|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
1-471 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 547.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 1 MTISCDVAILGGGTGGYVAAIRAAQLGKSVVVIEMDKLGGTCLHRGCIPSKSLLRSAEVYAEIQESESYGIETTGVQLVF 80
Cdd:PRK06416 1 FAFEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIKAENVGIDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 81 PKVQLRKEAVVEQLHQGVQFLMRKNKIQVVKGKGRIIGPsifsprsGAVAVELEDGDmETVVSTHLIVATGSRPRVLPGL 160
Cdd:PRK06416 81 KKVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDP-------NTVRVMTEDGE-QTYTAKNIILATGSRPRELPGI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 161 EPDGKVILSSEEALTLEALPSSIIIVGGGVIGVEWASMLADFGVQVTVVEAAGQLLPLEDEEIARELQRLLKKRGVKVLT 240
Cdd:PRK06416 153 EIDGRVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPGEDKEISKLAERALKKRGIKIKT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 241 GTTV-DAETcviTESGLTIEARKGEQSQSLSAEKLLVSVGRVANVENIGLENTDIHFAKGVIEVNDNMQTAEPHIYAIGD 319
Cdd:PRK06416 233 GAKAkKVEQ---TDDGVTVTLEDGGKEETLEADYVLVAVGRRPNTENLGLEELGVKTDRGFIEVDEQLRTNVPNIYAIGD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 320 CIGGLQLAHAASHEGIRAVNHLAGEAlHPYHPHLVPRCVYTRPEVASVGYTEKEAKALGTDVVTGKFPFSAIGKAIVYGM 399
Cdd:PRK06416 310 IVGGPMLAHKASAEGIIAAEAIAGNP-HPIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFDVKVVKFPFAGNGKALALGE 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518751641 400 KDGFVKVVADRTSGDILGVQMIGPHVTDLIGEAALAQLLDATPWEVGEAIHAHPTLSEVIGEAMLAVDGRAI 471
Cdd:PRK06416 389 TDGFVKLIFDKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEALGEAALAAAGKPL 460
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
2-469 |
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: 542.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 2 TISCDVAILGGGTGGYVAAIRAAQLGKSVVVIEMDKLGGTCLHRGCIPSKSLLRSAEVYAEIQESESYGIETTGVQLVFP 81
Cdd:COG1249 1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISAGAPSVDWA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 82 KVQLRKEAVVEQLHQGVQFLMRKNKIQVVKGKGRIIGPSifsprsgavAVELEDGdmETVVSTHLIVATGSRPRVLPGLE 161
Cdd:COG1249 81 ALMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPH---------TVEVTGG--ETLTADHIVIATGSRPRVPPIPG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 162 PDGKVILSSEEALTLEALPSSiiivgggvigvEWASMLADFGVQVTVVEAAGQLLPLEDEEIARELQRLLKKRGVKVLTG 241
Cdd:COG1249 150 LDEVRVLTSDEALELEELPKSlvvigggyiglEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 242 TTVdaETCVITESGLTIEARKGEQSQSLSAEKLLVSVGRVANVENIGLENTDIHF-AKGVIEVNDNMQTAEPHIYAIGDC 320
Cdd:COG1249 230 AKV--TSVEKTGDGVTVTLEDGGGEEAVEADKVLVATGRRPNTDGLGLEAAGVELdERGGIKVDEYLRTSVPGIYAIGDV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 321 IGGLQLAHAASHEGIRAVNHLAGEALHPYHPHLVPRCVYTRPEVASVGYTEKEAKALGTDVVTGKFPFSAIGKAIVYGMK 400
Cdd:COG1249 308 TGGPQLAHVASAEGRVAAENILGKKPRPVDYRAIPSVVFTDPEIASVGLTEEEAREAGIDVKVGKFPFAANGRALALGET 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518751641 401 DGFVKVVADRTSGDILGVQMIGPHVTDLIGEAALAQLLDATPWEVGEAIHAHPTLSEVIGEAMLAVDGR 469
Cdd:COG1249 388 EGFVKLIADAETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAALALLGR 456
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
6-471 |
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: 542.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 6 DVAILGGGTGGYVAAIRAAQLGKSVVVIEMDKLGGTCLHRGCIPSKSLLRSAEVYAEIQESESYGIETTGVQLVFPKVQL 85
Cdd:TIGR01350 3 DVIVIGGGPGGYVAAIRAAQLGLKVALVEKEYLGGTCLNVGCIPTKALLHSAEVYDEIKHAKDLGIEVENVSVDWEKMQK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 86 RKEAVVEQLHQGVQFLMRKNKIQVVKGKGRIIGPsifsprsGAVAVELEDGDmETVVSTHLIVATGSRPRVLPG-LEPDG 164
Cdd:TIGR01350 83 RKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDP-------GTVSVTGENGE-ETLEAKNIIIATGSRPRSLPGpFDFDG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 165 KVILSSEEALTLEALPSSIIIVGGGVIGVEWASMLADFGVQVTVVEAAGQLLPLEDEEIARELQRLLKKRGVKVLTGTTV 244
Cdd:TIGR01350 155 KVVITSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 245 daETCVITESGLTIEARKGEQsQSLSAEKLLVSVGRVANVENIGLENTDIHFAK-GVIEVNDNMQTAEPHIYAIGDCIGG 323
Cdd:TIGR01350 235 --TAVEKNDDQVTYENKGGET-ETLTGEKVLVAVGRKPNTEGLGLEKLGVELDErGRIVVDEYMRTNVPGIYAIGDVIGG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 324 LQLAHAASHEGIRAVNHLAGEALHPYHPHLVPRCVYTRPEVASVGYTEKEAKALGTDVVTGKFPFSAIGKAIVYGMKDGF 403
Cdd:TIGR01350 312 PMLAHVASHEGIVAAENIAGKEPAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGYDVKIGKFPFAANGKALALGETDGF 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518751641 404 VKVVADRTSGDILGVQMIGPHVTDLIGEAALAQLLDATPWEVGEAIHAHPTLSEVIGEAMLAVDGRAI 471
Cdd:TIGR01350 392 VKIIADKKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEAIKEAALAALGKPI 459
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
6-473 |
1.70e-150 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 437.05 E-value: 1.70e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 6 DVAILGGGTGGYVAAIRAAQLGKSVVVIEMDK-------LGGTCLHRGCIPSKSLLRSAEVYAEIQES-ESYGIETTGVQ 77
Cdd:PRK06327 6 DVVVIGAGPGGYVAAIRAAQLGLKVACIEAWKnpkgkpaLGGTCLNVGCIPSKALLASSEEFENAGHHfADHGIHVDGVK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 78 LVFPKVQLRKEAVVEQLHQGVQFLMRKNKIQVVKGKGRIIGPSifsprSGAVAVELEDGDMETVVSTHLIVATGSRPRVL 157
Cdd:PRK06327 86 IDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVGKT-----DAGYEIKVTGEDETVITAKHVIIATGSEPRHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 158 PGLEPDGKVILSSEEALTLEALPSSIIIVGGGVIGVEWASMLADFGVQVTVVEAAGQLLPLEDEEIARELQRLLKKRGVK 237
Cdd:PRK06327 161 PGVPFDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAAADEQVAKEAAKAFTKQGLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 238 VLTGTTVDAETcvITESGLTI--EARKGEQsQSLSAEKLLVSVGRVANVENIGLENTDIHF-AKGVIEVNDNMQTAEPHI 314
Cdd:PRK06327 241 IHLGVKIGEIK--TGGKGVSVayTDADGEA-QTLEVDKLIVSIGRVPNTDGLGLEAVGLKLdERGFIPVDDHCRTNVPNV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 315 YAIGDCIGGLQLAHAASHEGIRAVNHLAGEALHPYHpHLVPRCVYTRPEVASVGYTEKEAKALGTDVVTGKFPFSAIGKA 394
Cdd:PRK06327 318 YAIGDVVRGPMLAHKAEEEGVAVAERIAGQKGHIDY-NTIPWVIYTSPEIAWVGKTEQQLKAEGVEYKAGKFPFMANGRA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518751641 395 IVYGMKDGFVKVVADRTSGDILGVQMIGPHVTDLIGEAALAQLLDATPWEVGEAIHAHPTLSEVIGEAMLAVDGRAIGF 473
Cdd:PRK06327 397 LAMGEPDGFVKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEVWHEAALAVDKRPLHF 475
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
6-471 |
1.32e-146 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 426.52 E-value: 1.32e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 6 DVAILGGGTGGYVAAIRAAQLGKSVVVIEMDKLGGTCLHRGCIPSKSLLRSAEVYAEIQESESYGIETTGVQLVFPKVQL 85
Cdd:PRK06292 5 DVIVIGAGPAGYVAARRAAKLGKKVALIEKGPLGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHADGPKIDFKKVMA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 86 RKEAVVEQLHQGV-QFLMRKNKIQVVKGKGRIIGPSIfsprsgavaVELEDgdmETVVSTHLIVATGSRPRVLPGLE-PD 163
