|
Name |
Accession |
Description |
Interval |
E-value |
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
33-494 |
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: 588.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 33 IDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKnETLGGTCLNVGCIPSKALLNNSHYYHLAhgKDFASRGIEIPEVRLN 112
Cdd:COG1249 2 KDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEK-GRLGGTCLNVGCIPSKALLHAAEVAHEA--RHAAEFGISAGAPSVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 113 LEKMMEQKRSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQVTATTadgsTQVIGTKNILIATGSEVTPFPGITIDEDT 192
Cdd:COG1249 79 WAALMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVTG----GETLTADHIVIATGSRPRVPPIPGLDEVR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 193 IVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGiGIDMEISKNFQRILQKQGFKFKLNTKVT 272
Cdd:COG1249 155 VLTSDEALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLP-GEDPEISEALEKALEKEGIDILTGAKVT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 273 GATKKSDGkidVSVEAASGGKAEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNTRFQTKIPNIFAIGDVVAG 352
Cdd:COG1249 234 SVEKTGDG---VTVTLEDGGGEEAVEADKVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRTSVPGIYAIGDVTGG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 353 PMLAHKAEDEGIICVEGMAGGAVH-IDYNCVPSVIYTHPEVAWVGKSEEQLKEEGVEFKVGKFPFAANSRAKTNADTDGM 431
Cdd:COG1249 311 PQLAHVASAEGRVAAENILGKKPRpVDYRAIPSVVFTDPEIASVGLTEEEAREAGIDVKVGKFPFAANGRALALGETEGF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958782340 432 VKILGHKSTDRILGAHILGPGAGEMVNEAALALEYGASCEDVARVCHAHPTLSEAFREANLAA 494
Cdd:COG1249 391 VKLIADAETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAALAL 453
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
36-501 |
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: 569.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 36 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKnETLGGTCLNVGCIPSKALLNNSHYYH-LAHGKDFasrGIEIPEVRLNLE 114
Cdd:TIGR01350 3 DVIVIGGGPGGYVAAIRAAQLGLKVALVEK-EYLGGTCLNVGCIPTKALLHSAEVYDeIKHAKDL---GIEVENVSVDWE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 115 KMMEQKRSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQVTATTADGsTQVIGTKNILIATGSEVTPFPG-ITIDEDTI 193
Cdd:TIGR01350 79 KMQKRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGENG-EETLEAKNIIIATGSRPRSLPGpFDFDGKVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 194 VSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGiGIDMEISKNFQRILQKQGFKFKLNTKVTG 273
Cdd:TIGR01350 158 ITSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILP-GEDAEVSKVLQKALKKKGVKILTNTKVTA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 274 ATKKSDGkidVSVEAaSGGKAEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNTRFQTKIPNIFAIGDVVAGP 353
Cdd:TIGR01350 237 VEKNDDQ---VTYEN-KGGETETLTGEKVLVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDVIGGP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 354 MLAHKAEDEGIICVEGMAGGA-VHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGVEFKVGKFPFAANSRAKTNADTDGMV 432
Cdd:TIGR01350 313 MLAHVASHEGIVAAENIAGKEpAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGYDVKIGKFPFAANGKALALGETDGFV 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958782340 433 KILGHKSTDRILGAHILGPGAGEMVNEAALALEYGASCEDVARVCHAHPTLSEAFREANLAAsFGKPIN 501
Cdd:TIGR01350 393 KIIADKKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEAIKEAALAA-LGKPIH 460
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
36-502 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 568.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 36 DVTVIGSGPGGYVAAIKAAQLGFKTVCIE--KNET----LGGTCLNVGCIPSKALLNNSHYYHLAhGKDFASRGIEIPEV 109
Cdd:PRK06327 6 DVVVIGAGPGGYVAAIRAAQLGLKVACIEawKNPKgkpaLGGTCLNVGCIPSKALLASSEEFENA-GHHFADHGIHVDGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 110 RLNLEKMMEQKRSAVKALTGGIAHLFKQNKVVHVNGFGKITGK----NQVTATTADGSTqvIGTKNILIATGSEVTPFPG 185
Cdd:PRK06327 85 KIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVGKtdagYEIKVTGEDETV--ITAKHVIIATGSEPRHLPG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 186 ITIDEDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHVggigiDMEISKNFQRILQKQ 261
Cdd:PRK06327 163 VPFDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEalpaFLAAA-----DEQVAKEAAKAFTKQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 262 GFKFKLNTKVtGATKKSDGKIDVSVEAASGgKAEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNTRFQTKIP 341
Cdd:PRK06327 238 GLDIHLGVKI-GEIKTGGKGVSVAYTDADG-EAQTLEVDKLIVSIGRVPNTDGLGLEAVGLKLDERGFIPVDDHCRTNVP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 342 NIFAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGVEFKVGKFPFAANSR 421
Cdd:PRK06327 316 NVYAIGDVVRGPMLAHKAEEEGVAVAERIAGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLKAEGVEYKAGKFPFMANGR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 422 AKTNADTDGMVKILGHKSTDRILGAHILGPGAGEMVNEAALALEYGASCEDVARVCHAHPTLSEAFREANLAASfGKPIN 501
Cdd:PRK06327 396 ALAMGEPDGFVKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEVWHEAALAVD-KRPLH 474
|
.
