|
Name |
Accession |
Description |
Interval |
E-value |
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
2-457 |
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: 596.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 2 NYDLIIIGAGPAGYVAAEYAGKHKLKTLVVEKEYFGGVCLNVGCIPTKTLLKRAKIVDYLRHAQDYGISINGqVALNWNQ 81
Cdd:TIGR01350 1 AYDVIVIGGGPGGYVAAIRAAQLGLKVALVEKEYLGGTCLNVGCIPTKALLHSAEVYDEIKHAKDLGIEVEN-VSVDWEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 82 LLEQKGKVVSKLVGGVKAIIASAKAETVMGEAKVLDPNTVEVAGK----TYTTKSIVVATGSRPRYLTLPgFAEARQngF 157
Cdd:TIGR01350 80 MQKRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGEngeeTLEAKNIIIATGSRPRSLPGP-FDFDGK--V 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 158 VIDSTQALSLEGVPRKLVVVGGGVIGIEFAFLYASLGSEVTILQGVDRILEIFDTEVSDLVAKLLQTKNVKIITNAQVT- 236
Cdd:TIGR01350 157 VITSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTa 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 237 -RANNNEVFYSQNGQE-GSVVGDRILVSIGRIPNTE--CLDGLNLQRDERNRIVLNQDLQTSIPNIYIVGDANAQLMLAH 312
Cdd:TIGR01350 237 vEKNDDQVTYENKGGEtETLTGEKVLVAVGRKPNTEglGLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDVIGGPMLAH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 313 FAYQQGRYAVNHILNKKQVkPAQKLTCPSCIYTNPEVASVGYTEMELKKQGIPYVKTNLVLAHCGKAIADNETNGFVKMM 392
Cdd:TIGR01350 317 VASHEGIVAAENIAGKEPA-HIDYDAVPSVIYTDPEVASVGLTEEQAKEAGYDVKIGKFPFAANGKALALGETDGFVKII 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504387862 393 FDPQTGKILGCCIIAATASDMIAELALAMDAGLTLFDIANSISPHPTINEMIADVCKKALFDHFK 457
Cdd:TIGR01350 396 ADKKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEAIKEAALAALGKPIH 460
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
1-452 |
3.55e-175 |
|
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: 498.46 E-value: 3.55e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 1 MNYDLIIIGAGPAGYVAAEYAGKHKLKTLVVEKEYFGGVCLNVGCIPTKTLLKRAKIVDYLRHAQDYGISInGQVALNWN 80
Cdd:COG1249 2 KDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISA-GAPSVDWA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 81 QLLEQKGKVVSKLVGGVKAIIASAKAETVMGEAKVLDPNTVEVAG-KTYTTKSIVVATGSRPRYLTLPGFAEARqngfVI 159
Cdd:COG1249 81 ALMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVTGgETLTADHIVIATGSRPRVPPIPGLDEVR----VL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 160 DSTQALSLEGVPRKLvvvgggvigiEFAFLYASLGSEVTILQGVDRILEIFDTEVSDLVAKLLQTKNVKIITNAQVTRAN 239
Cdd:COG1249 157 TSDEALELEELPKSLvvigggyiglEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 240 NNE----VFYSQNGQEGSVVGDRILVSIGRIPNTEC--LDGLNLQRDERNRIVLNQDLQTSIPNIYIVGDANAQLMLAHF 313
Cdd:COG1249 237 KTGdgvtVTLEDGGGEEAVEADKVLVATGRRPNTDGlgLEAAGVELDERGGIKVDEYLRTSVPGIYAIGDVTGGPQLAHV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 314 AYQQGRYAVNHILNKKqVKPAQKLTCPSCIYTNPEVASVGYTEMELKKQGIPYVKTNLVLAHCGKAIADNETNGFVKMMF 393
Cdd:COG1249 317 ASAEGRVAAENILGKK-PRPVDYRAIPSVVFTDPEIASVGLTEEEAREAGIDVKVGKFPFAANGRALALGETEGFVKLIA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 504387862 394 DPQTGKILGCCIIAATASDMIAELALAMDAGLTLFDIANSISPHPTINEMIADVCKKAL 452
Cdd:COG1249 396 DAETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAALALL 454
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
1-444 |
1.05e-146 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 426.48 E-value: 1.05e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 1 MNYDLIIIGAGPAGYVAAEYAGKHKLKTLVVEKEYFGGVCLNVGCIPTKTLLKRAKIVDYLRHAQDYGISInGQVALNWN 80
Cdd:PRK06416 3 FEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIKA-ENVGIDFK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 81 QLLEQKGKVVSKLVGGVKAIIASAKAETVMGEAKVLDPNTVEV----AGKTYTTKSIVVATGSRPRylTLPGF-AEARqn 155
Cdd:PRK06416 82 KVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVmtedGEQTYTAKNIILATGSRPR--ELPGIeIDGR-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 156 gFVIDSTQALSLEGVPRKLVVVGGGVIGIEFAFLYASLGSEVTILQGVDRILEIFDTEVSDLVAKLLQTKNVKIITNAQV 235
Cdd:PRK06416 158 -VIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPGEDKEISKLAERALKKRGIKIKTGAKA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 236 TRA----NNNEVFYSQNGQEGSVVGDRILVSIGRIPNTECLdGLNLQRDERNR--IVLNQDLQTSIPNIYIVGDANAQLM 309
Cdd:PRK06416 237 KKVeqtdDGVTVTLEDGGKEETLEADYVLVAVGRRPNTENL-GLEELGVKTDRgfIEVDEQLRTNVPNIYAIGDIVGGPM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 310 LAHFAYQQGRYAVNHILNKKQvkPAQKLTCPSCIYTNPEVASVGYTEMELKKQGIPYVKTNLVLAHCGKAIADNETNGFV 389
Cdd:PRK06416 316 LAHKASAEGIIAAEAIAGNPH--PIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFDVKVVKFPFAGNGKALALGETDGFV 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 504387862 390 KMMFDPQTGKILGCCIIAATASDMIAELALAMDAGLTLFDIANSISPHPTINEMI 444
Cdd:PRK06416 394 KLIFDKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEAL 448
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
1-454 |
8.44e-142 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 413.80 E-value: 8.44e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 1 MNYDLIIIGAGPAGYVAAEYAGKHKLKTLVVEKEYFGGVCLNVGCIPTKTLLKRAKIVDYLRHAQDYGISINGqVALNWN 80
Cdd:PRK06292 2 EKYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGPLGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHADG-PKIDFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 81 QLLEQKGKVVSKLVGGV-KAIIASAKAETVMGEAKVLDPNTVEVAGKTYTTKSIVVATGSR-PRYLTLPGFAEARqngfV 158
Cdd:PRK06292 81 KVMARVRRERDRFVGGVvEGLEKKPKIDKIKGTARFVDPNTVEVNGERIEAKNIVIATGSRvPPIPGVWLILGDR----L 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 159 IDSTQALSLEGVPRKLVVVGGGVIGIEFAFLYASLGSEVTILQGVDRILEIFDTEVSDLVAKLLQtKNVKIITNAQVTRA 238
Cdd:PRK06292 157 LTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILS-KEFKIKLGAKVTSV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 239 ----NNNEVFYSQNGQEGSVVGDRILVSIGRIPNTECL--DGLNLQRDERNRIVLNQDLQTSIPNIYIVGDANAQLMLAH 312
Cdd:PRK06292 236 eksgDEKVEELEKGGKTETIEADYVLVATGRRPNTDGLglENTGIELDERGRPVVDEHTQTSVPGIYAAGDVNGKPPLLH 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 313 FAYQQGRYAVNHILNKKQVKpAQKLTCPSCIYTNPEVASVGYTEMELKKQGIPYVKTNLVLAHCGKAIADNETNGFVKMM 392
Cdd:PRK06292 316 EAADEGRIAAENAAGDVAGG-VRYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEVPFEAQGRARVMGKNDGFVKVY 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504387862 393 FDPQTGKILGCCIIAATASDMIAELALAMDAGLTLFDIANSISPHPTINEMIadvcKKALFD 454
Cdd:PRK06292 395 ADKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGL----RTALRD 452
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
3-457 |
5.72e-114 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 342.95 E-value: 5.72e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 3 YDLIIIGAGPAGYVAAEYAGKHKLKTLVVEKEYFGGVCLNVGCIPTKTLLKRAKIVDYLRHAQDYGISINGQVALNWNQL 82
Cdd:PRK06370 6 YDAIVIGAGQAGPPLAARAAGLGMKVALIERGLLGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGGPVSVDFKAV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 83 LEQKGKVVSKLVGGVKAIIASAKAETV-MGEAKVLDPNTVEVAGKTYTTKSIVVATGSRPRYLTLPGFAEArqnGFvIDS 161
