|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
24-498 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 568.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 24 NKSHDVVIIGGGPAGYVAAIKAAQLGFNTACVEK------RGKLGGTCLNVGCIPSKALLNNSHLYHQMHTEAQKRGIDV 97
Cdd:PRK06327 2 SKQFDVVVIGAGPGGYVAAIRAAQLGLKVACIEAwknpkgKPALGGTCLNVGCIPSKALLASSEEFENAGHHFADHGIHV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 98 nGDIKINVANFQKAKDDAVKQLTGGIELLFKKNKVTYYKGNGSF----EDETKIRVTpvdGLEGTVkedhiLDVKNIIVA 173
Cdd:PRK06327 82 -DGVKIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFvgktDAGYEIKVT---GEDETV-----ITAKHVIIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 174 TGSEVTPFPGIEIDEEKIVSSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQIGASMDGEVAKATQK 253
Cdd:PRK06327 153 TGSEPRHLPGVPFDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAAADEQVAKEAAK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 254 FLKKQGLDFKLSTKVISAKrnDDKNVVEIVVEDTKTNKQeNLEAEVLLVAVGRRPYIAGLGAEKIGLEVDKRGRLVIDDQ 333
Cdd:PRK06327 233 AFTKQGLDIHLGVKIGEIK--TGGKGVSVAYTDADGEAQ-TLEVDKLIVSIGRVPNTDGLGLEAVGLKLDERGFIPVDDH 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 334 FNSKFPHIKVVGDVTFGPMLAHKAEEEGIAAVEMLKTGHGHVNYNNIPSVMYSHPEVAWVGKTEEQLKEAGIDYKIGKFP 413
Cdd:PRK06327 310 CRTNVPNVYAIGDVVRGPMLAHKAEEEGVAVAERIAGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLKAEGVEYKAGKFP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 414 FAANSRAKTNQDTEGFVKILIDSKTERILGAHIIGPNAGEMIAEAGLALEYGASAEDVARVCHAHPTLSEAFKEANMAAY 493
Cdd:PRK06327 390 FMANGRALAMGEPDGFVKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEVWHEAALAVD 469
|
....*
gi 768798536 494 DKAIH 498
Cdd:PRK06327 470 KRPLH 474
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
24-495 |
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: 544.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 24 NKSHDVVIIGGGPAGYVAAIKAAQLGFNTACVEKrGKLGGTCLNVGCIPSKALLNNSHLYHQMHtEAQKRGIDVnGDIKI 103
Cdd:COG1249 1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEK-GRLGGTCLNVGCIPSKALLHAAEVAHEAR-HAAEFGISA-GAPSV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 104 NVANFQKAKDDAVKQLTGGIELLFKKNKVTYYKGNGSFEDETKIRVTpvdglegtvkEDHILDVKNIIVATGSEVTPFPG 183
Cdd:COG1249 78 DWAALMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVT----------GGETLTADHIVIATGSRPRVPPI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 184 IEIDEEKIVSSTGALSLKEIPKRLTiigggiigLEMGSVYSRLGSKVTVVEFQPQIGASMDGEVAKATQKFLKKQGLDFK 263
Cdd:COG1249 148 PGLDEVRVLTSDEALELEELPKSLVvigggyigLEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDIL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 264 LSTKVISAKRNDDKnvVEIVVEDTKTNKQEnlEAEVLLVAVGRRPYIAGLGAEKIGLEVDKRGRLVIDDQFNSKFPHIKV 343
Cdd:COG1249 228 TGAKVTSVEKTGDG--VTVTLEDGGGEEAV--EADKVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRTSVPGIYA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 344 VGDVTFGPMLAHKAEEEGIAAVEMLKTGHGH-VNYNNIPSVMYSHPEVAWVGKTEEQLKEAGIDYKIGKFPFAANSRAKT 422
Cdd:COG1249 304 IGDVTGGPQLAHVASAEGRVAAENILGKKPRpVDYRAIPSVVFTDPEIASVGLTEEEAREAGIDVKVGKFPFAANGRALA 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768798536 423 NQDTEGFVKILIDSKTERILGAHIIGPNAGEMIAEAGLALEYGASAEDVARVCHAHPTLSEAFKEANMAAYDK 495
Cdd:COG1249 384 LGETEGFVKLIADAETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAALALLGR 456
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
26-498 |
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: 535.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 26 SHDVVIIGGGPAGYVAAIKAAQLGFNTACVEKRgKLGGTCLNVGCIPSKALLNNSHLYHQMhTEAQKRGIDVNGdIKINV 105
Cdd:TIGR01350 1 AYDVIVIGGGPGGYVAAIRAAQLGLKVALVEKE-YLGGTCLNVGCIPTKALLHSAEVYDEI-KHAKDLGIEVEN-VSVDW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 106 ANFQKAKDDAVKQLTGGIELLFKKNKVTYYKGNGSFEDETKIRVTpvdglegTVKEDHILDVKNIIVATGSEVTPFPG-I 184
Cdd:TIGR01350 78 EKMQKRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVT-------GENGEETLEAKNIIIATGSRPRSLPGpF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 185 EIDEEKIVSSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQIGASMDGEVAKATQKFLKKQGLDFKL 264
Cdd:TIGR01350 151 DFDGKVVITSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 265 STKVISAKRNDDKNVVEIvvedtKTNKQENLEAEVLLVAVGRRPYIAGLGAEKIGLEVDKRGRLVIDDQFNSKFPHIKVV 344
Cdd:TIGR01350 231 NTKVTAVEKNDDQVTYEN-----KGGETETLTGEKVLVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRTNVPGIYAI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 345 GDVTFGPMLAHKAEEEGIAAVE-MLKTGHGHVNYNNIPSVMYSHPEVAWVGKTEEQLKEAGIDYKIGKFPFAANSRAKTN 423
Cdd:TIGR01350 306 GDVIGGPMLAHVASHEGIVAAEnIAGKEPAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGYDVKIGKFPFAANGKALAL 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768798536 424 QDTEGFVKILIDSKTERILGAHIIGPNAGEMIAEAGLALEYGASAEDVARVCHAHPTLSEAFKEANMAAYDKAIH 498
Cdd:TIGR01350 386 GETDGFVKIIADKKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEAIKEAALAALGKPIH 460
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
28-499 |
2.75e-176 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 503.17 E-value: 2.75e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 28 DVVIIGGGPAGYVAAIKAAQLGFNTACVEKrGKLGGTCLNVGCIPSKALLNNSHLYHQMHtEAQKRGIDVnGDIKINVAN 107
Cdd:PRK06292 5 DVIVIGAGPAGYVAARRAAKLGKKVALIEK-GPLGGTCLNVGCIPSKALIAAAEAFHEAK-HAEEFGIHA-DGPKIDFKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 108 FQKAKDDAVKQLTGGI-ELLFKKNKVTYYKGNGSFEDETKIRVtpvdglegtvkEDHILDVKNIIVATGSEVTPFPGIE- 185
Cdd:PRK06292 82 VMARVRRERDRFVGGVvEGLEKKPKIDKIKGTARFVDPNTVEV-----------NGERIEAKNIVIATGSRVPPIPGVWl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 186 IDEEKIVSSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQIGASMDGEVAKATQKFLKKQgLDFKLS 265
Cdd:PRK06292 151 ILGDRLLTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILSKE-FKIKLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 266 TKVISAKRNDDknvvEIVVEDTKTNKQENLEAEVLLVAVGRRPYIAGLGAEKIGLEVDKRGRLVIDDQFNSKFPHIKVVG 345
Cdd:PRK06292 230 AKVTSVEKSGD----EKVEELEKGGKTETIEADYVLVATGRRPNTDGLGLENTGIELDERGRPVVDEHTQTSVPGIYAAG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 346 DVTFGPMLAHKAEEEGIAAVEMLKTGH-GHVNYNNIPSVMYSHPEVAWVGKTEEQLKEAGIDYKIGKFPFAANSRAKTNQ 424
Cdd:PRK06292 306 DVNGKPPLLHEAADEGRIAAENAAGDVaGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEVPFEAQGRARVMG 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768798536 425 DTEGFVKILIDSKTERILGAHIIGPNAGEMIAEAGLALEYGASAEDVARVCHAHPTLSEAFKEANMAAYDKAIHC 499
Cdd:PRK06292 386 KNDGFVKVYADKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRTALRDLFSKLIHG 460
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
28-498 |
9.14e-175 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 499.29 E-value: 9.14e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 28 DVVIIGGGPAGYVAAIKAAQLGFNTACVEKrGKLGGTCLNVGCIPSKALLNNSHLYHQMHtEAQKRGIDVnGDIKINVAN 107
Cdd:PRK06416 6 DVIVIGAGPGGYVAAIRAAQLGLKVAIVEK-EKLGGTCLNRGCIPSKALLHAAERADEAR-HSEDFGIKA-ENVGIDFKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 108 FQKAKDDAVKQLTGGIELLFKKNKVTYYKGNGSFEDETKIRVTPVDGlegtvkeDHILDVKNIIVATGSEVTPFPGIEID 187
Cdd:PRK06416 83 VQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDG-------EQTYTAKNIILATGSRPRELPGIEID 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 188 EEKIVSSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQIGASMDGEVAKATQKFLKKQGLDFKLSTK 267
Cdd:PRK06416 156 GRVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPGEDKEISKLAERALKKRGIKIKTGAK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 268 VISAKRNDDKnvveIVVEDTKTNKQENLEAEVLLVAVGRRPYIAGLGAEKIGLEVDkRGRLVIDDQFNSKFPHIKVVGDV 347
Cdd:PRK06416 236 AKKVEQTDDG----VTVTLEDGGKEETLEADYVLVAVGRRPNTENLGLEELGVKTD-RGFIEVDEQLRTNVPNIYAIGDI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 348 TFGPMLAHKAEEEGIAAVEMLKtGHGH-VNYNNIPSVMYSHPEVAWVGKTEEQLKEAGIDYKIGKFPFAANSRAKTNQDT 426
