|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
1-470 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 651.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 1 MSQQFDLVVIGGGPGGYEAAIRAAQLGFKVACIEKRIH-NGKPSLGGTCLNVGCIPSKALLDSSHRYEATVHELAEHGIT 79
Cdd:PRK06327 1 MSKQFDVVVIGAGPGGYVAAIRAAQLGLKVACIEAWKNpKGKPALGGTCLNVGCIPSKALLASSEEFENAGHHFADHGIH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 80 TGEVKFDLDTLLARKDKVVDQLTGGVAQLLKGNGIEWLQGTGKLL----AGKKVEFTpfEGDVQVLEPKYVILATGSVPV 155
Cdd:PRK06327 81 VDGVKIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVgktdAGYEIKVT--GEDETVITAKHVIIATGSEPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 156 NIPVAPVDEDLIVDSTGALKFSEVPKRLGVIGAGVIGLELGSVWRRLGSEVVVFEALDAFLPMADKALAKEYQKILKKQG 235
Cdd:PRK06327 159 HLPGVPFDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAAADEQVAKEAAKAFTKQG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 236 LDIRIGAKVSGAETNGQEVTVKYNQA-GEDKEQVFDKLIVCVGRKAYAEGLLAEDSGIKLTERGLVDVNDQCQTSVEGVY 314
Cdd:PRK06327 239 LDIHLGVKIGEIKTGGKGVSVAYTDAdGEAQTLEVDKLIVSIGRVPNTDGLGLEAVGLKLDERGFIPVDDHCRTNVPNVY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 315 AIGDLVRGPMLAHKAMEEGVMAVERIHGHAAQVNYDTIISVIYTHPEAAWVGLTEEQAAEKGHEVKAGQFPFAVNGRALA 394
Cdd:PRK06327 319 AIGDVVRGPMLAHKAEEEGVAVAERIAGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLKAEGVEYKAGKFPFMANGRALA 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 696288927 395 AGDTAGFVKFVADAKTDRLLGMHVVGPNASDIVHQGMIALEFVSSVEDLQLMTFGHPTFSEVVHEAALSVDGRAIH 470
Cdd:PRK06327 399 MGEPDGFVKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEVWHEAALAVDKRPLH 474
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
2-467 |
0e+00 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 572.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 2 SQQFDLVVIGGGPGGYEAAIRAAQLGFKVACIEKRihngkpSLGGTCLNVGCIPSKALLDSSHRYEAtVHELAEHGITTG 81
Cdd:COG1249 1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKG------RLGGTCLNVGCIPSKALLHAAEVAHE-ARHAAEFGISAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 82 EVKFDLDTLLARKDKVVDQLTGGVAQLLKGNGIEWLQGTGKLLAGKKVEFTpfegDVQVLEPKYVILATGSVPVNIPVAP 161
Cdd:COG1249 74 APSVDWAALMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVT----GGETLTADHIVIATGSRPRVPPIPG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 162 VDEDLIVDSTGALKFSEVPKRLGVIGAGVIGLELGSVWRRLGSEVVVFEALDAFLPMADKALAKEYQKILKKQGLDIRIG 241
Cdd:COG1249 150 LDEVRVLTSDEALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 242 AKVSGAETNGQEVTVKYNQAGEDKEQVFDKLIVCVGRKAYAEGLLAEDSGIKLTERGLVDVNDQCQTSVEGVYAIGDLVR 321
Cdd:COG1249 230 AKVTSVEKTGDGVTVTLEDGGGEEAVEADKVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRTSVPGIYAIGDVTG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 322 GPMLAHKAMEEGVMAVERIHGH-AAQVNYDTIISVIYTHPEAAWVGLTEEQAAEKGHEVKAGQFPFAVNGRALAAGDTAG 400
Cdd:COG1249 310 GPQLAHVASAEGRVAAENILGKkPRPVDYRAIPSVVFTDPEIASVGLTEEEAREAGIDVKVGKFPFAANGRALALGETEG 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 696288927 401 FVKFVADAKTDRLLGMHVVGPNASDIVHQGMIALEFVSSVEDLQLMTFGHPTFSEVVHEAALSVDGR 467
Cdd:COG1249 390 FVKLIADAETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAALALLGR 456
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
1-471 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 537.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 1 MSQQFDLVVIGGGPGGYEAAIRAAQLGFKVACIEKRihngkpSLGGTCLNVGCIPSKALLDSSHRYEaTVHELAEHGITT 80
Cdd:PRK06416 1 FAFEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKE------KLGGTCLNRGCIPSKALLHAAERAD-EARHSEDFGIKA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 81 GEVKFDLDTLLARKDKVVDQLTGGVAQLLKGNGIEWLQGTGKLLAGKKVEFTPFEGDvQVLEPKYVILATGSVPVNIPVA 160
Cdd:PRK06416 74 ENVGIDFKKVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDGE-QTYTAKNIILATGSRPRELPGI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 161 PVDEDLIVDSTGALKFSEVPKRLGVIGAGVIGLELGSVWRRLGSEVVVFEALDAFLPMADKALAKEYQKILKKQGLDIRI 240
Cdd:PRK06416 153 EIDGRVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPGEDKEISKLAERALKKRGIKIKT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 241 GAKVSGAETNGQEVTVKYNQAGEDKEQVFDKLIVCVGRKAYAEGLLAEDSGIKlTERGLVDVNDQCQTSVEGVYAIGDLV 320
Cdd:PRK06416 233 GAKAKKVEQTDDGVTVTLEDGGKEETLEADYVLVAVGRRPNTENLGLEELGVK-TDRGFIEVDEQLRTNVPNIYAIGDIV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 321 RGPMLAHKAMEEGVMAVERIHGHAAQVNYDTIISVIYTHPEAAWVGLTEEQAAEKGHEVKAGQFPFAVNGRALAAGDTAG 400
Cdd:PRK06416 312 GGPMLAHKASAEGIIAAEAIAGNPHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFDVKVVKFPFAGNGKALALGETDG 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 696288927 401 FVKFVADAKTDRLLGMHVVGPNASDIVHQGMIALEFVSSVEDLQLMTFGHPTFSEVVHEAALSVDGRAIHA 471
Cdd:PRK06416 392 FVKLIFDKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEALGEAALAAAGKPLHA 462
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
5-470 |
0e+00 |
|
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.
Pssm-ID: 273568 [Multi-domain] Cd Length: 460 Bit Score: 536.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 5 FDLVVIGGGPGGYEAAIRAAQLGFKVACIEKrihngkPSLGGTCLNVGCIPSKALLDSSHRYEATVHeLAEHGITTGEVK 84
Cdd:TIGR01350 2 YDVIVIGGGPGGYVAAIRAAQLGLKVALVEK------EYLGGTCLNVGCIPTKALLHSAEVYDEIKH-AKDLGIEVENVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 85 FDLDTLLARKDKVVDQLTGGVAQLLKGNGIEWLQGTGKLLAGKKVEFTPfEGDVQVLEPKYVILATGSVPVNIPVA-PVD 163
Cdd:TIGR01350 75 VDWEKMQKRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTG-ENGEETLEAKNIIIATGSRPRSLPGPfDFD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 164 EDLIVDSTGALKFSEVPKRLGVIGAGVIGLELGSVWRRLGSEVVVFEALDAFLPMADKALAKEYQKILKKQGLDIRIGAK 243
Cdd:TIGR01350 154 GKVVITSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 244 VSGAETNGQEVTVKYNQAGEDKEQVfDKLIVCVGRKAYAEGLLAEDSGIKLTERGLVDVNDQCQTSVEGVYAIGDLVRGP 323
Cdd:TIGR01350 234 VTAVEKNDDQVTYENKGGETETLTG-EKVLVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDVIGGP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 324 MLAHKAMEEGVMAVERIHG-HAAQVNYDTIISVIYTHPEAAWVGLTEEQAAEKGHEVKAGQFPFAVNGRALAAGDTAGFV 402
Cdd:TIGR01350 313 MLAHVASHEGIVAAENIAGkEPAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGYDVKIGKFPFAANGKALALGETDGFV 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 696288927 403 KFVADAKTDRLLGMHVVGPNASDIVHQGMIALEFVSSVEDLQLMTFGHPTFSEVVHEAALSVDGRAIH 470
Cdd:TIGR01350 393 KIIADKKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEAIKEAALAALGKPIH 460
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
3-470 |
1.34e-162 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 467.73 E-value: 1.34e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 3 QQFDLVVIGGGPGGYEAAIRAAQLGFKVACIEKrihngkPSLGGTCLNVGCIPSKALLDSSHRYEaTVHELAEHGITTGE 82
Cdd:PRK06292 2 EKYDVIVIGAGPAGYVAARRAAKLGKKVALIEK------GPLGGTCLNVGCIPSKALIAAAEAFH-EAKHAEEFGIHADG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 83 VKFDLDTLLARKDKVVDQLTGGVAQ-LLKGNGIEWLQGTGKLLAGKKVEFtpfegDVQVLEPKYVILATGSVPVNIP-VA 160
Cdd:PRK06292 75 PKIDFKKVMARVRRERDRFVGGVVEgLEKKPKIDKIKGTARFVDPNTVEV-----NGERIEAKNIVIATGSRVPPIPgVW 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 161 PVDEDLIVDSTGALKFSEVPKRLGVIGAGVIGLELGSVWRRLGSEVVVFEALDAFLPMADKALAKEYQKILKKQgLDIRI 240
Cdd:PRK06292 150 LILGDRLLTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILSKE-FKIKL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 241 GAKVSGAETNGQEVTVKYNQAGEDKEQVFDKLIVCVGRKAYAEGLLAEDSGIKLTERGLVDVNDQCQTSVEGVYAIGDLV 320
Cdd:PRK06292 229 GAKVTSVEKSGDEKVEELEKGGKTETIEADYVLVATGRRPNTDGLGLENTGIELDERGRPVVDEHTQTSVPGIYAAGDVN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 321 RGPMLAHKAMEEGVMAVERI-HGHAAQVNYDTIISVIYTHPEAAWVGLTEEQAAEKGHEVKAGQFPFAVNGRALAAGDTA 399
Cdd:PRK06292 309 GKPPLLHEAADEGRIAAENAaGDVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEVPFEAQGRARVMGKND 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 696288927 400 GFVKFVADAKTDRLLGMHVVGPNASDIVHQGMIALEFVSSVEDLQLMTFGHPTFSEVVHEAALSVDGRAIH 470
Cdd:PRK06292 389 GFVKVYADKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRTALRDLFSKLIH 459
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
1-461 |
3.88e-99 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 305.59 E-value: 3.88e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 1 MSQQFDLVVIGGGPGGYEAAIRAAQLGFKVACIEKRihngkpSLGGTCLNVGCIPSKALLDSSHRYeATVHELAEHGIT- 79
Cdd:PRK06370 2 PAQRYDAIVIGAGQAGPPLAARAAGLGMKVALIERG------LLGGTCVNTGCVPTKTLIASARAA-HLARRAAEYGVSv 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 80 TGEVKFDLDTLLARKDKVVDQLTGGVAQLLKG-NGIEWLQGTGKLLAGKKVEFtpfegDVQVLEPKYVILATGSVPVNIP 158