gi 1958782340 502 F 502
Cdd:PRK06327 475 F 475
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
31-502 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 545.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 31 QPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKnETLGGTCLNVGCIPSKALLNNSHYYHLA-HGKDFasrGIEIPEV 109
Cdd:PRK06416 1 FAFEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEK-EKLGGTCLNRGCIPSKALLHAAERADEArHSEDF---GIKAENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 110 RLNLEKMMEQKRSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQVTATTADGsTQVIGTKNILIATGSEVTPFPGITID 189
Cdd:PRK06416 77 GIDFKKVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDG-EQTYTAKNIILATGSRPRELPGIEID 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 190 EDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGiGIDMEISKNFQRILQKQGFKFKLNT 269
Cdd:PRK06416 156 GRVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILP-GEDKEISKLAERALKKRGIKIKTGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 270 KVTGATKKSDGkidVSVEAASGGKAEVITCDVLLVCIGRRPFTQNLGLEELGIELDpKGRIPVNTRFQTKIPNIFAIGDV 349
Cdd:PRK06416 235 KAKKVEQTDDG---VTVTLEDGGKEETLEADYVLVAVGRRPNTENLGLEELGVKTD-RGFIEVDEQLRTNVPNIYAIGDI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 350 VAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGVEFKVGKFPFAANSRAKTNADTD 429
Cdd:PRK06416 311 VGGPMLAHKASAEGIIAAEAIAGNPHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFDVKVVKFPFAGNGKALALGETD 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958782340 430 GMVKILGHKSTDRILGAHILGPGAGEMVNEAALALEYGASCEDVARVCHAHPTLSEAFREANLAASfGKPINF 502
Cdd:PRK06416 391 GFVKLIFDKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEALGEAALAAA-GKPLHA 462
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
33-496 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 535.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 33 IDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKnETLGGTCLNVGCIPSKALLNNSHYYHLAhgKDFASRGIEIPEVRLN 112
Cdd:PRK06292 2 EKYDVIVIGAGPAGYVAARRAAKLGKKVALIEK-GPLGGTCLNVGCIPSKALIAAAEAFHEA--KHAEEFGIHADGPKID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 113 LEKMMEQKRSAVKALTGGIAH-LFKQNKVVHVNGFGKITGKNQVTAttadgSTQVIGTKNILIATGSEVTPFPGIT-IDE 190
Cdd:PRK06292 79 FKKVMARVRRERDRFVGGVVEgLEKKPKIDKIKGTARFVDPNTVEV-----NGERIEAKNIVIATGSRVPPIPGVWlILG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 191 DTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGiGIDMEISKNFQRILQKQgFKFKLNTK 270
Cdd:PRK06292 154 DRLLTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILP-LEDPEVSKQAQKILSKE-FKIKLGAK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 271 VTGATKKSDGKIdvsVEAASGGKAEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNTRFQTKIPNIFAIGDVV 350
Cdd:PRK06292 232 VTSVEKSGDEKV---EELEKGGKTETIEADYVLVATGRRPNTDGLGLENTGIELDERGRPVVDEHTQTSVPGIYAAGDVN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 351 AGPMLAHKAEDEGIICVEGMAGG-AVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGVEFKVGKFPFAANSRAKTNADTD 429
Cdd:PRK06292 309 GKPPLLHEAADEGRIAAENAAGDvAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEVPFEAQGRARVMGKND 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782340 430 GMVKILGHKSTDRILGAHILGPGAGEMVNEAALALEYGASCEDVARVCHAHPTLSEAFREANLAASF 496
Cdd:PRK06292 389 GFVKVYADKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRTALRDLFS 455
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
31-494 |
2.76e-106 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 324.80 E-value: 2.76e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 31 QPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKAL------LNNSHYYHLaHGKDFASRGI 104
Cdd:PRK05249 2 HMYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGGGCTHTGTIPSKALreavlrLIGFNQNPL-YSSYRVKLRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 105 EIPEVRLNLEKMMEQKRSAvkaltggIAHLFKQNKVVHVNGFGKITGKNQVTATTADGSTQVIGTKNILIATGSEvtPF- 183
Cdd:PRK05249 81 TFADLLARADHVINKQVEV-------RRGQYERNRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATGSR--PYr 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 184 -PGITIDEDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVE-------FLghvggigiDMEISKNFQ 255
Cdd:PRK05249 152 pPDVDFDHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINtrdrllsFL--------DDEISDALS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 256 RILQKQGFKFKLNTKVTGATKKSDGKIdvsVEAASGGKaevITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNTR 335
Cdd:PRK05249 224 YHLRDSGVTIRHNEEVEKVEGGDDGVI---VHLKSGKK---IKADCLLYANGRTGNTDGLNLENAGLEADSRGQLKVNEN 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 336 FQTKIPNIFAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGVEFKVGKFP 415
Cdd:PRK05249 298 YQTAVPHIYAVGDVIGFPSLASASMDQGRIAAQHAVGEATAHLIEDIPTGIYTIPEISSVGKTEQELTAAKVPYEVGRAR 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958782340 416 FAANSRAKTNADTDGMVKILGHKSTDRILGAHILGPGAGEMVNEAALALEYGASCEDVARVCHAHPTLSEAFREANLAA 494
Cdd:PRK05249 378 FKELARAQIAGDNVGMLKILFHRETLEILGVHCFGERATEIIHIGQAIMEQKGTIEYFVNTTFNYPTMAEAYRVAALDG 456
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
36-496 |
1.62e-104 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 320.23 E-value: 1.62e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 36 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNEtLGGTCLNVGCIPSKALLNNSHYYHLA-HGKDFasrGIEIP-EVRLNL 113
Cdd:PRK06370 7 DAIVIGAGQAGPPLAARAAGLGMKVALIERGL-LGGTCVNTGCVPTKTLIASARAAHLArRAAEY---GVSVGgPVSVDF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 114 EKMMEQKRSAVKALTGGIAHLFKQNKVVHV-NGFGKITGKNQVTAttaDGSTqvIGTKNILIATGSE--VTPFPGItiDE 190
Cdd:PRK06370 83 KAVMARKRRIRARSRHGSEQWLRGLEGVDVfRGHARFESPNTVRV---GGET--LRAKRIFINTGARaaIPPIPGL--DE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 191 DTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGiGIDMEISKNFQRILQKQGFKFKLNTK 270
Cdd:PRK06370 156 VGYLTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLP-REDEDVAAAVREILEREGIDVRLNAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 271 VTGATKKSDGKIdvsVEAASGGKAEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNTRFQTKIPNIFAIGDVV 350
Cdd:PRK06370 235 CIRVERDGDGIA---VGLDCNGGAPEITGSHILVAVGRVPNTDDLGLEAAGVETDARGYIKVDDQLRTTNPGIYAAGDCN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 351 AGPMLAHKAEDEGIICVEGMA-GGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGVEFKVGKFPFAANSRAKTNADTD 429
Cdd:PRK06370 312 GRGAFTHTAYNDARIVAANLLdGGRRKVSDRIVPYATYTDPPLARVGMTEAEARKSGRRVLVGTRPMTRVGRAVEKGETQ 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782340 430 GMVKILGHKSTDRILGAHILGPGAGEMVNEAALALEYGASCEDVARVCHAHPTLSEAFReaNLAASF 496
Cdd:PRK06370 392 GFMKVVVDADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIP--TLAQAL 456
