|
Name |
Accession |
Description |
Interval |
E-value |
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
40-501 |
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: 590.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 40 IDADVTVIGSGPGGYVAAIKAAQLGFKAVCVEKnETLGGTCLNVGCIPSKALLNNSHYYHLAhgKDFASRGIEMSEVRLN 119
Cdd:COG1249 2 KDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEK-GRLGGTCLNVGCIPSKALLHAAEVAHEA--RHAAEFGISAGAPSVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 120 LDKMMEQKSNAVKALTGGIAHLFKQNKVAHVNGYGKITGKNQVTATKadgsTQVIDTKNILIATGSEVTPFPGITIDEDT 199
Cdd:COG1249 79 WAALMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVTG----GETLTADHIVIATGSRPRVPPIPGLDEVR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 200 VVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGiGIDMEISKNFQRILQKQGFKFKLNTKVT 279
Cdd:COG1249 155 VLTSDEALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLP-GEDPEISEALEKALEKEGIDILTGAKVT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 280 GATRKPDGkidVFIEAASGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAG 359
Cdd:COG1249 234 SVEKTGDG---VTVTLEDGGGEEAVEADKVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRTSVPGIYAIGDVTGG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 360 PMLAHKAEDEGIICVEGMAGGAVH-IDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGM 438
Cdd:COG1249 311 PQLAHVASAEGRVAAENILGKKPRpVDYRAIPSVVFTDPEIASVGLTEEEAREAGIDVKVGKFPFAANGRALALGETEGF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246204903 439 VKILGQKSTDRVLGAHILGPGAGEMINEAALALEYGASCEDIARVCHAHPTLSEAFREANLAA 501
Cdd:COG1249 391 VKLIADAETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAALAL 453
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
43-508 |
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: 569.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 43 DVTVIGSGPGGYVAAIKAAQLGFKAVCVEKnETLGGTCLNVGCIPSKALLNNSHYYH-LAHGKDFasrGIEMSEVRLNLD 121
Cdd:TIGR01350 3 DVIVIGGGPGGYVAAIRAAQLGLKVALVEK-EYLGGTCLNVGCIPTKALLHSAEVYDeIKHAKDL---GIEVENVSVDWE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 122 KMMEQKSNAVKALTGGIAHLFKQNKVAHVNGYGKITGKNQVTATKADGsTQVIDTKNILIATGSEVTPFPG-ITIDEDTV 200
Cdd:TIGR01350 79 KMQKRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGENG-EETLEAKNIIIATGSRPRSLPGpFDFDGKVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 201 VSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGiGIDMEISKNFQRILQKQGFKFKLNTKVTG 280
Cdd:TIGR01350 158 ITSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILP-GEDAEVSKVLQKALKKKGVKILTNTKVTA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 281 ATRKPDGkidVFIEAaSGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGP 360
Cdd:TIGR01350 237 VEKNDDQ---VTYEN-KGGETETLTGEKVLVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDVIGGP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 361 MLAHKAEDEGIICVEGMAGGA-VHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMV 439
Cdd:TIGR01350 313 MLAHVASHEGIVAAENIAGKEpAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGYDVKIGKFPFAANGKALALGETDGFV 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246204903 440 KILGQKSTDRVLGAHILGPGAGEMINEAALALEYGASCEDIARVCHAHPTLSEAFREANLAAsFGKSIN 508
Cdd:TIGR01350 393 KIIADKKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEAIKEAALAA-LGKPIH 460
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
43-509 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 563.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 43 DVTVIGSGPGGYVAAIKAAQLGFKAVCVE--KNET----LGGTCLNVGCIPSKALLNNSHYYHLAhGKDFASRGIEMSEV 116
Cdd:PRK06327 6 DVVVIGAGPGGYVAAIRAAQLGLKVACIEawKNPKgkpaLGGTCLNVGCIPSKALLASSEEFENA-GHHFADHGIHVDGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 117 RLNLDKMMEQKSNAVKALTGGIAHLFKQNKVAHVNGYGKITGK----NQVTATKADGSTqvIDTKNILIATGSEVTPFPG 192
Cdd:PRK06327 85 KIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVGKtdagYEIKVTGEDETV--ITAKHVIIATGSEPRHLPG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 193 ITIDEDTVVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHVggigiDMEISKNFQRILQKQ 268
Cdd:PRK06327 163 VPFDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEalpaFLAAA-----DEQVAKEAAKAFTKQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 269 GFKFKLNTKVtGATRKPDGKIDVFIEAASGgKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIP 348
Cdd:PRK06327 238 GLDIHLGVKI-GEIKTGGKGVSVAYTDADG-EAQTLEVDKLIVSIGRVPNTDGLGLEAVGLKLDERGFIPVDDHCRTNVP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 349 NIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSR 428
Cdd:PRK06327 316 NVYAIGDVVRGPMLAHKAEEEGVAVAERIAGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLKAEGVEYKAGKFPFMANGR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 429 AKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMINEAALALEYGASCEDIARVCHAHPTLSEAFREANLAASfGKSIN 508
Cdd:PRK06327 396 ALAMGEPDGFVKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEVWHEAALAVD-KRPLH 474
|
.
gi 1246204903 509 F 509
Cdd:PRK06327 475 F 475
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
38-509 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 542.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 38 QPIDADVTVIGSGPGGYVAAIKAAQLGFKAVCVEKnETLGGTCLNVGCIPSKALLNNSHYYHLA-HGKDFasrGIEMSEV 116
Cdd:PRK06416 1 FAFEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEK-EKLGGTCLNRGCIPSKALLHAAERADEArHSEDF---GIKAENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 117 RLNLDKMMEQKSNAVKALTGGIAHLFKQNKVAHVNGYGKITGKNQVTATKADGsTQVIDTKNILIATGSEVTPFPGITID 196
Cdd:PRK06416 77 GIDFKKVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDG-EQTYTAKNIILATGSRPRELPGIEID 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 197 EDTVVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGiGIDMEISKNFQRILQKQGFKFKLNT 276
Cdd:PRK06416 156 GRVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILP-GEDKEISKLAERALKKRGIKIKTGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 277 KVTGATRKPDGkIDVFIEAasGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDpRGRIPVNTRFQTKIPNIYAIGDV 356
Cdd:PRK06416 235 KAKKVEQTDDG-VTVTLED--GGKEETLEADYVLVAVGRRPNTENLGLEELGVKTD-RGFIEVDEQLRTNVPNIYAIGDI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 357 VAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTD 436
Cdd:PRK06416 311 VGGPMLAHKASAEGIIAAEAIAGNPHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFDVKVVKFPFAGNGKALALGETD 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246204903 437 GMVKILGQKSTDRVLGAHILGPGAGEMINEAALALEYGASCEDIARVCHAHPTLSEAFREANLAASfGKSINF 509
Cdd:PRK06416 391 GFVKLIFDKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEALGEAALAAA-GKPLHA 462
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
40-503 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 539.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 40 IDADVTVIGSGPGGYVAAIKAAQLGFKAVCVEKnETLGGTCLNVGCIPSKALLNNSHYYHLAhgKDFASRGIEMSEVRLN 119
Cdd:PRK06292 2 EKYDVIVIGAGPAGYVAARRAAKLGKKVALIEK-GPLGGTCLNVGCIPSKALIAAAEAFHEA--KHAEEFGIHADGPKID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 120 LDKMMEQKSNAVKALTGGIAH-LFKQNKVAHVNGYGKITGKNQVTAtkadgSTQVIDTKNILIATGSEVTPFPGIT-IDE 197
Cdd:PRK06292 79 FKKVMARVRRERDRFVGGVVEgLEKKPKIDKIKGTARFVDPNTVEV-----NGERIEAKNIVIATGSRVPPIPGVWlILG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 198 DTVVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGiGIDMEISKNFQRILQKQgFKFKLNTK 277
Cdd:PRK06292 154 DRLLTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILP-LEDPEVSKQAQKILSKE-FKIKLGAK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 278 VTGATRKPDGKIDVFIEaasGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVV 357
Cdd:PRK06292 232 VTSVEKSGDEKVEELEK---GGKTETIEADYVLVATGRRPNTDGLGLENTGIELDERGRPVVDEHTQTSVPGIYAAGDVN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 358 AGPMLAHKAEDEGIICVEGMAGG-AVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTD 436
Cdd:PRK06292 309 GKPPLLHEAADEGRIAAENAAGDvAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEVPFEAQGRARVMGKND 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246204903 437 GMVKILGQKSTDRVLGAHILGPGAGEMINEAALALEYGASCEDIARVCHAHPTLSEAFREANLAASF 503
Cdd:PRK06292 389 GFVKVYADKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRTALRDLFS 455
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
38-501 |
2.40e-107 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 327.50 E-value: 2.40e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 38 QPIDADVTVIGSGPGGYVAAIKAAQLGFKAVCVEKNETLGGTCLNVGCIPSKAL------LNNSHYYHLaHGKDFASRGI 111
Cdd:PRK05249 2 HMYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGGGCTHTGTIPSKALreavlrLIGFNQNPL-YSSYRVKLRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 112 EMSEVRLNLDKMMEQKSNAvkaltggIAHLFKQNKVAHVNGYGKITGKNQVTATKADGSTQVIDTKNILIATGSEvtPF- 190
Cdd:PRK05249 81 TFADLLARADHVINKQVEV-------RRGQYERNRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATGSR--PYr 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 191 -PGITIDEDTVVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVE-------FLghvggigiDMEISKNFQ 262
