|
Name |
Accession |
Description |
Interval |
E-value |
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
4-474 |
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: 549.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 4 EYDVVILGGGTGGYVAAIRAAQLGLITAIVEKSKLGGTCLHSGCIPSKAMLKSAEVYRVTRQeANEFGVNTGDVSLDFSQ 83
Cdd:TIGR01350 1 AYDVIVIGGGPGGYVAAIRAAQLGLKVALVEKEYLGGTCLNVGCIPTKALLHSAEVYDEIKH-AKDLGIEVENVSVDWEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 84 VQKRKGKIVDQLHAGIEGLMKKGKIDVYHGTGRILGasifspmPGTISVemDNGNENEILILKNLVIATGSKPRSLPG-L 162
Cdd:TIGR01350 80 MQKRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLD-------PGTVSV--TGENGEETLEAKNIIIATGSRPRSLPGpF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 163 EVDEKSVMTSDGALLMNALPSSITIIGGGVIGIEWASMLVDFGVDVTVMDRLEQILATEDREVAVAMHKALAKRGVKFIL 242
Cdd:TIGR01350 151 DFDGKVVITSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 243 GAEIltESLQKNDSEVTISYKlGDEEQSITSEKMMVSVGRAPVIDDIGLQNTDIQVEK-GSIQTNNHYQTKDDHIYAIGD 321
Cdd:TIGR01350 231 NTKV--TAVEKNDDQVTYENK-GGETETLTGEKVLVAVGRKPNTEGLGLEKLGVELDErGRIVVDEYMRTNVPGIYAIGD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 322 VIGGLQLAHVAEHEGLHAIEHIAGKQVDSIDYDLVPRCVYSYPETAAVGLTEQQAKDRGFDVKIGKFPFKANGKALVNGH 401
Cdd:TIGR01350 308 VIGGPMLAHVASHEGIVAAENIAGKEPAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGYDVKIGKFPFAANGKALALGE 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1274541061 402 ADGFVKIIVDQQTDDIIGVHMMGSHVTDLISEAGLAMVMNAIPWEISSAIHPHPTLSEAFSEAALAVDGLAIH 474
Cdd:TIGR01350 388 TDGFVKIIADKKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEAIKEAALAALGKPIH 460
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
1-475 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 543.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 1 MSKEYDVVILGGGTGGYVAAIRAAQLGLITAIVEKSKLGGTCLHSGCIPSKAMLKSAEVYRVTRqEANEFGVNTGDVSLD 80
Cdd:PRK06416 1 FAFEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLGGTCLNRGCIPSKALLHAAERADEAR-HSEDFGIKAENVGID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 81 FSQVQKRKGKIVDQLHAGIEGLMKKGKIDVYHGTGRILGasifspmPGTISVEMDNGNEneILILKNLVIATGSKPRSLP 160
Cdd:PRK06416 80 FKKVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVD-------PNTVRVMTEDGEQ--TYTAKNIILATGSRPRELP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 161 GLEVDEKSVMTSDGALLMNALPSSITIIGGGVIGIEWASMLVDFGVDVTVMDRLEQILATEDREVAVAMHKALAKRGVKF 240
Cdd:PRK06416 151 GIEIDGRVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPGEDKEISKLAERALKKRGIKI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 241 ILGAeiLTESLQKNDSEVTISYKLGDEEQSITSEKMMVSVGRAPVIDDIGLQNTDIQVEKGSIQTNNHYQTKDDHIYAIG 320
Cdd:PRK06416 231 KTGA--KAKKVEQTDDGVTVTLEDGGKEETLEADYVLVAVGRRPNTENLGLEELGVKTDRGFIEVDEQLRTNVPNIYAIG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 321 DVIGGLQLAHVAEHEGLHAIEHIAGKQVDsIDYDLVPRCVYSYPETAAVGLTEQQAKDRGFDVKIGKFPFKANGKALVNG 400
Cdd:PRK06416 309 DIVGGPMLAHKASAEGIIAAEAIAGNPHP-IDYRGIPAVTYTHPEVASVGLTEAKAKEEGFDVKVVKFPFAGNGKALALG 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1274541061 401 HADGFVKIIVDQQTDDIIGVHMMGSHVTDLISEAGLAMVMNAIPWEISSAIHPHPTLSEAFSEAALAVDGLAIHM 475
Cdd:PRK06416 388 ETDGFVKLIFDKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEALGEAALAAAGKPLHA 462
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
2-470 |
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: 543.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 2 SKEYDVVILGGGTGGYVAAIRAAQLGLITAIVEKSKLGGTCLHSGCIPSKAMLKSAEVYRVTRqEANEFGVNTGDVSLDF 81
Cdd:COG1249 1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGRLGGTCLNVGCIPSKALLHAAEVAHEAR-HAAEFGISAGAPSVDW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 82 SQVQKRKGKIVDQLHAGIEGLMKKGKIDVYHGTGRILGasifspmPGTISVEmdngnENEILILKNLVIATGSKPRSLPG 161
Cdd:COG1249 80 AALMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVD-------PHTVEVT-----GGETLTADHIVIATGSRPRVPPI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 162 LEVDEKSVMTSDGALLMNALPSSitiigggvigiEWASMLVDFGVDVTVMDRLEQILATEDREVAVAMHKALAKRGVKFI 241
Cdd:COG1249 148 PGLDEVRVLTSDEALELEELPKSlvvigggyiglEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDIL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 242 LGAEIltESLQKNDSEVTISYKLGDEEQSITSEKMMVSVGRAPVIDDIGLQNTDIQV-EKGSIQTNNHYQTKDDHIYAIG 320
Cdd:COG1249 228 TGAKV--TSVEKTGDGVTVTLEDGGGEEAVEADKVLVATGRRPNTDGLGLEAAGVELdERGGIKVDEYLRTSVPGIYAIG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 321 DVIGGLQLAHVAEHEGLHAIEHIAGKQVDSIDYDLVPRCVYSYPETAAVGLTEQQAKDRGFDVKIGKFPFKANGKALVNG 400
Cdd:COG1249 306 DVTGGPQLAHVASAEGRVAAENILGKKPRPVDYRAIPSVVFTDPEIASVGLTEEEAREAGIDVKVGKFPFAANGRALALG 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 401 HADGFVKIIVDQQTDDIIGVHMMGSHVTDLISEAGLAMVMNAIPWEISSAIHPHPTLSEAFSEAALAVDG 470
Cdd:COG1249 386 ETEGFVKLIADAETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAALALLG 455
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
1-475 |
1.00e-161 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 465.94 E-value: 1.00e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 1 MSKEYDVVILGGGTGGYVAAIRAAQLGLITAIVEKSK-------LGGTCLHSGCIPSKAMLKSAEVYRVTRQEANEFGVN 73
Cdd:PRK06327 1 MSKQFDVVVIGAGPGGYVAAIRAAQLGLKVACIEAWKnpkgkpaLGGTCLNVGCIPSKALLASSEEFENAGHHFADHGIH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 74 TGDVSLDFSQVQKRKGKIVDQLHAGIEGLMKKGKIDVYHGTGRILGASifsPMPGTISVemdNGNENEILILKNLVIATG 153
Cdd:PRK06327 81 VDGVKIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVGKT---DAGYEIKV---TGEDETVITAKHVIIATG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 154 SKPRSLPGLEVDEKSVMTSDGALLMNALPSSITIIGGGVIGIEWASMLVDFGVDVTVMDRLEQILATEDREVAVAMHKAL 233
Cdd:PRK06327 155 SEPRHLPGVPFDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAAADEQVAKEAAKAF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 234 AKRGVKFILGAEIltESLQKNDSEVTISYKLGD-EEQSITSEKMMVSVGRAPVIDDIGLQNTDIQV-EKGSIQTNNHYQT 311
Cdd:PRK06327 235 TKQGLDIHLGVKI--GEIKTGGKGVSVAYTDADgEAQTLEVDKLIVSIGRVPNTDGLGLEAVGLKLdERGFIPVDDHCRT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 312 KDDHIYAIGDVIGGLQLAHVAEHEGLHAIEHIAGkQVDSIDYDLVPRCVYSYPETAAVGLTEQQAKDRGFDVKIGKFPFK 391
Cdd:PRK06327 313 NVPNVYAIGDVVRGPMLAHKAEEEGVAVAERIAG-QKGHIDYNTIPWVIYTSPEIAWVGKTEQQLKAEGVEYKAGKFPFM 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 392 ANGKALVNGHADGFVKIIVDQQTDDIIGVHMMGSHVTDLISEAGLAMVMNAIPWEISSAIHPHPTLSEAFSEAALAVDGL 471
Cdd:PRK06327 392 ANGRALAMGEPDGFVKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEVWHEAALAVDKR 471
|
....
