|
Name |
Accession |
Description |
Interval |
E-value |
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
38-499 |
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: 583.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 38 AIDADVTVVGSGPGGYVAAIKAAQLGFKTVCVEKnATLGGTCLNVGCIPSKALLNNSYLYHMAhgKDFESRGIEIQGISL 117
Cdd:COG1249 1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEK-GRLGGTCLNVGCIPSKALLHAAEVAHEA--RHAAEFGISAGAPSV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 118 NLEKMMAQKSGAVKALTGGIAHLFKQNKVTHVNGFGTITGKNQVTAktaDGEQVINTKNILIATGSEVTPFPGIEIDEDS 197
Cdd:COG1249 78 DWAALMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEV---TGGETLTADHIVIATGSRPRVPPIPGLDEVR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 198 VVSSTGALSLKNVPEELIVIGAGVIGVELGSVWQRLGAKVTAVEFLGHVGGmGIDMEISKNFQRILQKQGLKFKLSTKVM 277
Cdd:COG1249 155 VLTSDEALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLP-GEDPEISEALEKALEKEGIDILTGAKVT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 278 GATKRPDGkidVAVEAAAGGKNETLTCDVLLVCIGRRPFTGNLGLESVGIELDKRGRIPVNGRFQTNVPNIYAIGDVVAG 357
Cdd:COG1249 234 SVEKTGDG---VTVTLEDGGGEEAVEADKVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRTSVPGIYAIGDVTGG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 358 PMLAHKAEDEGIICVEGMAGGAVH-IDYNCVPSVIYTHPEVAWVGKTEEQLKEEGVPYKVGKFPFAANSRAKTNADTDGL 436
Cdd:COG1249 311 PQLAHVASAEGRVAAENILGKKPRpVDYRAIPSVVFTDPEIASVGLTEEEAREAGIDVKVGKFPFAANGRALALGETEGF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41393167 437 VKILSHKDTDRMLGAHILGSGAGEMINEAALAMEYGASCEDVARVCHAHPTVSEAFREANLAA 499
Cdd:COG1249 391 VKLIADAETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAALAL 453
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
42-507 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 577.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 42 DVTVVGSGPGGYVAAIKAAQLGFKTVCVEK------NATLGGTCLNVGCIPSKALLNNSYLYHMAhGKDFESRGIEIQGI 115
Cdd:PRK06327 6 DVVVIGAGPGGYVAAIRAAQLGLKVACIEAwknpkgKPALGGTCLNVGCIPSKALLASSEEFENA-GHHFADHGIHVDGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 116 SLNLEKMMAQKSGAVKALTGGIAHLFKQNKVTHVNGFGTITGK----NQVTAKTADGEqVINTKNILIATGSEVTPFPGI 191
Cdd:PRK06327 85 KIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVGKtdagYEIKVTGEDET-VITAKHVIIATGSEPRHLPGV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 192 EIDEDSVVSSTGALSLKNVPEELIVIGAGVIGVELGSVWQRLGAKVTAVEFLGHVGGMgIDMEISKNFQRILQKQGLKFK 271
Cdd:PRK06327 164 PFDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAA-ADEQVAKEAAKAFTKQGLDIH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 272 LSTKVmGATKRPDGKIDVAVEAAAGgKNETLTCDVLLVCIGRRPFTGNLGLESVGIELDKRGRIPVNGRFQTNVPNIYAI 351
Cdd:PRK06327 243 LGVKI-GEIKTGGKGVSVAYTDADG-EAQTLEVDKLIVSIGRVPNTDGLGLEAVGLKLDERGFIPVDDHCRTNVPNVYAI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 352 GDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKTEEQLKEEGVPYKVGKFPFAANSRAKTNA 431
Cdd:PRK06327 321 GDVVRGPMLAHKAEEEGVAVAERIAGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLKAEGVEYKAGKFPFMANGRALAMG 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41393167 432 DTDGLVKILSHKDTDRMLGAHILGSGAGEMINEAALAMEYGASCEDVARVCHAHPTVSEAFREANLAASfGKAINF 507
Cdd:PRK06327 401 EPDGFVKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEVWHEAALAVD-KRPLHF 475
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
42-506 |
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: 573.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 42 DVTVVGSGPGGYVAAIKAAQLGFKTVCVEKNaTLGGTCLNVGCIPSKALLNNSYLYH-MAHGKDFesrGIEIQGISLNLE 120
Cdd:TIGR01350 3 DVIVIGGGPGGYVAAIRAAQLGLKVALVEKE-YLGGTCLNVGCIPTKALLHSAEVYDeIKHAKDL---GIEVENVSVDWE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 121 KMMAQKSGAVKALTGGIAHLFKQNKVTHVNGFGTITGKNQVTAKTADGEQVINTKNILIATGSEVTPFPG-IEIDEDSVV 199
Cdd:TIGR01350 79 KMQKRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGENGEETLEAKNIIIATGSRPRSLPGpFDFDGKVVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 200 SSTGALSLKNVPEELIVIGAGVIGVELGSVWQRLGAKVTAVEFLGHVGGmGIDMEISKNFQRILQKQGLKFKLSTKVMGA 279
Cdd:TIGR01350 159 TSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILP-GEDAEVSKVLQKALKKKGVKILTNTKVTAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 280 TKRPDGkidVAVEAAaGGKNETLTCDVLLVCIGRRPFTGNLGLESVGIELDKRGRIPVNGRFQTNVPNIYAIGDVVAGPM 359
Cdd:TIGR01350 238 EKNDDQ---VTYENK-GGETETLTGEKVLVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDVIGGPM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 360 LAHKAEDEGIICVEGMAGGA-VHIDYNCVPSVIYTHPEVAWVGKTEEQLKEEGVPYKVGKFPFAANSRAKTNADTDGLVK 438
Cdd:TIGR01350 314 LAHVASHEGIVAAENIAGKEpAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGYDVKIGKFPFAANGKALALGETDGFVK 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41393167 439 ILSHKDTDRMLGAHILGSGAGEMINEAALAMEYGASCEDVARVCHAHPTVSEAFREANLAAsFGKAIN 506
Cdd:TIGR01350 394 IIADKKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEAIKEAALAA-LGKPIH 460
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
37-507 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 552.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 37 AAIDADVTVVGSGPGGYVAAIKAAQLGFKTVCVEKnATLGGTCLNVGCIPSKALLNNSYLYH-MAHGKDFesrGIEIQGI 115
Cdd:PRK06416 1 FAFEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEK-EKLGGTCLNRGCIPSKALLHAAERADeARHSEDF---GIKAENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 116 SLNLEKMMAQKSGAVKALTGGIAHLFKQNKVTHVNGFGTITGKNQVTAKTADGEQVINTKNILIATGSEVTPFPGIEIDE 195
Cdd:PRK06416 77 GIDFKKVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDGEQTYTAKNIILATGSRPRELPGIEIDG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 196 DSVVSSTGALSLKNVPEELIVIGAGVIGVELGSVWQRLGAKVTAVEFLGHVggM-GIDMEISKNFQRILQKQGLKFKLST 274
Cdd:PRK06416 157 RVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRI--LpGEDKEISKLAERALKKRGIKIKTGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 275 KVMGATKRPDGkidVAVEAAAGGKNETLTCDVLLVCIGRRPFTGNLGLESVGIELDkRGRIPVNGRFQTNVPNIYAIGDV 354
Cdd:PRK06416 235 KAKKVEQTDDG---VTVTLEDGGKEETLEADYVLVAVGRRPNTENLGLEELGVKTD-RGFIEVDEQLRTNVPNIYAIGDI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 355 VAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKTEEQLKEEGVPYKVGKFPFAANSRAKTNADTD 434
Cdd:PRK06416 311 VGGPMLAHKASAEGIIAAEAIAGNPHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFDVKVVKFPFAGNGKALALGETD 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41393167 435 GLVKILSHKDTDRMLGAHILGSGAGEMINEAALAMEYGASCEDVARVCHAHPTVSEAFREANLAASfGKAINF 507
Cdd:PRK06416 391 GFVKLIFDKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEALGEAALAAA-GKPLHA 462
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
39-501 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 522.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 39 IDADVTVVGSGPGGYVAAIKAAQLGFKTVCVEKnATLGGTCLNVGCIPSKALLNNSYLYHMAhgKDFESRGIEIQGISLN 118
Cdd:PRK06292 2 EKYDVIVIGAGPAGYVAARRAAKLGKKVALIEK-GPLGGTCLNVGCIPSKALIAAAEAFHEA--KHAEEFGIHADGPKID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 119 LEKMMAQKSGAVKALTGGIAH-LFKQNKVTHVNGFGTITGKNQVTAktadGEQVINTKNILIATGSEVTPFPGIE-IDED 196
Cdd:PRK06292 79 FKKVMARVRRERDRFVGGVVEgLEKKPKIDKIKGTARFVDPNTVEV----NGERIEAKNIVIATGSRVPPIPGVWlILGD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 197 SVVSSTGALSLKNVPEELIVIGAGVIGVELGSVWQRLGAKVTAVEFLGHVGGmGIDMEISKNFQRILQKQgLKFKLSTKV 276
Cdd:PRK06292 155 RLLTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILP-LEDPEVSKQAQKILSKE-FKIKLGAKV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 277 mgaTKRPDGKIDVAVEAAAGGKNETLTCDVLLVCIGRRPFTGNLGLESVGIELDKRGRIPVNGRFQTNVPNIYAIGDVVA 356
