|
Name |
Accession |
Description |
Interval |
E-value |
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
5-466 |
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: 587.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 5 IDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKnETLGGTCLNVGCIPSKALLNNSHYYHMAHgtDFASRGIEMSEVRLN 84
Cdd:COG1249 2 KDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEK-GRLGGTCLNVGCIPSKALLHAAEVAHEAR--HAAEFGISAGAPSVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 85 LDKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATkadgGTQVIDTKNILIATGSEVTPFPGITIDEDT 164
Cdd:COG1249 79 WAALMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVT----GGETLTADHIVIATGSRPRVPPIPGLDEVR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 165 IVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGvGIDMEISKNFQRILQKQGFKFKLNTKVT 244
Cdd:COG1249 155 VLTSDEALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLP-GEDPEISEALEKALEKEGIDILTGAKVT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 245 GATKKSDGkidVSIEAASGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAG 324
Cdd:COG1249 234 SVEKTGDG---VTVTLEDGGGEEAVEADKVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRTSVPGIYAIGDVTGG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 325 PMLAHKAEDEGIICVEGMAGGAVH-IDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGM 403
Cdd:COG1249 311 PQLAHVASAEGRVAAENILGKKPRpVDYRAIPSVVFTDPEIASVGLTEEEAREAGIDVKVGKFPFAANGRALALGETEGF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
1ZMC_D 404 VKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAA 466
Cdd:COG1249 391 VKLIADAETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAALAL 453
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
8-474 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 568.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 8 DVTVIGSGPGGYVAAIKAAQLGFKTVCIE--KNET----LGGTCLNVGCIPSKALLNNSHYYHMAhGTDFASRGIEMSEV 81
Cdd:PRK06327 6 DVVVIGAGPGGYVAAIRAAQLGLKVACIEawKNPKgkpaLGGTCLNVGCIPSKALLASSEEFENA-GHHFADHGIHVDGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 82 RLNLDKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQV-TATKADG-GTQVIDTKNILIATGSEVTPFPGIT 159
Cdd:PRK06327 85 KIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVGKTDAgYEIKVTGeDETVITAKHVIIATGSEPRHLPGVP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 160 IDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHVggvgiDMEISKNFQRILQKQGF 235
Cdd:PRK06327 165 FDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEalpaFLAAA-----DEQVAKEAAKAFTKQGL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 236 KFKLNTKVtGATKKSDGKIDVSIEAASGgKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNI 315
Cdd:PRK06327 240 DIHLGVKI-GEIKTGGKGVSVAYTDADG-EAQTLEVDKLIVSIGRVPNTDGLGLEAVGLKLDERGFIPVDDHCRTNVPNV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 316 YAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAK 395
Cdd:PRK06327 318 YAIGDVVRGPMLAHKAEEEGVAVAERIAGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLKAEGVEYKAGKFPFMANGRAL 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1ZMC_D 396 TNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAASfGKSINF 474
Cdd:PRK06327 398 AMGEPDGFVKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEVWHEAALAVD-KRPLHF 475
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
8-473 |
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: 559.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 8 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKnETLGGTCLNVGCIPSKALLNNSHYYH-MAHGTDFasrGIEMSEVRLNLD 86
Cdd:TIGR01350 3 DVIVIGGGPGGYVAAIRAAQLGLKVALVEK-EYLGGTCLNVGCIPTKALLHSAEVYDeIKHAKDL---GIEVENVSVDWE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 87 KMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATKaDGGTQVIDTKNILIATGSEVTPFPG-ITIDEDTI 165
Cdd:TIGR01350 79 KMQKRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTG-ENGEETLEAKNIIIATGSRPRSLPGpFDFDGKVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 166 VSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGvGIDMEISKNFQRILQKQGFKFKLNTKVTG 245
Cdd:TIGR01350 158 ITSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILP-GEDAEVSKVLQKALKKKGVKILTNTKVTA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 246 ATKKSDGkidVSIEAaSGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGP 325
Cdd:TIGR01350 237 VEKNDDQ---VTYEN-KGGETETLTGEKVLVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDVIGGP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 326 MLAHKAEDEGIICVEGMAGGA-VHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMV 404
Cdd:TIGR01350 313 MLAHVASHEGIVAAENIAGKEpAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGYDVKIGKFPFAANGKALALGETDGFV 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1ZMC_D 405 KILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAAsFGKSIN 473
Cdd:TIGR01350 393 KIIADKKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEAIKEAALAA-LGKPIH 460
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
3-474 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 537.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 3 QPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKnETLGGTCLNVGCIPSKALLNNSHYYH-MAHGTDFasrGIEMSEV 81
Cdd:PRK06416 1 FAFEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEK-EKLGGTCLNRGCIPSKALLHAAERADeARHSEDF---GIKAENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 82 RLNLDKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATKADGGtQVIDTKNILIATGSEVTPFPGITID 161
Cdd:PRK06416 77 GIDFKKVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDGE-QTYTAKNIILATGSRPRELPGIEID 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 162 EDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGvGIDMEISKNFQRILQKQGFKFKLNT 241
Cdd:PRK06416 156 GRVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILP-GEDKEISKLAERALKKRGIKIKTGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 242 KVTGATKKSDGkIDVSIEAasGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDpRGRIPVNTRFQTKIPNIYAIGDV 321
Cdd:PRK06416 235 KAKKVEQTDDG-VTVTLED--GGKEETLEADYVLVAVGRRPNTENLGLEELGVKTD-RGFIEVDEQLRTNVPNIYAIGDI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 322 VAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTD 401
Cdd:PRK06416 311 VGGPMLAHKASAEGIIAAEAIAGNPHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFDVKVVKFPFAGNGKALALGETD 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1ZMC_D 402 GMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAASfGKSINF 474
Cdd:PRK06416 391 GFVKLIFDKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEALGEAALAAA-GKPLHA 462
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
5-468 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 535.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 5 IDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKnETLGGTCLNVGCIPSKALLNNSHYYHMAHgtDFASRGIEMSEVRLN 84
Cdd:PRK06292 2 EKYDVIVIGAGPAGYVAARRAAKLGKKVALIEK-GPLGGTCLNVGCIPSKALIAAAEAFHEAK--HAEEFGIHADGPKID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 85 LDKMMEQKSTAVKALTGGIAH-LFKQNKVVHVNGYGKITGKNQVTAtkadgGTQVIDTKNILIATGSEVTPFPGIT-IDE 162
Cdd:PRK06292 79 FKKVMARVRRERDRFVGGVVEgLEKKPKIDKIKGTARFVDPNTVEV-----NGERIEAKNIVIATGSRVPPIPGVWlILG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 163 DTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGvGIDMEISKNFQRILQKQgFKFKLNTK 242
Cdd:PRK06292 154 DRLLTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILP-LEDPEVSKQAQKILSKE-FKIKLGAK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 243 VTGATKKSDGKIDVSIEaasGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVV 322
Cdd:PRK06292 232 VTSVEKSGDEKVEELEK---GGKTETIEADYVLVATGRRPNTDGLGLENTGIELDERGRPVVDEHTQTSVPGIYAAGDVN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 323 AGPMLAHKAEDEGIICVEGMAGG-AVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTD 401
Cdd:PRK06292 309 GKPPLLHEAADEGRIAAENAAGDvAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEVPFEAQGRARVMGKND 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
1ZMC_D 402 GMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAASF 468
Cdd:PRK06292 389 GFVKVYADKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRTALRDLFS 455
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
3-466 |
1.86e-106 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 324.03 E-value: 1.86e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 3 QPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKAL------LNNSHYYHMAHGTDFaSRGI 76
Cdd:PRK05249 2 HMYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGGGCTHTGTIPSKALreavlrLIGFNQNPLYSSYRV-KLRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 77 EMSEVRLNLDKMMeQKSTAVkaltggIAHLFKQNKVVHVNGYGKITGKNQVTATKADGGTQVIDTKNILIATGSEvtPF- 155
Cdd:PRK05249 81 TFADLLARADHVI-NKQVEV------RRGQYERNRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATGSR--PYr 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 156 -PGITIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVE-------FLghvggvgiDMEISKNFQ 227