gi 1274541061 472 AIHM 475
Cdd:PRK06327 472 PLHF 475
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
3-475 |
5.02e-149 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 433.06 E-value: 5.02e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 3 KEYDVVILGGGTGGYVAAIRAAQLGLITAIVEKSKLGGTCLHSGCIPSKAMLKSAEVYRvTRQEANEFGVNTGDVSLDFS 82
Cdd:PRK06292 2 EKYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGPLGGTCLNVGCIPSKALIAAAEAFH-EAKHAEEFGIHADGPKIDFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 83 QVQKRKGKIVDQLHAGI-EGLMKKGKIDVYHGTGRILGasifspmPGTISVEmdngneNEILILKNLVIATGSKPRSLPG 161
Cdd:PRK06292 81 KVMARVRRERDRFVGGVvEGLEKKPKIDKIKGTARFVD-------PNTVEVN------GERIEAKNIVIATGSRVPPIPG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 162 LE-VDEKSVMTSDGALLMNALPSSITIIGGGVIGIEWASMLVDFGVDVTVMDRLEQILATEDREVAVAMHKALAKRgVKF 240
Cdd:PRK06292 148 VWlILGDRLLTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILSKE-FKI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 241 ILGAEIltESLQKNDSEVTISYKLGDEEQSITSEKMMVSVGRAPVIDDIGLQNTDIQV-EKGSIQTNNHYQTKDDHIYAI 319
Cdd:PRK06292 227 KLGAKV--TSVEKSGDEKVEELEKGGKTETIEADYVLVATGRRPNTDGLGLENTGIELdERGRPVVDEHTQTSVPGIYAA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 320 GDVIGGLQLAHVAEHEGLHAIEHIAGKQVDSIDYDLVPRCVYSYPETAAVGLTEQQAKDRGFDVKIGKFPFKANGKALVN 399
Cdd:PRK06292 305 GDVNGKPPLLHEAADEGRIAAENAAGDVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEVPFEAQGRARVM 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1274541061 400 GHADGFVKIIVDQQTDDIIGVHMMGSHVTDLISEAGLAMVMNAIPWEISSAIHPHPTLSEAFSEAALAVDGLAIHM 475
Cdd:PRK06292 385 GKNDGFVKVYADKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRTALRDLFSKLIHG 460
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
1-460 |
2.86e-106 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 323.69 E-value: 2.86e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 1 MSKEYDVVILGGGTGGYVAAIRAAQLGLITAIVEKSKLGGTCLHSGCIPSKAMLKSAEVYRVTRQeANEFGVN-TGDVSL 79
Cdd:PRK06370 2 PAQRYDAIVIGAGQAGPPLAARAAGLGMKVALIERGLLGGTCVNTGCVPTKTLIASARAAHLARR-AAEYGVSvGGPVSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 80 DFSQVQKRKGKIVDQLHAGIEGLMKKGK-IDVYHGTGRILGasifspmPGTISVEmdngneNEILILKNLVIATGSKPR- 157
Cdd:PRK06370 81 DFKAVMARKRRIRARSRHGSEQWLRGLEgVDVFRGHARFES-------PNTVRVG------GETLRAKRIFINTGARAAi 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 158 -SLPGLevDEKSVMTSDGALLMNALPSSITIIGGGVIGIEWASMLVDFGVDVTVMDRLEQILATEDREVAVAMHKALAKR 236
Cdd:PRK06370 148 pPIPGL--DEVGYLTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILERE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 237 GVKFILGAEIltESLQKNDSEVTISYKLGDEEQSITSEKMMVSVGRAPVIDDIGLQNTDIQV-EKGSIQTNNHYQTKDDH 315
Cdd:PRK06370 226 GIDVRLNAEC--IRVERDGDGIAVGLDCNGGAPEITGSHILVAVGRVPNTDDLGLEAAGVETdARGYIKVDDQLRTTNPG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 316 IYAIGDVIGGLQLAHVAEHEGLHAIEHIAGKQVDSIDYDLVPRCVYSYPETAAVGLTEQQAKDRGFDVKIGKFPFKANGK 395
Cdd:PRK06370 304 IYAAGDCNGRGAFTHTAYNDARIVAANLLDGGRRKVSDRIVPYATYTDPPLARVGMTEAEARKSGRRVLVGTRPMTRVGR 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1274541061 396 ALVNGHADGFVKIIVDQQTDDIIGVHMMGSHVTDLISEAGLAMvMNAIPWE-ISSAIHPHPTLSEA 460
Cdd:PRK06370 384 AVEKGETQGFMKVVVDADTDRILGATILGVHGDEMIHEILDAM-YAGAPYTtLSRAIHIHPTVSEL 448
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
5-467 |
5.54e-93 |
|
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: 289.71 E-value: 5.54e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 5 YDVVILGGGTGGYVAAIRAAQLGLITAIVEKSKLGGTCLHSGCIPSKAMLKSAEVYRVTRqeANEFGVNTGDVSLDFSQV 84
Cdd:TIGR02053 1 YDLVIIGSGAAAFAAAIKAAELGASVAMVERGPLGGTCVNVGCVPSKMLLRAAEVAHYAR--KPPFGGLAATVAVDFGEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 85 QKRKGKIVDQL-HAGIEGLMKKGKIDVYHGTGRILGasifspmPGTISVemdnGNENEILILKNLVIATGSKPR--SLPG 161
Cdd:TIGR02053 79 LEGKREVVEELrHEKYEDVLSSYGVDYLRGRARFKD-------PKTVKV----DLGREVRGAKRFLIATGARPAipPIPG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 162 LevDEKSVMTSDGALLMNALPSSITIIGGGVIGIEWASMLVDFGVDVTVMDRLEQILATEDREVAVAMHKALAKRGVKFI 241
Cdd:TIGR02053 148 L--KEAGYLTSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSDRLLPREEPEISAAVEEALAEEGIEVV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 242 LGAEIltESLQKNDSEVTISYKLGDEEQSITSEKMMVSVGRAPVIDDIGLQNTDIQV-EKGSIQTNNHYQTKDDHIYAIG 320
Cdd:TIGR02053 226 TSAQV--KAVSVRGGGKIITVEKPGGQGEVEADELLVATGRRPNTDGLGLEKAGVKLdERGGILVDETLRTSNPGIYAAG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 321 DVIGGLQLAHVAEHEGLHAIEHIAGKQVDSIDYDLVPRCVYSYPETAAVGLTEQQAKDRGFDVKIGKFPFKANGKALVNG 400
Cdd:TIGR02053 304 DVTGGLQLEYVAAKEGVVAAENALGGANAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNVPRARINR 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1274541061 401 HADGFVKIIVDQQTDDIIGVHMMGSHVTDLISEAGLAMVMNAIPWEISSAIHPHPTLSEAFSEAALA 467
Cdd:TIGR02053 384 DTRGFIKLVAEPGTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGLKLAAQT 450
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
4-471 |
3.66e-80 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 256.24 E-value: 3.66e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 4 EYDVVILGGGTGGYVAAIRAAQLGLITAIVEK-SKLGGTCLHSGCIPSKAmLKSAeVYRVTRQEANEFGVNTGdVSLD-- 80
Cdd:PRK05249 5 DYDLVVIGSGPAGEGAAMQAAKLGKRVAVIERyRNVGGGCTHTGTIPSKA-LREA-VLRLIGFNQNPLYSSYR-VKLRit 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 81 FSQVQKRKGKIVDQLHAGIEGLMKKGKIDVYHGTGRILGasifspmPGTISVEMDNGnENEILILKNLVIATGSKPRSLP 160
Cdd:PRK05249 82 FADLLARADHVINKQVEVRRGQYERNRVDLIQGRARFVD-------PHTVEVECPDG-EVETLTADKIVIATGSRPYRPP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 161 GLEVDEKSVMTSDGALLMNALPSSITIIGGGVIGIEWASMLVDFGVDVTVMDRLEQILATEDREVAVAMHKALAKRGVKF 240
Cdd:PRK05249 154 DVDFDHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSFLDDEISDALSYHLRDSGVTI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 241 ILGAEIltESLQKNDSEVTISYKLGdeeQSITSEKMMVSVGRAPVIDDIGLQNTDIQV-EKGSIQTNNHYQTKDDHIYAI 319
Cdd:PRK05249 234 RHNEEV--EKVEGGDDGVIVHLKSG---KKIKADCLLYANGRTGNTDGLNLENAGLEAdSRGQLKVNENYQTAVPHIYAV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 320 GDVIGGLQLAHVAEHEGLHAIEHIAGKQVDSIdYDLVPRCVYSYPETAAVGLTEQQAKDRGFDVKIGKFPFKANGKALVN 399
Cdd:PRK05249 309 GDVIGFPSLASASMDQGRIAAQHAVGEATAHL-IEDIPTGIYTIPEISSVGKTEQELTAAKVPYEVGRARFKELARAQIA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 400 GHADGFVKIIVDQQTDDIIGVHMMGSHVTDLIsEAGLAmVMNaipweissaiHP------------HPTLSEAFSEAALa 467
Cdd:PRK05249 388 GDNVGMLKILFHRETLEILGVHCFGERATEII-HIGQA-IME----------QKgtieyfvnttfnYPTMAEAYRVAAL- 454
|
....