Cdd:PRK06292 233 ---TSVEKSGDEKVEELEKGGKTETIEADYVLVATGRRPNTDGLGLENTGIELDERGRPVVDEHTQTSVPGIYAAGDVNG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 357 GPMLAHKAEDEGIICVEGMAGG-AVHIDYNCVPSVIYTHPEVAWVGKTEEQLKEEGVPYKVGKFPFAANSRAKTNADTDG 435
Cdd:PRK06292 310 KPPLLHEAADEGRIAAENAAGDvAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEVPFEAQGRARVMGKNDG 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41393167 436 LVKILSHKDTDRMLGAHILGSGAGEMINEAALAMEYGASCEDVARVCHAHPTVSEAFREANLAASF 501
Cdd:PRK06292 390 FVKVYADKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRTALRDLFS 455
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
42-501 |
3.30e-110 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 334.86 E-value: 3.30e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 42 DVTVVGSGPGGYVAAIKAAQLGFKTVCVEKNAtLGGTCLNVGCIPSKALLNNSYLYHMA-HGKDFesrGIEIQG-ISLNL 119
Cdd:PRK06370 7 DAIVIGAGQAGPPLAARAAGLGMKVALIERGL-LGGTCVNTGCVPTKTLIASARAAHLArRAAEY---GVSVGGpVSVDF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 120 EKMMAQKSGAVKALTGGIAHLFKQ-NKVTHVNGFGTITGKNQVTAktadGEQVINTKNILIATGSE--VTPFPGIeiDED 196
Cdd:PRK06370 83 KAVMARKRRIRARSRHGSEQWLRGlEGVDVFRGHARFESPNTVRV----GGETLRAKRIFINTGARaaIPPIPGL--DEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 197 SVVSSTGALSLKNVPEELIVIGAGVIGVELGSVWQRLGAKVTAVEFLGHVGGmGIDMEISKNFQRILQKQGLKFKLSTKV 276
Cdd:PRK06370 157 GYLTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLP-REDEDVAAAVREILEREGIDVRLNAEC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 277 MGATKRPDGKIdvaVEAAAGGKNETLTCDVLLVCIGRRPFTGNLGLESVGIELDKRGRIPVNGRFQTNVPNIYAIGDVVA 356
Cdd:PRK06370 236 IRVERDGDGIA---VGLDCNGGAPEITGSHILVAVGRVPNTDDLGLEAAGVETDARGYIKVDDQLRTTNPGIYAAGDCNG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 357 GPMLAHKAEDEGIICVEGMA-GGAVHIDYNCVPSVIYTHPEVAWVGKTEEQLKEEGVPYKVGKFPFAANSRAKTNADTDG 435
Cdd:PRK06370 313 RGAFTHTAYNDARIVAANLLdGGRRKVSDRIVPYATYTDPPLARVGMTEAEARKSGRRVLVGTRPMTRVGRAVEKGETQG 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41393167 436 LVKILSHKDTDRMLGAHILGSGAGEMINEAALAMEYGASCEDVARVCHAHPTVSEAFReaNLAASF 501
Cdd:PRK06370 393 FMKVVVDADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIP--TLAQAL 456
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
39-499 |
8.45e-105 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 320.95 E-value: 8.45e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 39 IDADVTVVGSGPGGYVAAIKAAQLGFKTVCVEKNATLGGTCLNVGCIPSKALLNN-SYLYHMaHGKDFESRGIEIQGISL 117
Cdd:PRK05249 4 YDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGGGCTHTGTIPSKALREAvLRLIGF-NQNPLYSSYRVKLRITF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 118 nlEKMMAQKSGAVKALTGGIAHLFKQNKVTHVNGFGTITGKNQVTAKTADGE-QVINTKNILIATGSEvtPF--PGIEID 194
Cdd:PRK05249 83 --ADLLARADHVINKQVEVRRGQYERNRVDLIQGRARFVDPHTVEVECPDGEvETLTADKIVIATGSR--PYrpPDVDFD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 195 EDSVVSSTGALSLKNVPEELIVIGAGVIGVELGSVWQRLGAKVTAVE-------FLghvggmgiDMEISKNFQRILQKQG 267
Cdd:PRK05249 159 HPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINtrdrllsFL--------DDEISDALSYHLRDSG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 268 LKFKLSTKVMGATKRPDGKIdvaVEAAAGGKnetLTCDVLLVCIGRRPFTGNLGLESVGIELDKRGRIPVNGRFQTNVPN 347
Cdd:PRK05249 231 VTIRHNEEVEKVEGGDDGVI---VHLKSGKK---IKADCLLYANGRTGNTDGLNLENAGLEADSRGQLKVNENYQTAVPH 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 348 IYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKTEEQLKEEGVPYKVGKFPFAANSRA 427
Cdd:PRK05249 305 IYAVGDVIGFPSLASASMDQGRIAAQHAVGEATAHLIEDIPTGIYTIPEISSVGKTEQELTAAKVPYEVGRARFKELARA 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41393167 428 KTNADTDGLVKILSHKDTDRMLGAHILGSGAGEMINEAALAMEYGASCEDVARVCHAHPTVSEAFREANLAA 499
Cdd:PRK05249 385 QIAGDNVGMLKILFHRETLEILGVHCFGERATEIIHIGQAIMEQKGTIEYFVNTTFNYPTMAEAYRVAALDG 456
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
42-498 |
4.72e-97 |
|
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: 301.26 E-value: 4.72e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 42 DVTVVGSGPGGYVAAIKAAQLGFKTVCVEKnATLGGTCLNVGCIPSKALLNNSYLYHMAHGKdfeSRGIEIQGISLNLEK 121
Cdd:TIGR02053 2 DLVIIGSGAAAFAAAIKAAELGASVAMVER-GPLGGTCVNVGCVPSKMLLRAAEVAHYARKP---PFGGLAATVAVDFGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 122 MMAQKSGAVKAL-TGGIAHLFKQNKVTHVNGFGTITGKNQVtaKTADGEQVINTKNILIATGSE--VTPFPGIeiDEDSV 198
Cdd:TIGR02053 78 LLEGKREVVEELrHEKYEDVLSSYGVDYLRGRARFKDPKTV--KVDLGREVRGAKRFLIATGARpaIPPIPGL--KEAGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 199 VSSTGALSLKNVPEELIVIGAGVIGVELGSVWQRLGAKVTAVE----FLGHvggmgIDMEISKNFQRILQKQGLKFKLST 274
Cdd:TIGR02053 154 LTSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQrsdrLLPR-----EEPEISAAVEEALAEEGIEVVTSA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 275 KVMGATKRPDGKIdvaVEAAAGGKNETLTCDVLLVCIGRRPFTGNLGLESVGIELDKRGRIPVNGRFQTNVPNIYAIGDV 354
Cdd:TIGR02053 229 QVKAVSVRGGGKI---ITVEKPGGQGEVEADELLVATGRRPNTDGLGLEKAGVKLDERGGILVDETLRTSNPGIYAAGDV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 355 VAGPMLAHKAEDEGIICVEGMAGGA-VHIDYNCVPSVIYTHPEVAWVGKTEEQLKEEGVPYKVGKFPFAANSRAKTNADT 433
Cdd:TIGR02053 306 TGGLQLEYVAAKEGVVAAENALGGAnAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNVPRARINRDT 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41393167 434 DGLVKILSHKDTDRMLGAHILGSGAGEMINEAALAMEYGASCEDVARVCHAHPTVSEAFREANLA 498
Cdd:TIGR02053 386 RGFIKLVAEPGTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGLKLAAQT 450
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
38-492 |
6.65e-78 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 251.23 E-value: 6.65e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 38 AIDADVTVVGSGPGGYVAAIKAAQLGFKTVCVEKNAtLGGTCLNVGCIPSKALLNNSYLYHMAH--GKDFesrGIEIQGI 115
Cdd:PRK06116 2 TKDYDLIVIGGGSGGIASANRAAMYGAKVALIEAKR-LGGTCVNVGCVPKKLMWYGAQIAEAFHdyAPGY---GFDVTEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 116 SLNLEKMMAQKSGAVKALTGGIAHLFKQNKVTHVNGFGTITGKNQVTAktaDGEQvINTKNILIATGSEVTP--FPGIEI 193
Cdd:PRK06116 78 KFDWAKLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEV---NGER-YTADHILIATGGRPSIpdIPGAEY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 194 dedsVVSSTGALSLKNVPEELIVIGAGVIGVELGSVWQRLGAKVTAV----EFLghvggMGIDMEISKNFQRILQKQGLK 269
Cdd:PRK06116 154 ----GITSDGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFvrgdAPL-----RGFDPDIRETLVEEMEKKGIR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 270 FKLSTKVMGATKRPDGKIDVAVEaaaggKNETLTCDVLLVCIGRRPFTGNLGLESVGIELDKRGRIPVNGRFQTNVPNIY 349
Cdd:PRK06116 225 LHTNAVPKAVEKNADGSLTLTLE-----DGETLTVDCLIWAIGREPNTDGLGLENAGVKLNEKGYIIVDEYQNTNVPGIY 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 350 AIGDVVAGPMLAHKAEDEGIICVEGMAGG--AVHIDYNCVPSVIYTHPEVAWVGKTE----EQLKEEGVpyKVGKFPFAA 423
Cdd:PRK06116 300 AVGDVTGRVELTPVAIAAGRRLSERLFNNkpDEKLDYSNIPTVVFSHPPIGTVGLTEeearEQYGEDNV--KVYRSSFTP 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41393167 424 NSRAKTNADTDGLVKILSHKDTDRMLGAHILGSGAGEMINEAALAMEYGASCEDVARVCHAHPTVSEAF 492
Cdd:PRK06116 378 MYTALTGHRQPCLMKLVVVGKEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEF 446
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
42-500 |
1.48e-73 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 245.21 E-value: 1.48e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 42 DVTVVGSGPGGYVAAIKAAQLGFKTVCVEKNA-TLGGTCLNVGCIPSKALL----------NNSYLYHMA-HGKDFES-- 107
