|
Name |
Accession |
Description |
Interval |
E-value |
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
36-494 |
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: 593.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 36 SNDADVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNPtLGGTCLNVGCIPSKALLNNSHYYHMAHsgDLAKRGIESDNIRL 115
Cdd:COG1249 1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGR-LGGTCLNVGCIPSKALLHAAEVAHEAR--HAAEFGISAGAPSV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 116 NLDTLMQQKVHAVTALTGGIAQLFKKNKVDLIKGHGKITGVNQVTALKEdgssEVVNTKNILIATGSEVTPFPGIEIDEE 195
Cdd:COG1249 78 DWAALMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVTGG----ETLTADHIVIATGSRPRVPPIPGLDEV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 196 QVVSSTGALSLKEVPKRLIVIGAGVIGVELGSVWSRLGSEVTAIEFLPSIGGvGIDQEVSKTLQKILTKQGLNFKLGTKV 275
Cdd:COG1249 154 RVLTSDEALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLP-GEDPEISEALEKALEKEGIDILTGAKV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 276 TGATKSGGVVRVSVqdvKDSSKTDELECEVLLVCVGRRPYTENLGLEEMGIERDQKGRVPVNSVFQTVIPNIYAIGDCIH 355
Cdd:COG1249 233 TSVEKTGDGVTVTL---EDGGGEEAVEADKVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRTSVPGIYAIGDVTG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 356 GPMLAHKAEDEGIICIEGILGGPVH-IDYNCVPSVIYTHPEVGWVGRSEEDLKSEGVDYKVGKFPFLANSRAKTNNETDG 434
Cdd:COG1249 310 GPQLAHVASAEGRVAAENILGKKPRpVDYRAIPSVVFTDPEIASVGLTEEEAREAGIDVKVGKFPFAANGRALALGETEG 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 435 FVKVLADKATDRILGTHIVGPSAGELINEAVLAQEYGASSEDVARVCHAHPTCAEALREA 494
Cdd:COG1249 390 FVKLIADAETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEA 449
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
36-506 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 592.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 36 SNDADVVVIGSGPGGYVAAIKAAQLGLKTVCIEK------NPTLGGTCLNVGCIPSKALLNNSHYYHMAHSgDLAKRGIE 109
Cdd:PRK06327 2 SKQFDVVVIGAGPGGYVAAIRAAQLGLKVACIEAwknpkgKPALGGTCLNVGCIPSKALLASSEEFENAGH-HFADHGIH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 110 SDNIRLNLDTLMQQKVHAVTALTGGIAQLFKKNKVDLIKGHGKITGV----NQVTALKEDGssEVVNTKNILIATGSEVT 185
Cdd:PRK06327 81 VDGVKIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVGKtdagYEIKVTGEDE--TVITAKHVIIATGSEPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 186 PFPGIEIDEEQVVSSTGALSLKEVPKRLIVIGAGVIGVELGSVWSRLGSEVTAIEFLPSIGGVgIDQEVSKTLQKILTKQ 265
Cdd:PRK06327 159 HLPGVPFDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAA-ADEQVAKEAAKAFTKQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 266 GLNFKLGTKVTGATKSGGVVRVSVQDVKDSSKTdeLECEVLLVCVGRRPYTENLGLEEMGIERDQKGRVPVNSVFQTVIP 345
Cdd:PRK06327 238 GLDIHLGVKIGEIKTGGKGVSVAYTDADGEAQT--LEVDKLIVSIGRVPNTDGLGLEAVGLKLDERGFIPVDDHCRTNVP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 346 NIYAIGDCIHGPMLAHKAEDEGIICIEGILGGPVHIDYNCVPSVIYTHPEVGWVGRSEEDLKSEGVDYKVGKFPFLANSR 425
Cdd:PRK06327 316 NVYAIGDVVRGPMLAHKAEEEGVAVAERIAGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLKAEGVEYKAGKFPFMANGR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 426 AKTNNETDGFVKVLADKATDRILGTHIVGPSAGELINEAVLAQEYGASSEDVARVCHAHPTCAEALREANVsAAFGKPIN 505
Cdd:PRK06327 396 ALAMGEPDGFVKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEVWHEAAL-AVDKRPLH 474
|
.
gi 1746716866 506 F 506
Cdd:PRK06327 475 F 475
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
40-505 |
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: 569.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 40 DVVVIGSGPGGYVAAIKAAQLGLKTVCIEKnPTLGGTCLNVGCIPSKALLNNSHYYHMAhsGDLAKRGIESDNIRLNLDT 119
Cdd:TIGR01350 3 DVIVIGGGPGGYVAAIRAAQLGLKVALVEK-EYLGGTCLNVGCIPTKALLHSAEVYDEI--KHAKDLGIEVENVSVDWEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 120 LMQQKVHAVTALTGGIAQLFKKNKVDLIKGHGKITGVNQVTALKEDGSsEVVNTKNILIATGSEVTPFPG-IEIDEEQVV 198
Cdd:TIGR01350 80 MQKRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGENGE-ETLEAKNIIIATGSRPRSLPGpFDFDGKVVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 199 SSTGALSLKEVPKRLIVIGAGVIGVELGSVWSRLGSEVTAIEFLPSIGGvGIDQEVSKTLQKILTKQGLNFKLGTKVTGA 278
Cdd:TIGR01350 159 TSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILP-GEDAEVSKVLQKALKKKGVKILTNTKVTAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 279 TKSGGVVRVSVQDvkdsSKTDELECEVLLVCVGRRPYTENLGLEEMGIERDQKGRVPVNSVFQTVIPNIYAIGDCIHGPM 358
Cdd:TIGR01350 238 EKNDDQVTYENKG----GETETLTGEKVLVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDVIGGPM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 359 LAHKAEDEGIICIEGILGG-PVHIDYNCVPSVIYTHPEVGWVGRSEEDLKSEGVDYKVGKFPFLANSRAKTNNETDGFVK 437
Cdd:TIGR01350 314 LAHVASHEGIVAAENIAGKePAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGYDVKIGKFPFAANGKALALGETDGFVK 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1746716866 438 VLADKATDRILGTHIVGPSAGELINEAVLAQEYGASSEDVARVCHAHPTCAEALREAnVSAAFGKPIN 505
Cdd:TIGR01350 394 IIADKKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEAIKEA-ALAALGKPIH 460
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
35-506 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 540.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 35 SSNDADVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNpTLGGTCLNVGCIPSKALLNNSHYYH-MAHSGDLakrGIESDNI 113
Cdd:PRK06416 1 FAFEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKE-KLGGTCLNRGCIPSKALLHAAERADeARHSEDF---GIKAENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 114 RLNLdtlmqQKVHA-----VTALTGGIAQLFKKNKVDLIKGHGKITGVNQVTALKEDGSsEVVNTKNILIATGSEVTPFP 188
Cdd:PRK06416 77 GIDF-----KKVQEwkngvVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDGE-QTYTAKNIILATGSRPRELP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 189 GIEIDEEQVVSSTGALSLKEVPKRLIVIGAGVIGVELGSVWSRLGSEVTAIEFLPSIGGvGIDQEVSKTLQKILTKQGLN 268
Cdd:PRK06416 151 GIEIDGRVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILP-GEDKEISKLAERALKKRGIK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 269 FKLGTKVTGATKSGGVVRVSVQDvkdSSKTDELECEVLLVCVGRRPYTENLGLEEMGIERDqKGRVPVNSVFQTVIPNIY 348
Cdd:PRK06416 230 IKTGAKAKKVEQTDDGVTVTLED---GGKEETLEADYVLVAVGRRPNTENLGLEELGVKTD-RGFIEVDEQLRTNVPNIY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 349 AIGDCIHGPMLAHKAEDEGIICIEGILGGPVHIDYNCVPSVIYTHPEVGWVGRSEEDLKSEGVDYKVGKFPFLANSRAKT 428
Cdd:PRK06416 306 AIGDIVGGPMLAHKASAEGIIAAEAIAGNPHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFDVKVVKFPFAGNGKALA 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1746716866 429 NNETDGFVKVLADKATDRILGTHIVGPSAGELINEAVLAQEYGASSEDVARVCHAHPTCAEALREAnVSAAFGKPINF 506
Cdd:PRK06416 386 LGETDGFVKLIFDKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEALGEA-ALAAAGKPLHA 462
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
40-494 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 536.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 40 DVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNPtLGGTCLNVGCIPSKALLNNSHYYHMAHSGDlaKRGIESDNIRLNLDT 119
Cdd:PRK06292 5 DVIVIGAGPAGYVAARRAAKLGKKVALIEKGP-LGGTCLNVGCIPSKALIAAAEAFHEAKHAE--EFGIHADGPKIDFKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 120 LMQQKVHAVTALTGGIAQ-LFKKNKVDLIKGHGKITGVNQVTAlkedgSSEVVNTKNILIATGSEVTPFPGIE-IDEEQV 197
Cdd:PRK06292 82 VMARVRRERDRFVGGVVEgLEKKPKIDKIKGTARFVDPNTVEV-----NGERIEAKNIVIATGSRVPPIPGVWlILGDRL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 198 VSSTGALSLKEVPKRLIVIGAGVIGVELGSVWSRLGSEVTAIEFLPSIGGvGIDQEVSKTLQKILTKQgLNFKLGTKVTG 277
Cdd:PRK06292 157 LTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILP-LEDPEVSKQAQKILSKE-FKIKLGAKVTS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 278 ATKSGGVVRVSVqdvKDSSKTDELECEVLLVCVGRRPYTENLGLEEMGIERDQKGRVPVNSVFQTVIPNIYAIGDCIHGP 357
Cdd:PRK06292 235 VEKSGDEKVEEL---EKGGKTETIEADYVLVATGRRPNTDGLGLENTGIELDERGRPVVDEHTQTSVPGIYAAGDVNGKP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 358 MLAHKAEDEGIICIEGILGGP-VHIDYNCVPSVIYTHPEVGWVGRSEEDLKSEGVDYKVGKFPFLANSRAKTNNETDGFV 436