Cdd:PRK05249 152 pPDVDFDHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINtrdrllsFL--------DDEISDALS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 228 RILQKQGFKFKLNTKVTGATKKSDGKIdvsIEAASGGKaevITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTR 307
Cdd:PRK05249 224 YHLRDSGVTIRHNEEVEKVEGGDDGVI---VHLKSGKK---IKADCLLYANGRTGNTDGLNLENAGLEADSRGQLKVNEN 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 308 FQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFP 387
Cdd:PRK05249 298 YQTAVPHIYAVGDVIGFPSLASASMDQGRIAAQHAVGEATAHLIEDIPTGIYTIPEISSVGKTEQELTAAKVPYEVGRAR 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1ZMC_D 388 FAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAA 466
Cdd:PRK05249 378 FKELARAQIAGDNVGMLKILFHRETLEILGVHCFGERATEIIHIGQAIMEQKGTIEYFVNTTFNYPTMAEAYRVAALDG 456
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
8-472 |
1.70e-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: 319.37 E-value: 1.70e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 8 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNeTLGGTCLNVGCIPSKALLNNSHYYHMAHGTdfaSRGIEMSEVRLNLDK 87
Cdd:TIGR02053 2 DLVIIGSGAAAFAAAIKAAELGASVAMVERG-PLGGTCVNVGCVPSKMLLRAAEVAHYARKP---PFGGLAATVAVDFGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 88 MMEQKSTAVKAL-TGGIAHLFKQNKVVHVNGYGKITGKNQVtatKADGGTQVIDTKNILIATGSE--VTPFPGItiDEDT 164
Cdd:TIGR02053 78 LLEGKREVVEELrHEKYEDVLSSYGVDYLRGRARFKDPKTV---KVDLGREVRGAKRFLIATGARpaIPPIPGL--KEAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 165 IVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHvggvgIDMEISKNFQRILQKQGFKFKLN 240
Cdd:TIGR02053 153 YLTSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQrsdrLLPR-----EEPEISAAVEEALAEEGIEVVTS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 241 TKVTGATKKSDGKIDVSIEAASGGKAEVitcDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGD 320
Cdd:TIGR02053 228 AQVKAVSVRGGGKIITVEKPGGQGEVEA---DELLVATGRRPNTDGLGLEKAGVKLDERGGILVDETLRTSNPGIYAAGD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 321 VVAGPMLAHKAEDEGIICVEGMAGGA-VHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNAD 399
Cdd:TIGR02053 305 VTGGLQLEYVAAKEGVVAAENALGGAnAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNVPRARINRD 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1ZMC_D 400 TDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREAnlAASFGKSI 472
Cdd:TIGR02053 385 TRGFIKLVAEPGTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGLKLA--AQTFYRDV 455
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
8-468 |
3.36e-102 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 313.29 E-value: 3.36e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 8 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNEtLGGTCLNVGCIPSKALLNNSHYYHMA-HGTDFasrGIEMS-EVRLNL 85
Cdd:PRK06370 7 DAIVIGAGQAGPPLAARAAGLGMKVALIERGL-LGGTCVNTGCVPTKTLIASARAAHLArRAAEY---GVSVGgPVSVDF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 86 DKMMEQKSTAVKALTGGIAHLFKQNKVVHV-NGYGKITGKNQVTAtkadgGTQVIDTKNILIATGSE--VTPFPGItiDE 162
Cdd:PRK06370 83 KAVMARKRRIRARSRHGSEQWLRGLEGVDVfRGHARFESPNTVRV-----GGETLRAKRIFINTGARaaIPPIPGL--DE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 163 DTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGvGIDMEISKNFQRILQKQGFKFKLNTK 242
Cdd:PRK06370 156 VGYLTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLP-REDEDVAAAVREILEREGIDVRLNAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 243 VTGATKKSDGKIdvsIEAASGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVV 322
Cdd:PRK06370 235 CIRVERDGDGIA---VGLDCNGGAPEITGSHILVAVGRVPNTDDLGLEAAGVETDARGYIKVDDQLRTTNPGIYAAGDCN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 323 AGPMLAHKAEDEGIICVEGMA-GGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTD 401
Cdd:PRK06370 312 GRGAFTHTAYNDARIVAANLLdGGRRKVSDRIVPYATYTDPPLARVGMTEAEARKSGRRVLVGTRPMTRVGRAVEKGETQ 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
1ZMC_D 402 GMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFReaNLAASF 468
Cdd:PRK06370 392 GFMKVVVDADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIP--TLAQAL 456
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
6-459 |
2.83e-80 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 256.24 E-value: 2.83e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 6 DADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNEtLGGTCLNVGCIPSKALLNNSHYYHMAH--GTDFasrGIEMSEVRL 83
Cdd:PRK06116 4 DYDLIVIGGGSGGIASANRAAMYGAKVALIEAKR-LGGTCVNVGCVPKKLMWYGAQIAEAFHdyAPGY---GFDVTENKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 84 NLDKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVtatKADGgtQVIDTKNILIATGSEVTP--FPGItid 161
Cdd:PRK06116 80 DWAKLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTV---EVNG--ERYTADHILIATGGRPSIpdIPGA--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 162 EDTIvSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAV----EFLGhvggvGIDMEISKNFQRILQKQGFKF 237
Cdd:PRK06116 152 EYGI-TSDGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFvrgdAPLR-----GFDPDIRETLVEEMEKKGIRL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 238 KLNTKVTGATKKSDGKIDVSIEaasggKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYA 317
Cdd:PRK06116 226 HTNAVPKAVEKNADGSLTLTLE-----DGETLTVDCLIWAIGREPNTDGLGLENAGVKLNEKGYIIVDEYQNTNVPGIYA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 318 IGDVVAGPMLAHKAEDEGIICVEGMAGG--AVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEY--KVGKFPFAANSR 393
Cdd:PRK06116 301 VGDVTGRVELTPVAIAAGRRLSERLFNNkpDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDnvKVYRSSFTPMYT 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1ZMC_D 394 AKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAF 459
Cdd:PRK06116 381 ALTGHRQPCLMKLVVVGKEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEF 446
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
8-467 |
2.47e-74 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 246.36 E-value: 2.47e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 8 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNE-TLGGTCLNVGCIPSKALL----------NNSHYYHMAHGTDFASRGI 76
Cdd:PTZ00153 118 DVGIIGCGVGGHAAAINAMERGLKVIIFTGDDdSIGGTCVNVGCIPSKALLyatgkyrelkNLAKLYTYGIYTNAFKNGK 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 77 EM---------SEVRLNLDKMMEQKSTAVKALTGGIAHLFKQNK-------VVHVNGYGKITGKNQVTATKADGGTQVid 140
Cdd:PTZ00153 198 NDpvernqlvaDTVQIDITKLKEYTQSVIDKLRGGIENGLKSKKfcknsehVQVIYERGHIVDKNTIKSEKSGKEFKV-- 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 141 tKNILIATGSevTPF--PGITIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGvGI 218
Cdd:PTZ00153 276 -KNIIIATGS--TPNipDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSPQLLP-LL 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 219 DMEISKNFQRILQK-QGFKFKLNTKVT-------------GATKKSDGKIDVSIEAASGGKAevITCDVLLVCIGRRPFT 284
Cdd:PTZ00153 352 DADVAKYFERVFLKsKPVRVHLNTLIEyvragkgnqpviiGHSERQTGESDGPKKNMNDIKE--TYVDSCLVATGRKPNT 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 285 KNLGLEELGIELDpRGRIPVNTRFQTK------IPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVH---------- 348
Cdd:PTZ00153 430 NNLGLDKLKIQMK-RGFVSVDEHLRVLredqevYDNIFCIGDANGKQMLAHTASHQALKVVDWIEGKGKEnvninvenwa 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 349 ---IDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFP--FAANSRA----------------------KTNADTD 401
Cdd:PTZ00153 509 skpIIYKNIPSVCYTTPELAFIGLTEKEAKELYPPDNVGVEIsfYKANSKVlcennisfpnnsknnsynkgkyNTVDNTE 588
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1ZMC_D 402 GMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAAS 467
Cdd:PTZ00153 589 GMVKIVYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDAAFKAIA 654
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
8-335 |
2.01e-70 |
|
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: 226.05 E-value: 2.01e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 8 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEknetLGGTCLNVGCIPSKALLNnshyyhmahgtdfasrGIEMSEVRLNLDK 87
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIE----DEGTCPYGGCVLSKALLG----------------AAEAPEIASLWAD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 88 MMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVtatkaDGGTQVIDTKNILIATGSE--VTPFPGIT---IDE 162
Cdd:pfam07992 62 LYKRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELV-----DGDGETITYDRLVIATGARprLPPIPGVElnvGFL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 163 DTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGvGIDMEISKNFQRILQKQGFKFKLNTK 242
Cdd:pfam07992 137 VRTLDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLR-AFDEEISAALEKALEKNGVEVRLGTS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 243 VTGATKKSDGKidvsieAASGGKAEVITCDVLLVCIGRRPftKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDV- 321
Cdd:pfam07992 216 VKEIIGDGDGV------EVILKDGTEIDADLVVVAIGRRP--NTELLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDCr 287
|
330
....*....|....