Cdd:PRK06292 85 RVRRERDRFVGGVvEGLEKKPKIDKIKGTARFVDPNT---------VEVNG---ERIEAKNIVIATGSRVPPIPGVWlIL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 164 GKVILSSEEALTLEALPSSIIIVGGGVIGVEWASMLADFGVQVTVVEAAGQLLPLEDEEIARELQRLLKKRgVKVLTGTT 243
Cdd:PRK06292 153 GDRLLTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILSKE-FKIKLGAK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 244 VDAetcvITESG--LTIEARKGEQSQSLSAEKLLVSVGRVANVENIGLENTDIHF-AKGVIEVNDNMQTAEPHIYAIGDC 320
Cdd:PRK06292 232 VTS----VEKSGdeKVEELEKGGKTETIEADYVLVATGRRPNTDGLGLENTGIELdERGRPVVDEHTQTSVPGIYAAGDV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 321 IGGLQLAHAASHEGIRAVNHLAGEALHPYHPHLVPRCVYTRPEVASVGYTEKEAKALGTDVVTGKFPFSAIGKAIVYGMK 400
Cdd:PRK06292 308 NGKPPLLHEAADEGRIAAENAAGDVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEVPFEAQGRARVMGKN 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518751641 401 DGFVKVVADRTSGDILGVQMIGPHVTDLIGEAALAQLLDATPWEVGEAIHAHPTLSEVIGEAMLAVDGRAI 471
Cdd:PRK06292 388 DGFVKVYADKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRTALRDLFSKLI 458
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
6-459 |
1.08e-98 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 304.05 E-value: 1.08e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 6 DVAILGGGTGGYVAAIRAAQLGKSVVVIEMDKLGGTCLHRGCIPSKSLLRSAEVYAEIQESESYGIETTG-VQLVFPKVQ 84
Cdd:PRK06370 7 DAIVIGAGQAGPPLAARAAGLGMKVALIERGLLGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGGpVSVDFKAVM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 85 LRKEAVVEQLHQGVQFLMRK-NKIQVVKGKGRIIGPSifsprsgAVAVeledgDMETVVSTHLIVATGSRPRV--LPGLE 161
Cdd:PRK06370 87 ARKRRIRARSRHGSEQWLRGlEGVDVFRGHARFESPN-------TVRV-----GGETLRAKRIFINTGARAAIppIPGLD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 162 PDGkvILSSEEALTLEALPSSIIIVGGGVIGVEWASMLADFGVQVTVVEAAGQLLPLEDEEIARELQRLLKKRGVKVLTG 241
Cdd:PRK06370 155 EVG--YLTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILEREGIDVRLN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 242 TTVDAETcvITESGLTIEARKGEQSQSLSAEKLLVSVGRVANVENIGLENTDIHF-AKGVIEVNDNMQTAEPHIYAIGDC 320
Cdd:PRK06370 233 AECIRVE--RDGDGIAVGLDCNGGAPEITGSHILVAVGRVPNTDDLGLEAAGVETdARGYIKVDDQLRTTNPGIYAAGDC 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 321 IGGLQLAHAASHEGIRAVNHLAGEALHPYHPHLVPRCVYTRPEVASVGYTEKEAKALGTDVVTGKFPFSAIGKAIVYGMK 400
Cdd:PRK06370 311 NGRGAFTHTAYNDARIVAANLLDGGRRKVSDRIVPYATYTDPPLARVGMTEAEARKSGRRVLVGTRPMTRVGRAVEKGET 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 518751641 401 DGFVKVVADRTSGDILGVQMIGPHVTDLIGEAALAQLLDATPWEVGEAIHAHPTLSEVI 459
Cdd:PRK06370 391 QGFMKVVVDADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELI 449
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
6-465 |
3.98e-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: 290.09 E-value: 3.98e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 6 DVAILGGGTGGYVAAIRAAQLGKSVVVIEMDKLGGTCLHRGCIPSKSLLRSAEVYAEIQESeSYGIETTGVQLVFPKVQL 85
Cdd:TIGR02053 2 DLVIIGSGAAAFAAAIKAAELGASVAMVERGPLGGTCVNVGCVPSKMLLRAAEVAHYARKP-PFGGLAATVAVDFGELLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 86 RKEAVVEQL-HQGVQFLMRKNKIQVVKGKGRIIGPSIfsprsgavaVELEDGDmETVVSTHLIVATGSRPRV--LPGLEP 162
Cdd:TIGR02053 81 GKREVVEELrHEKYEDVLSSYGVDYLRGRARFKDPKT---------VKVDLGR-EVRGAKRFLIATGARPAIppIPGLKE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 163 DGkvILSSEEALTLEALPSSIIIVGGGVIGVEWASMLADFGVQVTVVEAAGQLLPLEDEEIARELQRLLKKRGVKVLTGT 242
Cdd:TIGR02053 151 AG--YLTSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSDRLLPREEPEISAAVEEALAEEGIEVVTSA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 243 TVDAETcvITESGLTIEARKGEQSQSLSAEKLLVSVGRVANVENIGLENTDIHF-AKGVIEVNDNMQTAEPHIYAIGDCI 321
Cdd:TIGR02053 229 QVKAVS--VRGGGKIITVEKPGGQGEVEADELLVATGRRPNTDGLGLEKAGVKLdERGGILVDETLRTSNPGIYAAGDVT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 322 GGLQLAHAASHEGIRAVNHLAGEALHPYHPHLVPRCVYTRPEVASVGYTEKEAKALGTDVVTGKFPFSAIGKAIVYGMKD 401
Cdd:TIGR02053 307 GGLQLEYVAAKEGVVAAENALGGANAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNVPRARINRDTR 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518751641 402 GFVKVVADRTSGDILGVQMIGPHVTDLIGEAALAQLLDATPWEVGEAIHAHPTLSEVIGEAMLA 465
Cdd:TIGR02053 387 GFIKLVAEPGTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGLKLAAQT 450
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
6-436 |
1.04e-89 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 280.89 E-value: 1.04e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 6 DVAILGGGTGGYVAAIRAAQLGKSVVVIEM-DKLGGTCLHRGCIPSKSL---------LRSAEVYAEIQESEsygiettg 75
Cdd:PRK05249 7 DLVVIGSGPAGEGAAMQAAKLGKRVAVIERyRNVGGGCTHTGTIPSKALreavlrligFNQNPLYSSYRVKL-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 76 vQLVFPKVQLRKEAVVEQLHQGVQ-FLMRkNKIQVVKGKGRIIGPSifsprsgAVAVELEDGDMETVVSTHLIVATGSRP 154
Cdd:PRK05249 79 -RITFADLLARADHVINKQVEVRRgQYER-NRVDLIQGRARFVDPH-------TVEVECPDGEVETLTADKIVIATGSRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 155 RVLPGLEPDGKVILSSEEALTLEALPSSIIIVGGGVIGVEWASMLADFGVQVTVVEAAGQLLPLEDEEIARELQRLLKKR 234
Cdd:PRK05249 150 YRPPDVDFDHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSFLDDEISDALSYHLRDS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 235 GVKVLTGTTVDA----ETCVIT--ESGLTIEarkgeqsqslsAEKLLVSVGRVANVENIGLENTDIHF-AKGVIEVNDNM 307
Cdd:PRK05249 230 GVTIRHNEEVEKveggDDGVIVhlKSGKKIK-----------ADCLLYANGRTGNTDGLNLENAGLEAdSRGQLKVNENY 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 308 QTAEPHIYAIGDCIGGLQLAHAASHEGIRAVNHLAGEALHPYHPhLVPRCVYTRPEVASVGYTEKEAKALGTDVVTGKFP 387
Cdd:PRK05249 299 QTAVPHIYAVGDVIGFPSLASASMDQGRIAAQHAVGEATAHLIE-DIPTGIYTIPEISSVGKTEQELTAAKVPYEVGRAR 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 518751641 388 FSAIGKAIVYGMKDGFVKVVADRTSGDILGVQMIGPHVTDL--IGEAALAQ 436
Cdd:PRK05249 378 FKELARAQIAGDNVGMLKILFHRETLEILGVHCFGERATEIihIGQAIMEQ 428
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
7-462 |
2.09e-71 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 233.60 E-value: 2.09e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 7 VAILGGGTGGYVAAIRAAQLGKSVVVIEMDKLGGTCLHRGCIPSKSLLRSAEVYAEIQESESYGIETTGVQLVfpKVQLr 86
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIERDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRFIDDGEA--RVDL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 87 keavvEQLHQGVQFL-----------MRKNKIQVVKGKGRIIGPSIFSPRsgaVAVELEDGDMETVVSTHLIVATGSRPR 155
Cdd:PRK07845 81 -----PAVNARVKALaaaqsadirarLEREGVRVIAGRGRLIDPGLGPHR---VKVTTADGGEETLDADVVLIATGASPR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 156 VLPGLEPDGKVILSSEEALTLEALPSSIIIVGGGVIGVEWASMLADFGVQVTVVEAAGQLLPLEDEEIARELQRLLKKRG 235
Cdd:PRK07845 153 ILPTAEPDGERILTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPGEDADAAEVLEEVFARRG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 236 VKVLTGTTvdAETCVITESGLTIEARKGeqsQSLSAEKLLVSVGRVANVENIGLENTDIHFAK-GVIEVNDNMQTAEPHI 314