Cdd:PRK05249 152 pPDVDFDHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINtrdrllsFL--------DDEISDALS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 263 RILQKQGFKFKLNTKVTGATRKPDGKIdvfIEAASGGKaevITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTR 342
Cdd:PRK05249 224 YHLRDSGVTIRHNEEVEKVEGGDDGVI---VHLKSGKK---IKADCLLYANGRTGNTDGLNLENAGLEADSRGQLKVNEN 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 343 FQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFP 422
Cdd:PRK05249 298 YQTAVPHIYAVGDVIGFPSLASASMDQGRIAAQHAVGEATAHLIEDIPTGIYTIPEISSVGKTEQELTAAKVPYEVGRAR 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246204903 423 FAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMINEAALALEYGASCEDIARVCHAHPTLSEAFREANLAA 501
Cdd:PRK05249 378 FKELARAQIAGDNVGMLKILFHRETLEILGVHCFGERATEIIHIGQAIMEQKGTIEYFVNTTFNYPTMAEAYRVAALDG 456
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
43-507 |
1.98e-105 |
|
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: 322.83 E-value: 1.98e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 43 DVTVIGSGPGGYVAAIKAAQLGFKAVCVEKNeTLGGTCLNVGCIPSKALLNNSHYYHLAHGkdfASRGIEMSEVRLNLDK 122
Cdd:TIGR02053 2 DLVIIGSGAAAFAAAIKAAELGASVAMVERG-PLGGTCVNVGCVPSKMLLRAAEVAHYARK---PPFGGLAATVAVDFGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 123 MMEQKSNAVKAL-TGGIAHLFKQNKVAHVNGYGKITGKNQVtatKADGSTQVIDTKNILIATGSE--VTPFPGItiDEDT 199
Cdd:TIGR02053 78 LLEGKREVVEELrHEKYEDVLSSYGVDYLRGRARFKDPKTV---KVDLGREVRGAKRFLIATGARpaIPPIPGL--KEAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 200 VVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHvggigIDMEISKNFQRILQKQGFKFKLN 275
Cdd:TIGR02053 153 YLTSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQrsdrLLPR-----EEPEISAAVEEALAEEGIEVVTS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 276 TKVTGATRKPDGKIDVFIEAASGGKAEVitcDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGD 355
Cdd:TIGR02053 228 AQVKAVSVRGGGKIITVEKPGGQGEVEA---DELLVATGRRPNTDGLGLEKAGVKLDERGGILVDETLRTSNPGIYAAGD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 356 VVAGPMLAHKAEDEGIICVEGMAGGA-VHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNAD 434
Cdd:TIGR02053 305 VTGGLQLEYVAAKEGVVAAENALGGAnAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNVPRARINRD 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246204903 435 TDGMVKILGQKSTDRVLGAHILGPGAGEMINEAALALEYGASCEDIARVCHAHPTLSEAFREAnlAASFGKSI 507
Cdd:TIGR02053 385 TRGFIKLVAEPGTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGLKLA--AQTFYRDV 455
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
43-503 |
2.94e-101 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 312.14 E-value: 2.94e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 43 DVTVIGSGPGGYVAAIKAAQLGFKAVCVEKNEtLGGTCLNVGCIPSKALLNNSHYYHLA-HGKDFasrGIEMS-EVRLNL 120
Cdd:PRK06370 7 DAIVIGAGQAGPPLAARAAGLGMKVALIERGL-LGGTCVNTGCVPTKTLIASARAAHLArRAAEY---GVSVGgPVSVDF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 121 DKMMEQKSNAVKALTGGIAHLFKQNKVAHV-NGYGKITGKNQVtatKADGSTqvIDTKNILIATGSE--VTPFPGItiDE 197
Cdd:PRK06370 83 KAVMARKRRIRARSRHGSEQWLRGLEGVDVfRGHARFESPNTV---RVGGET--LRAKRIFINTGARaaIPPIPGL--DE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 198 DTVVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGiGIDMEISKNFQRILQKQGFKFKLNTK 277
Cdd:PRK06370 156 VGYLTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLP-REDEDVAAAVREILEREGIDVRLNAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 278 VTGATRKPDGKIdvfIEAASGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVV 357
Cdd:PRK06370 235 CIRVERDGDGIA---VGLDCNGGAPEITGSHILVAVGRVPNTDDLGLEAAGVETDARGYIKVDDQLRTTNPGIYAAGDCN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 358 AGPMLAHKAEDEGIICVEGMA-GGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTD 436
Cdd:PRK06370 312 GRGAFTHTAYNDARIVAANLLdGGRRKVSDRIVPYATYTDPPLARVGMTEAEARKSGRRVLVGTRPMTRVGRAVEKGETQ 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246204903 437 GMVKILGQKSTDRVLGAHILGPGAGEMINEAALALEYGASCEDIARVCHAHPTLSEAFReaNLAASF 503
Cdd:PRK06370 392 GFMKVVVDADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIP--TLAQAL 456
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
41-494 |
2.16e-79 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 255.08 E-value: 2.16e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 41 DADVTVIGSGPGGYVAAIKAAQLGFKAVCVEKNEtLGGTCLNVGCIPSKALLNNSHYYHLAH--GKDFasrGIEMSEVRL 118
Cdd:PRK06116 4 DYDLIVIGGGSGGIASANRAAMYGAKVALIEAKR-LGGTCVNVGCVPKKLMWYGAQIAEAFHdyAPGY---GFDVTENKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 119 NLDKMMEQKSNAVKALTGGIAHLFKQNKVAHVNGYGKITGKNQVtatKADGstQVIDTKNILIATGSEVTP--FPGItid 196
Cdd:PRK06116 80 DWAKLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTV---EVNG--ERYTADHILIATGGRPSIpdIPGA--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 197 eDTVVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAV----EFLGhvggiGIDMEISKNFQRILQKQGFKF 272
Cdd:PRK06116 152 -EYGITSDGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFvrgdAPLR-----GFDPDIRETLVEEMEKKGIRL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 273 KLNTKVTGATRKPDGKIDVFIEaasggKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYA 352
Cdd:PRK06116 226 HTNAVPKAVEKNADGSLTLTLE-----DGETLTVDCLIWAIGREPNTDGLGLENAGVKLNEKGYIIVDEYQNTNVPGIYA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 353 IGDVVAGPMLAHKAEDEGIICVEGMAGG--AVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEY--KVGKFPFAANSR 428
Cdd:PRK06116 301 VGDVTGRVELTPVAIAAGRRLSERLFNNkpDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDnvKVYRSSFTPMYT 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246204903 429 AKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMINEAALALEYGASCEDIARVCHAHPTLSEAF 494
Cdd:PRK06116 381 ALTGHRQPCLMKLVVVGKEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEF 446
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
43-502 |
3.98e-74 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 247.13 E-value: 3.98e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 43 DVTVIGSGPGGYVAAIKAAQLGFKAVCVEKNE-TLGGTCLNVGCIPSKALL----------NNSHYY----HLAHGKDFA 107
Cdd:PTZ00153 118 DVGIIGCGVGGHAAAINAMERGLKVIIFTGDDdSIGGTCVNVGCIPSKALLyatgkyrelkNLAKLYtygiYTNAFKNGK 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 108 SRGIEMS-----EVRLNLDKMMEQKSNAVKALTGGIAHLFKQNKVA----HVN---GYGKITGKNQVtatKADGSTQVID 175
Cdd:PTZ00153 198 NDPVERNqlvadTVQIDITKLKEYTQSVIDKLRGGIENGLKSKKFCknseHVQviyERGHIVDKNTI---KSEKSGKEFK 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 176 TKNILIATGSevTPF--PGITIDEDTVVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGiGI 253
Cdd:PTZ00153 275 VKNIIIATGS--TPNipDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSPQLLP-LL 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 254 DMEISKNFQRILQK-QGFKFKLNTKVT-------------GATRKPDGKIDVFIEAASGGKAevITCDVLLVCIGRRPFT 319
Cdd:PTZ00153 352 DADVAKYFERVFLKsKPVRVHLNTLIEyvragkgnqpviiGHSERQTGESDGPKKNMNDIKE--TYVDSCLVATGRKPNT 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 320 KNLGLEELGIELDpRGRIPVNTRFQTK------IPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVH---------- 383
Cdd:PTZ00153 430 NNLGLDKLKIQMK-RGFVSVDEHLRVLredqevYDNIFCIGDANGKQMLAHTASHQALKVVDWIEGKGKEnvninvenwa 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 384 ---IDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFP--FAANSRA----------------------KTNADTD 436
Cdd:PTZ00153 509 skpIIYKNIPSVCYTTPELAFIGLTEKEAKELYPPDNVGVEIsfYKANSKVlcennisfpnnsknnsynkgkyNTVDNTE 588
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246204903 437 GMVKILGQKSTDRVLGAHILGPGAGEMINEAALALEYGASCEDIARVCHAHPTLSEAFREANLAAS 502
Cdd:PTZ00153 589 GMVKIVYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDAAFKAIA 654
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
43-370 |
1.46e-71 |
|
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: 229.90 E-value: 1.46e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 43 DVTVIGSGPGGYVAAIKAAQLGFKAVCVEknetLGGTCLNVGCIPSKALLNnshyyhlahgkdfasrGIEMSEVRLNLDK 122
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIE----DEGTCPYGGCVLSKALLG----------------AAEAPEIASLWAD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 123 MMEQKSNAVKALTGGIAHLFKQNKVAHVNGYGKITGKNQVtatkaDGSTQVIDTKNILIATGSE--VTPFPGIT---IDE 197
Cdd:pfam07992 62 LYKRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELV-----DGDGETITYDRLVIATGARprLPPIPGVElnvGFL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 198 DTVVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGiGIDMEISKNFQRILQKQGFKFKLNTK 277
Cdd:pfam07992 137 VRTLDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLR-AFDEEISAALEKALEKNGVEVRLGTS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 278 VTGATRKPDGKidvfieAASGGKAEVITCDVLLVCIGRRPftKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDV- 356
Cdd:pfam07992 216 VKEIIGDGDGV------EVILKDGTEIDADLVVVAIGRRP--NTELLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDCr 287
|
330
....*....|....