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
36-493 |
6.29e-102 |
|
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: 313.59 E-value: 6.29e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 36 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNeTLGGTCLNVGCIPSKALLNNSHYYHLAHGkdfASRGIEIPEVRLNLEK 115
Cdd:TIGR02053 2 DLVIIGSGAAAFAAAIKAAELGASVAMVERG-PLGGTCVNVGCVPSKMLLRAAEVAHYARK---PPFGGLAATVAVDFGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 116 MMEQKRSAVKAL-TGGIAHLFKQNKVVHVNGFGKITGKNQVTAttaDGSTQVIGTKNILIATGSE--VTPFPGItiDEDT 192
Cdd:TIGR02053 78 LLEGKREVVEELrHEKYEDVLSSYGVDYLRGRARFKDPKTVKV---DLGREVRGAKRFLIATGARpaIPPIPGL--KEAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 193 IVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHvggigIDMEISKNFQRILQKQGFKFKLN 268
Cdd:TIGR02053 153 YLTSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQrsdrLLPR-----EEPEISAAVEEALAEEGIEVVTS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 269 TKVTGATKKSDGKIDVSVEAASGGKAEVitcDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNTRFQTKIPNIFAIGD 348
Cdd:TIGR02053 228 AQVKAVSVRGGGKIITVEKPGGQGEVEA---DELLVATGRRPNTDGLGLEKAGVKLDERGGILVDETLRTSNPGIYAAGD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 349 VVAGPMLAHKAEDEGIICVEGMAGGA-VHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGVEFKVGKFPFAANSRAKTNAD 427
Cdd:TIGR02053 305 VTGGLQLEYVAAKEGVVAAENALGGAnAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNVPRARINRD 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958782340 428 TDGMVKILGHKSTDRILGAHILGPGAGEMVNEAALALEYGASCEDVARVCHAHPTLSEAFREANLA 493
Cdd:TIGR02053 385 TRGFIKLVAEPGTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGLKLAAQT 450
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
34-487 |
1.29e-79 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 255.47 E-value: 1.29e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 34 DADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNEtLGGTCLNVGCIPSKALLNNSHYYHLAH--GKDFasrGIEIPEVRL 111
Cdd:PRK06116 4 DYDLIVIGGGSGGIASANRAAMYGAKVALIEAKR-LGGTCVNVGCVPKKLMWYGAQIAEAFHdyAPGY---GFDVTENKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 112 NLEKMMEQKRSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQVTAT----TADgstqvigtkNILIATGSEVTP--FPG 185
Cdd:PRK06116 80 DWAKLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNgeryTAD---------HILIATGGRPSIpdIPG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 186 ItidEDTIvSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAV----EFLGhvggiGIDMEISKNFQRILQKQ 261
Cdd:PRK06116 151 A---EYGI-TSDGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFvrgdAPLR-----GFDPDIRETLVEEMEKK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 262 GFKFKLNTKVTGATKKSDGKIDVSVEaasggKAEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNTRFQTKIP 341
Cdd:PRK06116 222 GIRLHTNAVPKAVEKNADGSLTLTLE-----DGETLTVDCLIWAIGREPNTDGLGLENAGVKLNEKGYIIVDEYQNTNVP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 342 NIFAIGDVVAGPMLAHKAEDEGIICVEGMAGG--AVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGVEF--KVGKFPFA 417
Cdd:PRK06116 297 GIYAVGDVTGRVELTPVAIAAGRRLSERLFNNkpDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDnvKVYRSSFT 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 418 ANSRAKTNADTDGMVKILGHKSTDRILGAHILGPGAGEMVNEAALALEYGASCEDVARVCHAHPTLSEAF 487
Cdd:PRK06116 377 PMYTALTGHRQPCLMKLVVVGKEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEF 446
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
17-495 |
6.69e-74 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 245.98 E-value: 6.69e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 17 LQGASSVPLRTYSDQPIDadVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNE-TLGGTCLNVGCIPSKALL---------- 85
Cdd:PTZ00153 101 ANGFATSQSMNFSDEEYD--VGIIGCGVGGHAAAINAMERGLKVIIFTGDDdSIGGTCVNVGCIPSKALLyatgkyrelk 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 86 NNSHYYHLAHGKDFASRGIEIP---------EVRLNLEKMMEQKRSAVKALTGGIAHLFKQNK-------VVHVNGFGKI 149
Cdd:PTZ00153 179 NLAKLYTYGIYTNAFKNGKNDPvernqlvadTVQIDITKLKEYTQSVIDKLRGGIENGLKSKKfcknsehVQVIYERGHI 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 150 TGKNQVTAttaDGSTQVIGTKNILIATGSevTPF--PGITIDEDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQR 227
Cdd:PTZ00153 259 VDKNTIKS---EKSGKEFKVKNIIIATGS--TPNipDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTA 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 228 LGADVTAVEFLGHVGGiGIDMEISKNFQRILQK-QGFKFKLNTKVT-------------GATKKSDGKIDVSVEAASGGK 293
Cdd:PTZ00153 334 LGSEVVSFEYSPQLLP-LLDADVAKYFERVFLKsKPVRVHLNTLIEyvragkgnqpviiGHSERQTGESDGPKKNMNDIK 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 294 AevITCDVLLVCIGRRPFTQNLGLEELGIELDpKGRIPVNTRFQTK------IPNIFAIGDVVAGPMLAHKAEDEGIICV 367
Cdd:PTZ00153 413 E--TYVDSCLVATGRKPNTNNLGLDKLKIQMK-RGFVSVDEHLRVLredqevYDNIFCIGDANGKQMLAHTASHQALKVV 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 368 EGMAGGAVH-------------IDYNCVPSVIYTHPEVAWVGKSEEQLKEEGVEFKVGKFP--FAANSRA---------- 422
Cdd:PTZ00153 490 DWIEGKGKEnvninvenwaskpIIYKNIPSVCYTTPELAFIGLTEKEAKELYPPDNVGVEIsfYKANSKVlcennisfpn 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 423 ------------KTNADTDGMVKILGHKSTDRILGAHILGPGAGEMVNEAALALEYGASCEDVARVCHAHPTLSEAFREA 490
Cdd:PTZ00153 570 nsknnsynkgkyNTVDNTEGMVKIVYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDAA 649
|
....*
gi 1958782340 491 NLAAS 495
Cdd:PTZ00153 650 FKAIA 654
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
36-363 |
5.01e-72 |
|
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: 230.67 E-value: 5.01e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 36 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEknetLGGTCLNVGCIPSKALLNnshyyhlahgkdfasrGIEIPEVRLNLEK 115
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIE----DEGTCPYGGCVLSKALLG----------------AAEAPEIASLWAD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 116 MMEQKRSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQVtattaDGSTQVIGTKNILIATGSE--VTPFPGIT---IDE 190
Cdd:pfam07992 62 LYKRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELV-----DGDGETITYDRLVIATGARprLPPIPGVElnvGFL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 191 DTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGiGIDMEISKNFQRILQKQGFKFKLNTK 270
Cdd:pfam07992 137 VRTLDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLR-AFDEEISAALEKALEKNGVEVRLGTS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 271 VTGATKKSDGkidVSVEAASGgkaEVITCDVLLVCIGRRPFTQnlGLEELGIELDPKGRIPVNTRFQTKIPNIFAIGDV- 349
Cdd:pfam07992 216 VKEIIGDGDG---VEVILKDG---TEIDADLVVVAIGRRPNTE--LLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDCr 287
|
330
....*....|....