Cdd:PRK06370 86 MARKRRIRARSRHGSEQWLRGLEGVDVfRGHARFESPNTVRVGGETLRAKRIFINTGARAAIPPIPGLDEV---GY-LTN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 162 TQALSLEGVPRKLVVVGGGVIGIEFAFLYASLGSEVTILQGVDRILEIFDTEVSDLVAKLLQTKNVKIITNAQVTRANNN 241
Cdd:PRK06370 162 ETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILEREGIDVRLNAECIRVERD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 242 E----VFYSQNGQEGSVVGDRILVSIGRIPNTeclDGLNLQR-----DERNRIVLNQDLQTSIPNIYIVGDANAQLMLAH 312
Cdd:PRK06370 242 GdgiaVGLDCNGGAPEITGSHILVAVGRVPNT---DDLGLEAagvetDARGYIKVDDQLRTTNPGIYAAGDCNGRGAFTH 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 313 FAYQQGRYAVNHILNKKQVKPAQkLTCPSCIYTNPEVASVGYTEMELKKQGIPYVKTNLVLAHCGKAIADNETNGFVKMM 392
Cdd:PRK06370 319 TAYNDARIVAANLLDGGRRKVSD-RIVPYATYTDPPLARVGMTEAEARKSGRRVLVGTRPMTRVGRAVEKGETQGFMKVV 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504387862 393 FDPQTGKILGCCIIAATASDMIAELALAMDAGLTLFDIANSISPHPTINEMIadvckKALFDHFK 457
Cdd:PRK06370 398 VDADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELI-----PTLAQALR 457
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
2-456 |
1.40e-102 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 314.17 E-value: 1.40e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 2 NYDLIIIGAGPAGYVAAEYAGKHKLKTLVVEkEYF--------GGVCLNVGCIPTKTLLKRAKIVDYLRHA-QDYGISIN 72
Cdd:PRK06327 4 QFDVVVIGAGPGGYVAAIRAAQLGLKVACIE-AWKnpkgkpalGGTCLNVGCIPSKALLASSEEFENAGHHfADHGIHVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 73 GqVALNWNQLLEQKGKVVSKLVGGVKAIIASAKAETVMG----EAKVLDPNTVEVAGK---TYTTKSIVVATGSRPRylT 145
Cdd:PRK06327 83 G-VKIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGrgsfVGKTDAGYEIKVTGEdetVITAKHVIIATGSEPR--H 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 146 LPGFAEARQNgfVIDSTQALSLEGVPRKLVVVGGGVIGIEFAFLYASLGSEVTILQGVDRILEIFDTEVSDLVAKLLQTK 225
Cdd:PRK06327 160 LPGVPFDNKI--ILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAAADEQVAKEAAKAFTKQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 226 NVKIITNAQVTR----ANNNEVFYS-QNGQEGSVVGDRILVSIGRIPNTECL--DGLNLQRDERNRIVLNQDLQTSIPNI 298
Cdd:PRK06327 238 GLDIHLGVKIGEiktgGKGVSVAYTdADGEAQTLEVDKLIVSIGRVPNTDGLglEAVGLKLDERGFIPVDDHCRTNVPNV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 299 YIVGDANAQLMLAHFAYQQGRYAVNHILNKKQVkpAQKLTCPSCIYTNPEVASVGYTEMELKKQGIPYVKTNLVLAHCGK 378
Cdd:PRK06327 318 YAIGDVVRGPMLAHKAEEEGVAVAERIAGQKGH--IDYNTIPWVIYTSPEIAWVGKTEQQLKAEGVEYKAGKFPFMANGR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 379 AIADNETNGFVKMMFDPQTGKILGCCIIAATASDMIAELALAMDAGLTLFDIANSISPHPTINEMIAD----VCKKALfd 454
Cdd:PRK06327 396 ALAMGEPDGFVKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEVWHEaalaVDKRPL-- 473
|
..
gi 504387862 455 HF 456
Cdd:PRK06327 474 HF 475
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
3-444 |
5.63e-89 |
|
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: 278.54 E-value: 5.63e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 3 YDLIIIGAGPAGYVAAEYAGKHKLKTLVVEKEYFGGVCLNVGCIPTKTLLKRAKIVDYLRHAQDYGISINGQVALnwNQL 82
Cdd:TIGR02053 1 YDLVIIGSGAAAFAAAIKAAELGASVAMVERGPLGGTCVNVGCVPSKMLLRAAEVAHYARKPPFGGLAATVAVDF--GEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 83 LEQKGKVVSKL-VGGVKAIIASAKAETVMGEAKVLDPNTVEVAGKTYTT--KSIVVATGSRPRYLTLPGFAEARqngfVI 159
Cdd:TIGR02053 79 LEGKREVVEELrHEKYEDVLSSYGVDYLRGRARFKDPKTVKVDLGREVRgaKRFLIATGARPAIPPIPGLKEAG----YL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 160 DSTQALSLEGVPRKLVVVGGGVIGIEFAFLYASLGSEVTILQGVDRILEIFDTEVSDLVAKLLQTKNVKIITNAQVTRAN 239
Cdd:TIGR02053 155 TSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSDRLLPREEPEISAAVEEALAEEGIEVVTSAQVKAVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 240 NNE----VFYSQNGQEGSVVGDRILVSIGRIPNTeclDGLNLQR-----DERNRIVLNQDLQTSIPNIYIVGDANAQLML 310
Cdd:TIGR02053 235 VRGggkiITVEKPGGQGEVEADELLVATGRRPNT---DGLGLEKagvklDERGGILVDETLRTSNPGIYAAGDVTGGLQL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 311 AHFAYQQG-RYAVNHILNKKqvKPAQKLTCPSCIYTNPEVASVGYTEMELKKQGIPYVKTNLVLAHCGKAIADNETNGFV 389
Cdd:TIGR02053 312 EYVAAKEGvVAAENALGGAN--AKLDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNVPRARINRDTRGFI 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 504387862 390 KMMFDPQTGKILGCCIIAATASDMIAELALAMDAGLTLFDIANSISPHPTINEMI 444
Cdd:TIGR02053 390 KLVAEPGTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGL 444
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
3-318 |
7.74e-77 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 241.84 E-value: 7.74e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 3 YDLIIIGAGPAGYVAAEYAGKHKLKTLVVEKEyfgGVCLNVGCIPTKTLLKRAKIVDYLRHaqdygisingqvalnWNQL 82
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDE---GTCPYGGCVLSKALLGAAEAPEIASL---------------WADL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 83 LEQKGKVVSKLVGGVKAIIASAKAETVMGEAKVLDPNTVEVAGKTYTTKSIVVATGSRPRYLTLPGFAE-ARQNGFVIDS 161
Cdd:pfam07992 63 YKRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELVDGDGETITYDRLVIATGARPRLPPIPGVELnVGFLVRTLDS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 162 TQALSLEGVPRKLVVVGGGVIGIEFAFLYASLGSEVTILQGVDRILEIFDTEVSDLVAKLLQTKNVKIITNAQVTRANNN 241
Cdd:pfam07992 143 AEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGD 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504387862 242 EVFYSQNGQEGSVV-GDRILVSIGRIPNTECLDGLNLQRDERNRIVLNQDLQTSIPNIYIVGDANAQ-LMLAHFAYQQG 318
Cdd:pfam07992 223 GDGVEVILKDGTEIdADLVVVAIGRRPNTELLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDCRVGgPELAQNAVAQG 301
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
1-414 |
1.23e-73 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 238.90 E-value: 1.23e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 1 MNYDLIIIGAGPAGYVAAEYAGKHKLKTLVVEKEY-FGGVCLNVGCIPTKTLlkrakivdylRHA-------------QD 66
Cdd:PRK05249 4 YDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYRnVGGGCTHTGTIPSKAL----------REAvlrligfnqnplySS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 67 YGISINgqvaLNWNQLLEQKGKVVSKLVGGVKAIIASAKAETVMGEAKVLDPNTVEVAG-----KTYTTKSIVVATGSRP 141
Cdd:PRK05249 74 YRVKLR----ITFADLLARADHVINKQVEVRRGQYERNRVDLIQGRARFVDPHTVEVECpdgevETLTADKIVIATGSRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 142 RYLTLPGFAEARqngfVIDSTQALSLEGVPRKLVVVGGGVIGIEFAFLYASLGSEVTILQGVDRILEIFDTEVSDLVAKL 221
Cdd:PRK05249 150 YRPPDVDFDHPR----IYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSFLDDEISDALSYH 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 222 LQTKNVKIITNAQVTRANNNE---VFYSQNGQEgsVVGDRILVSIGRIPNTE--CLDGLNLQRDERNRIVLNQDLQTSIP 296
Cdd:PRK05249 226 LRDSGVTIRHNEEVEKVEGGDdgvIVHLKSGKK--IKADCLLYANGRTGNTDglNLENAGLEADSRGQLKVNENYQTAVP 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 297 NIYIVGDANAQLMLAHFAYQQGRYAVNHILNKKQVKPAQKLtcPSCIYTNPEVASVGYTEMELKKQGIPYVktnlvlahC 376