Cdd:PRK06370 75 GGPVSVDFKAVMARKRRIRARSRHGSEQWLRGlEGVDVFRGHARFESPNTVRV-----GGETLRAKRIFINTGARAAIPP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 159 VAPVDEDLIVDSTGALKFSEVPKRLGVIGAGVIGLELGSVWRRLGSEVVVFEALDAFLPMADKALAKEYQKILKKQGLDI 238
Cdd:PRK06370 150 IPGLDEVGYLTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILEREGIDV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 239 RIGAKVSGAETNGQEVTVKYNQAGEDKEQVFDKLIVCVGRKAYAEGLLAEDSGIKLTERGLVDVNDQCQTSVEGVYAIGD 318
Cdd:PRK06370 230 RLNAECIRVERDGDGIAVGLDCNGGAPEITGSHILVAVGRVPNTDDLGLEAAGVETDARGYIKVDDQLRTTNPGIYAAGD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 319 LVRGPMLAHKAMEEGVMAVERIHGHAAQVNYDTIIS-VIYTHPEAAWVGLTEEQAAEKGHEVKAGQFPFAVNGRALAAGD 397
Cdd:PRK06370 310 CNGRGAFTHTAYNDARIVAANLLDGGRRKVSDRIVPyATYTDPPLARVGMTEAEARKSGRRVLVGTRPMTRVGRAVEKGE 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 696288927 398 TAGFVKFVADAKTDRLLGMHVVGPNASDIVHQGMIALEFVSSVEDLQLMTFGHPTFSEVVHEAA 461
Cdd:PRK06370 390 TQGFMKVVVDADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIPTLA 453
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
5-463 |
4.49e-96 |
|
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon for the detoxification of mercury compounds. MerA is a FAD-containing flavoprotein which reduces Hg(II) to Hg(0) utilizing NADPH. [Cellular processes, Detoxification]
Pssm-ID: 273944 [Multi-domain] Cd Length: 463 Bit Score: 297.80 E-value: 4.49e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 5 FDLVVIGGGPGGYEAAIRAAQLGFKVACIEKRIhngkpsLGGTCLNVGCIPSKALLDSSHRYEATvhELAEHGITTGEVK 84
Cdd:TIGR02053 1 YDLVIIGSGAAAFAAAIKAAELGASVAMVERGP------LGGTCVNVGCVPSKMLLRAAEVAHYA--RKPPFGGLAATVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 85 FDLDTLLARKDKVVDQL-TGGVAQLLKGNGIEWLQGTGKLLAGKKVEftpFEGDVQVLEPKYVILATGSVPVNIPVAPVD 163
Cdd:TIGR02053 73 VDFGELLEGKREVVEELrHEKYEDVLSSYGVDYLRGRARFKDPKTVK---VDLGREVRGAKRFLIATGARPAIPPIPGLK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 164 EDLIVDSTGALKFSEVPKRLGVIGAGVIGLELGSVWRRLGSEVVVFEALDAFLPMADKALAKEYQKILKKQGLDIRIGAK 243
Cdd:TIGR02053 150 EAGYLTSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSDRLLPREEPEISAAVEEALAEEGIEVVTSAQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 244 VSGAETNGQEVTVKYNQAGEDKEQVFDKLIVCVGRKAYAEGLLAEDSGIKLTERGLVDVNDQCQTSVEGVYAIGDLVRGP 323
Cdd:TIGR02053 230 VKAVSVRGGGKIITVEKPGGQGEVEADELLVATGRRPNTDGLGLEKAGVKLDERGGILVDETLRTSNPGIYAAGDVTGGL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 324 MLAHKAMEEGVMAVERIHGHA-AQVNYDTIISVIYTHPEAAWVGLTEEQAAEKGHEVKAGQFPFAVNGRALAAGDTAGFV 402
Cdd:TIGR02053 310 QLEYVAAKEGVVAAENALGGAnAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNVPRARINRDTRGFI 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 696288927 403 KFVADAKTDRLLGMHVVGPNASDIVHQGMIALEFVSSVEDLQLMTFGHPTFSEVVHEAALS 463
Cdd:TIGR02053 390 KLVAEPGTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGLKLAAQT 450
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
1-462 |
2.76e-89 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 280.12 E-value: 2.76e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 1 MSQQFDLVVIGGGPGGYEAAIRAAQLGFKVACIEKRihngkPSLGGTCLNVGCIPSKALLDS-SHRYEATVHELAEHGIT 79
Cdd:PRK05249 2 HMYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIERY-----RNVGGGCTHTGTIPSKALREAvLRLIGFNQNPLYSSYRV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 80 TGEVKFDldTLLARKDKVVDQLTGGVAQLLKGNGIEWLQGTGKLLAGKKVEFTPFEGDVQVLEPKYVILATGSVPVNIPV 159
Cdd:PRK05249 77 KLRITFA--DLLARADHVINKQVEVRRGQYERNRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATGSRPYRPPD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 160 APVDEDLIVDSTGALKFSEVPKRLGVIGAGVIGLELGSVWRRLGSEVVVFEALDAFLPMADKALAKEYQKILKKQGLDIR 239
Cdd:PRK05249 155 VDFDHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSFLDDEISDALSYHLRDSGVTIR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 240 IGAKVSGAETNGQEVTVKYnQAGedKEQVFDKLIVCVGRKAYAEGLLAEDSGIKLTERGLVDVNDQCQTSVEGVYAIGDL 319
Cdd:PRK05249 235 HNEEVEKVEGGDDGVIVHL-KSG--KKIKADCLLYANGRTGNTDGLNLENAGLEADSRGQLKVNENYQTAVPHIYAVGDV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 320 VRGPMLAHKAMEEGVMAVERIHGHAAQVNYDTIISVIYTHPEAAWVGLTEEQAAEKG--HEVkaGQFPFAVNGRALAAGD 397
Cdd:PRK05249 312 IGFPSLASASMDQGRIAAQHAVGEATAHLIEDIPTGIYTIPEISSVGKTEQELTAAKvpYEV--GRARFKELARAQIAGD 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 696288927 398 TAGFVKFVADAKTDRLLGMHVVGPNASDIVHQGMIALEFVSSVEDLQLMTFGHPTFSEVVHEAAL 462
Cdd:PRK05249 390 NVGMLKILFHRETLEILGVHCFGERATEIIHIGQAIMEQKGTIEYFVNTTFNYPTMAEAYRVAAL 454
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
3-455 |
1.17e-82 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 261.99 E-value: 1.17e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 3 QQFDLVVIGGGPGGYEAAIRAAQLGFKVACIEKrihnGKPSLGGTCLNVGCIPSKALLDSshryeatvhelAEHGITTGE 82
Cdd:PRK07251 2 LTYDLIVIGFGKAGKTLAAKLASAGKKVALVEE----SKAMYGGTCINIGCIPTKTLLVA-----------AEKNLSFEQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 83 VkfdldtlLARKDKVVDQLTGGVAQLLKGNGIEWLQGTGKLLAGKKVEFTPFEgDVQVLEPKYVILATGSVPVNIPVAPV 162
Cdd:PRK07251 67 V-------MATKNTVTSRLRGKNYAMLAGSGVDLYDAEAHFVSNKVIEVQAGD-EKIELTAETIVINTGAVSNVLPIPGL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 163 DEDL-IVDSTGALKFSEVPKRLGVIGAGVIGLELGSVWRRLGSEVVVFEALDAFLPMADKALAKEYQKILKKQGLDIRIG 241
Cdd:PRK07251 139 ADSKhVYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYMEEDGITFLLN 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 242 AKVSGAETNGQEVTVKYNqageDKEQVFDKLIVCVGRKAYAEGLLAEDSGIKLTERGLVDVNDQCQTSVEGVYAIGDLVR 321
Cdd:PRK07251 219 AHTTEVKNDGDQVLVVTE----DETYRFDALLYATGRKPNTEPLGLENTDIELTERGAIKVDDYCQTSVPGVFAVGDVNG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 322 GPMLAHKAMEEGVMAVERIHGhAAQVNYDT---IISVIYTHPEAAWVGLTEEQAAEKGHEVKAGQFPFAVNGRALAAGDT 398
Cdd:PRK07251 295 GPQFTYISLDDFRIVFGYLTG-DGSYTLEDrgnVPTTMFITPPLSQVGLTEKEAKEAGLPYAVKELLVAAMPRAHVNNDL 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 696288927 399 AGFVKFVADAKTDRLLGMHVVGPNASDIVHQGMIALEFVSSVEDLQLMTFGHPTFSE 455
Cdd:PRK07251 374 RGAFKVVVNTETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAE 430
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
1-434 |
3.04e-81 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 258.93 E-value: 3.04e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 1 MSQQFDLVVIGGGPGGYEAAIRAAQLGFKVACIEKRihngkpSLGGTCLNVGCIPSKALLDSSHRYEATVHELAEHGITT 80
Cdd:PRK06116 1 MTKDYDLIVIGGGSGGIASANRAAMYGAKVALIEAK------RLGGTCVNVGCVPKKLMWYGAQIAEAFHDYAPGYGFDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 81 GEVKFDLDTLLARKDKVVDQLTGGVAQLLKGNGIEWLQGTGKLLAGKKVEFtpfeGDVQVLEPKYVIlATGSVPV--NIP 158
Cdd:PRK06116 75 TENKFDWAKLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEV----NGERYTADHILI-ATGGRPSipDIP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 159 VApvdeDLIVDSTGALKFSEVPKRLGVIGAGVIGLELGSVWRRLGSEVVVFEALDAFLPMADKALAKEYQKILKKQGLDI 238
Cdd:PRK06116 150 GA----EYGITSDGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 239 RIGAKVSGAETNGQ-EVTVKYNQAgedKEQVFDKLIVCVGRKAYAEGLLAEDSGIKLTERGLVDVNDQCQTSVEGVYAIG 317
Cdd:PRK06116 226 HTNAVPKAVEKNADgSLTLTLEDG---ETLTVDCLIWAIGREPNTDGLGLENAGVKLNEKGYIIVDEYQNTNVPGIYAVG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 318 DLVRGPMLAHKAMEEGVMAVERIHGH--AAQVNYDTIISVIYTHPEAAWVGLTEEQAAEKGHE--VKAGQFPFAVNGRAL 393
Cdd:PRK06116 303 DVTGRVELTPVAIAAGRRLSERLFNNkpDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEdnVKVYRSSFTPMYTAL 382
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 696288927 394 AAGDTAGFVKFVADAKTDRLLGMHVVGPNASDIVhQGM-IAL 434
Cdd:PRK06116 383 TGHRQPCLMKLVVVGKEEKVVGLHGIGFGADEMI-QGFaVAI 423
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
5-333 |
5.36e-78 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 245.69 E-value: 5.36e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 5 FDLVVIGGGPGGYEAAIRAAQLGFKVACIEkrihngkpsLGGTCLNVGCIPSKALLDSSHRYEATVHELAehgittgevk 84
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIE---------DEGTCPYGGCVLSKALLGAAEAPEIASLWAD---------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 85 fdldtLLARKDKVVDQLTGGVAQLLKGNGIEWLQGTGKLLAGKKVEftpfeGDVQVLEPKYVILATGSVPVNIPVAPVDE 164
Cdd:pfam07992 62 -----LYKRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELVD-----GDGETITYDRLVIATGARPRLPPIPGVEL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 165 DLI-----VDSTGALKFSEVPKRLGVIGAGVIGLELGSVWRRLGSEVVVFEALDAFLPMADKALAKEYQKILKKQGLDIR 239
Cdd:pfam07992 132 NVGflvrtLDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 240 IGAKVSGAETNGQEVTVKynqaGEDKEQV-FDKLIVCVGRKAYAEglLAEDSGIKLTERGLVDVNDQCQTSVEGVYAIGD 318
Cdd:pfam07992 212 LGTSVKEIIGDGDGVEVI----LKDGTEIdADLVVVAIGRRPNTE--LLEAAGLELDERGGIVVDEYLRTSVPGIYAAGD 285
|
330
....*....|....*.