Cdd:PRK06292 312 PLLHEAADEGRIAAENAAGDVaGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEVPFEAQGRARVMGKNDGFV 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1746716866 437 KVLADKATDRILGTHIVGPSAGELINEAVLAQEYGASSEDVARVCHAHPTCAEALREA 494
Cdd:PRK06292 392 KVYADKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRTA 449
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
40-492 |
1.27e-109 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 333.32 E-value: 1.27e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 40 DVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNPtLGGTCLNVGCIPSKALLNNSHYYHMA-HSGDLakrGIE-SDNIRLNL 117
Cdd:PRK06370 7 DAIVIGAGQAGPPLAARAAGLGMKVALIERGL-LGGTCVNTGCVPTKTLIASARAAHLArRAAEY---GVSvGGPVSVDF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 118 DTLMQQKVHAVTALTGGIAQLFKK-NKVDLIKGHGKITGVNQVTAlkedgSSEVVNTKNILIATGSE--VTPFPGIeiDE 194
Cdd:PRK06370 83 KAVMARKRRIRARSRHGSEQWLRGlEGVDVFRGHARFESPNTVRV-----GGETLRAKRIFINTGARaaIPPIPGL--DE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 195 EQVVSSTGALSLKEVPKRLIVIGAGVIGVELGSVWSRLGSEVTAIEFLPSIGGvGIDQEVSKTLQKILTKQGLNFKLGTK 274
Cdd:PRK06370 156 VGYLTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLP-REDEDVAAAVREILEREGIDVRLNAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 275 VTGATKSGGVVRVsvqDVKDSSKTDELECEVLLVCVGRRPYTENLGLEEMGIERDQKGRVPVNSVFQTVIPNIYAIGDCI 354
Cdd:PRK06370 235 CIRVERDGDGIAV---GLDCNGGAPEITGSHILVAVGRVPNTDDLGLEAAGVETDARGYIKVDDQLRTTNPGIYAAGDCN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 355 HGPMLAHKAEDEGIICIEGIL-GGPVHIDYNCVPSVIYTHPEVGWVGRSEEDLKSEGVDYKVGKFPFLANSRAKTNNETD 433
Cdd:PRK06370 312 GRGAFTHTAYNDARIVAANLLdGGRRKVSDRIVPYATYTDPPLARVGMTEAEARKSGRRVLVGTRPMTRVGRAVEKGETQ 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1746716866 434 GFVKVLADKATDRILGTHIVGPSAGELINEAVLAQEYGASSEDVARVCHAHPTCAEALR 492
Cdd:PRK06370 392 GFMKVVVDADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIP 450
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
40-494 |
1.89e-104 |
|
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: 320.14 E-value: 1.89e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 40 DVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNPtLGGTCLNVGCIPSKALLNNSHYYHMAHSgdlAKRGIESDNIRLNLDT 119
Cdd:TIGR02053 2 DLVIIGSGAAAFAAAIKAAELGASVAMVERGP-LGGTCVNVGCVPSKMLLRAAEVAHYARK---PPFGGLAATVAVDFGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 120 LMQQKVHAVTALtggiaqlfKKNK---------VDLIKGHGKITGVNQVtalKEDGSSEVVNTKNILIATGSE--VTPFP 188
Cdd:TIGR02053 78 LLEGKREVVEEL--------RHEKyedvlssygVDYLRGRARFKDPKTV---KVDLGREVRGAKRFLIATGARpaIPPIP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 189 GIeiDEEQVVSSTGALSLKEVPKRLIVIGAGVIGVELGSVWSRLGSEVTAIE----FLPsiggvGIDQEVSKTLQKILTK 264
Cdd:TIGR02053 147 GL--KEAGYLTSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQrsdrLLP-----REEPEISAAVEEALAE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 265 QGLNFKLGTKVTGATKSGGVVRVsvqDVKDSSKTDELECEVLLVCVGRRPYTENLGLEEMGIERDQKGRVPVNSVFQTVI 344
Cdd:TIGR02053 220 EGIEVVTSAQVKAVSVRGGGKII---TVEKPGGQGEVEADELLVATGRRPNTDGLGLEKAGVKLDERGGILVDETLRTSN 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 345 PNIYAIGDCIHGPMLAHKAEDEGIICIEGILGGP-VHIDYNCVPSVIYTHPEVGWVGRSEEDLKSEGVDYKVGKFPFLAN 423
Cdd:TIGR02053 297 PGIYAAGDVTGGLQLEYVAAKEGVVAAENALGGAnAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNV 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1746716866 424 SRAKTNNETDGFVKVLADKATDRILGTHIVGPSAGELINEAVLAQEYGASSEDVARVCHAHPTCAEALREA 494
Cdd:TIGR02053 377 PRARINRDTRGFIKLVAEPGTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGLKLA 447
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
34-494 |
1.50e-103 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 317.87 E-value: 1.50e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 34 SSSNDADVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNPTLGGTCLNVGCIPSKAL------LNNSHYYHMaHSGDLAKRG 107
Cdd:PRK05249 1 MHMYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGGGCTHTGTIPSKALreavlrLIGFNQNPL-YSSYRVKLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 108 IESDNIRLNLDTLMQQKVHAVTALtggiaqlFKKNKVDLIKGHGKITGVNQVTALKEDGSSEVVNTKNILIATGSEvtPF 187
Cdd:PRK05249 80 ITFADLLARADHVINKQVEVRRGQ-------YERNRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATGSR--PY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 188 --PGIEIDEEQVVSSTGALSLKEVPKRLIVIGAGVIGVELGSVWSRLGSEVTAIE-------FLpsiggvgiDQEVSKTL 258
Cdd:PRK05249 151 rpPDVDFDHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINtrdrllsFL--------DDEISDAL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 259 QKILTKQGLNFKLGTKVTG-ATKSGGVVrVSVQDVKdssktdELECEVLLVCVGRRPYTENLGLEEMGIERDQKGRVPVN 337
Cdd:PRK05249 223 SYHLRDSGVTIRHNEEVEKvEGGDDGVI-VHLKSGK------KIKADCLLYANGRTGNTDGLNLENAGLEADSRGQLKVN 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 338 SVFQTVIPNIYAIGDCIHGPMLAHKAEDEGIICIEGILGGPVHIDYNCVPSVIYTHPEVGWVGRSEEDLKSEGVDYKVGK 417
Cdd:PRK05249 296 ENYQTAVPHIYAVGDVIGFPSLASASMDQGRIAAQHAVGEATAHLIEDIPTGIYTIPEISSVGKTEQELTAAKVPYEVGR 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1746716866 418 FPFLANSRAKTNNETDGFVKVLADKATDRILGTHIVGPSAGEL--INEAVLAQeyGASSEDVARVCHAHPTCAEALREA 494
Cdd:PRK05249 376 ARFKELARAQIAGDNVGMLKILFHRETLEILGVHCFGERATEIihIGQAIMEQ--KGTIEYFVNTTFNYPTMAEAYRVA 452
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
36-489 |
3.97e-78 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 251.61 E-value: 3.97e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 36 SNDADVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNpTLGGTCLNVGCIPSKALLNNSHYYHMAHsgDLAKR-GIESDNIR 114
Cdd:PRK06116 2 TKDYDLIVIGGGSGGIASANRAAMYGAKVALIEAK-RLGGTCVNVGCVPKKLMWYGAQIAEAFH--DYAPGyGFDVTENK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 115 LNLDTLMQQKVHAVTALTGGIAQLFKKNKVDLIKGHGKITGVNQVTAlkedgSSEVVNTKNILIATGSEVTP--FPGIEi 192
Cdd:PRK06116 79 FDWAKLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEV-----NGERYTADHILIATGGRPSIpdIPGAE- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 193 deeQVVSSTGALSLKEVPKRLIVIGAGVIGVELGSVWSRLGSEVTAI----EFLPsiggvGIDQEVSKTLQKILTKQGLN 268
Cdd:PRK06116 153 ---YGITSDGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFvrgdAPLR-----GFDPDIRETLVEEMEKKGIR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 269 FKLGTKVTGATK-SGGVVRVSVQDVKdssktdELECEVLLVCVGRRPYTENLGLEEMGIERDQKGRVPVNSVFQTVIPNI 347
Cdd:PRK06116 225 LHTNAVPKAVEKnADGSLTLTLEDGE------TLTVDCLIWAIGREPNTDGLGLENAGVKLNEKGYIIVDEYQNTNVPGI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 348 YAIGDCIHGPMLAHKAEDEGIICIEGILGG--PVHIDYNCVPSVIYTHPEVGWVGRSEEDLKSEGVDY--KVGKFPFLAN 423
Cdd:PRK06116 299 YAVGDVTGRVELTPVAIAAGRRLSERLFNNkpDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDnvKVYRSSFTPM 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1746716866 424 SRAKTNNETDGFVKVLADKATDRILGTHIVGPSAGELINEAVLAQEYGASSEDVARVCHAHPTCAE 489
Cdd:PRK06116 379 YTALTGHRQPCLMKLVVVGKEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAE 444
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
40-367 |
3.09e-77 |
|
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: 244.53 E-value: 3.09e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 40 DVVVIGSGPGGYVAAIKAAQLGLKTVCIEknptLGGTCLNVGCIPSKALLnnshyyHMAHSGDLAKRGIEsdnirlnldt 119
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIE----DEGTCPYGGCVLSKALL------GAAEAPEIASLWAD---------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 120 LMQQKVHAVTALTGGIAQLFKKNKVDLIKGHGKITGVNQVtalkeDGSSEVVNTKNILIATGSE--VTPFPGIE---IDE 194
Cdd:pfam07992 62 LYKRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELV-----DGDGETITYDRLVIATGARprLPPIPGVElnvGFL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 195 EQVVSSTGALSLKEVPKRLIVIGAGVIGVELGSVWSRLGSEVTAIEFLPSIGGvGIDQEVSKTLQKILTKQGLNFKLGTK 274
Cdd:pfam07992 137 VRTLDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLR-AFDEEISAALEKALEKNGVEVRLGTS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 275 VTGATKSGGVVRVSVQDVkdssktDELECEVLLVCVGRRPYTEnlGLEEMGIERDQKGRVPVNSVFQTVIPNIYAIGDC- 353
Cdd:pfam07992 216 VKEIIGDGDGVEVILKDG------TEIDADLVVVAIGRRPNTE--LLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDCr 287
|
330
....*....|....