Cdd:PRK05249 304 HIYAVGDVIGFPSLASASMDQGRIAAQHAVGEATAHLIEDI--PTGIYTIPEISSVGKTEQELTAAKVPYE--------V 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 504387862 377 GKA---------IAdNETNGFVKMMFDPQTGKILGCCIIAATASDMI 414
Cdd:PRK05249 374 GRArfkelaraqIA-GDNVGMLKILFHRETLEILGVHCFGERATEII 419
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
3-439 |
7.83e-69 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 225.81 E-value: 7.83e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 3 YDLIIIGAGPAGYVAAEYAGKHKLKTLVVEKEYFGGVCLNVGCIPTKTLLKRAKIVDYLRH-AQDYGISInGQVALNWNQ 81
Cdd:PRK06116 5 YDLIVIGGGSGGIASANRAAMYGAKVALIEAKRLGGTCVNVGCVPKKLMWYGAQIAEAFHDyAPGYGFDV-TENKFDWAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 82 LLEQKGKVVSKLVGGVKAIIASAKAETVMGEAKVLDPNTVEVAGKTYTTKSIVVATGSRPRYLTLPGfAEarqngFVIDS 161
Cdd:PRK06116 84 LIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNGERYTADHILIATGGRPSIPDIPG-AE-----YGITS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 162 TQALSLEGVPRKLVVVGGGVIGIEFAFLYASLGSEVTILQGVDRILEIFDTEVSDLVAKLLQTKNVKIITNAQVTR---- 237
Cdd:PRK06116 158 DGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAvekn 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 238 ANNNEVFYSQNGQEGSVvgDRILVSIGRIPNTeclDGLNLQR-----DERNRIVLNQDLQTSIPNIYIVGDANAQLMLAH 312
Cdd:PRK06116 238 ADGSLTLTLEDGETLTV--DCLIWAIGREPNT---DGLGLENagvklNEKGYIIVDEYQNTNVPGIYAVGDVTGRVELTP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 313 FAYQQGRYAVNHILNKKQVKPAQKLTCPSCIYTNPEVASVGYTEMELKKQgipYVKTNLvlaHCGK--------AIADNE 384
Cdd:PRK06116 313 VAIAAGRRLSERLFNNKPDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQ---YGEDNV---KVYRssftpmytALTGHR 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 504387862 385 TNGFVKMMFDPQTGKILGCCIIAATASDMIAELALAMDAGLTLFDIANSISPHPT 439
Cdd:PRK06116 387 QPCLMKLVVVGKEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPT 441
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
2-448 |
1.33e-66 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 219.62 E-value: 1.33e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 2 NYDLIIIGAGPAG-YVAAEYAGKHKLKTLVVE-KEYFGGVCLNVGCIPTKTLLkrakivdylrHAQDYGISingqvalnW 79
Cdd:PRK07251 3 TYDLIVIGFGKAGkTLAAKLASAGKKVALVEEsKAMYGGTCINIGCIPTKTLL----------VAAEKNLS--------F 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 80 NQLLEQKGKVVSKLVGGVKAIIASAKAETVMGEAKVLDPNTVEVAG----KTYTTKSIVVATGSRPRYLTLPGFAEARQn 155
Cdd:PRK07251 65 EQVMATKNTVTSRLRGKNYAMLAGSGVDLYDAEAHFVSNKVIEVQAgdekIELTAETIVINTGAVSNVLPIPGLADSKH- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 156 gfVIDSTQALSLEGVPRKLVVVGGGVIGIEFAFLYASLGSEVTILQGVDRILEIFDTEVSDLVAKLLQTKNVKIITNAQV 235
Cdd:PRK07251 144 --VYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYMEEDGITFLLNAHT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 236 TRANN--NEVFYSQNGQEGSVvgDRILVSIGRIPNTE--CLDGLNLQRDERNRIVLNQDLQTSIPNIYIVGDANAQLMLA 311
Cdd:PRK07251 222 TEVKNdgDQVLVVTEDETYRF--DALLYATGRKPNTEplGLENTDIELTERGAIKVDDYCQTSVPGVFAVGDVNGGPQFT 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 312 HFAYQQGRYAVNHILNKKQVKPAQKLTCPSCIYTNPEVASVGYTEMELKKQGIPYVKTNLVLAHCGKAIADNETNGFVKM 391
Cdd:PRK07251 300 YISLDDFRIVFGYLTGDGSYTLEDRGNVPTTMFITPPLSQVGLTEKEAKEAGLPYAVKELLVAAMPRAHVNNDLRGAFKV 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 504387862 392 MFDPQTGKILGCCIIAATASDMIAELALAMDAGLTLFDIANSISPHPTINEMIADVC 448
Cdd:PRK07251 380 VVNTETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAENLNDLF 436
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
3-451 |
4.03e-62 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 213.24 E-value: 4.03e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 3 YDLIIIGAGPAGYVAAEYAGKHKLKTLVV--EKEYFGGVCLNVGCIPTKTLL---KRAKIVDYLRHAQDYGISIN----- 72
Cdd:PTZ00153 117 YDVGIIGCGVGGHAAAINAMERGLKVIIFtgDDDSIGGTCVNVGCIPSKALLyatGKYRELKNLAKLYTYGIYTNafkng 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 73 ------------GQVALNWNQLLEQKGKVVSKLVGGVKAIIASAKAE------TVMGE-AKVLDPNTV--EVAGKTYTTK 131
Cdd:PTZ00153 197 kndpvernqlvaDTVQIDITKLKEYTQSVIDKLRGGIENGLKSKKFCknsehvQVIYErGHIVDKNTIksEKSGKEFKVK 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 132 SIVVATGSRPrylTLPGFAEARQNGfVIDSTQALSLEGVPRKLVVVGGGVIGIEFAFLYASLGSEVTILQGVDRILEIFD 211
Cdd:PTZ00153 277 NIIIATGSTP---NIPDNIEVDQKS-VFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSPQLLPLLD 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 212 TEVSDLVAKL-LQTKNVKIITNAQVT--RANNNE----VFYSQ------------NGQEGSVVGDRILVSIGRIPNTE-- 270
Cdd:PTZ00153 353 ADVAKYFERVfLKSKPVRVHLNTLIEyvRAGKGNqpviIGHSErqtgesdgpkknMNDIKETYVDSCLVATGRKPNTNnl 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 271 CLDGLNLQRDeRNRIVLNQDLQTS------IPNIYIVGDANAQLMLAHFAYQQGRYAVNHILNKKQV-----------KP 333
Cdd:PTZ00153 433 GLDKLKIQMK-RGFVSVDEHLRVLredqevYDNIFCIGDANGKQMLAHTASHQALKVVDWIEGKGKEnvninvenwasKP 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 334 AQKLTCPSCIYTNPEVASVGYTEMELKKQGIP--------YVKTNlvlahcGKAIADNE--------------------- 384
Cdd:PTZ00153 512 IIYKNIPSVCYTTPELAFIGLTEKEAKELYPPdnvgveisFYKAN------SKVLCENNisfpnnsknnsynkgkyntvd 585
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504387862 385 -TNGFVKMMFDPQTGKILGCCIIAATASDMIAELALAMDAGLTLFDIANSISPHPTINEMIADVCKKA 451
Cdd:PTZ00153 586 nTEGMVKIVYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDAAFKAI 653
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
3-444 |
9.41e-62 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 207.50 E-value: 9.41e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 3 YDLIIIGAGPAGYV-AAEYAGKhklKTLVVEKEYFGGVCLNVGCIPTKTLLKRAKIVDYLRHAQDYGI--SINGqvaLNW 79
Cdd:PRK07846 2 YDLIIIGTGSGNSIlDERFADK---RIAIVEKGTFGGTCLNVGCIPTKMFVYAADVARTIREAARLGVdaELDG---VRW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 80 nqlleqkGKVVSKLVGGVKAIIASAKAE--------TVM-GEAKVLDPNTVEVA-GKTYTTKSIVVATGSRPRYLTLPGF 149
Cdd:PRK07846 76 -------PDIVSRVFGRIDPIAAGGEEYrgrdtpniDVYrGHARFIGPKTLRTGdGEEITADQVVIAAGSRPVIPPVIAD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 150 AEARqngfVIDSTQALSLEGVPRKLVVVGGGVIGIEFAFLYASLGSEVTILQGVDRILEIFDTEVSDLVAKLLQTKnVKI 229
Cdd:PRK07846 149 SGVR----YHTSDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLDDDISERFTELASKR-WDV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 230 ITNAQVTRANNNEVFYSQNGQEGSVV-GDRILVSIGRIPNTECLD----GLNLQRDerNRIVLNQDLQTSIPNIYIVGDA 304
Cdd:PRK07846 224 RLGRNVVGVSQDGSGVTLRLDDGSTVeADVLLVATGRVPNGDLLDaaaaGVDVDED--GRVVVDEYQRTSAEGVFALGDV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 305 NAQLMLAHFAYQQGRyAVNH-ILNKKQVKPAQKLTCPSCIYTNPEVASVGYTEMELKKQGIPY---VKTNLVLAHcGKAI 380
Cdd:PRK07846 302 SSPYQLKHVANHEAR-VVQHnLLHPDDLIASDHRFVPAAVFTHPQIASVGLTENEARAAGLDItvkVQNYGDVAY-GWAM 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504387862 381 ADneTNGFVKMMFDPQTGKILGCCIIAATASDMIAELALAMDAGLTLFDIANS-ISPHPTINEMI 444
Cdd:PRK07846 380 ED--TTGFVKLIADRDTGRLLGAHIIGPQASTLIQPLIQAMSFGLDAREMARGqYWIHPALPEVV 442
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
5-449 |