gi 696288927 319 -LVRGPMLAHKAMEEG 333
Cdd:pfam07992 286 cRVGGPELAQNAVAQG 301
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
3-470 |
1.30e-73 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 244.44 E-value: 1.30e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 3 QQFDLVVIGGGPGGYEAAIRAAQLGFKVACIEkrihNGKPSLGGTCLNVGCIPSKALLDSSHRYEA--TVHELAEHGITT 80
Cdd:PTZ00153 115 EEYDVGIIGCGVGGHAAAINAMERGLKVIIFT----GDDDSIGGTCVNVGCIPSKALLYATGKYRElkNLAKLYTYGIYT 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 81 ------------------GEVKFDLDTLLARKDKVVDQLTGGVAQLLKGNGI----EWLQGTG-------KLLAGKKVEF 131
Cdd:PTZ00153 191 nafkngkndpvernqlvaDTVQIDITKLKEYTQSVIDKLRGGIENGLKSKKFcknsEHVQVIYerghivdKNTIKSEKSG 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 132 TPFEgdvqvlePKYVILATGSVPvNIPV-APVDEDLIVDSTGALKFSEVPKRLGVIGAGVIGLELGSVWRRLGSEVVVFE 210
Cdd:PTZ00153 271 KEFK-------VKNIIIATGSTP-NIPDnIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFE 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 211 ALDAFLPMADKALAKEYQKI-LKKQGLDIRIGAKVS--GAETNGQEVTVKYN--QAGED----------KEQVFDKLIVC 275
Cdd:PTZ00153 343 YSPQLLPLLDADVAKYFERVfLKSKPVRVHLNTLIEyvRAGKGNQPVIIGHSerQTGESdgpkknmndiKETYVDSCLVA 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 276 VGRKAYAEGLLAEDSGIKLtERGLVDVNDQCQTSVE------GVYAIGDLVRGPMLAHKAMEEGVMAVERIHGHAAQ--- 346
Cdd:PTZ00153 423 TGRKPNTNNLGLDKLKIQM-KRGFVSVDEHLRVLREdqevydNIFCIGDANGKQMLAHTASHQALKVVDWIEGKGKEnvn 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 347 ----------VNYDTIISVIYTHPEAAWVGLTEEQAAEKG--HEVKAGQFPFAVNGRALAAGD----------------- 397
Cdd:PTZ00153 502 invenwaskpIIYKNIPSVCYTTPELAFIGLTEKEAKELYppDNVGVEISFYKANSKVLCENNisfpnnsknnsynkgky 581
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 696288927 398 -----TAGFVKFVADAKTDRLLGMHVVGPNASDIVHQGMIALEFVSSVEDLQLMTFGHPTFSEVVHEAALSVDGRAIH 470
Cdd:PTZ00153 582 ntvdnTEGMVKIVYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDAAFKAIAGVRTH 659
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
3-459 |
3.41e-64 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 214.26 E-value: 3.41e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 3 QQFDLVVIGGGPGGYEAAIRAAQLGFKVACIEKrihnGKPSLGGTCLNVGCIPSKALldsshryeatVHELAEHGittge 82
Cdd:NF040477 2 NHYQAIIIGFGKAGKTLAATLAKAGWRVAIIEQ----SAQMYGGTCINIGCIPTKTL----------VHDAEQHQ----- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 83 vkfDLDTLLARKDKVVDQLTGGVAQLLKG-NGIEWLQGTGKLLAGKKVEFTPFEGDvQVLEPKYVILATGSVPVNIPVAP 161
Cdd:NF040477 63 ---DFSTAMQRKSSVVGFLRDKNYHNLADlDNVDVINGRAEFIDNHTLRVFQADGE-QELRGEKIFINTGAQSVLPPIPG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 162 VDEDLIV-DSTGALKFSEVPKRLGVIGAGVIGLELGSVWRRLGSEVVVFEALDAFLPMADKALAKEYQKILKKQGLDIRI 240
Cdd:NF040477 139 LTTTPGVyDSTGLLNLTQLPARLGILGGGYIGVEFASMFARFGSKVTIFEAAELFLPREDRDIAQAIATILQDQGVELIL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 241 GAKVSGAETNGQEVTVKYNQAgedkEQVFDKLIVCVGRKAYAEGLLAEDSGIKLTERGLVDVNDQCQTSVEGVYAIGDLV 320
Cdd:NF040477 219 NAQVQRVSSHEGEVQLETAEG----VLTVDALLVASGRKPATAGLQLQNAGVAVNERGAIVVDKYLRTTADNIWAMGDVT 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 321 RGPMLAHKAMEEGVMAVERIHGHAAQVNYD--TIISVIYTHPEAAWVGLTEEQAAEKGHEVKAGQFPFAVNGRALAAGDT 398
Cdd:NF040477 295 GGLQFTYISLDDFRIVRDSLLGEGKRSTDDrqNVPYSVFMTPPLSRIGMTEEQARASGADIQVVTLPVAAIPRARVMNDT 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 696288927 399 AGFVKFVADAKTDRLLGMHVVGPNASDIVHQGMIALEFVSSVEDLQLMTFGHPTFSEVVHE 459
Cdd:NF040477 375 RGVLKAVVDNKTQRILGVSLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSESLND 435
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
5-466 |
3.70e-61 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 206.34 E-value: 3.70e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 5 FDLVVIGGGPGGYEAAIRAAQLgfKVACIEKRihngkpSLGGTCLNVGCIPSKALLdsshrYEATVHELAEHGittgeVK 84
Cdd:PRK07846 2 YDLIIIGTGSGNSILDERFADK--RIAIVEKG------TFGGTCLNVGCIPTKMFV-----YAADVARTIREA-----AR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 85 FDLDTLLARKD--KVVDQLTGGVAQLLKGN---------GIEWLQGTGKLLAGKKVEFtpfeGDVQVLEPKYVILATGSV 153
Cdd:PRK07846 64 LGVDAELDGVRwpDIVSRVFGRIDPIAAGGeeyrgrdtpNIDVYRGHARFIGPKTLRT----GDGEEITADQVVIAAGSR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 154 PVnIPVAPVDEDLIVD-STGALKFSEVPKRLGVIGAGVIGLELGSVWRRLGSEVVVFEALDAFLPMADKALAKEYQKILK 232
Cdd:PRK07846 140 PV-IPPVIADSGVRYHtSDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLDDDISERFTELAS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 233 KQgLDIRIGAKVSGAETNGQEVTVkynQAGEDKEQVFDKLIVCVGRKAYAEGLLAEDSGIKLTERGLVDVNDQCQTSVEG 312
Cdd:PRK07846 219 KR-WDVRLGRNVVGVSQDGSGVTL---RLDDGSTVEADVLLVATGRVPNGDLLDAAAAGVDVDEDGRVVVDEYQRTSAEG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 313 VYAIGDLVRGPMLAHKAMEEgvMAVER---IHGHAAQV-NYDTIISVIYTHPEAAWVGLTEEQAAEKGHEVKAGQFPFAV 388
Cdd:PRK07846 295 VFALGDVSSPYQLKHVANHE--ARVVQhnlLHPDDLIAsDHRFVPAAVFTHPQIASVGLTENEARAAGLDITVKVQNYGD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 389 NGRALAAGDTAGFVKFVADAKTDRLLGMHVVGPNASDIVhQGMIalefvssvedlQLMTFG-------------HPTFSE 455
Cdd:PRK07846 373 VAYGWAMEDTTGFVKLIADRDTGRLLGAHIIGPQASTLI-QPLI-----------QAMSFGldaremargqywiHPALPE 440
|
490
....*....|.