1ZMC_D 322 VAGPMLAHKAEDEG 335
Cdd:pfam07992 288 VGGPELAQNAVAQG 301
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
9-473 |
3.87e-70 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 232.73 E-value: 3.87e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 9 VTVIGSGPGGYVAAIKAAQLGFKTVCIEKNeTLGGTCLNVGCIPSKALLNNSHYYHMAHGTDFASrGIEMSEVRLNLDKM 88
Cdd:PRK13748 101 VAVIGSGGAAMAAALKAVEQGARVTLIERG-TIGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDG-GIAATVPTIDRSRL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 89 MEQKSTAVKALTG----GIAHLFKQNKVVHvnGYGKITGKNQVTATKADGGTQVIDTKNILIATGSE--VTPFPGITidE 162
Cdd:PRK13748 179 LAQQQARVDELRHakyeGILDGNPAITVLH--GEARFKDDQTLIVRLNDGGERVVAFDRCLIATGASpaVPPIPGLK--E 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 163 DTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHvggvgiDMEISKNFQRILQKQGFKFK 238
Cdd:PRK13748 255 TPYWTSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILArstlFFRE------DPAIGEAVTAAFRAEGIEVL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 239 LNTKVTgATKKSDGKIDVSIEAASggkaevITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAI 318
Cdd:PRK13748 329 EHTQAS-QVAHVDGEFVLTTGHGE------LRADKLLVATGRAPNTRSLALDAAGVTVNAQGAIVIDQGMRTSVPHIYAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 319 GDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNA 398
Cdd:PRK13748 402 GDCTDQPQFVYVAAAAGTRAAINMTGGDAALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRTLTLDNVPRALANF 481
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1ZMC_D 399 DTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREAnlAASFGKSIN 473
Cdd:PRK13748 482 DTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAALAIRNRMTVQELADQLFPYLTMVEGLKLA--AQTFNKDVK 554
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
11-461 |
4.00e-68 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 224.27 E-value: 4.00e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 11 VIGSGPGGYVAAIKAAQLGFKTVCIEKNETL-GGTCLNVGCIPSKALLNNSHYYHmahgtDFASrgiemsevrlnldkMM 89
Cdd:NF040477 8 IIGFGKAGKTLAATLAKAGWRVAIIEQSAQMyGGTCINIGCIPTKTLVHDAEQHQ-----DFST--------------AM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 90 EQKSTAVKALTGGIAH-LFKQNKVVHVNGYGKITGKNQVTATKADgGTQVIDTKNILIATGSEVT--PFPGITIDEDtIV 166
Cdd:NF040477 69 QRKSSVVGFLRDKNYHnLADLDNVDVINGRAEFIDNHTLRVFQAD-GEQELRGEKIFINTGAQSVlpPIPGLTTTPG-VY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 167 SSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGVGiDMEISKNFQRILQKQGFKFKLNTKVTGA 246
Cdd:NF040477 147 DSTGLLNLTQLPARLGILGGGYIGVEFASMFARFGSKVTIFEAAELFLPRE-DRDIAQAIATILQDQGVELILNAQVQRV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 247 TKKSDGkidVSIEAASGgkaeVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPM 326
Cdd:NF040477 226 SSHEGE---VQLETAEG----VLTVDALLVASGRKPATAGLQLQNAGVAVNERGAIVVDKYLRTTADNIWAMGDVTGGLQ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 327 LAHKAEDEGIICVEGMAG-GAVHI-DYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMV 404
Cdd:NF040477 299 FTYISLDDFRIVRDSLLGeGKRSTdDRQNVPYSVFMTPPLSRIGMTEEQARASGADIQVVTLPVAAIPRARVMNDTRGVL 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
1ZMC_D 405 KILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFRE 461
Cdd:NF040477 379 KAVVDNKTQRILGVSLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSESLND 435
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
8-459 |
1.27e-66 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 220.39 E-value: 1.27e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 8 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETL-GGTCLNVGCIPSKALlnnshyyhmahgtdfasrgIEMSEVRLNLD 86
Cdd:PRK07251 5 DLIVIGFGKAGKTLAAKLASAGKKVALVEESKAMyGGTCINIGCIPTKTL-------------------LVAAEKNLSFE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 87 KMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGkNQVTATKADGGTQVIDTKNILIATG--SEVTPFPGITiDEDT 164
Cdd:PRK07251 66 QVMATKNTVTSRLRGKNYAMLAGSGVDLYDAEAHFVS-NKVIEVQAGDEKIELTAETIVINTGavSNVLPIPGLA-DSKH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 165 IVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHVggvgiDMEISKNFQRILQKQGFKFKLN 240
Cdd:PRK07251 144 VYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDaastILPRE-----EPSVAALAKQYMEEDGITFLLN 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 241 TKVTgATKKSDGKIDVSIEAasggkaEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGD 320
Cdd:PRK07251 219 AHTT-EVKNDGDQVLVVTED------ETYRFDALLYATGRKPNTEPLGLENTDIELTERGAIKVDDYCQTSVPGVFAVGD 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 321 VVAGPMLAHKAEDEGIICVEGMAGGA--VHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNA 398
Cdd:PRK07251 292 VNGGPQFTYISLDDFRIVFGYLTGDGsyTLEDRGNVPTTMFITPPLSQVGLTEKEAKEAGLPYAVKELLVAAMPRAHVNN 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
1ZMC_D 399 DTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAF 459
Cdd:PRK07251 372 DLRGAFKVVVNTETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAENL 432
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
8-459 |
1.35e-65 |
|
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: 218.17 E-value: 1.35e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 8 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNEtLGGTCLNVGCIPSKALLNNSHYYHMAHgtDFASRGIEMS-EVRLNLD 86
Cdd:TIGR01421 4 DYLVIGGGSGGIASARRAAEHGAKALLVEAKK-LGGTCVNVGCVPKKVMWYASDLAERMH--DAADYGFYQNdENTFNWP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 87 KMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATKADggtqvIDTKNILIATGSEVTPFPGITIDEDTIv 166
Cdd:TIGR01421 81 ELKEKRDAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVNGRD-----YTAPHILIATGGKPSFPENIPGAELGT- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 167 SSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADvTAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGA 246
Cdd:TIGR01421 155 DSDGFFALEELPKRVVIVGAGYIAVELAGVLHGLGSE-THLVIRHERVLRSFDSMISETITEEYEKEGINVHKLSKPVKV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 247 TKKSDGKIDVSIEAASggkaEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPM 326
Cdd:TIGR01421 234 EKTVEGKLVIHFEDGK----SIDDVDELIWAIGRKPNTKGLGLENVGIKLNEKGQIIVDEYQNTNVPGIYALGDVVGKVE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 327 LAHKAEDEGIICVEGMAGGA--VHIDYNCVPSVIYTHPEVAWVGKSEEQ-LKEEGIE-YKVGKFPFAANSRAKTNADTDG 402
Cdd:TIGR01421 310 LTPVAIAAGRKLSERLFNGKtdDKLDYNNVPTVVFSHPPIGTIGLTEKEaIEKYGKEnIKVYNSSFTPMYYAMTSEKQKC 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
1ZMC_D 403 MVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAF 459
Cdd:TIGR01421 390 RMKLVCAGKEEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEEL 446
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
6-472 |
9.49e-64 |
|
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: 213.95 E-value: 9.49e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 6 DADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNET--------LGGTCLNVGCIPSKALLNNSHY-YHMAHGTDFASRGI 76
Cdd:TIGR01438 2 DYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPtplgtrwgIGGTCVNVGCIPKKLMHQAALLgQALKDSRNYGWKVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 77 EmsEVRLNLDKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATKADGGTQVIDTKNILIATGsEVTPFP 156
Cdd:TIGR01438 82 E--TVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATG-ERPRYP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 157 GITIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVeflghVGGV---GIDMEISKNFQRILQKQ 233
Cdd:TIGR01438 159 GIPGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVM-----VRSIllrGFDQDCANKVGEHMEEH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 234 GFKFKLNTKVTGATKKSDGKIDVSIEAASGGKAEVitcDVLLVCIGRRPFTKNLGLEELGIELDPR-GRIPVNTRFQTKI 312
Cdd:TIGR01438 234 GVKFKRQFVPIKVEQIEAKVLVEFTDSTNGIEEEY---DTVLLAIGRDACTRKLNLENVGVKINKKtGKIPADEEEQTNV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 313 PNIYAIGDVVAG-PMLAHKAEDEGIICVEGMAGGAVHI-DYNCVPSVIYTHPEVAWVGKSEEQ----LKEEGIEYKVGKF 386
Cdd:TIGR01438 311 PYIYAVGDILEDkPELTPVAIQAGRLLAQRLFKGSTVIcDYENVPTTVFTPLEYGACGLSEEKavekFGEENVEVFHSYF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 387 -PFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLA 465
Cdd:TIGR01438 391 wPLEWTIPSRDNHNKCYAKLVCNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTLSVT 470
|
....*..