gi 1746716866 354 IHGPMLAHKAEDEG 367
Cdd:pfam07992 288 VGGPELAQNAVAQG 301
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
35-499 |
3.94e-74 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 246.75 E-value: 3.94e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 35 SSNDADVVVIGSGPGGYVAAIKAAQLGLKTVCIE-KNPTLGGTCLNVGCIPSKALL----------NNSHYYHMAHSGDL 103
Cdd:PTZ00153 113 SDEEYDVGIIGCGVGGHAAAINAMERGLKVIIFTgDDDSIGGTCVNVGCIPSKALLyatgkyrelkNLAKLYTYGIYTNA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 104 AKRGIE---------SDNIRLNLDTLMQQKVHAVTALTGGIAQLFKKNKVDLIKGHGKITG-----VNQVTAlKEDGSSE 169
Cdd:PTZ00153 193 FKNGKNdpvernqlvADTVQIDITKLKEYTQSVIDKLRGGIENGLKSKKFCKNSEHVQVIYerghiVDKNTI-KSEKSGK 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 170 VVNTKNILIATGSevTPF--PGIEIDEEQVVSSTGALSLKEVPKRLIVIGAGVIGVELGSVWSRLGSEVTAIEFLPSIGG 247
Cdd:PTZ00153 272 EFKVKNIIIATGS--TPNipDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSPQLLP 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 248 vGIDQEVSKTLQKILTK-QGLNFKLGTKVTGATKSGGVVRVSVQ-----------DVKDSSKTDELECEVLLVCVGRRPY 315
Cdd:PTZ00153 350 -LLDADVAKYFERVFLKsKPVRVHLNTLIEYVRAGKGNQPVIIGhserqtgesdgPKKNMNDIKETYVDSCLVATGRKPN 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 316 TENLGLEEMGIeRDQKGRVPVNSVFQT------VIPNIYAIGDCIHGPMLAHKAEDEGIICIEGILG------------- 376
Cdd:PTZ00153 429 TNNLGLDKLKI-QMKRGFVSVDEHLRVlredqeVYDNIFCIGDANGKQMLAHTASHQALKVVDWIEGkgkenvninvenw 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 377 GPVHIDYNCVPSVIYTHPEVGWVGRSEEDLKSEGVDYKVGKFP--FLANSRA----------------------KTNNET 432
Cdd:PTZ00153 508 ASKPIIYKNIPSVCYTTPELAFIGLTEKEAKELYPPDNVGVEIsfYKANSKVlcennisfpnnsknnsynkgkyNTVDNT 587
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1746716866 433 DGFVKVLADKATDRILGTHIVGPSAGELINEAVLAQEYGASSEDVARVCHAHPTCAEALREANVSAA 499
Cdd:PTZ00153 588 EGMVKIVYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDAAFKAIA 654
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
40-491 |
1.31e-69 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 229.25 E-value: 1.31e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 40 DVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNPTL-GGTCLNVGCIPSKALLnnshyyHMAHSGdlakrgiesdnirLNLD 118
Cdd:PRK07251 5 DLIVIGFGKAGKTLAAKLASAGKKVALVEESKAMyGGTCINIGCIPTKTLL------VAAEKN-------------LSFE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 119 TLMQQKVHAVTALTGGIAQLFKKNKVDLIKGHGKITGvNQVTALKEDGSSEVVNTKNILIATG--SEVTPFPGIEiDEEQ 196
Cdd:PRK07251 66 QVMATKNTVTSRLRGKNYAMLAGSGVDLYDAEAHFVS-NKVIEVQAGDEKIELTAETIVINTGavSNVLPIPGLA-DSKH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 197 VVSSTGALSLKEVPKRLIVIGAGVIGVELGSVWSRLGSEVTAIEFLPSIGGvGIDQEVSKTLQKILTKQGLNFKLGTKVT 276
Cdd:PRK07251 144 VYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILP-REEPSVAALAKQYMEEDGITFLLNAHTT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 277 GATKSGGVVRVSVQDvkdssktDELECEVLLVCVGRRPYTENLGLEEMGIERDQKGRVPVNSVFQTVIPNIYAIGDCIHG 356
Cdd:PRK07251 223 EVKNDGDQVLVVTED-------ETYRFDALLYATGRKPNTEPLGLENTDIELTERGAIKVDDYCQTSVPGVFAVGDVNGG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 357 PMLAHKAEDEGIIcIEGILGGP---VHIDYNCVPSVIYTHPEVGWVGRSEEDLKSEGVDYKVGKFPFLANSRAKTNNETD 433
Cdd:PRK07251 296 PQFTYISLDDFRI-VFGYLTGDgsyTLEDRGNVPTTMFITPPLSQVGLTEKEAKEAGLPYAVKELLVAAMPRAHVNNDLR 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1746716866 434 GFVKVLADKATDRILGTHIVGPSAGELINEAVLAQEYGASSEDVARVCHAHPTCAEAL 491
Cdd:PRK07251 375 GAFKVVVNTETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAENL 432
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
41-467 |
1.68e-69 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 232.35 E-value: 1.68e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 41 VVVIGSGPGGYVAAIKAAQLGLKTVCIEKNpTLGGTCLNVGCIPSKALLNNSHYYHMAHSGDLAKrGIESDNIRLNLDTL 120
Cdd:PRK13748 101 VAVIGSGGAAMAAALKAVEQGARVTLIERG-TIGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDG-GIAATVPTIDRSRL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 121 MQQKVHAVTALTG----GIaqLFKKNKVDLIKGHGKITGVNQVTALKEDGSSEVVNTKNILIATGSE--VTPFPGIEidE 194
Cdd:PRK13748 179 LAQQQARVDELRHakyeGI--LDGNPAITVLHGEARFKDDQTLIVRLNDGGERVVAFDRCLIATGASpaVPPIPGLK--E 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 195 EQVVSSTGALSLKEVPKRLIVIGAGVIGVELGSVWSRLGSEVTaieflpsiggvgidqevsktlqkILTKQGLNFK---- 270
Cdd:PRK13748 255 TPYWTSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVT-----------------------ILARSTLFFRedpa 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 271 LGTKVTGATKSGGV--------VRVSVQDVKDSSKTD--ELECEVLLVCVGRRPYTENLGLEEMGIERDQKGRVPVNSVF 340
Cdd:PRK13748 312 IGEAVTAAFRAEGIevlehtqaSQVAHVDGEFVLTTGhgELRADKLLVATGRAPNTRSLALDAAGVTVNAQGAIVIDQGM 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 341 QTVIPNIYAIGDCIHGPMLAHKAEDEGIICIEGILGGPVHIDYNCVPSVIYTHPEVGWVGRSEEDLKSEGVDYKVGKFPF 420
Cdd:PRK13748 392 RTSVPHIYAAGDCTDQPQFVYVAAAAGTRAAINMTGGDAALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRTLTL 471
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1746716866 421 LANSRAKTNNETDGFVKVLADKATDRILGTHIVGPSAGELINEAVLA 467
Cdd:PRK13748 472 DNVPRALANFDTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAALA 518
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
38-489 |
7.08e-67 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 223.54 E-value: 7.08e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 38 DADVVVIGSGPGGYVAAIKAAQLGLKT---------VCIEKNPTLGGTCLNVGCIPSKALLnnshyYHMAHSGDL--AKR 106
Cdd:PLN02507 25 DFDLFVIGAGSGGVRAARFSANFGAKVgicelpfhpISSESIGGVGGTCVIRGCVPKKILV-----YGATFGGEFedAKN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 107 -GIE-SDNIRLNLDTLMQQKVHAVTALTGGIAQLFKKNKVDLIKGHGKITGVNQVTALKEDGSSEVVNTKNILIATGSEV 184
Cdd:PLN02507 100 yGWEiNEKVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRYTAKHILIATGSRA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 185 TP--FPGieidEEQVVSSTGALSLKEVPKRLIVIGAGVIGVELGSVWSRLGSEVTAIeFLPSIGGVGIDQEVSKTLQKIL 262
Cdd:PLN02507 180 QRpnIPG----KELAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLF-FRKELPLRGFDDEMRAVVARNL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 263 TKQGLNFKLGTKVTGATKSGGVVRVSVqdvkdsSKTDELECEVLLVCVGRRPYTENLGLEEMGIERDQKGRVPVNSVFQT 342
Cdd:PLN02507 255 EGRGINLHPRTNLTQLTKTEGGIKVIT------DHGEEFVADVVLFATGRAPNTKRLNLEAVGVELDKAGAVKVDEYSRT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 343 VIPNIYAIGDCIHGPMLAHKAEDEGIICIEGILGG-PVHIDYNCVPSVIYTHPEVGWVGRSEEdlksEGVDYKVGKFPFL 421
Cdd:PLN02507 329 NIPSIWAIGDVTNRINLTPVALMEGTCFAKTVFGGqPTKPDYENVACAVFCIPPLSVVGLSEE----EAVEQAKGDILVF 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1746716866 422 ANSRAKTNNETDG-----FVKVLADKATDRILGTHIVGPSAGELINEAVLAQEYGASSEDVARVCHAHPTCAE 489
Cdd:PLN02507 405 TSSFNPMKNTISGrqektVMKLIVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAE 477
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
41-479 |
1.92e-65 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 218.96 E-value: 1.92e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 41 VVVIGSGPGGYVAAIKAAQLGLKTVCIEKNpTLGGTCLNVGCIPSKALLNNSHYY-HMAHSGDLAKRGIESDNIRLNLDt 119
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIERD-GLGGAAVLTDCVPSKTLIATAEVRtELRRAAELGIRFIDDGEARVDLP- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 120 lmqqKVHA-VTALT----GGIAQLFKKNKVDLIKGHGKIT----GVNQVTALKEDGSSEVVNTKNILIATGSevTP--FP 188