Cdd:PTZ00153 118 DVGIIGCGVGGHAAAINAMERGLKVIIFTGDDdSIGGTCVNVGCIPSKALLyatgkyrelkNLAKLYTYGiYTNAFKNgk 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 108 -----RGIEIQG-ISLNLEKMMAQKSGAVKALTGGIAHLFKQNKVTHVNGFGTITGK--NQVTAKTADGEQVIN---TKN 176
Cdd:PTZ00153 198 ndpveRNQLVADtVQIDITKLKEYTQSVIDKLRGGIENGLKSKKFCKNSEHVQVIYErgHIVDKNTIKSEKSGKefkVKN 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 177 ILIATGSevTPF--PGIEIDEDSVVSSTGALSLKNVPEELIVIGAGVIGVELGSVWQRLGAKVTAVEFLGHVGGmGIDME 254
Cdd:PTZ00153 278 IIIATGS--TPNipDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSPQLLP-LLDAD 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 255 ISKNFQRILQK-QGLKFKLSTKV-------------MGATKRPDGKIDVAVEAAAGGKNetLTCDVLLVCIGRRPFTGNL 320
Cdd:PTZ00153 355 VAKYFERVFLKsKPVRVHLNTLIeyvragkgnqpviIGHSERQTGESDGPKKNMNDIKE--TYVDSCLVATGRKPNTNNL 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 321 GLESVGIELdKRGRIPVNGRFQTN------VPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVH------------- 381
Cdd:PTZ00153 433 GLDKLKIQM-KRGFVSVDEHLRVLredqevYDNIFCIGDANGKQMLAHTASHQALKVVDWIEGKGKEnvninvenwaskp 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 382 IDYNCVPSVIYTHPEVAWVGKTEEQLKEEGVPYKVGKFP--FAANSRA----------------------KTNADTDGLV 437
Cdd:PTZ00153 512 IIYKNIPSVCYTTPELAFIGLTEKEAKELYPPDNVGVEIsfYKANSKVlcennisfpnnsknnsynkgkyNTVDNTEGMV 591
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41393167 438 KILSHKDTDRMLGAHILGSGAGEMINEAALAMEYGASCEDVARVCHAHPTVSEAFREANLAAS 500
Cdd:PTZ00153 592 KIVYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDAAFKAIA 654
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
42-492 |
1.56e-70 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 231.56 E-value: 1.56e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 42 DVTVVGSGPGGYVAAIKAAQLGFKTVCVEKNATL-GGTCLNVGCIPSKALLnnsylyhMAHGKDfesrgieiqgisLNLE 120
Cdd:PRK07251 5 DLIVIGFGKAGKTLAAKLASAGKKVALVEESKAMyGGTCINIGCIPTKTLL-------VAAEKN------------LSFE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 121 KMMAQKSGAVKALTGGIAHLFKQNKVTHVNGFGTITGKNQVTAKTADGEQVINTKNILIATG--SEVTPFPGIEiDEDSV 198
Cdd:PRK07251 66 QVMATKNTVTSRLRGKNYAMLAGSGVDLYDAEAHFVSNKVIEVQAGDEKIELTAETIVINTGavSNVLPIPGLA-DSKHV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 199 VSSTGALSLKNVPEELIVIGAGVIGVELGSVWQRLGAKVTAVE----FLGHVggmgiDMEISKNFQRILQKQGLKFKLST 274
Cdd:PRK07251 145 YDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDaastILPRE-----EPSVAALAKQYMEEDGITFLLNA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 275 KVmGATKRPDGKIDVAVEaaaggkNETLTCDVLLVCIGRRPFTGNLGLESVGIELDKRGRIPVNGRFQTNVPNIYAIGDV 354
Cdd:PRK07251 220 HT-TEVKNDGDQVLVVTE------DETYRFDALLYATGRKPNTEPLGLENTDIELTERGAIKVDDYCQTSVPGVFAVGDV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 355 VAGPMLAHKAEDEGIICVEGMAGGA--VHIDYNCVPSVIYTHPEVAWVGKTEEQLKEEGVPYKVGKFPFAANSRAKTNAD 432
Cdd:PRK07251 293 NGGPQFTYISLDDFRIVFGYLTGDGsyTLEDRGNVPTTMFITPPLSQVGLTEKEAKEAGLPYAVKELLVAAMPRAHVNND 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 433 TDGLVKILSHKDTDRMLGAHILGSGAGEMINEAALAMEYGASCEDVARVCHAHPTVSEAF 492
Cdd:PRK07251 373 LRGAFKVVVNTETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAENL 432
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
45-494 |
1.94e-70 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 231.21 E-value: 1.94e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 45 VVGSGPGGYVAAIKAAQLGFKTVCVEKNATL-GGTCLNVGCIPSKALLNNSYLYHmahgkDFESrgieiqgislnlekMM 123
Cdd:NF040477 8 IIGFGKAGKTLAATLAKAGWRVAIIEQSAQMyGGTCINIGCIPTKTLVHDAEQHQ-----DFST--------------AM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 124 AQKSGAVKALTGGIAH-LFKQNKVTHVNGFGTITGKNQVTAKTADGEQVINTKNILIATGSEVT--PFPGIEIDEdSVVS 200
Cdd:NF040477 69 QRKSSVVGFLRDKNYHnLADLDNVDVINGRAEFIDNHTLRVFQADGEQELRGEKIFINTGAQSVlpPIPGLTTTP-GVYD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 201 STGALSLKNVPEELIVIGAGVIGVELGSVWQRLGAKVTAVEFLGHVGGMGiDMEISKNFQRILQKQGLKFKLSTKVMGAT 280
Cdd:NF040477 148 STGLLNLTQLPARLGILGGGYIGVEFASMFARFGSKVTIFEAAELFLPRE-DRDIAQAIATILQDQGVELILNAQVQRVS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 281 KRPDGkidVAVEAAAGgkneTLTCDVLLVCIGRRPFTGNLGLESVGIELDKRGRIPVNGRFQTNVPNIYAIGDVVAGPML 360
Cdd:NF040477 227 SHEGE---VQLETAEG----VLTVDALLVASGRKPATAGLQLQNAGVAVNERGAIVVDKYLRTTADNIWAMGDVTGGLQF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 361 AHKAEDEGIICVEGMAG-GAVHI-DYNCVPSVIYTHPEVAWVGKTEEQLKEEGVPYKVGKFPFAANSRAKTNADTDGLVK 438
Cdd:NF040477 300 TYISLDDFRIVRDSLLGeGKRSTdDRQNVPYSVFMTPPLSRIGMTEEQARASGADIQVVTLPVAAIPRARVMNDTRGVLK 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 41393167 439 ILSHKDTDRMLGAHILGSGAGEMINEAALAMEYGASCEDVARVCHAHPTVSEAFRE 494
Cdd:NF040477 380 AVVDNKTQRILGVSLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSESLND 435
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
42-368 |
6.88e-69 |
|
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: 222.96 E-value: 6.88e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 42 DVTVVGSGPGGYVAAIKAAQLGFKTVCVEknatLGGTCLNVGCIPSKALLNnsylyhmahgkdfesrGIEIQGISLNLEK 121
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIE----DEGTCPYGGCVLSKALLG----------------AAEAPEIASLWAD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 122 MMAQKSGAVKALTGGIAHLFKQNKVTHVNGFGTITGKNQVTaktaDGEQVINTKNILIATGSE--VTPFPGIE---IDED 196
Cdd:pfam07992 62 LYKRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELVD----GDGETITYDRLVIATGARprLPPIPGVElnvGFLV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 197 SVVSSTGALSLKNVPEELIVIGAGVIGVELGSVWQRLGAKVTAVEFLGHVGGMgIDMEISKNFQRILQKQGLKFKLSTKV 276
Cdd:pfam07992 138 RTLDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRA-FDEEISAALEKALEKNGVEVRLGTSV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 277 MGATKRPDGkidVAVEaaaGGKNETLTCDVLLVCIGRRPFTgnLGLESVGIELDKRGRIPVNGRFQTNVPNIYAIGDV-V 355
Cdd:pfam07992 217 KEIIGDGDG---VEVI---LKDGTEIDADLVVVAIGRRPNT--ELLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDCrV 288
|
330
....*....|...
gi 41393167 356 AGPMLAHKAEDEG 368
Cdd:pfam07992 289 GGPELAQNAVAQG 301
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
43-469 |
1.85e-67 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 226.96 E-value: 1.85e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 43 VTVVGSGPGGYVAAIKAAQLGFKTVCVEKnATLGGTCLNVGCIPSKALLNNSYLYHMAHGKDFESrGIEIQGISLNLEKM 122
Cdd:PRK13748 101 VAVIGSGGAAMAAALKAVEQGARVTLIER-GTIGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDG-GIAATVPTIDRSRL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 123 MAQKSGAVKALTG----GIahLFKQNKVTHVNGFGTITGKNQVTAKTADG-EQVINTKNILIATGSE--VTPFPGIEidE 195
Cdd:PRK13748 179 LAQQQARVDELRHakyeGI--LDGNPAITVLHGEARFKDDQTLIVRLNDGgERVVAFDRCLIATGASpaVPPIPGLK--E 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 196 DSVVSSTGALSLKNVPEELIVIGAGVIGVELGSVWQRLGAKVTAVE----FLGHvggmgiDMEISKNFQRILQKQGLKFK 271
Cdd:PRK13748 255 TPYWTSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILArstlFFRE------DPAIGEAVTAAFRAEGIEVL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 272 LSTKVmGATKRPDGKIdvAVEAAAGgkneTLTCDVLLVCIGRRPFTGNLGLESVGIELDKRGRIPVNGRFQTNVPNIYAI 351
Cdd:PRK13748 329 EHTQA-SQVAHVDGEF--VLTTGHG----ELRADKLLVATGRAPNTRSLALDAAGVTVNAQGAIVIDQGMRTSVPHIYAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 352 GDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKTEEQLKEEGVPYKVGKFPFAANSRAKTNA 431
Cdd:PRK13748 402 GDCTDQPQFVYVAAAAGTRAAINMTGGDAALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRTLTLDNVPRALANF 481
|
410 420 430
....*....|....*....|....*....|....*...