gi 1958782340 350 VAGPMLAHKAEDEG 363
Cdd:pfam07992 288 VGGPELAQNAVAQG 301
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
37-501 |
1.04e-68 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 230.04 E-value: 1.04e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 37 VTVIGSGPGGYVAAIKAAQLGFKTVCIEKNeTLGGTCLNVGCIPSKALLNNSHYYHLAHGKDFASrGIEIPEVRLNLEKM 116
Cdd:PRK13748 101 VAVIGSGGAAMAAALKAVEQGARVTLIERG-TIGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDG-GIAATVPTIDRSRL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 117 MEQKRSAVKALTG----GIAHLFKQNKVVHvnGFGKITGKNQVTATTADGSTQVIGTKNILIATGSE--VTPFPGITidE 190
Cdd:PRK13748 179 LAQQQARVDELRHakyeGILDGNPAITVLH--GEARFKDDQTLIVRLNDGGERVVAFDRCLIATGASpaVPPIPGLK--E 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 191 DTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHvggigiDMEISKNFQRILQKQGFKFK 266
Cdd:PRK13748 255 TPYWTSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILArstlFFRE------DPAIGEAVTAAFRAEGIEVL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 267 LNTKVTgATKKSDGKIDVSVEAASggkaevITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNTRFQTKIPNIFAI 346
Cdd:PRK13748 329 EHTQAS-QVAHVDGEFVLTTGHGE------LRADKLLVATGRAPNTRSLALDAAGVTVNAQGAIVIDQGMRTSVPHIYAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 347 GDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGVEFKVGKFPFAANSRAKTNA 426
Cdd:PRK13748 402 GDCTDQPQFVYVAAAAGTRAAINMTGGDAALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRTLTLDNVPRALANF 481
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958782340 427 DTDGMVKILGHKSTDRILGAHILGPGAGEMVNEAALALEYGASCEDVARVCHAHPTLSEAFREAnlAASFGKPIN 501
Cdd:PRK13748 482 DTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAALAIRNRMTVQELADQLFPYLTMVEGLKLA--AQTFNKDVK 554
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
39-489 |
1.63e-68 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 226.20 E-value: 1.63e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 39 VIGSGPGGYVAAIKAAQLGFKTVCIEKNETL-GGTCLNVGCIPSKALLNNSHYYHlahgkDFASrgieipevrlnlekMM 117
Cdd:NF040477 8 IIGFGKAGKTLAATLAKAGWRVAIIEQSAQMyGGTCINIGCIPTKTLVHDAEQHQ-----DFST--------------AM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 118 EQKRSAVKALTGGIAH-LFKQNKVVHVNGFGKITGKNQVTATTADGsTQVIGTKNILIATGSEVT--PFPGITIDEDtIV 194
Cdd:NF040477 69 QRKSSVVGFLRDKNYHnLADLDNVDVINGRAEFIDNHTLRVFQADG-EQELRGEKIFINTGAQSVlpPIPGLTTTPG-VY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 195 SSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGIGiDMEISKNFQRILQKQGFKFKLNTKVTGA 274
Cdd:NF040477 147 DSTGLLNLTQLPARLGILGGGYIGVEFASMFARFGSKVTIFEAAELFLPRE-DRDIAQAIATILQDQGVELILNAQVQRV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 275 TKKSDGkidVSVEAASGgkaeVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNTRFQTKIPNIFAIGDVVAGPM 354
Cdd:NF040477 226 SSHEGE---VQLETAEG----VLTVDALLVASGRKPATAGLQLQNAGVAVNERGAIVVDKYLRTTADNIWAMGDVTGGLQ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 355 LAHKAEDEGIICVEGMAG-GAVHI-DYNCVPSVIYTHPEVAWVGKSEEQLKEEGVEFKVGKFPFAANSRAKTNADTDGMV 432
Cdd:NF040477 299 FTYISLDDFRIVRDSLLGeGKRSTdDRQNVPYSVFMTPPLSRIGMTEEQARASGADIQVVTLPVAAIPRARVMNDTRGVL 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782340 433 KILGHKSTDRILGAHILGPGAGEMVNEAALALEYGASCEDVARVCHAHPTLSEAFRE 489
Cdd:NF040477 379 KAVVDNKTQRILGVSLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSESLND 435
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
36-487 |
5.46e-66 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 219.62 E-value: 5.46e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 36 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETL-GGTCLNVGCIPSKALLNNshyyhlahgkdfASRGieipevrLNLE 114
Cdd:PRK07251 5 DLIVIGFGKAGKTLAAKLASAGKKVALVEESKAMyGGTCINIGCIPTKTLLVA------------AEKN-------LSFE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 115 KMMEQKRSAVKALTGGIAHLFKQNKVVHVNGFGKITGkNQVTATTADGSTQVIGTKNILIATG--SEVTPFPGITiDEDT 192
Cdd:PRK07251 66 QVMATKNTVTSRLRGKNYAMLAGSGVDLYDAEAHFVS-NKVIEVQAGDEKIELTAETIVINTGavSNVLPIPGLA-DSKH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 193 IVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHVggigiDMEISKNFQRILQKQGFKFKLN 268
Cdd:PRK07251 144 VYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDaastILPRE-----EPSVAALAKQYMEEDGITFLLN 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 269 TKVTgATKKSDGKIDVSVEAasggkaEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNTRFQTKIPNIFAIGD 348
Cdd:PRK07251 219 AHTT-EVKNDGDQVLVVTED------ETYRFDALLYATGRKPNTEPLGLENTDIELTERGAIKVDDYCQTSVPGVFAVGD 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 349 VVAGPMLAHKAEDEGIICVEGMAGGA--VHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGVEFKVGKFPFAANSRAKTNA 426
Cdd:PRK07251 292 VNGGPQFTYISLDDFRIVFGYLTGDGsyTLEDRGNVPTTMFITPPLSQVGLTEKEAKEAGLPYAVKELLVAAMPRAHVNN 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958782340 427 DTDGMVKILGHKSTDRILGAHILGPGAGEMVNEAALALEYGASCEDVARVCHAHPTLSEAF 487
Cdd:PRK07251 372 DLRGAFKVVVNTETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAENL 432
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
34-487 |
5.93e-64 |
|
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member of the pyridine nucleotide disulfide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly, where SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily, Cys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-term arm of the protein is proposed to allow broad substrate specificity.
Pssm-ID: 273624 [Multi-domain] Cd Length: 484 Bit Score: 215.49 E-value: 5.93e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 34 DADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNET--------LGGTCLNVGCIPSKALLNNSHY-YHLAHGKDFASRGI 104
Cdd:TIGR01438 2 DYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPtplgtrwgIGGTCVNVGCIPKKLMHQAALLgQALKDSRNYGWKVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 105 EipEVRLNLEKMMEQKRSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQVTATTADGSTQVIGTKNILIATGsEVTPFP 184
Cdd:TIGR01438 82 E--TVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATG-ERPRYP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 185 GITIDEDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVeflghVGGI---GIDMEISKNFQRILQKQ 261
Cdd:TIGR01438 159 GIPGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVM-----VRSIllrGFDQDCANKVGEHMEEH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 262 GFKFKLNTKVTGATKKSDGKIDVSVEAASGGKAEVitcDVLLVCIGRRPFTQNLGLEELGIELDPK-GRIPVNTRFQTKI 340
Cdd:TIGR01438 234 GVKFKRQFVPIKVEQIEAKVLVEFTDSTNGIEEEY---DTVLLAIGRDACTRKLNLENVGVKINKKtGKIPADEEEQTNV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 341 PNIFAIGDVVAG-PMLAHKAEDEGIICVEGMAGGAVHI-DYNCVPSVIYTHPEVAWVGKSEEQ----LKEEGVEFKVGKF 414
Cdd:TIGR01438 311 PYIYAVGDILEDkPELTPVAIQAGRLLAQRLFKGSTVIcDYENVPTTVFTPLEYGACGLSEEKavekFGEENVEVFHSYF 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958782340 415 -PFAANSRAKTNADTDGMVKILGHKSTDRILGAHILGPGAGEMVNEAALALEYGASCEDVARVCHAHPTLSEAF 487
Cdd:TIGR01438 391 wPLEWTIPSRDNHNKCYAKLVCNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVF 464
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
36-487 |
5.32e-62 |
|
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: 209.31 E-value: 5.32e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 36 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNEtLGGTCLNVGCIPSKALLNNSHYYHLAHgkDFASRGIEI-PEVRLNLE 114
Cdd:TIGR01421 4 DYLVIGGGSGGIASARRAAEHGAKALLVEAKK-LGGTCVNVGCVPKKVMWYASDLAERMH--DAADYGFYQnDENTFNWP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 115 KMMEQKRSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQVTATTADgstqvIGTKNILIATGSEVTPFPGITIDEDTIv 194