gi 696288927 456 VVHEAALSVDG 466
Cdd:PRK07846 441 VVENALLGLDL 451
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
2-455 |
1.01e-60 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 208.08 E-value: 1.01e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 2 SQQFDLVVIGGGPGGYEAAIRAAQLGFKVACIEKRIhngkpsLGGTCLNVGCIPSKALLDSSHryeaTVHELAEH----G 77
Cdd:PRK13748 96 ERPLHVAVIGSGGAAMAAALKAVEQGARVTLIERGT------IGGTCVNVGCVPSKIMIRAAH----IAHLRRESpfdgG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 78 ITTGEVKFDLDTLLARKDKVVDQLTGGVAQ-LLKGN-GIEWLQGTGKLLAGKKVEFTPFEGDVQVLEPKYVILATGSVPV 155
Cdd:PRK13748 166 IAATVPTIDRSRLLAQQQARVDELRHAKYEgILDGNpAITVLHGEARFKDDQTLIVRLNDGGERVVAFDRCLIATGASPA 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 156 NIPVAPVDEDLIVDSTGALKFSEVPKRLGVIGAGVIGLELGSVWRRLGSEVVVFeALDAFLPMADKALAKEYQKILKKQG 235
Cdd:PRK13748 246 VPPIPGLKETPYWTSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTIL-ARSTLFFREDPAIGEAVTAAFRAEG 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 236 LDIRIGAKVSGAETNGQEVTVKYNQaGEDKEqvfDKLIVCVGRKAYAEGLLAEDSGIKLTERGLVDVNDQCQTSVEGVYA 315
Cdd:PRK13748 325 IEVLEHTQASQVAHVDGEFVLTTGH-GELRA---DKLLVATGRAPNTRSLALDAAGVTVNAQGAIVIDQGMRTSVPHIYA 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 316 IGDLVRGPMLAHKAMEEGVMAVERIHGHAAQVNYDTIISVIYTHPEAAWVGLTEEQAAEKGHEVKAGQFPFAVNGRALAA 395
Cdd:PRK13748 401 AGDCTDQPQFVYVAAAAGTRAAINMTGGDAALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRTLTLDNVPRALAN 480
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 396 GDTAGFVKFVADAKTDRLLGMHVVGPNASDIVHQGMIALEFVSSVEDLQLMTFGHPTFSE 455
Cdd:PRK13748 481 FDTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAALAIRNRMTVQELADQLFPYLTMVE 540
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
3-455 |
1.16e-60 |
|
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important reductant, e.g., for maintaining the cellular thiol/disulfide status and for protecting against reactive oxygen species such as hydrogen peroxide. Glutathione-disulfide reductase regenerates reduced glutathione from oxidized glutathione (glutathione disulfide) + NADPH. This model represents one of two closely related subfamilies of glutathione-disulfide reductase. Both are closely related to trypanothione reductase, and separate models are built so each of the three can describe proteins with conserved function. This model describes glutathione-disulfide reductases of animals, yeast, and a number of animal-resident bacteria. [Energy metabolism, Electron transport]
Pssm-ID: 273614 [Multi-domain] Cd Length: 450 Bit Score: 205.07 E-value: 1.16e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 3 QQFDLVVIGGGPGGYEAAIRAAQLGFKVACIEKRihngkpSLGGTCLNVGCIPSKALLDSSHRYEaTVHELAEHGI-TTG 81
Cdd:TIGR01421 1 KHYDYLVIGGGSGGIASARRAAEHGAKALLVEAK------KLGGTCVNVGCVPKKVMWYASDLAE-RMHDAADYGFyQND 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 82 EVKFDLDTLLARKDKVVDQLTGGVAQLLKGNGIEWLQGtgkllagkKVEFTPfEGDVQVLEPKY----VILATG---SVP 154
Cdd:TIGR01421 74 ENTFNWPELKEKRDAYVDRLNGIYQKNLEKNKVDVIFG--------HARFTK-DGTVEVNGRDYtaphILIATGgkpSFP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 155 VNIPvapvDEDLIVDSTGALKFSEVPKRLGVIGAGVIGLELGSVWRRLGSEVVVF----EALDAFLPMADKALAKEYQki 230
Cdd:TIGR01421 145 ENIP----GAELGTDSDGFFALEELPKRVVIVGAGYIAVELAGVLHGLGSETHLVirheRVLRSFDSMISETITEEYE-- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 231 lkKQGLDIRIGAKVSGAETNGQEVTVKYNQAGEDKEQVfDKLIVCVGRKAYAEGLLAEDSGIKLTERGLVDVNDQCQTSV 310
Cdd:TIGR01421 219 --KEGINVHKLSKPVKVEKTVEGKLVIHFEDGKSIDDV-DELIWAIGRKPNTKGLGLENVGIKLNEKGQIIVDEYQNTNV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 311 EGVYAIGDLVRGPMLAHKAMEEGVMAVERIHGHA--AQVNYDTIISVIYTHPEAAWVGLTEEQAAEK-GHE-VKAGQFPF 386
Cdd:TIGR01421 296 PGIYALGDVVGKVELTPVAIAAGRKLSERLFNGKtdDKLDYNNVPTVVFSHPPIGTIGLTEKEAIEKyGKEnIKVYNSSF 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 696288927 387 AVNGRALAAGDTAGFVKFVADAKTDRLLGMHVVGPNASDIVHQGMIALEFVSSVEDLQLMTFGHPTFSE 455
Cdd:TIGR01421 376 TPMYYAMTSEKQKCRMKLVCAGKEEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSE 444
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
4-459 |
9.26e-58 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 197.16 E-value: 9.26e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 4 QFDLVVIGGGPGGYEAAIRAAQLGFKVACIEKrihnGKPSLGGTCLNVGCIPSKALldsshryeatVHELAEHGittgev 83
Cdd:PRK08010 3 KYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQ----SNAMYGGTCINIGCIPTKTL----------VHDAQQHT------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 84 kfDLDTLLARKDKVVDQLTG-GVAQLLKGNGIEWLQGTGKLLAGKKVEFTPFEGDvQVLEPKYVILATGSVPVNIPVAPV 162
Cdd:PRK08010 63 --DFVRAIQRKNEVVNFLRNkNFHNLADMPNIDVIDGQAEFINNHSLRVHRPEGN-LEIHGEKIFINTGAQTVVPPIPGI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 163 DEDL-IVDSTGALKFSEVPKRLGVIGAGVIGLELGSVWRRLGSEVVVFEALDAFLPMADKALAKEYQKILKKQGLDIRIG 241
Cdd:PRK08010 140 TTTPgVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 242 AKVSGAETNGQEVTVKynqaGEDKEQVFDKLIVCVGRKAYAEGLLAEDSGIKLTERGLVDVNDQCQTSVEGVYAIGDLVR 321
Cdd:PRK08010 220 AHVERISHHENQVQVH----SEHAQLAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKYLHTTADNIWAMGDVTG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 322 GPMLAHKAMEEGVMAVERIHGHAAQVNYD--TIISVIYTHPEAAWVGLTEEQAAEKGHEVKAGQFPFAVNGRALAAGDTA 399
Cdd:PRK08010 296 GLQFTYISLDDYRIVRDELLGEGKRSTDDrkNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDTR 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 400 GFVKFVADAKTDRLLGMHVVGPNASDIVHQGMIALEFVSSVEDLQLMTFGHPTFSEVVHE 459
Cdd:PRK08010 376 GVLKAIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLND 435
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
5-455 |
1.09e-53 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 189.06 E-value: 1.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 5 FDLVVIGGGPGGYEAAIRAAQLGFKVACIEKRIhngkpsLGGTCLNVGCIPSKALLDSshryeATVHELAE----HGITT 80
Cdd:PTZ00058 49 YDLIVIGGGSGGMAAARRAARNKAKVALVEKDY------LGGTCVNVGCVPKKIMFNA-----ASIHDILEnsrhYGFDT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 81 GEVkFDLDTLLARKDKVVDQLTGGVAQLLKGNGIEWLQGTGKLLAGKKV------------------EFTPFEGDV---- 138
Cdd:PTZ00058 118 QFS-FNLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVlikkvsqvdgeadesdddEVTIVSAGVsqld 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 139 --QVLEPKYVILATGSVPVNIPVAPVDedLIVDSTGALKFSEvPKRLGVIGAGVIGLELGSVWRRLGSEVVVFEALDAFL 216
Cdd:PTZ00058 197 dgQVIEGKNILIAVGNKPIFPDVKGKE--FTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 217 PMADKALAKEYQKILKKQGLDIRIGAKVSGAETNGQEVTVKYNQAGEdKEQVFDKLIVCVGRKAYAEGLLAEDSGIKlTE 296
Cdd:PTZ00058 274 RKFDETIINELENDMKKNNINIITHANVEEIEKVKEKNLTIYLSDGR-KYEHFDYVIYCVGRSPNTEDLNLKALNIK-TP 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 297 RGLVDVNDQCQTSVEGVYAIGDLV------------------RGPMLAHK----------------AMEEGVMAVERIHG 342
Cdd:PTZ00058 352 KGYIKVDDNQRTSVKHIYAVGDCCmvkknqeiedlnllklynEEPYLKKKentsgesyynvqltpvAINAGRLLADRLFG 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 343 HAAQV-NYDTIISVIYTHPEAAWVGLTEEQAAEK-GHE-VKAGQFPFAVNGRALAAGDTAG----FVKFVADAKTDRLLG 415
Cdd:PTZ00058 432 PFSRTtNYKLIPSVIFSHPPIGTIGLSEQEAIDIyGKEnVKIYESRFTNLFFSVYDMDPAQkektYLKLVCVGKEELIKG 511
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 696288927 416 MHVVGPNASDIVHQGMIALEFVSSVEDLQLMTFGHPTFSE 455
Cdd:PTZ00058 512 LHIVGLNADEILQGFAVALKMNATKADFDETIPIHPTAAE 551
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
5-435 |
4.83e-53 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 186.17 E-value: 4.83e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 5 FDLVVIGGGPGGYEAAIRAAQLGFKVACIEKRIH----NGKPSLGGTCLNVGCIPSKALLDSSHrYEATVHELAEHGI-T 79
Cdd:PLN02507 26 FDLFVIGAGSGGVRAARFSANFGAKVGICELPFHpissESIGGVGGTCVIRGCVPKKILVYGAT-FGGEFEDAKNYGWeI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 80 TGEVKFDLDTLLARKDKVVDQLTGGVAQLLKGNGIEWLQGTGKLLAGKKVEFTPFEGDVQVLEPKYVILATGS--VPVNI 157
Cdd:PLN02507 105 NEKVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRYTAKHILIATGSraQRPNI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 158 PvapvDEDLIVDSTGALKFSEVPKRLGVIGAGVIGLELGSVWRRLGSEVVVFEALDAFLPMADKALAKEYQKILKKQGLD 237
Cdd:PLN02507 185 P----GKELAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRAVVARNLEGRGIN 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 238 IRIGAKVSGAETNGQEVTVkYNQAGEdkEQVFDKLIVCVGRKAYAEGLLAEDSGIKLTERGLVDVNDQCQTSVEGVYAIG 317
Cdd:PLN02507 261 LHPRTNLTQLTKTEGGIKV-ITDHGE--EFVADVVLFATGRAPNTKRLNLEAVGVELDKAGAVKVDEYSRTNIPSIWAIG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 318 DLVRGPMLAHKAMEEGV-MAVERIHGHAAQVNYDTIISVIYTHPEAAWVGLTEEQAAEKGH-EVKAGQFPFAVNGRALAA 395
Cdd:PLN02507 338 DVTNRINLTPVALMEGTcFAKTVFGGQPTKPDYENVACAVFCIPPLSVVGLSEEEAVEQAKgDILVFTSSFNPMKNTISG 417
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 696288927 396 GDTAGFVKFVADAKTDRLLGMHVVGPNASDIVhQGM-IALE 435
Cdd:PLN02507 418 RQEKTVMKLIVDAETDKVLGASMCGPDAPEIM-QGIaVALK 457
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
7-461 |
1.61e-51 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 181.21 E-value: 1.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 7 LVVIGGGPGGYEAAIRAAQLGFKVACIEKRihngkpSLGGTCLNVGCIPSKALLDSSHRyEATVHELAEHGITT---GEV 83
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIERD------GLGGAAVLTDCVPSKTLIATAEV-RTELRRAAELGIRFiddGEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 84 KFDLDTLLARKDKVVDQLTGGVAQLLKGNGIEWLQGTGKL----LAGKKVEFTPFEGDVQVLEPKYVILATGSVPVNIPV 159
Cdd:PRK07845 77 RVDLPAVNARVKALAAAQSADIRARLEREGVRVIAGRGRLidpgLGPHRVKVTTADGGEETLDADVVLIATGASPRILPT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 160 APVDEDLIVDSTGALKFSEVPKRLGVIGAGVIGLELGSVWRRLGSEVVVFEALDAFLPMADKALAKEYQKILKKQGLDIR 239
Cdd:PRK07845 157 AEPDGERILTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPGEDADAAEVLEEVFARRGMTVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 240 IGAKVSGAETNGQEVTVKYnqagEDKEQVF-DKLIVCVGRKAYAEGLLAEDSGIKLTERGLVDVNDQCQTSVEGVYAIGD 318
Cdd:PRK07845 237 KRSRAESVERTGDGVVVTL----TDGRTVEgSHALMAVGSVPNTAGLGLEEAGVELTPSGHITVDRVSRTSVPGIYAAGD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 319 LVRGPMLAHKAMEEGVMAVERIHGHAAQ-VNYDTIISVIYTHPEAAWVGLTEEQAAEKGHEVKAGQFPFAVNGRALAAGD 397
Cdd:PRK07845 313 CTGVLPLASVAAMQGRIAMYHALGEAVSpLRLKTVASNVFTRPEIATVGVSQAAIDSGEVPARTVMLPLATNPRAKMSGL 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 696288927 398 TAGFVKFVADAKTDRLLGMHVVGPNASDIVHQGMIALEFVSSVEDLQLmTFG-HPTFSEVVHEAA 461
Cdd:PRK07845 393 RDGFVKLFCRPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQ-TFTvYPSLSGSITEAA 456
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
2-455 |
1.66e-51 |
|
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase.