Cdd:PRK07845 82 ----AVNArVKALAaaqsADIRARLEREGVRVIAGRGRLIdpglGPHRVKVTTADGGEETLDADVVLIATGA--SPriLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 189 GIEIDEEQVVSSTGALSLKEVPKRLIVIGAGVIGVELGSVWSRLGSEVTAI----EFLPsiggvGIDQEVSKTLQKILTK 264
Cdd:PRK07845 156 TAEPDGERILTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVssrdRVLP-----GEDADAAEVLEEVFAR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 265 QGLNFKLGTKVTGATKSGGVVRVSVQDVKdssktdELECEVLLVCVGRRPYTENLGLEEMGIERDQKGRVPVNSVFQTVI 344
Cdd:PRK07845 231 RGMTVLKRSRAESVERTGDGVVVTLTDGR------TVEGSHALMAVGSVPNTAGLGLEEAGVELTPSGHITVDRVSRTSV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 345 PNIYAIGDCIHGPMLAHKAEDEGIICIEGILGGPVH-IDYNCVPSVIYTHPEVGWVGRSEEDLKSEGVDYKVGKFPFLAN 423
Cdd:PRK07845 305 PGIYAAGDCTGVLPLASVAAMQGRIAMYHALGEAVSpLRLKTVASNVFTRPEIATVGVSQAAIDSGEVPARTVMLPLATN 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1746716866 424 SRAKTNNETDGFVKVLADKATDRILGTHIVGPSAGELINEAVLAQEYGASSEDVAR 479
Cdd:PRK07845 385 PRAKMSGLRDGFVKLFCRPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQ 440
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
37-493 |
2.88e-64 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 215.03 E-value: 2.88e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 37 NDADVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNPTL-GGTCLNVGCIPSKALLNNSHYYHmahsgdlakrgiesdnirl 115
Cdd:NF040477 2 NHYQAIIIGFGKAGKTLAATLAKAGWRVAIIEQSAQMyGGTCINIGCIPTKTLVHDAEQHQ------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 116 NLDTLMQQKVHAVtaltggiAQLFKKN--------KVDLIKGHGKITGVNQVTALKEDGSSEVVNTKnILIATGSEVT-- 185
Cdd:NF040477 63 DFSTAMQRKSSVV-------GFLRDKNyhnladldNVDVINGRAEFIDNHTLRVFQADGEQELRGEK-IFINTGAQSVlp 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 186 PFPGIEIdEEQVVSSTGALSLKEVPKRLIVIGAGVIGVELGSVWSRLGSEVTAIE----FLPSiggvgIDQEVSKTLQKI 261
Cdd:NF040477 135 PIPGLTT-TPGVYDSTGLLNLTQLPARLGILGGGYIGVEFASMFARFGSKVTIFEaaelFLPR-----EDRDIAQAIATI 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 262 LTKQGLNFKLGTKVTGATKSGGVVRVSVQDvkdssktDELECEVLLVCVGRRPYTENLGLEEMGIERDQKGRVPVNSVFQ 341
Cdd:NF040477 209 LQDQGVELILNAQVQRVSSHEGEVQLETAE-------GVLTVDALLVASGRKPATAGLQLQNAGVAVNERGAIVVDKYLR 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 342 TVIPNIYAIGDCIHGPMLAHKAEDEGIICIEGILG-GPVHI-DYNCVPSVIYTHPEVGWVGRSEEDLKSEGVDYKVGKFP 419
Cdd:NF040477 282 TTADNIWAMGDVTGGLQFTYISLDDFRIVRDSLLGeGKRSTdDRQNVPYSVFMTPPLSRIGMTEEQARASGADIQVVTLP 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1746716866 420 FLANSRAKTNNETDGFVKVLADKATDRILGTHIVGPSAGELINEAVLAQEYGASSEDVARVCHAHPTCAEALRE 493
Cdd:NF040477 362 VAAIPRARVMNDTRGVLKAVVDNKTQRILGVSLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSESLND 435
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
40-491 |
1.41e-63 |
|
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: 213.55 E-value: 1.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 40 DVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNpTLGGTCLNVGCIPSKALLNNSHYYHMAHsgDLAKRGIES-DNIRLNLD 118
Cdd:TIGR01421 4 DYLVIGGGSGGIASARRAAEHGAKALLVEAK-KLGGTCVNVGCVPKKVMWYASDLAERMH--DAADYGFYQnDENTFNWP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 119 TLMQQKVHAVTALTGGIAQLFKKNKVDLIKGHGKITGVNQVTALKEDGSSevvntKNILIATGSEVTPFPGIEiDEEQVV 198
Cdd:TIGR01421 81 ELKEKRDAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVNGRDYTA-----PHILIATGGKPSFPENIP-GAELGT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 199 SSTGALSLKEVPKRLIVIGAGVIGVELGSVWSRLGSEvTAIEFLPSIGGVGIDQEVSKTLQKILTKQGLNF-KLGTKVTG 277
Cdd:TIGR01421 155 DSDGFFALEELPKRVVIVGAGYIAVELAGVLHGLGSE-THLVIRHERVLRSFDSMISETITEEYEKEGINVhKLSKPVKV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 278 ATKSGGVVRVSVQDVKDSSKTDElecevLLVCVGRRPYTENLGLEEMGIERDQKGRVPVNSVFQTVIPNIYAIGDCIHGP 357
Cdd:TIGR01421 234 EKTVEGKLVIHFEDGKSIDDVDE-----LIWAIGRKPNTKGLGLENVGIKLNEKGQIIVDEYQNTNVPGIYALGDVVGKV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 358 MLAHKAEDEGIICIEGILGGP--VHIDYNCVPSVIYTHPEVGWVGRSEED-LKSEGVD-YKVGKFPFLANSRAKTNNETD 433
Cdd:TIGR01421 309 ELTPVAIAAGRKLSERLFNGKtdDKLDYNNVPTVVFSHPPIGTIGLTEKEaIEKYGKEnIKVYNSSFTPMYYAMTSEKQK 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1746716866 434 GFVKVLADKATDRILGTHIVGPSAGELINEAVLAQEYGASSEDVARVCHAHPTCAEAL 491
Cdd:TIGR01421 389 CRMKLVCAGKEEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEEL 446
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
40-479 |
8.56e-62 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 209.04 E-value: 8.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 40 DVVVIGSGPGGYVAAIKAAqlGLKTVCIEKNpTLGGTCLNVGCIPSKALLnnshyyhmaHSGDLAKRGIESDniRLNLDT 119
Cdd:PRK07846 3 DLIIIGTGSGNSILDERFA--DKRIAIVEKG-TFGGTCLNVGCIPTKMFV---------YAADVARTIREAA--RLGVDA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 120 LM-----QQKVHAVTALTGGIAQ------LFKKNKVDLIKGHGKITGVNQVTAlkedGSSEVVNTKNILIATGSEVTPFP 188
Cdd:PRK07846 69 ELdgvrwPDIVSRVFGRIDPIAAggeeyrGRDTPNIDVYRGHARFIGPKTLRT----GDGEEITADQVVIAAGSRPVIPP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 189 GIEIDEEQVVSSTGALSLKEVPKRLIVIGAGVIGVELGSVWSRLGSEVTAI---EFLPSiggvGIDQEVSKTLQKIlTKQ 265
Cdd:PRK07846 145 VIADSGVRYHTSDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVnrsGRLLR----HLDDDISERFTEL-ASK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 266 GLNFKLGTKVTGATKSGGVVRVSVQDvkdsskTDELECEVLLVCVGRRPYTENLGLEEMGIERDQKGRVPVNSVFQTVIP 345
Cdd:PRK07846 220 RWDVRLGRNVVGVSQDGSGVTLRLDD------GSTVEADVLLVATGRVPNGDLLDAAAAGVDVDEDGRVVVDEYQRTSAE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 346 NIYAIGDCIHGPMLAHKAEDEGIICIEGILGG--PVHIDYNCVPSVIYTHPEVGWVGRSEEDLKSEGVDY--KVGKFPFL 421
Cdd:PRK07846 294 GVFALGDVSSPYQLKHVANHEARVVQHNLLHPddLIASDHRFVPAAVFTHPQIASVGLTENEARAAGLDItvKVQNYGDV 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1746716866 422 ANSRAKTNneTDGFVKVLADKATDRILGTHIVGPSAGELINEAVLAQEYGASSEDVAR 479
Cdd:PRK07846 374 AYGWAMED--TTGFVKLIADRDTGRLLGAHIIGPQASTLIQPLIQAMSFGLDAREMAR 429
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
37-504 |
1.89e-58 |
|
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: 200.85 E-value: 1.89e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 37 NDADVVVIGSGPGGYVAAIKAAQLGLKTVCIEK-NPT-------LGGTCLNVGCIPSKALlnnsHYyhMAHSG----DLA 104
Cdd:TIGR01438 1 YDYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFvTPTplgtrwgIGGTCVNVGCIPKKLM----HQ--AALLGqalkDSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 105 KRGIESDN-IRLNLDTLMQQKVHAVTALTGGIAQLFKKNKVDLIKGHGKITGVNQVTALKEDGSSEVVNTKNILIATGsE 183
Cdd:TIGR01438 75 NYGWKVEEtVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATG-E 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 184 VTPFPGIEIDEEQVVSSTGALSLKEVPKRLIVIGAGVIGVELGSVWSRLGSEVTAIefLPSIGGVGIDQEVSKTLQKILT 263
Cdd:TIGR01438 154 RPRYPGIPGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVM--VRSILLRGFDQDCANKVGEHME 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 264 KQGLNFKLGTKVTGATKSGGVVRVSVQDvkdSSKTDELECEVLLVCVGRRPYTENLGLEEMGIERDQK-GRVPVNSVFQT 342
Cdd:TIGR01438 232 EHGVKFKRQFVPIKVEQIEAKVLVEFTD---STNGIEEEYDTVLLAIGRDACTRKLNLENVGVKINKKtGKIPADEEEQT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 343 VIPNIYAIGDCIHG-PMLAHKAEDEGIICIEGILGGPVHI-DYNCVPSVIYTHPEVGWVGRSEED----LKSEGVDYKVG 416
Cdd:TIGR01438 309 NVPYIYAVGDILEDkPELTPVAIQAGRLLAQRLFKGSTVIcDYENVPTTVFTPLEYGACGLSEEKavekFGEENVEVFHS 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 417 KFPFLANSRAKTNNETDGFVKVLADKATD-RILGTHIVGPSAGELINEAVLAQEYGASSEDVARVCHAHPTCAEALREAN 495
Cdd:TIGR01438 389 YFWPLEWTIPSRDNHNKCYAKLVCNKKENeRVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTLS 468
|
....*....