Cdd:TIGR01421 81 ELKEKRDAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVNGRD-----YTAPHILIATGGKPSFPENIPGAELGT- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 195 SSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADvTAVEFLGHVGGIGIDMEISKNFQRILQKQGFKFKLNTKVTGA 274
Cdd:TIGR01421 155 DSDGFFALEELPKRVVIVGAGYIAVELAGVLHGLGSE-THLVIRHERVLRSFDSMISETITEEYEKEGINVHKLSKPVKV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 275 TKKSDGKIDVSVEAASggkaEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNTRFQTKIPNIFAIGDVVAGPM 354
Cdd:TIGR01421 234 EKTVEGKLVIHFEDGK----SIDDVDELIWAIGRKPNTKGLGLENVGIKLNEKGQIIVDEYQNTNVPGIYALGDVVGKVE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 355 LAHKAEDEGIICVEGMAGGA--VHIDYNCVPSVIYTHPEVAWVGKSEEQ-LKEEGVE-FKVGKFPFAANSRAKTNADTDG 430
Cdd:TIGR01421 310 LTPVAIAAGRKLSERLFNGKtdDKLDYNNVPTVVFSHPPIGTIGLTEKEaIEKYGKEnIKVYNSSFTPMYYAMTSEKQKC 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782340 431 MVKILGHKSTDRILGAHILGPGAGEMVNEAALALEYGASCEDVARVCHAHPTLSEAF 487
Cdd:TIGR01421 390 RMKLVCAGKEEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEEL 446
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
34-487 |
9.79e-62 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 210.06 E-value: 9.79e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 34 DADVTVIGSGPGGYVAAIKAAQLG---------FKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYhlAHGKDFASRGI 104
Cdd:PLN02507 25 DFDLFVIGAGSGGVRAARFSANFGakvgicelpFHPISSESIGGVGGTCVIRGCVPKKILVYGATFG--GEFEDAKNYGW 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 105 EIPE-VRLNLEKMMEQKRSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQVTATTADGSTQVIGTKNILIATGSEVTP- 182
Cdd:PLN02507 103 EINEkVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRYTAKHILIATGSRAQRp 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 183 -FPG----ITIDEdtivsstgALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVeFLGHVGGIGIDMEISKNFQRI 257
Cdd:PLN02507 183 nIPGkelaITSDE--------ALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLF-FRKELPLRGFDDEMRAVVARN 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 258 LQKQGFKFKLNTKVTGATKKSDGkIDVSVEaasggKAEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNTRFQ 337
Cdd:PLN02507 254 LEGRGINLHPRTNLTQLTKTEGG-IKVITD-----HGEEFVADVVLFATGRAPNTKRLNLEAVGVELDKAGAVKVDEYSR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 338 TKIPNIFAIGDVVAGPMLAHKAEDEGIICVEGMAGG-AVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEG---VEFKVGK 413
Cdd:PLN02507 328 TNIPSIWAIGDVTNRINLTPVALMEGTCFAKTVFGGqPTKPDYENVACAVFCIPPLSVVGLSEEEAVEQAkgdILVFTSS 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958782340 414 FPFAANSRAKTNADTdgMVKILGHKSTDRILGAHILGPGAGEMVNEAALALEYGASCEDVARVCHAHPTLSEAF 487
Cdd:PLN02507 408 FNPMKNTISGRQEKT--VMKLIVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEF 479
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
37-490 |
5.90e-57 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 196.23 E-value: 5.90e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 37 VTVIGSGPGGYVAAIKAAQLGFKTVCIEkNETLGGTCLNVGCIPSKALLNNSHYY-HLAHGKDFASRGIEIPEVRLNLEK 115
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIE-RDGLGGAAVLTDCVPSKTLIATAEVRtELRRAAELGIRFIDDGEARVDLPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 116 MMEQKRSAVKALTGGIAHLFKQNKVVHVNGFGKIT----GKNQVTATTADGSTQVIGTKNILIATGSevTP--FPGITID 189
Cdd:PRK07845 83 VNARVKALAAAQSADIRARLEREGVRVIAGRGRLIdpglGPHRVKVTTADGGEETLDADVVLIATGA--SPriLPTAEPD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 190 EDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGiGIDMEISKNFQRILQKQGFKFKLNT 269
Cdd:PRK07845 161 GERILTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLP-GEDADAAEVLEEVFARRGMTVLKRS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 270 KVTGATKKSDGkidVSVEAASGGKAEVITCdvlLVCIGRRPFTQNLGLEELGIELDPKGRIPVNTRFQTKIPNIFAIGDV 349
Cdd:PRK07845 240 RAESVERTGDG---VVVTLTDGRTVEGSHA---LMAVGSVPNTAGLGLEEAGVELTPSGHITVDRVSRTSVPGIYAAGDC 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 350 VAGPMLAHKAEDEGIICVEGMAGGAVH-IDYNCVPSVIYTHPEVAWVGKSEEQLKEEGVEFKVGKFPFAANSRAKTNADT 428
Cdd:PRK07845 314 TGVLPLASVAAMQGRIAMYHALGEAVSpLRLKTVASNVFTRPEIATVGVSQAAIDSGEVPARTVMLPLATNPRAKMSGLR 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958782340 429 DGMVKILGHKSTDRILGAHILGPGAGEMVNEAALALEYGASCEDVARVCHAHPTLSEAFREA 490
Cdd:PRK07845 394 DGFVKLFCRPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYPSLSGSITEA 455
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
36-496 |
2.31e-56 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 194.40 E-value: 2.31e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 36 DVTVIGSGPGGyvaAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLnnsHYYHLAHGKDFASR-GI--EIPEVRln 112
Cdd:PRK07846 3 DLIIIGTGSGN---SILDERFADKRIAIVEKGTFGGTCLNVGCIPTKMFV---YAADVARTIREAARlGVdaELDGVR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 113 lekmMEQKRSAVKALT-----GGIAHLFKQNKVVHV-NGFGKITGknQVTATTADGStqVIGTKNILIATGSEVTPFPGI 186
Cdd:PRK07846 75 ----WPDIVSRVFGRIdpiaaGGEEYRGRDTPNIDVyRGHARFIG--PKTLRTGDGE--EITADQVVIAAGSRPVIPPVI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 187 TIDEDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHvggigIDMEISKNFQRILQKQg 262
Cdd:PRK07846 147 ADSGVRYHTSDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNrsgrLLRH-----LDDDISERFTELASKR- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 263 FKFKLNTKVTGATKKSDGkidVSVEAASGgkaEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNTRFQTKIPN 342
Cdd:PRK07846 221 WDVRLGRNVVGVSQDGSG---VTLRLDDG---STVEADVLLVATGRVPNGDLLDAAAAGVDVDEDGRVVVDEYQRTSAEG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 343 IFAIGDVVAGPMLAHKAEDEGIICVEGMAGGA--VHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGVEFKVGKFPFAANS 420
Cdd:PRK07846 295 VFALGDVSSPYQLKHVANHEARVVQHNLLHPDdlIASDHRFVPAAVFTHPQIASVGLTENEARAAGLDITVKVQNYGDVA 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782340 421 RAKTNADTDGMVKILGHKSTDRILGAHILGPGAGEMVNEAALALEYGASCEDVARVCH-AHPTLSEAFREANLAASF 496
Cdd:PRK07846 375 YGWAMEDTTGFVKLIADRDTGRLLGAHIIGPQASTLIQPLIQAMSFGLDAREMARGQYwIHPALPEVVENALLGLDL 451
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
39-489 |
2.99e-56 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 193.69 E-value: 2.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 39 VIGSGPGGYVAAIKAAQLGFKTVCIEK-NETLGGTCLNVGCIPSKALLNNSHyyhlAHGkDFAsrgieipevrlnleKMM 117
Cdd:PRK08010 8 IIGFGKAGKTLAVTLAKAGWRVALIEQsNAMYGGTCINIGCIPTKTLVHDAQ----QHT-DFV--------------RAI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 118 EQKRSAVKALTGGIAH-LFKQNKVVHVNGFGKITGKNQVTATTADGSTQVIGTKnILIATGSE--VTPFPGITIDEDtIV 194
Cdd:PRK08010 69 QRKNEVVNFLRNKNFHnLADMPNIDVIDGQAEFINNHSLRVHRPEGNLEIHGEK-IFINTGAQtvVPPIPGITTTPG-VY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 195 SSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHVggigiDMEISKNFQRILQKQGFKFKLNTK 270
Cdd:PRK08010 147 DSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEaaslFLPRE-----DRDIADNIATILRDQGVDIILNAH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 271 VTGATKKsDGKIDVSVEAASggkaevITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNTRFQTKIPNIFAIGDVV 350
Cdd:PRK08010 222 VERISHH-ENQVQVHSEHAQ------LAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKYLHTTADNIWAMGDVT 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 351 AGPMLAHKAEDEGIICVEGMAGGAVHI--DYNCVPSVIYTHPEVAWVGKSEEQLKEEGVEFKVGKFPFAANSRAKTNADT 428
Cdd:PRK08010 295 GGLQFTYISLDDYRIVRDELLGEGKRStdDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDT 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958782340 429 DGMVKILGHKSTDRILGAHILGPGAGEMVNEAALALEYGASCEDVARVCHAHPTLSEAFRE 489
Cdd:PRK08010 375 RGVLKAIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLND 435
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
382-490 |
7.87e-53 |
|
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases.