2.13e-57 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 196.23 E-value: 2.13e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 5 LIIIGAGPAGYVAAEYAGKHKLKTLVVEKEYFGGVCLNVGCIPTKTLLKRAKIVDYLRHAQDYGISI--NGQVALNWNQL 82
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIERDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRFidDGEARVDLPAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 83 --------LEQKGKVVSKLVG-GVKAIIASAKAETVmgeakVLDPNTVEVAGKTYTTKSI-----VVATGSRPRylTLPG 148
Cdd:PRK07845 84 narvkalaAAQSADIRARLEReGVRVIAGRGRLIDP-----GLGPHRVKVTTADGGEETLdadvvLIATGASPR--ILPT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 149 faeARQNGFVI-DSTQALSLEGVPRKLVVVGGGVIGIEFAFLYASLGSEVTILQGVDRILEIFDTEVSDLVAKLLQTKNV 227
Cdd:PRK07845 157 ---AEPDGERIlTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPGEDADAAEVLEEVFARRGM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 228 KIITNAQ---VTRANNNEVFYSQNGQEgsVVGDRILVSIGRIPNTEcldGLNLQR-----DERNRIVLNQDLQTSIPNIY 299
Cdd:PRK07845 234 TVLKRSRaesVERTGDGVVVTLTDGRT--VEGSHALMAVGSVPNTA---GLGLEEagvelTPSGHITVDRVSRTSVPGIY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 300 IVGDANAQLMLAHFAYQQGRYAVNHILNKKqVKPAQKLTCPSCIYTNPEVASVGYTEMELKKQGIPYVKTNLVLAHCGKA 379
Cdd:PRK07845 309 AAGDCTGVLPLASVAAMQGRIAMYHALGEA-VSPLRLKTVASNVFTRPEIATVGVSQAAIDSGEVPARTVMLPLATNPRA 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 380 IADNETNGFVKMMFDPQTGKILGCCIIAATASDMIAELALAMDAGLTLFDIANSISPHPTINEMIADVCK 449
Cdd:PRK07845 388 KMSGLRDGFVKLFCRPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYPSLSGSITEAAR 457
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
7-442 |
2.05e-55 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 193.06 E-value: 2.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 7 IIGAGPAGYVAAEYAGKHKLKTLVVEKEYFGGVCLNVGCIPTKTLLKRAKIVDYLRHAQ-DYGISiNGQVALNWNQLLEQ 85
Cdd:PRK13748 103 VIGSGGAAMAAALKAVEQGARVTLIERGTIGGTCVNVGCVPSKIMIRAAHIAHLRRESPfDGGIA-ATVPTIDRSRLLAQ 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 86 KGKVVSKL-VGGVKAIIASAKAETVM-GEAKVLDPNTVEVAGKTYTTKSIV-----VATGSRPRYLTLPGFAEARqngfV 158
Cdd:PRK13748 182 QQARVDELrHAKYEGILDGNPAITVLhGEARFKDDQTLIVRLNDGGERVVAfdrclIATGASPAVPPIPGLKETP----Y 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 159 IDSTQALSLEGVPRKLVVVGGGVIGIEFAFLYASLGSEVTILQgvdRILEIF--DTEVSDLVAKLLQTKNVKIITNAQVT 236
Cdd:PRK13748 258 WTSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILA---RSTLFFreDPAIGEAVTAAFRAEGIEVLEHTQAS 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 237 R-ANNNEVFYSQNGQeGSVVGDRILVSIGRIPNTEcldGLNLQR-----DERNRIVLNQDLQTSIPNIYIVGDANAQLML 310
Cdd:PRK13748 335 QvAHVDGEFVLTTGH-GELRADKLLVATGRAPNTR---SLALDAagvtvNAQGAIVIDQGMRTSVPHIYAAGDCTDQPQF 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 311 AHFAYQQG-RYAVNHILNKKqvkpAQKLTC-PSCIYTNPEVASVGYTEMELKKQGIPYVKTNLVLAHCGKAIADNETNGF 388
Cdd:PRK13748 411 VYVAAAAGtRAAINMTGGDA----ALDLTAmPAVVFTDPQVATVGYSEAEAHHDGIETDSRTLTLDNVPRALANFDTRGF 486
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 504387862 389 VKMMFDPQTGKILGCCIIAATASDMIAELALAMDAGLTLFDIANSISPHPTINE 442
Cdd:PRK13748 487 IKLVIEEGSGRLIGVQAVAPEAGELIQTAALAIRNRMTVQELADQLFPYLTMVE 540
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
2-442 |
3.98e-55 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 191.18 E-value: 3.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 2 NYDLIIIGAGPAGYVAAEYAGKHKLKTLVVEKEY----------FGGVCLNVGCIPTKTLLKRAKIVDYLRHAQDYGISI 71
Cdd:PLN02507 25 DFDLFVIGAGSGGVRAARFSANFGAKVGICELPFhpissesiggVGGTCVIRGCVPKKILVYGATFGGEFEDAKNYGWEI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 72 NGQVALNWNQLLEQKGKVVSKLVGGVKAIIASAKAETVMGEAKVLDPNTVEV-----AGKTYTTKSIVVATGSRPRYLTL 146
Cdd:PLN02507 105 NEKVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVtqldgTKLRYTAKHILIATGSRAQRPNI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 147 PGFAEArqngfvIDSTQALSLEGVPRKLVVVGGGVIGIEFAFLYASLGSEVTILQGVDRILEIFDTEVSDLVAKLLQTKN 226
Cdd:PLN02507 185 PGKELA------ITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRAVVARNLEGRG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 227 VKI--ITN-AQVTRANNNEVFYSQNGQEgsVVGDRILVSIGRIPNTEcldGLNLQR-----DERNRIVLNQDLQTSIPNI 298
Cdd:PLN02507 259 INLhpRTNlTQLTKTEGGIKVITDHGEE--FVADVVLFATGRAPNTK---RLNLEAvgvelDKAGAVKVDEYSRTNIPSI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 299 YIVGDANAQLMLAHFAYQQGRYAVNHILNKKQVKPAQKlTCPSCIYTNPEVASVGYTEMELKKQGipyvkTNLVLAHCG- 377
Cdd:PLN02507 334 WAIGDVTNRINLTPVALMEGTCFAKTVFGGQPTKPDYE-NVACAVFCIPPLSVVGLSEEEAVEQA-----KGDILVFTSs 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 378 -----KAIADNETNGFVKMMFDPQTGKILGCCIIAATASDMIAELALAMDAGLTLFDIANSISPHPTINE 442
Cdd:PLN02507 408 fnpmkNTISGRQEKTVMKLIVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAE 477
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
2-442 |
1.37e-52 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 185.46 E-value: 1.37e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 2 NYDLIIIGAGPAGYVAAEYAGKHKLKTLVVEKEY----------FGGVCLNVGCIPTKTLLKRAKIVDYLRHAQDYGISI 71
Cdd:PLN02546 79 DFDLFTIGAGSGGVRASRFASNFGASAAVCELPFatissdtlggVGGTCVLRGCVPKKLLVYASKYSHEFEESRGFGWKY 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 72 NGQVALNWNQLLEQKGKVVSKLVGGVKAIIASAKAETVMGEAKVLDPNTVEVAGKTYTTKSIVVATGSRPRYLTLPGFAe 151
Cdd:PLN02546 159 ETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDVDGKLYTARNILIAVGGRPFIPDIPGIE- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 152 arqngFVIDSTQALSLEGVPRKLVVVGGGVIGIEFAFLYASLGSEVTILQGVDRILEIFDTEVSDLVAKLLQTKNVKIIT 231
Cdd:PLN02546 238 -----HAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKKVLRGFDEEVRDFVAEQMSLRGIEFHT 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 232 NAQ---VTRANNNEVFYSQNgqEGSVVG-DRILVSIGRIPNTE--CLDGLNLQRDERNRIVLNQDLQTSIPNIYIVGDAN 305
Cdd:PLN02546 313 EESpqaIIKSADGSLSLKTN--KGTVEGfSHVMFATGRKPNTKnlGLEEVGVKMDKNGAIEVDEYSRTSVPSIWAVGDVT 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 306 AQLMLAHFAYQQGRYAVNHILNKKQVKPAQKlTCPSCIYTNPEVASVGYTEMELKKQgipYVKTNLVLAH---CGKAIAD 382
Cdd:PLN02546 391 DRINLTPVALMEGGALAKTLFGNEPTKPDYR-AVPSAVFSQPPIGQVGLTEEQAIEE---YGDVDVFTANfrpLKATLSG 466
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 383 NETNGFVKMMFDPQTGKILGCCIIAATASDMIAELALAMDAGLTLFDIANSISPHPTINE 442
Cdd:PLN02546 467 LPDRVFMKLIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAE 526
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
3-447 |
2.57e-48 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 171.35 E-value: 2.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 3 YDLIIIGAGPAGYVAAEYAGKHKLKTLVVEKE--YFGGVCLNVGCIPTKTLLKRA-KIVDYLRHAQDYGISINGQVALNW 79
Cdd:PRK08010 4 YQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSnaMYGGTCINIGCIPTKTLVHDAqQHTDFVRAIQRKNEVVNFLRNKNF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 80 NQLLEQKgkvvsklvggvkaiiasaKAETVMGEAKVLDPNTVEV--AGKTYTTK--SIVVATGSRPRYLTLPGFAEARQn 155