gi 1246204903 357 VAGPMLAHKAEDEG 370
Cdd:pfam07992 288 VGGPELAQNAVAQG 301
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
44-508 |
1.43e-70 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 235.05 E-value: 1.43e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 44 VTVIGSGPGGYVAAIKAAQLGFKAVCVEKNeTLGGTCLNVGCIPSKALLNNSHYYHLAHGKDFASrGIEMSEVRLNLDKM 123
Cdd:PRK13748 101 VAVIGSGGAAMAAALKAVEQGARVTLIERG-TIGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDG-GIAATVPTIDRSRL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 124 MEQKSNAVKALTG----GIahLFKQNKVAHVNGYGKITGKNQVTATKADGSTQVIDTKNILIATGSE--VTPFPGITidE 197
Cdd:PRK13748 179 LAQQQARVDELRHakyeGI--LDGNPAITVLHGEARFKDDQTLIVRLNDGGERVVAFDRCLIATGASpaVPPIPGLK--E 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 198 DTVVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHvggigiDMEISKNFQRILQKQGFKFK 273
Cdd:PRK13748 255 TPYWTSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILArstlFFRE------DPAIGEAVTAAFRAEGIEVL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 274 LNTKVTgATRKPDGKidvFIEAASGGKaevITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAI 353
Cdd:PRK13748 329 EHTQAS-QVAHVDGE---FVLTTGHGE---LRADKLLVATGRAPNTRSLALDAAGVTVNAQGAIVIDQGMRTSVPHIYAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 354 GDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNA 433
Cdd:PRK13748 402 GDCTDQPQFVYVAAAAGTRAAINMTGGDAALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRTLTLDNVPRALANF 481
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246204903 434 DTDGMVKILGQKSTDRVLGAHILGPGAGEMINEAALALEYGASCEDIARVCHAHPTLSEAFREAnlAASFGKSIN 508
Cdd:PRK13748 482 DTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAALAIRNRMTVQELADQLFPYLTMVEGLKLA--AQTFNKDVK 554
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
46-496 |
2.16e-68 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 226.20 E-value: 2.16e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 46 VIGSGPGGYVAAIKAAQLGFKAVCVEKNETL-GGTCLNVGCIPSKALLNNSHYYHlahgkDFASrgiemsevrlnldkMM 124
Cdd:NF040477 8 IIGFGKAGKTLAATLAKAGWRVAIIEQSAQMyGGTCINIGCIPTKTLVHDAEQHQ-----DFST--------------AM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 125 EQKSNAVKALTGGIAH-LFKQNKVAHVNGYGKITGKNQVTATKADGsTQVIDTKNILIATGSEVT--PFPGITIDEDtVV 201
Cdd:NF040477 69 QRKSSVVGFLRDKNYHnLADLDNVDVINGRAEFIDNHTLRVFQADG-EQELRGEKIFINTGAQSVlpPIPGLTTTPG-VY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 202 SSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGIGiDMEISKNFQRILQKQGFKFKLNTKVTGA 281
Cdd:NF040477 147 DSTGLLNLTQLPARLGILGGGYIGVEFASMFARFGSKVTIFEAAELFLPRE-DRDIAQAIATILQDQGVELILNAQVQRV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 282 TRKPDGkidVFIEAASGgkaeVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPM 361
Cdd:NF040477 226 SSHEGE---VQLETAEG----VLTVDALLVASGRKPATAGLQLQNAGVAVNERGAIVVDKYLRTTADNIWAMGDVTGGLQ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 362 LAHKAEDEGIICVEGMAG-GAVHI-DYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMV 439
Cdd:NF040477 299 FTYISLDDFRIVRDSLLGeGKRSTdDRQNVPYSVFMTPPLSRIGMTEEQARASGADIQVVTLPVAAIPRARVMNDTRGVL 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1246204903 440 KILGQKSTDRVLGAHILGPGAGEMINEAALALEYGASCEDIARVCHAHPTLSEAFRE 496
Cdd:NF040477 379 KAVVDNKTQRILGVSLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSESLND 435
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
41-507 |
2.57e-66 |
|
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: 222.03 E-value: 2.57e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 41 DADVTVIGSGPGGYVAAIKAAQLGFKAVCVEKNET--------LGGTCLNVGCIPSKALLNNSHY-YHLAHGKDFASRGI 111
Cdd:TIGR01438 2 DYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPtplgtrwgIGGTCVNVGCIPKKLMHQAALLgQALKDSRNYGWKVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 112 EmsEVRLNLDKMMEQKSNAVKALTGGIAHLFKQNKVAHVNGYGKITGKNQVTATKADGSTQVIDTKNILIATGsEVTPFP 191
Cdd:TIGR01438 82 E--TVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATG-ERPRYP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 192 GITIDEDTVVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVeflghVGGI---GIDMEISKNFQRILQKQ 268
Cdd:TIGR01438 159 GIPGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVM-----VRSIllrGFDQDCANKVGEHMEEH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 269 GFKFKLNTKVTGATRKPDGKIDVFIEAASGGKAEVitcDVLLVCIGRRPFTKNLGLEELGIELDPR-GRIPVNTRFQTKI 347
Cdd:TIGR01438 234 GVKFKRQFVPIKVEQIEAKVLVEFTDSTNGIEEEY---DTVLLAIGRDACTRKLNLENVGVKINKKtGKIPADEEEQTNV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 348 PNIYAIGDVVAG-PMLAHKAEDEGIICVEGMAGGAVHI-DYNCVPSVIYTHPEVAWVGKSEEQ----LKEEGIEYKVGKF 421
Cdd:TIGR01438 311 PYIYAVGDILEDkPELTPVAIQAGRLLAQRLFKGSTVIcDYENVPTTVFTPLEYGACGLSEEKavekFGEENVEVFHSYF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 422 -PFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMINEAALALEYGASCEDIARVCHAHPTLSEAFREANLA 500
Cdd:TIGR01438 391 wPLEWTIPSRDNHNKCYAKLVCNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTLSVT 470
|
....*..
gi 1246204903 501 ASFGKSI 507
Cdd:TIGR01438 471 KRSGQDI 477
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
43-494 |
3.34e-66 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 220.39 E-value: 3.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 43 DVTVIGSGPGGYVAAIKAAQLGFKAVCVEKNETL-GGTCLNVGCIPSKALlnnshyyhlahgkdfasrgIEMSEVRLNLD 121
Cdd:PRK07251 5 DLIVIGFGKAGKTLAAKLASAGKKVALVEESKAMyGGTCINIGCIPTKTL-------------------LVAAEKNLSFE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 122 KMMEQKSNAVKALTGGIAHLFKQNKVAHVNGYGKITGkNQVTATKADGSTQVIDTKNILIATG--SEVTPFPGITiDEDT 199
Cdd:PRK07251 66 QVMATKNTVTSRLRGKNYAMLAGSGVDLYDAEAHFVS-NKVIEVQAGDEKIELTAETIVINTGavSNVLPIPGLA-DSKH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 200 VVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHVggigiDMEISKNFQRILQKQGFKFKLN 275
Cdd:PRK07251 144 VYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDaastILPRE-----EPSVAALAKQYMEEDGITFLLN 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 276 TKVTGATRKPDgkiDVFIEAasggKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGD 355
Cdd:PRK07251 219 AHTTEVKNDGD---QVLVVT----EDETYRFDALLYATGRKPNTEPLGLENTDIELTERGAIKVDDYCQTSVPGVFAVGD 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 356 VVAGPMLAHKAEDEGIICVEGMAGGA--VHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNA 433
Cdd:PRK07251 292 VNGGPQFTYISLDDFRIVFGYLTGDGsyTLEDRGNVPTTMFITPPLSQVGLTEKEAKEAGLPYAVKELLVAAMPRAHVNN 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246204903 434 DTDGMVKILGQKSTDRVLGAHILGPGAGEMINEAALALEYGASCEDIARVCHAHPTLSEAF 494
Cdd:PRK07251 372 DLRGAFKVVVNTETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAENL 432
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
43-494 |
7.28e-65 |
|
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important reductant, e.g., for maintaining the cellular thiol/disulfide status and for protecting against reactive oxygen species such as hydrogen peroxide. Glutathione-disulfide reductase regenerates reduced glutathione from oxidized glutathione (glutathione disulfide) + NADPH. This model represents one of two closely related subfamilies of glutathione-disulfide reductase. Both are closely related to trypanothione reductase, and separate models are built so each of the three can describe proteins with conserved function. This model describes glutathione-disulfide reductases of animals, yeast, and a number of animal-resident bacteria. [Energy metabolism, Electron transport]
Pssm-ID: 273614 [Multi-domain] Cd Length: 450 Bit Score: 217.02 E-value: 7.28e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 43 DVTVIGSGPGGYVAAIKAAQLGFKAVCVEKNEtLGGTCLNVGCIPSKALLNNSHYYHLAHgkDFASRGIEMS-EVRLNLD 121
Cdd:TIGR01421 4 DYLVIGGGSGGIASARRAAEHGAKALLVEAKK-LGGTCVNVGCVPKKVMWYASDLAERMH--DAADYGFYQNdENTFNWP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 122 KMMEQKSNAVKALTGGIAHLFKQNKVAHVNGYGKITGKNQVTATKADgstqvIDTKNILIATGSEVTpFPGITIDEDTVV 201