Pssm-ID: 427019 [Multi-domain] Cd Length: 109 Bit Score: 173.89 E-value: 7.87e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 382 VPSVIYTHPEVAWVGKSEEQLKEEGVEFKVGKFPFAANSRAKTNADTDGMVKILGHKSTDRILGAHILGPGAGEMVNEAA 461
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGEVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQEAA 80
|
90 100
....*....|....*....|....*....
gi 1958782340 462 LALEYGASCEDVARVCHAHPTLSEAFREA 490
Cdd:pfam02852 81 LAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
36-485 |
1.72e-52 |
|
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: 184.79 E-value: 1.72e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 36 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNET---------LGGTCLNVGCIPSKALLNNSHYyhLAHGKDFASRGIEI 106
Cdd:TIGR01423 5 DLVVIGAGSGGLEAGWNAATLYKKRVAVVDVQThhgppfyaaLGGTCVNVGCVPKKLMVTGAQY--MDTLRESAGFGWEF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 107 --PEVRLNLEKMMEQKRSAVKALTGGIAHLFKQNK-VVHVNGFGKITGKNQVTA-TTADGSTQV---IGTKNILIATGS- 178
Cdd:TIGR01423 83 drSSVKANWKALIAAKNKAVLDINKSYEGMFADTEgLTFFLGWGALEDKNVVLVrESADPKSAVkerLQAEHILLATGSw 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 179 -EVTPFPGItideDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSV---WQRLGADVTaVEFLGHVGGIGIDMEISKNF 254
Cdd:TIGR01423 163 pQMLGIPGI----EHCISSNEAFYLDEPPRRVLTVGGGFISVEFAGIfnaYKPRGGKVT-LCYRNNMILRGFDSTLRKEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 255 QRILQKQGFKFKLNTKVTGATKKSDGKIDVSVEaaSGGKAEVitcDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNT 334
Cdd:TIGR01423 238 TKQLRANGINIMTNENPAKVTLNADGSKHVTFE--SGKTLDV---DVVMMAIGRVPRTQTLQLDKVGVELTKKGAIQVDE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 335 RFQTKIPNIFAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVH-IDYNCVPSVIYTHPEVAWVGKSEEQL--KEEGVEFKV 411
Cdd:TIGR01423 313 FSRTNVPNIYAIGDVTDRVMLTPVAINEGAAFVDTVFGNKPRkTDHTRVASAVFSIPPIGTCGLVEEDAakKFEKVAVYE 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958782340 412 GKF-PFAANSRAKTNADTdgMVKILGHKSTDRILGAHILGPGAGEMVNEAALALEYGASCEDVARVCHAHPTLSE 485
Cdd:TIGR01423 393 SSFtPLMHNISGSKYKKF--VAKIVTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAE 465
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
34-487 |
1.12e-49 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 177.71 E-value: 1.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 34 DADVTVIGSGPGGYVAAIKAAQLGFKTVCIE--KNET------LGGTCLNVGCIPSKALLNNSHYYHLAHgKDFASRGIE 105
Cdd:PTZ00052 5 MYDLVVIGGGSGGMAAAKEAAAHGKKVALFDyvKPSTqgtkwgLGGTCVNVGCVPKKLMHYAANIGSIFH-HDSQMYGWK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 106 IPEVrLNLEKMMEQKRSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQVtATTADGSTQVIGTKNILIATGSEvtpfPG 185
Cdd:PTZ00052 84 TSSS-FNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTV-SYGDNSQEETITAKYILIATGGR----PS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 186 ITID----EDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVeflghVGGI---GIDMEISKNFQRIL 258
Cdd:PTZ00052 158 IPEDvpgaKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVA-----VRSIplrGFDRQCSEKVVEYM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 259 QKQGFKFKlNTKVTGATKKSDGKIDVSVeaaSGGKAEVItcDVLLVCIGRRPFTQNLGLEELGIELDPKGRIpVNTRFQT 338
Cdd:PTZ00052 233 KEQGTLFL-EGVVPINIEKMDDKIKVLF---SDGTTELF--DTVLYATGRKPDIKGLNLNAIGVHVNKSNKI-IAPNDCT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 339 KIPNIFAIGDVVAG-PMLAHKAEDEGIICVEGMAGGAVHI-DYNCVPSVIYTHPEVAWVGKSEEQLKEEGVEFKVGKFPF 416
Cdd:PTZ00052 306 NIPNIFAVGDVVEGrPELTPVAIKAGILLARRLFKQSNEFiDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 417 AANS------------RAKTNA-DTD----GMVKILGHKSTD-RILGAHILGPGAGEMVNEAALALEYGASCEDVARVCH 478
Cdd:PTZ00052 386 EFNTleiaavhrekheRARKDEyDFDvssnCLAKLVCVKSEDnKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIG 465
|
....*....