gi 1274541061 468 vDGL 471
Cdd:PRK05249 455 -DGL 457
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
1-461 |
1.18e-73 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 238.90 E-value: 1.18e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 1 MSKEYDVVILGGGTGGYVAAIRAAQLGLITAIVEKSKLGGTCLHSGCIPSKAMLKSAEVYRVTRQEANEFGVNTGDVSLD 80
Cdd:PRK06116 1 MTKDYDLIVIGGGSGGIASANRAAMYGAKVALIEAKRLGGTCVNVGCVPKKLMWYGAQIAEAFHDYAPGYGFDVTENKFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 81 FSQVQKRKGKIVDQLHAGIEGLMKKGKIDVYHGTGRILGASifspmpgTISVemdNGnenEILILKNLVIATGSKPR--S 158
Cdd:PRK06116 81 WAKLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAH-------TVEV---NG---ERYTADHILIATGGRPSipD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 159 LPGLEVdeksVMTSDGALLMNALPSSITIIGGGVIGIEWASMLVDFGVDVTVMDRLEQILATEDREVAVAMHKALAKRGV 238
Cdd:PRK06116 148 IPGAEY----GITSDGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 239 KFILGAEIltESLQKN-DSEVTISYKLGdeeQSITSEKMMVSVGRAPVIDDIGLQNTDIQV-EKGSIQTNNHYQTKDDHI 316
Cdd:PRK06116 224 RLHTNAVP--KAVEKNaDGSLTLTLEDG---ETLTVDCLIWAIGREPNTDGLGLENAGVKLnEKGYIIVDEYQNTNVPGI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 317 YAIGDVIGGLQLAHVAEHEGLHAIE-HIAGKQVDSIDYDLVPRCVYSYPETAAVGLTEQQAKDRGFD--VKIGKFPFKAn 393
Cdd:PRK06116 299 YAVGDVTGRVELTPVAIAAGRRLSErLFNNKPDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEdnVKVYRSSFTP- 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1274541061 394 GKALVNGHADG-FVKIIVDQQTDDIIGVHMMGSHVTDLISEAGLAMVMNAIPWEISSAIHPHPTLSEAF 461
Cdd:PRK06116 378 MYTALTGHRQPcLMKLVVVGKEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEF 446
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
3-474 |
2.32e-68 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 230.57 E-value: 2.32e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 3 KEYDVVILGGGTGGYVAAIRAAQLGLITAIV--EKSKLGGTCLHSGCIPSKAMLKSAEVYRVTRQEAN--EFGVNT---- 74
Cdd:PTZ00153 115 EEYDVGIIGCGVGGHAAAINAMERGLKVIIFtgDDDSIGGTCVNVGCIPSKALLYATGKYRELKNLAKlyTYGIYTnafk 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 75 --------------GDVSLDFSQVQKRKGKIVDQLHAGIEGLMKKGKIDVYHGTGRILGAsifspmPGTISVEMDNGNEN 140
Cdd:PTZ00153 195 ngkndpvernqlvaDTVQIDITKLKEYTQSVIDKLRGGIENGLKSKKFCKNSEHVQVIYE------RGHIVDKNTIKSEK 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 141 EI--LILKNLVIATGSKPRSLPGLEVDEKSVMTSDGALLMNALPSSITIIGGGVIGIEWASMLVDFGVDVTVMDRLEQIL 218
Cdd:PTZ00153 269 SGkeFKVKNIIIATGSTPNIPDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSPQLL 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 219 ATEDREVAVAMHKALAK-RGVKFILGAEILTESLQKNDSEVTISYKLGDEEQSITSEKMM------------VSVGRAPV 285
Cdd:PTZ00153 349 PLLDADVAKYFERVFLKsKPVRVHLNTLIEYVRAGKGNQPVIIGHSERQTGESDGPKKNMndiketyvdsclVATGRKPN 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 286 IDDIGLQNTDIQVEKGSIQTNNHYQTKD------DHIYAIGDVIGGLQLAHVAEHEGLHAIEHIAGKQVDS--------- 350
Cdd:PTZ00153 429 TNNLGLDKLKIQMKRGFVSVDEHLRVLRedqevyDNIFCIGDANGKQMLAHTASHQALKVVDWIEGKGKENvninvenwa 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 351 ---IDYDLVPRCVYSYPETAAVGLTEQQAKDRGFDVKIGKFP--FKANGKAL----------------------VNGHAD 403
Cdd:PTZ00153 509 skpIIYKNIPSVCYTTPELAFIGLTEKEAKELYPPDNVGVEIsfYKANSKVLcennisfpnnsknnsynkgkynTVDNTE 588
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1274541061 404 GFVKIIVDQQTDDIIGVHMMGSHVTDLISEAGLAMVMNAIPWEISSAIHPHPTLSEAFSEAALAVDGLAIH 474
Cdd:PTZ00153 589 GMVKIVYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDAAFKAIAGVRTH 659
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
3-463 |
2.74e-62 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 208.84 E-value: 2.74e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 3 KEYDVVILGGGTGGYVAAIRAAQLGLITAIVEKSKL--GGTCLHSGCIPSKAMLKSAEVyrvtrqeanefgvntgdvSLD 80
Cdd:PRK07251 2 LTYDLIVIGFGKAGKTLAAKLASAGKKVALVEESKAmyGGTCINIGCIPTKTLLVAAEK------------------NLS 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 81 FSQVQKRKGKIVDQLHAGIEGLMKKGKIDVYHGTGRILGASIfspmpgtisVEMDNGNENEILILKNLVIATGSKPRSLP 160
Cdd:PRK07251 64 FEQVMATKNTVTSRLRGKNYAMLAGSGVDLYDAEAHFVSNKV---------IEVQAGDEKIELTAETIVINTGAVSNVLP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 161 --GLEvDEKSVMTSDGALLMNALPSSITIIGGGVIGIEWASMLVDFGVDVTVMDRLEQILATEDREVAVAMHKALAKRGV 238
Cdd:PRK07251 135 ipGLA-DSKHVYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYMEEDGI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 239 KFILGAEIltESLQKNDSEVTISYklgdEEQSITSEKMMVSVGRAPVIDDIGLQNTDIQV-EKGSIQTNNHYQTKDDHIY 317
Cdd:PRK07251 214 TFLLNAHT--TEVKNDGDQVLVVT----EDETYRFDALLYATGRKPNTEPLGLENTDIELtERGAIKVDDYCQTSVPGVF 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 318 AIGDVIGGLQLAHVAehegLHAIEHIAGKQVDSIDYDL-----VPRCVYSYPETAAVGLTEQQAKDRGFDVKIGKFPFKA 392
Cdd:PRK07251 288 AVGDVNGGPQFTYIS----LDDFRIVFGYLTGDGSYTLedrgnVPTTMFITPPLSQVGLTEKEAKEAGLPYAVKELLVAA 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1274541061 393 NGKALVNGHADGFVKIIVDQQTDDIIGVHMMGSHVTDLISEAGLAMvMNAIPWE-ISSAIHPHPTLSEAFSE 463
Cdd:PRK07251 364 MPRAHVNNDLRGAFKVVVNTETKEILGATLFGEGSQEIINLITMAM-DNKIPYTyFKKQIFTHPTMAENLND 434
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
4-470 |
9.17e-61 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 205.19 E-value: 9.17e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 4 EYDVVILGGGTGGYVAAIRAAqlGLITAIVEKSKLGGTCLHSGCIPSKAMLKSAEVYRVTRqEANEFGVNTGDVSLDFSQ 83
Cdd:PRK07846 1 HYDLIIIGTGSGNSILDERFA--DKRIAIVEKGTFGGTCLNVGCIPTKMFVYAADVARTIR-EAARLGVDAELDGVRWPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 84 VQKRKGKIVDQLHAGieGLMKKGK----IDVYHGTGRILGasifspmPGTISVEMDngnenEILILKNLVIATGSKPRSL 159
Cdd:PRK07846 78 IVSRVFGRIDPIAAG--GEEYRGRdtpnIDVYRGHARFIG-------PKTLRTGDG-----EEITADQVVIAAGSRPVIP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 160 PGLEVDEKSVMTSDGALLMNALPSSITIIGGGVIGIEWASMLVDFGVDVTVMDRLEQILATEDREVAVAMHKaLAKRGVK 239
Cdd:PRK07846 144 PVIADSGVRYHTSDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLDDDISERFTE-LASKRWD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 240 FILGAEILteSLQKNDSEVTISYklgDEEQSITSEKMMVSVGRAPVIDDIGLQNTDIQV-EKGSIQTNNHYQTKDDHIYA 318
Cdd:PRK07846 223 VRLGRNVV--GVSQDGSGVTLRL---DDGSTVEADVLLVATGRVPNGDLLDAAAAGVDVdEDGRVVVDEYQRTSAEGVFA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 319 IGDVIGGLQLAHVAEHEgLHAIEH--IAGKQVDSIDYDLVPRCVYSYPETAAVGLTEQQAKDRGFD--VKIGKFPFKANG 394
Cdd:PRK07846 298 LGDVSSPYQLKHVANHE-ARVVQHnlLHPDDLIASDHRFVPAAVFTHPQIASVGLTENEARAAGLDitVKVQNYGDVAYG 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1274541061 395 KALVNghADGFVKIIVDQQTDDIIGVHMMGSHVTDLISEAGLAMVMNAIPWEISSAIH-PHPTLSEAFSEAALAVDG 470
Cdd:PRK07846 377 WAMED--TTGFVKLIADRDTGRLLGAHIIGPQASTLIQPLIQAMSFGLDAREMARGQYwIHPALPEVVENALLGLDL 451
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
3-468 |
6.58e-53 |
|
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: 184.58 E-value: 6.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 3 KEYDVVILGGGTGGYVAAIRAAQLGLitAIVEKSKLGGTCLHSGCIPSKAMLKSAEVYRVTRqEANEFGVNTGDVSLDFS 82
Cdd:TIGR03452 1 RHYDLIIIGTGSGNSIPDPRFADKRI--AIVEKGTFGGTCLNVGCIPTKMFVYAAEVAQSIG-ESARLGIDAEIDSVRWP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 83 QVQKRK-GKIVDQLHAGIEGLMKKGK---IDVYHGTGRILGasifspmPGTISVEmdngnENEILILKNLVIATGSKPRS 158