Cdd:PRK06416 311 VGGPMLAHKASAEGIIAAEAIA-GNPHpIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFDVKVVKFPFAGNGKALALGET 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768798536 427 EGFVKILIDSKTERILGAHIIGPNAGEMIAEAGLALEYGASAEDVARVCHAHPTLSEAFKEANMAAYDKAIH 498
Cdd:PRK06416 390 DGFVKLIFDKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEALGEAALAAAGKPLH 461
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
25-491 |
3.01e-102 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 314.06 E-value: 3.01e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 25 KSHDVVIIGGGPAGYVAAIKAAQLGFNTACVEkRGKLGGTCLNVGCIPSKALLNNSHLYHQMHTeAQKRGIDVNGDIKIN 104
Cdd:PRK06370 4 QRYDAIVIGAGQAGPPLAARAAGLGMKVALIE-RGLLGGTCVNTGCVPTKTLIASARAAHLARR-AAEYGVSVGGPVSVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 105 VANFQKAKDDAVKQLTGGIELLFKK-NKVTYYKGNGSFEDETKIRVTpvdglegtvkeDHILDVKNIIVATGSE--VTPF 181
Cdd:PRK06370 82 FKAVMARKRRIRARSRHGSEQWLRGlEGVDVFRGHARFESPNTVRVG-----------GETLRAKRIFINTGARaaIPPI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 182 PGIeiDEEKIVSSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQIGASMDGEVAKATQKFLKKQGLD 261
Cdd:PRK06370 151 PGL--DEVGYLTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILEREGID 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 262 FKLSTKVISAKRNDDknvvEIVVEDTKTNKQENLEAEVLLVAVGRRPYIAGLGAEKIGLEVDKRGRLVIDDQFNSKFPHI 341
Cdd:PRK06370 229 VRLNAECIRVERDGD----GIAVGLDCNGGAPEITGSHILVAVGRVPNTDDLGLEAAGVETDARGYIKVDDQLRTTNPGI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 342 KVVGDVTFGPMLAHKAEEEG-IAAVEMLKTGHGHVNYNNIPSVMYSHPEVAWVGKTEEQLKEAGIDYKIGKFPFAANSRA 420
Cdd:PRK06370 305 YAAGDCNGRGAFTHTAYNDArIVAANLLDGGRRKVSDRIVPYATYTDPPLARVGMTEAEARKSGRRVLVGTRPMTRVGRA 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768798536 421 KTNQDTEGFVKILIDSKTERILGAHIIGPNAGEMIAEAGLALEYGASAEDVARVCHAHPTLSEAFKEANMA 491
Cdd:PRK06370 385 VEKGETQGFMKVVVDADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIPTLAQA 455
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
27-493 |
5.64e-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: 300.88 E-value: 5.64e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 27 HDVVIIGGGPAGYVAAIKAAQLGFNTACVEkRGKLGGTCLNVGCIPSKALLNNSHLYHqmHTEAQKRGIdVNGDIKINVA 106
Cdd:TIGR02053 1 YDLVIIGSGAAAFAAAIKAAELGASVAMVE-RGPLGGTCVNVGCVPSKMLLRAAEVAH--YARKPPFGG-LAATVAVDFG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 107 NFQKAKDDAVKQL-TGGIELLFKKNKVTYYKGNGSFEDETKIRVTPvdglegtvkEDHILDVKNIIVATGSE--VTPFPG 183
Cdd:TIGR02053 77 ELLEGKREVVEELrHEKYEDVLSSYGVDYLRGRARFKDPKTVKVDL---------GREVRGAKRFLIATGARpaIPPIPG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 184 IeiDEEKIVSSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQIGASMDGEVAKATQKFLKKQGLDFK 263
Cdd:TIGR02053 148 L--KEAGYLTSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSDRLLPREEPEISAAVEEALAEEGIEVV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 264 LSTKVISAKRNDDKnvveIVVEDTKTNKQENLEAEVLLVAVGRRPYIAGLGAEKIGLEVDKRGRLVIDDQFNSKFPHIKV 343
Cdd:TIGR02053 226 TSAQVKAVSVRGGG----KIITVEKPGGQGEVEADELLVATGRRPNTDGLGLEKAGVKLDERGGILVDETLRTSNPGIYA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 344 VGDVTFGPMLAHKAEEEG-IAAVEMLKTGHGHVNYNNIPSVMYSHPEVAWVGKTEEQLKEAGIDYKIGKFPFAANSRAKT 422
Cdd:TIGR02053 302 AGDVTGGLQLEYVAAKEGvVAAENALGGANAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNVPRARI 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768798536 423 NQDTEGFVKILIDSKTERILGAHIIGPNAGEMIAEAGLALEYGASAEDVARVCHAHPTLSEAFKEANMAAY 493
Cdd:TIGR02053 382 NRDTRGFIKLVAEPGTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGLKLAAQTFY 452
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
28-494 |
2.62e-89 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 280.89 E-value: 2.62e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 28 DVVIIGGGPAGYVAAIKAAQLGFNTACVEKRGKLGGTCLNVGCIPSKALLNN-SHLyhqmhTEAQKRGIDVNGDIKINV- 105
Cdd:PRK05249 7 DLVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGGGCTHTGTIPSKALREAvLRL-----IGFNQNPLYSSYRVKLRIt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 106 -ANFQKAKDDAVKQLTGGIELLFKKNKVTYYKGNGSFEDETKIRVTPVDGLEGTVKEDHIldvkniIVATGSEvtPF--P 182
Cdd:PRK05249 82 fADLLARADHVINKQVEVRRGQYERNRVDLIQGRARFVDPHTVEVECPDGEVETLTADKI------VIATGSR--PYrpP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 183 GIEIDEEKIVSSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQIGASMDGEVAKATQKFLKKQGLDF 262
Cdd:PRK05249 154 DVDFDHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSFLDDEISDALSYHLRDSGVTI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 263 KLSTKVISAKRNDDKnvVEIVVEDTKTnkqenLEAEVLLVAVGRRPYIAGLGAEKIGLEVDKRGRLVIDDQFNSKFPHIK 342
Cdd:PRK05249 234 RHNEEVEKVEGGDDG--VIVHLKSGKK-----IKADCLLYANGRTGNTDGLNLENAGLEADSRGQLKVNENYQTAVPHIY 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 343 VVGDVTFGPMLAHKAEEEG-IAAVEMLKTGHGHVnYNNIPSVMYSHPEVAWVGKTEEQLKEAGIDYKIGKFPFAANSRAK 421
Cdd:PRK05249 307 AVGDVIGFPSLASASMDQGrIAAQHAVGEATAHL-IEDIPTGIYTIPEISSVGKTEQELTAAKVPYEVGRARFKELARAQ 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768798536 422 TNQDTEGFVKILIDSKTERILGAHIIGPNAGEMIAEAGLALEYGASAEDVARVCHAHPTLSEAFKeanMAAYD 494
Cdd:PRK05249 386 IAGDNVGMLKILFHRETLEILGVHCFGERATEIIHIGQAIMEQKGTIEYFVNTTFNYPTMAEAYR---VAALD 455
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
25-488 |
1.97e-68 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 231.34 E-value: 1.97e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 25 KSHDVVIIGGGPAGYVAAIKAAQLGFNTACVE-KRGKLGGTCLNVGCIPSKALL----------NNSHLY-HQMHTEAQK 92
Cdd:PTZ00153 115 EEYDVGIIGCGVGGHAAAINAMERGLKVIIFTgDDDSIGGTCVNVGCIPSKALLyatgkyrelkNLAKLYtYGIYTNAFK 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 93 RGID--------VNGDIKINVANFQKAKDDAVKQLTGGIELLFKKNKVTYYKGNGSfedetkirvtpVDGLEGTVKEDHI 164
Cdd:PTZ00153 195 NGKNdpvernqlVADTVQIDITKLKEYTQSVIDKLRGGIENGLKSKKFCKNSEHVQ-----------VIYERGHIVDKNT 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 165 L---------DVKNIIVATGSevTPF--PGIEIDEEKIVSSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTVV 233
Cdd:PTZ00153 264 IkseksgkefKVKNIIIATGS--TPNipDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSF 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 234 EFQPQIGASMDGEVAKATQK-FLKKQGLDFKLSTKVISAKRNDDKNVVEIVVEDTKT----------NKQENLEAEVLLV 302
Cdd:PTZ00153 342 EYSPQLLPLLDADVAKYFERvFLKSKPVRVHLNTLIEYVRAGKGNQPVIIGHSERQTgesdgpkknmNDIKETYVDSCLV 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 303 AVGRRPYIAGLGAEKIGLEVdKRGRLVIDDQF------NSKFPHIKVVGDVTFGPMLAHKAEEEGIAAVEML--KTGHGH 374
Cdd:PTZ00153 422 ATGRKPNTNNLGLDKLKIQM-KRGFVSVDEHLrvlredQEVYDNIFCIGDANGKQMLAHTASHQALKVVDWIegKGKENV 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 375 -----------VNYNNIPSVMYSHPEVAWVGKTEEQLKEAGIDYKIGKFP--FAANSRA--------------------- 420
Cdd:PTZ00153 501 ninvenwaskpIIYKNIPSVCYTTPELAFIGLTEKEAKELYPPDNVGVEIsfYKANSKVlcennisfpnnsknnsynkgk 580
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768798536 421 -KTNQDTEGFVKILIDSKTERILGAHIIGPNAGEMIAEAGLALEYGASAEDVARVCHAHPTLSE----AFKEA 488
Cdd:PTZ00153 581 yNTVDNTEGMVKIVYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEvldaAFKAI 653
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
28-485 |
1.31e-66 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 221.18 E-value: 1.31e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 28 DVVIIGGGPAGYVAAIKAAQLGFNTACVEKRgKLGGTCLNVGCIPSKALLNNSHLYHQMHTEAQKRGIDVnGDIKINVAN 107
Cdd:PRK06116 6 DLIVIGGGSGGIASANRAAMYGAKVALIEAK-RLGGTCVNVGCVPKKLMWYGAQIAEAFHDYAPGYGFDV-TENKFDWAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 108 FQKAKDDAVKQLTGGIELLFKKNKVTYYKGNGSFEDETKIRVTpvdgleG-TVKEDHILdvkniiVATGSEVTP--FPGI 184
Cdd:PRK06116 84 LIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVN------GeRYTADHIL------IATGGRPSIpdIPGA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 185 E--IDeekivsSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQIGASMDGEVAKATQKFLKKQGLDF 262