1ZMC_D 466 ASFGKSI 472
Cdd:TIGR01438 471 KRSGQDI 477
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
6-459 |
7.06e-62 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 209.67 E-value: 7.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 6 DADVTVIGSGPGGYVAAIKAAQLG---------FKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYyhMAHGTDFASRGI 76
Cdd:PLN02507 25 DFDLFVIGAGSGGVRAARFSANFGakvgicelpFHPISSESIGGVGGTCVIRGCVPKKILVYGATF--GGEFEDAKNYGW 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 77 EMSE-VRLNLDKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATKADGGTQVIDTKNILIATGSEVTPf 155
Cdd:PLN02507 103 EINEkVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRYTAKHILIATGSRAQR- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 156 PGITIDEDTIVSSTgALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVeFLGHVGGVGIDMEISKNFQRILQKQGF 235
Cdd:PLN02507 182 PNIPGKELAITSDE-ALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLF-FRKELPLRGFDDEMRAVVARNLEGRGI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 236 KFKLNTKVTGATKKSDGkIDVSIEaasggKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNI 315
Cdd:PLN02507 260 NLHPRTNLTQLTKTEGG-IKVITD-----HGEEFVADVVLFATGRAPNTKRLNLEAVGVELDKAGAVKVDEYSRTNIPSI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 316 YAIGDVVAGPMLAHKAEDEGIICVEGMAGG-AVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEG---IEYKVGKFPFAAN 391
Cdd:PLN02507 334 WAIGDVTNRINLTPVALMEGTCFAKTVFGGqPTKPDYENVACAVFCIPPLSVVGLSEEEAVEQAkgdILVFTSSFNPMKN 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1ZMC_D 392 SRAKTNADTdgMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAF 459
Cdd:PLN02507 414 TISGRQEKT--VMKLIVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEF 479
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
9-462 |
6.59e-58 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 198.16 E-value: 6.59e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 9 VTVIGSGPGGYVAAIKAAQLGFKTVCIEkNETLGGTCLNVGCIPSKALLNNSHYY-HMAHGTDFASRGIEMSEVRLNLDK 87
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIE-RDGLGGAAVLTDCVPSKTLIATAEVRtELRRAAELGIRFIDDGEARVDLPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 88 MMEQkstaVKALT----GGIAHLFKQNKVVHVNGYGKIT----GKNQVTATKADGGTQVIDTKNILIATGSevTP--FPG 157
Cdd:PRK07845 83 VNAR----VKALAaaqsADIRARLEREGVRVIAGRGRLIdpglGPHRVKVTTADGGEETLDADVVLIATGA--SPriLPT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 158 ITIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGvGIDMEISKNFQRILQKQGFKF 237
Cdd:PRK07845 157 AEPDGERILTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLP-GEDADAAEVLEEVFARRGMTV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 238 KLNTKVTGATKKSDGkidVSIEAASGGKAEVITCdvlLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYA 317
Cdd:PRK07845 236 LKRSRAESVERTGDG---VVVTLTDGRTVEGSHA---LMAVGSVPNTAGLGLEEAGVELTPSGHITVDRVSRTSVPGIYA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 318 IGDVVAGPMLAHKAEDEGIICVEGMAGGAVH-IDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKT 396
Cdd:PRK07845 310 AGDCTGVLPLASVAAMQGRIAMYHALGEAVSpLRLKTVASNVFTRPEIATVGVSQAAIDSGEVPARTVMLPLATNPRAKM 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1ZMC_D 397 NADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREA 462
Cdd:PRK07845 390 SGLRDGFVKLFCRPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYPSLSGSITEA 455
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
11-461 |
1.19e-56 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 194.08 E-value: 1.19e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 11 VIGSGPGGYVAAIKAAQLGFKTVCIEK-NETLGGTCLNVGCIPSKALLNNSHYYhmahgTDFAsrgiemsevrlnldKMM 89
Cdd:PRK08010 8 IIGFGKAGKTLAVTLAKAGWRVALIEQsNAMYGGTCINIGCIPTKTLVHDAQQH-----TDFV--------------RAI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 90 EQKSTAVKALTGGIAH-LFKQNKVVHVNGYGKITGKNQVTATKADGgTQVIDTKNILIATGSE--VTPFPGITIDEDtIV 166
Cdd:PRK08010 69 QRKNEVVNFLRNKNFHnLADMPNIDVIDGQAEFINNHSLRVHRPEG-NLEIHGEKIFINTGAQtvVPPIPGITTTPG-VY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 167 SSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHVggvgiDMEISKNFQRILQKQGFKFKLNTK 242
Cdd:PRK08010 147 DSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEaaslFLPRE-----DRDIADNIATILRDQGVDIILNAH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 243 VTGATKKsDGKIDVSIEAASggkaevITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVV 322
Cdd:PRK08010 222 VERISHH-ENQVQVHSEHAQ------LAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKYLHTTADNIWAMGDVT 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 323 AGPMLAHKAEDEGIICVEGMAGGAVHI--DYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADT 400
Cdd:PRK08010 295 GGLQFTYISLDDYRIVRDELLGEGKRStdDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDT 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
1ZMC_D 401 DGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFRE 461
Cdd:PRK08010 375 RGVLKAIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLND 435
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
8-468 |
4.96e-55 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 190.17 E-value: 4.96e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 8 DVTVIGSGPGGyvaAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLnnsHYYHMAHGTDFASR-GIEMSEVRLNLD 86
Cdd:PRK07846 3 DLIIIGTGSGN---SILDERFADKRIAIVEKGTFGGTCLNVGCIPTKMFV---YAADVARTIREAARlGVDAELDGVRWP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 87 KMMEQKSTAVKAL-TGGIAHLFKQNKVVHV-NGYGKITGknQVTATKADGGtqVIDTKNILIATGSEVTPFPGITIDEDT 164
Cdd:PRK07846 77 DIVSRVFGRIDPIaAGGEEYRGRDTPNIDVyRGHARFIG--PKTLRTGDGE--EITADQVVIAAGSRPVIPPVIADSGVR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 165 IVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHvggvgIDMEISKNFQRILQKQgFKFKLN 240
Cdd:PRK07846 153 YHTSDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNrsgrLLRH-----LDDDISERFTELASKR-WDVRLG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 241 TKVTGATKKSDGkidVSIEAASGgkaEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGD 320
Cdd:PRK07846 227 RNVVGVSQDGSG---VTLRLDDG---STVEADVLLVATGRVPNGDLLDAAAAGVDVDEDGRVVVDEYQRTSAEGVFALGD 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 321 VVAGPMLAHKAEDEGIICVEGMAGGA--VHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNA 398
Cdd:PRK07846 301 VSSPYQLKHVANHEARVVQHNLLHPDdlIASDHRFVPAAVFTHPQIASVGLTENEARAAGLDITVKVQNYGDVAYGWAME 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1ZMC_D 399 DTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCH-AHPTLSEAFREANLAASF 468
Cdd:PRK07846 381 DTTGFVKLIADRDTGRLLGAHIIGPQASTLIQPLIQAMSFGLDAREMARGQYwIHPALPEVVENALLGLDL 451
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
354-462 |
2.62e-53 |
|
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: 174.66 E-value: 2.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 354 VPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAA 433
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGEVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQEAA 80
|
90 100
....*....|....*....|....*....