Cdd:PRK08010 84 HNLADMP------------------NIDVIDGQAEFINNHSLRVhrPEGNLEIHgeKIFINTGAQTVVPPIPGITTTPG- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 156 gfVIDSTQALSLEGVPRKLVVVGGGVIGIEFAFLYASLGSEVTILQGVDRILEIFDTEVSDLVAKLLQTKNVKIITNAQV 235
Cdd:PRK08010 145 --VYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 236 TRANNNEVFYSQNGQEGSVVGDRILVSIGRIPNTECLDGLN--LQRDERNRIVLNQDLQTSIPNIYIVGDANAQLMLAHF 313
Cdd:PRK08010 223 ERISHHENQVQVHSEHAQLAVDALLIASGRQPATASLHPENagIAVNERGAIVVDKYLHTTADNIWAMGDVTGGLQFTYI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 314 AYQQGRYAVNHILNKKQVKPAQKLTCPSCIYTNPEVASVGYTEMELKKQGIPYVKTNLVLAHCGKAIADNETNGFVKMMF 393
Cdd:PRK08010 303 SLDDYRIVRDELLGEGKRSTDDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDTRGVLKAIV 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 504387862 394 DPQTGKILGCCIIAATASDMIAELALAMDAGLTLFDIANSISPHPTINEMIADV 447
Cdd:PRK08010 383 DNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLNDL 436
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
2-442 |
5.40e-47 |
|
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: 168.88 E-value: 5.40e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 2 NYDLIIIGAGPAGYVAAEYAGKHKLKTLVVE---------KEYFGGVCLNVGCIPTKTLLKRAKIVDYLRHAQDYGISIN 72
Cdd:TIGR01438 2 DYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDfvtptplgtRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 73 GQVALNWNQLLEQKGKVVSKLVGGVKAIIASAKAETVMGEAKVLDPNTVEVAGK-----TYTTKSIVVATGSRPRYLTLP 147
Cdd:TIGR01438 82 ETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKkgkekIYSAERFLIATGERPRYPGIP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 148 GFAEarqngFVIDSTQALSLEGVPRKLVVVGGGVIGIEFAFLYASLGSEVTILqgVDRI-LEIFDTEVSDLVAKLLQTKN 226
Cdd:TIGR01438 162 GAKE-----LCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVM--VRSIlLRGFDQDCANKVGEHMEEHG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 227 VKIITNAQVTRANNNE----VFYSQNGQEGSVVGDRILVSIGRIPNTEC--LDGLNLQRDERN-RIVLNQDLQTSIPNIY 299
Cdd:TIGR01438 235 VKFKRQFVPIKVEQIEakvlVEFTDSTNGIEEEYDTVLLAIGRDACTRKlnLENVGVKINKKTgKIPADEEEQTNVPYIY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 300 IVGD-ANAQLMLAHFAYQQGRYAVNHILNKKQVKpAQKLTCPSCIYTNPEVASVGYTEME-LKKQGipyvKTNLVLAHC- 376
Cdd:TIGR01438 315 AVGDiLEDKPELTPVAIQAGRLLAQRLFKGSTVI-CDYENVPTTVFTPLEYGACGLSEEKaVEKFG----EENVEVFHSy 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504387862 377 ----GKAIADNETNGF--VKMMFD-PQTGKILGCCIIAATASDMIAELALAMDAGLTLFDIANSISPHPTINE 442
Cdd:TIGR01438 390 fwplEWTIPSRDNHNKcyAKLVCNkKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAE 462
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
3-442 |
2.65e-43 |
|
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: 158.98 E-value: 2.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 3 YDLIIIGAGPAGYVAAEYAGK-HKLKTLVVEKEY---------FGGVCLNVGCIPTKTLLKRAKIVDYLRHAQDYGISIN 72
Cdd:TIGR01423 4 FDLVVIGAGSGGLEAGWNAATlYKKRVAVVDVQThhgppfyaaLGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGWEFD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 73 GQ-VALNWNQLLEQKGKVVSKLVGGVKAIIASAKA-ETVMGEAKVLDPNTVEV---------AGKTYTTKSIVVATGSRP 141
Cdd:TIGR01423 84 RSsVKANWKALIAAKNKAVLDINKSYEGMFADTEGlTFFLGWGALEDKNVVLVresadpksaVKERLQAEHILLATGSWP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 142 RYLTLPGFAEArqngfvIDSTQALSLEGVPRKLVVVGGGVIGIEFAFL---YASLGSEVTILQGVDRILEIFDTEVSDLV 218
Cdd:TIGR01423 164 QMLGIPGIEHC------ISSNEAFYLDEPPRRVLTVGGGFISVEFAGIfnaYKPRGGKVTLCYRNNMILRGFDSTLRKEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 219 AKLLQTKNVKIITN---AQVTR-ANNNEVFYSQNGQEGSVvgDRILVSIGRIPNTEC--LDGLNLQRDERNRIVLNQDLQ 292
Cdd:TIGR01423 238 TKQLRANGINIMTNenpAKVTLnADGSKHVTFESGKTLDV--DVVMMAIGRVPRTQTlqLDKVGVELTKKGAIQVDEFSR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 293 TSIPNIYIVGDANAQLMLAHFAYQQGRYAVNHIL-NKKQVKPAQKLTCpsCIYTNPEVASVGYTEMELKK---QGIPYVK 368
Cdd:TIGR01423 316 TNVPNIYAIGDVTDRVMLTPVAINEGAAFVDTVFgNKPRKTDHTRVAS--AVFSIPPIGTCGLVEEDAAKkfeKVAVYES 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504387862 369 TNLVLAHcgkAIADNETNGFV-KMMFDPQTGKILGCCIIAATASDMIAELALAMDAGLTLFDIANSISPHPTINE 442
Cdd:TIGR01423 394 SFTPLMH---NISGSKYKKFVaKIVTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAE 465
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
340-444 |
1.14e-40 |
|
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: 141.15 E-value: 1.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 340 PSCIYTNPEVASVGYTEMELKKQGIPYVKTNLVLAHCGKAIADNETNGFVKMMFDPQTGKILGCCIIAATASDMIAELAL 419
Cdd:pfam02852 2 PSVVFTDPEIASVGLTEEEAKEKGGEVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQEAAL 81
|
90 100
....*....|....*....|....*
gi 504387862 420 AMDAGLTLFDIANSISPHPTINEMI 444
Cdd:pfam02852 82 AIKMGATVEDLANTIHIHPTLSEAL 106
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
1-444 |
3.85e-40 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 151.31 E-value: 3.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 1 MNYDLIIIGAGPAGYVAAEYAGKHKLKTLVVEKEYFGGVCLNVGCIPTKTLLKRAKIVDYLRHAQDYGIsiNGQVALNWN 80
Cdd:PTZ00058 47 MVYDLIVIGGGSGGMAAARRAARNKAKVALVEKDYLGGTCVNVGCVPKKIMFNAASIHDILENSRHYGF--DTQFSFNLP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 81 QLLEQKGKVVSKLVGGVKAIIASAKAETVMGEAKVLDPNTVEVA-----------------------------GKTYTTK 131
Cdd:PTZ00058 125 LLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLIKkvsqvdgeadesdddevtivsagvsqlddGQVIEGK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 132 SIVVATGSRPRYLTLPGFAearqngFVIDSTQALSLEGvPRKLVVVGGGVIGIEFAFLYASLGSEVTILQGVDRILEIFD 211
Cdd:PTZ00058 205 NILIAVGNKPIFPDVKGKE------FTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLRKFD 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 212 TEVSDLVAKLLQTKNVKIITNAQVTRANNNE-----VFYSQNGQEGSVvgDRILVSIGRIPNTECLD--GLNLqRDERNR 284
Cdd:PTZ00058 278 ETIINELENDMKKNNINIITHANVEEIEKVKeknltIYLSDGRKYEHF--DYVIYCVGRSPNTEDLNlkALNI-KTPKGY 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 285 IVLNQDLQTSIPNIYIVGDA------------------NAQLMLAHFAYQQGRYAVNHILNKKQVKPAQKL--------- 337
Cdd:PTZ00058 355 IKVDDNQRTSVKHIYAVGDCcmvkknqeiedlnllklyNEEPYLKKKENTSGESYYNVQLTPVAINAGRLLadrlfgpfs 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 338 ------TCPSCIYTNPEVASVGYTEME-LKKQGIPYVK------TNLVLAHCGKAIADNETNgFVKMMFDPQTGKILGCC 404
Cdd:PTZ00058 435 rttnykLIPSVIFSHPPIGTIGLSEQEaIDIYGKENVKiyesrfTNLFFSVYDMDPAQKEKT-YLKLVCVGKEELIKGLH 513
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 504387862 405 IIAATASDMIAELALAMDAGLTLFDIANSISPHPTINEMI 444
Cdd:PTZ00058 514 IVGLNADEILQGFAVALKMNATKADFDETIPIHPTAAEEF 553
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
3-325 |
7.19e-33 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 126.39 E-value: 7.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 3 YDLIIIGAGPAGYVAAEYAGKHKLKTLVVEKEYFGGVCLNVGCI------PTKT----LLKRAKivdylRHAQDYGISIn 72
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQLATTKEIenypgfPEGIsgpeLAERLR-----EQAERFGAEI- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 73 gqvalnwnqLLEQkgkvvsklvggVKAIiasakaeTVMGEAKVLDPNTvevaGKTYTTKSIVVATGSRPRYLTLPGFAEA 152