Cdd:PRK07845 233 MTVLKRSR--AESVERTGDGVVVTLTDG---RTVEGSHALMAVGSVPNTAGLGLEEAGVELTPsGHITVDRVSRTSVPGI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 315 YAIGDCIGGLQLAHAASHEGIRAVNHLAGEALHPYHPHLVPRCVYTRPEVASVGYTEKEAKALGTDVVTGKFPFSAIGKA 394
Cdd:PRK07845 308 YAAGDCTGVLPLASVAAMQGRIAMYHALGEAVSPLRLKTVASNVFTRPEIATVGVSQAAIDSGEVPARTVMLPLATNPRA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518751641 395 IVYGMKDGFVKVVADRTSGDILGVQMIGPHVTDLIGEAALAQLLDATPWEVGEAIHAHPTLSEVIGEA 462
Cdd:PRK07845 388 KMSGLRDGFVKLFCRPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYPSLSGSITEA 455
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
6-468 |
4.68e-68 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 229.80 E-value: 4.68e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 6 DVAILGGGTGGYVAAIRAAQLGKSVVVIEMDK--LGGTCLHRGCIPSKSLLRSAEVYAEIQESE---SYGIETTG----- 75
Cdd:PTZ00153 118 DVGIIGCGVGGHAAAINAMERGLKVIIFTGDDdsIGGTCVNVGCIPSKALLYATGKYRELKNLAklyTYGIYTNAfkngk 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 76 -------------VQLVFPKVQLRKEAVVEQLHQGVQFLMRKNKI-------QVVKGKGRIIGPSIF-SPRSGavavele 134
Cdd:PTZ00153 198 ndpvernqlvadtVQIDITKLKEYTQSVIDKLRGGIENGLKSKKFcknsehvQVIYERGHIVDKNTIkSEKSG------- 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 135 dgdmETVVSTHLIVATGSRPRVLPGLEPDGKVILSSEEALTLEALPSSIIIVGGGVIGVEWASMLADFGVQVTVVEAAGQ 214
Cdd:PTZ00153 271 ----KEFKVKNIIIATGSTPNIPDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSPQ 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 215 LLPLEDEEIARELQRL-LKKRGVKVLTGTTVDAETCVITESGLTI---EARKGE---------QSQSLSAEKLLVSVGRV 281
Cdd:PTZ00153 347 LLPLLDADVAKYFERVfLKSKPVRVHLNTLIEYVRAGKGNQPVIIghsERQTGEsdgpkknmnDIKETYVDSCLVATGRK 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 282 ANVENIGLENTDIHFAKGVIEVNDNMQTAEP------HIYAIGDCIGGLQLAHAASHEGIRAVNHLA--GEALHPYHPHL 353
Cdd:PTZ00153 427 PNTNNLGLDKLKIQMKRGFVSVDEHLRVLREdqevydNIFCIGDANGKQMLAHTASHQALKVVDWIEgkGKENVNINVEN 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 354 ----------VPRCVYTRPEVASVGYTEKEAKALGTDVVTGKFP--FSAIGKAIV-------------------YGMKD- 401
Cdd:PTZ00153 507 waskpiiyknIPSVCYTTPELAFIGLTEKEAKELYPPDNVGVEIsfYKANSKVLCennisfpnnsknnsynkgkYNTVDn 586
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518751641 402 --GFVKVVADRTSGDILGVQMIGPHVTDLIGEAALAQLLDATPWEVGEAIHAHPTLSEVIGEAMLAVDG 468
Cdd:PTZ00153 587 teGMVKIVYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDAAFKAIAG 655
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
6-468 |
3.00e-66 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 219.83 E-value: 3.00e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 6 DVAILGGGTGGYVAAIRAAqlGKSVVVIEMDKLGGTCLHRGCIPSKSLLRSAEVYAEIQESESYGI--ETTGVQlvFPKV 83
Cdd:PRK07846 3 DLIIIGTGSGNSILDERFA--DKRIAIVEKGTFGGTCLNVGCIPTKMFVYAADVARTIREAARLGVdaELDGVR--WPDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 84 QLRKEAVVEQL-HQGVQFLMRKN-KIQVVKGKGRIIGPSifsprsgavavELEDGDMETVVSTHLIVATGSRPRVlPGLE 161
Cdd:PRK07846 79 VSRVFGRIDPIaAGGEEYRGRDTpNIDVYRGHARFIGPK-----------TLRTGDGEEITADQVVIAAGSRPVI-PPVI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 162 PDGKVIL-SSEEALTLEALPSSIIIVGGGVIGVEWASMLADFGVQVTVVEAAGQLLPLEDEEIARELQRLLKKRgVKVLT 240
Cdd:PRK07846 147 ADSGVRYhTSDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLDDDISERFTELASKR-WDVRL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 241 GTTVDAETCviTESGLTIEARKGEqsqSLSAEKLLVSVGRVANVENIGLENTDIHF-AKGVIEVNDNMQTAEPHIYAIGD 319
Cdd:PRK07846 226 GRNVVGVSQ--DGSGVTLRLDDGS---TVEADVLLVATGRVPNGDLLDAAAAGVDVdEDGRVVVDEYQRTSAEGVFALGD 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 320 CIGGLQLAHAASHEGiRAVNH--LAGEALHPYHPHLVPRCVYTRPEVASVGYTEKEAKALGTDVVTGKFPFSAIGkaivY 397
Cdd:PRK07846 301 VSSPYQLKHVANHEA-RVVQHnlLHPDDLIASDHRFVPAAVFTHPQIASVGLTENEARAAGLDITVKVQNYGDVA----Y 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518751641 398 G--MKD--GFVKVVADRTSGDILGVQMIGPHVTDLIGEAALAQLLDATPWEVGEAIH-AHPTLSEVIGEAMLAVDG 468
Cdd:PRK07846 376 GwaMEDttGFVKLIADRDTGRLLGAHIIGPQASTLIQPLIQAMSFGLDAREMARGQYwIHPALPEVVENALLGLDL 451
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
7-435 |
1.25e-62 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 213.09 E-value: 1.25e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 7 VAILGGGTGGYVAAIRAAQLGKSVVVIEMDKLGGTCLHRGCIPSKSLLRSAEVyAEIQESESY--GIETTGVQLVFPKVQ 84
Cdd:PRK13748 101 VAVIGSGGAAMAAALKAVEQGARVTLIERGTIGGTCVNVGCVPSKIMIRAAHI-AHLRRESPFdgGIAATVPTIDRSRLL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 85 LRKEAVVEQL-HQGVQFLMRKN-KIQVVKGKGRIigpsifsPRSGAVAVELEDGDMETVVSTHLIVATGSRPRV--LPGL 160
Cdd:PRK13748 180 AQQQARVDELrHAKYEGILDGNpAITVLHGEARF-------KDDQTLIVRLNDGGERVVAFDRCLIATGASPAVppIPGL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 161 EpdGKVILSSEEALTLEALPSSIIIVGGGVIGVEWASMLADFGVQVTVVeAAGQLLPLEDEEIARELQRLLKKRGVKVLT 240
Cdd:PRK13748 253 K--ETPYWTSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTIL-ARSTLFFREDPAIGEAVTAAFRAEGIEVLE 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 241 GTTVDAETCVITESGLTIEArkGEqsqsLSAEKLLVSVGRVANVENIGLENTDIHF-AKGVIEVNDNMQTAEPHIYAIGD 319
Cdd:PRK13748 330 HTQASQVAHVDGEFVLTTGH--GE----LRADKLLVATGRAPNTRSLALDAAGVTVnAQGAIVIDQGMRTSVPHIYAAGD 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 320 CIGGLQLAHAASHEGIRA-VNHLAGEAlhPYHPHLVPRCVYTRPEVASVGYTEKEAKALGTDVVTGKFPFSAIGKAIVYG 398
Cdd:PRK13748 404 CTDQPQFVYVAAAAGTRAaINMTGGDA--ALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRTLTLDNVPRALANF 481
|
410 420 430
....*....|....*....|....*....|....*..
gi 518751641 399 MKDGFVKVVADRTSGDILGVQMIGPHVTDLIGEAALA 435
Cdd:PRK13748 482 DTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAALA 518
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
6-334 |
1.11e-59 |
|
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: 197.93 E-value: 1.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 6 DVAILGGGTGGYVAAIRAAQLGKSVVVIEmdkLGGTCLHRGCIPSKSLLRSAEVYAEIQEsesygiettgvqlvFPKVQL 85
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIE---DEGTCPYGGCVLSKALLGAAEAPEIASL--------------WADLYK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 86 RKEAVVEQLHQGVQFLMRKNKIQVVKGKGRIIGPsifsprsgavavELEDGDMETVVSTHLIVATGSRPRVL--PGLEP- 162
Cdd:pfam07992 65 RKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLE------------ELVDGDGETITYDRLVIATGARPRLPpiPGVELn 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 163 --DGKVILSSEEALTLEALPSSIIIVGGGVIGVEWASMLADFGVQVTVVEAAGQLLPLEDEEIARELQRLLKKRGVKVLT 240
Cdd:pfam07992 133 vgFLVRTLDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 241 GTTVDAetcvITESGLTIEArKGEQSQSLSAEKLLVSVGRVAN---VENIGLEntdiHFAKGVIEVNDNMQTAEPHIYAI 317
Cdd:pfam07992 213 GTSVKE----IIGDGDGVEV-ILKDGTEIDADLVVVAIGRRPNtelLEAAGLE----LDERGGIVVDEYLRTSVPGIYAA 283
|
330
....*....|....*...