Cdd:PRK06116 152 EygIT------SDGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 263 KLSTKVISAKRNDDkNVVEIVVEDTKTnkqenLEAEVLLVAVGRRPYIAGLGAEKIGLEVDKRGRLVIDDQFNSKFPHIK 342
Cdd:PRK06116 226 HTNAVPKAVEKNAD-GSLTLTLEDGET-----LTVDCLIWAIGREPNTDGLGLENAGVKLNEKGYIIVDEYQNTNVPGIY 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 343 VVGDVTFGPMLAHKAEEEGIAAVEMLKTG--HGHVNYNNIPSVMYSHPEVAWVGKTEEQLKEAGIDY--KIGKFPFAANS 418
Cdd:PRK06116 300 AVGDVTGRVELTPVAIAAGRRLSERLFNNkpDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDnvKVYRSSFTPMY 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768798536 419 RAKTNQDTEGFVKILIDSKTERILGAHIIGPNAGEMIAEAGLALEYGASAEDVARVCHAHPTLSEAF 485
Cdd:PRK06116 380 TALTGHRQPCLMKLVVVGKEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEF 446
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
25-485 |
2.18e-66 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 220.39 E-value: 2.18e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 25 KSHDVVIIGGGPAGYVAAIKAAQLGFNTACVEKRGKL-GGTCLNVGCIPSKALLnnshlyhqmhTEAQKRgidvngdiki 103
Cdd:PRK07251 2 LTYDLIVIGFGKAGKTLAAKLASAGKKVALVEESKAMyGGTCINIGCIPTKTLL----------VAAEKN---------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 104 nvANFQKA---KDDAVKQLTGGIELLFKKNKVTYYKGNGSFEDETKIRVTPVDglegtvkEDHILDVKNIIVATG--SEV 178
Cdd:PRK07251 62 --LSFEQVmatKNTVTSRLRGKNYAMLAGSGVDLYDAEAHFVSNKVIEVQAGD-------EKIELTAETIVINTGavSNV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 179 TPFPGIEiDEEKIVSSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQIGASMDGEVAKATQKFLKKQ 258
Cdd:PRK07251 133 LPIPGLA-DSKHVYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYMEED 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 259 GLDFKLSTKVISAKrNDDKNVVeIVVEDtktnkqENLEAEVLLVAVGRRPYIAGLGAEKIGLEVDKRGRLVIDDQFNSKF 338
Cdd:PRK07251 212 GITFLLNAHTTEVK-NDGDQVL-VVTED------ETYRFDALLYATGRKPNTEPLGLENTDIELTERGAIKVDDYCQTSV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 339 PHIKVVGDVTFGPMLAHKAEEEGIAAVEMLkTGHG---HVNYNNIPSVMYSHPEVAWVGKTEEQLKEAGIDYKIGKFPFA 415
Cdd:PRK07251 284 PGVFAVGDVNGGPQFTYISLDDFRIVFGYL-TGDGsytLEDRGNVPTTMFITPPLSQVGLTEKEAKEAGLPYAVKELLVA 362
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 416 ANSRAKTNQDTEGFVKILIDSKTERILGAHIIGPNAGEMIAEAGLALEYGASAEDVARVCHAHPTLSEAF 485
Cdd:PRK07251 363 AMPRAHVNNDLRGAFKVVVNTETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAENL 432
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
30-487 |
9.91e-65 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 216.18 E-value: 9.91e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 30 VIIGGGPAGYVAAIKAAQLGFNTACVEKRGKL-GGTCLNVGCIPSKALLNNSHLYHQMHTEAQKrgidvngdiKINVANF 108
Cdd:NF040477 7 IIIGFGKAGKTLAATLAKAGWRVAIIEQSAQMyGGTCINIGCIPTKTLVHDAEQHQDFSTAMQR---------KSSVVGF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 109 QKAKDdavkqltggIELLFKKNKVTYYKGNGSFEDETKIRVTPVDGlegtvkeDHILDVKNIIVATGSEVT--PFPGIEI 186
Cdd:NF040477 78 LRDKN---------YHNLADLDNVDVINGRAEFIDNHTLRVFQADG-------EQELRGEKIFINTGAQSVlpPIPGLTT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 187 dEEKIVSSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQIGASMDGEVAKATQKFLKKQGLDFKLST 266
Cdd:NF040477 142 -TPGVYDSTGLLNLTQLPARLGILGGGYIGVEFASMFARFGSKVTIFEAAELFLPREDRDIAQAIATILQDQGVELILNA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 267 KVISAKRNDDKnvVEIVVEDTKtnkqenLEAEVLLVAVGRRPYIAGLGAEKIGLEVDKRGRLVIDDQFNSKFPHIKVVGD 346
Cdd:NF040477 221 QVQRVSSHEGE--VQLETAEGV------LTVDALLVASGRKPATAGLQLQNAGVAVNERGAIVVDKYLRTTADNIWAMGD 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 347 VTFGPMLAHKA-EEEGIAAVEMLKTGHGHV-NYNNIPSVMYSHPEVAWVGKTEEQLKEAGIDYKIGKFPFAANSRAKTNQ 424
Cdd:NF040477 293 VTGGLQFTYISlDDFRIVRDSLLGEGKRSTdDRQNVPYSVFMTPPLSRIGMTEEQARASGADIQVVTLPVAAIPRARVMN 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768798536 425 DTEGFVKILIDSKTERILGAHIIGPNAGEMIAEAGLALEYGASAEDVARVCHAHPTLSEAFKE 487
Cdd:NF040477 373 DTRGVLKAVVDNKTQRILGVSLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSESLND 435
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
27-361 |
1.05e-61 |
|
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: 203.70 E-value: 1.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 27 HDVVIIGGGPAGYVAAIKAAQLGFNTACVEkrgkLGGTCLNVGCIPSKALLNNSHLYHQMHTEAQkrgidvngdikinva 106
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIE----DEGTCPYGGCVLSKALLGAAEAPEIASLWAD--------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 107 nFQKAKDDAVKQLTGGIELLFKKNKVTYYKGNGSFEDEtkirvtpvdglEGTVKEDHILDVKNIIVATGSE--VTPFPGI 184
Cdd:pfam07992 62 -LYKRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLE-----------ELVDGDGETITYDRLVIATGARprLPPIPGV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 185 E---IDEEKIVSSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQIGASMDGEVAKATQKFLKKQGLD 261
Cdd:pfam07992 130 ElnvGFLVRTLDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 262 FKLSTKVISAKRNDDknVVEIVVEDTKTnkqenLEAEVLLVAVGRRPYIAGLgaEKIGLEVDKRGRLVIDDQFNSKFPHI 341
Cdd:pfam07992 210 VRLGTSVKEIIGDGD--GVEVILKDGTE-----IDADLVVVAIGRRPNTELL--EAAGLELDERGGIVVDEYLRTSVPGI 280
|
330 340
....*....|....*....|.
gi 768798536 342 KVVGDVT-FGPMLAHKAEEEG 361
Cdd:pfam07992 281 YAAGDCRvGGPELAQNAVAQG 301
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
23-488 |
3.27e-61 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 210.01 E-value: 3.27e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 23 INKSHDVVIIGGGPAGYVAAIKAAQLGFNTACVEkRGKLGGTCLNVGCIPSKALLNNSHLYHQmhteaqKRGIDVNGDIK 102
Cdd:PRK13748 95 NERPLHVAVIGSGGAAMAAALKAVEQGARVTLIE-RGTIGGTCVNVGCVPSKIMIRAAHIAHL------RRESPFDGGIA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 103 INVANFQKAKddAVKQLTGGIE---------LLFKKNKVTYYKGNGSFEDETKIRVTPVDGLEGTVKEDHILdvkniiVA 173
Cdd:PRK13748 168 ATVPTIDRSR--LLAQQQARVDelrhakyegILDGNPAITVLHGEARFKDDQTLIVRLNDGGERVVAFDRCL------IA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 174 TGSE--VTPFPGIEidEEKIVSSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTVVE-----FQ--PQIGASMd 244
Cdd:PRK13748 240 TGASpaVPPIPGLK--ETPYWTSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILArstlfFRedPAIGEAV- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 245 gevakaTQKFlKKQGLDFKLSTKViSAKRNDDKnvveivvEDTKTNKQENLEAEVLLVAVGRRPYIAGLGAEKIGLEVDK 324
Cdd:PRK13748 317 ------TAAF-RAEGIEVLEHTQA-SQVAHVDG-------EFVLTTGHGELRADKLLVATGRAPNTRSLALDAAGVTVNA 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 325 RGRLVIDDQFNSKFPHIKVVGDVTFGPMLAHKAEEEGI-AAVEMLKtGHGHVNYNNIPSVMYSHPEVAWVGKTEEQLKEA 403
Cdd:PRK13748 382 QGAIVIDQGMRTSVPHIYAAGDCTDQPQFVYVAAAAGTrAAINMTG-GDAALDLTAMPAVVFTDPQVATVGYSEAEAHHD 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 404 GIDYKIGKFPFAANSRAKTNQDTEGFVKILIDSKTERILGAHIIGPNAGEMIAEAGLALEYGASAEDVARVCHAHPTLSE 483
Cdd:PRK13748 461 GIETDSRTLTLDNVPRALANFDTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAALAIRNRMTVQELADQLFPYLTMVE 540
|
....*
gi 768798536 484 AFKEA 488
Cdd:PRK13748 541 GLKLA 545
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
27-483 |
1.18e-59 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 202.88 E-value: 1.18e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 27 HDVVIIGGGPAGYVAAIKAAQLgfNTACVEKrGKLGGTCLNVGCIPSKALLNNSHLYHQMhTEAQKRGID--VNG----D 100
Cdd:PRK07846 2 YDLIIIGTGSGNSILDERFADK--RIAIVEK-GTFGGTCLNVGCIPTKMFVYAADVARTI-REAARLGVDaeLDGvrwpD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 101 IKINVanFQKAKDDAvkqlTGGIELLFKKN-KVTYYKGNGSFEDETKIRVTpvdglegtvkEDHILDVKNIIVATGSEVT 179
Cdd:PRK07846 78 IVSRV--FGRIDPIA----AGGEEYRGRDTpNIDVYRGHARFIGPKTLRTG----------DGEEITADQVVIAAGSRPV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 180 PFPGIEIDEEKIVSSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQIGASMDGEVAKA-TQkfLKKQ 258