1ZMC_D 434 LALEYGASCEDIARVCHAHPTLSEAFREA 462
Cdd:pfam02852 81 LAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
8-457 |
3.76e-53 |
|
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: 185.95 E-value: 3.76e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 8 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNET---------LGGTCLNVGCIPSKALLNNSHYyhMAHGTDFASRGIEM 78
Cdd:TIGR01423 5 DLVVIGAGSGGLEAGWNAATLYKKRVAVVDVQThhgppfyaaLGGTCVNVGCVPKKLMVTGAQY--MDTLRESAGFGWEF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 79 --SEVRLNLDKMMEQKSTAVKALTGGIAHLFKQNK-VVHVNGYGKITGKNQVTATK-ADGGTQV---IDTKNILIATGS- 150
Cdd:TIGR01423 83 drSSVKANWKALIAAKNKAVLDINKSYEGMFADTEgLTFFLGWGALEDKNVVLVREsADPKSAVkerLQAEHILLATGSw 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 151 -EVTPFPGItideDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSV---WQRLGADVTaVEFLGHVGGVGIDMEISKNF 226
Cdd:TIGR01423 163 pQMLGIPGI----EHCISSNEAFYLDEPPRRVLTVGGGFISVEFAGIfnaYKPRGGKVT-LCYRNNMILRGFDSTLRKEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 227 QRILQKQGFKFKLNTKVTGATKKSDGKIDVSIEaaSGGKAEVitcDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNT 306
Cdd:TIGR01423 238 TKQLRANGINIMTNENPAKVTLNADGSKHVTFE--SGKTLDV---DVVMMAIGRVPRTQTLQLDKVGVELTKKGAIQVDE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 307 RFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVH-IDYNCVPSVIYTHPEVAWVGKSEEQL--KEEGIEYKV 383
Cdd:TIGR01423 313 FSRTNVPNIYAIGDVTDRVMLTPVAINEGAAFVDTVFGNKPRkTDHTRVASAVFSIPPIGTCGLVEEDAakKFEKVAVYE 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1ZMC_D 384 GKF-PFAANSRAKTNADTdgMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSE 457
Cdd:TIGR01423 393 SSFtPLMHNISGSKYKKF--VAKIVTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAE 465
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
6-471 |
1.03e-49 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 176.94 E-value: 1.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 6 DADVTVIGSGPGGYVAAIKAAQLGFKTVCIE--KNET------LGGTCLNVGCIPSKALlnnsHYY-HMAH--GTDFASR 74
Cdd:PTZ00052 5 MYDLVVIGGGSGGMAAAKEAAAHGKKVALFDyvKPSTqgtkwgLGGTCVNVGCVPKKLM----HYAaNIGSifHHDSQMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 75 GIEMSEVrLNLDKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVtATKADGGTQVIDTKNILIATGSEvtp 154
Cdd:PTZ00052 81 GWKTSSS-FNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTV-SYGDNSQEETITAKYILIATGGR--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 155 fPGITID----EDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVefLGHVGGVGIDMEISKNFQRIL 230
Cdd:PTZ00052 156 -PSIPEDvpgaKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVA--VRSIPLRGFDRQCSEKVVEYM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 231 QKQGFKFKlNTKVTGATKKSDGKIDVSIeaaSGGKAEVItcDVLLVCIGRRPFTKNLGLEELGIELDPRGRIpVNTRFQT 310
Cdd:PTZ00052 233 KEQGTLFL-EGVVPINIEKMDDKIKVLF---SDGTTELF--DTVLYATGRKPDIKGLNLNAIGVHVNKSNKI-IAPNDCT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 311 KIPNIYAIGDVVAG-PMLAHKAEDEGIICVEGMAGGAVHI-DYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPF 388
Cdd:PTZ00052 306 NIPNIFAVGDVVEGrPELTPVAIKAGILLARRLFKQSNEFiDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 389 AANS------------RAKTNA-DTD----GMVKILGQKSTD-RVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCH 450
Cdd:PTZ00052 386 EFNTleiaavhrekheRARKDEyDFDvssnCLAKLVCVKSEDnKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIG 465
|
490 500
....*....|....*....|.
1ZMC_D 451 AHPTLSEAFREANLAASFGKS 471
Cdd:PTZ00052 466 IHPTDAEVFMNLSVTRRSGES 486
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
6-459 |
1.12e-48 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 175.45 E-value: 1.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 6 DADVTVIGSGPGG---------YVAAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHmahgtDF-ASRG 75
Cdd:PLN02546 79 DFDLFTIGAGSGGvrasrfasnFGASAAVCELPFATISSDTLGGVGGTCVLRGCVPKKLLVYASKYSH-----EFeESRG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 76 IEM---SEVRLNLDKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTAtkaDGgtQVIDTKNILIATGSEv 152
Cdd:PLN02546 154 FGWkyeTEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDV---DG--KLYTARNILIAVGGR- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 153 tPF----PGItideDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVtaveflgHV----GGV--GIDMEI 222
Cdd:PLN02546 228 -PFipdiPGI----EHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDV-------HVfirqKKVlrGFDEEV 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 223 SKNFQRILQKQGFKFKLNTKVTGATKKSDGKIDVSIEAAS-GGKAEVitcdvlLVCIGRRPFTKNLGLEELGIELDPRGR 301
Cdd:PLN02546 296 RDFVAEQMSLRGIEFHTEESPQAIIKSADGSLSLKTNKGTvEGFSHV------MFATGRKPNTKNLGLEEVGVKMDKNGA 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 302 IPVNTRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGG-AVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIE 380
Cdd:PLN02546 370 IEVDEYSRTSVPSIWAVGDVTDRINLTPVALMEGGALAKTLFGNePTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYGD 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 381 YKVgkfpFAANSRAkTNADTDGM-----VKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTL 455
Cdd:PLN02546 450 VDV----FTANFRP-LKATLSGLpdrvfMKLIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTA 524
|
....
1ZMC_D 456 SEAF 459
Cdd:PLN02546 525 AEEF 528
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
8-465 |
4.94e-48 |
|
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: 171.48 E-value: 4.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 8 DVTVIGSGPGGyvaAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLnnsHYYHMAHGTDFASR-GIEMSEVRLNLD 86
Cdd:TIGR03452 4 DLIIIGTGSGN---SIPDPRFADKRIAIVEKGTFGGTCLNVGCIPTKMFV---YAAEVAQSIGESARlGIDAEIDSVRWP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 87 KMMEQK-STAVKALTGGIAHLFKQNKVVHVNGY-GKITGKNQVTATKADGGTqvIDTKNILIATGSEVTPFPGITIDEDT 164
Cdd:TIGR03452 78 DIVSRVfGDRIDPIAAGGEDYRRGDETPNIDVYdGHARFVGPRTLRTGDGEE--ITGDQIVIAAGSRPYIPPAIADSGVR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 165 IVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAV----EFLGHvggvgIDMEISKNFQRILQKQgFKFKLN 240
Cdd:TIGR03452 156 YHTNEDIMRLPELPESLVIVGGGYIAAEFAHVFSALGTRVTIVnrstKLLRH-----LDEDISDRFTEIAKKK-WDIRLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 241 TKVTGATKKSDGkidVSIEAASGgkaEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGD 320
Cdd:TIGR03452 230 RNVTAVEQDGDG---VTLTLDDG---STVTADVLLVATGRVPNGDLLDAEAAGVEVDEDGRIKVDEYGRTSARGVWALGD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 321 VVAGPMLAHKAEDEGIICVEGMA--GGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEG--IEYKVGKFPFAANSRAKt 396
Cdd:TIGR03452 304 VSSPYQLKHVANAEARVVKHNLLhpNDLRKMPHDFVPSAVFTHPQIATVGLTEQEAREAGhdITVKIQNYGDVAYGWAM- 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 397 nADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCH-AHPTLSEAFREANLA 465
Cdd:TIGR03452 383 -EDTTGFCKLIADRDTGKLLGAHIIGPQASSLIQPLITAMAFGLDAREMARKQYwIHPALPEVVENALLG 451
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
5-459 |
9.88e-44 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 161.71 E-value: 9.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 5 IDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKnETLGGTCLNVGCIPSKALLNNSHYYHMAHgtDFASRGIEMSEVrLN 84
Cdd:PTZ00058 47 MVYDLIVIGGGSGGMAAARRAARNKAKVALVEK-DYLGGTCVNVGCVPKKIMFNAASIHDILE--NSRHYGFDTQFS-FN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 85 LDKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATK------------------------ADGGTQVID 140
Cdd:PTZ00058 123 LPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLIKKvsqvdgeadesdddevtivsagvsQLDDGQVIE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 141 TKNILIATGSEvTPFPGITIDEDTIvSSTGALSLKKvPEKMVVIGAGVIGVELGSVWQRLGADvTAVEFLGHVGGVGIDM 220
Cdd:PTZ00058 203 GKNILIAVGNK-PIFPDVKGKEFTI-SSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAE-SYIFARGNRLLRKFDE 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 221 EISKNFQRILQKQGFKFKLNTKVTGATKksDGKIDVSIEAASGGKAEVITCdvLLVCIGRRPFTKNLGLEELGIeLDPRG 300
Cdd:PTZ00058 279 TIINELENDMKKNNINIITHANVEEIEK--VKEKNLTIYLSDGRKYEHFDY--VIYCVGRSPNTEDLNLKALNI-KTPKG 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 301 RIPVNTRFQTKIPNIYAIGDVVAGP---------MLAHKAEDEGIICVEGMAGGAVH----------------------- 348
Cdd:PTZ00058 354 YIKVDDNQRTSVKHIYAVGDCCMVKknqeiedlnLLKLYNEEPYLKKKENTSGESYYnvqltpvainagrlladrlfgpf 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 349 ---IDYNCVPSVIYTHPEVAWVGKSEEQL-----KEEGIEYK-------VGKFPFAANSRAKTnadtdgMVKILGQKSTD 413
Cdd:PTZ00058 434 srtTNYKLIPSVIFSHPPIGTIGLSEQEAidiygKENVKIYEsrftnlfFSVYDMDPAQKEKT------YLKLVCVGKEE 507
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
1ZMC_D 414 RVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAF 459
Cdd:PTZ00058 508 LIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIHPTAAEEF 553
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
124-358 |
9.14e-30 |
|
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: 9.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 124 KNQVTATKADGGTQVIDTKN--------ILIATGSE--VTPFPGITIDE-DTIVSSTGALSLKKV-----PEKMVVIGAG 187
Cdd:COG0446 54 RTGTEVTAIDPEAKTVTLRDgetlsydkLVLATGARprPPPIPGLDLPGvFTLRTLDDADALREAlkefkGKRAVVIGGG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 188 VIGVELGSVWQRLGADVTAVEFLGHVGGVgIDMEISKNFQRILQKQGFKFKLNTKVTGAtkksDGKIDVSIEAASGgkaE 267
Cdd:COG0446 134 PIGLELAEALRKRGLKVTLVERAPRLLGV-LDPEMAALLEEELREHGVELRLGETVVAI----DGDDKVAVTLTDG---E 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 268 VITCDVLLVCIGRRPftkNLGL-EELGIELDPRGRIPVNTRFQTKIPNIYAIGDVV----------AGPMLAHKAEDEGI 336
Cdd:COG0446 206 EIPADLVVVAPGVRP---NTELaKDAGLALGERGWIKVDETLQTSDPDVYAAGDCAevphpvtgktVYIPLASAANKQGR 282
|
250 260
....*....|....*....|..