Cdd:TIGR01421 81 ELKEKRDAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVNGRD-----YTAPHILIATGGKPS-FPENIPGAELGT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 202 SSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADvTAVEFLGHVGGIGIDMEISKNFQRILQKQGFKFKLNTKVTGA 281
Cdd:TIGR01421 155 DSDGFFALEELPKRVVIVGAGYIAVELAGVLHGLGSE-THLVIRHERVLRSFDSMISETITEEYEKEGINVHKLSKPVKV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 282 TRKPDGKIDVFIEAASggkaEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPM 361
Cdd:TIGR01421 234 EKTVEGKLVIHFEDGK----SIDDVDELIWAIGRKPNTKGLGLENVGIKLNEKGQIIVDEYQNTNVPGIYALGDVVGKVE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 362 LAHKAEDEGIICVEGMAGGA--VHIDYNCVPSVIYTHPEVAWVGKSEEQ-LKEEGIE-YKVGKFPFAANSRAKTNADTDG 437
Cdd:TIGR01421 310 LTPVAIAAGRKLSERLFNGKtdDKLDYNNVPTVVFSHPPIGTIGLTEKEaIEKYGKEnIKVYNSSFTPMYYAMTSEKQKC 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1246204903 438 MVKILGQKSTDRVLGAHILGPGAGEMINEAALALEYGASCEDIARVCHAHPTLSEAF 494
Cdd:TIGR01421 390 RMKLVCAGKEEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEEL 446
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
41-494 |
4.84e-63 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 213.52 E-value: 4.84e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 41 DADVTVIGSGPGGYVAAIKAAQLGFK-AVC--------VEKNETLGGTCLNVGCIPSKALLNNSHYYhlAHGKDFASRGI 111
Cdd:PLN02507 25 DFDLFVIGAGSGGVRAARFSANFGAKvGICelpfhpisSESIGGVGGTCVIRGCVPKKILVYGATFG--GEFEDAKNYGW 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 112 EMSE-VRLNLDKMMEQKSNAVKALTGGIAHLFKQNKVAHVNGYGKITGKNQVTATKADGSTQVIDTKNILIATGSEVTP- 189
Cdd:PLN02507 103 EINEkVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRYTAKHILIATGSRAQRp 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 190 -FPG----ITIDEdtvvsstgALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVeFLGHVGGIGIDMEISKNFQRI 264
Cdd:PLN02507 183 nIPGkelaITSDE--------ALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLF-FRKELPLRGFDDEMRAVVARN 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 265 LQKQGFKFKLNTKVTGATRKPDGkIDVFIEaasggKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQ 344
Cdd:PLN02507 254 LEGRGINLHPRTNLTQLTKTEGG-IKVITD-----HGEEFVADVVLFATGRAPNTKRLNLEAVGVELDKAGAVKVDEYSR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 345 TKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGG-AVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEG---IEYKVGK 420
Cdd:PLN02507 328 TNIPSIWAIGDVTNRINLTPVALMEGTCFAKTVFGGqPTKPDYENVACAVFCIPPLSVVGLSEEEAVEQAkgdILVFTSS 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246204903 421 FPFAANSRAKTNADTdgMVKILGQKSTDRVLGAHILGPGAGEMINEAALALEYGASCEDIARVCHAHPTLSEAF 494
Cdd:PLN02507 408 FNPMKNTISGRQEKT--VMKLIVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEF 479
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
44-497 |
2.98e-58 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 200.09 E-value: 2.98e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 44 VTVIGSGPGGYVAAIKAAQLGFKAVCVEkNETLGGTCLNVGCIPSKALLNNSHYY-HLAHGKDFASRGIEMSEVRLNLDK 122
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIE-RDGLGGAAVLTDCVPSKTLIATAEVRtELRRAAELGIRFIDDGEARVDLPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 123 MmeqksNA-VKALT----GGIAHLFKQNKVAHVNGYGKIT----GKNQVTATKADGSTQVIDTKNILIATGSevTP--FP 191
Cdd:PRK07845 83 V-----NArVKALAaaqsADIRARLEREGVRVIAGRGRLIdpglGPHRVKVTTADGGEETLDADVVLIATGA--SPriLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 192 GITIDEDTVVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGiGIDMEISKNFQRILQKQGFK 271
Cdd:PRK07845 156 TAEPDGERILTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLP-GEDADAAEVLEEVFARRGMT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 272 FKLNTKVTGATRKPDGkidVFIEAASGGKAEVITCdvlLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIY 351
Cdd:PRK07845 235 VLKRSRAESVERTGDG---VVVTLTDGRTVEGSHA---LMAVGSVPNTAGLGLEEAGVELTPSGHITVDRVSRTSVPGIY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 352 AIGDVVAGPMLAHKAEDEGIICVEGMAGGAVH-IDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAK 430
Cdd:PRK07845 309 AAGDCTGVLPLASVAAMQGRIAMYHALGEAVSpLRLKTVASNVFTRPEIATVGVSQAAIDSGEVPARTVMLPLATNPRAK 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246204903 431 TNADTDGMVKILGQKSTDRVLGAHILGPGAGEMINEAALALEYGASCEDIARVCHAHPTLSEAFREA 497
Cdd:PRK07845 389 MSGLRDGFVKLFCRPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYPSLSGSITEA 455
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
46-496 |
1.37e-56 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 194.85 E-value: 1.37e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 46 VIGSGPGGYVAAIKAAQLGFKAVCVEK-NETLGGTCLNVGCIPSKALLNNSHyyhlAHGkDFAsrgiemsevrlnldKMM 124
Cdd:PRK08010 8 IIGFGKAGKTLAVTLAKAGWRVALIEQsNAMYGGTCINIGCIPTKTLVHDAQ----QHT-DFV--------------RAI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 125 EQKSNAVKALTGGIAH-LFKQNKVAHVNGYGKITGKNQVTATKADGStQVIDTKNILIATGSE--VTPFPGITIDEDtVV 201
Cdd:PRK08010 69 QRKNEVVNFLRNKNFHnLADMPNIDVIDGQAEFINNHSLRVHRPEGN-LEIHGEKIFINTGAQtvVPPIPGITTTPG-VY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 202 SSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHVggigiDMEISKNFQRILQKQGFKFKLNTK 277
Cdd:PRK08010 147 DSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEaaslFLPRE-----DRDIADNIATILRDQGVDIILNAH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 278 VTGATRKpDGKIDVFIEAASggkaevITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVV 357
Cdd:PRK08010 222 VERISHH-ENQVQVHSEHAQ------LAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKYLHTTADNIWAMGDVT 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 358 AGPMLAHKAEDEGIICVEGMAGGAVHI--DYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADT 435
Cdd:PRK08010 295 GGLQFTYISLDDYRIVRDELLGEGKRStdDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDT 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246204903 436 DGMVKILGQKSTDRVLGAHILGPGAGEMINEAALALEYGASCEDIARVCHAHPTLSEAFRE 496
Cdd:PRK08010 375 RGVLKAIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLND 435
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
43-503 |
1.95e-54 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 189.39 E-value: 1.95e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 43 DVTVIGSGPGGYVAAIKAAQLgfKAVCVEKNeTLGGTCLNVGCIPSKALLnnsHYYHLAHGKDFASR-GIEMSEVRLNLD 121
Cdd:PRK07846 3 DLIIIGTGSGNSILDERFADK--RIAIVEKG-TFGGTCLNVGCIPTKMFV---YAADVARTIREAARlGVDAELDGVRWP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 122 KMMEQKSNAVKALTGGIAHlFKQNKVAHV---NGYGKITGknQVTATKADGStqVIDTKNILIATGSEVTPFPGITIDED 198
Cdd:PRK07846 77 DIVSRVFGRIDPIAAGGEE-YRGRDTPNIdvyRGHARFIG--PKTLRTGDGE--EITADQVVIAAGSRPVIPPVIADSGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 199 TVVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHvggigIDMEISKNFQRILQKQgFKFKL 274
Cdd:PRK07846 152 RYHTSDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNrsgrLLRH-----LDDDISERFTELASKR-WDVRL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 275 NTKVTGATRKPDGkidVFIEAASGgkaEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIG 354
Cdd:PRK07846 226 GRNVVGVSQDGSG---VTLRLDDG---STVEADVLLVATGRVPNGDLLDAAAAGVDVDEDGRVVVDEYQRTSAEGVFALG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 355 DVVAGPMLAHKAEDEGIICVEGMAGGA--VHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTN 432
Cdd:PRK07846 300 DVSSPYQLKHVANHEARVVQHNLLHPDdlIASDHRFVPAAVFTHPQIASVGLTENEARAAGLDITVKVQNYGDVAYGWAM 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246204903 433 ADTDGMVKILGQKSTDRVLGAHILGPGAGEMINEAALALEYGASCEDIARVCH-AHPTLSEAFREANLAASF 503
Cdd:PRK07846 380 EDTTGFVKLIADRDTGRLLGAHIIGPQASTLIQPLIQAMSFGLDAREMARGQYwIHPALPEVVENALLGLDL 451
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
389-497 |
2.05e-54 |
|
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: 178.13 E-value: 2.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 389 VPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMINEAA 468
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGEVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQEAA 80
|
90 100
....*....|....*....|....*....