Cdd:PRK07846 142 IPPVIADSGVRYHTSDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLDDDISERfTE--LASK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 259 GLDFKLSTKVISAKRNDDKnvVEIVVEDTKTnkqenLEAEVLLVAVGRRPYIAGLGAEKIGLEVDKRGRLVIDDQFNSKF 338
Cdd:PRK07846 220 RWDVRLGRNVVGVSQDGSG--VTLRLDDGST-----VEADVLLVATGRVPNGDLLDAAAAGVDVDEDGRVVVDEYQRTSA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 339 PHIKVVGDVTFGPMLAHKAEEEgiAAV---------EMLKTGHGHVnynniPSVMYSHPEVAWVGKTEEQLKEAGIDYKI 409
Cdd:PRK07846 293 EGVFALGDVSSPYQLKHVANHE--ARVvqhnllhpdDLIASDHRFV-----PAAVFTHPQIASVGLTENEARAAGLDITV 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768798536 410 GKFPFAANSRAKTNQDTEGFVKILIDSKTERILGAHIIGPNAGEMIAEAGLALEYGASAEDVARVCH-AHPTLSE 483
Cdd:PRK07846 366 KVQNYGDVAYGWAMEDTTGFVKLIADRDTGRLLGAHIIGPQASTLIQPLIQAMSFGLDAREMARGQYwIHPALPE 440
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
25-485 |
1.49e-59 |
|
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: 202.76 E-value: 1.49e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 25 KSHDVVIIGGGPAGYVAAIKAAQLGFNTACVEKRgKLGGTCLNVGCIPSKALLNNSHLYHQMHtEAQKRGIDVNGDIKIN 104
Cdd:TIGR01421 1 KHYDYLVIGGGSGGIASARRAAEHGAKALLVEAK-KLGGTCVNVGCVPKKVMWYASDLAERMH-DAADYGFYQNDENTFN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 105 VANFQKAKDDAVKQLTGGIELLFKKNKVTYYKGNGSFEDETKIRVTpvdglegtvKEDHilDVKNIIVATGSEVTPFPGI 184
Cdd:TIGR01421 79 WPELKEKRDAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVN---------GRDY--TAPHILIATGGKPSFPENI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 185 EiDEEKIVSSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQIGASMDGEVAKATQKFLKKQGLDFKL 264
Cdd:TIGR01421 148 P-GAELGTDSDGFFALEELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRHERVLRSFDSMISETITEEYEKEGINVHK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 265 STKVISAKRNDDKNVVeIVVEDTKTnkqeNLEAEVLLVAVGRRPYIAGLGAEKIGLEVDKRGRLVIDDQFNSKFPHIKVV 344
Cdd:TIGR01421 227 LSKPVKVEKTVEGKLV-IHFEDGKS----IDDVDELIWAIGRKPNTKGLGLENVGIKLNEKGQIIVDEYQNTNVPGIYAL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 345 GDVTFGPMLAHKAEEEGIAAVEMLKTGH--GHVNYNNIPSVMYSHPEVAWVGKTEEQ-LKEAGID-YKIGKFPFAANSRA 420
Cdd:TIGR01421 302 GDVVGKVELTPVAIAAGRKLSERLFNGKtdDKLDYNNVPTVVFSHPPIGTIGLTEKEaIEKYGKEnIKVYNSSFTPMYYA 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768798536 421 KTNQDTEGFVKILIDSKTERILGAHIIGPNAGEMIAEAGLALEYGASAEDVARVCHAHPTLSEAF 485
Cdd:TIGR01421 382 MTSEKQKCRMKLVCAGKEEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEEL 446
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
27-487 |
4.23e-57 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 196.00 E-value: 4.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 27 HDVVIIGGGPAGYVAAIKAAQLGFNTACVEKRGKL-GGTCLNVGCIPSKALLNNSHLYHQMHTEAQKrgidvngdiKINV 105
Cdd:PRK08010 4 YQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNAMyGGTCINIGCIPTKTLVHDAQQHTDFVRAIQR---------KNEV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 106 ANFQKAKDdavkqltggIELLFKKNKVTYYKGNGSFEDETKIRVTPVDGlegtvkeDHILDVKNIIVATGSE--VTPFPG 183
Cdd:PRK08010 75 VNFLRNKN---------FHNLADMPNIDVIDGQAEFINNHSLRVHRPEG-------NLEIHGEKIFINTGAQtvVPPIPG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 184 IEIdEEKIVSSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQIGASMDGEVAKATQKFLKKQGLDFK 263
Cdd:PRK08010 139 ITT-TPGVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDII 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 264 LSTKV--ISAKrnddKNVVEIVVEDTKtnkqenLEAEVLLVAVGRRPYIAGLGAEKIGLEVDKRGRLVIDDQFNSKFPHI 341
Cdd:PRK08010 218 LNAHVerISHH----ENQVQVHSEHAQ------LAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKYLHTTADNI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 342 KVVGDVTFGPMLAHKA-EEEGIAAVEMLKTGHGHV-NYNNIPSVMYSHPEVAWVGKTEEQLKEAGIDYKIGKFPFAANSR 419
Cdd:PRK08010 288 WAMGDVTGGLQFTYISlDDYRIVRDELLGEGKRSTdDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPR 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768798536 420 AKTNQDTEGFVKILIDSKTERILGAHIIGPNAGEMIAEAGLALEYGASAEDVARVCHAHPTLSEAFKE 487
Cdd:PRK08010 368 ARVMNDTRGVLKAIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLND 435
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
380-488 |
1.74e-56 |
|
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: 183.52 E-value: 1.74e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 380 IPSVMYSHPEVAWVGKTEEQLKEAGIDYKIGKFPFAANSRAKTNQDTEGFVKILIDSKTERILGAHIIGPNAGEMIAEAG 459
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGEVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQEAA 80
|
90 100
....*....|....*....|....*....
gi 768798536 460 LALEYGASAEDVARVCHAHPTLSEAFKEA 488
Cdd:pfam02852 81 LAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
28-485 |
1.25e-50 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 180.01 E-value: 1.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 28 DVVIIGGGPAGYVAAIKAAQLG---------FNTACVEKRGKLGGTCLNVGCIPSKALLNNSHLYHQMHtEAQKRGIDVN 98
Cdd:PLN02507 27 DLFVIGAGSGGVRAARFSANFGakvgicelpFHPISSESIGGVGGTCVIRGCVPKKILVYGATFGGEFE-DAKNYGWEIN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 99 GDIKINVANFQKAKDDAVKQLTGGIELLFKKNKVTYYKGNGSFEDETKIRVTPVDGLEGTVKEDHILdvkniiVATGSEV 178
Cdd:PLN02507 106 EKVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRYTAKHIL------IATGSRA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 179 TP--FPGIEIDeekiVSSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQIGASMDGEVAKATQKFLK 256
Cdd:PLN02507 180 QRpnIPGKELA----ITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRAVVARNLE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 257 KQGLDFKLSTKVISAKRNDDknvvEIVVedtKTNKQENLEAEVLLVAVGRRPYIAGLGAEKIGLEVDKRGRLVIDDQFNS 336
Cdd:PLN02507 256 GRGINLHPRTNLTQLTKTEG----GIKV---ITDHGEEFVADVVLFATGRAPNTKRLNLEAVGVELDKAGAVKVDEYSRT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 337 KFPHIKVVGDVTFGPMLAHKAEEEGIAaveMLKTGHG----HVNYNNIPSVMYSHPEVAWVGKTEEQ-LKEAGIDYKIGK 411
Cdd:PLN02507 329 NIPSIWAIGDVTNRINLTPVALMEGTC---FAKTVFGgqptKPDYENVACAVFCIPPLSVVGLSEEEaVEQAKGDILVFT 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768798536 412 FPFAANSRAKTNQDTEGFVKILIDSKTERILGAHIIGPNAGEMIAEAGLALEYGASAEDVARVCHAHPTLSEAF 485
Cdd:PLN02507 406 SSFNPMKNTISGRQEKTVMKLIVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEF 479
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
27-485 |
1.27e-49 |
|
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: 176.97 E-value: 1.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 27 HDVVIIGGGPAGYVAAIKAAQLGFNTACVE--------KRGKLGGTCLNVGCIPSKaLLNNSHLYHQMHTEAQKRGIDVN 98
Cdd:TIGR01438 3 YDLIVIGGGSGGLAAAKEAAAYGAKVMLLDfvtptplgTRWGIGGTCVNVGCIPKK-LMHQAALLGQALKDSRNYGWKVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 99 GDIKINVANFQKAKDDAVKQLTGGIELLFKKNKVTYYKGNGSFEDETKIRVTPVDGLEgtvkedHILDVKNIIVATGsEV 178
Cdd:TIGR01438 82 ETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKE------KIYSAERFLIATG-ER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 179 TPFPGIEIDEEKIVSSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTV-VEFQPQIGasMDGEVAKATQKFLKK 257
Cdd:TIGR01438 155 PRYPGIPGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVmVRSILLRG--FDQDCANKVGEHMEE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 258 QGLDFKLSTKVISAKRNDDKNVVEIvvedtkTNKQENLEAE--VLLVAVGRRPYIAGLGAEKIGLEVDKR-GRLVIDDQF 334
Cdd:TIGR01438 233 HGVKFKRQFVPIKVEQIEAKVLVEF------TDSTNGIEEEydTVLLAIGRDACTRKLNLENVGVKINKKtGKIPADEEE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 335 NSKFPHIKVVGDVTFG-PMLAHKAEEEG-IAAVEMLKTGHGHVNYNNIPSVMYSHPEVAWVGKTEEQLKEagidyKIGK- 411
Cdd:TIGR01438 307 QTNVPYIYAVGDILEDkPELTPVAIQAGrLLAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAVE-----KFGEe 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 412 -----------FPFAANSRAKTNQdteGFVKILIDSK-TERILGAHIIGPNAGEMIAEAGLALEYGASAEDVARVCHAHP 479
Cdd:TIGR01438 382 nvevfhsyfwpLEWTIPSRDNHNK---CYAKLVCNKKeNERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHP 458
|
....*.