Cdd:COG0492 75 ---------LLEE-----------VTSV-------DKDDGPFRVTTDD----GTEYEAKAVIIATGAGPRKLGLPGEEEF 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 153 RQNG-----------------FVI---DS--TQALSLegvprklvvvgggvigiefaflyASLGSEVTIlqgVDRILEIF 210
Cdd:COG0492 124 EGRGvsycatcdgfffrgkdvVVVgggDSalEEALYL-----------------------TKFASKVTL---IHRRDELR 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 211 DTEVsdLVAKLLQTKNVKIITNAQVTRANNNE------VFYSQNGQEGSVVGDRILVSIGRIPNTECLDGLNLQRDERNR 284
Cdd:COG0492 178 ASKI--LVERLRANPKIEVLWNTEVTEIEGDGrvegvtLKNVKTGEEKELEVDGVFVAIGLKPNTELLKGLGLELDEDGY 255
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 504387862 285 IVLNQDLQTSIPNIYIVGDANA-QLMLAHFAYQQGRYAVNHI 325
Cdd:COG0492 256 IVVDEDMETSVPGVFAAGDVRDyKYRQAATAAGEGAIAALSA 297
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
3-447 |
6.76e-32 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 127.25 E-value: 6.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 3 YDLIIIGAGPAGYVAAEYAGKHKLKTLVVE---------KEYFGGVCLNVGCIPTKTLLKRAKIVDYLRH-AQDYGISIN 72
Cdd:PTZ00052 6 YDLVVIGGGSGGMAAAKEAAAHGKKVALFDyvkpstqgtKWGLGGTCVNVGCVPKKLMHYAANIGSIFHHdSQMYGWKTS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 73 GqvALNWNQLLEQKGKVVSKLVGGVKAIIASAKAETVMGEAKVLDPNTVEVAG----KTYTTKSIVVATGSRPRYL-TLP 147
Cdd:PTZ00052 86 S--SFNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTVSYGDnsqeETITAKYILIATGGRPSIPeDVP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 148 GFAEarqngFVIDSTQALSLEGVPRKLVVVGGGVIGIEFAFLYASLGSEVTIlqGVDRI-LEIFDTEVSDLVAKLLQTKN 226
Cdd:PTZ00052 164 GAKE-----YSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTV--AVRSIpLRGFDRQCSEKVVEYMKEQG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 227 VKI---ITNAQVTRANNN-EVFYSQNGQEgsvVGDRILVSIGRIPNTECL--DGLNLQRDERNRIVLNQDLqTSIPNIYI 300
Cdd:PTZ00052 237 TLFlegVVPINIEKMDDKiKVLFSDGTTE---LFDTVLYATGRKPDIKGLnlNAIGVHVNKSNKIIAPNDC-TNIPNIFA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 301 VGD-ANAQLMLAHFAYQQGRyavnhILNKKQVKPAQKLT----CPSCIYTNPEVASVGYT-EMELKKQGIPYVK------ 368
Cdd:PTZ00052 313 VGDvVEGRPELTPVAIKAGI-----LLARRLFKQSNEFIdytfIPTTIFTPIEYGACGYSsEAAIAKYGEDDIEeylqef 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 369 TNLVLA--HCGKAIA--------DNETNGFVKMM-FDPQTGKILGCCIIAATASDMIAELALAMDAGLTLFDIANSISPH 437
Cdd:PTZ00052 388 NTLEIAavHREKHERarkdeydfDVSSNCLAKLVcVKSEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIH 467
|
490
....*....|
gi 504387862 438 PTINEMIADV 447
Cdd:PTZ00052 468 PTDAEVFMNL 477
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
108-353 |
6.21e-24 |
|
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: 101.81 E-value: 6.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 108 TVMGEAKV--LDP--NTVEVA-GKTYTTKSIVVATGSRPRYLTLPGFAEarQNGFVI------DSTQALSLEGVPRKLVV 176
Cdd:COG0446 52 DVRTGTEVtaIDPeaKTVTLRdGETLSYDKLVLATGARPRPPPIPGLDL--PGVFTLrtlddaDALREALKEFKGKRAVV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 177 VGGGVIGIEFAFLYASLGSEVTILQGVDRILEIFDTEVSDLVAKLLQTKNVKIITNAQVTR--ANNNEVFYSQNGQEgsV 254
Cdd:COG0446 130 IGGGPIGLELAEALRKRGLKVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAidGDDKVAVTLTDGEE--I 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 255 VGDRILVSIGRIPNTECLDGLNLQRDERNRIVLNQDLQTSIPNIYIVGDA----------NAQLMLAHFAYQQGRYAVNH 324
Cdd:COG0446 208 PADLVVVAPGVRPNTELAKDAGLALGERGWIKVDETLQTSDPDVYAAGDCaevphpvtgkTVYIPLASAANKQGRVAAEN 287
|
250 260
....*....|....*....|....*....
gi 504387862 325 ILNKKQVKPAQKlTCPSCIYTNpEVASVG 353
Cdd:COG0446 288 ILGGPAPFPGLG-TFISKVFDL-CIASTG 314
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
97-333 |
7.41e-22 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 96.74 E-value: 7.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 97 VKAIIASAKAETVMGEAKVLDP--NTVEVA-GKTYTTKSIVVATGSRPRYLTLPGFAEarqNGFVIDST-QALSLEgvpR 172
Cdd:COG1252 62 LRELLRRAGVRFIQGEVTGIDPeaRTVTLAdGRTLSYDYLVIATGSVTNFFGIPGLAE---HALPLKTLeDALALR---E 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 173 KLVVVGGGVIGI---------------EFAFLYASLGS-------------EVTILQGVDRILEIFDTEVSDLVAKLLQT 224
Cdd:COG1252 136 RLLAAFERAERRrlltivvvgggptgvELAGELAELLRkllrypgidpdkvRITLVEAGPRILPGLGEKLSEAAEKELEK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 225 KNVKIITNAQVTRANNNEVFYSqNGQEgsVVGDRILVSIGRIPNtECLDGLNLQRDERNRIVLNQDLQT-SIPNIYIVGD 303
Cdd:COG1252 216 RGVEVHTGTRVTEVDADGVTLE-DGEE--IPADTVIWAAGVKAP-PLLADLGLPTDRRGRVLVDPTLQVpGHPNVFAIGD 291
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 504387862 304 ANAQL--------MLAHFAYQQGRYAVNHI---LNKKQVKP 333
Cdd:COG1252 292 CAAVPdpdgkpvpKTAQAAVQQAKVLAKNIaalLRGKPLKP 332
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
4-303 |
5.86e-20 |
|
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a member of the pyridine nucleotide-disulphide oxidoreductases (pfam00070). [Energy metabolism, Electron transport]
Pssm-ID: 273540 [Multi-domain] Cd Length: 299 Bit Score: 89.99 E-value: 5.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 4 DLIIIGAGPAGYVAAEYAGKHKLKTLVVEKEYFGGvclnvgciptkTLLKRAKIVDYlrhaQDYGISING-QVALNW-NQ 81
Cdd:TIGR01292 1 DVIIIGAGPAGLTAAIYAARANLKPLLIEGMEPGG-----------QLTTTTEVENY----PGFPEGISGpELMEKMkEQ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 82 LLEQKGKVVSKlvgGVKAIIASAKAETVMGEakvldpntvevAGKTYTTKSIVVATGSRPRYLTLPGFAEARQNG----- 156
Cdd:TIGR01292 66 AVKFGAEIIYE---EVIKVDKSDRPFKVYTG-----------DGKEYTAKAVIIATGASARKLGIPGEDEFWGRGvsyca 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 157 ------------FVI-DSTQALslegvprklvvvgggvigiEFAFLYASLGSEVTILqgVDRilEIFDTEvSDLVAKLLQ 223
Cdd:TIGR01292 132 tcdgpffknkevAVVgGGDSAI-------------------EEALYLTRIAKKVTLV--HRR--DKFRAE-KILLDRLKK 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 224 TKNVKIITNAQV------TRANNNEVFYSQNGQEGSVVGDRILVSIGRIPNTECLDGLnLQRDERNRIVLNQDLQTSIPN 297
Cdd:TIGR01292 188 NPKIEFLWNSTVeeivgdNKVEGVKIKNTVTGEEEELEVDGVFIAIGHEPNTELLKGL-LELDENGYIVTDEGMRTSVPG 266
|
....*.
gi 504387862 298 IYIVGD 303
Cdd:TIGR01292 267 VFAAGD 272
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
192-426 |
3.56e-18 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 86.25 E-value: 3.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 192 SLGSEVTILQGVDRIL-EIFDTEVSDLVAKLLQTKNVKIITNAQVTRANNNEVFYSQNGQEGSVVGDRILVSIGRIPNTE 270
Cdd:PRK09564 170 HLGKNVRIIQLEDRILpDSFDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEGVVTDKGEYEADVVIVATGVKPNTE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 271 CLDGLNLQRDERNRIVLNQDLQTSIPNIYIVGDA----------NAQLMLAHFAYQQGRyAVNHILNKKQVKPAQKLTCP 340
Cdd:PRK09564 250 FLEDTGLKTLKNGAIIVDEYGETSIENIYAAGDCatiynivsnkNVYVPLATTANKLGR-MVGENLAGRHVSFKGTLGSA 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 341 SCIYTNPEVASVGYTEMELKKQGIPYvKTNLVLAHCGKAIADNETNGFVKMMFDPQTGKILGCCIIAAT-ASDMIAELAL 419
Cdd:PRK09564 329 CIKVLDLEAARTGLTEEEAKKLGIDY-KTVFIKDKNHTNYYPGQEDLYVKLIYEADTKVILGGQIIGKKgAVLRIDALAV 407
|
....*..