gi 1246204903 469 LALEYGASCEDIARVCHAHPTLSEAFREA 497
Cdd:pfam02852 81 LAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
43-492 |
3.54e-54 |
|
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: 189.80 E-value: 3.54e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 43 DVTVIGSGPGGYVAAIKAAQLGFKAVCVEKNET---------LGGTCLNVGCIPSKALLNNSHYyhLAHGKDFASRGIEM 113
Cdd:TIGR01423 5 DLVVIGAGSGGLEAGWNAATLYKKRVAVVDVQThhgppfyaaLGGTCVNVGCVPKKLMVTGAQY--MDTLRESAGFGWEF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 114 --SEVRLNLDKMMEQKSNAVKALTGGIAHLFKQNK-VAHVNGYGKITGKNQVTATK-ADGSTQV---IDTKNILIATGS- 185
Cdd:TIGR01423 83 drSSVKANWKALIAAKNKAVLDINKSYEGMFADTEgLTFFLGWGALEDKNVVLVREsADPKSAVkerLQAEHILLATGSw 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 186 -EVTPFPGItideDTVVSSTGALSLKKVPEKMVVIGAGVIGVELGSV---WQRLGADVTaVEFLGHVGGIGIDMEISKNF 261
Cdd:TIGR01423 163 pQMLGIPGI----EHCISSNEAFYLDEPPRRVLTVGGGFISVEFAGIfnaYKPRGGKVT-LCYRNNMILRGFDSTLRKEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 262 QRILQKQGFKFKLNTKVTGATRKPDGKIDVFIEaaSGGKAEVitcDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNT 341
Cdd:TIGR01423 238 TKQLRANGINIMTNENPAKVTLNADGSKHVTFE--SGKTLDV---DVVMMAIGRVPRTQTLQLDKVGVELTKKGAIQVDE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 342 RFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVH-IDYNCVPSVIYTHPEVAWVGKSEEQL--KEEGIEYKV 418
Cdd:TIGR01423 313 FSRTNVPNIYAIGDVTDRVMLTPVAINEGAAFVDTVFGNKPRkTDHTRVASAVFSIPPIGTCGLVEEDAakKFEKVAVYE 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246204903 419 GKF-PFAANSRAKTNADTdgMVKILGQKSTDRVLGAHILGPGAGEMINEAALALEYGASCEDIARVCHAHPTLSE 492
Cdd:TIGR01423 393 SSFtPLMHNISGSKYKKF--VAKIVTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAE 465
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
41-506 |
5.44e-51 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 181.17 E-value: 5.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 41 DADVTVIGSGPGGYVAAIKAAQLGFKAVCVE--KNET------LGGTCLNVGCIPSKALLNNSHYYHLAHgKDFASRGIE 112
Cdd:PTZ00052 5 MYDLVVIGGGSGGMAAAKEAAAHGKKVALFDyvKPSTqgtkwgLGGTCVNVGCVPKKLMHYAANIGSIFH-HDSQMYGWK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 113 MSEVrLNLDKMMEQKSNAVKALTGGIAHLFKQNKVAHVNGYGKITGKNQVtATKADGSTQVIDTKNILIATGSEvtpfPG 192
Cdd:PTZ00052 84 TSSS-FNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTV-SYGDNSQEETITAKYILIATGGR----PS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 193 ITID----EDTVVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVeflghVGGI---GIDMEISKNFQRIL 265
Cdd:PTZ00052 158 IPEDvpgaKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVA-----VRSIplrGFDRQCSEKVVEYM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 266 QKQGFKFKlNTKVTGATRKPDGKIDVFIeaaSGGKAEVItcDVLLVCIGRRPFTKNLGLEELGIELDPRGRIpVNTRFQT 345
Cdd:PTZ00052 233 KEQGTLFL-EGVVPINIEKMDDKIKVLF---SDGTTELF--DTVLYATGRKPDIKGLNLNAIGVHVNKSNKI-IAPNDCT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 346 KIPNIYAIGDVVAG-PMLAHKAEDEGIICVEGMAGGAVHI-DYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPF 423
Cdd:PTZ00052 306 NIPNIFAVGDVVEGrPELTPVAIKAGILLARRLFKQSNEFiDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 424 AANS------------RAKTNA-DTD----GMVKILGQKSTD-RVLGAHILGPGAGEMINEAALALEYGASCEDIARVCH 485
Cdd:PTZ00052 386 EFNTleiaavhrekheRARKDEyDFDvssnCLAKLVCVKSEDnKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIG 465
|
490 500
....*....|....*....|.
gi 1246204903 486 AHPTLSEAFREANLAASFGKS 506
Cdd:PTZ00052 466 IHPTDAEVFMNLSVTRRSGES 486
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
43-500 |
6.20e-47 |
|
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: 169.17 E-value: 6.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 43 DVTVIGSGPGGyvaAIKAAQLGFKAVCVEKNETLGGTCLNVGCIPSKALLnnsHYYHLAHGKDFASR-GIEMSEVRLNLD 121
Cdd:TIGR03452 4 DLIIIGTGSGN---SIPDPRFADKRIAIVEKGTFGGTCLNVGCIPTKMFV---YAAEVAQSIGESARlGIDAEIDSVRWP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 122 KMMEQK-SNAVKALTGGIAHLFKQNKVAHVNGY-GKITGKNQVTATKADGSTqvIDTKNILIATGSEVTPFPGITIDEDT 199
Cdd:TIGR03452 78 DIVSRVfGDRIDPIAAGGEDYRRGDETPNIDVYdGHARFVGPRTLRTGDGEE--ITGDQIVIAAGSRPYIPPAIADSGVR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 200 VVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAV----EFLGHvggigIDMEISKNFQRILQKQgFKFKLN 275
Cdd:TIGR03452 156 YHTNEDIMRLPELPESLVIVGGGYIAAEFAHVFSALGTRVTIVnrstKLLRH-----LDEDISDRFTEIAKKK-WDIRLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 276 TKVTGATRKPDGkidVFIEAASGgkaEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGD 355
Cdd:TIGR03452 230 RNVTAVEQDGDG---VTLTLDDG---STVTADVLLVATGRVPNGDLLDAEAAGVEVDEDGRIKVDEYGRTSARGVWALGD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 356 VVAGPMLAHKAEDEGIICVEGMA--GGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEG--IEYKVGKFPFAANSRAKt 431
Cdd:TIGR03452 304 VSSPYQLKHVANAEARVVKHNLLhpNDLRKMPHDFVPSAVFTHPQIATVGLTEQEAREAGhdITVKIQNYGDVAYGWAM- 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 432 nADTDGMVKILGQKSTDRVLGAHILGPGAGEMINEAALALEYGASCEDIARVCH-AHPTLSEAFREANLA 500
Cdd:TIGR03452 383 -EDTTGFCKLIADRDTGKLLGAHIIGPQASSLIQPLITAMAFGLDAREMARKQYwIHPALPEVVENALLG 451
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
41-494 |
8.94e-47 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 171.21 E-value: 8.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 41 DADVTVIGSGPGGYVAAIKAAQLGFK-AVC------VEKNET--LGGTCLNVGCIPSKALLNNSHYYHlahgkDF-ASRG 110
Cdd:PLN02546 79 DFDLFTIGAGSGGVRASRFASNFGASaAVCelpfatISSDTLggVGGTCVLRGCVPKKLLVYASKYSH-----EFeESRG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 111 IEM---SEVRLNLDKMMEQKSNAVKALTGGIAHLFKQNKVAHVNGYGKITGKNQVTAtkaDGstQVIDTKNILIATGSEv 187
Cdd:PLN02546 154 FGWkyeTEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDV---DG--KLYTARNILIAVGGR- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 188 tPF----PGItideDTVVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAveFLGHVGGI-GIDMEISKNFQ 262
Cdd:PLN02546 228 -PFipdiPGI----EHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHV--FIRQKKVLrGFDEEVRDFVA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 263 RILQKQGFKFKLNTKVTGATRKPDGKIDVfieaaSGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTR 342
Cdd:PLN02546 301 EQMSLRGIEFHTEESPQAIIKSADGSLSL-----KTNKGTVEGFSHVMFATGRKPNTKNLGLEEVGVKMDKNGAIEVDEY 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 343 FQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGG-AVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVgkf 421
Cdd:PLN02546 376 SRTSVPSIWAVGDVTDRINLTPVALMEGGALAKTLFGNePTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYGDVDV--- 452
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246204903 422 pFAANSRAkTNADTDGM-----VKILGQKSTDRVLGAHILGPGAGEMINEAALALEYGASCEDIARVCHAHPTLSEAF 494
Cdd:PLN02546 453 -FTANFRP-LKATLSGLpdrvfMKLIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEEF 528
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
21-494 |
5.25e-44 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 163.63 E-value: 5.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 21 SHGLQGVSAvPLRTYADQPIDADVTVIGSGPGGYVAAIKAAQLGFKAVCVEKnETLGGTCLNVGCIPSKALLNNSHYYHL 100
Cdd:PTZ00058 29 YHNLEASSA-PTHLKKKPRMVYDLIVIGGGSGGMAAARRAARNKAKVALVEK-DYLGGTCVNVGCVPKKIMFNAASIHDI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 101 AHgkDFASRGIEMSEVrLNLDKMMEQKSNAVKALTGGIAHLFKQNKVAHVNGYGKITGKNQVTATK-------------- 166
Cdd:PTZ00058 107 LE--NSRHYGFDTQFS-FNLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLIKKvsqvdgeadesddd 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 167 ----------ADGSTQVIDTKNILIATGSEvTPFPGITIDEDTvVSSTGALSLKKvPEKMVVIGAGVIGVELGSVWQRLG 236
Cdd:PTZ00058 184 evtivsagvsQLDDGQVIEGKNILIAVGNK-PIFPDVKGKEFT-ISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 237 ADvTAVEFLGHVGGIGIDMEISKNFQRILQKQGFKFKLNTKVTGATRkpDGKIDVFIEAASGGKAEVITCdvLLVCIGRR 316
Cdd:PTZ00058 261 AE-SYIFARGNRLLRKFDETIINELENDMKKNNINIITHANVEEIEK--VKEKNLTIYLSDGRKYEHFDY--VIYCVGRS 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 317 PFTKNLGLEELGIeLDPRGRIPVNTRFQTKIPNIYAIGDVVAGP---------MLAHKAEDEGIICVEGMAGGAVH---- 383
Cdd:PTZ00058 336 PNTEDLNLKALNI-KTPKGYIKVDDNQRTSVKHIYAVGDCCMVKknqeiedlnLLKLYNEEPYLKKKENTSGESYYnvql 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 384 ----------------------IDYNCVPSVIYTHPEVAWVGKSEEQL-----KEEGIEYK-------VGKFPFAANSRA 429
Cdd:PTZ00058 415 tpvainagrlladrlfgpfsrtTNYKLIPSVIFSHPPIGTIGLSEQEAidiygKENVKIYEsrftnlfFSVYDMDPAQKE 494
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246204903 430 KTnadtdgMVKILGQKSTDRVLGAHILGPGAGEMINEAALALEYGASCEDIARVCHAHPTLSEAF 494
Cdd:PTZ00058 495 KT------YLKLVCVGKEELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIHPTAAEEF 553
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
159-393 |
2.37e-29 |
|
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: 117.60 E-value: 2.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 159 KNQVTATKADGSTQVIDTKN--------ILIATGSE--VTPFPGITIDE-DTVVSSTGALSLKKV-----PEKMVVIGAG 222
Cdd:COG0446 54 RTGTEVTAIDPEAKTVTLRDgetlsydkLVLATGARprPPPIPGLDLPGvFTLRTLDDADALREAlkefkGKRAVVIGGG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 223 VIGVELGSVWQRLGADVTAVEFLGHVGGiGIDMEISKNFQRILQKQGFKFKLNTKVTGAtrKPDGKIDVFIEaaSGgkaE 302
Cdd:COG0446 134 PIGLELAEALRKRGLKVTLVERAPRLLG-VLDPEMAALLEEELREHGVELRLGETVVAI--DGDDKVAVTLT--DG---E 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 303 VITCDVLLVCIGRRPftkNLGL-EELGIELDPRGRIPVNTRFQTKIPNIYAIGDVV----------AGPMLAHKAEDEGI 371
Cdd:COG0446 206 EIPADLVVVAPGVRP---NTELaKDAGLALGERGWIKVDETLQTSDPDVYAAGDCAevphpvtgktVYIPLASAANKQGR 282
|
250 260
....*....|....*....|..