gi 768798536 480 TLSEAF 485
Cdd:TIGR01438 459 VCAEVF 464
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
29-488 |
2.92e-49 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 175.43 E-value: 2.92e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 29 VVIIGGGPAGYVAAIKAAQLGFNTACVEKRGkLGGTCLNVGCIPSKALLNNSHLYHQMHtEAQKRGIDVNGDIKINV--- 105
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIERDG-LGGAAVLTDCVPSKTLIATAEVRTELR-RAAELGIRFIDDGEARVdlp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 106 ANFQKAKDDAVKQlTGGIELLFKKNKVTYYKGNGSFEDET----KIRVTPVDGLEGTVKEDHILdvkniiVATGSevTP- 180
Cdd:PRK07845 82 AVNARVKALAAAQ-SADIRARLEREGVRVIAGRGRLIDPGlgphRVKVTTADGGEETLDADVVL------IATGA--SPr 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 181 -FPGIEIDEEKIVSSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQIGASMDGEVAKATQKFLKKQG 259
Cdd:PRK07845 153 iLPTAEPDGERILTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPGEDADAAEVLEEVFARRG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 260 LDFKLSTKVISAKRNDDKnvVEIVVEDTKTnkqenLEAEVLLVAVGRRPYIAGLGAEKIGLEVDKRGRLVIDDQFNSKFP 339
Cdd:PRK07845 233 MTVLKRSRAESVERTGDG--VVVTLTDGRT-----VEGSHALMAVGSVPNTAGLGLEEAGVELTPSGHITVDRVSRTSVP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 340 HIKVVGDVTFGPMLAHKAEEEG-IA-------AVEMLKTGhghvnynNIPSVMYSHPEVAWVGKTEEQLKEAGIDYKIGK 411
Cdd:PRK07845 306 GIYAAGDCTGVLPLASVAAMQGrIAmyhalgeAVSPLRLK-------TVASNVFTRPEIATVGVSQAAIDSGEVPARTVM 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768798536 412 FPFAANSRAKTNQDTEGFVKILIDSKTERILGAHIIGPNAGEMIAEAGLALEYGASAEDVARVCHAHPTLSEAFKEA 488
Cdd:PRK07845 379 LPLATNPRAKMSGLRDGFVKLFCRPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYPSLSGSITEA 455
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
25-488 |
5.82e-48 |
|
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and related species, can form a disulfide-linked dimer called mycothione. This enzyme can reduce mycothione to regenerate two mycothiol molecules. The enzyme shows some sequence similarity to glutathione-disulfide reductase, trypanothione-disulfide reductase, and dihydrolipoamide dehydrogenase. The characterized protein from M. tuberculosis, a homodimer, has FAD as a cofactor, one per monomer, and uses NADPH as a substrate.
Pssm-ID: 132493 [Multi-domain] Cd Length: 452 Bit Score: 171.86 E-value: 5.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 25 KSHDVVIIGGGPAGYVAAIKAAqlGFNTACVEKrGKLGGTCLNVGCIPSKALLNNSHLYHQMhTEAQKRGIDvngdikin 104
Cdd:TIGR03452 1 RHYDLIIIGTGSGNSIPDPRFA--DKRIAIVEK-GTFGGTCLNVGCIPTKMFVYAAEVAQSI-GESARLGID-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 105 vANFQKAK-DDAVKQLTGG-IELLF----------KKNKVTYYKGNGSFEDETKIRVTPVDGLEGTvkedhildvkNIIV 172
Cdd:TIGR03452 69 -AEIDSVRwPDIVSRVFGDrIDPIAaggedyrrgdETPNIDVYDGHARFVGPRTLRTGDGEEITGD----------QIVI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 173 ATGSEVTPFPGIEIDEEKIVSSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQIGASMDGEVAKATQ 252
Cdd:TIGR03452 138 AAGSRPYIPPAIADSGVRYHTNEDIMRLPELPESLVIVGGGYIAAEFAHVFSALGTRVTIVNRSTKLLRHLDEDISDRFT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 253 KFLKKQgLDFKLSTKVISAKRNDDKNVVEIvvEDTKTnkqenLEAEVLLVAVGRRPYIAGLGAEKIGLEVDKRGRLVIDD 332
Cdd:TIGR03452 218 EIAKKK-WDIRLGRNVTAVEQDGDGVTLTL--DDGST-----VTADVLLVATGRVPNGDLLDAEAAGVEVDEDGRIKVDE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 333 QFNSKFPHIKVVGDVTFGPMLAHKAEEEGIAAVE-------MLKTGHGHVnynniPSVMYSHPEVAWVGKTEEQLKEAG- 404
Cdd:TIGR03452 290 YGRTSARGVWALGDVSSPYQLKHVANAEARVVKHnllhpndLRKMPHDFV-----PSAVFTHPQIATVGLTEQEAREAGh 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 405 -IDYKIGKFPFAANSRAKtnQDTEGFVKILIDSKTERILGAHIIGPNAGEMIAEAGLALEYGASAEDVARVCH-AHPTLS 482
Cdd:TIGR03452 365 dITVKIQNYGDVAYGWAM--EDTTGFCKLIADRDTGKLLGAHIIGPQASSLIQPLITAMAFGLDAREMARKQYwIHPALP 442
|
....*.
gi 768798536 483 EAFKEA 488
Cdd:TIGR03452 443 EVVENA 448
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
24-493 |
5.29e-41 |
|
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: 153.59 E-value: 5.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 24 NKSHDVVIIGGGPAGYVAAIKAAQL-GFNTACVEKR--------GKLGGTCLNVGCIPSKALLNNSHLYHQMHtEAQKRG 94
Cdd:TIGR01423 1 SKAFDLVVIGAGSGGLEAGWNAATLyKKRVAVVDVQthhgppfyAALGGTCVNVGCVPKKLMVTGAQYMDTLR-ESAGFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 95 IDVNGD-IKINVANFQKAKDDAVKQLTGGIELLFKKNK-VTYYKGNGSFEDETKIRVTPVDGLEGTVKEDhiLDVKNIIV 172
Cdd:TIGR01423 80 WEFDRSsVKANWKALIAAKNKAVLDINKSYEGMFADTEgLTFFLGWGALEDKNVVLVRESADPKSAVKER--LQAEHILL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 173 ATGS--EVTPFPGIEIdeekIVSSTGALSLKEIPKRLTIIGGGIIGLEMGSV---YSRLGSKVTVVEFQPQIGASMDGEV 247
Cdd:TIGR01423 158 ATGSwpQMLGIPGIEH----CISSNEAFYLDEPPRRVLTVGGGFISVEFAGIfnaYKPRGGKVTLCYRNNMILRGFDSTL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 248 AKATQKFLKKQGLDFKLSTKVISAKRNDDKNVvEIVVEDTKTnkqenLEAEVLLVAVGRRPYIAGLGAEKIGLEVDKRGR 327
Cdd:TIGR01423 234 RKELTKQLRANGINIMTNENPAKVTLNADGSK-HVTFESGKT-----LDVDVVMMAIGRVPRTQTLQLDKVGVELTKKGA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 328 LVIDDQFNSKFPHIKVVGDVTFGPMLAHKAEEEGIAAVEML------KTGHGHVnynniPSVMYSHPEVAWVGKTEEqlk 401
Cdd:TIGR01423 308 IQVDEFSRTNVPNIYAIGDVTDRVMLTPVAINEGAAFVDTVfgnkprKTDHTRV-----ASAVFSIPPIGTCGLVEE--- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 402 EAGIDY-KIGKF-----PFAANSRAKTNQdtEGFVKILIDSKTERILGAHIIGPNAGEMIAEAGLALEYGASAEDVARVC 475
Cdd:TIGR01423 380 DAAKKFeKVAVYessftPLMHNISGSKYK--KFVAKIVTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTI 457
|
490
....*....|....*...