gi 1958782340 479 AHPTLSEAF 487
Cdd:PTZ00052 466 IHPTDAEVF 474
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
36-493 |
5.21e-49 |
|
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: 174.56 E-value: 5.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 36 DVTVIGSGPGGyvaAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLnnsHYYHLAHGKDFASR-GI--EIPEVRLN 112
Cdd:TIGR03452 4 DLIIIGTGSGN---SIPDPRFADKRIAIVEKGTFGGTCLNVGCIPTKMFV---YAAEVAQSIGESARlGIdaEIDSVRWP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 113 --LEKMMEQKrsaVKALTGGIAHLFKQNKVVHVNGF-GKITGKNQVTATTADGSTqvIGTKNILIATGSEVTPFPGITID 189
Cdd:TIGR03452 78 diVSRVFGDR---IDPIAAGGEDYRRGDETPNIDVYdGHARFVGPRTLRTGDGEE--ITGDQIVIAAGSRPYIPPAIADS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 190 EDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAV----EFLGHvggigIDMEISKNFQRILQKQgFKF 265
Cdd:TIGR03452 153 GVRYHTNEDIMRLPELPESLVIVGGGYIAAEFAHVFSALGTRVTIVnrstKLLRH-----LDEDISDRFTEIAKKK-WDI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 266 KLNTKVTGATKKSDGkidVSVEAASGgkaEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNTRFQTKIPNIFA 345
Cdd:TIGR03452 227 RLGRNVTAVEQDGDG---VTLTLDDG---STVTADVLLVATGRVPNGDLLDAEAAGVEVDEDGRIKVDEYGRTSARGVWA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 346 IGDVVAGPMLAHKAEDEGIICVEGMA--GGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEG--VEFKVGKFPFAANSR 421
Cdd:TIGR03452 301 LGDVSSPYQLKHVANAEARVVKHNLLhpNDLRKMPHDFVPSAVFTHPQIATVGLTEQEAREAGhdITVKIQNYGDVAYGW 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958782340 422 AKtnADTDGMVKILGHKSTDRILGAHILGPGAGEMVNEAALALEYGASCEDVARVCH-AHPTLSEAFREANLA 493
Cdd:TIGR03452 381 AM--EDTTGFCKLIADRDTGKLLGAHIIGPQASSLIQPLITAMAFGLDAREMARKQYwIHPALPEVVENALLG 451
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
20-487 |
2.46e-46 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 169.67 E-value: 2.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 20 ASSVPLRTYSDQPIDADVTVIGSGPGG---------YVAAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHY 90
Cdd:PLN02546 65 RAAAPNGAESERHYDFDLFTIGAGSGGvrasrfasnFGASAAVCELPFATISSDTLGGVGGTCVLRGCVPKKLLVYASKY 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 91 YHlahgkDF-ASRG---IEIPEVRLNLEKMMEQKRSAVKALTGGIAHLFKQNKVVHVNGFGKItgknqVTATTADGSTQV 166
Cdd:PLN02546 145 SH-----EFeESRGfgwKYETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKI-----VDPHTVDVDGKL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 167 IGTKNILIATGSEvtPF----PGItideDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAveFLGHVG 242
Cdd:PLN02546 215 YTARNILIAVGGR--PFipdiPGI----EHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHV--FIRQKK 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 243 GI-GIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGKIDVSVEAAS-GGKAEVitcdvlLVCIGRRPFTQNLGLEEL 320
Cdd:PLN02546 287 VLrGFDEEVRDFVAEQMSLRGIEFHTEESPQAIIKSADGSLSLKTNKGTvEGFSHV------MFATGRKPNTKNLGLEEV 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 321 GIELDPKGRIPVNTRFQTKIPNIFAIGDVVAGPMLAHKAEDEGIICVEGMAGG-AVHIDYNCVPSVIYTHPEVAWVGKSE 399
Cdd:PLN02546 361 GVKMDKNGAIEVDEYSRTSVPSIWAVGDVTDRINLTPVALMEGGALAKTLFGNePTKPDYRAVPSAVFSQPPIGQVGLTE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 400 EQLKEEGVEFKVgkfpFAANSRAkTNADTDGM-----VKILGHKSTDRILGAHILGPGAGEMVNEAALALEYGASCEDVA 474
Cdd:PLN02546 441 EQAIEEYGDVDV----FTANFRP-LKATLSGLpdrvfMKLIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFD 515
|
490
....*....|...
gi 1958782340 475 RVCHAHPTLSEAF 487
Cdd:PLN02546 516 ATVGIHPTAAEEF 528
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
14-487 |
7.52e-44 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 162.86 E-value: 7.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 14 SHGLQgASSVPLRTYSDQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKnETLGGTCLNVGCIPSKALLNNSHYYHL 93
Cdd:PTZ00058 29 YHNLE-ASSAPTHLKKKPRMVYDLIVIGGGSGGMAAARRAARNKAKVALVEK-DYLGGTCVNVGCVPKKIMFNAASIHDI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 94 AHgkDFASRGIEIPEVrLNLEKMMEQKRSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQV------------------ 155
Cdd:PTZ00058 107 LE--NSRHYGFDTQFS-FNLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVlikkvsqvdgeadesddd 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 156 ------TATTADGSTQVIGTKNILIATGSEvTPFPGITIDEDTIvSSTGALSLKKvPEKLVVIGAGVIGVELGSVWQRLG 229
Cdd:PTZ00058 184 evtivsAGVSQLDDGQVIEGKNILIAVGNK-PIFPDVKGKEFTI-SSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 230 ADvTAVEFLGHVGGIGIDMEISKNFQRILQKQGFKFKLNTKVTGATKksDGKIDVSVEAASGGKAEVITCdvLLVCIGRR 309
Cdd:PTZ00058 261 AE-SYIFARGNRLLRKFDETIINELENDMKKNNINIITHANVEEIEK--VKEKNLTIYLSDGRKYEHFDY--VIYCVGRS 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 310 PFTQNLGLEELGIeLDPKGRIPVNTRFQTKIPNIFAIGDVVAGP---------MLAHKAEDEGIICVEGMAGGAVH---- 376
Cdd:PTZ00058 336 PNTEDLNLKALNI-KTPKGYIKVDDNQRTSVKHIYAVGDCCMVKknqeiedlnLLKLYNEEPYLKKKENTSGESYYnvql 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 377 ----------------------IDYNCVPSVIYTHPEVAWVGKSEEQLKE------------EGVEFKVGKFPFAANSRA 422
Cdd:PTZ00058 415 tpvainagrlladrlfgpfsrtTNYKLIPSVIFSHPPIGTIGLSEQEAIDiygkenvkiyesRFTNLFFSVYDMDPAQKE 494
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958782340 423 KTnadtdgMVKILGHKSTDRILGAHILGPGAGEMVNEAALALEYGASCEDVARVCHAHPTLSEAF 487
Cdd:PTZ00058 495 KT------YLKLVCVGKEELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIHPTAAEEF 553
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
173-386 |
1.19e-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: 118.38 E-value: 1.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 173 LIATGSE--VTPFPGITIDedtivsstGALSLKKV--------------PEKLVVIGAGVIGVELGSVWQRLGADVTAVE 236
Cdd:COG0446 83 VLATGARprPPPIPGLDLP--------GVFTLRTLddadalrealkefkGKRAVVIGGGPIGLELAEALRKRGLKVTLVE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 237 FLGHVGGiGIDMEISKNFQRILQKQGFKFKLNTKVTGAtkksDGKIDVSVEAASGgkaEVITCDVLLVCIGRRPFTQnLg 316
Cdd:COG0446 155 RAPRLLG-VLDPEMAALLEEELREHGVELRLGETVVAI----DGDDKVAVTLTDG---EEIPADLVVVAPGVRPNTE-L- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 317 LEELGIELDPKGRIPVNTRFQTKIPNIFAIGDVV----------AGPMLAHKAEDEGIICVEGMAGGAvhIDYNCVPSVI 386
Cdd:COG0446 225 AKDAGLALGERGWIKVDETLQTSDPDVYAAGDCAevphpvtgktVYIPLASAANKQGRVAAENILGGP--APFPGLGTFI 302
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
36-354 |
1.33e-27 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 112.14 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 36 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNEtLGGTCLNVGCIpskallNNshYYHLAHGKdfasRGIEIpevrlnLEK 115
Cdd:COG0492 2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEGGE-PGGQLATTKEI------EN--YPGFPEGI----SGPEL------AER 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 116 MMEQ-KRSAVKALTGGIAHLFKQNKVVHVngfgkitgknqvtaTTADGSTqvIGTKNILIATGSEVT--PFPGITIDEDT 192
Cdd:COG0492 63 LREQaERFGAEILLEEVTSVDKDDGPFRV--------------TTDDGTE--YEAKAVIIATGAGPRklGLPGEEEFEGR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 193 IVSSTGALSLKKVP-EKLVVIGAGVIGVELGSVWQRLGADVTAVeflgHVGGigiDMEISKNFQ-RILQKQGFKFKLNTK 270
Cdd:COG0492 127 GVSYCATCDGFFFRgKDVVVVGGGDSALEEALYLTKFASKVTLI----HRRD---ELRASKILVeRLRANPKIEVLWNTE 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 271 VTGAtkKSDGKID-VSVEAASGGKAEVITCDVLLVCIGRRPftqNLGL-EELGIELDPKGRIPVNTRFQTKIPNIFAIGD 348
Cdd:COG0492 200 VTEI--EGDGRVEgVTLKNVKTGEEKELEVDGVFVAIGLKP---NTELlKGLGLELDEDGYIVVDEDMETSVPGVFAAGD 274
|
....*.