gi 1246204903 372 ICVEGMAGGAvhIDYNCVPSVI 393
Cdd:COG0446 283 VAAENILGGP--APFPGLGTFI 302
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
43-361 |
6.34e-24 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 101.74 E-value: 6.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 43 DVTVIGSGPGGYVAAIKAAQLGFKAVCVEKNEtLGGTCLNVGCIpskallNNshYYHLAHGKdfasRGIEMsevrlnLDK 122
Cdd:COG0492 2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEGGE-PGGQLATTKEI------EN--YPGFPEGI----SGPEL------AER 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 123 MMEQ-KSNAVKALTGGIAHLFKQNKVAHVNGygkitgknqvtatkadGSTQVIDTKNILIATGSEVT--PFPGITIDEDT 199
Cdd:COG0492 63 LREQaERFGAEILLEEVTSVDKDDGPFRVTT----------------DDGTEYEAKAVIIATGAGPRklGLPGEEEFEGR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 200 VVSSTGALSLKKVP-EKMVVIGAGVIGVELGSVWQRLGADVTAVeflgHVGGigiDMEISKNFQ-RILQKQGFKFKLNTK 277
Cdd:COG0492 127 GVSYCATCDGFFFRgKDVVVVGGGDSALEEALYLTKFASKVTLI----HRRD---ELRASKILVeRLRANPKIEVLWNTE 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 278 VTGAtrKPDGKID-VFIEAASGGKAEVITCDVLLVCIGRRPftkNLGL-EELGIELDPRGRIPVNTRFQTKIPNIYAIGD 355
Cdd:COG0492 200 VTEI--EGDGRVEgVTLKNVKTGEEKELEVDGVFVAIGLKP---NTELlKGLGLELDEDGYIVVDEDMETSVPGVFAAGD 274
|
....*.
gi 1246204903 356 VVAGPM 361
Cdd:COG0492 275 VRDYKY 280
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
180-382 |
8.30e-22 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 97.52 E-value: 8.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 180 LIATGSE--VTPFPGITID--------EDTVVSSTGALSLKKVpekmVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVG 249
Cdd:COG1251 103 VLATGSRprVPPIPGADLPgvftlrtlDDADALRAALAPGKRV----VVIGGGLIGLEAAAALRKRGLEVTVVERAPRLL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 250 GIGIDMEISKNFQRILQKQGFKFKLNTKVTGATRkpDGKIDVfIEAASGgkaEVITCDVLLVCIGRRPftkNLGL-EELG 328
Cdd:COG1251 179 PRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEG--DDRVTG-VRLADG---EELPADLVVVAIGVRP---NTELaRAAG 249
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246204903 329 IELDpRGrIPVNTRFQTKIPNIYAIGDVVA-------GPMLAH--KAEDEGIICVEGMAGGAV 382
Cdd:COG1251 250 LAVD-RG-IVVDDYLRTSDPDIYAAGDCAEhpgpvygRRVLELvaPAYEQARVAAANLAGGPA 310
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
155-488 |
3.29e-17 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 83.94 E-value: 3.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 155 KITGKNQVTATKADGSTQVIDTK--NILIATG--SEVTPFPGITIDE-DTVVSSTGALSLKKVPEK-----MVVIGAGVI 224
Cdd:PRK09564 81 KVDAKNKTITVKNLKTGSIFNDTydKLMIATGarPIIPPIKNINLENvYTLKSMEDGLALKELLKDeeiknIVIIGAGFI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 225 GVELGSVWQRLGADVTAVEFLGHVGGIGIDMEISKNFQRILQKQGFKFKLNTKVTGAtrkpDGKIDVFIEAASGGKAEVi 304
Cdd:PRK09564 161 GLEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSL----IGEDKVEGVVTDKGEYEA- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 305 tcDVLLVCIGRRPFTKnlGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGD-------VVAGPM---LAHKAEDEGIICV 374
Cdd:PRK09564 236 --DVVIVATGVKPNTE--FLEDTGLKTLKNGAIIVDEYGETSIENIYAAGDcatiyniVSNKNVyvpLATTANKLGRMVG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 375 EGMAGGAVH----IDYNCVPSVIYthpEVAWVGKSEEQLKEEGIEYKVgKFPFAANSRAKTNADTDGMVKILGQKSTDRV 450
Cdd:PRK09564 312 ENLAGRHVSfkgtLGSACIKVLDL---EAARTGLTEEEAKKLGIDYKT-VFIKDKNHTNYYPGQEDLYVKLIYEADTKVI 387
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1246204903 451 LGAHILGP-GAGEMINEAALALEYGASCEDIARV--CHAHP 488
Cdd:PRK09564 388 LGGQIIGKkGAVLRIDALAVAIYAKLTTQELGMMdfCYAPP 428
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
42-375 |
8.85e-16 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 79.02 E-value: 8.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 42 ADVTVIGSGPGGYVAAIKAAQLGFKAVCVekneTLggtclnvgcIpSKallNNSHYY-HLAHGkdFASRGIEMSEVRLNL 120
Cdd:COG1252 2 KRIVIVGGGFAGLEAARRLRKKLGGDAEV----TL---------I-DP---NPYHLFqPLLPE--VAAGTLSPDDIAIPL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 121 DKMMEQKsnavkaltgGIAhlFKQNKVAHVNgygkiTGKNQVTAtkADGSTQVIDTknILIATGSeVTPFPGIT-IDEDt 199
Cdd:COG1252 63 RELLRRA---------GVR--FIQGEVTGID-----PEARTVTL--ADGRTLSYDY--LVIATGS-VTNFFGIPgLAEH- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 200 vvsstgALSLKKVPE---------------------KMVVIGAGVIGVEL-GSVWQRLG------------ADVTAVEFL 245
Cdd:COG1252 121 ------ALPLKTLEDalalrerllaaferaerrrllTIVVVGGGPTGVELaGELAELLRkllrypgidpdkVRITLVEAG 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 246 GHVGGiGIDMEISKNFQRILQKQGFKFKLNTKVTGATrkPDGkidvfIEAASGgkaEVITCDVLLVCIGRR--PFTKNLG 323
Cdd:COG1252 195 PRILP-GLGEKLSEAAEKELEKRGVEVHTGTRVTEVD--ADG-----VTLEDG---EEIPADTVIWAAGVKapPLLADLG 263
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246204903 324 LEelgieLDPRGRIPVNTRFQTK-IPNIYAIGDVVAG--------PMLAHKAEDEGIICVE 375
Cdd:COG1252 264 LP-----TDRRGRVLVDPTLQVPgHPNVFAIGDCAAVpdpdgkpvPKTAQAAVQQAKVLAK 319
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
215-292 |
1.13e-15 |
|
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: 71.85 E-value: 1.13e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246204903 215 KMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGiGIDMEISKNFQRILQKQGFKFKLNTKVTGATRKPDGKIDVF 292
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLP-GFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVL 77
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
214-357 |
4.29e-14 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 74.05 E-value: 4.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 214 EKMVVIGAGVIGVE-LGSVWQRlGADVTAVEFLGHVGGIgIDMEISKNFQRILQKQGFKFKLNTKVTgatrKPDGKIDVF 292
Cdd:PRK13512 149 DKALVVGAGYISLEvLENLYER-GLHPTLIHRSDKINKL-MDADMNQPILDELDKREIPYRLNEEID----AINGNEVTF 222
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246204903 293 ieaaSGGKAEviTCDVLLVCIGRRPFTKNLglEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVV 357
Cdd:PRK13512 223 ----KSGKVE--HYDMIIEGVGTHPNSKFI--ESSNIKLDDKGFIPVNDKFETNVPNIYAIGDII 279
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
166-355 |
2.10e-13 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 71.49 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 166 KADGstQVIDTKNILIATGSE--VTPFPGitiDEDTVV--------SSTGALSLKKvpeKMVVIGAGVIGVELGSVWQRL 235
Cdd:PRK04965 92 KSQG--NQWQYDKLVLATGASafVPPIPG---RELMLTlnsqqeyrAAETQLRDAQ---RVLVVGGGLIGTELAMDLCRA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 236 GADVTAVEFLGHVGGIGIDMEISKNFQRILQKQGFKFKLNTKVTGATRKPDGkidVFIEAASGgkaEVITCDVLLVCIGR 315
Cdd:PRK04965 164 GKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSG---IRATLDSG---RSIEVDAVIAAAGL 237
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1246204903 316 RPftkNLGL-EELGIELDpRGrIPVNTRFQTKIPNIYAIGD 355
Cdd:PRK04965 238 RP---NTALaRRAGLAVN-RG-IVVDSYLQTSAPDIYALGD 273
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
298-370 |
9.50e-12 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 66.55 E-value: 9.50e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246204903 298 GGKAEVITCDVLLVCIGRRPfTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPMLAHKAEDEG 370
Cdd:PRK12770 267 PGSEFVLEADTVVFAIGEIP-TPPFAKECLGIELNRKGEIVVDEKHMTSREGVFAAGDVVTGPSKIGKAIKSG 338
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
155-358 |