gi 504387862 420 AMDAGLT 426
Cdd:PRK09564 408 AIYAKLT 414
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
3-304 |
9.52e-16 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 79.43 E-value: 9.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 3 YDLIIIGAGPAGYVAAEYAGKHKLKTLVVeKEYFGGVCL------NVGCIPtKTllKRAKIVDYLR-HAQDYGISI-NGQ 74
Cdd:PRK15317 212 YDVLVVGGGPAGAAAAIYAARKGIRTGIV-AERFGGQVLdtmgieNFISVP-ET--EGPKLAAALEeHVKEYDVDImNLQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 75 VAlnwnqlleqkgkvvSKLVGGVKAIiasakaetvmgeakvldpnTVEVA-GKTYTTKSIVVATGSRPRYLTLPGFAEAR 153
Cdd:PRK15317 288 RA--------------SKLEPAAGLI-------------------EVELAnGAVLKAKTVILATGARWRNMNVPGEDEYR 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 154 QNG-----------F------VI---DStqalsleGVprklvvvgggvigiEFAFLYASLGSEVTILQgvdrileiFDTE 213
Cdd:PRK15317 335 NKGvaycphcdgplFkgkrvaVIgggNS-------GV--------------EAAIDLAGIVKHVTVLE--------FAPE 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 214 V-SD--LVAKLLQTKNVKIITNAQVTrannnEVfysqNGQEGSVVG----DR------------ILVSIGRIPNTECLDG 274
Cdd:PRK15317 386 LkADqvLQDKLRSLPNVTIITNAQTT-----EV----TGDGDKVTGltykDRttgeehhlelegVFVQIGLVPNTEWLKG 456
|
330 340 350
....*....|....*....|....*....|
gi 504387862 275 LnLQRDERNRIVLNQDLQTSIPNIYIVGDA 304
Cdd:PRK15317 457 T-VELNRRGEIIVDARGATSVPGVFAAGDC 485
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
134-326 |
5.55e-15 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 76.33 E-value: 5.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 134 VVATGSRPRYLTLPGfaEARQNGFV---IDSTQALslegvpRKLVVVGGG-------VIGIEFAFLYASLGSEVTILQGV 203
Cdd:COG1251 103 VLATGSRPRVPPIPG--ADLPGVFTlrtLDDADAL------RAALAPGKRvvvigggLIGLEAAAALRKRGLEVTVVERA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 204 DRILE-IFDTEVSDLVAKLLQTKNVKIITNAQVTRANNNEVFYS---QNGQEgsVVGDRILVSIGRIPNTECLDGLNLQR 279
Cdd:COG1251 175 PRLLPrQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGvrlADGEE--LPADLVVVAIGVRPNTELARAAGLAV 252
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504387862 280 DerNRIVLNQDLQTSIPNIYIVGD-ANA------QLMLAHF--AYQQGRYAVNHIL 326
Cdd:COG1251 253 D--RGIVVDDYLRTSDPDIYAAGDcAEHpgpvygRRVLELVapAYEQARVAAANLA 306
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
194-430 |
1.45e-13 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 72.12 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 194 GSEVTILQGVDRILEIFDTEVSDLVAKLLQTKNVKIITNAQVTRANNNEVFYSQNGQEGSvvgDRILVSIGRIPNTECLD 273
Cdd:PRK13512 171 GLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDAINGNEVTFKSGKVEHY---DMIIEGVGTHPNSKFIE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 274 GLNLQRDERNRIVLNQDLQTSIPNIYIVGDA----------NAQLMLAHFAYQQGRYAVNHILNKKQVKPAQKLTCPSCI 343
Cdd:PRK13512 248 SSNIKLDDKGFIPVNDKFETNVPNIYAIGDIitshyrhvdlPASVPLAWGAHRAASIVAEQIAGNDTIEFKGFLGNNIVK 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 344 YTNPEVASVGYTEMELKKQGIPYVKTNlVLAHCGkaIADNETNGFVKMMFDPQTGKILGCCIIAATASDM-IAELALAMD 422
Cdd:PRK13512 328 FFDYTFASVGVKPNELKQFDYKMVEVT-QGAHAN--YYPGNSPLHLRVYYDTSNRKILRAAAVGKEGADKrIDVLSMAMM 404
|
....*...
gi 504387862 423 AGLTLFDI 430
Cdd:PRK13512 405 NQLTVDEL 412
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
196-336 |
1.39e-08 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 56.70 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 196 EVTILQGVDRILEIFDTEVSDLVAKLLQTKNVKIITNAQVTRANNNEVFYsqngQEGSVVGDRILV---SIGRIPNTECL 272
Cdd:PTZ00318 212 KVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEVLDKEVVL----KDGEVIPTGLVVwstGVGPGPLTKQL 287
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 273 DglnLQRDERNRIVLNQDLQTS-IPNIYIVGD--ANAQLML---AHFAYQQGRYAVNHILNKKQVKPAQK 336
Cdd:PTZ00318 288 K---VDKTSRGRISVDDHLRVKpIPNVFALGDcaANEERPLptlAQVASQQGVYLAKEFNNELKGKPMSK 354
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
2-76 |
1.23e-07 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 53.89 E-value: 1.23e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504387862 2 NYDLIIIGAGPAGYVAAEYAGKHKLKTLVVEK-EYFGGVCLNVGC---IPTKTLLKRAKIVDYLRHAQDYGISINGQVA 76
Cdd:PRK07843 7 EYDVVVVGSGAAGMVAALTAAHRGLSTVVVEKaPHYGGSTARSGGgvwIPNNEVLKRAGVPDTPEAARTYLHSIVGDVV 85
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
181-243 |
2.34e-07 |
|
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: 47.97 E-value: 2.34e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504387862 181 VIGIEFAFLYASLGSEVTILQGVDRILEIFDTEVSDLVAKLLQTKNVKIITNAQVTRANNNEV 243
Cdd:pfam00070 9 YIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGD 71
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
3-63 |
8.51e-07 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 51.26 E-value: 8.51e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504387862 3 YDLIIIGAGPAGYVAAEYAGKHKLKTLVVEKE-YFGGVCLNVG---CIPTKTLLKRAKIVD-------YLRH 63
Cdd:PRK06134 13 CDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDpVFGGTTAWSGgwmWIPRNPLARRAGIVEdieqprtYLRH 84
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
3-39 |
1.28e-06 |
|
geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 273936 [Multi-domain] Cd Length: 295 Bit Score: 50.01 E-value: 1.28e-06
10 20 30
....*....|....*....|....*....|....*..
gi 504387862 3 YDLIIIGAGPAGYVAAEYAGKHKLKTLVVEKEYFGGV 39
Cdd:TIGR02032 1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPRY 37
|
|
| PRK12844 |
PRK12844 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
3-67 |
1.86e-06 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 183787 [Multi-domain] Cd Length: 557 Bit Score: 50.14 E-value: 1.86e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504387862 3 YDLIIIGAGPAGYVAAEYAGKHKLKTLVVEKE--YFGGVCLNVGC--IPTKTLLKRAKIVDYLRHAQDY 67
Cdd:PRK12844 7 YDVVVVGSGGGGMCAALAAADSGLEPLIVEKQdkVGGSTAMSGGVlwLPNNPLMKAAGVPDSHEDALAY 75
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
124-326 |
1.86e-05 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 47.13 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 124 AGKTYTTKSIVVATGSRPRYLTLPGFAEARQNGF-VIDSTQALsLEGVPR--KLVVVGGGVIGIEFAFLYASLGSEVTIL 200
Cdd:TIGR02374 91 AGRTLSYDKLILATGSYPFILPIPGADKKGVYVFrTIEDLDAI-MAMAQRfkKAAVIGGGLLGLEAAVGLQNLGMDVSVI 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 201 QGVDRIL-EIFDTEVSDLVAKLLQTKNVKIITNAQVTRANNNEVFYSQNGQEGSVV-GDRILVSIGRIPNTECL--DGLN 276
Cdd:TIGR02374 170 HHAPGLMaKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVGATKADRIRFKDGSSLeADLIVMAAGIRPNDELAvsAGIK 249
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504387862 277 LQRDernrIVLNQDLQTSIPNIYIVGDA----NAQLMLAHFAYQQGRYAVNHIL 326
Cdd:TIGR02374 250 VNRG----IIVNDSMQTSDPDIYAVGECaehnGRVYGLVAPLYEQAKVLADHIC 299
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
3-33 |
1.89e-05 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 46.81 E-value: 1.89e-05
10 20 30
....*....|....*....|....*....|.