gi 1746716866 496 VSAAFGKPI 504
Cdd:TIGR01438 469 VTKRSGQDI 477
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
37-493 |
7.02e-55 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 190.22 E-value: 7.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 37 NDADVVVIGSGPGGYVAAIKAAQLGLKTVCIEK-NPTLGGTCLNVGCIPSKALLNNSHyyhmaHSGDLAkRGIESDNIRL 115
Cdd:PRK08010 2 NKYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQsNAMYGGTCINIGCIPTKTLVHDAQ-----QHTDFV-RAIQRKNEVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 116 NLdtLMQQKVHAVTALtggiaqlfkkNKVDLIKGHGKITGVNQVTALKEDGSSEVVNTKnILIATGSE--VTPFPGIEId 193
Cdd:PRK08010 76 NF--LRNKNFHNLADM----------PNIDVIDGQAEFINNHSLRVHRPEGNLEIHGEK-IFINTGAQtvVPPIPGITT- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 194 EEQVVSSTGALSLKEVPKRLIVIGAGVIGVELGSVWSRLGSEVTAIE----FLPSIggvgiDQEVSKTLQKILTKQGLNF 269
Cdd:PRK08010 142 TPGVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEaaslFLPRE-----DRDIADNIATILRDQGVDI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 270 KLGTKVTGATKSGGVVRVSvqdvkdsSKTDELECEVLLVCVGRRPYTENLGLEEMGIERDQKGRVPVNSVFQTVIPNIYA 349
Cdd:PRK08010 217 ILNAHVERISHHENQVQVH-------SEHAQLAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKYLHTTADNIWA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 350 IGDCIHGPMLAHKAEDEGIICIEGILGGPVHI--DYNCVPSVIYTHPEVGWVGRSEEDLKSEGVDYKVGKFPFLANSRAK 427
Cdd:PRK08010 290 MGDVTGGLQFTYISLDDYRIVRDELLGEGKRStdDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRAR 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1746716866 428 TNNETDGFVKVLADKATDRILGTHIVGPSAGELINEAVLAQEYGASSEDVARVCHAHPTCAEALRE 493
Cdd:PRK08010 370 VMNDTRGVLKAIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLND 435
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
40-491 |
5.80e-52 |
|
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: 183.64 E-value: 5.80e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 40 DVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNPT---------LGGTCLNVGCIPSKALLNNSHYyhMAHSGDLAKRGIES 110
Cdd:TIGR01423 5 DLVVIGAGSGGLEAGWNAATLYKKRVAVVDVQThhgppfyaaLGGTCVNVGCVPKKLMVTGAQY--MDTLRESAGFGWEF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 111 D--NIRLNLDTLMQQKVHAVTALTGGIAQLFKKNK-VDLIKGHGKITGVNQV----TALKEDGSSEVVNTKNILIATGS- 182
Cdd:TIGR01423 83 DrsSVKANWKALIAAKNKAVLDINKSYEGMFADTEgLTFFLGWGALEDKNVVlvreSADPKSAVKERLQAEHILLATGSw 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 183 -EVTPFPGIEideeQVVSSTGALSLKEVPKRLIVIGAGVIGVELGSV---WSRLGSEVTaIEFLPSIGGVGIDQEVSKTL 258
Cdd:TIGR01423 163 pQMLGIPGIE----HCISSNEAFYLDEPPRRVLTVGGGFISVEFAGIfnaYKPRGGKVT-LCYRNNMILRGFDSTLRKEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 259 QKILTKQGLNFKLGTKVTGATKSG-GVVRVSVQDVKdssktdELECEVLLVCVGRRPYTENLGLEEMGIERDQKGRVPVN 337
Cdd:TIGR01423 238 TKQLRANGINIMTNENPAKVTLNAdGSKHVTFESGK------TLDVDVVMMAIGRVPRTQTLQLDKVGVELTKKGAIQVD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 338 SVFQTVIPNIYAIGDCIHGPMLAHKAEDEGIICIEGILGG-PVHIDYNCVPSVIYTHPEVGWVGRSEEDL--KSEGVDYK 414
Cdd:TIGR01423 312 EFSRTNVPNIYAIGDVTDRVMLTPVAINEGAAFVDTVFGNkPRKTDHTRVASAVFSIPPIGTCGLVEEDAakKFEKVAVY 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1746716866 415 VGKF-PFLANSRAKTNNETdgFVKVLADKATDRILGTHIVGPSAGELINEAVLAQEYGASSEDVARVCHAHPTCAEAL 491
Cdd:TIGR01423 392 ESSFtPLMHNISGSKYKKF--VAKIVTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAEEL 467
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
386-494 |
1.73e-51 |
|
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: 170.43 E-value: 1.73e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 386 VPSVIYTHPEVGWVGRSEEDLKSEGVDYKVGKFPFLANSRAKTNNETDGFVKVLADKATDRILGTHIVGPSAGELINEAV 465
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGEVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQEAA 80
|
90 100
....*....|....*....|....*....
gi 1746716866 466 LAQEYGASSEDVARVCHAHPTCAEALREA 494
Cdd:pfam02852 81 LAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
40-494 |
7.30e-49 |
|
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: 174.56 E-value: 7.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 40 DVVVIGSGPGGyvaAIKAAQLGLKTVCIEKNPTLGGTCLNVGCIPSKALLnnshyyhmaHSGDLAKRGIESDniRLNLDT 119
Cdd:TIGR03452 4 DLIIIGTGSGN---SIPDPRFADKRIAIVEKGTFGGTCLNVGCIPTKMFV---------YAAEVAQSIGESA--RLGIDA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 120 LMQ--------QKV--HAVTALTGGIAQLFKKNK---VDLIKGHGKITGVNQVtalkEDGSSEVVNTKNILIATGSEVTP 186
Cdd:TIGR03452 70 EIDsvrwpdivSRVfgDRIDPIAAGGEDYRRGDEtpnIDVYDGHARFVGPRTL----RTGDGEEITGDQIVIAAGSRPYI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 187 FPGIEIDEEQVVSSTGALSLKEVPKRLIVIGAGVIGVELGSVWSRLGSEVTAIEFLPSIGGVgIDQEVSKTLQKIlTKQG 266
Cdd:TIGR03452 146 PPAIADSGVRYHTNEDIMRLPELPESLVIVGGGYIAAEFAHVFSALGTRVTIVNRSTKLLRH-LDEDISDRFTEI-AKKK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 267 LNFKLGTKVTGATKSGGVVRVSVQDVKDssktdeLECEVLLVCVGRRPYTENLGLEEMGIERDQKGRVPVNSVFQTVIPN 346
Cdd:TIGR03452 224 WDIRLGRNVTAVEQDGDGVTLTLDDGST------VTADVLLVATGRVPNGDLLDAEAAGVEVDEDGRIKVDEYGRTSARG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 347 IYAIGDCIHGPMLAHKAEDEGIICIEGIL--GGPVHIDYNCVPSVIYTHPEVGWVGRSEEDLKSEGVDY--KVGKFPFLA 422
Cdd:TIGR03452 298 VWALGDVSSPYQLKHVANAEARVVKHNLLhpNDLRKMPHDFVPSAVFTHPQIATVGLTEQEAREAGHDItvKIQNYGDVA 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1746716866 423 NSRAKtnNETDGFVKVLADKATDRILGTHIVGPSAGELINEAVLAQEYGASSEDVARVCH-AHPTCAEALREA 494
Cdd:TIGR03452 378 YGWAM--EDTTGFCKLIADRDTGKLLGAHIIGPQASSLIQPLITAMAFGLDAREMARKQYwIHPALPEVVENA 448
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
38-489 |
9.77e-48 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 173.52 E-value: 9.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 38 DADVVVIGSGPGG---------YVAAIKAAQLGLKTVCIEKNPTLGGTCLNVGCIPSKALLNNSHYYHMAHSgdlaKRGI 108
Cdd:PLN02546 79 DFDLFTIGAGSGGvrasrfasnFGASAAVCELPFATISSDTLGGVGGTCVLRGCVPKKLLVYASKYSHEFEE----SRGF 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 109 ----ESDNiRLNLDTLMQQKVHAVTALTGGIAQLFKKNKVDLIKGHGKITGVNQVTAlkeDGssEVVNTKNILIATGSEv 184
Cdd:PLN02546 155 gwkyETEP-KHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDV---DG--KLYTARNILIAVGGR- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 185 tPF----PGIEideeQVVSSTGALSLKEVPKRLIVIGAGVIGVELGSVWSRLGSEVTAieFLPSIGGV-GIDQEVSKTLQ 259
Cdd:PLN02546 228 -PFipdiPGIE----HAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHV--FIRQKKVLrGFDEEVRDFVA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 260 KILTKQGLNFKLGTKVTGATKSGgvvrvsvqDVKDSSKTDELECE---VLLVCVGRRPYTENLGLEEMGIERDQKGRVPV 336
Cdd:PLN02546 301 EQMSLRGIEFHTEESPQAIIKSA--------DGSLSLKTNKGTVEgfsHVMFATGRKPNTKNLGLEEVGVKMDKNGAIEV 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 337 NSVFQTVIPNIYAIGDCIHGPMLAHKAEDEGIICIEGILGG-PVHIDYNCVPSVIYTHPEVGWVGRSEEDLKSEGVDYKV 415
Cdd:PLN02546 373 DEYSRTSVPSIWAVGDVTDRINLTPVALMEGGALAKTLFGNePTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYGDVDV 452
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1746716866 416 gkfpFLANSR---AKTNNETDG-FVKVLADKATDRILGTHIVGPSAGELINEAVLAQEYGASSEDVARVCHAHPTCAE 489
Cdd:PLN02546 453 ----FTANFRplkATLSGLPDRvFMKLIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAE 526
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
38-489 |
1.32e-47 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 173.26 E-value: 1.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 38 DADVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNpTLGGTCLNVGCIPSKALLNNSHYYHMAHsgDLAKRGIESDNIrLNL 117
Cdd:PTZ00058 48 VYDLIVIGGGSGGMAAARRAARNKAKVALVEKD-YLGGTCVNVGCVPKKIMFNAASIHDILE--NSRHYGFDTQFS-FNL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 118 DTLMQQKVHAVTALTGGIAQLFKKNKVDLIKGHGKITGVNQVTALK------------------------EDGSSEVVNT 173
Cdd:PTZ00058 124 PLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLIKKvsqvdgeadesdddevtivsagvsQLDDGQVIEG 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 174 KNILIATGSEvTPFPGIEiDEEQVVSSTGALSLKEvPKRLIVIGAGVIGVELGSVWSRLGSEvTAIEFLPSIGGVGIDQE 253
Cdd:PTZ00058 204 KNILIAVGNK-PIFPDVK-GKEFTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAE-SYIFARGNRLLRKFDET 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 254 VSKTLQKILTKQGLNFKLGTKVTGATK--SGGVVRVsvqdVKDSSKTDELECevLLVCVGRRPYTENLGLEEMGIeRDQK 331
Cdd:PTZ00058 280 IINELENDMKKNNINIITHANVEEIEKvkEKNLTIY----LSDGRKYEHFDY--VIYCVGRSPNTEDLNLKALNI-KTPK 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 332 GRVPVNSVFQTVIPNIYAIGDCI---------HGPMLAHKAEDEGIICIEGILGG--------PVHI------------- 381
Cdd:PTZ00058 353 GYIKVDDNQRTSVKHIYAVGDCCmvkknqeieDLNLLKLYNEEPYLKKKENTSGEsyynvqltPVAInagrlladrlfgp 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 382 -----DYNCVPSVIYTHPEVGWVGRSE---------EDLK---SEGVDYKVGKFPFLANSRAKTnnetdgFVKVLADKAT 444
Cdd:PTZ00058 433 fsrttNYKLIPSVIFSHPPIGTIGLSEqeaidiygkENVKiyeSRFTNLFFSVYDMDPAQKEKT------YLKLVCVGKE 506
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1746716866 445 DRILGTHIVGPSAGELINEAVLAQEYGASSEDVARVCHAHPTCAE 489
Cdd:PTZ00058 507 ELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIHPTAAE 551
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
38-501 |
8.89e-45 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 164.23 E-value: 8.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 38 DADVVVIGSGPGGYVAAIKAAQLGLKTVCIE--KNPT------LGGTCLNVGCIPSKALlnnsHYyhMAHSGDLAKR--- 106
Cdd:PTZ00052 5 MYDLVVIGGGSGGMAAAKEAAAHGKKVALFDyvKPSTqgtkwgLGGTCVNVGCVPKKLM----HY--AANIGSIFHHdsq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 107 --GIESDNIRL--NLDTLMQQKVHAV--TALTGgiaqlFKKNKVDLIKGHGKITGVNQVtALKEDGSSEVVNTKNILIAT 180
Cdd:PTZ00052 79 myGWKTSSSFNwgKLVTTVQNHIRSLnfSYRTG-----LRSSKVEYINGLAKLKDEHTV-SYGDNSQEETITAKYILIAT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 181 GSEVTPFPGIEIDEEQVVSSTGALSLKEVPKRLIVIGAGVIGVELGSVWSRLGSEVTAIefLPSIGGVGIDQEVSKTLQK 260
Cdd:PTZ00052 153 GGRPSIPEDVPGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVA--VRSIPLRGFDRQCSEKVVE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 261 ILTKQGLNFKLGTKVTGATKSGGVVRVSVQDvkdssKTDELeCEVLLVCVGRRPYTENLGLEEMGIERDQKGRVPVNSvF 340
Cdd:PTZ00052 231 YMKEQGTLFLEGVVPINIEKMDDKIKVLFSD-----GTTEL-FDTVLYATGRKPDIKGLNLNAIGVHVNKSNKIIAPN-D 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 341 QTVIPNIYAIGDCIHG-PMLAHKAEDEGIICIEGILGGPVHI-DYNCVPSVIYTHPEVGWVGRSEE----DLKSEGVDYK 414
Cdd:PTZ00052 304 CTNIPNIFAVGDVVEGrPELTPVAIKAGILLARRLFKQSNEFiDYTFIPTTIFTPIEYGACGYSSEaaiaKYGEDDIEEY 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 415 VGKFPFL---ANSRAK----TNNETD------GFVKVLADKATD-RILGTHIVGPSAGELINEAVLAQEYGASSEDVARV 480
Cdd:PTZ00052 384 LQEFNTLeiaAVHREKheraRKDEYDfdvssnCLAKLVCVKSEDnKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSM 463
|
490 500
....*....|....*....|.