1ZMC_D 337 ICVEGMAGGAvhIDYNCVPSVI 358
Cdd:COG0446 283 VAAENILGGP--APFPGLGTFI 302
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
8-326 |
1.17e-26 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 109.44 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 8 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNEtLGGTCLNVGCIpskallNNshYYHMAHGTdfasRGIEMsevrlnLDK 87
Cdd:COG0492 2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEGGE-PGGQLATTKEI------EN--YPGFPEGI----SGPEL------AER 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 88 MMEQ-KSTAVKALTGGIAHLFKQNKVVHVngygkitgknqvtatKADGGTqVIDTKNILIATGSEVT--PFPGITIDEDT 164
Cdd:COG0492 63 LREQaERFGAEILLEEVTSVDKDDGPFRV---------------TTDDGT-EYEAKAVIIATGAGPRklGLPGEEEFEGR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 165 IVSSTGALSLKKVP-EKMVVIGAGVIGVELGSVWQRLGADVTAVeflgHVGGvgiDMEISKNFQ-RILQKQGFKFKLNTK 242
Cdd:COG0492 127 GVSYCATCDGFFFRgKDVVVVGGGDSALEEALYLTKFASKVTLI----HRRD---ELRASKILVeRLRANPKIEVLWNTE 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 243 VTGAtkKSDGKID-VSIEAASGGKAEVITCDVLLVCIGRRPftkNLGL-EELGIELDPRGRIPVNTRFQTKIPNIYAIGD 320
Cdd:COG0492 200 VTEI--EGDGRVEgVTLKNVKTGEEKELEVDGVFVAIGLKP---NTELlKGLGLELDEDGYIVVDEDMETSVPGVFAAGD 274
|
....*.
1ZMC_D 321 VVAGPM 326
Cdd:COG0492 275 VRDYKY 280
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
145-347 |
1.49e-22 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 99.06 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 145 LIATGSE--VTPFPGI---------TIDE-DTIVSSTGAlslkkvPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGH 212
Cdd:COG1251 103 VLATGSRprVPPIPGAdlpgvftlrTLDDaDALRAALAP------GKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPR 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 213 VGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGKidvSIEAASGgkaEVITCDVLLVCIGRRPftkNLGL-EE 291
Cdd:COG1251 177 LLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVT---GVRLADG---EELPADLVVVAIGVRP---NTELaRA 247
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
1ZMC_D 292 LGIELDpRGrIPVNTRFQTKIPNIYAIGDVVA-------GPMLAH--KAEDEGIICVEGMAGGAV 347
Cdd:COG1251 248 AGLAVD-RG-IVVDDYLRTSDPDIYAAGDCAEhpgpvygRRVLELvaPAYEQARVAAANLAGGPA 310
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
120-453 |
1.25e-16 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 82.01 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 120 KITGKNQVTatkadgGTQVIDTKNIL-IATG--SEVTPFPGITIDE-DTIVSSTGALSLKKVPEK-----MVVIGAGVIG 190
Cdd:PRK09564 88 TITVKNLKT------GSIFNDTYDKLmIATGarPIIPPIKNINLENvYTLKSMEDGLALKELLKDeeiknIVIIGAGFIG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 191 VELGSVWQRLGADVTAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVtgatKKSDGKIDVSIEAASGGKAEVit 270
Cdd:PRK09564 162 LEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHLNEFV----KSLIGEDKVEGVVTDKGEYEA-- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 271 cDVLLVCIGRRPFTKnlGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGD-------VVAGPM---LAHKAEDEGIICVE 340
Cdd:PRK09564 236 -DVVIVATGVKPNTE--FLEDTGLKTLKNGAIIVDEYGETSIENIYAAGDcatiyniVSNKNVyvpLATTANKLGRMVGE 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 341 GMAGGAVH----IDYNCVPSVIYthpEVAWVGKSEEQLKEEGIEYKVgKFPFAANSRAKTNADTDGMVKILGQKSTDRVL 416
Cdd:PRK09564 313 NLAGRHVSfkgtLGSACIKVLDL---EAARTGLTEEEAKKLGIDYKT-VFIKDKNHTNYYPGQEDLYVKLIYEADTKVIL 388
|
330 340 350 360
....*....|....*....|....*....|....*....|
1ZMC_D 417 GAHILGP-GAGEMVNEAALALEYGASCEDIARV--CHAHP 453
Cdd:PRK09564 389 GGQIIGKkGAVLRIDALAVAIYAKLTTQELGMMdfCYAPP 428
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
7-340 |
2.12e-16 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 80.56 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 7 ADVTVIGSGPGGYVAAIKAAQLGFKTVCIekneTLggtclnvgcIpSKallNNSHYY-HMAHGtdFASRGIEMSEVRLNL 85
Cdd:COG1252 2 KRIVIVGGGFAGLEAARRLRKKLGGDAEV----TL---------I-DP---NPYHLFqPLLPE--VAAGTLSPDDIAIPL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 86 DKMMEQKSTAvkaltggiahlFKQNKVVHVNgygkiTGKNQVTAtkADGGTQVIDTknILIATGSEVTPF--PGI----- 158
Cdd:COG1252 63 RELLRRAGVR-----------FIQGEVTGID-----PEARTVTL--ADGRTLSYDY--LVIATGSVTNFFgiPGLaehal 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 159 ---TIDE-----DTIVSstgALSLKKVPEKM--VVIGAGVIGVEL-GSVWQRLG------------ADVTAVEFLGHVGG 215
Cdd:COG1252 123 plkTLEDalalrERLLA---AFERAERRRLLtiVVVGGGPTGVELaGELAELLRkllrypgidpdkVRITLVEAGPRILP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 216 vGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSdgkidvsIEAASGgkaEVITCDVLLVCIGRR--PFTKNLGLEelg 293
Cdd:COG1252 200 -GLGEKLSEAAEKELEKRGVEVHTGTRVTEVDADG-------VTLEDG---EEIPADTVIWAAGVKapPLLADLGLP--- 265
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
1ZMC_D 294 ieLDPRGRIPVNTRFQTK-IPNIYAIGDVVAG--------PMLAHKAEDEGIICVE 340
Cdd:COG1252 266 --TDRRGRVLVDPTLQVPgHPNVFAIGDCAAVpdpdgkpvPKTAQAAVQQAKVLAK 319
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
180-253 |
5.71e-16 |
|
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: 72.62 E-value: 5.71e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1ZMC_D 180 KMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGvGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGK 253
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLP-GFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGV 73
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
135-320 |
9.69e-15 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 75.72 E-value: 9.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 135 GTQVIDTKNILIATGSE--VTPFPGitiDEDTIV--------SSTGALSLKKvpeKMVVIGAGVIGVELGSVWQRLGADV 204
Cdd:PRK04965 94 QGNQWQYDKLVLATGASafVPPIPG---RELMLTlnsqqeyrAAETQLRDAQ---RVLVVGGGLIGTELAMDLCRAGKAV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 205 TAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGkidVSIEAASGgkaEVITCDVLLVCIGRRPft 284
Cdd:PRK04965 168 TLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSG---IRATLDSG---RSIEVDAVIAAAGLRP-- 239
|
170 180 190
....*....|....*....|....*....|....*..