gi 518751641 318 GDC-IGGLQLAHAASHEG 334
Cdd:pfam07992 284 GDCrVGGPELAQNAVAQG 301
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
6-466 |
3.72e-59 |
|
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: 201.14 E-value: 3.72e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 6 DVAILGGGTGGYVAAIRAAqlGKSVVVIEMDKLGGTCLHRGCIPSKSLLRSAEVYAEIQESESYGIETTGVQLVFPKVQL 85
Cdd:TIGR03452 4 DLIIIGTGSGNSIPDPRFA--DKRIAIVEKGTFGGTCLNVGCIPTKMFVYAAEVAQSIGESARLGIDAEIDSVRWPDIVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 86 RK-EAVVEQLHQGVQFLMRKNK---IQVVKGKGRIIGPSIfsprsgavaveLEDGDMETVVSTHLIVATGSRPRVLPGLE 161
Cdd:TIGR03452 82 RVfGDRIDPIAAGGEDYRRGDEtpnIDVYDGHARFVGPRT-----------LRTGDGEEITGDQIVIAAGSRPYIPPAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 162 PDGKVILSSEEALTLEALPSSIIIVGGGVIGVEWASMLADFGVQVTVVEAAGQLLPLEDEEIARELQRLLKKRGVKVLTG 241
Cdd:TIGR03452 151 DSGVRYHTNEDIMRLPELPESLVIVGGGYIAAEFAHVFSALGTRVTIVNRSTKLLRHLDEDISDRFTEIAKKKWDIRLGR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 242 TTVDAETcviTESGLTIEARKGEqsqSLSAEKLLVSVGRVANVENIGLENTDIHFAK-GVIEVNDNMQTAEPHIYAIGDC 320
Cdd:TIGR03452 231 NVTAVEQ---DGDGVTLTLDDGS---TVTADVLLVATGRVPNGDLLDAEAAGVEVDEdGRIKVDEYGRTSARGVWALGDV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 321 IGGLQLAHAASHEgIRAVNH--LAGEALHPYHPHLVPRCVYTRPEVASVGYTEKEAKALGTDVVTGKFPFSAIgkAIVYG 398
Cdd:TIGR03452 305 SSPYQLKHVANAE-ARVVKHnlLHPNDLRKMPHDFVPSAVFTHPQIATVGLTEQEAREAGHDITVKIQNYGDV--AYGWA 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518751641 399 MKD--GFVKVVADRTSGDILGVQMIGPHVTDLIGEAALAQLLDATPWEVGEAIH-AHPTLSEVIGEAMLAV 466
Cdd:TIGR03452 382 MEDttGFCKLIADRDTGKLLGAHIIGPQASSLIQPLITAMAFGLDAREMARKQYwIHPALPEVVENALLGL 452
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
1-457 |
6.29e-59 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 200.38 E-value: 6.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 1 MTISCDVAILGGGTGGYVAAIRAAQLGKSVVVIEMDKLGGTCLHRGCIPSKSLLRSAEVYAEI-QESESYGIETTGVQLV 79
Cdd:PRK06116 1 MTKDYDLIVIGGGSGGIASANRAAMYGAKVALIEAKRLGGTCVNVGCVPKKLMWYGAQIAEAFhDYAPGYGFDVTENKFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 80 FPKVQLRKEAVVEQLHQGVQFLMRKNKIQVVKGKGRIIGPSifsprsgavAVELEDgdmETVVSTHLIVATGSRPRV--L 157
Cdd:PRK06116 81 WAKLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAH---------TVEVNG---ERYTADHILIATGGRPSIpdI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 158 PGLEpdgkVILSSEEALTLEALPSSIIIVGGGVIGVEWASMLADFGVQVTvveaagQL----LPLE--DEEIARELQRLL 231
Cdd:PRK06116 149 PGAE----YGITSDGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETH------LFvrgdAPLRgfDPDIRETLVEEM 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 232 KKRGVKVLTGTTVdaETCVITESG-LTIEARKGEqsqSLSAEKLLVSVGRVANVENIGLENTDIHF-AKGVIEVNDNMQT 309
Cdd:PRK06116 219 EKKGIRLHTNAVP--KAVEKNADGsLTLTLEDGE---TLTVDCLIWAIGREPNTDGLGLENAGVKLnEKGYIIVDEYQNT 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 310 AEPHIYAIGDCIGGLQLAHAASHEGIRAVNHLAG--EALHPYHpHLVPRCVYTRPEVASVGYTEKEAKA-LGTDVVTgkf 386
Cdd:PRK06116 294 NVPGIYAVGDVTGRVELTPVAIAAGRRLSERLFNnkPDEKLDY-SNIPTVVFSHPPIGTVGLTEEEAREqYGEDNVK--- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 387 pfsaigkaiVY-----GMKDGF--------VKVVADRTSGDILGVQMIGPHVTDLIGEAALAQLLDATPWEVGEAIHAHP 453
Cdd:PRK06116 370 ---------VYrssftPMYTALtghrqpclMKLVVVGKEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHP 440
|
....
gi 518751641 454 TLSE 457
Cdd:PRK06116 441 TAAE 444
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
6-457 |
1.97e-58 |
|
glutathione-disulfide reductase, plant; 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 plants and some bacteria, including cyanobacteria. [Energy metabolism, Electron transport]
Pssm-ID: 213618 [Multi-domain] Cd Length: 446 Bit Score: 198.88 E-value: 1.97e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 6 DVAILGGGTGGYVAAIRAAQLGKSVVVIEMDKLGGTCLHRGCIPSKSLLRSAEVYAEIQESESYGIETTGVQLVFPKVQL 85
Cdd:TIGR01424 4 DLFVIGAGSGGVRAARLAAALGAKVAIAEEFRVGGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGWTVGKARFDWKKLLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 86 RKEAVVEQLHQGVQFLMRKNKIQVVKGKGRIIGPSIFSPRSGAvaveledgdmETVVSTHLIVATGSRPR--VLPGLEpd 163
Cdd:TIGR01424 84 AKDQEIARLSGLYRKGLANAGAELLDGRAELVGPNTVEVLASG----------KTYTAEKILIAVGGRPPkpALPGHE-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 164 gkVILSSEEALTLEALPSSIIIVGGGVIGVEWASMLADFGVQVTVVEAAGQLLPLEDEEIARELQRLLKKRGVKVLTGTT 243
Cdd:TIGR01424 152 --LGITSNEAFHLPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRGKEILRGFDDDMRRGLAAALEERGIRILPEDS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 244 VDAETCViTESGLTIEARKGEQsqsLSAEKLLVSVGRVANVENIGLENTDIHFA-KGVIEVNDNMQTAEPHIYAIGDCIG 322
Cdd:TIGR01424 230 ITSISKD-DDGRLKATLSKHEE---IVADVVLFATGRSPNTNGLGLEAAGVRLNdLGAIAVDEYSRTSTPSIYAVGDVTD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 323 GLQLAHAASHEGIRAVNHLAGEALHPYHPHLVPRCVYTRPEVASVGYTEKEAKALGTDVVTGKFPFSAIgKAIVYGMKDG 402
Cdd:TIGR01424 306 RINLTPVAIHEATCFAETEFGNNPTSFDHDLIATAVFSQPPIGTVGLTEEEARRKFGDIEVYRAEFRPM-KATFSGRQEK 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 518751641 403 -FVKVVADRTSGDILGVQMIGPHVTDLIGEAALAQLLDATPWEVGEAIHAHPTLSE 457
Cdd:TIGR01424 385 tLMKLVVDAKDDKVLGAHMVGPDAAEIIQGLAIALKMGATKDDFDSTVAVHPTSAE 440
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
6-457 |
1.64e-55 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 191.12 E-value: 1.64e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 6 DVAILGGGTGGYVAAIRAAQLGKSVVVIEMDKL--GGTCLHRGCIPSKSLLRSAEVyaeiqesesygiettgvQLVFPKV 83
Cdd:PRK07251 5 DLIVIGFGKAGKTLAAKLASAGKKVALVEESKAmyGGTCINIGCIPTKTLLVAAEK-----------------NLSFEQV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 84 QLRKEAVVEQLHQGVQFLMRKNKIQVVKGKGRIIGPSIFSPRSGAVAVELEdgdmetvvSTHLIVATGSRPRVL--PGLE 161
Cdd:PRK07251 68 MATKNTVTSRLRGKNYAMLAGSGVDLYDAEAHFVSNKVIEVQAGDEKIELT--------AETIVINTGAVSNVLpiPGLA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 162 pDGKVILSSEEALTLEALPSSIIIVGGGVIGVEWASMLADFGVQVTVVEAAGQLLPLEDEEIARELQRLLKKRGVKVLTG 241
Cdd:PRK07251 140 -DSKHVYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYMEEDGITFLLN 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 242 TTV-----DAETCVITESGltiearkgeqsQSLSAEKLLVSVGRVANVENIGLENTDIHFA-KGVIEVNDNMQTAEPHIY 315
Cdd:PRK07251 219 AHTtevknDGDQVLVVTED-----------ETYRFDALLYATGRKPNTEPLGLENTDIELTeRGAIKVDDYCQTSVPGVF 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 316 AIGDCIGGLQLAHaASHEGIRAV-NHLAGEALHPYHPHL-VPRCVYTRPEVASVGYTEKEAKALGTDVVTGKFPFSAIGK 393
Cdd:PRK07251 288 AVGDVNGGPQFTY-ISLDDFRIVfGYLTGDGSYTLEDRGnVPTTMFITPPLSQVGLTEKEAKEAGLPYAVKELLVAAMPR 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518751641 394 AIVYGMKDGFVKVVADRTSGDILGVQMIGPHVTDLIGEAALAqLLDATPWE-VGEAIHAHPTLSE 457
Cdd:PRK07251 367 AHVNNDLRGAFKVVVNTETKEILGATLFGEGSQEIINLITMA-MDNKIPYTyFKKQIFTHPTMAE 430
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
9-461 |
3.66e-52 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 182.29 E-value: 3.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 9 ILGGGTGGYVAAIRAAQLGKSVVVIEM--DKLGGTCLHRGCIPSKSLLRSAEVYAEiqesesygiettgvqlvFPKVQLR 86
Cdd:NF040477 8 IIGFGKAGKTLAATLAKAGWRVAIIEQsaQMYGGTCINIGCIPTKTLVHDAEQHQD-----------------FSTAMQR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 87 KEAVVEQLH-QGVQFLMRKNKIQVVKGKGRIIGPSifsprsgAVAVELEDGDMEtVVSTHLIVATGSRPRV--LPGLEPD 163
Cdd:NF040477 71 KSSVVGFLRdKNYHNLADLDNVDVINGRAEFIDNH-------TLRVFQADGEQE-LRGEKIFINTGAQSVLppIPGLTTT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 164 GKViLSSEEALTLEALPSSIIIVGGGVIGVEWASMLADFGVQVTVVEAAGQLLPLEDEEIARELQRLLKKRGVKVLTGTT 243
Cdd:NF040477 143 PGV-YDSTGLLNLTQLPARLGILGGGYIGVEFASMFARFGSKVTIFEAAELFLPREDRDIAQAIATILQDQGVELILNAQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 244 VDAETCVitESGLTIEARKGEQsqslSAEKLLVSVGRVANVENIGLENTDIHF-AKGVIEVNDNMQTAEPHIYAIGDCIG 322
Cdd:NF040477 222 VQRVSSH--EGEVQLETAEGVL----TVDALLVASGRKPATAGLQLQNAGVAVnERGAIVVDKYLRTTADNIWAMGDVTG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 323 GLQLAHaASHEGIRAV-NHLAGEAL-HPYHPHLVPRCVYTRPEVASVGYTEKEAKALGTDVVTGKFPFSAIGKAIVYGMK 400
Cdd:NF040477 296 GLQFTY-ISLDDFRIVrDSLLGEGKrSTDDRQNVPYSVFMTPPLSRIGMTEEQARASGADIQVVTLPVAAIPRARVMNDT 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518751641 401 DGFVKVVADRTSGDILGVQMIGPHVTDLIGeaALAQLLDA-TPWEV-GEAIHAHPTLSEVIGE 461
Cdd:NF040477 375 RGVLKAVVDNKTQRILGVSLLCVDSHEMIN--IVKTVMDAgLPYTVlRDQIFTHPTMSESLND 435
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
6-457 |
8.29e-46 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 166.53 E-value: 8.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 6 DVAILGGGTGGYVAAIRAAQLGKSVVVIEM----------DKLGGTCLHRGCIPSKSLLRSAEVYAEIQESESYGIETTG 75
Cdd:PLN02507 27 DLFVIGAGSGGVRAARFSANFGAKVGICELpfhpissesiGGVGGTCVIRGCVPKKILVYGATFGGEFEDAKNYGWEINE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 76 -VQLVFPKVQLRKEAVVEQLHQGVQFLMRKNKIQVVKGKGRIIGPSifsprsgAVAVELEDGDMETVVSTHLIVATGSR- 153
Cdd:PLN02507 107 kVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPN-------EVEVTQLDGTKLRYTAKHILIATGSRa 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 154 -PRVLPGLEpdgkVILSSEEALTLEALPSSIIIVGGGVIGVEWASMLADFGVQVTVVEAagQLLPLE--DEEIARELQRL 230
Cdd:PLN02507 180 qRPNIPGKE----LAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFR--KELPLRgfDDEMRAVVARN 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 231 LKKRGVKVLTGTTVDAETcvITESGLTIEARKGEQsqsLSAEKLLVSVGRVANVENIGLENTDIHFAK-GVIEVNDNMQT 309
Cdd:PLN02507 254 LEGRGINLHPRTNLTQLT--KTEGGIKVITDHGEE---FVADVVLFATGRAPNTKRLNLEAVGVELDKaGAVKVDEYSRT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 310 AEPHIYAIGDCIGGLQLAHAASHEGI-RAVNHLAGEALHPYHPHlVPRCVYTRPEVASVGYTEKEA-KALGTDVVTGKFP 387
Cdd:PLN02507 329 NIPSIWAIGDVTNRINLTPVALMEGTcFAKTVFGGQPTKPDYEN-VACAVFCIPPLSVVGLSEEEAvEQAKGDILVFTSS 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 388 FSAIGKAIVYGMKDGFVKVVADRTSGDILGVQMIGPHVTDLIGEAALAQLLDATPWEVGEAIHAHPTLSE 457
Cdd:PLN02507 408 FNPMKNTISGRQEKTVMKLIVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAE 477
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
354-462 |
6.39e-45 |
|
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: 152.71 E-value: 6.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 354 VPRCVYTRPEVASVGYTEKEAKALGTDVVTGKFPFSAIGKAIVYGMKDGFVKVVADRTSGDILGVQMIGPHVTDLIGEAA 433
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGEVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQEAA 80
|
90 100
....*....|....*....|....*....