4.95e-11 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 65.23 E-value: 4.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 155 KITGKNQVTATKAdGSTQVIDTknILIATGSE--VTPFPGI---------TIDE-DTVvsstgaLSLKKVPEKMVVIGAG 222
Cdd:TIGR02374 79 QIDTDQKQVITDA-GRTLSYDK--LILATGSYpfILPIPGAdkkgvyvfrTIEDlDAI------MAMAQRFKKAAVIGGG 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 223 VIGVELGSVWQRLGADVTAVEFLGHVGGIGIDMEISKNFQRILQKQGFKFKLNT---KVTGATRKPDgkidvfIEAASGg 299
Cdd:TIGR02374 150 LLGLEAAVGLQNLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEKdtvEIVGATKADR------IRFKDG- 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246204903 300 kaEVITCDVLLVCIGRRPFTknlgleELGIE--LDPRGRIPVNTRFQTKIPNIYAIGDVVA 358
Cdd:TIGR02374 223 --SSLEADLIVMAAGIRPND------ELAVSagIKVNRGIIVNDSMQTSDPDIYAVGECAE 275
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
299-385 |
1.09e-10 |
|
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 440259 [Multi-domain] Cd Length: 434 Bit Score: 63.62 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 299 GKAEVITCDVLLVCIGRRPFTKNLgLEELGIELDPRGRIPVNTR-FQTKIPNIYAIGDVVAGPMLAhkaedegiicVEGM 377
Cdd:COG0493 353 GSEFTLPADLVILAIGQTPDPSGL-EEELGLELDKRGTIVVDEEtYQTSLPGVFAGGDAVRGPSLV----------VWAI 421
|
90
....*....|.
gi 1246204903 378 AGG---AVHID 385
Cdd:COG0493 422 AEGrkaARAID 432
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
179-356 |
1.25e-09 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 59.94 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 179 ILIATGSEVTPFPGI-TIDED--TVVSSTGALSLKKV--PEKMVVI-GAGVIGVELGSVWQRLGADVTAVEFLGHVGGIG 252
Cdd:PRK09754 104 LFIATGAAARPLPLLdALGERcfTLRHAGDAARLREVlqPERSVVIvGAGTIGLELAASATQRRCKVTVIELAATVMGRN 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 253 IDMEISKNFQRILQKQGFKFKLNTKVTGATrkpDGKiDVFIEAASGgkaEVITCDVLLVCIGRRpFTKNLGLEElgiELD 332
Cdd:PRK09754 184 APPPVQRYLLQRHQQAGVRILLNNAIEHVV---DGE-KVELTLQSG---ETLQADVVIYGIGIS-ANDQLAREA---NLD 252
|
170 180
....*....|....*....|....
gi 1246204903 333 PRGRIPVNTRFQTKIPNIYAIGDV 356
Cdd:PRK09754 253 TANGIVIDEACRTCDPAIFAGGDV 276
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
275-377 |
1.13e-07 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 54.01 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 275 NTKVTG----ATRKPDGKIDVfIEaasgGKAEVITCDVLLVCIGRRPFTKNLgLEELGIELDPRGRIPVNTR-FQTKIPN 349
Cdd:PRK12810 359 NGKVTGvkvvRTELGEGDFEP-VE----GSEFVLPADLVLLAMGFTGPEAGL-LAQFGVELDERGRVAAPDNaYQTSNPK 432
|
90 100
....*....|....*....|....*...
gi 1246204903 350 IYAIGDVVAGPMLAHKAEDEGIICVEGM 377
Cdd:PRK12810 433 VFAAGDMRRGQSLVVWAIAEGRQAARAI 460
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
31-79 |
4.17e-07 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 52.42 E-value: 4.17e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1246204903 31 PLRTYADQPIDADVTVIGSGPGGYVAAIKAAQLGFKAVCVEKNETLGGT 79
Cdd:PRK06134 2 PSAAAYPPDLECDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGGT 50
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
43-78 |
3.02e-06 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 49.85 E-value: 3.02e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1246204903 43 DVTVIGSGPGGYVAAIKAAQLGFKaVCV-EKNETLGG 78
Cdd:COG1233 5 DVVVIGAGIGGLAAAALLARAGYR-VTVlEKNDTPGG 40
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
27-368 |
3.16e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 49.77 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 27 VSAVPLRTY---ADQPI---DADVTVIGSGPGGYVAAIKAAQLGFKAVCVEKNETLGGTcLNVGcIPSkallnnshyYHL 100
Cdd:PRK13984 263 VDNVPVEKYseiLDDEPekkNKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGV-MRYG-IPS---------YRL 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 101 AhgkdfasrgiemsevrlnlDKMMEQKSNAVKALTGGIahlfkqnkvaHVNgygkitgknqvTATKADGSTQVIDTKN-- 178
Cdd:PRK13984 332 P-------------------DEALDKDIAFIEALGVKI----------HLN-----------TRVGKDIPLEELREKHda 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 179 ILIATG---SEVTPFPGItiDEDTVVSSTGALSL-----------KKVPEKMVVIGAGVIGVELGSVWQRLG------AD 238
Cdd:PRK13984 372 VFLSTGftlGRSTRIPGT--DHPDVIQALPLLREirdylrgegpkPKIPRSLVVIGGGNVAMDIARSMARLQkmeygeVN 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 239 VTAV-------EFLGHVGGI------GIDMEISKNFQRIL----QKQGFKFKLNTKVTGATRK--P--DGKIDVFIEAas 297
Cdd:PRK13984 450 VKVTslertfeEMPADMEEIeegleeGVVIYPGWGPMEVViendKVKGVKFKKCVEVFDEEGRfnPkfDESDQIIVEA-- 527
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246204903 298 ggkaevitcDVLLVCIGRRPFTKNLGlEELGIELD-PRGRIPVNTRFQTKIPNIYAIGDVVAGPMLAHKAED 368
Cdd:PRK13984 528 ---------DMVVEAIGQAPDYSYLP-EELKSKLEfVRGRILTNEYGQTSIPWLFAGGDIVHGPDIIHGVAD 589
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
39-184 |
4.85e-06 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 49.09 E-value: 4.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 39 PIDADVTVIGSGPGGYVAAIKAAQLGFKAVCVEKNETLGGtclnvgcipsKAllnnSHYYHLAHGKDFASRGIE--MSEV 116
Cdd:COG1148 138 PVNKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGG----------RA----AQLHKTFPGLDCPQCILEplIAEV 203
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246204903 117 RLNldkmmeqksnavkaltGGIaHLFKQNKVAHVNGYGkitGKNQVTATKADGSTQVIDTKNILIATG 184
Cdd:COG1148 204 EAN----------------PNI-TVYTGAEVEEVSGYV---GNFTVTIKKGPREEIEIEVGAIVLATG 251
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
43-79 |
4.94e-06 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 48.76 E-value: 4.94e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1246204903 43 DVTVIGSGPGGYVAAIKAAQLGFKAVCVEKNETLGGT 79
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGM 37
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
38-79 |
7.27e-06 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 48.54 E-value: 7.27e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1246204903 38 QPIDADVTVIGSGPGGYVAAIKAAQLGFKAVCVEKNETLGGT 79
Cdd:PRK12842 6 NELTCDVLVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGGT 47
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
39-78 |
1.21e-05 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 47.90 E-value: 1.21e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1246204903 39 PIDADVTVIGSGPGGYVAAIKAAQLGFKAVCVEKNETLGG 78
Cdd:PRK12839 6 THTYDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKASTCGG 45
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
43-79 |
1.44e-05 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 47.81 E-value: 1.44e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1246204903 43 DVTVIGSGPGGYVAAIKAAQLGFKAVCVEKNETLGGT 79
Cdd:PRK12843 18 DVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGT 54
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
217-370 |
2.17e-05 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 46.68 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 217 VVIGAGVIGVELGSVWQRLGAD--------------VTAVEFLGHVGGiGIDMEISKNFQRILQKQGFKFKLNTKVTGAT 282
Cdd:PTZ00318 177 VVVGGGPTGVEFAAELADFFRDdvrnlnpelveeckVTVLEAGSEVLG-SFDQALRKYGQRRLRRLGVDIRTKTAVKEVL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 283 RKpdgkiDVFIEaaSGgkaEVITCDVLL--VCIGRRPFTKNLGleelgIELDPRGRIPVNTRFQTK-IPNIYAIGDVVAG 359
Cdd:PTZ00318 256 DK-----EVVLK--DG---EVIPTGLVVwsTGVGPGPLTKQLK-----VDKTSRGRISVDDHLRVKpIPNVFALGDCAAN 320
|
170
....*....|....*.