Cdd:TIGR03452 78 DIVSRVfGDRIDPIAAGGEDYRRGDEtpnIDVYDGHARFVG-------PRTLRTG-----DGEEITGDQIVIAAGSRPYI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 159 LPGLEVDEKSVMTSDGALLMNALPSSITIIGGGVIGIEWASMLVDFGVDVTVMDRLEQILATEDREVAvamHKALAKRGV 238
Cdd:TIGR03452 146 PPAIADSGVRYHTNEDIMRLPELPESLVIVGGGYIAAEFAHVFSALGTRVTIVNRSTKLLRHLDEDIS---DRFTEIAKK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 239 KFILGAEILTESLQKNDSEVTISYklgDEEQSITSEKMMVSVGRAPVIDDIGLQNTDIQV-EKGSIQTNNHYQTKDDHIY 317
Cdd:TIGR03452 223 KWDIRLGRNVTAVEQDGDGVTLTL---DDGSTVTADVLLVATGRVPNGDLLDAEAAGVEVdEDGRIKVDEYGRTSARGVW 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 318 AIGDVIGGLQLAHVAEHEgLHAIEH--IAGKQVDSIDYDLVPRCVYSYPETAAVGLTEQQAKDRGFD--VKIGKFPFKAN 393
Cdd:TIGR03452 300 ALGDVSSPYQLKHVANAE-ARVVKHnlLHPNDLRKMPHDFVPSAVFTHPQIATVGLTEQEAREAGHDitVKIQNYGDVAY 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1274541061 394 GKALVNghADGFVKIIVDQQTDDIIGVHMMGSHVTDLISEAGLAMVMNAIPWEISSAIH-PHPTLSEAFSEAALAV 468
Cdd:TIGR03452 379 GWAMED--TTGFCKLIADRDTGKLLGAHIIGPQASSLIQPLITAMAFGLDAREMARKQYwIHPALPEVVENALLGL 452
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
4-463 |
8.05e-53 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 183.83 E-value: 8.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 4 EYDVVILGGGTGGYVAAIRAAQLGLITAIVEKS--KLGGTCLHSGCIPSKAMLKSAEVYRvtrqeanefgvntgdvslDF 81
Cdd:NF040477 3 HYQAIIIGFGKAGKTLAATLAKAGWRVAIIEQSaqMYGGTCINIGCIPTKTLVHDAEQHQ------------------DF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 82 SQVQKRKGKIVDQLH-AGIEGLMKKGKIDVYHGTGRILGASifspmpgTISVEMDNGneNEILILKNLVIATGSKPR--S 158
Cdd:NF040477 65 STAMQRKSSVVGFLRdKNYHNLADLDNVDVINGRAEFIDNH-------TLRVFQADG--EQELRGEKIFINTGAQSVlpP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 159 LPGLEVDEKsVMTSDGALLMNALPSSITIIGGGVIGIEWASMLVDFGVDVTVMDRLEQILATEDREVAVAMHKALAKRGV 238
Cdd:NF040477 136 IPGLTTTPG-VYDSTGLLNLTQLPARLGILGGGYIGVEFASMFARFGSKVTIFEAAELFLPREDRDIAQAIATILQDQGV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 239 KFILGAEIltESLQKNDSEVtisyKLGDEEQSITSEKMMVSVGRAPVIDDIGLQNTDIQV-EKGSIQTNNHYQTKDDHIY 317
Cdd:NF040477 215 ELILNAQV--QRVSSHEGEV----QLETAEGVLTVDALLVASGRKPATAGLQLQNAGVAVnERGAIVVDKYLRTTADNIW 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 318 AIGDVIGGLQLAHVAEHEGLHAIEHIAGK-QVDSIDYDLVPRCVYSYPETAAVGLTEQQAKDRGFDVKIGKFPFKANGKA 396
Cdd:NF040477 289 AMGDVTGGLQFTYISLDDFRIVRDSLLGEgKRSTDDRQNVPYSVFMTPPLSRIGMTEEQARASGADIQVVTLPVAAIPRA 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1274541061 397 LVNGHADGFVKIIVDQQTDDIIGVHMMGSHVTDLISEagLAMVMNA-IPWEI-SSAIHPHPTLSEAFSE 463
Cdd:NF040477 369 RVMNDTRGVLKAVVDNKTQRILGVSLLCVDSHEMINI--VKTVMDAgLPYTVlRDQIFTHPTMSESLND 435
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
5-336 |
1.03e-52 |
|
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: 179.82 E-value: 1.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 5 YDVVILGGGTGGYVAAIRAAQLGLITAIVEkskLGGTCLHSGCIPSKAMLKSAEVYrvtrqeanefgvntgDVSLDFSQV 84
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIE---DEGTCPYGGCVLSKALLGAAEAP---------------EIASLWADL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 85 QKRKGKIVDQLHAGIEGLMKKGKIDVYHGTGRILGAsifspmpgtisvEMDNGNENEILIlKNLVIATGSKPRSL--PGL 162
Cdd:pfam07992 63 YKRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLE------------ELVDGDGETITY-DRLVIATGARPRLPpiPGV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 163 E---VDEKSVMTSDGALLMNALPSSITIIGGGVIGIEWASMLVDFGVDVTVMDRLEQILATEDREVAVAMHKALAKRGVK 239
Cdd:pfam07992 130 ElnvGFLVRTLDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 240 FILGAEIltESLQKNDSEVTIsykLGDEEQSITSEKMMVSVGRAPVIDdiGLQNTDIQV-EKGSIQTNNHYQTKDDHIYA 318
Cdd:pfam07992 210 VRLGTSV--KEIIGDGDGVEV---ILKDGTEIDADLVVVAIGRRPNTE--LLEAAGLELdERGGIVVDEYLRTSVPGIYA 282
|
330
....*....|....*....
gi 1274541061 319 IGDV-IGGLQLAHVAEHEG 336
Cdd:pfam07992 283 AGDCrVGGPELAQNAVAQG 301
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
4-463 |
2.87e-48 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 171.74 E-value: 2.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 4 EYDVVILGGGTGGYVAAIRAAQLGLITAIVEKSK--LGGTCLHSGCIPSKAMLKSAEvyrvtrQEAnefgvntgdvslDF 81
Cdd:PRK08010 3 KYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNamYGGTCINIGCIPTKTLVHDAQ------QHT------------DF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 82 SQVQKRKGKIVDQL-HAGIEGLMKKGKIDVYHGTGRILGASifspmpgtiSVEMDNGNENEILILKNLVIATGSKP--RS 158
Cdd:PRK08010 65 VRAIQRKNEVVNFLrNKNFHNLADMPNIDVIDGQAEFINNH---------SLRVHRPEGNLEIHGEKIFINTGAQTvvPP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 159 LPGLEVdEKSVMTSDGALLMNALPSSITIIGGGVIGIEWASMLVDFGVDVTVMDRLEQILATEDREVAVAMHKALAKRGV 238
Cdd:PRK08010 136 IPGITT-TPGVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 239 KFILGAEILTESLQKNDSEVTisyklgDEEQSITSEKMMVSVGRAPVIDDIGLQNTDIQV-EKGSIQTNNHYQTKDDHIY 317
Cdd:PRK08010 215 DIILNAHVERISHHENQVQVH------SEHAQLAVDALLIASGRQPATASLHPENAGIAVnERGAIVVDKYLHTTADNIW 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 318 AIGDVIGGLQLAHVAEHEGLHAIEHIAGKQVDSI-DYDLVPRCVYSYPETAAVGLTEQQAKDRGFDVKIGKFPFKANGKA 396
Cdd:PRK08010 289 AMGDVTGGLQFTYISLDDYRIVRDELLGEGKRSTdDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRA 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1274541061 397 LVNGHADGFVKIIVDQQTDDIIGVHMMGSHVTDLISEagLAMVMNA-IPWEI-SSAIHPHPTLSEAFSE 463
Cdd:PRK08010 369 RVMNDTRGVLKAIVDNKTQRILGASLLCVDSHEMINI--VKMVMDAgLPYSIlRDQIFTHPSMSESLND 435
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
5-461 |
8.67e-47 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 170.18 E-value: 8.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 5 YDVVILGGGTGGYVAAIRAAQLGLITAIVEKSKLGGTCLHSGCIPSKAMLKSAEVYRVTRqEANEFGVNTgDVSLDFSQV 84
Cdd:PTZ00058 49 YDLIVIGGGSGGMAAARRAARNKAKVALVEKDYLGGTCVNVGCVPKKIMFNAASIHDILE-NSRHYGFDT-QFSFNLPLL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 85 QKRKGKIVDQLHAGIEGLMKKGKIDVYHGTGRILGASIFSPMPGTISVEMDNGNENE----------------ILILKNL 148
Cdd:PTZ00058 127 VERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLIKKVSQVDGEADESDDDevtivsagvsqlddgqVIEGKNI 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 149 VIATGSKPRSlPGLEVDEkSVMTSDGALLMNAlPSSITIIGGGVIGIEWASMLVDFGVDVTVMDRLEQILATEDREVAVA 228
Cdd:PTZ00058 207 LIAVGNKPIF-PDVKGKE-FTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLRKFDETIINE 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 229 MHKALAKRGVKFILGAEIltESLQKnDSEVTISYKLGDEEQSITSEKMMVSVGRAPVIDDIGLQNTDIQVEKGSIQTNNH 308
Cdd:PTZ00058 284 LENDMKKNNINIITHANV--EEIEK-VKEKNLTIYLSDGRKYEHFDYVIYCVGRSPNTEDLNLKALNIKTPKGYIKVDDN 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 309 YQTKDDHIYAIGDVIG----------------------------------GLQLAHVAEHEGLHAIEHIAGKQVDSIDYD 354
Cdd:PTZ00058 361 QRTSVKHIYAVGDCCMvkknqeiedlnllklyneepylkkkentsgesyyNVQLTPVAINAGRLLADRLFGPFSRTTNYK 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 355 LVPRCVYSYPETAAVGLTEQQAKDrgfdvKIGKFPFKANGKALVN-----------GHADGFVKIIVDQQTDDIIGVHMM 423
Cdd:PTZ00058 441 LIPSVIFSHPPIGTIGLSEQEAID-----IYGKENVKIYESRFTNlffsvydmdpaQKEKTYLKLVCVGKEELIKGLHIV 515
|
490 500 510
....*....|....*....|....*....|....*...