gi 518751641 434 LAQLLDATPWEVGEAIHAHPTLSEVIGEA 462
Cdd:pfam02852 81 LAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
9-461 |
2.30e-42 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 155.94 E-value: 2.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 9 ILGGGTGGYVAAIRAAQLGKSVVVIEMDK--LGGTCLHRGCIPSKSLLRSAEvyaeiQESEsygiettgvqlvFPKVQLR 86
Cdd:PRK08010 8 IIGFGKAGKTLAVTLAKAGWRVALIEQSNamYGGTCINIGCIPTKTLVHDAQ-----QHTD------------FVRAIQR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 87 KEAVVEQL-HQGVQFLMRKNKIQVVKGKGRIIGpsifsprSGAVAVELEDGDMEtVVSTHLIVATGSRPRV--LPGLEPD 163
Cdd:PRK08010 71 KNEVVNFLrNKNFHNLADMPNIDVIDGQAEFIN-------NHSLRVHRPEGNLE-IHGEKIFINTGAQTVVppIPGITTT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 164 GKViLSSEEALTLEALPSSIIIVGGGVIGVEWASMLADFGVQVTVVEAAGQLLPLEDEEIARELQRLLKKRGVKVLTGTT 243
Cdd:PRK08010 143 PGV-YDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 244 VDAETCviTESGLTIEARKGEqsqsLSAEKLLVSVGRVANVENIGLENTDIHF-AKGVIEVNDNMQTAEPHIYAIGDCIG 322
Cdd:PRK08010 222 VERISH--HENQVQVHSEHAQ----LAVDALLIASGRQPATASLHPENAGIAVnERGAIVVDKYLHTTADNIWAMGDVTG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 323 GLQLAHaASHEGIRAV-NHLAGEALHPYHPHL-VPRCVYTRPEVASVGYTEKEAKALGTDVVTGKFPFSAIGKAIVYGMK 400
Cdd:PRK08010 296 GLQFTY-ISLDDYRIVrDELLGEGKRSTDDRKnVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDT 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518751641 401 DGFVKVVADRTSGDILGVQMIGPHVTDLIGeaALAQLLDA-TPWEV-GEAIHAHPTLSEVIGE 461
Cdd:PRK08010 375 RGVLKAIVDNKTQRILGASLLCVDSHEMIN--IVKMVMDAgLPYSIlRDQIFTHPSMSESLND 435
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
6-459 |
8.47e-42 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 156.31 E-value: 8.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 6 DVAILGGGTGGYVAAIRAAQLGKSVVVIEMDKLGGTCLHRGCIPSKSLLRSAEVYAEIQESESYGIETTGVqLVFPKVQL 85
Cdd:PTZ00058 50 DLIVIGGGSGGMAAARRAARNKAKVALVEKDYLGGTCVNVGCVPKKIMFNAASIHDILENSRHYGFDTQFS-FNLPLLVE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 86 RKEAVVEQLHQGVQFLMRKNKIQVVKGKGRIIGPSIFSPRSGAVAVELEDG---DMETVVST--------------HLIV 148
Cdd:PTZ00058 129 RRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLIKKVSQVDGEADEsddDEVTIVSAgvsqlddgqviegkNILI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 149 ATGSRPrVLPGLEPDGKVIlSSEEALTLEAlPSSIIIVGGGVIGVEWASMLADFGVQVTVVEAAGQLLPLEDEEIARELQ 228
Cdd:PTZ00058 209 AVGNKP-IFPDVKGKEFTI-SSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLRKFDETIINELE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 229 RLLKKRGVKVLTGTTVDaETCVITESGLTI---EARKGEqsqslSAEKLLVSVGRVANVENIGLENTDIHFAKGVIEVND 305
Cdd:PTZ00058 286 NDMKKNNINIITHANVE-EIEKVKEKNLTIylsDGRKYE-----HFDYVIYCVGRSPNTEDLNLKALNIKTPKGYIKVDD 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 306 NMQTAEPHIYAIGDCIG----------------------------------GLQLAHAASHEGIRAVNHLAGEALHPYHP 351
Cdd:PTZ00058 360 NQRTSVKHIYAVGDCCMvkknqeiedlnllklyneepylkkkentsgesyyNVQLTPVAINAGRLLADRLFGPFSRTTNY 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 352 HLVPRCVYTRPEVASVGYTEKEA-KALGTD---VVTGKFPFSAIGkaiVYGMKDG-----FVKVVADRTSGDILGVQMIG 422
Cdd:PTZ00058 440 KLIPSVIFSHPPIGTIGLSEQEAiDIYGKEnvkIYESRFTNLFFS---VYDMDPAqkektYLKLVCVGKEELIKGLHIVG 516
|
490 500 510
....*....|....*....|....*....|....*..