Pssm-ID: 200098 [Multi-domain] Cd Length: 486 Bit Score: 181.71 E-value: 1.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 2 SQQFDLVVIGGGPGGYEAAIRAAQL-GFKVACIEKRIHNGKP---SLGGTCLNVGCIPSKaLLDSSHRYEATVHELAEHG 77
Cdd:TIGR01423 1 SKAFDLVVIGAGSGGLEAGWNAATLyKKRVAVVDVQTHHGPPfyaALGGTCVNVGCVPKK-LMVTGAQYMDTLRESAGFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 78 --ITTGEVKFDLDTLLARKDKVVDQLTGGVAQLLKGN-GIEWLQGTGKLLAGKKVEF----TPFEGDVQVLEPKYVILAT 150
Cdd:TIGR01423 80 weFDRSSVKANWKALIAAKNKAVLDINKSYEGMFADTeGLTFFLGWGALEDKNVVLVresaDPKSAVKERLQAEHILLAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 151 GSVPvNIPVAPVDEdLIVDSTGALKFSEVPKRLGVIGAGVIGLELGSV---WRRLGSEVVVFEALDAFLPMADKALAKEY 227
Cdd:TIGR01423 160 GSWP-QMLGIPGIE-HCISSNEAFYLDEPPRRVLTVGGGFISVEFAGIfnaYKPRGGKVTLCYRNNMILRGFDSTLRKEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 228 QKILKKQGLDIRIG---AKVSGAETNGQEVTVKynqagEDKEQVFDKLIVCVGRKAYAEGLLAEDSGIKLTERGLVDVND 304
Cdd:TIGR01423 238 TKQLRANGINIMTNenpAKVTLNADGSKHVTFE-----SGKTLDVDVVMMAIGRVPRTQTLQLDKVGVELTKKGAIQVDE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 305 QCQTSVEGVYAIGDLVRGPMLAHKAMEEGVMAVERIHGHAAQ-VNYDTIISVIYTHPEAAWVGLTEEQAAEKGHEVKAGQ 383
Cdd:TIGR01423 313 FSRTNVPNIYAIGDVTDRVMLTPVAINEGAAFVDTVFGNKPRkTDHTRVASAVFSIPPIGTCGLVEEDAAKKFEKVAVYE 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 696288927 384 FPFAVNGRALAAGDTAGFV-KFVADAKTDRLLGMHVVGPNASDIVHQGMIALEFVSSVEDLQLMTFGHPTFSE 455
Cdd:TIGR01423 393 SSFTPLMHNISGSKYKKFVaKIVTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAE 465
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
5-462 |
4.00e-51 |
|
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and related species, can form a disulfide-linked dimer called mycothione. This enzyme can reduce mycothione to regenerate two mycothiol molecules. The enzyme shows some sequence similarity to glutathione-disulfide reductase, trypanothione-disulfide reductase, and dihydrolipoamide dehydrogenase. The characterized protein from M. tuberculosis, a homodimer, has FAD as a cofactor, one per monomer, and uses NADPH as a substrate.
Pssm-ID: 132493 [Multi-domain] Cd Length: 452 Bit Score: 179.95 E-value: 4.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 5 FDLVVIGGGPGGYEAAIRAAqlGFKVACIEKrihngkPSLGGTCLNVGCIPSKALLDSSHrYEATVHELAEHGITTGEVK 84
Cdd:TIGR03452 3 YDLIIIGTGSGNSIPDPRFA--DKRIAIVEK------GTFGGTCLNVGCIPTKMFVYAAE-VAQSIGESARLGIDAEIDS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 85 FDLDTLLARK-DKVVDQLTGGVAQLLKGN---GIEWLQGTGKLLAGKKVEftpfEGDVQVLEPKYVILATGSVPVnIPva 160
Cdd:TIGR03452 74 VRWPDIVSRVfGDRIDPIAAGGEDYRRGDetpNIDVYDGHARFVGPRTLR----TGDGEEITGDQIVIAAGSRPY-IP-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 161 PVDEDLIVD---STGALKFSEVPKRLGVIGAGVIGLELGSVWRRLGSEVVVFEALDAFLPMADKALAKEYQKILKKQgLD 237
Cdd:TIGR03452 147 PAIADSGVRyhtNEDIMRLPELPESLVIVGGGYIAAEFAHVFSALGTRVTIVNRSTKLLRHLDEDISDRFTEIAKKK-WD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 238 IRIGAKVSGAETNGQEVTVKYNQaGEDKEQvfDKLIVCVGRKAYAEGLLAEDSGIKLTERGLVDVNDQCQTSVEGVYAIG 317
Cdd:TIGR03452 226 IRLGRNVTAVEQDGDGVTLTLDD-GSTVTA--DVLLVATGRVPNGDLLDAEAAGVEVDEDGRIKVDEYGRTSARGVWALG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 318 DLVRGPMLAHKAMEEG-VMAVERIHGHAAQV-NYDTIISVIYTHPEAAWVGLTEEQAAEKGHE--VKAGQFPFAVNGRAL 393
Cdd:TIGR03452 303 DVSSPYQLKHVANAEArVVKHNLLHPNDLRKmPHDFVPSAVFTHPQIATVGLTEQEAREAGHDitVKIQNYGDVAYGWAM 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 394 AagDTAGFVKFVADAKTDRLLGMHVVGPNASDIVHQGMIALEFVSSVEDLQLMTFG-HPTFSEVVHEAAL 462
Cdd:TIGR03452 383 E--DTTGFCKLIADRDTGKLLGAHIIGPQASSLIQPLITAMAFGLDAREMARKQYWiHPALPEVVENALL 450
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
5-456 |
4.62e-51 |
|
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member of the pyridine nucleotide disulfide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly, where SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily, Cys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-term arm of the protein is proposed to allow broad substrate specificity.
Pssm-ID: 273624 [Multi-domain] Cd Length: 484 Bit Score: 180.43 E-value: 4.62e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 5 FDLVVIGGGPGGYEAAIRAAQLGFKVACI---EKRIHNGKPSLGGTCLNVGCIPSKALLDSSHRYEATVHELAEHGITTG 81
Cdd:TIGR01438 3 YDLIVIGGGSGGLAAAKEAAAYGAKVMLLdfvTPTPLGTRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 82 EVKFDLDTLLARKDKVVDQLTGGVAQLLKGNGIEWLQGTGKLLAGKKVEFTPFEGDVQVLEPKYVILATGSVPvNIPVAP 161
Cdd:TIGR01438 83 TVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERP-RYPGIP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 162 VDEDLIVDSTGALKFSEVPKRLGVIGAGVIGLELGSVWRRLGSEVVVFE---ALDAFlpmaDKALAKEYQKILKKQGLDI 238
Cdd:TIGR01438 162 GAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVrsiLLRGF----DQDCANKVGEHMEEHGVKF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 239 RIGAKVSGAETNGQEVTVKYNQAGEDKEQVFDKLIVCVGRKAYAEGLLAEDSGIKLTER-GLVDVNDQCQTSVEGVYAIG 317
Cdd:TIGR01438 238 KRQFVPIKVEQIEAKVLVEFTDSTNGIEEEYDTVLLAIGRDACTRKLNLENVGVKINKKtGKIPADEEEQTNVPYIYAVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 318 DLVRG-PMLAHKAMEEGVMAVERIHGHAAQ-VNYDTIISVIYTHPEAAWVGLTEEQAAEK----GHEVKAGQF-PFAVng 390
Cdd:TIGR01438 318 DILEDkPELTPVAIQAGRLLAQRLFKGSTViCDYENVPTTVFTPLEYGACGLSEEKAVEKfgeeNVEVFHSYFwPLEW-- 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 391 rALAAGDTAGF--VKFVADAKTD-RLLGMHVVGPNASDIVhQGM-IALEFVSSVEDLQLMTFGHPTFSEV 456
Cdd:TIGR01438 396 -TIPSRDNHNKcyAKLVCNKKENeRVVGFHVVGPNAGEVT-QGFaAALRCGLTKKDLDNTIGIHPVCAEV 463
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
5-455 |
6.54e-46 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 167.75 E-value: 6.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 5 FDLVVIGGGPGGYEAAIRAAQLGFKVACIEKRI----HNGKPSLGGTCLNVGCIPSKALLDSShRYEatvHELAE-HG-- 77
Cdd:PLN02546 80 FDLFTIGAGSGGVRASRFASNFGASAAVCELPFatisSDTLGGVGGTCVLRGCVPKKLLVYAS-KYS---HEFEEsRGfg 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 78 -ITTGEVKFDLDTLLARKDKVVDQLTGGVAQLLKGNGIEWLQGTGKLLAGKKVEFtpfegDVQVLEPKYVILATGSVPvN 156
Cdd:PLN02546 156 wKYETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDV-----DGKLYTARNILIAVGGRP-F 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 157 IPVAPVDEDLIvDSTGALKFSEVPKRLGVIGAGVIGLELGSVWRRLGSEVVVFealdaflpmadkalaKEYQKILKKQGL 236
Cdd:PLN02546 230 IPDIPGIEHAI-DSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVF---------------IRQKKVLRGFDE 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 237 DIR--IGAKVS--GAETNGQEVTVKYNQAGE-------DKEQV--FDKLIVCVGRKAYAEGLLAEDSGIKLTERGLVDVN 303
Cdd:PLN02546 294 EVRdfVAEQMSlrGIEFHTEESPQAIIKSADgslslktNKGTVegFSHVMFATGRKPNTKNLGLEEVGVKMDKNGAIEVD 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 304 DQCQTSVEGVYAIGDLVRGPMLAHKA-MEEGVMAVERIHGHAAQVNYDTIISVIYTHPEAAWVGLTEEQAAEKGHEVKAg 382
Cdd:PLN02546 374 EYSRTSVPSIWAVGDVTDRINLTPVAlMEGGALAKTLFGNEPTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYGDVDV- 452
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 696288927 383 qfpFAVNGRALAAGDTA----GFVKFVADAKTDRLLGMHVVGPNASDIVHQGMIALEFVSSVEDLQLMTFGHPTFSE 455
Cdd:PLN02546 453 ---FTANFRPLKATLSGlpdrVFMKLIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAE 526
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
5-456 |
5.21e-42 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 156.14 E-value: 5.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 5 FDLVVIGGGPGGYEAAIRAAQLGFKVACIEKRihngKPS-------LGGTCLNVGCIPSKALLDSSHRYEATVHELAEHG 77
Cdd:PTZ00052 6 YDLVVIGGGSGGMAAAKEAAAHGKKVALFDYV----KPStqgtkwgLGGTCVNVGCVPKKLMHYAANIGSIFHHDSQMYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 78 ITTGEvKFDLDTLLARKDKVVDQLTGGVAQLLKGNGIEWLQGTGKLLAGKKVEFTPFeGDVQVLEPKYVILATGSVPvNI 157
Cdd:PTZ00052 82 WKTSS-SFNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTVSYGDN-SQEETITAKYILIATGGRP-SI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 158 P-VAPVDEDLIVDSTGALKFSEVPKRLGVIGAGVIGLELGSVWRRLGSEVVVfeALDAF-LPMADKALAKEYQKILKKQG 235
Cdd:PTZ00052 159 PeDVPGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTV--AVRSIpLRGFDRQCSEKVVEYMKEQG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 236 LDIRIGAKVSGAETNGQEVTVKYNqagEDKEQVFDKLIVCVGRKAYAEGLLAEDSGIKLTERGLVDVNDQCqTSVEGVYA 315
Cdd:PTZ00052 237 TLFLEGVVPINIEKMDDKIKVLFS---DGTTELFDTVLYATGRKPDIKGLNLNAIGVHVNKSNKIIAPNDC-TNIPNIFA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 316 IGDLVRG-PMLAHKAMEEGVMAVERIHGHAAQ-VNYDTIISVIYTHPEAAWVGLTEEQAAEKGHEVKAGQFPFAVNGRAL 393
Cdd:PTZ00052 313 VGDVVEGrPELTPVAIKAGILLARRLFKQSNEfIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQEFNTLEI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 394 AA-------------GDTA----GFVKFVADAKTD-RLLGMHVVGPNASDIVhQGM-IALEFVSSVEDLQLMTFGHPTFS 454
Cdd:PTZ00052 393 AAvhrekherarkdeYDFDvssnCLAKLVCVKSEDnKVVGFHFVGPNAGEIT-QGFsLALKLGAKKSDFDSMIGIHPTDA 471
|
..
gi 696288927 455 EV 456
Cdd:PTZ00052 472 EV 473
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
354-460 |
7.65e-42 |
|
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases.