gi 1274541061 424 GSHVTDLISEAGLAMVMNAIPWEISSAIHPHPTLSEAF 461
Cdd:PTZ00058 516 GLNADEILQGFAVALKMNATKADFDETIPIHPTAAEEF 553
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
7-465 |
1.03e-46 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 168.11 E-value: 1.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 7 VVILGGGTGGYVAAIRAAQLGLITAIVEKSKLGGTCLHSGCIPSKAMLKSAEVyRVTRQEANEFGVNTGD---VSLDFSQ 83
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIERDGLGGAAVLTDCVPSKTLIATAEV-RTELRRAAELGIRFIDdgeARVDLPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 84 VQKRKGKIVDQLHAGIEGLMKKGKIDVYHGTGRILGASIfspMPGTISVEMDNGNENEI---LILknlvIATGSKPRSLP 160
Cdd:PRK07845 83 VNARVKALAAAQSADIRARLEREGVRVIAGRGRLIDPGL---GPHRVKVTTADGGEETLdadVVL----IATGASPRILP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 161 GLEVDEKSVMTSDGALLMNALPSSITIIGGGVIGIEWASMLVDFGVDVTVMDRLEQILATEDREVAVAMHKALAKRGVKF 240
Cdd:PRK07845 156 TAEPDGERILTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPGEDADAAEVLEEVFARRGMTV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 241 ILGAEilTESLQKNDSEVTIsyKLGDEeQSITSEKMMVSVGRAPVIDDIGLQNTDIQV-EKGSIQTNNHYQTKDDHIYAI 319
Cdd:PRK07845 236 LKRSR--AESVERTGDGVVV--TLTDG-RTVEGSHALMAVGSVPNTAGLGLEEAGVELtPSGHITVDRVSRTSVPGIYAA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 320 GDVIGGLQLAHVAEHEGLHAIEHIAGKQVDSIDYDLVPRCVYSYPETAAVGLTEQQAKDRGFDVKIGKFPFKANGKALVN 399
Cdd:PRK07845 311 GDCTGVLPLASVAAMQGRIAMYHALGEAVSPLRLKTVASNVFTRPEIATVGVSQAAIDSGEVPARTVMLPLATNPRAKMS 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1274541061 400 GHADGFVKIIVDQQTDDIIGVHMMGSHVTDLISEAGLAmVMNAIPW-EISSAIHPHPTLSEAFSEAA 465
Cdd:PRK07845 391 GLRDGFVKLFCRPGTGVVIGGVVVAPRASELILPIALA-VQNRLTVdDLAQTFTVYPSLSGSITEAA 456
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
4-461 |
4.57e-44 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 161.52 E-value: 4.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 4 EYDVVILGGGTGGYVAAIRAAQLGLITAIVE----------KSKLGGTCLHSGCIPSKAMLKSAEvYRVTRQEANEFGVN 73
Cdd:PLN02507 25 DFDLFVIGAGSGGVRAARFSANFGAKVGICElpfhpissesIGGVGGTCVIRGCVPKKILVYGAT-FGGEFEDAKNYGWE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 74 -TGDVSLDFSQVQKRKGKIVDQLHAGIEGLMKKGKIDVYHGTGRILGasifspmPGTISVEMDNGNENEiLILKNLVIAT 152
Cdd:PLN02507 104 iNEKVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVG-------PNEVEVTQLDGTKLR-YTAKHILIAT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 153 GSK--PRSLPGLEVdeksVMTSDGALLMNALPSSITIIGGGVIGIEWASMLVDFGVDVTVMDRLEQILATEDREVAVAMH 230
Cdd:PLN02507 176 GSRaqRPNIPGKEL----AITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRAVVA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 231 KALAKRGVKFILGAEiLTEsLQKNDSEVTISYKLGDEeqsITSEKMMVSVGRAPVIDDIGLQNTDIQVEK-GSIQTNNHY 309
Cdd:PLN02507 252 RNLEGRGINLHPRTN-LTQ-LTKTEGGIKVITDHGEE---FVADVVLFATGRAPNTKRLNLEAVGVELDKaGAVKVDEYS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 310 QTKDDHIYAIGDVIGGLQLAHVAEHEGLHAIEHIAGKQVDSIDYDLVPRCVYSYPETAAVGLTEQQAKDRGF-DVKIGKF 388
Cdd:PLN02507 327 RTNIPSIWAIGDVTNRINLTPVALMEGTCFAKTVFGGQPTKPDYENVACAVFCIPPLSVVGLSEEEAVEQAKgDILVFTS 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1274541061 389 PFKANGKALVNGHADGFVKIIVDQQTDDIIGVHMMGSHVTDLISEAGLAMVMNAIPWEISSAIHPHPTLSEAF 461
Cdd:PLN02507 407 SFNPMKNTISGRQEKTVMKLIVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEF 479
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
7-465 |
9.23e-44 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 161.86 E-value: 9.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 7 VVILGGGTGGYVAAIRAAQLGLITAIVEKSKLGGTCLHSGCIPSKAMLKSAEVYRVTRQEANEFGVNTGDVSLDFSQVQK 86
Cdd:PRK13748 101 VAVIGSGGAAMAAALKAVEQGARVTLIERGTIGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDGGIAATVPTIDRSRLLA 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 87 RKGKIVDQL-HAGIEGLMKKG-KIDVYHGTGRILGASifspmpgTISVEMDNGNENEILILKNLvIATGSKPR--SLPGL 162
Cdd:PRK13748 181 QQQARVDELrHAKYEGILDGNpAITVLHGEARFKDDQ-------TLIVRLNDGGERVVAFDRCL-IATGASPAvpPIPGL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 163 EvdEKSVMTSDGALLMNALPSSITIIGGGVIGIEWASMLVDFGVDVTVMDRlEQILATEDREVAVAMHKALAKRGVkfil 242
Cdd:PRK13748 253 K--ETPYWTSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILAR-STLFFREDPAIGEAVTAAFRAEGI---- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 243 gaEILTESLQKNDSEVTISYKLGDEEQSITSEKMMVSVGRAPVIDDIGLQNTDIQVEK-GSIQTNNHYQTKDDHIYAIGD 321
Cdd:PRK13748 326 --EVLEHTQASQVAHVDGEFVLTTGHGELRADKLLVATGRAPNTRSLALDAAGVTVNAqGAIVIDQGMRTSVPHIYAAGD 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 322 VIGGLQLAHVAEHEGLHAIEHIAGKQVdSIDYDLVPRCVYSYPETAAVGLTEQQAKDRGFDVKIGKFPFKANGKALVNGH 401
Cdd:PRK13748 404 CTDQPQFVYVAAAAGTRAAINMTGGDA-ALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRTLTLDNVPRALANFD 482
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1274541061 402 ADGFVKIIVDQQTDDIIGVHMMGSHVTDLISEAGLAMVMNAIPWEISSAIHPHPTLSEAFSEAA 465
Cdd:PRK13748 483 TRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAALAIRNRMTVQELADQLFPYLTMVEGLKLAA 546
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
4-461 |
1.54e-43 |
|
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: 160.02 E-value: 1.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 4 EYDVVILGGGTGGYVAAIRAAQLGLITAIVEKSK---------LGGTCLHSGCIPSKAMLKSAEVYRVTRqEANEFGVNT 74
Cdd:TIGR01438 2 DYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTptplgtrwgIGGTCVNVGCIPKKLMHQAALLGQALK-DSRNYGWKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 75 GD-VSLDFSQVQKRKGKIVDQLHAGIEGLMKKGKIDVYHGTGRILGasifspmPGTISVEMDNGNENeILILKNLVIATG 153
Cdd:TIGR01438 81 EEtVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVD-------KHRIKATNKKGKEK-IYSAERFLIATG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 154 SKPRsLPGLEVDEKSVMTSDGALLMNALPSSITIIGGGVIGIEWASMLVDFGVDVTVMDRlEQILATEDREVAVAMHKAL 233
Cdd:TIGR01438 153 ERPR-YPGIPGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVR-SILLRGFDQDCANKVGEHM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 234 AKRGVKFILGaeILTESLQKNDSEVTISYKlgDEEQSITSE--KMMVSVGRAPVIDDIGLQNTDIQVEK--GSIQTNNHY 309
Cdd:TIGR01438 231 EEHGVKFKRQ--FVPIKVEQIEAKVLVEFT--DSTNGIEEEydTVLLAIGRDACTRKLNLENVGVKINKktGKIPADEEE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 310 QTKDDHIYAIGDVIGG-LQLAHVAEHEGLHAIEHIAGKQVDSIDYDLVPRCVYSYPETAAVGLTEQQAKDRGFDVKIGKF 388
Cdd:TIGR01438 307 QTNVPYIYAVGDILEDkPELTPVAIQAGRLLAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENVEVF 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1274541061 389 -----PFKANGKALVNgHADGFVKIIVDQQTDD-IIGVHMMGSHVTDLISEAGLAMVMNAIPWEISSAIHPHPTLSEAF 461
Cdd:TIGR01438 387 hsyfwPLEWTIPSRDN-HNKCYAKLVCNKKENErVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVF 464
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
356-464 |
5.74e-43 |
|
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: 147.32 E-value: 5.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 356 VPRCVYSYPETAAVGLTEQQAKDRGFDVKIGKFPFKANGKALVNGHADGFVKIIVDQQTDDIIGVHMMGSHVTDLISEAG 435
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGEVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQEAA 80
|
90 100
....*....|....*....|....*....