gi 504387862 3 YDLIIIGAGPAGYVAAEYAGKHKLKTLVVEK 33
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEK 31
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
120-309 |
3.27e-05 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 46.06 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 120 TVEVAGKTYTTKSIVVATGSRP---------RYLTLPGFAEARQNGFVIDSTQALSLEGvprklvvvgGGVIGIEFAFLY 190
Cdd:PRK04965 90 VVKSQGNQWQYDKLVLATGASAfvppipgreLMLTLNSQQEYRAAETQLRDAQRVLVVG---------GGLIGTELAMDL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 191 ASLGSEVTILQGVDRIL-EIFDTEVSDLVAKLLQTKNVKIITNAQVTRANNNEVFYS---QNGQEGSVvgDRILVSIGRI 266
Cdd:PRK04965 161 CRAGKAVTLVDNAASLLaSLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRatlDSGRSIEV--DAVIAAAGLR 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504387862 267 PNTECLDGLNLQrdeRNR-IVLNQDLQTSIPNIYIVGDA---NAQLM 309
Cdd:PRK04965 239 PNTALARRAGLA---VNRgIVVDSYLQTSAPDIYALGDCaeiNGQVL 282
|
|
| COG2509 |
COG2509 |
FAD-dependent dehydrogenase [General function prediction only]; |
1-33 |
5.83e-05 |
|
FAD-dependent dehydrogenase [General function prediction only];
Pssm-ID: 441999 [Multi-domain] Cd Length: 466 Bit Score: 45.49 E-value: 5.83e-05
10 20 30
....*....|....*....|....*....|...
gi 504387862 1 MNYDLIIIGAGPAGYVAAEYAGKHKLKTLVVEK 33
Cdd:COG2509 29 LKYDVVIVGAGPAGLFAALELAEAGLKPLVLER 61
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
6-33 |
9.57e-05 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 44.66 E-value: 9.57e-05
10 20
....*....|....*....|....*...
gi 504387862 6 IIIGAGPAGYVAAEYAGKHKLKTLVVEK 33
Cdd:COG2081 1 IVIGAGAAGLMAAITAAERGARVLLLEK 28
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
1-38 |
1.08e-04 |
|
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: 44.44 E-value: 1.08e-04
10 20 30
....*....|....*....|....*....|....*...
gi 504387862 1 MNYDLIIIGAGPAGYVAAEYAGKHKLKTLVVEKEYFGG 38
Cdd:COG1053 2 HEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRG 39
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
1-38 |
1.13e-04 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 44.46 E-value: 1.13e-04
10 20 30
....*....|....*....|....*....|....*....
gi 504387862 1 MNYDLIIIGAGPAGYVAAEYAGKHKLKTLVVEK-EYFGG 38
Cdd:COG1233 2 MMYDVVVIGAGIGGLAAAALLARAGYRVTVLEKnDTPGG 40
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
4-38 |
1.53e-04 |
|
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: 43.82 E-value: 1.53e-04
10 20 30
....*....|....*....|....*....|....*.
gi 504387862 4 DLIIIGAGPAGYVAAEYAGKHKLKTLVVEKE-YFGG 38
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGqPFGG 36
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
1-63 |
2.01e-04 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 43.91 E-value: 2.01e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504387862 1 MNYDLIIIGAGPAGYVAAEYAGKHKLKTLVVEKE-YFGG---VCLNVGCIPTKTLLKRAKIVD-------YLRH 63
Cdd:PRK12842 8 LTCDVLVIGSGAGGLSAAITARKLGLDVVVLEKEpVFGGttaFSGGVLWIPGNPHAREAGVADsreaartYLKH 81
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
7-40 |
2.52e-04 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 39.05 E-value: 2.52e-04
10 20 30
....*....|....*....|....*....|....*
gi 504387862 7 IIGAGPAGYVAAEYAGKHKLKTLVVEK-EYFGGVC 40
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKrDRLGGNA 35
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
257-304 |
2.71e-04 |
|
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: 43.20 E-value: 2.71e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 504387862 257 DRILVSIGRIPNTECL-DGLNLQRDERNRIVLN-QDLQTSIPNIYIVGDA 304
Cdd:COG0493 361 DLVILAIGQTPDPSGLeEELGLELDKRGTIVVDeETYQTSLPGVFAGGDA 410
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
3-38 |
3.71e-04 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 42.80 E-value: 3.71e-04
10 20 30
....*....|....*....|....*....|....*..
gi 504387862 3 YDLIIIGAGPAGYVAAEYAGKHKLKTLVVEK-EYFGG 38
Cdd:PRK12843 17 FDVIVIGAGAAGMSAALFAAIAGLKVLLVERtEYVGG 53
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
120-302 |
4.78e-04 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 41.83 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 120 TVEVAGKTYTTKSIVVATG--SRPRYLTLPGFAE-----------ARQNGFVIdstqalsleGvprklvvvgGGVIGIEF 186
Cdd:pfam13738 109 VVTTSKGTYQARYVIIATGefDFPNKLGVPELPKhysyvkdfhpyAGQKVVVI---------G---------GYNSAVDA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 187 AFLYASLGSEVTIlqgVDR--ILEIFDTEVS--------DLVAKLLQTKNVKIITNAQVTRANNNEVFYSQNGQEGSVV- 255
Cdd:pfam13738 171 ALELVRKGARVTV---LYRgsEWEDRDSDPSyslspdtlNRLEELVKNGKIKAHFNAEVKEITEVDVSYKVHTEDGRKVt 247
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504387862 256 -GDRILVSIGRIPNTECLDGLNLQRDERNRIVLN-QDLQTSIPNIYIVG 302
Cdd:pfam13738 248 sNDDPILATGYHPDLSFLKKGLFELDEDGRPVLTeETESTNVPGLFLAG 296
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
4-139 |
1.13e-03 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 41.00 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 4 DLIIIGAGPAGYVAAEYAGKHKLKT-LVVEKeyfGGVCLNVGCIPT-----KTLLKRAkiVDYLrhaqdYGISING--QV 75
Cdd:pfam01134 1 DVIVIGGGHAGCEAALAAARMGAKVlLITHN---TDTIAELSCNPSiggiaKGHLVRE--IDAL-----GGLMGKAadKT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 76 ALNWNQLLEQKGKVVSKLVGGV---------KAIIASAKAETVM-GEAKVLDPNTVEVAG------KTYTTKSIVVATGS 139
Cdd:pfam01134 71 GIQFRMLNTSKGPAVRALRAQVdrdlyskemTETLENHPNLTLIqGEVTDLIPENGKVKGvvtedgEEYKAKAVVLATGT 150
|
|
| TIGR00275 |
TIGR00275 |
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ... |
6-33 |
2.31e-03 |
|
flavoprotein, HI0933 family; The model when searched with a partial length search brings in proteins with a dinucleotide-binding motif (Rossman fold) over the initial 40 residues of the model, including oxidoreductases and dehydrogenases. Partially characterized members include an FAD-binding protein from Bacillus cereus and flavoprotein HI0933 from Haemophilus influenzae. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 272992 [Multi-domain] Cd Length: 400 Bit Score: 40.27 E-value: 2.31e-03
10 20
....*....|....*....|....*...
gi 504387862 6 IIIGAGPAGYVAAEYAGKHKLKTLVVEK 33
Cdd:TIGR00275 1 IIIGGGAAGLMAAITAARAGLSVLLLEK 28
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
5-303 |
3.35e-03 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 39.27 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 5 LIIIGAGPAGYVAAEYAGKHKLKTLVVEKEYFGGvclnvgciptkTLLKRAKIVDYLRHAQDygisingqvaLNWNQLLE 84
Cdd:PRK10262 9 LLILGSGPAGYTAAVYAARANLQPVLITGMEKGG-----------QLTTTTEVENWPGDPND----------LTGPLLME 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 85 QKGKVVSKLvggvkaiiasaKAETVMGEAKVLD----PNTVEVAGKTYTTKSIVVATGSRPRYLTLPGFAEARQNGFvid 160
Cdd:PRK10262 68 RMHEHATKF-----------ETEIIFDHINKVDlqnrPFRLTGDSGEYTCDALIIATGASARYLGLPSEEAFKGRGV--- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 161 sTQALSLEGV---PRKLVVVGGGVIGIEFAFLYASLGSEVTILQGVD--RILEIFDTEVSDLVAK----LLQTKNVKIIT 231
Cdd:PRK10262 134 -SACATCDGFfyrNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDgfRAEKILIKRLMDKVENgniiLHTNRTLEEVT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504387862 232 NAQ--VTRANNNEVFYSQNGQEGSVVGdrILVSIGRIPNTECLDGlnlQRDERNRIVLNQD------LQTSIPNIYIVGD 303
Cdd:PRK10262 213 GDQmgVTGVRLRDTQNSDNIESLDVAG--LFVAIGHSPNTAIFEG---QLELENGYIKVQSgihgnaTQTSIPGVFAAGD 287
|
|
| PRK12834 |
PRK12834 |
putative FAD-binding dehydrogenase; Reviewed |
1-34 |
3.50e-03 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 183782 [Multi-domain] Cd Length: 549 Bit Score: 39.88 E-value: 3.50e-03
10 20 30
....*....|....*....|....*....|....
gi 504387862 1 MNYDLIIIGAGPAGYVAAEYAGKHKLKTLVVEKE 34
Cdd:PRK12834 3 MDADVIVVGAGLAGLVAAAELADAGKRVLLLDQE 36
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
1-31 |
5.23e-03 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 39.06 E-value: 5.23e-03
10 20 30
....*....|....*....|....*....|.
gi 504387862 1 MNYDLIIIGAGPAGYVAAEYAGKHKLKTLVV 31
Cdd:PRK05329 1 MKFDVLVIGGGLAGLTAALAAAEAGKRVALV 31
|
|
| |