Pssm-ID: 427019 [Multi-domain] Cd Length: 109 Bit Score: 144.62 E-value: 7.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 354 SVIYTHPEAAWVGLTEEQAAEKGHEVKAGQFPFAVNGRALAAGDTAGFVKFVADAKTDRLLGMHVVGPNASDIVHQGMIA 433
Cdd:pfam02852 3 SVVFTDPEIASVGLTEEEAKEKGGEVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQEAALA 82
|
90 100
....*....|....*....|....*..
gi 696288927 434 LEFVSSVEDLQLMTFGHPTFSEVVHEA 460
Cdd:pfam02852 83 IKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
145-345 |
1.62e-29 |
|
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];
Pssm-ID: 440215 [Multi-domain] Cd Length: 322 Bit Score: 117.60 E-value: 1.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 145 YVILATGSVPVNIPVAPVDEDLI-----VDSTGALK---FSEVPKRLGVIGAGVIGLELGSVWRRLGSEVVVFEALDAFL 216
Cdd:COG0446 81 KLVLATGARPRPPPIPGLDLPGVftlrtLDDADALRealKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 217 PMADKALAKEYQKILKKQGLDIRIGAKVSGAE-TNGQEVTVKynqagEDKEQVFDKLIVCVGRKAYAEglLAEDSGIKLT 295
Cdd:COG0446 161 GVLDPEMAALLEEELREHGVELRLGETVVAIDgDDKVAVTLT-----DGEEIPADLVVVAPGVRPNTE--LAKDAGLALG 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 296 ERGLVDVNDQCQTSVEGVYAIGDLVRGP----------MLAHKAMEEGVMAVERIHGHAA 345
Cdd:COG0446 234 ERGWIKVDETLQTSDPDVYAAGDCAEVPhpvtgktvyiPLASAANKQGRVAAENILGGPA 293
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
5-341 |
2.31e-25 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 105.59 E-value: 2.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 5 FDLVVIGGGPGGYEAAIRAAQLGFKVACIEKrihngkPSLGGTCLNVGCIpskalldssHRY-----EATVHELAEHGIT 79
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEG------GEPGGQLATTKEI---------ENYpgfpeGISGPELAERLRE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 80 TGEvKFDLDTLLARkdkvvdqltggvaqllkgngIEWLQGTGKllaGKKVEFtpfeGDVQVLEPKYVILATGSVPVNIPV 159
Cdd:COG0492 66 QAE-RFGAEILLEE--------------------VTSVDKDDG---PFRVTT----DDGTEYEAKAVIIATGAGPRKLGL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 160 aPVDEDLI---VDSTGALKFSEVP-KRLGVIGAGVIGLELGSVWRRLGSEVVVFEALDAFlpMADKALAkeyQKILKKQG 235
Cdd:COG0492 118 -PGEEEFEgrgVSYCATCDGFFFRgKDVVVVGGGDSALEEALYLTKFASKVTLIHRRDEL--RASKILV---ERLRANPK 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 236 LDIRIGAKVSGAETNG--QEVTVKYNQAGEDKEQVFDKLIVCVGRKAYAEglLAEDSGIKLTERGLVDVNDQCQTSVEGV 313
Cdd:COG0492 192 IEVLWNTEVTEIEGDGrvEGVTLKNVKTGEEKELEVDGVFVAIGLKPNTE--LLKGLGLELDEDGYIVVDEDMETSVPGV 269
|
330 340
....*....|....*....|....*....
gi 696288927 314 YAIGDLVRGPM-LAHKAMEEGVMAVERIH 341
Cdd:COG0492 270 FAAGDVRDYKYrQAATAAGEGAIAALSAA 298
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
147-345 |
6.67e-24 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 103.30 E-value: 6.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 147 ILATGSVPVNIPVAPVDEDLIV------DSTGALKFSEVPKRLGVIGAGVIGLELGSVWRRLGSEVVVFEALDAFLP-MA 219
Cdd:COG1251 103 VLATGSRPRVPPIPGADLPGVFtlrtldDADALRAALAPGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPrQL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 220 DKALAKEYQKILKKQGLDIRIGAKVSGAETNGQEVTVKYnqagEDKEQV-FDKLIVCVGRKAYAEglLAEDSGIKlTERG 298
Cdd:COG1251 183 DEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRL----ADGEELpADLVVVAIGVRPNTE--LARAAGLA-VDRG 255
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 696288927 299 LVdVNDQCQTSVEGVYAIGD--LVRGPMLAHK-------AMEEGVMAVERIHGHAA 345
Cdd:COG1251 256 IV-VDDYLRTSDPDIYAAGDcaEHPGPVYGRRvlelvapAYEQARVAAANLAGGPA 310
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
182-257 |
5.29e-17 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 75.70 E-value: 5.29e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 696288927 182 RLGVIGAGVIGLELGSVWRRLGSEVVVFEALDAFLPMADKALAKEYQKILKKQGLDIRIGAKVSGAETNGQEVTVK 257
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVV 76
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
181-454 |
2.80e-15 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 77.77 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 181 KRLGVIGAGVIGLELGSVWRRLGSEVVVFEALDAFLPMA-DKALAKEYQKILKKQGLDIRIGAKVSGAETNGQEVTVKYN 259
Cdd:PRK09564 150 KNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRILPDSfDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEGVVTD 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 260 QagedKEQVFDKLIVCVGRKAYAEglLAEDSGIKLTERGLVDVNDQCQTSVEGVYAIGD------LVRGPM----LAHKA 329
Cdd:PRK09564 230 K----GEYEADVVIVATGVKPNTE--FLEDTGLKTLKNGAIIVDEYGETSIENIYAAGDcatiynIVSNKNvyvpLATTA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 330 MEEGVMAVERIHG-HAAQVNYDTIISVIYTHPEAAWVGLTEEQAAEKGHEVKAgQFPFAVNGRALAAGDTAGFVKFVADA 408
Cdd:PRK09564 304 NKLGRMVGENLAGrHVSFKGTLGSACIKVLDLEAARTGLTEEEAKKLGIDYKT-VFIKDKNHTNYYPGQEDLYVKLIYEA 382
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 696288927 409 KTDRLLGMHVVGPNASDI-VHQGMIALEFVSSVEDLQLMTFGH-PTFS 454
Cdd:PRK09564 383 DTKVILGGQIIGKKGAVLrIDALAVAIYAKLTTQELGMMDFCYaPPFA 430
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
6-340 |
1.89e-14 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 74.78 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 6 DLVVIGGGPGGYEAAIRAAQL---GFKVACIEKR-IHNGKPSLggtclnvgcipskalldsshryeatvHELAEHGITTG 81
Cdd:COG1252 3 RIVIVGGGFAGLEAARRLRKKlggDAEVTLIDPNpYHLFQPLL--------------------------PEVAAGTLSPD 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 82 EVKFDLDTLLARKdkvvdqltggvaqllkgnGIEWLQG--TGKLLAGKKVEFTpfegDVQVLEPKYVILATGSVPVNIPV 159
Cdd:COG1252 57 DIAIPLRELLRRA------------------GVRFIQGevTGIDPEARTVTLA----DGRTLSYDYLVIATGSVTNFFGI 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 160 APVDEDLI-VDSTG-ALKFSE---------VPKRLG---VIGAGVIGLEL-GSVWRRLGS------------EVVVFEAL 212
Cdd:COG1252 115 PGLAEHALpLKTLEdALALRErllaaferaERRRLLtivVVGGGPTGVELaGELAELLRKllrypgidpdkvRITLVEAG 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 213 DAFLPMADKALAKEYQKILKKQGLDIRIGAKVSGAETNGqeVTVKynqagEDKEQVFDKLIVCVGRKAYAeglLAEDSGI 292
Cdd:COG1252 195 PRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDADG--VTLE-----DGEEIPADTVIWAAGVKAPP---LLADLGL 264
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 696288927 293 KLTERGLVDVNDQCQT-SVEGVYAIGDLV-------RG-PMLAHKAMEEGVMAVERI 340
Cdd:COG1252 265 PTDRRGRVLVDPTLQVpGHPNVFAIGDCAavpdpdgKPvPKTAQAAVQQAKVLAKNI 321
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
147-318 |
5.25e-12 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 67.25 E-value: 5.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 147 ILATGSVPVnIPVAPVDEDLI-VDSTGALKFSEVP----KRLGVIGAGVIGLELGSVWRRLGSEVVVFEALDAFLP-MAD 220
Cdd:PRK04965 104 VLATGASAF-VPPIPGRELMLtLNSQQEYRAAETQlrdaQRVLVVGGGLIGTELAMDLCRAGKAVTLVDNAASLLAsLMP 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 221 KALAKEYQKILKKQGLDIRIGAKVSGAETNGQEVTVKYNqagEDKEQVFDKLIVCVGRKAyaEGLLAEDSGIKlTERGLV 300
Cdd:PRK04965 183 PEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRATLD---SGRSIEVDAVIAAAGLRP--NTALARRAGLA-VNRGIV 256
|
170
....*....|....*...
gi 696288927 301 dVNDQCQTSVEGVYAIGD 318
Cdd:PRK04965 257 -VDSYLQTSAPDIYALGD 273
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
181-320 |
5.82e-11 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 64.42 E-value: 5.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 181 KRLGVIGAGVIGLELGSVWRRLGSEVVVFEALDAFLPMADKALAKEYQKILKKQGLDIRIGAKVSgaETNGQEVTVKynq 260
Cdd:PRK13512 149 DKALVVGAGYISLEVLENLYERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEID--AINGNEVTFK--- 223
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 261 agEDKEQVFDKLIVCVGRKAYAEGLlaEDSGIKLTERGLVDVNDQCQTSVEGVYAIGDLV 320
Cdd:PRK13512 224 --SGKVEHYDMIIEGVGTHPNSKFI--ESSNIKLDDKGFIPVNDKFETNVPNIYAIGDII 279
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
146-318 |
4.81e-10 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 62.15 E-value: 4.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 146 VILATGSVPVNIPVAPVD----------EDLIVDSTGALKFsevpKRLGVIGAGVIGLELGSVWRRLGSEVVVFEaLDAF 215
Cdd:TIGR02374 100 LILATGSYPFILPIPGADkkgvyvfrtiEDLDAIMAMAQRF----KKAAVIGGGLLGLEAAVGLQNLGMDVSVIH-HAPG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 216 LpMA---DKALAKEYQKILKKQGLDIRIGAKVSGAETNGQEVTVKYNQAGEDKEqvfDKLIVCVGRKAYAEglLAEDSGI 292
Cdd:TIGR02374 175 L-MAkqlDQTAGRLLQRELEQKGLTFLLEKDTVEIVGATKADRIRFKDGSSLEA---DLIVMAAGIRPNDE--LAVSAGI 248
|
170 180
....*....|....*....|....*.