gi 1274541061 436 LAMVMNAIPWEISSAIHPHPTLSEAFSEA 464
Cdd:pfam02852 81 LAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
4-461 |
1.44e-39 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 150.41 E-value: 1.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 4 EYDVVILGGGTGGYVAAIRAAQLGLITAIVE----------KSKLGGTCLHSGCIPSKaMLKSAEVYRVTRQEANEFG-V 72
Cdd:PLN02546 79 DFDLFTIGAGSGGVRASRFASNFGASAAVCElpfatissdtLGGVGGTCVLRGCVPKK-LLVYASKYSHEFEESRGFGwK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 73 NTGDVSLDFSQVQKRKGKIVDQLHAGIEGLMKKGKIDVYHGTGRILGasifspmPGTISVEmdngneNEILILKNLVIAT 152
Cdd:PLN02546 158 YETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVD-------PHTVDVD------GKLYTARNILIAV 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 153 GSKPR--SLPGLEvdekSVMTSDGALLMNALPSSITIIGGGVIGIEWASMLVDFGVDVTVMDRLEQILATEDREVAVAMH 230
Cdd:PLN02546 225 GGRPFipDIPGIE----HAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKKVLRGFDEEVRDFVA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 231 KALAKRGVKFilgaeilteslQKNDSEVTISyKLGDEEQSITSEK--------MMVSVGRAPVIDDIGLQNTDIQVEK-G 301
Cdd:PLN02546 301 EQMSLRGIEF-----------HTEESPQAII-KSADGSLSLKTNKgtvegfshVMFATGRKPNTKNLGLEEVGVKMDKnG 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 302 SIQTNNHYQTKDDHIYAIGDVIGGLQLAHVAEHEGLHAIEHIAGKQVDSIDYDLVPRCVYSYPETAAVGLTEQQAKDRGF 381
Cdd:PLN02546 369 AIEVDEYSRTSVPSIWAVGDVTDRINLTPVALMEGGALAKTLFGNEPTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYG 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 382 DVKIGKFPFKANgKALVNGHADG-FVKIIVDQQTDDIIGVHMMGSHVTDLISEAGLAMVMNAIPWEISSAIHPHPTLSEA 460
Cdd:PLN02546 449 DVDVFTANFRPL-KATLSGLPDRvFMKLIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEE 527
|
.
gi 1274541061 461 F 461
Cdd:PLN02546 528 F 528
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
2-459 |
7.36e-39 |
|
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: 147.04 E-value: 7.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 2 SKEYDVVILGGGTGGYVAAIRAAQL-GLITAIVEKSK---------LGGTCLHSGCIPSKAMLKSAEvYRVTRQEANEFG 71
Cdd:TIGR01423 1 SKAFDLVVIGAGSGGLEAGWNAATLyKKRVAVVDVQThhgppfyaaLGGTCVNVGCVPKKLMVTGAQ-YMDTLRESAGFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 72 --VNTGDVSLDFSQVQKRKGKIVDQLHAGIEGLMKKGK-IDVYHGTGRILGASIFspmpgTISVEMD-NGNENEILILKN 147
Cdd:TIGR01423 80 weFDRSSVKANWKALIAAKNKAVLDINKSYEGMFADTEgLTFFLGWGALEDKNVV-----LVRESADpKSAVKERLQAEH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 148 LVIATGSKPRsLPGLEVDEKSVmTSDGALLMNALPSSITIIGGGVIGIEWASMLVDF---GVDVTVMDRLEQILATEDRE 224
Cdd:TIGR01423 155 ILLATGSWPQ-MLGIPGIEHCI-SSNEAFYLDEPPRRVLTVGGGFISVEFAGIFNAYkprGGKVTLCYRNNMILRGFDST 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 225 VAVAMHKALAKRGVkfilgaEILTeslQKNDSEVTISyklGDEEQSITSEK--------MMVSVGRAPVIDDIGLQNTDI 296
Cdd:TIGR01423 233 LRKELTKQLRANGI------NIMT---NENPAKVTLN---ADGSKHVTFESgktldvdvVMMAIGRVPRTQTLQLDKVGV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 297 QV-EKGSIQTNNHYQTKDDHIYAIGDVIGGLQLAHVAEHEGLHAIEHIAGKQVDSIDYDLVPRCVYSYPETAAVGLTEQQ 375
Cdd:TIGR01423 301 ELtKKGAIQVDEFSRTNVPNIYAIGDVTDRVMLTPVAINEGAAFVDTVFGNKPRKTDHTRVASAVFSIPPIGTCGLVEED 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 376 AKDRGFDVKIGKFPFKANGKALVNGHADGFV-KIIVDQQTDDIIGVHMMGSHVTDLISEAGLAMVMNAIPWEISSAIHPH 454
Cdd:TIGR01423 381 AAKKFEKVAVYESSFTPLMHNISGSKYKKFVaKIVTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVH 460
|
....*
gi 1274541061 455 PTLSE 459
Cdd:TIGR01423 461 PTSAE 465
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
5-462 |
2.99e-32 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 128.79 E-value: 2.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 5 YDVVILGGGTGGYVAAIRAAQLGLITAIVEKSK---------LGGTCLHSGCIPSKAMLKSAEVYRVTRQEANEFGVNTG 75
Cdd:PTZ00052 6 YDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKpstqgtkwgLGGTCVNVGCVPKKLMHYAANIGSIFHHDSQMYGWKTS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 76 DVSldfsqvqkRKGKIVDQLHAGIEGL-------MKKGKIDVYHGTgrilgASIFSPMpgtiSVEMDNGNENEILILKNL 148
Cdd:PTZ00052 86 SSF--------NWGKLVTTVQNHIRSLnfsyrtgLRSSKVEYINGL-----AKLKDEH----TVSYGDNSQEETITAKYI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 149 VIATGSKPRSLPGLEVDEKSVMTSDGALLMNALPSSITIIGGGVIGIEWASMLVDFGVDVTVMDRlEQILATEDREVAVA 228
Cdd:PTZ00052 149 LIATGGRPSIPEDVPGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVR-SIPLRGFDRQCSEK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 229 MHKALAKRGVKFILGaeILTESLQKNDSEVTISYKLGDEEQSITsekMMVSVGRAPVIDDIGLQNTDIQVEKGSIQTNNH 308
Cdd:PTZ00052 228 VVEYMKEQGTLFLEG--VVPINIEKMDDKIKVLFSDGTTELFDT---VLYATGRKPDIKGLNLNAIGVHVNKSNKIIAPN 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 309 YQTKDDHIYAIGDVIGGL-QLAHVAEHEGLHAIEHIAGKQVDSIDYDLVPRCVYSYPETAAVGLTEQQAKDRGFDVKIGK 387
Cdd:PTZ00052 303 DCTNIPNIFAVGDVVEGRpELTPVAIKAGILLARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 388 FPFKANGKALVNGHADGFVK------------------IIVDQQTDDIIGVHMMGSHVTDLISEAGLAMVMNAIPWEISS 449
Cdd:PTZ00052 383 YLQEFNTLEIAAVHREKHERarkdeydfdvssnclaklVCVKSEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDS 462
|
490
....*....|...