gi 1746716866 481 CHAHPTCAEALREANVSAAFG 501
Cdd:PTZ00052 464 IGIHPTDAEVFMNLSVTRRSG 484
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
139-390 |
1.24e-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: 118.38 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 139 FKKNKVDLIKGHgKITGV----NQVTAlkEDGssEVVNTKNILIATGSE--VTPFPGIeiDEEQVVSSTG---ALSLKEV 209
Cdd:COG0446 46 FERKGIDVRTGT-EVTAIdpeaKTVTL--RDG--ETLSYDKLVLATGARprPPPIPGL--DLPGVFTLRTlddADALREA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 210 -----PKRLIVIGAGVIGVELGSVWSRLGSEVTAIEFLPSIGGVgIDQEVSKTLQKILTKQGLNFKLGTKVTGATKSGGV 284
Cdd:COG0446 119 lkefkGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGV-LDPEMAALLEEELREHGVELRLGETVVAIDGDDKV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 285 vRVSVQDvkdsskTDELECEVLLVCVGRRPYTEnLgLEEMGIERDQKGRVPVNSVFQTVIPNIYAIGDC--IHGP----- 357
Cdd:COG0446 198 -AVTLTD------GEEIPADLVVVAPGVRPNTE-L-AKDAGLALGERGWIKVDETLQTSDPDVYAAGDCaeVPHPvtgkt 268
|
250 260 270
....*....|....*....|....*....|....*.
gi 1746716866 358 ---MLAHKAEDEGIICIEGILGGPvhIDYNCVPSVI 390
Cdd:COG0446 269 vyiPLASAANKQGRVAAENILGGP--APFPGLGTFI 302
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
136-379 |
7.47e-28 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 114.85 E-value: 7.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 136 AQLFKKNKVDLIKGHgKITGVN----QVTAlkEDGssEVVNTKNILIATGSE--VTPFPGIEIDEEQVVSS-TGALSLKE 208
Cdd:COG1251 63 ADFYEENGIDLRLGT-RVTAIDraarTVTL--ADG--ETLPYDKLVLATGSRprVPPIPGADLPGVFTLRTlDDADALRA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 209 V---PKRLIVIGAGVIGVELGSVWSRLGSEVTAIEFLPSIGGVGIDQEVSKTLQKILTKQGLNFKLGTKVTGATKSGGVV 285
Cdd:COG1251 138 AlapGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 286 RVSVQDvkdsskTDELECEVLLVCVGRRPYTEnLgLEEMGIERDqkGRVPVNSVFQTVIPNIYAIGDC--IHGPMLAHK- 362
Cdd:COG1251 218 GVRLAD------GEELPADLVVVAIGVRPNTE-L-ARAAGLAVD--RGIVVDDYLRTSDPDIYAAGDCaeHPGPVYGRRv 287
|
250 260
....*....|....*....|...
gi 1746716866 363 ------AEDEGIICIEGILGGPV 379
Cdd:COG1251 288 lelvapAYEQARVAAANLAGGPA 310
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
40-358 |
7.94e-28 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 112.91 E-value: 7.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 40 DVVVIGSGPGGYVAAIKAAQLGLKTVCIEKnPTLGGTCLNVGCIpskallNNshY--YHMAHSG-DLAKRGIEsdnirln 116
Cdd:COG0492 2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEG-GEPGGQLATTKEI------EN--YpgFPEGISGpELAERLRE------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 117 ldtlmqqkvHAvtaltggiaqlfKKNKVDLIKGHgkitgvnqVTALKEDGSSEVVNTKN--------ILIATGSEVT--P 186
Cdd:COG0492 66 ---------QA------------ERFGAEILLEE--------VTSVDKDDGPFRVTTDDgteyeakaVIIATGAGPRklG 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 187 FPGIEIDEEQVVSSTGALSLKEVP-KRLIVIGAGVIGVELGSVWSRLGSEVTAI----EFLPSiggvgidqevSKTLQKI 261
Cdd:COG0492 117 LPGEEEFEGRGVSYCATCDGFFFRgKDVVVVGGGDSALEEALYLTKFASKVTLIhrrdELRAS----------KILVERL 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 262 LTKQGLNFKLGTKVTGATKSGGVVRVSVQDVKDSSKTdELECEVLLVCVGRRPYTEnlGLEEMGIERDQKGRVPVNSVFQ 341
Cdd:COG0492 187 RANPKIEVLWNTEVTEIEGDGRVEGVTLKNVKTGEEK-ELEVDGVFVAIGLKPNTE--LLKGLGLELDEDGYIVVDEDME 263
|
330
....*....|....*..
gi 1746716866 342 TVIPNIYAIGDCIHGPM 358
Cdd:COG0492 264 TSVPGVFAAGDVRDYKY 280
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
139-454 |
5.54e-20 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 92.41 E-value: 5.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 139 FKKNKVDLIKGHG--KITGVNQVTALKEDGSSEVVNTK--NILIATG--SEVTPFPGIEIDEEQVVSS-TGALSLKEV-- 209
Cdd:PRK09564 66 FIKSGIDVKTEHEvvKVDAKNKTITVKNLKTGSIFNDTydKLMIATGarPIIPPIKNINLENVYTLKSmEDGLALKELlk 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 210 ---PKRLIVIGAGVIGVELGSVWSRLGSEVTAIEFLPSIGGVGIDQEVSKTLQKILTKQGLNFKLGTKVTGATKSGGVVR 286
Cdd:PRK09564 146 deeIKNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 287 VsvqdvkdssKTD--ELECEVLLVCVGRRPYTEnlGLEEMGIERDQKGRVPVNSVFQTVIPNIYAIGDC--IHGPM---- 358
Cdd:PRK09564 226 V---------VTDkgEYEADVVIVATGVKPNTE--FLEDTGLKTLKNGAIIVDEYGETSIENIYAAGDCatIYNIVsnkn 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 359 ----LAHKAEDEGIICIEGILGGPVH----IDYNCVPSVIYthpEVGWVGRSEEDLKSEGVDYKVgKFPFLANSRAKTNN 430
Cdd:PRK09564 295 vyvpLATTANKLGRMVGENLAGRHVSfkgtLGSACIKVLDL---EAARTGLTEEEAKKLGIDYKT-VFIKDKNHTNYYPG 370
|
330 340
....*....|....*....|....