gi 696288927 293 KLTeRGLVdVNDQCQTSVEGVYAIGD 318
Cdd:TIGR02374 249 KVN-RGII-VNDSMQTSDPDIYAVGE 272
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
260-341 |
1.89e-09 |
|
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 440259 [Multi-domain] Cd Length: 434 Bit Score: 59.38 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 260 QAGEDKEQVF--DKLIVCVGRKAyAEGLLAEDSGIKLTERGLVDVNDQC-QTSVEGVYAIGDLVRGPMLAHKAMEEGVMA 336
Cdd:COG0493 349 VPIEGSEFTLpaDLVILAIGQTP-DPSGLEEELGLELDKRGTIVVDEETyQTSLPGVFAGGDAVRGPSLVVWAIAEGRKA 427
|
....*
gi 696288927 337 VERIH 341
Cdd:COG0493 428 ARAID 432
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
181-341 |
8.14e-09 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 57.82 E-value: 8.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 181 KRLGVIGAGVIGLELGSVWRRLGSEVVVF------EALDAFLPMADKALAkeyqkilkkQGLDIRIGAKVSGAET--NGQ 252
Cdd:PRK12814 324 KKVVVIGGGNTAIDAARTALRLGAESVTIlyrrtrEEMPANRAEIEEALA---------EGVSLRELAAPVSIERseGGL 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 253 EVTVKYNQAGEDKEQ---------------VFDKLIVCVGRkaYAEGLLAEDSGIKLTERGLVDVNDQ-CQTSVEGVYAI 316
Cdd:PRK12814 395 ELTAIKMQQGEPDESgrrrpvpvegseftlQADTVISAIGQ--QVDPPIAEAAGIGTSRNGTVKVDPEtLQTSVAGVFAG 472
|
170 180
....*....|....*....|....*
gi 696288927 317 GDLVRGPMLAHKAMEEGVMAVERIH 341
Cdd:PRK12814 473 GDCVTGADIAINAVEQGKRAAHAID 497
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
6-64 |
4.74e-08 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 54.86 E-value: 4.74e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 696288927 6 DLVVIGGGPGGYEAAIRAAQLGFKVACIekrIHNgkpslGGTCLNVGCIPSKALLDSSH 64
Cdd:pfam01134 1 DVIVIGGGHAGCEAALAAARMGAKVLLI---THN-----TDTIAELSCNPSIGGIAKGH 51
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
146-318 |
4.34e-07 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 52.43 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 146 VILATGSVPVNIPVAPVD----------EDLIVDSTGALKfsevPKRLGVIGAGVIGLELGSVWRRLGSEVVVFEaldaF 215
Cdd:PRK14989 105 LIMATGSYPWIPPIKGSEtqdcfvyrtiEDLNAIEACARR----SKRGAVVGGGLLGLEAAGALKNLGVETHVIE----F 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 216 LP--MADKALAKEYQKILKKQGldiRIGAKVSGAEtNGQEVTVKYNQAG------EDKEQVFDKLIVCVGRKAyaEGLLA 287
Cdd:PRK14989 177 APmlMAEQLDQMGGEQLRRKIE---SMGVRVHTSK-NTLEIVQEGVEARktmrfaDGSELEVDFIVFSTGIRP--QDKLA 250
|
170 180 190
....*....|....*....|....*....|.
gi 696288927 288 EDSGIKLTERGLVDVNDQCQTSVEGVYAIGD 318
Cdd:PRK14989 251 TQCGLAVAPRGGIVINDSCQTSDPDIYAIGE 281
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
5-154 |
5.27e-07 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 51.81 E-value: 5.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 5 FDLVVIGGGPGGYEAAIRAAQLGFKVACIEkriHNGKP------SLGGTClNV--GCIPSKALLD-------------SS 63
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIE---KGKKLgrkiliSGGGRC-NVtnLSEEPDNFLSrypgnpkflksalSR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 64 HRYEATVHELAEHGITTgEVKfDLDTLLARKDK---VVDQLTggvaQLLKGNGIEWLQGT--GKLLAGKKVEFTpFEGDV 138
Cdd:pfam03486 77 FTPWDFIAFFESLGVPL-KEE-DHGRLFPDSDKasdIVDALL----NELKELGVKIRLRTrvLSVEKDDDGRFR-VKTGG 149
|
170
....*....|....*...
gi 696288927 139 QVLEPKYVILATG--SVP 154
Cdd:pfam03486 150 EELEADSLVLATGglSWP 167
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
288-341 |
5.72e-07 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 51.53 E-value: 5.72e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 696288927 288 EDSGIKLTERGLVDVNDQCQTSVEGVYAIGDLVRGPMLAHKAMEEGVMAVERIH 341
Cdd:PRK12770 293 ECLGIELNRKGEIVVDEKHMTSREGVFAAGDVVTGPSKIGKAIKSGLRAAQSIH 346
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
6-47 |
1.99e-06 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 49.91 E-value: 1.99e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 696288927 6 DLVVIGGGPGGYEAAIRAAQLGFKVACIEKRihngkPSLGGT 47
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERR-----GFLGGM 37
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
181-319 |
3.53e-06 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 49.15 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 181 KRLGVIGAGVIGLELGSVWRRLGSEVVVFEALDAFL-----PMADKALAKEYQkilkKQGLDIRIGAKVSGAEtNGQEVT 255
Cdd:PRK09754 145 RSVVIVGAGTIGLELAASATQRRCKVTVIELAATVMgrnapPPVQRYLLQRHQ----QAGVRILLNNAIEHVV-DGEKVE 219
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 696288927 256 VKYNQAgedkEQVFDKLIVcVGRKAYAEGLLAEDSGIkLTERGLVdVNDQCQTSVEGVYAIGDL 319
Cdd:PRK09754 220 LTLQSG----ETLQADVVI-YGIGISANDQLAREANL-DTANGIV-IDEACRTCDPAIFAGGDV 276
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
283-341 |
7.46e-06 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 48.24 E-value: 7.46e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 283 EGLLAEdSGIKLTERGLVDVNDQC-QTSVEGVYAIGDLVRGPMLAHKAMEEGVMAVERIH 341
Cdd:PRK12810 403 AGLLAQ-FGVELDERGRVAAPDNAyQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAID 461
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
6-77 |
1.92e-05 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 46.90 E-value: 1.92e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 696288927 6 DLVVIGGGPGGYEAAIRAAQLGFKVACIEK----RIHNGKpSLGGTCLnVGCIPSkALLDS--SHRYEaTVHELAEHG 77
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKgqpfGGATAW-SSGGIDA-LGNPPQ-GGIDSpeLHPTD-TLKGLDELA 74
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
4-35 |
2.04e-05 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 46.75 E-value: 2.04e-05
10 20 30
....*....|....*....|....*....|..
gi 696288927 4 QFDLVVIGGGPGGYEAAIRAAQLGFKVACIEK 35
Cdd:COG1053 3 EYDVVVVGSGGAGLRAALEAAEAGLKVLVLEK 34
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
285-341 |
2.46e-05 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 46.71 E-value: 2.46e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 696288927 285 LLAEDSGIKLTERGLVDVNDQ-CQTSVEGVYAIGDLVRGPMLAHKAMEEGVMAVERIH 341
Cdd:PRK11749 391 ILSTTPGLELNRWGTIIADDEtGRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAEAIH 448
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
3-46 |
8.64e-05 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 44.84 E-value: 8.64e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 696288927 3 QQFDLVVIGGGPGGYEAAIRAAQLGFKVACIEKRihngkPSLGG 46
Cdd:COG1233 2 MMYDVVVIGAGIGGLAAAALLARAGYRVTVLEKN-----DTPGG 40
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
5-318 |
1.19e-04 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 44.38 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 5 FDLVVIGGGPGGYEAAIRAAQLGFKVACIEKRIhngkpslGGTCLNVGCIPSkalLDSSHRYEAT--VHELAEHgittge 82
Cdd:PRK15317 212 YDVLVVGGGPAGAAAAIYAARKGIRTGIVAERF-------GGQVLDTMGIEN---FISVPETEGPklAAALEEH------ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 83 VK-FDLDTLLARKdkvvdqltggVAQLLKGNGIewlqgtgkllagKKVEFtpfEGDVqVLEPKYVILATGSV--PVNIP- 158
Cdd:PRK15317 276 VKeYDVDIMNLQR----------ASKLEPAAGL------------IEVEL---ANGA-VLKAKTVILATGARwrNMNVPg 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 159 --------VA-------PVDEDlivdstgalkfsevpKRLGVIGAGVIGLEL-----GSVwrrlgSEVVVFEaldaFLPM 218
Cdd:PRK15317 330 edeyrnkgVAycphcdgPLFKG---------------KRVAVIGGGNSGVEAaidlaGIV-----KHVTVLE----FAPE 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 219 --ADKALakeyQKILKKQG-LDIRIGAKVSGAETNGQEVT---VKYNQAGEDKEQVFDKLIVCVGRKAYAEGLlaEDSgI 292
Cdd:PRK15317 386 lkADQVL----QDKLRSLPnVTIITNAQTTEVTGDGDKVTgltYKDRTTGEEHHLELEGVFVQIGLVPNTEWL--KGT-V 458
|
330 340
....*....|....*....|....*.
gi 696288927 293 KLTERGLVDVNDQCQTSVEGVYAIGD 318
Cdd:PRK15317 459 ELNRRGEIIVDARGATSVPGVFAAGD 484
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
291-343 |
2.59e-04 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 43.58 E-value: 2.59e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 696288927 291 GIKLTERGLVDVNDQCQTSVEGVYAIGDLVRGPMLAHKAMEEGVMAVERIHGH 343
Cdd:PRK12778 696 GLELNRKGTIVVDEEMQSSIPGIYAGGDIVRGGATVILAMGDGKRAAAAIDEY 748
|
|
| PRK07494 |
PRK07494 |
UbiH/UbiF family hydroxylase; |
1-33 |
2.99e-04 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181001 [Multi-domain] Cd Length: 388 Bit Score: 42.97 E-value: 2.99e-04
10 20 30
....*....|....*....|....*....|...
gi 696288927 1 MSQQFDLVVIGGGPGGYEAAIRAAQLGFKVACI 33
Cdd:PRK07494 4 EKEHTDIAVIGGGPAGLAAAIALARAGASVALV 36
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
9-46 |
3.82e-04 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 42.92 E-value: 3.82e-04
10 20 30
....*....|....*....|....*....|....*...
gi 696288927 9 VIGGGPGGYEAAIRAAQLGFKVACIEKrihngKPSLGG 46
Cdd:COG1148 145 VIGGGIAGMTAALELAEQGYEVYLVEK-----EPELGG 177
|
|
| carotene-cycl |
TIGR01790 |
lycopene cyclase family protein; This family includes lycopene beta and epsilion cyclases ... |
6-161 |
4.61e-04 |
|
lycopene cyclase family protein; This family includes lycopene beta and epsilion cyclases (which form beta and delta carotene, respectively) from bacteria and plants as well as the plant capsanthin/capsorubin and neoxanthin cyclases which appear to have evolved from the plant lycopene cyclases. The plant lycopene epsilon cyclases also transform neurosporene to alpha zeacarotene.