gi 1274541061 450 AIHPHPTLSEAFS 462
Cdd:PTZ00052 463 MIGIHPTDAEVFM 475
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
148-348 |
1.14e-18 |
|
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: 86.79 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 148 LVIATGSKPRSLPGLEVDEKSVMT----SDGALLMNALPSSITI----IGGGVIGIEWASMLVDFGVDVTVMDRLEQILA 219
Cdd:COG0446 82 LVLATGARPRPPPIPGLDLPGVFTlrtlDDADALREALKEFKGKravvIGGGPIGLELAEALRKRGLKVTLVERAPRLLG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 220 TEDREVAVAMHKALAKRGVKFILGAEiLTESLQKNDSEVTISyklgdEEQSITSEKMMVSVGRAP---VIDDIGLQNTdi 296
Cdd:COG0446 162 VLDPEMAALLEEELREHGVELRLGET-VVAIDGDDKVAVTLT-----DGEEIPADLVVVAPGVRPnteLAKDAGLALG-- 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1274541061 297 qvEKGSIQTNNHYQTKDDHIYAIGDVIG----------GLQLAHVAEHEGLHAIEHIAGKQV 348
Cdd:COG0446 234 --ERGWIKVDETLQTSDPDVYAAGDCAEvphpvtgktvYIPLASAANKQGRVAAENILGGPA 293
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
5-346 |
2.48e-17 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 82.48 E-value: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 5 YDVVILGGGTGGYVAAIRAAQLGLITAIVEKSKLGGTCLHSGCIpskamlksaevyrvtrqeANEFGvntgdvsldfsqv 84
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQLATTKEI------------------ENYPG------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 85 qkrkgkivdqLHAGIEG--LMKKGKIDVYH-GTgRILGASIFS--PMPGTISVEMDNGnenEILILKNLVIATGSKPRSL 159
Cdd:COG0492 50 ----------FPEGISGpeLAERLREQAERfGA-EILLEEVTSvdKDDGPFRVTTDDG---TEYEAKAVIIATGAGPRKL 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 160 --PGL-EVDEKSVM---TSDGALLMN-----------ALpssitiigggvigiEWASMLVDFGVDVTVMDRLEQILATEd 222
Cdd:COG0492 116 glPGEeEFEGRGVSycaTCDGFFFRGkdvvvvgggdsAL--------------EEALYLTKFASKVTLIHRRDELRASK- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 223 revaVAMHKALAKRGVKFILGAEIltESLQKND--SEVTISYKLGDEEQSITSEKMMVSVGRAP---VIDDIGLqNTDiq 297
Cdd:COG0492 181 ----ILVERLRANPKIEVLWNTEV--TEIEGDGrvEGVTLKNVKTGEEKELEVDGVFVAIGLKPnteLLKGLGL-ELD-- 251
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1274541061 298 vEKGSIQTNNHYQTKDDHIYAIGDVIGG-LQLAHVAEHEG----LHAIEHIAGK 346
Cdd:COG0492 252 -EDGYIVVDEDMETSVPGVFAAGDVRDYkYRQAATAAGEGaiaaLSAARYLEPL 304
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
148-348 |
4.68e-13 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 70.56 E-value: 4.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 148 LVIATGSKPRSLPGLEVDEKSVMT----SDGALLMNALPSSItii--gggVIGIEWASMLVDFGVDVTVMDRLEQILATE 221
Cdd:COG1251 102 LVLATGSRPRVPPIPGADLPGVFTlrtlDDADALRAALAPGKrvvvigggLIGLEAAAALRKRGLEVTVVERAPRLLPRQ 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 222 -DREVAVAMHKALAKRGVKFILGAEilTESLQKNDSEVTIsyKLGDEEQsITSEKMMVSVGRAPvidDIGL-QNTDIQVE 299
Cdd:COG1251 182 lDEEAGALLQRLLEALGVEVRLGTG--VTEIEGDDRVTGV--RLADGEE-LPADLVVVAIGVRP---NTELaRAAGLAVD 253
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1274541061 300 KGsIQTNNHYQTKDDHIYAIGDV-------IGGLQLAHV--AEHEGLHAIEHIAGKQV 348
Cdd:COG1251 254 RG-IVVDDYLRTSDPDIYAAGDCaehpgpvYGRRVLELVapAYEQARVAAANLAGGPA 310
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
194-260 |
3.29e-10 |
|
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: 56.44 E-value: 3.29e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1274541061 194 GIEWASMLVDFGVDVTVMDRLEQILATEDREVAVAMHKALAKRGVKFILGAEIltESLQKNDSEVTI 260
Cdd:pfam00070 11 GLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTV--EAIEGNGDGVVV 75
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
206-344 |
1.49e-09 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 59.76 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 206 VDVTVMDRLEQILATEDREVAVAMHKALAKRGVKFILGAEIlteslqkndSEVT---ISYKLGDEeqsITSEKMMVSVG- 281
Cdd:COG1252 186 VRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRV---------TEVDadgVTLEDGEE---IPADTVIWAAGv 253
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1274541061 282 RA-PVIDDIGLQnTDiqvEKGSIQTNNHYQTKD-DHIYAIGDVI-------GGL-QLAHVAEHEGLHAIEHIA 344
Cdd:COG1252 254 KApPLLADLGLP-TD---RRGRVLVDPTLQVPGhPNVFAIGDCAavpdpdgKPVpKTAQAAVQQAKVLAKNIA 322
|
|
| PRK12844 |
PRK12844 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
4-59 |
4.11e-07 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 183787 [Multi-domain] Cd Length: 557 Bit Score: 52.45 E-value: 4.11e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 4 EYDVVILGGGTGGYVAAIRAAQLGLITAIVEK-SKLGGTCLHSGC---IPSKAMLKSAEV 59
Cdd:PRK12844 6 TYDVVVVGSGGGGMCAALAAADSGLEPLIVEKqDKVGGSTAMSGGvlwLPNNPLMKAAGV 65
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
4-59 |
5.17e-07 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 51.96 E-value: 5.17e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 4 EYDVVILGGGTGGYVAAIRAAQLGLITAIVEKSK-LGGTCLHSGC---IPSKAMLKSAEV 59
Cdd:PRK07843 7 EYDVVVVGSGAAGMVAALTAAHRGLSTVVVEKAPhYGGSTARSGGgvwIPNNEVLKRAGV 66
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
148-321 |
1.24e-06 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 50.30 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 148 LVIATGSKP--RSLPGLEVdeksVMTSDG--------ALLMNAlpSSITIIGGGVIGIEWASMLVDFGVDVTVMDRLEQI 217
Cdd:PRK04965 103 LVLATGASAfvPPIPGREL----MLTLNSqqeyraaeTQLRDA--QRVLVVGGGLIGTELAMDLCRAGKAVTLVDNAASL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 218 LAT-EDREVAVAMHKALAKRGVKFILGAEIltESLQKNDSevTISYKLGDEEQSITSEkmmvsvgrapVIDDIGLQ-NT- 294
Cdd:PRK04965 177 LASlMPPEVSSRLQHRLTEMGVHLLLKSQL--QGLEKTDS--GIRATLDSGRSIEVDA----------VIAAAGLRpNTa 242
|
170 180 190
....*....|....*....|....*....|..
gi 1274541061 295 -----DIQVEKGsIQTNNHYQTKDDHIYAIGD 321
Cdd:PRK04965 243 larraGLAVNRG-IVVDSYLQTSAPDIYALGD 273
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
6-41 |
1.50e-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: 50.30 E-value: 1.50e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1274541061 6 DVVILGGGTGGYVAAIRAAQLGLITAIVEKSK-LGGT 41
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRGfLGGM 37
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
3-46 |
5.42e-06 |
|
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: 48.68 E-value: 5.42e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1274541061 3 KEYDVVILGGGTGGYVAAIRAAQLGLITAIVEK-SKLGGTCLHSG 46
Cdd:COG1053 2 HEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKvPPRGGHTAAAQ 46
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
148-424 |
5.80e-06 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 48.50 E-value: 5.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 148 LVIATGSKPRSLPGLEVDEKSVMT----SDG----ALLMNALPSSITIIGGGVIGIEWASMLVDFGVDVTVMDRLEQIL- 218
Cdd:PRK09564 107 LMIATGARPIIPPIKNINLENVYTlksmEDGlalkELLKDEEIKNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRILp 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 219 ATEDREVAVAMHKALAKRGVKFILGaEILTESLQKNDSEVTISYKlGDEEQSItsekMMVSVGRAPVIDdiGLQNTDIQ- 297
Cdd:PRK09564 187 DSFDKEITDVMEEELRENGVELHLN-EFVKSLIGEDKVEGVVTDK-GEYEADV----VIVATGVKPNTE--FLEDTGLKt 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 298 VEKGSIQTNNHYQTKDDHIYAIGD------VIGGLQ----LAHVAEHEGLHAIEHIAGKQVDSIDYdLVPRC--VYSYpE 365
Cdd:PRK09564 259 LKNGAIIVDEYGETSIENIYAAGDcatiynIVSNKNvyvpLATTANKLGRMVGENLAGRHVSFKGT-LGSACikVLDL-E 336
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1274541061 366 TAAVGLTEQQAKDRGFDVKIgKFPFKANGKALVNGHADGFVKIIVDQQTDDIIGVHMMG 424
Cdd:PRK09564 337 AARTGLTEEEAKKLGIDYKT-VFIKDKNHTNYYPGQEDLYVKLIYEADTKVILGGQIIG 394
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
148-336 |
7.01e-06 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 48.67 E-value: 7.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 148 LVIATGSKPRSLPGLEVDEKSVMT----SDGALLMNALPSSITIIGGGVIGI--EWASMLVDFGVDVTVMDRLEQILATE 221
Cdd:TIGR02374 100 LILATGSYPFILPIPGADKKGVYVfrtiEDLDAIMAMAQRFKKAAVIGGGLLglEAAVGLQNLGMDVSVIHHAPGLMAKQ 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 222 -DREVAVAMHKALAKRGVKFILGAEilTESLQKNDSEVTISYKLGdeeQSITSEKMMVSVGRAPViDDIGLQnTDIQVEK 300
Cdd:TIGR02374 180 lDQTAGRLLQRELEQKGLTFLLEKD--TVEIVGATKADRIRFKDG---SSLEADLIVMAAGIRPN-DELAVS-AGIKVNR 252
|
170 180 190
....*....|....*....|....*....|....*.