1ZMC_D 285 kNLGL-EELGIELDpRGrIPVNTRFQTKIPNIYAIGD 320
Cdd:PRK04965 240 -NTALaRRAGLAVN-RG-IVVDSYLQTSAPDIYALGD 273
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
161-322 |
1.71e-14 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 75.20 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 161 DEDTIVSSTGALSLKKVPekmvVIGAGVIGVE-LGSVWQRlGADVTAVEFLGHVGGVgIDMEISKNFQRILQKQGFKFKL 239
Cdd:PRK13512 135 DTDAIDQFIKANQVDKAL----VVGAGYISLEvLENLYER-GLHPTLIHRSDKINKL-MDADMNQPILDELDKREIPYRL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 240 NTKVTgatkksdgKIDVSIEAASGGKAEviTCDVLLVCIGRRPFTKNLglEELGIELDPRGRIPVNTRFQTKIPNIYAIG 319
Cdd:PRK13512 209 NEEID--------AINGNEVTFKSGKVE--HYDMIIEGVGTHPNSKFI--ESSNIKLDDKGFIPVNDKFETNVPNIYAIG 276
|
...
1ZMC_D 320 DVV 322
Cdd:PRK13512 277 DII 279
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
263-335 |
1.03e-11 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 66.17 E-value: 1.03e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1ZMC_D 263 GGKAEVITCDVLLVCIGRRPfTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPMLAHKAEDEG 335
Cdd:PRK12770 267 PGSEFVLEADTVVFAIGEIP-TPPFAKECLGIELNRKGEIVVDEKHMTSREGVFAAGDVVTGPSKIGKAIKSG 338
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
120-323 |
1.10e-11 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 67.16 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 120 KITGKNQVTATKAdGGTQVIDTknILIATGSE--VTPFPGI---------TIDE-DTIvsstgaLSLKKVPEKMVVIGAG 187
Cdd:TIGR02374 79 QIDTDQKQVITDA-GRTLSYDK--LILATGSYpfILPIPGAdkkgvyvfrTIEDlDAI------MAMAQRFKKAAVIGGG 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 188 VIGVELGSVWQRLGADVTAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKksDGKIDvSIEAASGgkaE 267
Cdd:TIGR02374 150 LLGLEAAVGLQNLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVG--ATKAD-RIRFKDG---S 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
1ZMC_D 268 VITCDVLLVCIGRRPFTknlgleELGIE--LDPRGRIPVNTRFQTKIPNIYAIGDVVA 323
Cdd:TIGR02374 224 SLEADLIVMAAGIRPND------ELAVSagIKVNRGIIVNDSMQTSDPDIYAVGECAE 275
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
88-321 |
2.53e-11 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 65.33 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 88 MMEQKSTAVKALTGgiAHLFKQNKV-VHVNGYGKITGKNQVTATKADGGTQVIDtkNILIATGSEVTPFPGI-TIDED-- 163
Cdd:PRK09754 51 MLLEDSPQLQQVLP--ANWWQENNVhLHSGVTIKTLGRDTRELVLTNGESWHWD--QLFIATGAAARPLPLLdALGERcf 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 164 TIVSSTGALSLKKV--PEKMVVI-GAGVIGVELGSVWQRLGADVTAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLN 240
Cdd:PRK09754 127 TLRHAGDAARLREVlqPERSVVIvGAGTIGLELAASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLN 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 241 TKVTGATKKSdgkiDVSIEAASGgkaEVITCDVLLVCIGRRpFTKNLGLEElgiELDPRGRIPVNTRFQTKIPNIYAIGD 320
Cdd:PRK09754 207 NAIEHVVDGE----KVELTLQSG---ETLQADVVIYGIGIS-ANDQLAREA---NLDTANGIVIDEACRTCDPAIFAGGD 275
|
.
1ZMC_D 321 V 321
Cdd:PRK09754 276 V 276
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
264-350 |
1.27e-10 |
|
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: 63.23 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 264 GKAEVITCDVLLVCIGRRPFTKNLgLEELGIELDPRGRIPVNTR-FQTKIPNIYAIGDVVAGPMLAhkaedegiicVEGM 342
Cdd:COG0493 353 GSEFTLPADLVILAIGQTPDPSGL-EEELGLELDKRGTIVVDEEtYQTSLPGVFAGGDAVRGPSLV----------VWAI 421
|
90
....*....|.
1ZMC_D 343 AGG---AVHID 350
Cdd:COG0493 422 AEGrkaARAID 432
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
267-342 |
1.83e-07 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 53.24 E-value: 1.83e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1ZMC_D 267 EVITCDVLLVCIGRRPFTKNLgLEELGIELDPRGRIPVNTR-FQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGM 342
Cdd:PRK12810 385 FVLPADLVLLAMGFTGPEAGL-LAQFGVELDERGRVAAPDNaYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAI 460
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
8-43 |
5.07e-07 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 52.16 E-value: 5.07e-07
10 20 30
....*....|....*....|....*....|....*.
1ZMC_D 8 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGG 43
Cdd:COG1233 5 DVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
8-44 |
6.80e-07 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 51.46 E-value: 6.80e-07
10 20 30
....*....|....*....|....*....|....*..
1ZMC_D 8 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 44
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGM 37
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
1-44 |
1.27e-06 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 50.87 E-value: 1.27e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
1ZMC_D 1 ADQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 44
Cdd:PRK06134 7 YPPDLECDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGGT 50
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
8-57 |
2.07e-06 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 49.86 E-value: 2.07e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
1ZMC_D 8 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNetlGGTCLNVGCIPSKALL 57
Cdd:pfam01134 1 DVIVIGGGHAGCEAALAAARMGAKVLLITHN---TDTIAELSCNPSIGGI 47
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
5-149 |
2.70e-06 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 49.45 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 5 IDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT------CLNVGCIP-SKALLNNS---HYYHMAHGTD---- 70
Cdd:COG1053 2 HEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGGHtaaaqgGINAAGTNvQKAAGEDSpeeHFYDTVKGGDglad 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 71 ------FASRGIEM--------------SEVRLNLDKMMEQKSTAVKALTGG---IAHLFKQN--------------KVV 113
Cdd:COG1053 82 qdlveaLAEEAPEAidwleaqgvpfsrtPDGRLPQFGGHSVGRTCYAGDGTGhalLATLYQAAlrlgveiftetevlDLI 161
|
170 180 190
....*....|....*....|....*....|....*.
1ZMC_D 114 HVNgyGKITGknqVTATKADGGTQVIDTKNILIATG 149
Cdd:COG1053 162 VDD--GRVVG---VVARDRTGEIVRIRAKAVVLATG 192
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
4-149 |
5.11e-06 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 48.70 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 4 PIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGtclnvgcipskallNNSHYYHMAHGTDFASRGIE--MSEV 81
Cdd:COG1148 138 PVNKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGG--------------RAAQLHKTFPGLDCPQCILEplIAEV 203
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1ZMC_D 82 RLNldkmmeqkstavkaltGGIaHLFKQNKVVHVNGYGkitGKNQVTATKADGGTQVIDTKNILIATG 149
Cdd:COG1148 204 EAN----------------PNI-TVYTGAEVEEVSGYV---GNFTVTIKKGPREEIEIEVGAIVLATG 251
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
3-44 |
5.80e-06 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 48.92 E-value: 5.80e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
1ZMC_D 3 QPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 44
Cdd:PRK12842 6 NELTCDVLVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGGT 47
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
8-44 |
1.04e-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: 47.67 E-value: 1.04e-05
10 20 30
....*....|....*....|....*....|....*..