gi 1746716866 431 ETDGFVKVLADKATDRILGTHIVG 454
Cdd:PRK09564 371 QEDLYVKLIYEADTKVILGGQIIG 394
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
212-291 |
4.41e-18 |
|
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: 78.79 E-value: 4.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 212 RLIVIGAGVIGVELGSVWSRLGSEVTAIEFLPSIGGvGIDQEVSKTLQKILTKQGLNFKLGTKVTGATKSGGVVRVSVQD 291
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLP-GFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLTD 79
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
178-360 |
4.78e-18 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 85.74 E-value: 4.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 178 IATGSE--VTPFPGieidEEQVVSSTgalSLKEV---------PKRLIVIGAGVIGVELGSVWSRLGSEVTAIE----FL 242
Cdd:PRK04965 105 LATGASafVPPIPG----RELMLTLN---SQQEYraaetqlrdAQRVLVVGGGLIGTELAMDLCRAGKAVTLVDnaasLL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 243 PSIggvgIDQEVSKTLQKILTKQGLNFKLGTKVTGATKSGGVVRVSVQDVKdssktdELECEVLLVCVGRRPyteNLGL- 321
Cdd:PRK04965 178 ASL----MPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRATLDSGR------SIEVDAVIAAAGLRP---NTALa 244
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1746716866 322 EEMGIERdQKGRVpVNSVFQTVIPNIYAIGDC--IHGPMLA 360
Cdd:PRK04965 245 RRAGLAV-NRGIV-VDSYLQTSAPDIYALGDCaeINGQVLP 283
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
39-355 |
2.78e-17 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 83.64 E-value: 2.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 39 ADVVVIGSGPGGYVAAIKAAQLGLKTVCIeknpTLggtclnvgcIpSKallNNSHYY-HMAHsgDLAKRGIESDNIRLNL 117
Cdd:COG1252 2 KRIVIVGGGFAGLEAARRLRKKLGGDAEV----TL---------I-DP---NPYHLFqPLLP--EVAAGTLSPDDIAIPL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 118 dtlmqqkvhavtaltggiAQLFKKNKVDLIkgHGKITGV----NQVTAlkEDGSS----EVVntknilIATGSeVTPFPG 189
Cdd:COG1252 63 ------------------RELLRRAGVRFI--QGEVTGIdpeaRTVTL--ADGRTlsydYLV------IATGS-VTNFFG 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 190 IEIDEEqvvsstGALSLKEV---------------------PKRLIVIGAGVIGVEL-GSVWSRLGS------------E 235
Cdd:COG1252 114 IPGLAE------HALPLKTLedalalrerllaaferaerrrLLTIVVVGGGPTGVELaGELAELLRKllrypgidpdkvR 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 236 VTAIEFLPSIGGvGIDQEVSKTLQKILTKQGLNFKLGTKVTGATKsGGVVrvsvqdvkdSSKTDELECEVLLVCVGRRPY 315
Cdd:COG1252 188 ITLVEAGPRILP-GLGEKLSEAAEKELEKRGVEVHTGTRVTEVDA-DGVT---------LEDGEEIPADTVIWAAGVKAP 256
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1746716866 316 TEnlgLEEMGIERDQKGRVPVNSVFQTV-IPNIYAIGDCIH 355
Cdd:COG1252 257 PL---LADLGLPTDRRGRVLVDPTLQVPgHPNVFAIGDCAA 294
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
176-456 |
1.48e-14 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 76.41 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 176 ILIATGSE--VTPFPGIE---------IDEEQVVSSTGALSLKEVpkrliVIGAGVIGVELGSVWSRLGSEVTAIEFLPS 244
Cdd:TIGR02374 100 LILATGSYpfILPIPGADkkgvyvfrtIEDLDAIMAMAQRFKKAA-----VIGGGLLGLEAAVGLQNLGMDVSVIHHAPG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 245 IGGVGIDQEVSKTLQKILTKQGLNFKLGTKVTGATKSGGVVRVSVQDvkdsskTDELECEVLLVCVGRRPYTEnLGLEEm 324
Cdd:TIGR02374 175 LMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVGATKADRIRFKD------GSSLEADLIVMAAGIRPNDE-LAVSA- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 325 GIerDQKGRVPVNSVFQTVIPNIYAIGDC------IHGpmLAHKAEDEGIICIEGILGGPVHIDYNCVPSViythpevgw 398
Cdd:TIGR02374 247 GI--KVNRGIIVNDSMQTSDPDIYAVGECaehngrVYG--LVAPLYEQAKVLADHICGVECEEYEGSDLSA--------- 313
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1746716866 399 vgrseeDLKSEGVD-YKVGKFPFLANSRA-KTNNETDGFVK--VLADkatDRILGTHIVGPS 456
Cdd:TIGR02374 314 ------KLKLLGVDvWSAGDAQETERTTSiKIYDEQKGIYKklVLSD---DKLLGAVLFGDT 366
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
38-181 |
1.20e-11 |
|
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: 66.40 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 38 DADVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNPTLGGT------CLNVGCIP-SKALLNNS---HYYHMAHSGD----- 102
Cdd:COG1053 3 EYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGGHtaaaqgGINAAGTNvQKAAGEDSpeeHFYDTVKGGDgladq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 103 ----------------LAKRGIESDniRLNLDTLMQQKVHAV-----TALTGG---IAQLFKKNK------------VDL 146
Cdd:COG1053 83 dlvealaeeapeaidwLEAQGVPFS--RTPDGRLPQFGGHSVgrtcyAGDGTGhalLATLYQAALrlgveiftetevLDL 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1746716866 147 IKGHGKITGvnqVTALKEDGSSEVVNTKNILIATG 181
Cdd:COG1053 161 IVDDGRVVG---VVARDRTGEIVRIRAKAVVLATG 192
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
211-354 |
2.06e-11 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 65.96 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 211 KRLIVIGAGVIGVE-LGSVWSRlGSEVTAIEFLPSIGGVgIDQEVSKTLQKILTKQGLNFKLGTKVtgatksggvVRVSV 289
Cdd:PRK13512 149 DKALVVGAGYISLEvLENLYER-GLHPTLIHRSDKINKL-MDADMNQPILDELDKREIPYRLNEEI---------DAING 217
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1746716866 290 QDVK-DSSKTDELEceVLLVCVGRRPYTENLglEEMGIERDQKGRVPVNSVFQTVIPNIYAIGDCI 354
Cdd:PRK13512 218 NEVTfKSGKVEHYD--MIIEGVGTHPNSKFI--ESSNIKLDDKGFIPVNDKFETNVPNIYAIGDII 279
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
40-76 |
5.33e-10 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 61.47 E-value: 5.33e-10
10 20 30
....*....|....*....|....*....|....*..
gi 1746716866 40 DVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNPTLGGT 76
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGM 37
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
138-353 |
5.97e-10 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 62.06 E-value: 5.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 138 LFKKNKVDLIKGHGKITgVNQVTALKEDGSSEVVNTKNILIATGSE--VTPFPGIE---------IDEEQVVSSTGALSl 206
Cdd:PRK14989 68 FYEKHGIKVLVGERAIT-INRQEKVIHSSAGRTVFYDKLIMATGSYpwIPPIKGSEtqdcfvyrtIEDLNAIEACARRS- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 207 kevpKRLIVIGAGVIGVELGSVWSRLGSEVTAIEFLPSIGGVGIDQEVSKTLQKILTKQGLNFKLGTKVTGATKSGGVVR 286
Cdd:PRK14989 146 ----KRGAVVGGGLLGLEAAGALKNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSKNTLEIVQEGVEAR 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1746716866 287 VSVQDVKDSsktdELECEVLLVCVGRRPyTENLGlEEMGIERDQKGRVPVNSVFQTVIPNIYAIGDC 353
Cdd:PRK14989 222 KTMRFADGS----ELEVDFIVFSTGIRP-QDKLA-TQCGLAVAPRGGIVINDSCQTSDPDIYAIGEC 282
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
38-76 |
3.57e-08 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 55.88 E-value: 3.57e-08
10 20 30
....*....|....*....|....*....|....*....
gi 1746716866 38 DADVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNPTLGGT 76
Cdd:PRK06134 12 ECDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGGT 50
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
41-374 |
4.27e-08 |
|
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: 55.53 E-value: 4.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 41 VVVIGSGPGGYVAAIKAAQLGLKTVCIEKNPTLGGTcLNVGcIPS----KALLNNSHYYhmahsgdLAKRGIEsdnIRLN 116
Cdd:COG0493 124 VAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGGL-LRYG-IPEfrlpKDVLDREIEL-------IEALGVE---FRTN 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 117 ldtlmqqkVHAVTALTggIAQLFKKNKvdlikghgkitgvnqvtAlkedgssevvntknILIATGSEVTPFPGIE-IDEE 195
Cdd:COG0493 192 --------VEVGKDIT--LDELLEEFD-----------------A--------------VFLATGAGKPRDLGIPgEDLK 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 196 QVVS----------STGALSLKEVPKRLIVIGAG-----VIGVELgsvwsRLGSE-VT---------------------- 237
Cdd:COG0493 231 GVHSamdfltavnlGEAPDTILAVGKRVVVIGGGntamdCARTAL-----RLGAEsVTivyrrtreempaskeeveeale 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 238 -AIEFLPSIGGVGIDQEVSKTLQKILTKQglnfklgTKVTGATKSGgvvRVSVQDVKDSSKTdeLECEVLLVCVGRRPYT 316
Cdd:COG0493 306 eGVEFLFLVAPVEIIGDENGRVTGLECVR-------MELGEPDESG---RRRPVPIEGSEFT--LPADLVILAIGQTPDP 373
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1746716866 317 ENLgLEEMGIERDQKGRVPVNSV-FQTVIPNIYAIGDCIHGPMLAHKAEDEGIICIEGI 374
Cdd:COG0493 374 SGL-EEELGLELDKRGTIVVDEEtYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAI 431
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
40-76 |
4.38e-08 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 55.81 E-value: 4.38e-08
10 20 30
....*....|....*....|....*....|....*..
gi 1746716866 40 DVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNPTLGGT 76
Cdd:PRK07843 9 DVVVVGSGAAGMVAALTAAHRGLSTVVVEKAPHYGGS 45
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
40-75 |
4.82e-08 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 55.24 E-value: 4.82e-08
10 20 30
....*....|....*....|....*....|....*.