Pssm-ID: 130850 [Multi-domain] Cd Length: 388 Bit Score: 42.42 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 6 DLVVIGGGPGGYEAAIRAAQLGFKVACIEkrihnGKPSLGGTclnvgcipskalldssHRYEATVHELAEHGIT------ 79
Cdd:TIGR01790 1 DLAVIGGGPAGLAIALELARPGLRVQLIE-----PHPPIPGN----------------HTYGVWDDDLSDLGLAdcvehv 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 80 ---TGEVKFDLD-TLLARKDKVVD--QLTGGVAQLLKGNGIEWLQGTGKLLAGKKVEFTPFE-GDVQVLEPKYVILATGS 152
Cdd:TIGR01790 60 wpdVYEYRFPKQpRKLGTAYGSVDstRLHEELLQKCPEGGVLWLERKAIHAEADGVALSTVYcAGGQRIQARLVIDARGF 139
|
....*....
gi 696288927 153 VPVNIPVAP 161
Cdd:TIGR01790 140 GPLVQYVRF 148
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
285-341 |
5.16e-04 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 42.31 E-value: 5.16e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 696288927 285 LLAEDSGIKLTERGLVDVNDQC-QTSVEGVYAIGDLVRGPMLAHKAMEEGVMAVERIH 341
Cdd:PRK12831 400 ISSTTKGLKINKRGCIVADEETgLTSKEGVFAGGDAVTGAATVILAMGAGKKAAKAID 457
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
1-35 |
5.75e-04 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 42.51 E-value: 5.75e-04
10 20 30
....*....|....*....|....*....|....*
gi 696288927 1 MSQQFDLVVIGGGPGGYEAAIRAAQLGFKVACIEK 35
Cdd:PRK12839 5 MTHTYDVVVVGSGAGGLSAAVAAAYGGAKVLVVEK 39
|
|
| PLN02463 |
PLN02463 |
lycopene beta cyclase |
2-34 |
6.78e-04 |
|
lycopene beta cyclase
Pssm-ID: 178082 [Multi-domain] Cd Length: 447 Bit Score: 42.01 E-value: 6.78e-04
10 20 30
....*....|....*....|....*....|...
gi 696288927 2 SQQFDLVVIGGGPGGYEAAIRAAQLGFKVACIE 34
Cdd:PLN02463 26 SRVVDLVVVGGGPAGLAVAQQVSEAGLSVCCID 58
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
1-47 |
7.34e-04 |
|
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];
Pssm-ID: 441675 [Multi-domain] Cd Length: 414 Bit Score: 41.77 E-value: 7.34e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 696288927 1 MSQQFDLVVIGGGPGGYEAAIRAAQLGFKVACIEKRihngkPSLGGT 47
Cdd:COG2072 3 ATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKA-----DDVGGT 44
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
178-334 |
7.50e-04 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 41.68 E-value: 7.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 178 EVPKRL---GVIGAGVIGLELGSVW--------RRLGSEVV------VFEALDAFLPMADKALAKEYQKILKKQGLDIRI 240
Cdd:PTZ00318 168 EERKRLlhfVVVGGGPTGVEFAAELadffrddvRNLNPELVeeckvtVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRT 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 241 GAKVsgAETNGQEVTVKynqageDKEQVFDKLIVCvgRKAYAEGLLAEDSGIKLTERGLVDVNDQCQTS-VEGVYAIGDL 319
Cdd:PTZ00318 248 KTAV--KEVLDKEVVLK------DGEVIPTGLVVW--STGVGPGPLTKQLKVDKTSRGRISVDDHLRVKpIPNVFALGDC 317
|
170 180
....*....|....*....|
gi 696288927 320 -----VRGPMLAHKAMEEGV 334
Cdd:PTZ00318 318 aaneeRPLPTLAQVASQQGV 337
|
|
| GlpB |
COG3075 |
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism]; |
4-31 |
9.34e-04 |
|
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 442309 Cd Length: 415 Bit Score: 41.32 E-value: 9.34e-04
10 20
....*....|....*....|....*...
gi 696288927 4 QFDLVVIGGGPGGYEAAIRAAQLGFKVA 31
Cdd:COG3075 2 KFDVVVIGGGLAGLTAAIRAAEAGLRVA 29
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
5-36 |
1.25e-03 |
|
geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 273936 [Multi-domain] Cd Length: 295 Bit Score: 40.77 E-value: 1.25e-03
10 20 30
....*....|....*....|....*....|..
gi 696288927 5 FDLVVIGGGPGGYEAAIRAAQLGFKVACIEKR 36
Cdd:TIGR02032 1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEKK 32
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
6-47 |
1.27e-03 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 41.24 E-value: 1.27e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 696288927 6 DLVVIGGGPGGYEAAIRAAQLGFKVACIEKrihngKPSLGGT 47
Cdd:PRK06134 14 DVLVIGSGAAGLSAAVTAAWHGLKVIVVEK-----DPVFGGT 50
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
6-47 |
1.71e-03 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 40.83 E-value: 1.71e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 696288927 6 DLVVIGGGPGGYEAAIRAAQLGFKVACIEKrihngKPSLGGT 47
Cdd:PRK12842 11 DVLVIGSGAGGLSAAITARKLGLDVVVLEK-----EPVFGGT 47
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
9-48 |
2.55e-03 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 36.36 E-value: 2.55e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 696288927 9 VIGGGPGGYEAAIRAAQLGFKVACIEKRihngkPSLGGTC 48
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKR-----DRLGGNA 35
|
|
| PTZ00139 |
PTZ00139 |
Succinate dehydrogenase [ubiquinone] flavoprotein subunit; Provisional |
5-35 |
2.95e-03 |
|
Succinate dehydrogenase [ubiquinone] flavoprotein subunit; Provisional
Pssm-ID: 240286 [Multi-domain] Cd Length: 617 Bit Score: 40.11 E-value: 2.95e-03
10 20 30
....*....|....*....|....*....|.
gi 696288927 5 FDLVVIGGGPGGYEAAIRAAQLGFKVACIEK 35
Cdd:PTZ00139 30 YDAVVVGAGGAGLRAALGLVELGYKTACISK 60
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
2-35 |
3.27e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 40.10 E-value: 3.27e-03
10 20 30
....*....|....*....|....*....|....
gi 696288927 2 SQQFDLVVIGGGPGGYEAAIRAAQLGFKVACIEK 35
Cdd:PRK12843 14 DAEFDVIVIGAGAAGMSAALFAAIAGLKVLLVER 47
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
5-31 |
3.60e-03 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 39.45 E-value: 3.60e-03
10 20
....*....|....*....|....*..
gi 696288927 5 FDLVVIGGGPGGYEAAIRAAQLGFKVA 31
Cdd:PRK05329 3 FDVLVIGGGLAGLTAALAAAEAGKRVA 29
|
|
| TIGR00275 |
TIGR00275 |
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ... |
8-35 |
3.61e-03 |
|
flavoprotein, HI0933 family; The model when searched with a partial length search brings in proteins with a dinucleotide-binding motif (Rossman fold) over the initial 40 residues of the model, including oxidoreductases and dehydrogenases. Partially characterized members include an FAD-binding protein from Bacillus cereus and flavoprotein HI0933 from Haemophilus influenzae. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 272992 [Multi-domain] Cd Length: 400 Bit Score: 39.50 E-value: 3.61e-03
10 20
....*....|....*....|....*...
gi 696288927 8 VVIGGGPGGYEAAIRAAQLGFKVACIEK 35
Cdd:TIGR00275 1 IIIGGGAAGLMAAITAARAGLSVLLLEK 28
|
|
| sdhA |
PRK07803 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
3-35 |
6.74e-03 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 236101 [Multi-domain] Cd Length: 626 Bit Score: 38.86 E-value: 6.74e-03
10 20 30
....*....|....*....|....*....|...
gi 696288927 3 QQFDLVVIGGGPGGYEAAIRAAQLGFKVACIEK 35
Cdd:PRK07803 7 HSYDVVVIGAGGAGLRAAIEARERGLRVAVVCK 39
|
|
| MnmG |
COG0445 |
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ... |
1-33 |
6.88e-03 |
|
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440214 [Multi-domain] Cd Length: 626 Bit Score: 38.83 E-value: 6.88e-03
10 20 30
....*....|....*....|....*....|...
gi 696288927 1 MSQQFDLVVIGGGPGGYEAAIRAAQLGFKVACI 33
Cdd:COG0445 3 YPKEYDVIVVGGGHAGCEAALAAARMGAKTLLL 35
|
|
| PLN00128 |
PLN00128 |
Succinate dehydrogenase [ubiquinone] flavoprotein subunit |
4-35 |
7.47e-03 |
|
Succinate dehydrogenase [ubiquinone] flavoprotein subunit
Pssm-ID: 177739 [Multi-domain] Cd Length: 635 Bit Score: 38.68 E-value: 7.47e-03
10 20 30
....*....|....*....|....*....|..
gi 696288927 4 QFDLVVIGGGPGGYEAAIRAAQLGFKVACIEK 35
Cdd:PLN00128 50 TYDAVVVGAGGAGLRAAIGLSEHGFNTACITK 81
|
|
| ubiF |
PRK08020 |
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed |
1-35 |
8.09e-03 |
|
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed
Pssm-ID: 181199 [Multi-domain] Cd Length: 391 Bit Score: 38.43 E-value: 8.09e-03
10 20 30
....*....|....*....|....*....|....*.
gi 696288927 1 MSQQ-FDLVVIGGGPGGYEAAIRAAQLGFKVACIEK 35
Cdd:PRK08020 1 MTNQpTDIAIVGGGMVGAALALGLAQHGFSVAVLEH 36
|
|
| PRK13800 |
PRK13800 |
fumarate reductase/succinate dehydrogenase flavoprotein subunit; |
6-58 |
8.31e-03 |
|
fumarate reductase/succinate dehydrogenase flavoprotein subunit;
Pssm-ID: 237512 [Multi-domain] Cd Length: 897 Bit Score: 38.68 E-value: 8.31e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 696288927 6 DLVVIGGGPGGYEAAIRAAQLGFKVACIEKR--IHNGKPSLGGTCLNVGCIPSKA 58
Cdd:PRK13800 15 DVLVIGGGTAGTMAALTAAEHGANVLLLEKAhvRHSGALAMGMDGVNNAVIPGKA 69
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
181-280 |
8.94e-03 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 38.48 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696288927 181 KRLGVIGAGVIGLELGSVWRRL--GSEVVVFEALDA--------------FLPMADKALAKEYQKiLKKQGLDIRIGAKV 244
Cdd:PRK09564 1 MKIIIIGGTAAGMSAAAKAKRLnkELEITVYEKTDIvsfgacglpyfvggFFDDPNTMIARTPEE-FIKSGIDVKTEHEV 79
|
90 100 110
....*....|....*....|....*....|....*.
gi 696288927 245 SGAETNGQEVTVKYNQAGEDKEQVFDKLIVCVGRKA 280
Cdd:PRK09564 80 VKVDAKNKTITVKNLKTGSIFNDTYDKLMIATGARP 115
|
|
| |