gi 1274541061 301 GsIQTNNHYQTKDDHIYAIGDvigglqlahVAEHEG 336
Cdd:TIGR02374 253 G-IIVNDSMQTSDPDIYAVGE---------CAEHNG 278
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
3-48 |
8.90e-06 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 47.92 E-value: 8.90e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1274541061 3 KEYDVVILGGGTGGYVAAIRAAQLGLITAIVEKsKLGGTCLHSGCI 48
Cdd:PRK05329 1 MKFDVLVIGGGLAGLTAALAAAEAGKRVALVAK-GQGALHFSSGSI 45
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
6-44 |
9.27e-06 |
|
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: 47.67 E-value: 9.27e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1274541061 6 DVVILGGGTGGYVAAIRAAQLGLITAIVEKSKLGGTCLH 44
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGATA 39
|
|
| GlpB |
COG3075 |
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism]; |
4-33 |
3.17e-05 |
|
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 442309 Cd Length: 415 Bit Score: 45.94 E-value: 3.17e-05
10 20 30
....*....|....*....|....*....|
gi 1274541061 4 EYDVVILGGGTGGYVAAIRAAQLGLITAIV 33
Cdd:COG3075 2 KFDVVVIGGGLAGLTAAIRAAEAGLRVAIV 31
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
193-433 |
4.72e-05 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 45.54 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 193 IGIEWASMLVDFGVDVTVMDRLEQILATEDREVAVAMHKALAKRGVKFILGAEIltesLQKNDSEVTisYKLGDEEqsiT 272
Cdd:PRK13512 159 ISLEVLENLYERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEI----DAINGNEVT--FKSGKVE---H 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 273 SEKMMVSVGRAP---VIDDIGLQNTDiqveKGSIQTNNHYQTKDDHIYAIGDVIGGLQL-----AHVA----EHEGLHAI 340
Cdd:PRK13512 230 YDMIIEGVGTHPnskFIESSNIKLDD----KGFIPVNDKFETNVPNIYAIGDIITSHYRhvdlpASVPlawgAHRAASIV 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 341 -EHIAGKqvDSIDY------DLVPRCVYSYpetAAVGLTEQQAKDrgFDVKI---------GKFP----------FKANG 394
Cdd:PRK13512 306 aEQIAGN--DTIEFkgflgnNIVKFFDYTF---ASVGVKPNELKQ--FDYKMvevtqgahaNYYPgnsplhlrvyYDTSN 378
|
250 260 270
....*....|....*....|....*....|....*....
gi 1274541061 395 KALVNGHADGfvKIIVDQQTdDIIGVHMMGSHVTDLISE 433
Cdd:PRK13512 379 RKILRAAAVG--KEGADKRI-DVLSMAMMNQLTVDELTE 414
|
|
| sdhA |
PRK07803 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
4-39 |
6.34e-05 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 236101 [Multi-domain] Cd Length: 626 Bit Score: 45.41 E-value: 6.34e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1274541061 4 EYDVVILGGGTGGYVAAIRAAQLGLITAIVEKSKLG 39
Cdd:PRK07803 8 SYDVVVIGAGGAGLRAAIEARERGLRVAVVCKSLFG 43
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
1-46 |
6.38e-05 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 45.59 E-value: 6.38e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1274541061 1 MSKEYDVVILGGGTGGYVAAIRAAQLGLITAIVEK-SKLGGTCLHSG 46
Cdd:PRK12839 5 MTHTYDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKaSTCGGATAWSG 51
|
|
| PRK12835 |
PRK12835 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
4-48 |
1.24e-04 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237221 [Multi-domain] Cd Length: 584 Bit Score: 44.41 E-value: 1.24e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1274541061 4 EYDVVILGGGTGGYVAAIRAAQLGLITAIVEKSKL--GGTCLHSGCI 48
Cdd:PRK12835 11 EVDVLVVGSGGGGMTAALTAAARGLDTLVVEKSAHfgGSTALSGGGI 57
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
3-45 |
2.36e-04 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 43.68 E-value: 2.36e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1274541061 3 KEYDVVILGGGTGGYVAAIRAAQLGLITAIVEK-SKLGGtCLHS 45
Cdd:COG1233 2 MMYDVVVIGAGIGGLAAAALLARAGYRVTVLEKnDTPGG-RART 44
|
|
| glycerol3P_GlpB |
TIGR03378 |
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are ... |
5-48 |
2.39e-04 |
|
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are the B subunit, product of the glpB gene, of a three-subunit, membrane-anchored, FAD-dependent anaerobic glycerol-3-phosphate dehydrogenase. [Energy metabolism, Anaerobic]
Pssm-ID: 213807 Cd Length: 419 Bit Score: 43.47 E-value: 2.39e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1274541061 5 YDVVILGGGTGGYVAAIRAAQLGLITAIVEKsklGGTCLH--SGCI 48
Cdd:TIGR03378 1 FDVIIIGGGLAGLSCALRLAEAGKKCAIIAA---GQSALHfsSGSL 43
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
2-46 |
2.42e-04 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 43.57 E-value: 2.42e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1274541061 2 SKEYDVVILGGGTGGYVAAIRAAQLGLITAIVEKSK-LGGTCLHSG 46
Cdd:PRK12843 14 DAEFDVIVIGAGAAGMSAALFAAIAGLKVLLVERTEyVGGTTATSA 59
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
4-46 |
2.58e-04 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 43.56 E-value: 2.58e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1274541061 4 EYDVVILGGGTGGYVAAIRAAQLGLITAIVEKS-KLGGTCLHSG 46
Cdd:PRK06134 12 ECDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDpVFGGTTAWSG 55
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
4-46 |
5.57e-04 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 42.37 E-value: 5.57e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1274541061 4 EYDVVILGGGTGGYVAAIRAAQLGLITAIVEKSK-LGGTCLHSG 46
Cdd:PRK12842 9 TCDVLVIGSGAGGLSAAITARKLGLDVVVLEKEPvFGGTTAFSG 52
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
5-55 |
5.99e-04 |
|
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: 41.92 E-value: 5.99e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1274541061 5 YDVVILGGGTGGYVAAIRAAQLGLITAIVEKSKLGG--TClhSGCIPSKAMLK 55
Cdd:TIGR02032 1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPRykPC--GGALSPRALEE 51
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
6-51 |
8.49e-04 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 41.38 E-value: 8.49e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1274541061 6 DVVILGGGTGGYVAAIRAAQLGLITA-IVEKsklGGTCLHSGCIPSK 51
Cdd:pfam01134 1 DVIVIGGGHAGCEAALAAARMGAKVLlITHN---TDTIAELSCNPSI 44
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
5-37 |
2.21e-03 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 40.26 E-value: 2.21e-03
10 20 30
....*....|....*....|....*....|...
gi 1274541061 5 YDVVILGGGTGGYVAAIRAAQLGLITAIVEKSK 37
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGK 33
|
|
| PRK06481 |
PRK06481 |
flavocytochrome c; |
1-40 |
3.02e-03 |
|
flavocytochrome c;
Pssm-ID: 180584 [Multi-domain] Cd Length: 506 Bit Score: 39.82 E-value: 3.02e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1274541061 1 MSKEYDVVILGGGTGGYVAAIRAAQLGLITAIVEKSKLGG 40
Cdd:PRK06481 58 LKDKYDIVIVGAGGAGMSAAIEAKDAGMNPVILEKMPVAG 97
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
118-322 |
5.33e-03 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 39.14 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 118 LGASIFSPMPGTISVEMDNGnenEILILKNLVIATGSKPRSLPGLEVDEKSVMT----SDGALLMNALPS--SITIIGGG 191
Cdd:PRK09754 77 SGVTIKTLGRDTRELVLTNG---ESWHWDQLFIATGAAARPLPLLDALGERCFTlrhaGDAARLREVLQPerSVVIVGAG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274541061 192 VIGIEWASMLVDFGVDVTVMDRLEQILAtedREVAVAMHKALAKR----GVKFILGAEIltESLQKNDsEVTISYKLGde 267
Cdd:PRK09754 154 TIGLELAASATQRRCKVTVIELAATVMG---RNAPPPVQRYLLQRhqqaGVRILLNNAI--EHVVDGE-KVELTLQSG-- 225
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1274541061 268 eQSITSEKMMVSVG---RAPVIDDIGLQNTdiqvekGSIQTNNHYQTKDDHIYAIGDV 322
Cdd:PRK09754 226 -ETLQADVVIYGIGisaNDQLAREANLDTA------NGIVIDEACRTCDPAIFAGGDV 276
|
|
| |