gi 41393167 432 DTDGLVKILSHKDTDRMLGAHILGSGAGEMINEAALAM 469
Cdd:PRK13748 482 DTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAALAI 519
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
42-492 |
2.66e-61 |
|
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: 207.77 E-value: 2.66e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 42 DVTVVGSGPGGYVAAIKAAQLGFKTVCVEKNAtLGGTCLNVGCIPSKALLNNSYLYHMAHgkDFESRGI--EIQGiSLNL 119
Cdd:TIGR01421 4 DYLVIGGGSGGIASARRAAEHGAKALLVEAKK-LGGTCVNVGCVPKKVMWYASDLAERMH--DAADYGFyqNDEN-TFNW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 120 EKMMAQKSGAVKALTGGIAHLFKQNKVTHVNGFGTITGKNQVTAKTADgeqvINTKNILIATG---SEVTPFPGIEIDed 196
Cdd:TIGR01421 80 PELKEKRDAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVNGRD----YTAPHILIATGgkpSFPENIPGAELG-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 197 svVSSTGALSLKNVPEELIVIGAGVIGVELGSVWQRLGAKvTAVEFLGHVGGMGIDMEISKNFQRILQKQGLKFKLSTKV 276
Cdd:TIGR01421 154 --TDSDGFFALEELPKRVVIVGAGYIAVELAGVLHGLGSE-THLVIRHERVLRSFDSMISETITEEYEKEGINVHKLSKP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 277 MGATKRPDGKIDVAVEAAaggkNETLTCDVLLVCIGRRPFTGNLGLESVGIELDKRGRIPVNGRFQTNVPNIYAIGDVVA 356
Cdd:TIGR01421 231 VKVEKTVEGKLVIHFEDG----KSIDDVDELIWAIGRKPNTKGLGLENVGIKLNEKGQIIVDEYQNTNVPGIYALGDVVG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 357 GPMLAHKAEDEGIICVEGMAGGA--VHIDYNCVPSVIYTHPEVAWVGKTEEQ-LKEEGVP-YKVGKFPFAANSRAKTNAD 432
Cdd:TIGR01421 307 KVELTPVAIAAGRKLSERLFNGKtdDKLDYNNVPTVVFSHPPIGTIGLTEKEaIEKYGKEnIKVYNSSFTPMYYAMTSEK 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 433 TDGLVKILSHKDTDRMLGAHILGSGAGEMINEAALAMEYGASCEDVARVCHAHPTVSEAF 492
Cdd:TIGR01421 387 QKCRMKLVCAGKEEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEEL 446
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
34-492 |
8.96e-60 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 204.66 E-value: 8.96e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 34 ADKAAIDADVTVVGSGPGGYVAAIKAAQLG---------FKTVCVEKNATLGGTCLNVGCIPSKALLnnsylYHMAHGKD 104
Cdd:PLN02507 19 ANATHYDFDLFVIGAGSGGVRAARFSANFGakvgicelpFHPISSESIGGVGGTCVIRGCVPKKILV-----YGATFGGE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 105 FESR---GIEIQG-ISLNLEKMMAQKSGAVKALTGGIAHLFKQNKVTHVNGFGTITGKNQVTAKTADGEQVINT-KNILI 179
Cdd:PLN02507 94 FEDAknyGWEINEkVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRYTaKHILI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 180 ATGSEVTP--FPGIEIdedsVVSSTGALSLKNVPEELIVIGAGVIGVELGSVWQRLGAKVTAVeFLGHVGGMGIDMEISK 257
Cdd:PLN02507 174 ATGSRAQRpnIPGKEL----AITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLF-FRKELPLRGFDDEMRA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 258 NFQRILQKQGLKFKLSTKVMGATKRPDGkIDVAVEaaaggKNETLTCDVLLVCIGRRPFTGNLGLESVGIELDKRGRIPV 337
Cdd:PLN02507 249 VVARNLEGRGINLHPRTNLTQLTKTEGG-IKVITD-----HGEEFVADVVLFATGRAPNTKRLNLEAVGVELDKAGAVKV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 338 NGRFQTNVPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGG-AVHIDYNCVPSVIYTHPEVAWVGKTEEQLKEEG---VP 413
Cdd:PLN02507 323 DEYSRTNIPSIWAIGDVTNRINLTPVALMEGTCFAKTVFGGqPTKPDYENVACAVFCIPPLSVVGLSEEEAVEQAkgdIL 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41393167 414 YKVGKFPFAANSRAKTNADTdgLVKILSHKDTDRMLGAHILGSGAGEMINEAALAMEYGASCEDVARVCHAHPTVSEAF 492
Cdd:PLN02507 403 VFTSSFNPMKNTISGRQEKT--VMKLIVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEF 479
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
45-494 |
3.87e-59 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 201.78 E-value: 3.87e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 45 VVGSGPGGYVAAIKAAQLGFKTVCVEK-NATLGGTCLNVGCIPSKALLNnsylyhmahgkDFESRGieiqgislNLEKMM 123
Cdd:PRK08010 8 IIGFGKAGKTLAVTLAKAGWRVALIEQsNAMYGGTCINIGCIPTKTLVH-----------DAQQHT--------DFVRAI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 124 AQKSGAVKALTGGIAH-LFKQNKVTHVNGFGTITGKNQVTAKTADGEQVINTKNILIATGSE--VTPFPGIEIDEdSVVS 200
Cdd:PRK08010 69 QRKNEVVNFLRNKNFHnLADMPNIDVIDGQAEFINNHSLRVHRPEGNLEIHGEKIFINTGAQtvVPPIPGITTTP-GVYD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 201 STGALSLKNVPEELIVIGAGVIGVELGSVWQRLGAKVTAVE----FLGHVggmgiDMEISKNFQRILQKQGLKFKLSTKV 276
Cdd:PRK08010 148 STGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEaaslFLPRE-----DRDIADNIATILRDQGVDIILNAHV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 277 MGATKRpDGKIDVAVEAAAggknetLTCDVLLVCIGRRPFTGNLGLESVGIELDKRGRIPVNGRFQTNVPNIYAIGDVVA 356
Cdd:PRK08010 223 ERISHH-ENQVQVHSEHAQ------LAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKYLHTTADNIWAMGDVTG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 357 GPMLAHKAEDEGIICVEGMAGGAVHI--DYNCVPSVIYTHPEVAWVGKTEEQLKEEGVPYKVGKFPFAANSRAKTNADTD 434
Cdd:PRK08010 296 GLQFTYISLDDYRIVRDELLGEGKRStdDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDTR 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 435 GLVKILSHKDTDRMLGAHILGSGAGEMINEAALAMEYGASCEDVARVCHAHPTVSEAFRE 494
Cdd:PRK08010 376 GVLKAIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLND 435
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
42-501 |
1.10e-56 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 195.17 E-value: 1.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 42 DVTVVGSGPGGYVAAIKAAQLgfKTVCVEKnATLGGTCLNVGCIPSKALLnnsYLYHMAH--------GKDFESRGIEIQ 113
Cdd:PRK07846 3 DLIIIGTGSGNSILDERFADK--RIAIVEK-GTFGGTCLNVGCIPTKMFV---YAADVARtireaarlGVDAELDGVRWP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 114 GIslnlekmMAQKSGAVKAL-TGGIAHLFKQN-KVTHVNGFGTITGknQVTAKTADGEqVINTKNILIATGSEVTPFPGI 191
Cdd:PRK07846 77 DI-------VSRVFGRIDPIaAGGEEYRGRDTpNIDVYRGHARFIG--PKTLRTGDGE-EITADQVVIAAGSRPVIPPVI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 192 EIDEDSVVSSTGALSLKNVPEELIVIGAGVIGVELGSVWQRLGAKVTAVE----FLGHvggmgIDMEISKNFQRILQKQg 267
Cdd:PRK07846 147 ADSGVRYHTSDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNrsgrLLRH-----LDDDISERFTELASKR- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 268 LKFKLSTKVMGATKRPDGkidVAVEAAAGgknETLTCDVLLVCIGRRPFTGNLGLESVGIELDKRGRIPVNGRFQTNVPN 347
Cdd:PRK07846 221 WDVRLGRNVVGVSQDGSG---VTLRLDDG---STVEADVLLVATGRVPNGDLLDAAAAGVDVDEDGRVVVDEYQRTSAEG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 348 IYAIGDVVAGPMLAHKAEDEGIICVEGMAGGA--VHIDYNCVPSVIYTHPEVAWVGKTEEQLKEEGVPYKVGKFPFAANS 425
Cdd:PRK07846 295 VFALGDVSSPYQLKHVANHEARVVQHNLLHPDdlIASDHRFVPAAVFTHPQIASVGLTENEARAAGLDITVKVQNYGDVA 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41393167 426 RAKTNADTDGLVKILSHKDTDRMLGAHILGSGAGEMINEAALAMEYGASCEDVARVCH-AHPTVSEAFREANLAASF 501
Cdd:PRK07846 375 YGWAMEDTTGFVKLIADRDTGRLLGAHIIGPQASTLIQPLIQAMSFGLDAREMARGQYwIHPALPEVVENALLGLDL 451
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
42-490 |
6.07e-56 |
|
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: 194.42 E-value: 6.07e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 42 DVTVVGSGPGGYVAAIKAAQLGFKTVCV---EKN------ATLGGTCLNVGCIPSKALLNNS-YLYHMAHGKDFesrGIE 111
Cdd:TIGR01423 5 DLVVIGAGSGGLEAGWNAATLYKKRVAVvdvQTHhgppfyAALGGTCVNVGCVPKKLMVTGAqYMDTLRESAGF---GWE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 112 IQGISL--NLEKMMAQKSGAVKALTGGIAHLFKQNK-VTHVNGFGTITGKNQVTAK-TADGE----QVINTKNILIATGS 183