1ZMC_D 8 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 44
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGA 37
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
182-335 |
1.09e-05 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 47.45 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 182 VVIGAGVIGVELGSVWQRLGAD--------------VTAVEFLGHVGGVgIDMEISKNFQRILQKQGFKFKLNTKVTGAT 247
Cdd:PTZ00318 177 VVVGGGPTGVEFAAELADFFRDdvrnlnpelveeckVTVLEAGSEVLGS-FDQALRKYGQRRLRRLGVDIRTKTAVKEVL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 248 KKSdgkidvsIEAASGgkaEVITCDVLL--VCIGRRPFTKNLGleelgIELDPRGRIPVNTRFQTK-IPNIYAIGDVVAG 324
Cdd:PTZ00318 256 DKE-------VVLKDG---EVIPTGLVVwsTGVGPGPLTKQLK-----VDKTSRGRISVDDHLRVKpIPNVFALGDCAAN 320
|
170
....*....|....*.
1ZMC_D 325 -----PMLAHKAEDEG 335
Cdd:PTZ00318 321 eerplPTLAQVASQQG 336
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
8-44 |
1.11e-05 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 47.72 E-value: 1.11e-05
10 20 30
....*....|....*....|....*....|....*..
1ZMC_D 8 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 44
Cdd:PRK07843 9 DVVVVGSGAAGMVAALTAAHRGLSTVVVEKAPHYGGS 45
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
4-43 |
1.59e-05 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 47.52 E-value: 1.59e-05
10 20 30 40
....*....|....*....|....*....|....*....|
1ZMC_D 4 PIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGG 43
Cdd:PRK12839 6 THTYDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKASTCGG 45
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
8-44 |
3.32e-05 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 46.27 E-value: 3.32e-05
10 20 30
....*....|....*....|....*....|....*..
1ZMC_D 8 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 44
Cdd:PRK12843 18 DVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGT 54
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
11-45 |
3.32e-05 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 41.75 E-value: 3.32e-05
10 20 30
....*....|....*....|....*....|....*
1ZMC_D 11 VIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTC 45
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNA 35
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
182-320 |
3.33e-05 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 46.65 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 182 VVIGAGVIGVELGSVWQRLGADVTAVEF--------LGHVGG---------VGIDMEISKNFQRILQkQGfkfklntkvT 244
Cdd:PRK14989 149 AVVGGGLLGLEAAGALKNLGVETHVIEFapmlmaeqLDQMGGeqlrrkiesMGVRVHTSKNTLEIVQ-EG---------V 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1ZMC_D 245 GATKksdgkidvSIEAASGGKAEVitcDVLLVCIGRRPFTKnLGlEELGIELDPRGRIPVNTRFQTKIPNIYAIGD 320
Cdd:PRK14989 219 EARK--------TMRFADGSELEV---DFIVFSTGIRPQDK-LA-TQCGLAVAPRGGIVINDSCQTSDPDIYAIGE 281
|
|
| PRK12835 |
PRK12835 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
8-51 |
6.03e-05 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237221 [Multi-domain] Cd Length: 584 Bit Score: 45.57 E-value: 6.03e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
1ZMC_D 8 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGG-TCLNVGCI 51
Cdd:PRK12835 13 DVLVVGSGGGGMTAALTAAARGLDTLVVEKSAHFGGsTALSGGGI 57
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
4-333 |
1.13e-04 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 44.76 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 4 PIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTcLNVGcIPSKALLNNShyyhMAHGTDF-ASRGIEM-SEV 81
Cdd:PRK13984 281 KKNKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGV-MRYG-IPSYRLPDEA----LDKDIAFiEALGVKIhLNT 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 82 RLNLDKMMEQkstavkaltggiahLFKQNKVVHVNgygkiTGKNQVTATKADGGtqviDTKNILIAtgsevtpfpgITID 161
Cdd:PRK13984 355 RVGKDIPLEE--------------LREKHDAVFLS-----TGFTLGRSTRIPGT----DHPDVIQA----------LPLL 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 162 EDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLG------ADVTAVEFLGHVGGVGIDM-EISKNF-------- 226
Cdd:PRK13984 402 REIRDYLRGEGPKPKIPRSLVVIGGGNVAMDIARSMARLQkmeygeVNVKVTSLERTFEEMPADMeEIEEGLeegvviyp 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 227 ----QRIL----QKQGFKFKLNTKVTGATKKSDGKIDVSIEAasggkaeVITCDVLLVCIGRRPFTKNLGlEELGIELD- 297
Cdd:PRK13984 482 gwgpMEVViendKVKGVKFKKCVEVFDEEGRFNPKFDESDQI-------IVEADMVVEAIGQAPDYSYLP-EELKSKLEf 553
|
330 340 350
....*....|....*....|....*....|....*.
1ZMC_D 298 PRGRIPVNTRFQTKIPNIYAIGDVVAGPMLAHKAED 333
Cdd:PRK13984 554 VRGRILTNEYGQTSIPWLFAGGDIVHGPDIIHGVAD 589
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
264-324 |
1.23e-04 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 44.40 E-value: 1.23e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
1ZMC_D 264 GKAEVITCDVLLVCIGRRPFTKNLGLEElGIELDPRG-RIPVNTRFQTKIPNIYAIGDVVAG 324
Cdd:PRK11749 369 GSEFTLPADLVIKAIGQTPNPLILSTTP-GLELNRWGtIIADDETGRTSLPGVFAGGDIVTG 429
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
8-44 |
1.78e-04 |
|
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];
Pssm-ID: 441675 [Multi-domain] Cd Length: 414 Bit Score: 43.70 E-value: 1.78e-04
10 20 30
....*....|....*....|....*....|....*..
1ZMC_D 8 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 44
Cdd:COG2072 8 DVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGT 44
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
8-42 |
2.17e-04 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 43.34 E-value: 2.17e-04
10 20 30
....*....|....*....|....*....|....*
1ZMC_D 8 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLG 42
Cdd:pfam03486 2 DVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
|
|
| PRK12844 |
PRK12844 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
7-44 |
2.17e-04 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 183787 [Multi-domain] Cd Length: 557 Bit Score: 43.59 E-value: 2.17e-04
10 20 30
....*....|....*....|....*....|....*...
1ZMC_D 7 ADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 44
Cdd:PRK12844 7 YDVVVVGSGGGGMCAALAAADSGLEPLIVEKQDKVGGS 44
|
|
| PRK07494 |
PRK07494 |
UbiH/UbiF family hydroxylase; |
1-35 |
2.05e-03 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181001 [Multi-domain] Cd Length: 388 Bit Score: 40.27 E-value: 2.05e-03
10 20 30
....*....|....*....|....*....|....*
1ZMC_D 1 ADQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCI 35
Cdd:PRK07494 2 LMEKEHTDIAVIGGGPAGLAAAIALARAGASVALV 36
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
289-343 |
4.55e-03 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 39.34 E-value: 4.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
1ZMC_D 289 LEELGIELDPRGRIPVNT----RFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMA 343
Cdd:PRK12769 590 LESHGVTVDKWGRIIADVesqyRYQTSNPKIFAGGDAVRGADLVVTAMAEGRHAAQGII 648
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
9-324 |
7.25e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 38.85 E-value: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 9 VTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTcLNVGcIPskallnnshyyhmahgtdfasrgiemsEVRLNLDKM 88
Cdd:PRK12831 143 VAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGGV-LVYG-IP---------------------------EFRLPKETV 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 89 MEQKSTAVKALtgGIAhlFKQNKVVhvngygkitgknqvtatkadGGTQVIDT-------KNILIATGSEVTPFPGIT-I 160
Cdd:PRK12831 194 VKKEIENIKKL--GVK--IETNVVV--------------------GKTVTIDElleeegfDAVFIGSGAGLPKFMGIPgE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 161 DEDTIVSSTGALS----LK----------KVPEKMVVIGAGVIGVELGSVWQRLGADVTAV------------EFLGHVG 214
Cdd:PRK12831 250 NLNGVFSANEFLTrvnlMKaykpeydtpiKVGKKVAVVGGGNVAMDAARTALRLGAEVHIVyrrseeelparvEEVHHAK 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZMC_D 215 GVGIDMEISKNFQRILQKQgfkfklNTKVTGAT--KKSDGKIDvsieaASG--------GKAEVITCDVLLVCIGRRPfT 284
Cdd:PRK12831 330 EEGVIFDLLTNPVEILGDE------NGWVKGMKciKMELGEPD-----ASGrrrpveieGSEFVLEVDTVIMSLGTSP-N 397
|
330 340 350 360
....*....|....*....|....*....|....*....|.
1ZMC_D 285 KNLGLEELGIELDPRGRIPVNTRF-QTKIPNIYAIGDVVAG 324
Cdd:PRK12831 398 PLISSTTKGLKINKRGCIVADEETgLTSKEGVFAGGDAVTG 438
|
|
| |