gi 768798536 476 HAHPTLSEAFKEANMAAY 493
Cdd:TIGR01423 458 GVHPTSAEELCSMRTPSY 475
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
28-485 |
9.90e-39 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 148.49 E-value: 9.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 28 DVVIIGGGPAG---------YVAAIKAAQLGFNTACVEKRGKLGGTCLNVGCIPSKALL---NNSHLYHQMHTEAQKRGI 95
Cdd:PLN02546 81 DLFTIGAGSGGvrasrfasnFGASAAVCELPFATISSDTLGGVGGTCVLRGCVPKKLLVyasKYSHEFEESRGFGWKYET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 96 DVNGDIKINVANfqkaKDDAVKQLTGGIELLFKKNKVTYYKGNGSFEDETKIrvtPVDGlegtvkedHILDVKNIIVATG 175
Cdd:PLN02546 161 EPKHDWNTLIAN----KNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTV---DVDG--------KLYTARNILIAVG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 176 SEvtPF----PGIEideeKIVSSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQIGASMDGEVAKAT 251
Cdd:PLN02546 226 GR--PFipdiPGIE----HAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKKVLRGFDEEVRDFV 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 252 QKFLKKQGLDFKLSTKVISAKRNDDKNVveivveDTKTNKQENLEAEVLLVAVGRRPYIAGLGAEKIGLEVDKRGRLVID 331
Cdd:PLN02546 300 AEQMSLRGIEFHTEESPQAIIKSADGSL------SLKTNKGTVEGFSHVMFATGRKPNTKNLGLEEVGVKMDKNGAIEVD 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 332 DQFNSKFPHIKVVGDVTFGPMLAHKAEEEGIAaveMLKTGHGH----VNYNNIPSVMYSHPEVAWVGKTEEQLKEAGIDY 407
Cdd:PLN02546 374 EYSRTSVPSIWAVGDVTDRINLTPVALMEGGA---LAKTLFGNeptkPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYGDV 450
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768798536 408 KIGKFPFAANSRAKTNQDTEGFVKILIDSKTERILGAHIIGPNAGEMIAEAGLALEYGASAEDVARVCHAHPTLSEAF 485
Cdd:PLN02546 451 DVFTANFRPLKATLSGLPDRVFMKLIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEEF 528
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
24-485 |
2.27e-37 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 144.76 E-value: 2.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 24 NKSHDVVIIGGGPAGYVAAIKAAQLGFNTACVEkRGKLGGTCLNVGCIPSKALLNNSHLyHQMHTEAQKRGIDVngDIKI 103
Cdd:PTZ00058 46 RMVYDLIVIGGGSGGMAAARRAARNKAKVALVE-KDYLGGTCVNVGCVPKKIMFNAASI-HDILENSRHYGFDT--QFSF 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 104 NVANFQKAKDDAVKQLTGGIELLFKKNKVTYYKGNGSFEDETKIRVTPVDGLEGTVKE------------------DHIL 165
Cdd:PTZ00058 122 NLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLIKKVSQVDGEADEsdddevtivsagvsqlddGQVI 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 166 DVKNIIVATGSEvTPFPGIEiDEEKIVSSTGALSLKEiPKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQIGASMDG 245
Cdd:PTZ00058 202 EGKNILIAVGNK-PIFPDVK-GKEFTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLRKFDE 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 246 EVAKATQKFLKKQGLDFKLSTKVISAKRNDDKNVVEIVVEDTKtnkqeNLEAEVLLVAVGRRPYIAGLGAEKIGLEVDKr 325
Cdd:PTZ00058 279 TIINELENDMKKNNINIITHANVEEIEKVKEKNLTIYLSDGRK-----YEHFDYVIYCVGRSPNTEDLNLKALNIKTPK- 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 326 GRLVIDDQFNSKFPHIKVVGD------------------VTFGPMLAHKAEEEG------------IAAVEMLK-----T 370
Cdd:PTZ00058 353 GYIKVDDNQRTSVKHIYAVGDccmvkknqeiedlnllklYNEEPYLKKKENTSGesyynvqltpvaINAGRLLAdrlfgP 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 371 GHGHVNYNNIPSVMYSHPEVAWVGKTEEQLKEagidyKIGKFPFAANSRAKTN-----------QDTEGFVKILIDSKTE 439
Cdd:PTZ00058 433 FSRTTNYKLIPSVIFSHPPIGTIGLSEQEAID-----IYGKENVKIYESRFTNlffsvydmdpaQKEKTYLKLVCVGKEE 507
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 768798536 440 RILGAHIIGPNAGEMIAEAGLALEYGASAEDVARVCHAHPTLSEAF 485
Cdd:PTZ00058 508 LIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIHPTAAEEF 553
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
27-485 |
4.82e-36 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 139.96 E-value: 4.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 27 HDVVIIGGGPAGYVAAIKAAQLGFNTACVE---------KRGkLGGTCLNVGCIPSKALLNNSHLYHQMHTEAQKRGIDV 97
Cdd:PTZ00052 6 YDLVVIGGGSGGMAAAKEAAAHGKKVALFDyvkpstqgtKWG-LGGTCVNVGCVPKKLMHYAANIGSIFHHDSQMYGWKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 98 NGdiKINVANFQKAKDDAVKQLTGGIELLFKKNKVTYYKGNGSFEDETKIrvtpvdgLEGTVKEDHILDVKNIIVATGSE 177
Cdd:PTZ00052 85 SS--SFNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTV-------SYGDNSQEETITAKYILIATGGR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 178 VTPFPGIEIDEEKIVSSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTV-VEFQPQIGasMDGEVAKATQKFLK 256
Cdd:PTZ00052 156 PSIPEDVPGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVaVRSIPLRG--FDRQCSEKVVEYMK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 257 KQGLDFKLSTKVISAKRNDDKnvVEIVVEDTKTNkqenlEAEVLLVAVGRRPYIAGLGAEKIGLEVDKRGRLVIDDQFNS 336
Cdd:PTZ00052 234 EQGTLFLEGVVPINIEKMDDK--IKVLFSDGTTE-----LFDTVLYATGRKPDIKGLNLNAIGVHVNKSNKIIAPNDCTN 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 337 kFPHIKVVGDVTFG-PMLAHKAEEEG-IAAVEMLKTGHGHVNYNNIPSVMYSHPEVAWVGKTEEQLKEAGIDYKIGKFPF 414
Cdd:PTZ00052 307 -IPNIFAVGDVVEGrPELTPVAIKAGiLLARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 415 AANS------------RAKTNQ-DTE----GFVK-ILIDSKTERILGAHIIGPNAGEMIAEAGLALEYGASAEDVARVCH 476
Cdd:PTZ00052 386 EFNTleiaavhrekheRARKDEyDFDvssnCLAKlVCVKSEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIG 465
|
....*....
gi 768798536 477 AHPTLSEAF 485
Cdd:PTZ00052 466 IHPTDAEVF 474
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
171-366 |
1.18e-15 |
|
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: 77.93 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 171 IVATGSE--VTPFPGIeiDEEKIVSSTGALSLKEIPKRLTIIGGGI--------IGLEMGSVYSRLGSKVTVVEFQPQIG 240
Cdd:COG0446 83 VLATGARprPPPIPGL--DLPGVFTLRTLDDADALREALKEFKGKRavvigggpIGLELAEALRKRGLKVTLVERAPRLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 241 ASMDGEVAKATQKFLKKQGLDFKLSTKVISAkrnDDKNVVEIVVEDTKTnkqenLEAEVLLVAVGRRPYIAgLgAEKIGL 320
Cdd:COG0446 161 GVLDPEMAALLEEELREHGVELRLGETVVAI---DGDDKVAVTLTDGEE-----IPADLVVVAPGVRPNTE-L-AKDAGL 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 768798536 321 EVDKRGRLVIDDQFNSKFPHIKVVGDV----------TFGPMLAHKAEEEGIAAVE 366
Cdd:COG0446 231 ALGERGWIKVDETLQTSDPDVYAAGDCaevphpvtgkTVYIPLASAANKQGRVAAE 286
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
27-348 |
1.74e-14 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 74.00 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 27 HDVVIIGGGPAGYVAAIKAAQLGFNTACVEkRGKLGGTCLNVGCI------PSK----ALLNNshlyhqMHTEAQKRGID 96
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIE-GGEPGGQLATTKEIenypgfPEGisgpELAER------LREQAERFGAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 97 VngdikinvanfqkaKDDAVKQLTggiellfkknkvtyykgngsFEDETKiRVTPVDGLEgtvkedhiLDVKNIIVATGS 176
Cdd:COG0492 74 I--------------LLEEVTSVD--------------------KDDGPF-RVTTDDGTE--------YEAKAVIIATGA 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 177 EVT--PFPGIEIDEEKIVSSTGALSLKEIP-KRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQIGASmdgevaKATQK 253
Cdd:COG0492 111 GPRklGLPGEEEFEGRGVSYCATCDGFFFRgKDVVVVGGGDSALEEALYLTKFASKVTLIHRRDELRAS------KILVE 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 254 FLKK-QGLDFKLSTKVISAKrnDDKNVVEIVVEDTKTNKQENLEAEVLLVAVGRRPyIAGLgAEKIGLEVDKRGRLVIDD 332
Cdd:COG0492 185 RLRAnPKIEVLWNTEVTEIE--GDGRVEGVTLKNVKTGEEKELEVDGVFVAIGLKP-NTEL-LKGLGLELDEDGYIVVDE 260
|
330
....*....|....*.
gi 768798536 333 QFNSKFPHIKVVGDVT 348
Cdd:COG0492 261 DMETSVPGVFAAGDVR 276
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
215-282 |
6.84e-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: 63.76 E-value: 6.84e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768798536 215 IGLEMGSVYSRLGSKVTVVEFQPQIGASMDGEVAKATQKFLKKQGLDFKLSTKVISAKRNDDKNVVEI 282
Cdd:pfam00070 10 IGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVL 77
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
229-369 |
8.37e-11 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 63.61 E-value: 8.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 229 KVTVVEFQPQIGASMDGEVAKATQKFLKKQGLDFKLSTKVISAKRNddknvvEIVVEDTKTnkqenLEAEVLLVAVGRRP 308
Cdd:COG1252 187 RITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDAD------GVTLEDGEE-----IPADTVIWAAGVKA 255
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 309 yiAGLGAEkIGLEVDKRGRLVIDDQFNSK-FPHIKVVGDV--------TFGPMLAHKAEEEGIAAVEMLK 369
Cdd:COG1252 256 --PPLLAD-LGLPTDRRGRVLVDPTLQVPgHPNVFAIGDCaavpdpdgKPVPKTAQAAVQQAKVLAKNIA 322
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
145-450 |
1.49e-09 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 60.05 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 145 TKIRVTPVDGLEGTVKEDHIL--DVKN-----IIVATG--SEVTPFPGIEIDE-EKIVSSTGALSLKEI-----PKRLTI 209
Cdd:PRK09564 75 TEHEVVKVDAKNKTITVKNLKtgSIFNdtydkLMIATGarPIIPPIKNINLENvYTLKSMEDGLALKELlkdeeIKNIVI 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 210 IGGGIIGLEMGSVYSRLGSKVTVVEFQPQI-GASMDGEVAKATQKFLKKQGLDFKLSTKVISAkrnDDKNVVEIVVedtk 288
Cdd:PRK09564 155 IGAGFIGLEAVEAAKHLGKNVRIIQLEDRIlPDSFDKEITDVMEEELRENGVELHLNEFVKSL---IGEDKVEGVV---- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 289 TNKQEnLEAEVLLVAVGRRPYIAGLgaEKIGLEVDKRGRLVIDDQFNSKFPHIKVVGD-------VTFGPM---LAHKAE 358
Cdd:PRK09564 228 TDKGE-YEADVVIVATGVKPNTEFL--EDTGLKTLKNGAIIVDEYGETSIENIYAAGDcatiyniVSNKNVyvpLATTAN 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 359 EEGIAAVEMLKTGH----GHVNYNNIPSVMYshpEVAWVGKTEEQLKEAGIDYKIgKFPFAANSRAKTNQDTEGFVKILI 434
Cdd:PRK09564 305 KLGRMVGENLAGRHvsfkGTLGSACIKVLDL---EAARTGLTEEEAKKLGIDYKT-VFIKDKNHTNYYPGQEDLYVKLIY 380
|
330
....*....|....*.