Cdd:TIGR01423 82 FDRSSVkaNWKALIAAKNKAVLDINKSYEGMFADTEgLTFFLGWGALEDKNVVLVReSADPKsavkERLQAEHILLATGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 184 --EVTPFPGIEIdedsVVSSTGALSLKNVPEELIVIGAGVIGVELGSV---WQRLGAKVTavefLGHVGGM---GIDMEI 255
Cdd:TIGR01423 162 wpQMLGIPGIEH----CISSNEAFYLDEPPRRVLTVGGGFISVEFAGIfnaYKPRGGKVT----LCYRNNMilrGFDSTL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 256 SKNFQRILQKQGLKFKLSTKVMGATKRPDGKIDVAVEAAAggkneTLTCDVLLVCIGRRPFTGNLGLESVGIELDKRGRI 335
Cdd:TIGR01423 234 RKELTKQLRANGINIMTNENPAKVTLNADGSKHVTFESGK-----TLDVDVVMMAIGRVPRTQTLQLDKVGVELTKKGAI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 336 PVNGRFQTNVPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVH-IDYNCVPSVIYTHPEVAWVGKTEEQL--KEEGV 412
Cdd:TIGR01423 309 QVDEFSRTNVPNIYAIGDVTDRVMLTPVAINEGAAFVDTVFGNKPRkTDHTRVASAVFSIPPIGTCGLVEEDAakKFEKV 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41393167 413 PYKVGKF-PFAANSRAKTNADTdgLVKILSHKDTDRMLGAHILGSGAGEMINEAALAMEYGASCEDVARVCHAHPTVSE 490
Cdd:TIGR01423 389 AVYESSFtPLMHNISGSKYKKF--VAKIVTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAE 465
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
40-492 |
2.15e-55 |
|
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: 192.76 E-value: 2.15e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 40 DADVTVVGSGPGGYVAAIKAAQLGFKTVCVE--------KNATLGGTCLNVGCIPSK-----ALLNNSYLYHMAHGKDFE 106
Cdd:TIGR01438 2 DYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDfvtptplgTRWGIGGTCVNVGCIPKKlmhqaALLGQALKDSRNYGWKVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 107 SRgieiqgISLNLEKMMAQKSGAVKALTGGIAHLFKQNKVTHVNGFGTITGKNQVTAKTADG-EQVINTKNILIATGsEV 185
Cdd:TIGR01438 82 ET------VKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGkEKIYSAERFLIATG-ER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 186 TPFPGIEIDEDSVVSSTGALSLKNVPEELIVIGAGVIGVELGSVWQRLGAKVTAVefLGHVGGMGIDMEISKNFQRILQK 265
Cdd:TIGR01438 155 PRYPGIPGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVM--VRSILLRGFDQDCANKVGEHMEE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 266 QGLKFKLSTKVMGATKRPDGKIDVAVEAAAGGKNETltcDVLLVCIGRRPFTGNLGLESVGIELDKR-GRIPVNGRFQTN 344
Cdd:TIGR01438 233 HGVKFKRQFVPIKVEQIEAKVLVEFTDSTNGIEEEY---DTVLLAIGRDACTRKLNLENVGVKINKKtGKIPADEEEQTN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 345 VPNIYAIGDVVAG-PMLAHKAEDEGIICVEGMAGGAVHI-DYNCVPSVIYTHPEVAWVGKTEEQLKEegvpyKVGK---- 418
Cdd:TIGR01438 310 VPYIYAVGDILEDkPELTPVAIQAGRLLAQRLFKGSTVIcDYENVPTTVFTPLEYGACGLSEEKAVE-----KFGEenve 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 419 --------FPFAANSRAKTNAdtdGLVKIL-SHKDTDRMLGAHILGSGAGEMINEAALAMEYGASCEDVARVCHAHPTVS 489
Cdd:TIGR01438 385 vfhsyfwpLEWTIPSRDNHNK---CYAKLVcNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCA 461
|
...
gi 41393167 490 EAF 492
Cdd:TIGR01438 462 EVF 464
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
43-493 |
1.17e-54 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 190.46 E-value: 1.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 43 VTVVGSGPGGYVAAIKAAQLGFKTVCVEKNAtLGGTCLNVGCIPSKALLNNSYLyhMAHGKDFESRGIEIQGISlNLEKM 122
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIERDG-LGGAAVLTDCVPSKTLIATAEV--RTELRRAAELGIRFIDDG-EARVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 123 MAQKSGAVKALT----GGIAHLFKQNKVTHVNGFGTIT----GKNQVTAKTADG-EQVINTKNILIATGSevTP--FPGI 191
Cdd:PRK07845 80 LPAVNARVKALAaaqsADIRARLEREGVRVIAGRGRLIdpglGPHRVKVTTADGgEETLDADVVLIATGA--SPriLPTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 192 EIDEDSVVSSTGALSLKNVPEELIVIGAGVIGVELGSVWQRLGAKVTAVEFLGHVggM-GIDMEISKNFQRILQKQGLKF 270
Cdd:PRK07845 158 EPDGERILTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRV--LpGEDADAAEVLEEVFARRGMTV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 271 KLSTKVMGATKRPDGkidVAVEAAAGGKNETLTCdvlLVCIGRRPFTGNLGLESVGIELDKRGRIPVNGRFQTNVPNIYA 350
Cdd:PRK07845 236 LKRSRAESVERTGDG---VVVTLTDGRTVEGSHA---LMAVGSVPNTAGLGLEEAGVELTPSGHITVDRVSRTSVPGIYA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 351 IGDVVAGPMLAHKAEDEGIICVEGMAGGAVH-IDYNCVPSVIYTHPEVAWVGKTEEQLKEEGVPYKVGKFPFAANSRAKT 429
Cdd:PRK07845 310 AGDCTGVLPLASVAAMQGRIAMYHALGEAVSpLRLKTVASNVFTRPEIATVGVSQAAIDSGEVPARTVMLPLATNPRAKM 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41393167 430 NADTDGLVKILSHKDTDRMLGAHILGSGAGEMINEAALAMEYGASCEDVARVCHAHP----TVSEAFR 493
Cdd:PRK07845 390 SGLRDGFVKLFCRPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYPslsgSITEAAR 457
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
387-495 |
1.29e-52 |
|
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: 173.51 E-value: 1.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 387 VPSVIYTHPEVAWVGKTEEQLKEEGVPYKVGKFPFAANSRAKTNADTDGLVKILSHKDTDRMLGAHILGSGAGEMINEAA 466
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGEVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQEAA 80
|
90 100
....*....|....*....|....*....
gi 41393167 467 LAMEYGASCEDVARVCHAHPTVSEAFREA 495
Cdd:pfam02852 81 LAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
42-498 |
5.76e-50 |
|
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: 177.26 E-value: 5.76e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 42 DVTVVGSGPGGyvaAIKAAQLGFKTVCVEKNATLGGTCLNVGCIPSKALLnnsYLYHMAHGKDFESR-GI--EIQGISLN 118
Cdd:TIGR03452 4 DLIIIGTGSGN---SIPDPRFADKRIAIVEKGTFGGTCLNVGCIPTKMFV---YAAEVAQSIGESARlGIdaEIDSVRWP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 119 --LEKMMAQKsgaVKALTGGIAHLFKQNKVTHVNGF-GTITGKNQVTAKTADGEQvINTKNILIATGSEVTPFPGIeidE 195
Cdd:TIGR03452 78 diVSRVFGDR---IDPIAAGGEDYRRGDETPNIDVYdGHARFVGPRTLRTGDGEE-ITGDQIVIAAGSRPYIPPAI---A 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 196 DSVV---SSTGALSLKNVPEELIVIGAGVIGVELGSVWQRLGAKVTAV----EFLGHvggmgIDMEISKNFQRILQKQgL 268
Cdd:TIGR03452 151 DSGVryhTNEDIMRLPELPESLVIVGGGYIAAEFAHVFSALGTRVTIVnrstKLLRH-----LDEDISDRFTEIAKKK-W 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 269 KFKLSTKVMGATKRPDGkidVAVEAAAGgknETLTCDVLLVCIGRRPFTGNLGLESVGIELDKRGRIPVNGRFQTNVPNI 348
Cdd:TIGR03452 225 DIRLGRNVTAVEQDGDG---VTLTLDDG---STVTADVLLVATGRVPNGDLLDAEAAGVEVDEDGRIKVDEYGRTSARGV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 349 YAIGDVVAGPMLAHKAEDEGIICVEGMA--GGAVHIDYNCVPSVIYTHPEVAWVGKTEEQLKEEGVPY--KVGKFPFAAN 424
Cdd:TIGR03452 299 WALGDVSSPYQLKHVANAEARVVKHNLLhpNDLRKMPHDFVPSAVFTHPQIATVGLTEQEAREAGHDItvKIQNYGDVAY 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41393167 425 SRAKtnADTDGLVKILSHKDTDRMLGAHILGSGAGEMINEAALAMEYGASCEDVARVCH-AHPTVSEAFREANLA 498
Cdd:TIGR03452 379 GWAM--EDTTGFCKLIADRDTGKLLGAHIIGPQASSLIQPLITAMAFGLDAREMARKQYwIHPALPEVVENALLG 451
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
3-492 |
1.58e-47 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 173.14 E-value: 1.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 3 SRNHLYRTLATRGQHLPC--KLHGATVLSARTYADKAA-----IDADVTVVGSGPGGYVAAIKAAQLG---------FKT 66
Cdd:PLN02546 35 SSSHLPLPKTLTRLSSPRplSHHHRRRSVSRAAAPNGAeserhYDFDLFTIGAGSGGVRASRFASNFGasaavcelpFAT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 67 VCVEKNATLGGTCLNVGCIPSKALLNNSYLYHmahgkDF-ESRGIeiqGISLNLE------KMMAQKSGAVKALTGGIAH 139