gi 1746716866 40 DVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNPTLGG 75
Cdd:COG1233 5 DVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
40-236 |
5.92e-08 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 54.86 E-value: 5.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 40 DVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNptlGGTCLNVGCIPSKALLNNSHYYH-MAHSGDLAKRGIesDNIRLNLD 118
Cdd:pfam01134 1 DVIVIGGGHAGCEAALAAARMGAKVLLITHN---TDTIAELSCNPSIGGIAKGHLVReIDALGGLMGKAA--DKTGIQFR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 119 TLMQQKVHAVTALTggiAQ----LFKKNKVDLIKGH-----------------GKITGVnqvtaLKEDGssEVVNTKNIL 177
Cdd:pfam01134 76 MLNTSKGPAVRALR---AQvdrdLYSKEMTETLENHpnltliqgevtdlipenGKVKGV-----VTEDG--EEYKAKAVV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1746716866 178 IATGsevtPFPGIEIDEEQVVSSTG----------ALSLKEVPKRLIVIGAGV------IGVELGSVWSRLGSEV 236
Cdd:pfam01134 146 LATG----TFLNGKIHIGLKCYPAGrlgeltseglSESLKELGFELGRFKTGTppridkDSIDFSKLEEQPGDKP 216
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
40-76 |
1.14e-07 |
|
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: 53.83 E-value: 1.14e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1746716866 40 DVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNPTLGGT 76
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGA 37
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
300-367 |
1.83e-07 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 53.07 E-value: 1.83e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1746716866 300 ELECEVLLVCVGRRPyTENLGLEEMGIERDQKGRVPVNSVFQTVIPNIYAIGDCIHGPMLAHKAEDEG 367
Cdd:PRK12770 272 VLEADTVVFAIGEIP-TPPFAKECLGIELNRKGEIVVDEKHMTSREGVFAAGDVVTGPSKIGKAIKSG 338
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
40-76 |
2.53e-07 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 53.16 E-value: 2.53e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1746716866 40 DVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNPTLGGT 76
Cdd:PRK12842 11 DVLVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGGT 47
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
136-354 |
8.93e-07 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 51.08 E-value: 8.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 136 AQLFKKNKVDLIKGHG-KITGVNQVTALKEDGSSevVNTKNILIATGSEVTPFPGIEIDEEQVVS---STGALSLKEV-- 209
Cdd:PRK09754 65 ANWWQENNVHLHSGVTiKTLGRDTRELVLTNGES--WHWDQLFIATGAAARPLPLLDALGERCFTlrhAGDAARLREVlq 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 210 -PKRLIVIGAGVIGVELGSVWSRLGSEVTAIEFLPSIGGVGIDQEVSKTLQKILTKQGLNFKLGTKVTGATKSGGVVRVs 288
Cdd:PRK09754 143 pERSVVIVGAGTIGLELAASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVELT- 221
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 289 vqdvkdSSKTDELECEVLLVCVG---RRPYTENLGLeemgierDQKGRVPVNSVFQTVIPNIYAIGD-CI 354
Cdd:PRK09754 222 ------LQSGETLQADVVIYGIGisaNDQLAREANL-------DTANGIVIDEACRTCDPAIFAGGDvAI 278
|
|
| PRK12835 |
PRK12835 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
40-83 |
9.80e-07 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237221 [Multi-domain] Cd Length: 584 Bit Score: 51.35 E-value: 9.80e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1746716866 40 DVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNPTLGG-TCLNVGCI 83
Cdd:PRK12835 13 DVLVVGSGGGGMTAALTAAARGLDTLVVEKSAHFGGsTALSGGGI 57
|
|
| PRK12844 |
PRK12844 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
39-76 |
1.30e-06 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 183787 [Multi-domain] Cd Length: 557 Bit Score: 50.91 E-value: 1.30e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1746716866 39 ADVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNPTLGGT 76
Cdd:PRK12844 7 YDVVVVGSGGGGMCAALAAADSGLEPLIVEKQDKVGGS 44
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
38-374 |
2.33e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 50.15 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 38 DADVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNPTLGGTcLNVGcIPSKALLnnshyyhmahsgdlakrgiesdnirlnl 117
Cdd:PRK13984 283 NKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGV-MRYG-IPSYRLP---------------------------- 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 118 DTLMQQKVHAVTALtggiaqlfkknkvdlikghgkitGVNQVTALK--EDGSSEVVNTKN--ILIATG---SEVTPFPGI 190
Cdd:PRK13984 333 DEALDKDIAFIEAL-----------------------GVKIHLNTRvgKDIPLEELREKHdaVFLSTGftlGRSTRIPGT 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 191 eiDEEQVVSSTGALSL-----------KEVPKRLIVIGAGVIGVELGSVWSRLGS--------EVTAIEflpsiggvGID 251
Cdd:PRK13984 390 --DHPDVIQALPLLREirdylrgegpkPKIPRSLVVIGGGNVAMDIARSMARLQKmeygevnvKVTSLE--------RTF 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 252 QEVSKTLQKIL--TKQGLNFKLG---TKV---TGATKsgGVVRVSVQDVKDSS-----KTDE-----LECEVLLVCVGRR 313
Cdd:PRK13984 460 EEMPADMEEIEegLEEGVVIYPGwgpMEVvieNDKVK--GVKFKKCVEVFDEEgrfnpKFDEsdqiiVEADMVVEAIGQA 537
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1746716866 314 PYTENLGLE---EMGIERdqkGRVPVNSVFQTVIPNIYAIGDCIHGPMLAHKAEDeGIICIEGI 374
Cdd:PRK13984 538 PDYSYLPEElksKLEFVR---GRILTNEYGQTSIPWLFAGGDIVHGPDIIHGVAD-GYWAAEGI 597
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
40-94 |
5.44e-06 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 48.73 E-value: 5.44e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1746716866 40 DVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNPTLG--------GTClNV--GCIPSKALLnnSHY 94
Cdd:pfam03486 2 DVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLGrkilisggGRC-NVtnLSEEPDNFL--SRY 63
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
151-367 |
6.04e-06 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 48.61 E-value: 6.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 151 GKITGVN----QVTALKEDGS-SEVVNTKNI-----LIATGSEVTPF--PGI--------EIDE-----EQVVSSTGALS 205
Cdd:PTZ00318 82 AVVYDVDfeekRVKCGVVSKSnNANVNTFSVpydklVVAHGARPNTFniPGVeerafflkEVNHargirKRIVQCIERAS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 206 LK----EVPKRL---IVIGAGVIGVELGSVWSRLGSE--------------VTAIEFLPSIGGVgIDQEVSKTLQKILTK 264
Cdd:PTZ00318 162 LPttsvEERKRLlhfVVVGGGPTGVEFAAELADFFRDdvrnlnpelveeckVTVLEAGSEVLGS-FDQALRKYGQRRLRR 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 265 QGLNFKLGTKVTGA------TKSGGVVRVSvqdvkdssktdelecevLLVC---VGRRPYTENLGleemgIERDQKGRVP 335
Cdd:PTZ00318 241 LGVDIRTKTAVKEVldkevvLKDGEVIPTG-----------------LVVWstgVGPGPLTKQLK-----VDKTSRGRIS 298
|
250 260 270
....*....|....*....|....*....|....*...
gi 1746716866 336 VNSVFQTV-IPNIYAIGDCIHG-----PMLAHKAEDEG 367
Cdd:PTZ00318 299 VDDHLRVKpIPNVFALGDCAANeerplPTLAQVASQQG 336
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
259-375 |
7.12e-06 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 48.62 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1746716866 259 QKILTKQGlnfklgtKVTGATksggVVRVSVQD-----VKDSSKtdELECEVLLVCVGRRPYTENLgLEEMGIERDQKGR 333
Cdd:PRK12810 353 KEFEGENG-------KVTGVK----VVRTELGEgdfepVEGSEF--VLPADLVLLAMGFTGPEAGL-LAQFGVELDERGR 418
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1746716866 334 VPVNSV-FQTVIPNIYAIGDCIHGPMLAHKAEDEGIICIEGIL 375
Cdd:PRK12810 419 VAAPDNaYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAID 461
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
38-75 |
8.79e-06 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 48.29 E-value: 8.79e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1746716866 38 DADVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNPTLGG 75
Cdd:PRK12839 8 TYDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKASTCGG 45
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
40-76 |
9.60e-06 |
|
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: 47.94 E-value: 9.60e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1746716866 40 DVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNPTLGGT 76
Cdd:COG2072 8 DVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGT 44
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
40-76 |
1.56e-05 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 47.42 E-value: 1.56e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1746716866 40 DVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNPTLGGT 76
Cdd:PRK12843 18 DVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGT 54
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
43-77 |
2.55e-05 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 42.13 E-value: 2.55e-05
10 20 30
....*....|....*....|....*....|....*
gi 1746716866 43 VIGSGPGGYVAAIKAAQLGLKTVCIEKNPTLGGTC 77
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNA 35
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
40-75 |
9.56e-05 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 44.85 E-value: 9.56e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1746716866 40 DVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNPTLGG 75
Cdd:COG1148 142 RALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGG 177
|
|
| mhpA |
PRK06183 |
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase; |
34-73 |
3.34e-04 |
|
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
Pssm-ID: 235727 [Multi-domain] Cd Length: 500 Bit Score: 42.97 E-value: 3.34e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1746716866 34 SSSNDADVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNPTL 73
Cdd:PRK06183 6 PDAHDTDVVIVGAGPVGLTLANLLGQYGVRVLVLERWPTL 45
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
38-83 |
7.60e-04 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 41.76 E-value: 7.60e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1746716866 38 DADVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNPtlGGTCLNVGCI 83
Cdd:PRK05329 2 KFDVLVIGGGLAGLTAALAAAEAGKRVALVAKGQ--GALHFSSGSI 45
|
|
| PRK06481 |
PRK06481 |
flavocytochrome c; |
40-78 |
9.83e-04 |
|
flavocytochrome c;
Pssm-ID: 180584 [Multi-domain] Cd Length: 506 Bit Score: 41.74 E-value: 9.83e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1746716866 40 DVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNPTLGGTCL 78
Cdd:PRK06481 63 DIVIVGAGGAGMSAAIEAKDAGMNPVILEKMPVAGGNTM 101
|
|
| GlpB |
COG3075 |
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism]; |
40-65 |
1.94e-03 |
|
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 442309 Cd Length: 415 Bit Score: 40.55 E-value: 1.94e-03
10 20
....*....|....*....|....*.
gi 1746716866 40 DVVVIGSGPGGYVAAIKAAQLGLKTV 65
Cdd:COG3075 4 DVVVIGGGLAGLTAAIRAAEAGLRVA 29
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
40-77 |
2.62e-03 |
|
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440845 [Multi-domain] Cd Length: 443 Bit Score: 40.20 E-value: 2.62e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1746716866 40 DVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNPTLGGTC 77
Cdd:COG1232 3 RVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLI 40
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
36-74 |
3.02e-03 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 39.92 E-value: 3.02e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1746716866 36 SNDADVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNPTLG 74
Cdd:COG0654 1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPR 39
|
|
| PRK12834 |
PRK12834 |
putative FAD-binding dehydrogenase; Reviewed |
36-75 |
3.68e-03 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 183782 [Multi-domain] Cd Length: 549 Bit Score: 39.88 E-value: 3.68e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1746716866 36 SNDADVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNP--TLGG 75
Cdd:PRK12834 2 AMDADVIVVGAGLAGLVAAAELADAGKRVLLLDQENeaNLGG 43
|
|
| PTZ00306 |
PTZ00306 |
NADH-dependent fumarate reductase; Provisional |
34-75 |
7.07e-03 |
|
NADH-dependent fumarate reductase; Provisional
Pssm-ID: 140327 [Multi-domain] Cd Length: 1167 Bit Score: 39.38 E-value: 7.07e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1746716866 34 SSSNDADVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNPTLGG 75
Cdd:PTZ00306 405 AGSLPARVIVVGGGLAGCSAAIEAASCGAQVILLEKEAKLGG 446
|
|
| COG3573 |
COG3573 |
Predicted oxidoreductase [General function prediction only]; |
35-75 |
7.25e-03 |
|
Predicted oxidoreductase [General function prediction only];
Pssm-ID: 442794 [Multi-domain] Cd Length: 551 Bit Score: 39.01 E-value: 7.25e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1746716866 35 SSNDADVVVIGSGPGGYVAAIKAAQLGLKTVCIEKNP--TLGG 75
Cdd:COG3573 2 AAMDADVIVVGAGLAGLVAAAELADAGRRVLLLDQEPeaNLGG 44
|
|
| |