gi 518751641 423 PHVTDLIGEAALAQLLDATPWEVGEAIHAHPTLSEVI 459
Cdd:PTZ00058 517 LNADEILQGFAVALKMNATKADFDETIPIHPTAAEEF 553
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
6-458 |
3.84e-39 |
|
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: 147.69 E-value: 3.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 6 DVAILGGGTGGYVAAIRAAQLGKSVVVIEMDK---------LGGTCLHRGCIPSKSLLRSAEVYAEIQESESYGIEttGV 76
Cdd:TIGR01438 4 DLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTptplgtrwgIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWK--VE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 77 QLVFPKVQLRKEAV---VEQLHQGVQFLMRKNKIQVVKGKGRIIGPSIfsprsgaVAVELEDGDMETVVSTHLIVATGSR 153
Cdd:TIGR01438 82 ETVKHDWKRLVEAVqnhIGSLNWGYRVALREKKVKYENAYAEFVDKHR-------IKATNKKGKEKIYSAERFLIATGER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 154 PRVlPGLEPDGKVILSSEEALTLEALPSSIIIVGGGVIGVEWASMLADFGVQVTVveaAGQLLPLE--DEEIARELQRLL 231
Cdd:TIGR01438 155 PRY-PGIPGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTV---MVRSILLRgfDQDCANKVGEHM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 232 KKRGVKVLTGTTVDAETCVitESGLTIEARKGEQSQSLSAEKLLVSVGRVANVENIGLENTDIHFAK--GVIEVNDNMQT 309
Cdd:TIGR01438 231 EEHGVKFKRQFVPIKVEQI--EAKVLVEFTDSTNGIEEEYDTVLLAIGRDACTRKLNLENVGVKINKktGKIPADEEEQT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 310 AEPHIYAIGDCIGG-LQLAHAASHEGIRAVNHLAGEALHPYHPHLVPRCVYTRPEVASVGYTEKEA-KALGTDVVTGKFP 387
Cdd:TIGR01438 309 NVPYIYAVGDILEDkPELTPVAIQAGRLLAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAvEKFGEENVEVFHS 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518751641 388 -FSAIGKAIVYGMKDGF--VKVVADRTSGD-ILGVQMIGPHVTDLIGEAALAQLLDATPWEVGEAIHAHPTLSEV 458
Cdd:TIGR01438 389 yFWPLEWTIPSRDNHNKcyAKLVCNKKENErVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEV 463
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
6-457 |
3.63e-37 |
|
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: 142.42 E-value: 3.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 6 DVAILGGGTGGYVAAIRAAQL-GKSVVVIEMDK---------LGGTCLHRGCIPSKSLLRSAEVYAEIQESESYGIETTG 75
Cdd:TIGR01423 5 DLVVIGAGSGGLEAGWNAATLyKKRVAVVDVQThhgppfyaaLGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGWEFDR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 76 --VQLVFPKVQLRKEAVVEQLHQGVQFLMRKNK-IQVVKGKGRIIGPSIFSPRSGAvavELEDGDMETVVSTHLIVATGS 152
Cdd:TIGR01423 85 ssVKANWKALIAAKNKAVLDINKSYEGMFADTEgLTFFLGWGALEDKNVVLVRESA---DPKSAVKERLQAEHILLATGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 153 RPRVL--PGLEpdgkVILSSEEALTLEALPSSIIIVGGGVIGVEWASMLADF---GVQVTVVEAAGQLLPLEDEEIAREL 227
Cdd:TIGR01423 162 WPQMLgiPGIE----HCISSNEAFYLDEPPRRVLTVGGGFISVEFAGIFNAYkprGGKVTLCYRNNMILRGFDSTLRKEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 228 QRLLKKRGVKVLTGT-------TVDAETCVITESGLTiearkgeqsqsLSAEKLLVSVGRVANVENIGLENTDIHFA-KG 299
Cdd:TIGR01423 238 TKQLRANGINIMTNEnpakvtlNADGSKHVTFESGKT-----------LDVDVVMMAIGRVPRTQTLQLDKVGVELTkKG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 300 VIEVNDNMQTAEPHIYAIGDCIGGLQLAHAASHEGIRAVNHLAGEALHPYHPHLVPRCVYTRPEVASVGYTEKEAKALGT 379
Cdd:TIGR01423 307 AIQVDEFSRTNVPNIYAIGDVTDRVMLTPVAINEGAAFVDTVFGNKPRKTDHTRVASAVFSIPPIGTCGLVEEDAAKKFE 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518751641 380 DVVTGKFPFSAIGKAIVYGMKDGFV-KVVADRTSGDILGVQMIGPHVTDLIGEAALAQLLDATPWEVGEAIHAHPTLSE 457
Cdd:TIGR01423 387 KVAVYESSFTPLMHNISGSKYKKFVaKIVTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAE 465
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
6-457 |
1.04e-33 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 133.46 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 6 DVAILGGGTGGYVAAIRAAQLGKSVVVIEM----------DKLGGTCLHRGCIPSKSLLRSAEVYAEIQESESYG--IET 73
Cdd:PLN02546 81 DLFTIGAGSGGVRASRFASNFGASAAVCELpfatissdtlGGVGGTCVLRGCVPKKLLVYASKYSHEFEESRGFGwkYET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 74 TgvqlvfPKVQLR-----KEAVVEQLHQGVQFLMRKNKIQVVKGKGRIIGPSifsprsgAVAVeleDGDMETvvSTHLIV 148
Cdd:PLN02546 161 E------PKHDWNtlianKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPH-------TVDV---DGKLYT--ARNILI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 149 ATGSRPRV--LPGLEpdgkVILSSEEALTLEALPSSIIIVGGGVIGVEWASMLADFGVQVTVVEAAGQLLPLEDEEIARE 226
Cdd:PLN02546 223 AVGGRPFIpdIPGIE----HAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKKVLRGFDEEVRDF 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 227 LQRLLKKRGVKVLTGTTVDAetcvITESG---LTIEARKGEQSqslSAEKLLVSVGRVANVENIGLENTDIHFAK-GVIE 302
Cdd:PLN02546 299 VAEQMSLRGIEFHTEESPQA----IIKSAdgsLSLKTNKGTVE---GFSHVMFATGRKPNTKNLGLEEVGVKMDKnGAIE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 303 VNDNMQTAEPHIYAIGDCIGGLQLAHAASHEGIRAVNHLAGEalHPYHP--HLVPRCVYTRPEVASVGYTEKEA-KALG- 378
Cdd:PLN02546 372 VDEYSRTSVPSIWAVGDVTDRINLTPVALMEGGALAKTLFGN--EPTKPdyRAVPSAVFSQPPIGQVGLTEEQAiEEYGd 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 379 TDVVTGKF-PFsaigKAIVYGMKDG-FVKVVADRTSGDILGVQMIGPHVTDLIGEAALAQLLDATPWEVGEAIHAHPTLS 456
Cdd:PLN02546 450 VDVFTANFrPL----KATLSGLPDRvFMKLIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAA 525
|
.
gi 518751641 457 E 457
Cdd:PLN02546 526 E 526
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
6-460 |
7.67e-26 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 109.91 E-value: 7.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 6 DVAILGGGTGGYVAAIRAAQLGKSVVVIEMDK---------LGGTCLHRGCIPSKSLLRSAEVYAEIQ-ESESYGIETTG 75
Cdd:PTZ00052 7 DLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKpstqgtkwgLGGTCVNVGCVPKKLMHYAANIGSIFHhDSQMYGWKTSS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 76 VQlvfpkvqlRKEAVVEQLHQGVQFL-------MRKNKIQVVKGKGRIIGPSifsprsgavAVELED-GDMETVVSTHLI 147
Cdd:PTZ00052 87 SF--------NWGKLVTTVQNHIRSLnfsyrtgLRSSKVEYINGLAKLKDEH---------TVSYGDnSQEETITAKYIL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 148 VATGSRPRVLPGLEPDGKVILSSEEALTLEALPSSIIIVGGGVIGVEWASMLADFGVQVTVveaAGQLLPLE--DEEIAR 225
Cdd:PTZ00052 150 IATGGRPSIPEDVPGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTV---AVRSIPLRgfDRQCSE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 226 ELQRLLKKRGVKVLTG------TTVDAETCVITESGLTIEarkgeqsqslsAEKLLVSVGRVANVENIGLENTDIHFAKG 299
Cdd:PTZ00052 227 KVVEYMKEQGTLFLEGvvpiniEKMDDKIKVLFSDGTTEL-----------FDTVLYATGRKPDIKGLNLNAIGVHVNKS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 300 VIEVNDNMQTAEPHIYAIGDCIGGL-QLAHAASHEGIRAVNHLAGEALHPYHPHLVPRCVYTRPEVASVGYTEKEAKAL- 377
Cdd:PTZ00052 296 NKIIAPNDCTNIPNIFAVGDVVEGRpELTPVAIKAGILLARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKy 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 378 GT-DVVTGKFPFSAIGKAIVYGMK---------------DGFVKVVADRTSGD-ILGVQMIGPHVTDLIGEAALAQLLDA 440
Cdd:PTZ00052 376 GEdDIEEYLQEFNTLEIAAVHREKherarkdeydfdvssNCLAKLVCVKSEDNkVVGFHFVGPNAGEITQGFSLALKLGA 455
|
490 500
....*....|....*....|
gi 518751641 441 TPWEVGEAIHAHPTLSEVIG 460
Cdd:PTZ00052 456 KKSDFDSMIGIHPTDAEVFM 475
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
131-353 |
5.08e-24 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 103.68 E-value: 5.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 131 VELEDGdmETVVSTHLIVATGSRPRVLP--GLEPDGKVILSS-EEALTLEALPSSIIIVGGG---VIGVEWASMLADFGV 204
Cdd:COG1251 89 VTLADG--ETLPYDKLVLATGSRPRVPPipGADLPGVFTLRTlDDADALRAALAPGKRVVVIgggLIGLEAAAALRKRGL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 205 QVTVVEAAGQLLP-LEDEEIARELQRLLKKRGVKVLTGTTV------DAETCVITESGLTIEarkgeqsqslsAEKLLVS 277
Cdd:COG1251 167 EVTVVERAPRLLPrQLDEEAGALLQRLLEALGVEVRLGTGVteiegdDRVTGVRLADGEELP-----------ADLVVVA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 278 VGRVANVEniGLENTDIHFAKGVIeVNDNMQTAEPHIYAIGDC-------IGGLQLAH--AASHEGIRAVNHLAGEAlHP 348
Cdd:COG1251 236 IGVRPNTE--LARAAGLAVDRGIV-VDDYLRTSDPDIYAAGDCaehpgpvYGRRVLELvaPAYEQARVAAANLAGGP-AA 311
|
....*
gi 518751641 349 YHPHL 353
Cdd:COG1251 312 YEGSV 316
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
131-346 |
3.55e-23 |
|
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: 99.89 E-value: 3.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 131 VELEDGdmETVVSTHLIVATGSRPRVL--PGLEPDGKVILSS-EEALTLEAL-----PSSIIIVGGGVIGVEWASMLADF 202
Cdd:COG0446 69 VTLRDG--ETLSYDKLVLATGARPRPPpiPGLDLPGVFTLRTlDDADALREAlkefkGKRAVVIGGGPIGLELAEALRKR 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 203 GVQVTVVEAAGQLLPLEDEEIARELQRLLKKRGVKVLTGTTVDAetcVITESGLTIEARKGEqsqSLSAEKLLVSVGRVA 282
Cdd:COG0446 147 GLKVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVVA---IDGDDKVAVTLTDGE---EIPADLVVVAPGVRP 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518751641 283 NVE---NIGLEntdiHFAKGVIEVNDNMQTAEPHIYAIGDCIG----------GLQLAHAASHEGIRAVNHLAGEAL 346
Cdd:COG0446 221 NTElakDAGLA----LGERGWIKVDETLQTSDPDVYAAGDCAEvphpvtgktvYIPLASAANKQGRVAAENILGGPA 293
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
5-339 |
5.40e-22 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 95.96 E-value: 5.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 5 CDVAILGGGTGGYVAAIRAAQLGKSVVVIEMDKLGGTCLHRGCIpsksllrsaEVYAEIQEsesygiETTGVQLVfpkVQ 84
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQLATTKEI---------ENYPGFPE------GISGPELA---ER 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 85 LRKEAvveqLHQGVQFLMRknkiQVVKgkgriigpsiFSPRSGAVAVELEDGdmETVVSTHLIVATGSRPRVL--PGLEP 162
Cdd:COG0492 63 LREQA----ERFGAEILLE----EVTS----------VDKDDGPFRVTTDDG--TEYEAKAVIIATGAGPRKLglPGEEE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 163 ------------DGK--------VILSSEEALtlealpssiiivgggvigvEWASMLADFGVQVTVVeaagqlLPLEDEE 222
Cdd:COG0492 123 fegrgvsycatcDGFffrgkdvvVVGGGDSAL-------------------EEALYLTKFASKVTLI------HRRDELR 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 223 IARELQ-RLLKKRGVKVLTGTTVDA---ETCViteSGLTIEARKGEQSQSLSAEKLLVSVGRVAN---VENIGLENTDih 295
Cdd:COG0492 178 ASKILVeRLRANPKIEVLWNTEVTEiegDGRV---EGVTLKNVKTGEEKELEVDGVFVAIGLKPNtelLKGLGLELDE-- 252
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 518751641 296 faKGVIEVNDNMQTAEPHIYAIGDCIGG-LQLAHAASHEGIRAVN 339
Cdd:COG0492 253 --DGYIVVDEDMETSVPGVFAAGDVRDYkYRQAATAAGEGAIAAL 295
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
131-352 |
3.41e-17 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 83.26 E-value: 3.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 131 VELEDGdmETVVSTHLIVATGSRPRV--LPGLEPDGKVILSSEEALTL-EALPSSIIIVGGGVIG--------------- 192
Cdd:COG1252 88 VTLADG--RTLSYDYLVIATGSVTNFfgIPGLAEHALPLKTLEDALALrERLLAAFERAERRRLLtivvvgggptgvela 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 193 ---VEWASMLADFG------VQVTVVEAAGQLLPLEDEEIARELQRLLKKRGVKVLTGTTVDA--ETCVITESGLTIEAR 261
Cdd:COG1252 166 gelAELLRKLLRYPgidpdkVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEvdADGVTLEDGEEIPAD 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 262 kgeqsqslsaekLLVSVGRV-AN--VENIGLEnTDihfAKGVIEVNDNMQTAE-PHIYAIGDCI-------GGL-QLAHA 329
Cdd:COG1252 246 ------------TVIWAAGVkAPplLADLGLP-TD---RRGRVLVDPTLQVPGhPNVFAIGDCAavpdpdgKPVpKTAQA 309
|
250 260
....*....|....*....|....*..