Cdd:PLN02546 115 ISSDTLGGVGGTCVLRGCVPKKLLVYASKYSH-----EFeESRGF---GWKYETEpkhdwnTLIANKNAELQRLTGIYKN 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 140 LFKQNKVTHVNGFGTITGKNQVTAktaDGeQVINTKNILIATGSEvtPF----PGIEidedSVVSSTGALSLKNVPEELI 215
Cdd:PLN02546 187 ILKNAGVTLIEGRGKIVDPHTVDV---DG-KLYTARNILIAVGGR--PFipdiPGIE----HAIDSDAALDLPSKPEKIA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 216 VIGAGVIGVELGSVWQRLGAKVTAveFLGHVGGM-GIDMEISKNFQRILQKQGLKFKLSTKVMGATKRPDGKIDVAV-EA 293
Cdd:PLN02546 257 IVGGGYIALEFAGIFNGLKSDVHV--FIRQKKVLrGFDEEVRDFVAEQMSLRGIEFHTEESPQAIIKSADGSLSLKTnKG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 294 AAGGKNEtltcdvLLVCIGRRPFTGNLGLESVGIELDKRGRIPVNGRFQTNVPNIYAIGDVVAGPMLAHKAEDEGIICVE 373
Cdd:PLN02546 335 TVEGFSH------VMFATGRKPNTKNLGLEEVGVKMDKNGAIEVDEYSRTSVPSIWAVGDVTDRINLTPVALMEGGALAK 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 374 GMAGG-AVHIDYNCVPSVIYTHPEVAWVGKTEEQLKEEGVPYKVgkfpFAANSRAkTNADTDGL-----VKILSHKDTDR 447
Cdd:PLN02546 409 TLFGNePTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYGDVDV----FTANFRP-LKATLSGLpdrvfMKLIVCAKTNK 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 41393167 448 MLGAHILGSGAGEMINEAALAMEYGASCEDVARVCHAHPTVSEAF 492
Cdd:PLN02546 484 VLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEEF 528
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
40-492 |
2.62e-43 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 160.37 E-value: 2.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 40 DADVTVVGSGPGGYVAAIKAAQLGFKTVCVE--KNAT------LGGTCLNVGCIPSKAL---LNNSYLYHMahgkDFESR 108
Cdd:PTZ00052 5 MYDLVVIGGGSGGMAAAKEAAAHGKKVALFDyvKPSTqgtkwgLGGTCVNVGCVPKKLMhyaANIGSIFHH----DSQMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 109 GIEIQGiSLNLEKMMAQKSGAVKALTGGIAHLFKQNKVTHVNGFGTITGKNQVTAKTADGEQVINTKNILIATGSEVTPF 188
Cdd:PTZ00052 81 GWKTSS-SFNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTVSYGDNSQEETITAKYILIATGGRPSIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 189 PGIEIDEDSVVSSTGALSLKNVPEELIVIGAGVIGVELGSVWQRLGAKVT-AVEflgHVGGMGIDMEISKNFQRILQKQG 267
Cdd:PTZ00052 160 EDVPGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTvAVR---SIPLRGFDRQCSEKVVEYMKEQG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 268 LKFKLSTKVMGATKRPDgkiDVAVEAAAGGKNETltcDVLLVCIGRRPFTGNLGLESVGIELDKRGRIpVNGRFQTNVPN 347
Cdd:PTZ00052 237 TLFLEGVVPINIEKMDD---KIKVLFSDGTTELF---DTVLYATGRKPDIKGLNLNAIGVHVNKSNKI-IAPNDCTNIPN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 348 IYAIGDVVAG-PMLAHKAEDEGIICVEGMAGGAVHI-DYNCVPSVIYTHPEVAWVGKTEEQLKEEGVPYKVGKFPFAANS 425
Cdd:PTZ00052 310 IFAVGDVVEGrPELTPVAIKAGILLARRLFKQSNEFiDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQEFNT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 426 ------------RAKTNA-DTD----GLVKILSHKDTD-RMLGAHILGSGAGEMINEAALAMEYGASCEDVARVCHAHPT 487
Cdd:PTZ00052 390 leiaavhrekheRARKDEyDFDvssnCLAKLVCVKSEDnKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHPT 469
|
....*
gi 41393167 488 VSEAF 492
Cdd:PTZ00052 470 DAEVF 474
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
23-492 |
1.87e-42 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 159.01 E-value: 1.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 23 HGATVLSARTYADKAA-IDADVTVVGSGPGGYVAAIKAAQLGFKTVCVEKnATLGGTCLNVGCIPSKALLNNSYLYHMAH 101
Cdd:PTZ00058 30 HNLEASSAPTHLKKKPrMVYDLIVIGGGSGGMAAARRAARNKAKVALVEK-DYLGGTCVNVGCVPKKIMFNAASIHDILE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 102 gkDFESRGIEIQgISLNLEKMMAQKSGAVKALTGGIAHLFKQNKVTHVNGFGTITGKNQVTAKTA--------------- 166
Cdd:PTZ00058 109 --NSRHYGFDTQ-FSFNLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLIKKVsqvdgeadesdddev 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 167 ----------DGEQVINTKNILIATGSEvTPFPGIEIDEdSVVSSTGALSLKNvPEELIVIGAGVIGVELGSVWQRLGAK 236
Cdd:PTZ00058 186 tivsagvsqlDDGQVIEGKNILIAVGNK-PIFPDVKGKE-FTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 237 vTAVEFLGHVGGMGIDMEISKNFQRILQKQGLKFKLSTKVMGATKrpDGKIDVAVEAAAGGKNETLTCdvLLVCIGRRPF 316
Cdd:PTZ00058 263 -SYIFARGNRLLRKFDETIINELENDMKKNNINIITHANVEEIEK--VKEKNLTIYLSDGRKYEHFDY--VIYCVGRSPN 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 317 TGNLGLESVGIeLDKRGRIPVNGRFQTNVPNIYAIGDVVAGP---------MLAHKAEDEGIICVEGMAGGAVH------ 381
Cdd:PTZ00058 338 TEDLNLKALNI-KTPKGYIKVDDNQRTSVKHIYAVGDCCMVKknqeiedlnLLKLYNEEPYLKKKENTSGESYYnvqltp 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 382 --------------------IDYNCVPSVIYTHPEVAWVGKTEEQL-----KEEGVPYK-------VGKFPFAANSRAKT 429
Cdd:PTZ00058 417 vainagrlladrlfgpfsrtTNYKLIPSVIFSHPPIGTIGLSEQEAidiygKENVKIYEsrftnlfFSVYDMDPAQKEKT 496
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41393167 430 nadtdgLVKILSHKDTDRMLGAHILGSGAGEMINEAALAMEYGASCEDVARVCHAHPTVSEAF 492
Cdd:PTZ00058 497 ------YLKLVCVGKEELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIHPTAAEEF 553
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
138-391 |
1.93e-28 |
|
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: 115.29 E-value: 1.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 138 AHLFKQNKVTHVNgfgtiTGKNQVTakTADGEQVINTKnILIATGSE--VTPFPGIEIDedsvvsstGALSLKNV----- 210
Cdd:COG0446 51 IDVRTGTEVTAID-----PEAKTVT--LRDGETLSYDK-LVLATGARprPPPIPGLDLP--------GVFTLRTLddada 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 211 ---------PEELIVIGAGVIGVELGSVWQRLGAKVTAVEFLGHVGGmGIDMEISKNFQRILQKQGLKFKLSTKVMGAtk 281
Cdd:COG0446 115 lrealkefkGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLG-VLDPEMAALLEEELREHGVELRLGETVVAI-- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 282 rpDGKIDVAVEAAAGgknETLTCDVLLVCIGRRPftgNLGL-ESVGIELDKRGRIPVNGRFQTNVPNIYAIGDVV----- 355
Cdd:COG0446 192 --DGDDKVAVTLTDG---EEIPADLVVVAPGVRP---NTELaKDAGLALGERGWIKVDETLQTSDPDVYAAGDCAevphp 263
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 41393167 356 -----AGPMLAHKAEDEGIICVEGMAGGAvhIDYNCVPSVI 391
Cdd:COG0446 264 vtgktVYIPLASAANKQGRVAAENILGGP--APFPGLGTFI 302
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
42-359 |
5.80e-26 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 107.51 E-value: 5.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 42 DVTVVGSGPGGYVAAIKAAQLGFKTVCVEKNAtLGGTCLNVGCIpskallNNsYLyhmahgkdfesrGI--EIQGISLnL 119
Cdd:COG0492 2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEGGE-PGGQLATTKEI------EN-YP------------GFpeGISGPEL-A 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 120 EKMMAQ--KSGAVkaltggiahlFKQNKVTHVNgfgtiTGKNQVTAKTADGEqVINTKNILIATGSEVT--PFPGIEIDE 195
Cdd:COG0492 61 ERLREQaeRFGAE----------ILLEEVTSVD-----KDDGPFRVTTDDGT-EYEAKAVIIATGAGPRklGLPGEEEFE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 196 DSVVSSTGALSLKNVP-EELIVIGAGVIGVELGSVWQRLGAKVTAVeflgHVGGmgiDMEISKNFQ-RILQKQGLKFKLS 273
Cdd:COG0492 125 GRGVSYCATCDGFFFRgKDVVVVGGGDSALEEALYLTKFASKVTLI----HRRD---ELRASKILVeRLRANPKIEVLWN 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 274 TKVMGATKrpDGKID-VAVEAAAGGKNETLTCDVLLVCIGrrpFTGNLGL-ESVGIELDKRGRIPVNGRFQTNVPNIYAI 351
Cdd:COG0492 198 TEVTEIEG--DGRVEgVTLKNVKTGEEKELEVDGVFVAIG---LKPNTELlKGLGLELDEDGYIVVDEDMETSVPGVFAA 272
|
....*...