gi 1246204903 360 -----PMLAHKAEDEG 370
Cdd:PTZ00318 321 eerplPTLAQVASQQG 336
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
40-79 |
2.40e-05 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 46.75 E-value: 2.40e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1246204903 40 IDADVTVIGSGPGGYVAAIKAAQLGFKAVCVEKNETLGGT 79
Cdd:COG1053 2 HEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGGH 41
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
43-92 |
3.06e-05 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 46.39 E-value: 3.06e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1246204903 43 DVTVIGSGPGGYVAAIKAAQLGFK-AVCVEKNETLGgtclNVGCIPSKALL 92
Cdd:pfam01134 1 DVIVIGGGHAGCEAALAAARMGAKvLLITHNTDTIA----ELSCNPSIGGI 47
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
43-79 |
3.14e-05 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 46.13 E-value: 3.14e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1246204903 43 DVTVIGSGPGGYVAAIKAAQLGFKAVCVEKNETLGGT 79
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGA 37
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
43-79 |
4.11e-05 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 46.18 E-value: 4.11e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1246204903 43 DVTVIGSGPGGYVAAIKAAQLGFKAVCVEKNETLGGT 79
Cdd:PRK07843 9 DVVVVGSGAAGMVAALTAAHRGLSTVVVEKAPHYGGS 45
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
217-355 |
4.91e-05 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 46.26 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 217 VVIGAGVIGVELGSVWQRLGADVTAVEF--------LGHVGG---------IGIDMEISKNFQRILQkQGfkfklntkvt 279
Cdd:PRK14989 149 AVVGGGLLGLEAAGALKNLGVETHVIEFapmlmaeqLDQMGGeqlrrkiesMGVRVHTSKNTLEIVQ-EG---------- 217
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246204903 280 gatrKPDGKIDVFieaASGGKAEVitcDVLLVCIGRRPFTKnLGlEELGIELDPRGRIPVNTRFQTKIPNIYAIGD 355
Cdd:PRK14989 218 ----VEARKTMRF---ADGSELEV---DFIVFSTGIRPQDK-LA-TQCGLAVAPRGGIVINDSCQTSDPDIYAIGE 281
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
299-359 |
1.11e-04 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 44.78 E-value: 1.11e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246204903 299 GKAEVITCDVLLVCIGRRPFTKNLGLEElGIELDPRG-RIPVNTRFQTKIPNIYAIGDVVAG 359
Cdd:PRK11749 369 GSEFTLPADLVIKAIGQTPNPLILSTTP-GLELNRWGtIIADDETGRTSLPGVFAGGDIVTG 429
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
43-79 |
1.19e-04 |
|
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];
Pssm-ID: 441675 [Multi-domain] Cd Length: 414 Bit Score: 44.47 E-value: 1.19e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1246204903 43 DVTVIGSGPGGYVAAIKAAQLGFKAVCVEKNETLGGT 79
Cdd:COG2072 8 DVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGT 44
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
46-80 |
1.27e-04 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 40.21 E-value: 1.27e-04
10 20 30
....*....|....*....|....*....|....*
gi 1246204903 46 VIGSGPGGYVAAIKAAQLGFKAVCVEKNETLGGTC 80
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNA 35
|
|
| PRK12835 |
PRK12835 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
43-86 |
2.23e-04 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237221 [Multi-domain] Cd Length: 584 Bit Score: 43.64 E-value: 2.23e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1246204903 43 DVTVIGSGPGGYVAAIKAAQLGFKAVCVEKNETLGG-TCLNVGCI 86
Cdd:PRK12835 13 DVLVVGSGGGGMTAALTAAARGLDTLVVEKSAHFGGsTALSGGGI 57
|
|
| PRK12844 |
PRK12844 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
42-79 |
5.69e-04 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 183787 [Multi-domain] Cd Length: 557 Bit Score: 42.43 E-value: 5.69e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1246204903 42 ADVTVIGSGPGGYVAAIKAAQLGFKAVCVEKNETLGGT 79
Cdd:PRK12844 7 YDVVVVGSGGGGMCAALAAADSGLEPLIVEKQDKVGGS 44
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
43-77 |
1.05e-03 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 41.41 E-value: 1.05e-03
10 20 30
....*....|....*....|....*....|....*
gi 1246204903 43 DVTVIGSGPGGYVAAIKAAQLGFKAVCVEKNETLG 77
Cdd:pfam03486 2 DVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
|
|
| LhgO |
COG0579 |
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism]; |
249-339 |
2.04e-03 |
|
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
Pssm-ID: 440344 [Multi-domain] Cd Length: 418 Bit Score: 40.51 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 249 GGIgID-MEISKNFQRILQKQGFKFKLNTKVTGATRKPDGkidVFIEAASGgkaeVITCDVLLVCIGrrpftknLG---- 323
Cdd:COG0579 147 TGI-VDpGALTRALAENAEANGVELLLNTEVTGIEREGDG---WEVTTNGG----TIRARFVINAAG-------LYadrl 211
|
90
....*....|....*.
gi 1246204903 324 LEELGIELDPRGrIPV 339
Cdd:COG0579 212 AQMAGIGKDFGI-FPV 226
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
44-359 |
2.57e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 40.39 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 44 VTVIGSGPGGYVAAIKAAQLGFKAVCVEKNETLGGTclnvgcipskallnnshyyhLAHGkdfasrgieMSEVRLNLDKM 123
Cdd:PRK12831 143 VAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGGV--------------------LVYG---------IPEFRLPKETV 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 124 MEQKSNAVKALtgGIAhlFKQNKVAhvngygkitgknqvtatkadGSTQVIDT-------KNILIATGSEVTPFPGIT-I 195
Cdd:PRK12831 194 VKKEIENIKKL--GVK--IETNVVV--------------------GKTVTIDElleeegfDAVFIGSGAGLPKFMGIPgE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 196 DEDTVVSSTGALS----LK----------KVPEKMVVIGAGVIGVELGSVWQRLGADVTAV------------EFLGHVG 249
Cdd:PRK12831 250 NLNGVFSANEFLTrvnlMKaykpeydtpiKVGKKVAVVGGGNVAMDAARTALRLGAEVHIVyrrseeelparvEEVHHAK 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 250 GIGIDMEISKNFQRILQKQ-----GFKF---KLNTKVTGATRKPdgkidVFIEaasgGKAEVITCDVLLVCIGRRPfTKN 321
Cdd:PRK12831 330 EEGVIFDLLTNPVEILGDEngwvkGMKCikmELGEPDASGRRRP-----VEIE----GSEFVLEVDTVIMSLGTSP-NPL 399
|
330 340 350
....*....|....*....|....*....|....*....
gi 1246204903 322 LGLEELGIELDPRGRIPVNTRF-QTKIPNIYAIGDVVAG 359
Cdd:PRK12831 400 ISSTTKGLKINKRGCIVADEETgLTSKEGVFAGGDAVTG 438
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
324-378 |
5.35e-03 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 39.34 E-value: 5.35e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1246204903 324 LEELGIELDPRGRIPVNT----RFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMA 378
Cdd:PRK12769 590 LESHGVTVDKWGRIIADVesqyRYQTSNPKIFAGGDAVRGADLVVTAMAEGRHAAQGII 648
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
44-359 |
9.47e-03 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 38.57 E-value: 9.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 44 VTVIGSGPGGYVAAIKAAQLGFKAVCVEKNETLGGTcLNVGcIPSKALLNNSHYYHLahgKDFASRGIE-MSEV----RL 118
Cdd:PRK12778 434 VAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGGV-LKYG-IPEFRLPKKIVDVEI---ENLKKLGVKfETDVivgkTI 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 119 NLDKMMEQKSNAVKALTGgiahlfkqnkvAHVNGYGKITGKNQVTATKadgSTQVIDTKNILIATGSevtpfpgitiDED 198
Cdd:PRK12778 509 TIEELEEEGFKGIFIASG-----------AGLPNFMNIPGENSNGVMS---SNEYLTRVNLMDAASP----------DSD 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 199 TVVsstgalslkKVPEKMVVIGAGVIGVELGSVWQRLGAD-VTAV------------EFLGHVGGIGIDMEISKNFQRIL 265
Cdd:PRK12778 565 TPI---------KFGKKVAVVGGGNTAMDSARTAKRLGAErVTIVyrrseeemparlEEVKHAKEEGIEFLTLHNPIEYL 635
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246204903 266 -QKQGF-------KFKLNTKVTGATRKPdgkidVFIEaasgGKAEVITCDVLLVCIGRRPfTKNLGLEELGIELDPRGRI 337
Cdd:PRK12778 636 aDEKGWvkqvvlqKMELGEPDASGRRRP-----VAIP----GSTFTVDVDLVIVSVGVSP-NPLVPSSIPGLELNRKGTI 705
|
330 340
....*....|....*....|..
gi 1246204903 338 PVNTRFQTKIPNIYAIGDVVAG 359
Cdd:PRK12778 706 VVDEEMQSSIPGIYAGGDIVRG 727
|
|
| PRK07494 |
PRK07494 |
UbiH/UbiF family hydroxylase; |
36-70 |
9.98e-03 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181001 [Multi-domain] Cd Length: 388 Bit Score: 38.34 E-value: 9.98e-03
10 20 30
....*....|....*....|....*....|....*
gi 1246204903 36 ADQPIDADVTVIGSGPGGYVAAIKAAQLGFKAVCV 70
Cdd:PRK07494 2 LMEKEHTDIAVIGGGPAGLAAAIALARAGASVALV 36
|
|
| |