gi 518751641 330 ASHEGIRA----VNHLAGEALHPYHPH 352
Cdd:COG1252 310 AVQQAKVLakniAALLRGKPLKPFRYR 336
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
146-335 |
2.45e-12 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 69.09 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 146 LIVATGSRPRVLPGLEPDGKVILSSEEALTLEALPSSIIIVGGGVIG------VEWASMLADFGVQVTVVEAAGQLLPLE 219
Cdd:TIGR02374 100 LILATGSYPFILPIPGADKKGVYVFRTIEDLDAIMAMAQRFKKAAVIgggllgLEAAVGLQNLGMDVSVIHHAPGLMAKQ 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 220 -DEEIARELQRLLKKRGVKVLTGTtvDAETCVITESGLTIEARKGEqsqSLSAEKLLVSVGRVANVEnIGLEnTDIHFAK 298
Cdd:TIGR02374 180 lDQTAGRLLQRELEQKGLTFLLEK--DTVEIVGATKADRIRFKDGS---SLEADLIVMAAGIRPNDE-LAVS-AGIKVNR 252
|
170 180 190
....*....|....*....|....*....|....*..
gi 518751641 299 GVIeVNDNMQTAEPHIYAIGDCigglqlahaASHEGI 335
Cdd:TIGR02374 253 GII-VNDSMQTSDPDIYAVGEC---------AEHNGR 279
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
192-246 |
2.99e-12 |
|
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: 62.22 E-value: 2.99e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 518751641 192 GVEWASMLADFGVQVTVVEAAGQLLPLEDEEIARELQRLLKKRGVKVLTGTTVDA 246
Cdd:pfam00070 11 GLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEA 65
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
190-327 |
6.78e-11 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 63.78 E-value: 6.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 190 VIGVEWASMLADFGVQVTVVEAAGQLLP-LEDEEIARELQRLLKKRGVKVLTGTTVDAETcvITESGLTIEARKGeqsQS 268
Cdd:PRK04965 151 LIGTELAMDLCRAGKAVTLVDNAASLLAsLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLE--KTDSGIRATLDSG---RS 225
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518751641 269 LSAEKLLVSVGRVAnveNIGL-ENTDIHFAKGVIeVNDNMQTAEPHIYAIGDC--IGGLQLA 327
Cdd:PRK04965 226 IEVDAVIAAAGLRP---NTALaRRAGLAVNRGIV-VDSYLQTSAPDIYALGDCaeINGQVLP 283
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
1-125 |
6.95e-08 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 54.83 E-value: 6.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 1 MTISCDVAILGGGTGGYVAAIRAAQLGKSVVVIE-MDKLGGTCLHRG---CIPSKSLLRSAEVYAEIQESESYGIETTGV 76
Cdd:PRK12839 5 MTHTYDVVVVGSGAGGLSAAVAAAYGGAKVLVVEkASTCGGATAWSGgwmWTPGNSLARADGVVEDKEEPRTYLEHRLGE 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518751641 77 QLVFPKVqlrkEAVVEQLHQGVQFLMRKNKIQVVKGK---------------GRIIGPSIFSPR 125
Cdd:PRK12839 85 NYDADKV----DALLDGAPEMVDFFEKKTALQFVPGAkiadiygdlpgagtgHRSVGPKPVNLR 144
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
146-422 |
1.85e-07 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 53.12 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 146 LIVATGSRPRV--LPGLEPDGKVILSS-EEALTLEAL-----PSSIIIVGGGVIGVEWASMLADFGVQVTVVEAAGQLLP 217
Cdd:PRK09564 107 LMIATGARPIIppIKNINLENVYTLKSmEDGLALKELlkdeeIKNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRILP 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 218 LE-DEEIARELQRLLKKRGVKVLTGTTVDAetcVITESGLT-IEARKGEqsqsLSAEKLLVSVGRVANVEniGLENTDIH 295
Cdd:PRK09564 187 DSfDKEITDVMEEELRENGVELHLNEFVKS---LIGEDKVEgVVTDKGE----YEADVVIVATGVKPNTE--FLEDTGLK 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 296 FAK-GVIEVNDNMQTAEPHIYAIGDCIGGLQ----------LAHAASHEGIRAVNHLAGEALhPYHPHLVPRCVYTRP-E 363
Cdd:PRK09564 258 TLKnGAIIVDEYGETSIENIYAAGDCATIYNivsnknvyvpLATTANKLGRMVGENLAGRHV-SFKGTLGSACIKVLDlE 336
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 364 VASVGYTEKEAKALGTDVVTgKFpFSAIGKAIVY-GMKDGFVKVVADRTSGDILGVQMIG 422
Cdd:PRK09564 337 AARTGLTEEEAKKLGIDYKT-VF-IKDKNHTNYYpGQEDLYVKLIYEADTKVILGGQIIG 394
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
6-41 |
2.26e-06 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 49.91 E-value: 2.26e-06
10 20 30
....*....|....*....|....*....|....*..
gi 518751641 6 DVAILGGGTGGYVAAIRAAQLGKSVVVIE-MDKLGGT 41
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVErRGFLGGM 37
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
5-256 |
2.79e-06 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 49.50 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 5 CDVAILGGGTGGYVAAIRAAQLGKSVVVIE-MDKLG--------GTC-LHRGCIPSKSLL-----RSAEVYAEIQE---- 65
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEkGKKLGrkilisggGRCnVTNLSEEPDNFLsrypgNPKFLKSALSRftpw 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 66 -----SESYGIET---TGVQlVFPkVQLRKEAVVEQL-----HQGVQFLMRKNKIQVVKGKGRIIGPSIfsprsgavave 132
Cdd:pfam03486 81 dfiafFESLGVPLkeeDHGR-LFP-DSDKASDIVDALlnelkELGVKIRLRTRVLSVEKDDDGRFRVKT----------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 133 ledgDMETVVSTHLIVATGSRPrvLPGLEPDGKvilsseealtlealpssiiivgggvigveWASMLADFGVQVTVVEAA 212
Cdd:pfam03486 148 ----GGEELEADSLVLATGGLS--WPKTGSTGF-----------------------------GYPLAEQFGHTIIPLRPA 192
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 518751641 213 gqLLPL---EDEEIARELQRL-LKKRGVKVLTGTTVDAETCVITESGL 256
Cdd:pfam03486 193 --LVPFtidEPFLFLKRLSGIsLKNVVLSNGKGGITFRGELLFTHRGL 238
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
146-320 |
7.21e-06 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 48.58 E-value: 7.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 146 LIVATGSRPRVLPGLEPDGK---VILSSEEALTLEA---LPSSIIIVGGGVIGVEWASMLADFGVQVTVVEAAGQLLPLE 219
Cdd:PRK14989 105 LIMATGSYPWIPPIKGSETQdcfVYRTIEDLNAIEAcarRSKRGAVVGGGLLGLEAAGALKNLGVETHVIEFAPMLMAEQ 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 220 -DEEIARELQRLLKKRGVKVLTGTTvdaeTCVITESGLtiEARKGEQ---SQSLSAEKLLVSVG-----RVANVENIGLE 290
Cdd:PRK14989 185 lDQMGGEQLRRKIESMGVRVHTSKN----TLEIVQEGV--EARKTMRfadGSELEVDFIVFSTGirpqdKLATQCGLAVA 258
|
170 180 190
....*....|....*....|....*....|
gi 518751641 291 ntdihfAKGVIEVNDNMQTAEPHIYAIGDC 320
Cdd:PRK14989 259 ------PRGGIVINDSCQTSDPDIYAIGEC 282
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
2-130 |
1.06e-05 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 47.79 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 2 TISCDVAILGGGTGGYVAAIRAAQLGKSVVVIEMD-KLGGTCLHRG---CIPSKSLLRSAEVYAEIQESESYGIETTGVQ 77
Cdd:PRK06134 10 DLECDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDpVFGGTTAWSGgwmWIPRNPLARRAGIVEDIEQPRTYLRHELGAR 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 518751641 78 LvfpkVQLRKEAVVEQLHQGVQFLMRKNKIQVVKGKGRiigPSIFSPRSGAVA 130
Cdd:PRK06134 90 Y----DAARIDAFLEAGPHMVAFFERHTALRFADGNAI---PDYHGDTPGAAT 135
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
145-344 |
1.73e-05 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 47.07 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 145 HLIVATGSRPRVL--PGLEPDGKVILSSEEALTLE----------ALPSSIIIVGGGVIG----------VEWASMLADF 202
Cdd:PTZ00318 116 KLVVAHGARPNTFniPGVEERAFFLKEVNHARGIRkrivqcieraSLPTTSVEERKRLLHfvvvgggptgVEFAAELADF 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 203 --------------GVQVTVVEAAGQLLPLEDEEIARELQRLLKKRGVKVLTGTTVDA--ETCVITESGLTIEArkgeqs 266
Cdd:PTZ00318 196 frddvrnlnpelveECKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEvlDKEVVLKDGEVIPT------ 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 267 qslsaeKLLV---SVGRVANVENIGLENTdihfAKGVIEVNDNMQTAE-PHIYAIGDCIGGLQ-----LAHAASHEGIRA 337
Cdd:PTZ00318 270 ------GLVVwstGVGPGPLTKQLKVDKT----SRGRISVDDHLRVKPiPNVFALGDCAANEErplptLAQVASQQGVYL 339
|
....*..