gi 41393167 352 GDVVAGPM 359
Cdd:COG0492 273 GDVRDYKY 280
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
145-380 |
3.31e-23 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 101.37 E-value: 3.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 145 KVTHVNgfgtiTGKNQVTakTADGEqVINTKNILIATGSE--VTPFPGIEIDedsvvsstGALSLKNV------------ 210
Cdd:COG1251 78 RVTAID-----RAARTVT--LADGE-TLPYDKLVLATGSRprVPPIPGADLP--------GVFTLRTLddadalraalap 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 211 PEELIVIGAGVIGVELGSVWQRLGAKVTAVEFLGHVGGMGIDMEISKNFQRILQKQGLKFKLSTKVmgATKRPDGKIdVA 290
Cdd:COG1251 142 GKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGV--TEIEGDDRV-TG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 291 VEAAAGgknETLTCDVLLVCIGRRPftgNLGL-ESVGIELDkRGrIPVNGRFQTNVPNIYAIGDVVA-------GPMLAH 362
Cdd:COG1251 219 VRLADG---EELPADLVVVAIGVRP---NTELaRAAGLAVD-RG-IVVDDYLRTSDPDIYAAGDCAEhpgpvygRRVLEL 290
|
250 260
....*....|....*....|
gi 41393167 363 --KAEDEGIICVEGMAGGAV 380
Cdd:COG1251 291 vaPAYEQARVAAANLAGGPA 310
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
159-468 |
5.74e-17 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 83.17 E-value: 5.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 159 NQVTAKTADGEQVINTK--NILIATG--SEVTPFPGIEIDEDSVVSS-TGALSLKNVPEE-----LIVIGAGVIGVELGS 228
Cdd:PRK09564 87 KTITVKNLKTGSIFNDTydKLMIATGarPIIPPIKNINLENVYTLKSmEDGLALKELLKDeeiknIVIIGAGFIGLEAVE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 229 VWQRLGAKVTAVEFLGHVGGMGIDMEISKNFQRILQKQGLKFKLSTKVmgatKRPDGkiDVAVEAAAGGKNETLTcDVLL 308
Cdd:PRK09564 167 AAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHLNEFV----KSLIG--EDKVEGVVTDKGEYEA-DVVI 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 309 VCIGRRPFTGnlGLESVGIELDKRGRIPVNGRFQTNVPNIYAIGD-------VVAGPM---LAHKAEDEGIICVEGMAGG 378
Cdd:PRK09564 240 VATGVKPNTE--FLEDTGLKTLKNGAIIVDEYGETSIENIYAAGDcatiyniVSNKNVyvpLATTANKLGRMVGENLAGR 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 379 AVH----IDYNCVPSVIYthpEVAWVGKTEEQLKEEGVPYKVgKFPFAANSRAKTNADTDGLVKILSHKDTDRMLGAHIL 454
Cdd:PRK09564 318 HVSfkgtLGSACIKVLDL---EAARTGLTEEEAKKLGIDYKT-VFIKDKNHTNYYPGQEDLYVKLIYEADTKVILGGQII 393
|
330
....*....|....*
gi 41393167 455 G-SGAGEMINEAALA 468
Cdd:PRK09564 394 GkKGAVLRIDALAVA 408
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
137-356 |
7.08e-14 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 73.24 E-value: 7.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 137 IAHLFKQNKVTHVNGfgTITG----KNQVTakTADGEQV-----IntknilIATGSeVTPFPGIE-IDEDsvvsstgALS 206
Cdd:COG1252 62 LRELLRRAGVRFIQG--EVTGidpeARTVT--LADGRTLsydylV------IATGS-VTNFFGIPgLAEH-------ALP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 207 LKNVPE---------------------ELIVIGAGVIGVEL-GSVWQRLG------------AKVTAVEFLGHVGGmGID 252
Cdd:COG1252 124 LKTLEDalalrerllaaferaerrrllTIVVVGGGPTGVELaGELAELLRkllrypgidpdkVRITLVEAGPRILP-GLG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 253 MEISKNFQRILQKQGLKFKLSTKVMGATkrPDGkidvaVEAAAGgknETLTCDVLLVCIGrrpFTGNLGLESVGIELDKR 332
Cdd:COG1252 203 EKLSEAAEKELEKRGVEVHTGTRVTEVD--ADG-----VTLEDG---EEIPADTVIWAAG---VKAPPLLADLGLPTDRR 269
|
250 260
....*....|....*....|....*
gi 41393167 333 GRIPVNGRFQT-NVPNIYAIGDVVA 356
Cdd:COG1252 270 GRVLVDPTLQVpGHPNVFAIGDCAA 294
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
216-353 |
9.35e-14 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 72.64 E-value: 9.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 216 VIGAGVIGVELGSVWQRLGAKVTAVEFLGHVGGMGIDMEISKNFQRILQKQGLKFKLSTKVMGATKRPDGkidVAVEAAA 295
Cdd:PRK04965 146 VVGGGLIGTELAMDLCRAGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSG---IRATLDS 222
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 41393167 296 GgknETLTCDVLLVCIGRRPFTGnLGLESvGIELdKRGrIPVNGRFQTNVPNIYAIGD 353
Cdd:PRK04965 223 G---RSIEVDAVIAAAGLRPNTA-LARRA-GLAV-NRG-IVVDSYLQTSAPDIYALGD 273
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
214-286 |
1.27e-13 |
|
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: 66.07 E-value: 1.27e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41393167 214 LIVIGAGVIGVELGSVWQRLGAKVTAVEFLGHVGGmGIDMEISKNFQRILQKQGLKFKLSTKVMGATKRPDGK 286
Cdd:pfam00070 2 VVVVGGGYIGLELAGALARLGSKVTVVERRDRLLP-GFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGV 73
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
215-355 |
1.20e-12 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 69.81 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 215 IVIGAGVIGVE-LGSVWQRlGAKVTAVEFLGHVGGMgIDMEISKNFQRILQKQGLKFKLSTKVmgatkrpdGKIDVAVEA 293
Cdd:PRK13512 152 LVVGAGYISLEvLENLYER-GLHPTLIHRSDKINKL-MDADMNQPILDELDKREIPYRLNEEI--------DAINGNEVT 221
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41393167 294 AAGGKNETLtcDVLLVCIGRRPFTGNLglESVGIELDKRGRIPVNGRFQTNVPNIYAIGDVV 355
Cdd:PRK13512 222 FKSGKVEHY--DMIIEGVGTHPNSKFI--ESSNIKLDDKGFIPVNDKFETNVPNIYAIGDII 279
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
297-383 |
8.56e-11 |
|
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: 64.00 E-value: 8.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 297 GKNETLTCDVLLVCIGrrpFTGNLG--LESVGIELDKRGRIPVNGR-FQTNVPNIYAIGDVVAGPMLAhkaedegiicVE 373
Cdd:COG0493 353 GSEFTLPADLVILAIG---QTPDPSglEEELGLELDKRGTIVVDEEtYQTSLPGVFAGGDAVRGPSLV----------VW 419
|
90
....*....|...
gi 41393167 374 GMAGG---AVHID 383
Cdd:COG0493 420 AIAEGrkaARAID 432
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
296-368 |
1.08e-09 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 60.00 E-value: 1.08e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41393167 296 GGKNETLTCDVLLVCIGRRPfTGNLGLESVGIELDKRGRIPVNGRFQTNVPNIYAIGDVVAGPMLAHKAEDEG 368
Cdd:PRK12770 267 PGSEFVLEADTVVFAIGEIP-TPPFAKECLGIELNRKGEIVVDEKHMTSREGVFAAGDVVTGPSKIGKAIKSG 338
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
177-354 |
1.63e-09 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 59.55 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 177 ILIATGSEVTPFPGIEIDEDSVVS---STGALSLKNVPEE---LIVIGAGVIGVELGSVWQRLGAKVTAVEFLGHVGGMG 250
Cdd:PRK09754 104 LFIATGAAARPLPLLDALGERCFTlrhAGDAARLREVLQPersVVIVGAGTIGLELAASATQRRCKVTVIELAATVMGRN 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 251 IDMEISKNFQRILQKQGLKFKLSTKVMGATKRPdgkiDVAVEAAAGgknETLTCDVLLVCIGRRpFTGNLGLESvgiELD 330
Cdd:PRK09754 184 APPPVQRYLLQRHQQAGVRILLNNAIEHVVDGE----KVELTLQSG---ETLQADVVIYGIGIS-ANDQLAREA---NLD 252
|
170 180
....*....|....*....|....
gi 41393167 331 KRGRIPVNGRFQTNVPNIYAIGDV 354
Cdd:PRK09754 253 TANGIVIDEACRTCDPAIFAGGDV 276
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
167-356 |
9.32e-09 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 57.92 E-value: 9.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 167 DGEQVINTKNILIATGSE--VTPFPGIE---------IDEDSVVSSTGALSLKNVpeeliVIGAGVIGVELGSVWQRLGA 235
Cdd:TIGR02374 90 DAGRTLSYDKLILATGSYpfILPIPGADkkgvyvfrtIEDLDAIMAMAQRFKKAA-----VIGGGLLGLEAAVGLQNLGM 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 236 KVTAVEFLGHVGGMGIDMEISKNFQRILQKQGLKFKLSTKVMGATKrpdgkiDVAVEAAAGGKNETLTCDVLLVCIGRRP 315
Cdd:TIGR02374 165 DVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVG------ATKADRIRFKDGSSLEADLIVMAAGIRP 238
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 41393167 316 FTgNLGLESvGIELDkrGRIPVNGRFQTNVPNIYAIGDVVA 356
Cdd:TIGR02374 239 ND-ELAVSA-GIKVN--RGIIVNDSMQTSDPDIYAVGECAE 275
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
300-375 |
1.30e-07 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 54.01 E-value: 1.30e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41393167 300 ETLTCDVLLVCIGRRPFTGNLgLESVGIELDKRGRIPVN-GRFQTNVPNIYAIGDVVAGPMLAHKAEDEGIICVEGM 375
Cdd:PRK12810 385 FVLPADLVLLAMGFTGPEAGL-LAQFGVELDERGRVAAPdNAYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAI 460
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
42-78 |
1.88e-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: 53.38 E-value: 1.88e-07
10 20 30
....*....|....*....|....*....|....*..
