binding subdomain, and an NADH binding subdomain. Oxygenases oxidize hydrocarbons using dioxygen as the oxidant. Dioxygenases add both atom of oxygen to the substrate, while mono-oxygenases add one atom to the substrate and one atom to water.
Pssm-ID: 99806 Cd Length: 236 Bit Score: 39.63 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 32 PGQFIILRVDEYGERIPITMAGHDAEKGTVDIIVQSV--GRTSILLSQ-LNVGDCLaDLVGPLGQPSHME-GLKKVAIVG 107
Cdd:cd06210 37 PGQFVEIEIPGTDTRRSYSLANTPNWDGRLEFLIRLLpgGAFSTYLETrAKVGQRL-NLRGPLGAFGLREnGLRPRWFVA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222105945 108 GGVGNAlayPLAIGMHKAGIHVDM-----ICGFKTKDIVILEDEFRAGVD-------RVFMMTDDGTY-GEKGFTTDKLK 174
Cdd:cd06210 116 GGTGLA---PLLSMLRRMAEWGEPqearlFFGVNTEAELFYLDELKRLADslpnltvRICVWRPGGEWeGYRGTVVDALR 192
|
170 180 190
....*....|....*....|....*....|....
gi 1222105945 175 ALLDSGEKYDEIVAVGPAIMMKFVCGIAQDYGIP 208
Cdd:cd06210 193 EDLASSDAKPDIYLCGPPGMVDAAFAAAREAGVP 226
|
|
| PRK06847 |
PRK06847 |
hypothetical protein; Provisional |
97-132 |
9.36e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235874 [Multi-domain] Cd Length: 375 Bit Score: 37.16 E-value: 9.36e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1222105945 97 MEGLKKVAIVGGGVGNALAyplAIGMHKAGIHVDMI 132
Cdd:PRK06847 1 MAAVKKVLIVGGGIGGLSA---AIALRRAGIAVDLV 33
|
|
| |