gi 518751641 338 VNHLAGE 344
Cdd:PTZ00318 340 AKEFNNE 346
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
6-63 |
2.44e-05 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 46.39 E-value: 2.44e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 518751641 6 DVAILGGGTGGYVAAIRAAQLGKSVVVIEMDklGGTCLHRGCIPSKSLLRSAEVYAEI 63
Cdd:pfam01134 1 DVIVIGGGHAGCEAALAAARMGAKVLLITHN--TDTIAELSCNPSIGGIAKGHLVREI 56
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
2-41 |
2.88e-05 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 46.36 E-value: 2.88e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 518751641 2 TISCDVAILGGGTGGYVAAIRAAQLGKSVVVIE-MDKLGGT 41
Cdd:COG1053 1 DHEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEkVPPRGGH 41
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
6-40 |
9.31e-05 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 44.84 E-value: 9.31e-05
10 20 30
....*....|....*....|....*....|....*.
gi 518751641 6 DVAILGGGTGGYVAAIRAAQLGKSVVVIEM-DKLGG 40
Cdd:COG1233 5 DVVVIGAGIGGLAAAALLARAGYRVTVLEKnDTPGG 40
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
6-41 |
9.68e-05 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 44.59 E-value: 9.68e-05
10 20 30
....*....|....*....|....*....|....*..
gi 518751641 6 DVAILGGGTGGYVAAIRAAQLGKSVVVIE-MDKLGGT 41
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEkGQPFGGA 37
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
2-110 |
1.31e-04 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 44.30 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 2 TISCDVAILGGGTGGYVAAIRAAQLGKSVVVIEMDK-LGGTCLHRG---CIPSKSLLRSAEVYAEIQESESYGIETTGVQ 77
Cdd:PRK12842 7 ELTCDVLVIGSGAGGLSAAITARKLGLDVVVLEKEPvFGGTTAFSGgvlWIPGNPHAREAGVADSREAARTYLKHETGAF 86
|
90 100 110
....*....|....*....|....*....|...
gi 518751641 78 LVFPKVqlrkEAVVEQLHQGVQFLMRKNKIQVV 110
Cdd:PRK12842 87 FDAAAV----EAFLDNGPEMVEFFERETEVKFV 115
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
203-382 |
1.93e-04 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 43.62 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 203 GVQVTVVEAAGQLLPLEDEEIARELQRLLKKRGVKVLTGTTVDAetcvITESGLTIEARKGEQsqslsAEKLLVSVGRVA 282
Cdd:PRK13512 171 GLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDA----INGNEVTFKSGKVEH-----YDMIIEGVGTHP 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 283 NVENIglENTDIHF-AKGVIEVNDNMQTAEPHIYAIGDCI----------GGLQLAHAAsHEGIRAV-NHLAGEALHPYH 350
Cdd:PRK13512 242 NSKFI--ESSNIKLdDKGFIPVNDKFETNVPNIYAIGDIItshyrhvdlpASVPLAWGA-HRAASIVaEQIAGNDTIEFK 318
|
170 180 190
....*....|....*....|....*....|....*.
gi 518751641 351 PHLVPRCV----YTrpeVASVGYTEKEAKALGTDVV 382
Cdd:PRK13512 319 GFLGNNIVkffdYT---FASVGVKPNELKQFDYKMV 351
|
|
| PRK12844 |
PRK12844 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
6-104 |
4.19e-04 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 183787 [Multi-domain] Cd Length: 557 Bit Score: 42.82 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 6 DVAILGGGTGGYVAAIRAAQLGKSVVVIE-MDKLGGTCLHRGC---IPSKSLLRSAEVYAEIQESESYGIETTGVQLVFP 81
Cdd:PRK12844 8 DVVVVGSGGGGMCAALAAADSGLEPLIVEkQDKVGGSTAMSGGvlwLPNNPLMKAAGVPDSHEDALAYLDAVVGDQGPAS 87
|
90 100
....*....|....*....|...
gi 518751641 82 KVQlRKEAVVEQLHQGVQFLMRK 104
Cdd:PRK12844 88 SPE-RREAYLRAGPAMVSFLEHQ 109
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
5-33 |
6.48e-04 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 42.14 E-value: 6.48e-04
10 20
....*....|....*....|....*....
gi 518751641 5 CDVAILGGGTGGYVAAIRAAQLGKSVVVI 33
Cdd:PRK05329 3 FDVLVIGGGLAGLTAALAAAEAGKRVALV 31
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
9-42 |
7.62e-04 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 37.90 E-value: 7.62e-04
10 20 30
....*....|....*....|....*....|....*
gi 518751641 9 ILGGGTGGYVAAIRAAQLGKSVVVIEM-DKLGGTC 42
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKrDRLGGNA 35
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
1-171 |
3.46e-03 |
|
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: 39.85 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 1 MTISCDVAILGGGTGGYVAAIRAAQLGKSVVVIEM-DKLGGTCLHR---GC---IPSKSLL-------RSAEVYA---EI 63
Cdd:COG2072 3 ATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKaDDVGGTWRDNrypGLrldTPSHLYSlpffpnwSDDPDFPtgdEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518751641 64 QE-----SESYGIEttgvqlvfPKVQLRKEavVEQLHqgvqflmrknkiqvvkgkgriigpsiFSPRSGAVAVELEDGdm 138
Cdd:COG2072 83 LAyleayADKFGLR--------RPIRFGTE--VTSAR--------------------------WDEADGRWTVTTDDG-- 124
|
170 180 190
....*....|....*....|....*....|....*...
gi 518751641 139 ETVVSTHLIVATG--SRPRV--LPGLEP-DGKVILSSE 171
Cdd:COG2072 125 ETLTARFVVVATGplSRPKIpdIPGLEDfAGEQLHSAD 162
|
|
| PRK13800 |
PRK13800 |
fumarate reductase/succinate dehydrogenase flavoprotein subunit; |
3-34 |
4.24e-03 |
|
fumarate reductase/succinate dehydrogenase flavoprotein subunit;
Pssm-ID: 237512 [Multi-domain] Cd Length: 897 Bit Score: 39.83 E-value: 4.24e-03
10 20 30
....*....|....*....|....*....|..
gi 518751641 3 ISCDVAILGGGTGGYVAAIRAAQLGKSVVVIE 34
Cdd:PRK13800 12 LDCDVLVIGGGTAGTMAALTAAEHGANVLLLE 43
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
6-40 |
4.89e-03 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 39.13 E-value: 4.89e-03
10 20 30
....*....|....*....|....*....|....*.
gi 518751641 6 DVAILGGGTGGYVAAIRAAQLGKSVVVIEM-DKLGG 40
Cdd:COG1231 9 DVVIVGAGLAGLAAARELRKAGLDVTVLEArDRVGG 44
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
7-74 |
5.10e-03 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 39.47 E-value: 5.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518751641 7 VAILGGGTGGYVAAIRAAQLGKSVVVIEM-DKLGGTcLHRGcIPSKSLLRsAEVYAEIQESESYGIETT 74
Cdd:PRK12771 140 VAVIGGGPAGLSAAYHLRRMGHAVTIFEAgPKLGGM-MRYG-IPAYRLPR-EVLDAEIQRILDLGVEVR 205
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
6-69 |
5.60e-03 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 39.25 E-value: 5.60e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518751641 6 DVAILGGGTGGYVAAIRAAQLGKSVVVIE-MDKLGGTCLHRGC---IPSKSLLRSAEVYAEIQESESY 69
Cdd:PRK07843 9 DVVVVGSGAAGMVAALTAAHRGLSTVVVEkAPHYGGSTARSGGgvwIPNNEVLKRAGVPDTPEAARTY 76
|
|
| PRK08275 |
PRK08275 |
putative oxidoreductase; Provisional |
2-37 |
6.13e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 181346 [Multi-domain] Cd Length: 554 Bit Score: 38.88 E-value: 6.13e-03
10 20 30
....*....|....*....|....*....|....*.
gi 518751641 2 TISCDVAILGGGTGGYVAAIRAAQLGKSVVVIEMDK 37
Cdd:PRK08275 7 EVETDILVIGGGTAGPMAAIKAKERNPALRVLLLEK 42
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
3-40 |
7.76e-03 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 38.35 E-value: 7.76e-03
10 20 30
....*....|....*....|....*....|....*...
gi 518751641 3 ISCDVAILGGGTGGYVAAIRAAQLGKSVVVIEMDKLGG 40
Cdd:COG0665 1 ATADVVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGS 38
|
|
| |