gi 768798536 435 DSKTERILGAHIIGPN 450
Cdd:PRK09564 381 EADTKVILGGQIIGKK 396
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
215-367 |
2.33e-09 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 59.38 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 215 IGLEMGSVYSRLGSKVTVVEFQPQIGAS-MDGEVAKATQKFLKKQGLDFKLSTKVISAKRNDdkNVVEIVVEDTKTnkqe 293
Cdd:COG1251 153 IGLEAAAALRKRGLEVTVVERAPRLLPRqLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDD--RVTGVRLADGEE---- 226
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768798536 294 nLEAEVLLVAVGRRPYIAgLgAEKIGLEVDkRGrLVIDDQFNSKFPHIKVVGDVT--FGPMLAHKAEEEGIAAVEM 367
Cdd:COG1251 227 -LPADLVVVAIGVRPNTE-L-ARAAGLAVD-RG-IVVDDYLRTSDPDIYAAGDCAehPGPVYGRRVLELVAPAYEQ 297
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
28-64 |
3.07e-09 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 58.77 E-value: 3.07e-09
10 20 30
....*....|....*....|....*....|....*..
gi 768798536 28 DVVIIGGGPAGYVAAIKAAQLGFNTACVEKRGKLGGT 64
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGM 37
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
28-365 |
5.04e-09 |
|
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: 57.64 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 28 DVVIIGGGPAGYVAAIKAAQLGFNTACVEKR---GKLGGTCLnVGCIPS-KALLNNSHLYHQMHTEAQKRGIDVngdIKI 103
Cdd:TIGR01292 1 DVIIIGAGPAGLTAAIYAARANLKPLLIEGMepgGQLTTTTE-VENYPGfPEGISGPELMEKMKEQAVKFGAEI---IYE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 104 NVanfqkakddavkqltggIELLFKKNKVTYYKGNGsfedetkirvtpvdgleGTVKedhildVKNIIVATGSEVTPFpG 183
Cdd:TIGR01292 77 EV-----------------IKVDKSDRPFKVYTGDG-----------------KEYT------AKAVIIATGASARKL-G 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 184 IEIDEE---KIVSST----GALSLKeipKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQIGASmdgevaKATQ-KFL 255
Cdd:TIGR01292 116 IPGEDEfwgRGVSYCatcdGPFFKN---KEVAVVGGGDSAIEEALYLTRIAKKVTLVHRRDKFRAE------KILLdRLK 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 256 KKQGLDFKLSTKVISAKrnDDKNVVEIVVEDTKTNKQENLEAEVLLVAVGRRPYIAGLGAEkigLEVDKRGRLVIDDQFN 335
Cdd:TIGR01292 187 KNPKIEFLWNSTVEEIV--GDNKVEGVKIKNTVTGEEEELEVDGVFIAIGHEPNTELLKGL---LELDENGYIVTDEGMR 261
|
330 340 350
....*....|....*....|....*....|.
gi 768798536 336 SKFPHIKVVGDVT-FGPMLAHKAEEEGIAAV 365
Cdd:TIGR01292 262 TSVPGVFAAGDVRdKGYRQAVTAAGDGCIAA 292
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
28-86 |
2.25e-08 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 56.02 E-value: 2.25e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 28 DVVIIGGGPAGYVAAIKAAQLGFNTA-CVEKrgklGGTCLNVGCIPSKALLNNSHLYHQM 86
Cdd:pfam01134 1 DVIVIGGGHAGCEAALAAARMGAKVLlITHN----TDTIAELSCNPSIGGIAKGHLVREI 56
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
25-64 |
5.36e-08 |
|
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: 55.22 E-value: 5.36e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 768798536 25 KSHDVVIIGGGPAGYVAAIKAAQLGFNTACVEKRGKLGGT 64
Cdd:COG1053 2 HEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGGH 41
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
28-64 |
9.62e-08 |
|
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: 54.22 E-value: 9.62e-08
10 20 30
....*....|....*....|....*....|....*..
gi 768798536 28 DVVIIGGGPAGYVAAIKAAQLGFNTACVEKRGKLGGT 64
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGA 37
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
27-64 |
9.78e-07 |
|
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: 51.02 E-value: 9.78e-07
10 20 30
....*....|....*....|....*....|....*...
gi 768798536 27 HDVVIIGGGPAGYVAAIKAAQLGFNTACVEKRGKLGGT 64
Cdd:COG2072 7 VDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGT 44
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
127-448 |
1.42e-06 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 50.98 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 127 FKKNKVTYYKGNgsfedetkiRVTPVDGLEGTVKED--HILDVKNIIVATGSE--VTPFPGIEIDE----EKIVSSTGAL 198
Cdd:TIGR02374 64 YEKHGITLYTGE---------TVIQIDTDQKQVITDagRTLSYDKLILATGSYpfILPIPGADKKGvyvfRTIEDLDAIM 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 199 SLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQIGA-SMDGEVAKATQKFLKKQGLDFKLSTKVISAkrnddk 277
Cdd:TIGR02374 135 AMAQRFKKAAVIGGGLLGLEAAVGLQNLGMDVSVIHHAPGLMAkQLDQTAGRLLQRELEQKGLTFLLEKDTVEI------ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 278 nVVEIVVEDTKTNKQENLEAEVLLVAVGRRPYIAgLGAEKiGLEVDkrGRLVIDDQFNSKFPHIKVVGDVTfgpmlAHKA 357
Cdd:TIGR02374 209 -VGATKADRIRFKDGSSLEADLIVMAAGIRPNDE-LAVSA-GIKVN--RGIIVNDSMQTSDPDIYAVGECA-----EHNG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 358 EEEGIAA--VEMLKTGHGHVnyNNIPSVMYSHPEVAwvgkteEQLKEAGID-YKIGKFPFAANSRA-KTNQDTEGFVKIL 433
Cdd:TIGR02374 279 RVYGLVAplYEQAKVLADHI--CGVECEEYEGSDLS------AKLKLLGVDvWSAGDAQETERTTSiKIYDEQKGIYKKL 350
|
330
....*....|....*
gi 768798536 434 IDSKtERILGAHIIG 448
Cdd:TIGR02374 351 VLSD-DKLLGAVLFG 364
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
27-62 |
2.83e-06 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 49.50 E-value: 2.83e-06
10 20 30
....*....|....*....|....*....|....*.
gi 768798536 27 HDVVIIGGGPAGYVAAIKAAQLGFNTACVEKRGKLG 62
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
|
|
| COG2509 |
COG2509 |
FAD-dependent dehydrogenase [General function prediction only]; |
1-60 |
3.63e-06 |
|
FAD-dependent dehydrogenase [General function prediction only];
Pssm-ID: 441999 [Multi-domain] Cd Length: 466 Bit Score: 49.34 E-value: 3.63e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768798536 1 MLR--IRSLLNNKRAFSSTV-RTLTI-NKSHDVVIIGGGPAGYVAAIKAAQLGFNTACVEkRGK 60
Cdd:COG2509 1 MIRtnLKLPLDDEEALKAAIaKKLGIpSLKYDVVIVGAGPAGLFAALELAEAGLKPLVLE-RGK 63
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
24-63 |
3.76e-06 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 49.46 E-value: 3.76e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 768798536 24 NKSHDVVIIGGGPAGYVAAIKAAQLGFNTACVEKRGKLGG 63
Cdd:COG1233 1 MMMYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
225-369 |
4.62e-06 |
|
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: 48.98 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 225 RLGSK-VTVVEFQPQigASM---DGEVAKAtqkflKKQGLDFKLSTKVISAKRNDDKNVVEIVVEDTK------------ 288
Cdd:COG0493 276 RLGAEsVTIVYRRTR--EEMpasKEEVEEA-----LEEGVEFLFLVAPVEIIGDENGRVTGLECVRMElgepdesgrrrp 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 289 ---TNKQENLEAEVLLVAVGRRPYIAGLGAEKiGLEVDKRGRLVIDDQ-FNSKFPHIKVVGDVTFGPMLAHKAEEEG-IA 363
Cdd:COG0493 349 vpiEGSEFTLPADLVILAIGQTPDPSGLEEEL-GLELDKRGTIVVDEEtYQTSLPGVFAGGDAVRGPSLVVWAIAEGrKA 427
|
....*.
gi 768798536 364 AVEMLK 369
Cdd:COG0493 428 ARAIDR 433
|
|
| PRK07494 |
PRK07494 |
UbiH/UbiF family hydroxylase; |
20-55 |
6.84e-06 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181001 [Multi-domain] Cd Length: 388 Bit Score: 48.36 E-value: 6.84e-06
10 20 30
....*....|....*....|....*....|....*.
gi 768798536 20 TLTINKSHDVVIIGGGPAGYVAAIKAAQLGFNTACV 55
Cdd:PRK07494 1 SLMEKEHTDIAVIGGGPAGLAAAIALARAGASVALV 36
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
145-346 |
1.65e-05 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 47.22 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 145 TKIRVTPVDGLEGTVK-EDHILDVKNIIVATGSE--VTPFPGieidEEKIVSSTgalSLKEI---------PKRLTIIGG 212
Cdd:PRK04965 77 PHTWVTDIDAEAQVVKsQGNQWQYDKLVLATGASafVPPIPG----RELMLTLN---SQQEYraaetqlrdAQRVLVVGG 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 213 GIIGLEMGSVYSRLGSKVTVVEFQPQIGAS-MDGEVAKATQKFLKKQGLDFKLSTKVISAKRNDDKNVVeivvedtKTNK 291
Cdd:PRK04965 150 GLIGTELAMDLCRAGKAVTLVDNAASLLASlMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRA-------TLDS 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 768798536 292 QENLEAEVLLVAVGRRPYIAgLgAEKIGLEVdKRGrLVIDDQFNSKFPHIKVVGD 346
Cdd:PRK04965 223 GRSIEVDAVIAAAGLRPNTA-L-ARRAGLAV-NRG-IVVDSYLQTSAPDIYALGD 273
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
19-63 |
2.98e-05 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 46.39 E-value: 2.98e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 768798536 19 RTLTINKShdVVIIGGGPAGYVAAIKAAQLGFNTACVEKRGKLGG 63
Cdd:COG1148 135 IKVPVNKR--ALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGG 177
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
229-361 |
3.98e-05 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 45.91 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 229 KVTVVEFQPQIGASMDGEVAKATQKFLKKQGLDFKLSTKVISAKrndDKNVVeivvedTKTNKQENLEAEVLLVAVGRRP 308
Cdd:PTZ00318 212 KVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEVL---DKEVV------LKDGEVIPTGLVVWSTGVGPGP 282
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 768798536 309 YIAGLGAEKiglevDKRGRLVIDDQFNSK-FPHIKVVGDVTFG-----PMLAHKAEEEG 361
Cdd:PTZ00318 283 LTKQLKVDK-----TSRGRISVDDHLRVKpIPNVFALGDCAANeerplPTLAQVASQQG 336
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
31-65 |
4.39e-05 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 41.36 E-value: 4.39e-05
10 20 30
....*....|....*....|....*....|....*
gi 768798536 31 IIGGGPAGYVAAIKAAQLGFNTACVEKRGKLGGTC 65
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNA 35
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
24-58 |
1.46e-04 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 43.77 E-value: 1.46e-04
10 20 30
....*....|....*....|....*....|....*
gi 768798536 24 NKSHDVVIIGGGPAGYVAAIKAAQLGFNTACVEKR 58
Cdd:COG0654 1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVERA 35
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
28-64 |
1.82e-04 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 43.87 E-value: 1.82e-04
10 20 30
....*....|....*....|....*....|....*..