gi 41393167 42 DVTVVGSGPGGYVAAIKAAQLGFKTVCVEKNATLGGT 78
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGM 37
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
40-366 |
6.95e-07 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 51.69 E-value: 6.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 40 DADVTVVGSGPGGYVAAIKAAQLGFKTVCVEKNATLGGTcLNVGcIPSKALLNNsylyhmAHGKD---FESRGIEIQ--- 113
Cdd:PRK13984 283 NKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGV-MRYG-IPSYRLPDE------ALDKDiafIEALGVKIHlnt 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 114 --GISLNLEKMmAQKSGAVKALTGgiahlFKQNKVTHVNGfgtitgknqvtaktADGEQVINTKNILiatgSEVTPF--- 188
Cdd:PRK13984 355 rvGKDIPLEEL-REKHDAVFLSTG-----FTLGRSTRIPG--------------TDHPDVIQALPLL----REIRDYlrg 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 189 --PGIEIdedsvvsstgalslknvPEELIVIGAGVIGVELGSVWQRL--------GAKVTAVEflGHVGGMGIDM-EISK 257
Cdd:PRK13984 411 egPKPKI-----------------PRSLVVIGGGNVAMDIARSMARLqkmeygevNVKVTSLE--RTFEEMPADMeEIEE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 258 NF------------QRIL----QKQGLKFKLSTKVMGATKRPDGKIDVAVEAaaggkneTLTCDVLLVCIGRRPFTGNLG 321
Cdd:PRK13984 472 GLeegvviypgwgpMEVViendKVKGVKFKKCVEVFDEEGRFNPKFDESDQI-------IVEADMVVEAIGQAPDYSYLP 544
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 41393167 322 lESVGIELD-KRGRIPVNGRFQTNVPNIYAIGDVVAGPMLAHKAED 366
Cdd:PRK13984 545 -EELKSKLEfVRGRILTNEYGQTSIPWLFAGGDIVHGPDIIHGVAD 589
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
42-77 |
1.42e-06 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 50.62 E-value: 1.42e-06
10 20 30
....*....|....*....|....*....|....*.
gi 41393167 42 DVTVVGSGPGGYVAAIKAAQLGFKTVCVEKNATLGG 77
Cdd:COG1233 5 DVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
42-78 |
2.09e-06 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 50.42 E-value: 2.09e-06
10 20 30
....*....|....*....|....*....|....*..
gi 41393167 42 DVTVVGSGPGGYVAAIKAAQLGFKTVCVEKNATLGGT 78
Cdd:PRK07843 9 DVVVVGSGAAGMVAALTAAHRGLSTVVVEKAPHYGGS 45
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
39-78 |
3.04e-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: 3.04e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 41393167 39 IDADVTVVGSGPGGYVAAIKAAQLGFKTVCVEKNATLGGT 78
Cdd:COG1053 2 HEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGGH 41
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
38-78 |
3.30e-06 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 49.72 E-value: 3.30e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 41393167 38 AIDADVTVVGSGPGGYVAAIKAAQLGFKTVCVEKNATLGGT 78
Cdd:PRK06134 10 DLECDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGGT 50
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
42-91 |
5.44e-06 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 48.70 E-value: 5.44e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 41393167 42 DVTVVGSGPGGYVAAIKAAQLGFKTVCVeknATLGGTCLNVGCIPSKALL 91
Cdd:pfam01134 1 DVIVIGGGHAGCEAALAAARMGAKVLLI---THNTDTIAELSCNPSIGGI 47
|
|
| PRK12835 |
PRK12835 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
42-85 |
1.39e-05 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237221 [Multi-domain] Cd Length: 584 Bit Score: 47.49 E-value: 1.39e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 41393167 42 DVTVVGSGPGGYVAAIKAAQLGFKTVCVEKNATLGG-TCLNVGCI 85
Cdd:PRK12835 13 DVLVVGSGGGGMTAALTAAARGLDTLVVEKSAHFGGsTALSGGGI 57
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
170-353 |
3.23e-05 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 46.65 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 170 QVINTKNILIATGSE--VTPFPGIE---------IDEDSVVSSTGALSLKNVpeeliVIGAGVIGVELGSVWQRLGAKVT 238
Cdd:PRK14989 98 RTVFYDKLIMATGSYpwIPPIKGSEtqdcfvyrtIEDLNAIEACARRSKRGA-----VVGGGLLGLEAAGALKNLGVETH 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 239 AVEF--------LGHVGG---------MGIDMEISKNFQRILQkQGLKfklSTKVMgatKRPDGkidvaveaaaggknET 301
Cdd:PRK14989 173 VIEFapmlmaeqLDQMGGeqlrrkiesMGVRVHTSKNTLEIVQ-EGVE---ARKTM---RFADG--------------SE 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 41393167 302 LTCDVLLVCIGRRPfTGNLGLESvGIELDKRGRIPVNGRFQTNVPNIYAIGD 353
Cdd:PRK14989 232 LEVDFIVFSTGIRP-QDKLATQC-GLAVAPRGGIVINDSCQTSDPDIYAIGE 281
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
36-182 |
3.83e-05 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 46.39 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 36 KAAIDADVTVVGSGPGGYVAAIKAAQLGFKTVCVEKNATLGGtclnvgcipskallnnsylyHMAH-GKDFESRGIEIQG 114
Cdd:COG1148 136 KVPVNKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGG--------------------RAAQlHKTFPGLDCPQCI 195
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41393167 115 islnLEKMMAQksgaVKAlTGGIaHLFKQNKVTHVNGFGtitGKNQVT-AKTADGEQVINTKNILIATG 182
Cdd:COG1148 196 ----LEPLIAE----VEA-NPNI-TVYTGAEVEEVSGYV---GNFTVTiKKGPREEIEIEVGAIVLATG 251
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
42-78 |
3.95e-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: 45.74 E-value: 3.95e-05
10 20 30
....*....|....*....|....*....|....*..
gi 41393167 42 DVTVVGSGPGGYVAAIKAAQLGFKTVCVEKNATLGGT 78
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGA 37
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
38-77 |
4.69e-05 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 45.98 E-value: 4.69e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 41393167 38 AIDADVTVVGSGPGGYVAAIKAAQLGFKTVCVEKNATLGG 77
Cdd:PRK12839 6 THTYDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKASTCGG 45
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
37-78 |
6.09e-05 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 45.45 E-value: 6.09e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 41393167 37 AAIDADVTVVGSGPGGYVAAIKAAQLGFKTVCVEKNATLGGT 78
Cdd:PRK12842 6 NELTCDVLVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGGT 47
|
|
| PRK12844 |
PRK12844 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
41-78 |
6.12e-05 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 183787 [Multi-domain] Cd Length: 557 Bit Score: 45.52 E-value: 6.12e-05
10 20 30
....*....|....*....|....*....|....*...
gi 41393167 41 ADVTVVGSGPGGYVAAIKAAQLGFKTVCVEKNATLGGT 78
Cdd:PRK12844 7 YDVVVVGSGGGGMCAALAAADSGLEPLIVEKQDKVGGS 44
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
45-79 |
7.30e-05 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 40.98 E-value: 7.30e-05
10 20 30
....*....|....*....|....*....|....*
gi 41393167 45 VVGSGPGGYVAAIKAAQLGFKTVCVEKNATLGGTC 79
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNA 35
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
42-78 |
1.42e-04 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 44.34 E-value: 1.42e-04
10 20 30
....*....|....*....|....*....|....*..
gi 41393167 42 DVTVVGSGPGGYVAAIKAAQLGFKTVCVEKNATLGGT 78
Cdd:PRK12843 18 DVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGT 54
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
297-357 |
1.58e-04 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 44.01 E-value: 1.58e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41393167 297 GKNETLTCDVLLVCIGRRPFTgNLGLESVGIELDKRG-RIPVNGRFQTNVPNIYAIGDVVAG 357
Cdd:PRK11749 369 GSEFTLPADLVIKAIGQTPNP-LILSTTPGLELNRWGtIIADDETGRTSLPGVFAGGDIVTG 429
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
289-357 |
4.01e-04 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 43.19 E-value: 4.01e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 289 VAVEaaagGKNETLTCDVLLVCIGRRPftGNLGLESV-GIELDKRGRIPVNGRFQTNVPNIYAIGDVVAG 357
Cdd:PRK12778 664 VAIP----GSTFTVDVDLVIVSVGVSP--NPLVPSSIpGLELNRKGTIVVDEEMQSSIPGIYAGGDIVRG 727
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
322-376 |
4.48e-04 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 42.81 E-value: 4.48e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 41393167 322 LESVGIELDKRGRI--PVNGRF--QTNVPNIYAIGDVVAGPMLAHKAEDEGIICVEGMA 376
Cdd:PRK12769 590 LESHGVTVDKWGRIiaDVESQYryQTSNPKIFAGGDAVRGADLVVTAMAEGRHAAQGII 648
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
42-78 |
6.06e-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: 42.16 E-value: 6.06e-04
10 20 30
....*....|....*....|....*....|....*..
gi 41393167 42 DVTVVGSGPGGYVAAIKAAQLGFKTVCVEKNATLGGT 78
Cdd:COG2072 8 DVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGT 44
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
42-111 |
2.42e-03 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 40.26 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393167 42 DVTVVGSGPGGYVAAIKAAQLGFKTVCVEKNATLG--------GTClNV--GCIPSKALL-----NNSYLYHM--AHGKD 104
Cdd:pfam03486 2 DVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLGrkilisggGRC-NVtnLSEEPDNFLsrypgNPKFLKSAlsRFTPW 80
|
90
....*....|..
gi 41393167 105 -----FESRGIE 111
Cdd:pfam03486 81 dfiafFESLGVP 92
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
327-354 |
5.10e-03 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 39.37 E-value: 5.10e-03
10 20
....*....|....*....|....*...
gi 41393167 327 IELDKRGRIPVNGRFQTNVPNIYAIGDV 354
Cdd:PRK15317 458 VELNRRGEIIVDARGATSVPGVFAAGDC 485
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
24-66 |
8.00e-03 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 38.60 E-value: 8.00e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 41393167 24 GATVLSARTYADKAAIDadVTVVGSGPGGYVAAIKAAQLGFKT 66
Cdd:PRK15317 197 GAAARAAEELNAKDPYD--VLVVGGGPAGAAAAIYAARKGIRT 237
|
|
| |