gi 768798536 28 DVVIIGGGPAGYVAAIKAAQLGFNTACVEKRGKLGGT 64
Cdd:PRK07843 9 DVVVVGSGAAGMVAALTAAHRGLSTVVVEKAPHYGGS 45
|
|
| TIGR00275 |
TIGR00275 |
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ... |
30-62 |
2.10e-04 |
|
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: 43.74 E-value: 2.10e-04
10 20 30
....*....|....*....|....*....|...
gi 768798536 30 VIIGGGPAGYVAAIKAAQLGFNTACVEKRGKLG 62
Cdd:TIGR00275 1 IIIGGGAAGLMAAITAARAGLSVLLLEKNKKIG 33
|
|
| PRK12844 |
PRK12844 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
22-64 |
2.41e-04 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 183787 [Multi-domain] Cd Length: 557 Bit Score: 43.59 E-value: 2.41e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 768798536 22 TINKSHDVVIIGGGPAGYVAAIKAAQLGFNTACVEKRGKLGGT 64
Cdd:PRK12844 2 TWDETYDVVVVGSGGGGMCAALAAADSGLEPLIVEKQDKVGGS 44
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
24-64 |
2.67e-04 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 43.57 E-value: 2.67e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 768798536 24 NKSHDVVIIGGGPAGYVAAIKAAQLGFNTACVEKRGKLGGT 64
Cdd:PRK12843 14 DAEFDVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGT 54
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
295-366 |
3.45e-04 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 42.67 E-value: 3.45e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768798536 295 LEAEVLLVAVGRRPyIAGLGAEKIGLEVDKRGRLVIDDQFNSKFPHIKVVGDVTFGPMLAHKAEEEGIAAVE 366
Cdd:PRK12770 273 LEADTVVFAIGEIP-TPPFAKECLGIELNRKGEIVVDEKHMTSREGVFAAGDVVTGPSKIGKAIKSGLRAAQ 343
|
|
| PLN00128 |
PLN00128 |
Succinate dehydrogenase [ubiquinone] flavoprotein subunit |
23-57 |
3.56e-04 |
|
Succinate dehydrogenase [ubiquinone] flavoprotein subunit
Pssm-ID: 177739 [Multi-domain] Cd Length: 635 Bit Score: 43.31 E-value: 3.56e-04
10 20 30
....*....|....*....|....*....|....*
gi 768798536 23 INKSHDVVIIGGGPAGYVAAIKAAQLGFNTACVEK 57
Cdd:PLN00128 47 VDHTYDAVVVGAGGAGLRAAIGLSEHGFNTACITK 81
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
26-65 |
4.36e-04 |
|
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440845 [Multi-domain] Cd Length: 443 Bit Score: 42.51 E-value: 4.36e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 768798536 26 SHDVVIIGGGPAGYVAAIKAAQLGFNTACVEKRGKLGGTC 65
Cdd:COG1232 1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLI 40
|
|
| GlpB |
COG3075 |
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism]; |
28-55 |
4.50e-04 |
|
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 442309 Cd Length: 415 Bit Score: 42.47 E-value: 4.50e-04
10 20
....*....|....*....|....*...
gi 768798536 28 DVVIIGGGPAGYVAAIKAAQLGFNTACV 55
Cdd:COG3075 4 DVVVIGGGLAGLTAAIRAAEAGLRVAIV 31
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
8-63 |
6.13e-04 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 42.45 E-value: 6.13e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 768798536 8 LNNKRAFsstvrtltinkshDVVIIGGGPAGYVAAIKAAQLGFNTACVEKRgkLGG 63
Cdd:PRK15317 206 LNAKDPY-------------DVLVVGGGPAGAAAAIYAARKGIRTGIVAER--FGG 246
|
|
| sdhA |
PRK07803 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
26-57 |
7.17e-04 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 236101 [Multi-domain] Cd Length: 626 Bit Score: 42.33 E-value: 7.17e-04
10 20 30
....*....|....*....|....*....|..
gi 768798536 26 SHDVVIIGGGPAGYVAAIKAAQLGFNTACVEK 57
Cdd:PRK07803 8 SYDVVVIGAGGAGLRAAIEARERGLRVAVVCK 39
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
28-64 |
1.02e-03 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 41.63 E-value: 1.02e-03
10 20 30
....*....|....*....|....*....|....*..
gi 768798536 28 DVVIIGGGPAGYVAAIKAAQLGFNTACVEKRGKLGGT 64
Cdd:PRK06134 14 DVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGGT 50
|
|
| PTZ00306 |
PTZ00306 |
NADH-dependent fumarate reductase; Provisional |
29-63 |
1.02e-03 |
|
NADH-dependent fumarate reductase; Provisional
Pssm-ID: 140327 [Multi-domain] Cd Length: 1167 Bit Score: 42.07 E-value: 1.02e-03
10 20 30
....*....|....*....|....*....|....*
gi 768798536 29 VVIIGGGPAGYVAAIKAAQLGFNTACVEKRGKLGG 63
Cdd:PTZ00306 412 VIVVGGGLAGCSAAIEAASCGAQVILLEKEAKLGG 446
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
30-62 |
1.34e-03 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 41.19 E-value: 1.34e-03
10 20 30
....*....|....*....|....*....|...
gi 768798536 30 VIIGGGPAGYVAAIKAAQLGFNTACVEKRGKLG 62
Cdd:COG2081 1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVG 33
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
28-71 |
1.46e-03 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 40.99 E-value: 1.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 768798536 28 DVVIIGGGPAGYVAAIKAAQLGFNTACVekRGKLGGTCLNVGCI 71
Cdd:PRK05329 4 DVLVIGGGLAGLTAALAAAEAGKRVALV--AKGQGALHFSSGSI 45
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
170-347 |
1.47e-03 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 41.06 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 170 IIVATGSEVTPFPGIEIDEEKIVS---STGALSLKEI---PKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEfqpQIGASM 243
Cdd:PRK09754 104 LFIATGAAARPLPLLDALGERCFTlrhAGDAARLREVlqpERSVVIVGAGTIGLELAASATQRRCKVTVIE---LAATVM 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768798536 244 DGEVAKATQKFL----KKQGLDFKLSTKVISAKRNDdknvvEIVVedtKTNKQENLEAEVLlvavgrrpyIAGLGAE--- 316
Cdd:PRK09754 181 GRNAPPPVQRYLlqrhQQAGVRILLNNAIEHVVDGE-----KVEL---TLQSGETLQADVV---------IYGIGISand 243
|
170 180 190
....*....|....*....|....*....|...
gi 768798536 317 KIGLE--VDKRGRLVIDDQFNSKFPHIKVVGDV 347
Cdd:PRK09754 244 QLAREanLDTANGIVIDEACRTCDPAIFAGGDV 276
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
28-62 |
1.67e-03 |
|
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: 40.38 E-value: 1.67e-03
10 20 30
....*....|....*....|....*....|....*
gi 768798536 28 DVVIIGGGPAGYVAAIKAAQLGFNTACVEKRGKLG 62
Cdd:TIGR02032 2 DVVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPR 36
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
28-64 |
1.68e-03 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 40.83 E-value: 1.68e-03
10 20 30
....*....|....*....|....*....|....*..
gi 768798536 28 DVVIIGGGPAGYVAAIKAAQLGFNTACVEKRGKLGGT 64
Cdd:PRK12842 11 DVLVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGGT 47
|
|
| PRK06481 |
PRK06481 |
flavocytochrome c; |
22-66 |
1.98e-03 |
|
flavocytochrome c;
Pssm-ID: 180584 [Multi-domain] Cd Length: 506 Bit Score: 40.59 E-value: 1.98e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 768798536 22 TINKSHDVVIIGGGPAGYVAAIKAAQLGFNTACVEKRGKLGGTCL 66
Cdd:PRK06481 57 ELKDKYDIVIVGAGGAGMSAAIEAKDAGMNPVILEKMPVAGGNTM 101
|
|
| PRK12835 |
PRK12835 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
28-71 |
2.83e-03 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237221 [Multi-domain] Cd Length: 584 Bit Score: 40.17 E-value: 2.83e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 768798536 28 DVVIIGGGPAGYVAAIKAAQLGFNTACVEKRGKLGG-TCLNVGCI 71
Cdd:PRK12835 13 DVLVVGSGGGGMTAALTAAARGLDTLVVEKSAHFGGsTALSGGGI 57
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
25-68 |
3.96e-03 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 39.52 E-value: 3.96e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 768798536 25 KSHDVVIIGGGPAGYVAAIKAAQLGFNTACVEKRGKLGGTCLNV 68
Cdd:COG1231 6 RGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTL 49
|
|
| glycerol3P_GlpB |
TIGR03378 |
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are ... |
28-55 |
9.57e-03 |
|
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are the B subunit, product of the glpB gene, of a three-subunit, membrane-anchored, FAD-dependent anaerobic glycerol-3-phosphate dehydrogenase. [Energy metabolism, Anaerobic]
Pssm-ID: 213807 Cd Length: 419 Bit Score: 38.46 E-value: 9.57e-03
10 20
....*....|....*....|....*...
gi 768798536 28 DVVIIGGGPAGYVAAIKAAQLGFNTACV 55
Cdd:TIGR03378 2 DVIIIGGGLAGLSCALRLAEAGKKCAII 29
|
|
| |