gi 1958782340 349 VVAGPM 354
Cdd:COG0492 275 VRDYKY 280
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
156-375 |
8.11e-23 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 100.22 E-value: 8.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 156 TATTADGSTqvIGTKNILIATGSE--VTPFPGI---------TIDE-DTIVSSTGAlslkkvPEKLVVIGAGVIGVELGS 223
Cdd:COG1251 88 TVTLADGET--LPYDKLVLATGSRprVPPIPGAdlpgvftlrTLDDaDALRAALAP------GKRVVVIGGGLIGLEAAA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 224 VWQRLGADVTAVEFLGHVGGIGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGKidvSVEAASGgkaEVITCDVLL 303
Cdd:COG1251 160 ALRKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVT---GVRLADG---EELPADLVV 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 304 VCIGRRPftqNLGL-EELGIELDpkGRIPVNTRFQTKIPNIFAIGDVVA-------GPMLAH--KAEDEGIICVEGMAGG 373
Cdd:COG1251 234 VAIGVRP---NTELaRAAGLAVD--RGIVVDDYLRTSDPDIYAAGDCAEhpgpvygRRVLELvaPAYEQARVAAANLAGG 308
|
..
gi 1958782340 374 AV 375
Cdd:COG1251 309 PA 310
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
172-464 |
1.17e-16 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 82.01 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 172 ILIATG--SEVTPFPGITIDE-DTIVSSTGALSLKKVPEK-----LVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGG 243
Cdd:PRK09564 107 LMIATGarPIIPPIKNINLENvYTLKSMEDGLALKELLKDeeiknIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRILP 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 244 IGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGKIDVSveaasgGKAEVITcDVLLVCIGRRPFTQnlGLEELGIE 323
Cdd:PRK09564 187 DSFDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEGVVT------DKGEYEA-DVVIVATGVKPNTE--FLEDTGLK 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 324 LDPKGRIPVNTRFQTKIPNIFAIGD-------VVAGPM---LAHKAEDEGIICVEGMAGGAVH----IDYNCVPSVIYth 389
Cdd:PRK09564 258 TLKNGAIIVDEYGETSIENIYAAGDcatiyniVSNKNVyvpLATTANKLGRMVGENLAGRHVSfkgtLGSACIKVLDL-- 335
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958782340 390 pEVAWVGKSEEQLKEEGVEFKVgKFPFAANSRAKTNADTDGMVKILGHKSTDRILGAHILGP-GAGEMVNEAALAL 464
Cdd:PRK09564 336 -EAARTGLTEEEAKKLGIDYKT-VFIKDKNHTNYYPGQEDLYVKLIYEADTKVILGGQIIGKkGAVLRIDALAVAI 409
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
208-281 |
3.12e-16 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 73.39 E-value: 3.12e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958782340 208 KLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGiGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGK 281
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLP-GFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGV 73
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
35-368 |
3.27e-16 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 80.18 E-value: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 35 ADVTVIGSGPGGYVAAIKAAQLGFKTVCIekneTLggtclnvgcIpSKallNNSHYY-HLAHGkdFASRGIEIPEVRLNL 113
Cdd:COG1252 2 KRIVIVGGGFAGLEAARRLRKKLGGDAEV----TL---------I-DP---NPYHLFqPLLPE--VAAGTLSPDDIAIPL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 114 EKMMEQKRsaVKaltggiahlFKQNKVVHVNgfgkiTGKNQVTatTADGST----QVIgtknilIATGSeVTPFPGIT-I 188
Cdd:COG1252 63 RELLRRAG--VR---------FIQGEVTGID-----PEARTVT--LADGRTlsydYLV------IATGS-VTNFFGIPgL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 189 DEDtivsstgALSLKKVPE---------------------KLVVIGAGVIGVEL-GSVWQRLG------------ADVTA 234
Cdd:COG1252 118 AEH-------ALPLKTLEDalalrerllaaferaerrrllTIVVVGGGPTGVELaGELAELLRkllrypgidpdkVRITL 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 235 VEFLGHVGGiGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSdgkidvsVEAASGgkaEVITCDVLLVCIGRR--PFT 312
Cdd:COG1252 191 VEAGPRILP-GLGEKLSEAAEKELEKRGVEVHTGTRVTEVDADG-------VTLEDG---EEIPADTVIWAAGVKapPLL 259
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958782340 313 QNLGLEelgieLDPKGRIPVNTRFQTK-IPNIFAIGDVVAG--------PMLAHKAEDEGIICVE 368
Cdd:COG1252 260 ADLGLP-----TDRRGRVLVDPTLQVPgHPNVFAIGDCAAVpdpdgkpvPKTAQAAVQQAKVLAK 319
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
189-350 |
4.60e-14 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 74.05 E-value: 4.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 189 DEDTIVSSTGALSLKKVPeklvVIGAGVIGVE-LGSVWQRlGADVTAVEFLGHVGGIgIDMEISKNFQRILQKQGFKFKL 267
Cdd:PRK13512 135 DTDAIDQFIKANQVDKAL----VVGAGYISLEvLENLYER-GLHPTLIHRSDKINKL-MDADMNQPILDELDKREIPYRL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 268 NTKVTgatkksdgKIDVSVEAASGGKAEviTCDVLLVCIGRRPFTQNLglEELGIELDPKGRIPVNTRFQTKIPNIFAIG 347
Cdd:PRK13512 209 NEEID--------AINGNEVTFKSGKVE--HYDMIIEGVGTHPNSKFI--ESSNIKLDDKGFIPVNDKFETNVPNIYAIG 276
|
...
gi 1958782340 348 DVV 350
Cdd:PRK13512 277 DII 279
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
174-348 |
7.94e-14 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 73.03 E-value: 7.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 174 IATGSE--VTPFPGitiDEDTIV--------SSTGALSLKKvpeKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGG 243
Cdd:PRK04965 105 LATGASafVPPIPG---RELMLTlnsqqeyrAAETQLRDAQ---RVLVVGGGLIGTELAMDLCRAGKAVTLVDNAASLLA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 244 IGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGkidVSVEAASGgkaEVITCDVLLVCIGRRPftqNLGL-EELGI 322
Cdd:PRK04965 179 SLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSG---IRATLDSG---RSIEVDAVIAAAGLRP---NTALaRRAGL 249
|
170 180
....*....|....*....|....*.
gi 1958782340 323 ELDpKGrIPVNTRFQTKIPNIFAIGD 348
Cdd:PRK04965 250 AVN-RG-IVVDSYLQTSAPDIYALGD 273
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
291-363 |
8.74e-13 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 69.63 E-value: 8.74e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958782340 291 GGKAEVITCDVLLVCIGRRPfTQNLGLEELGIELDPKGRIPVNTRFQTKIPNIFAIGDVVAGPMLAHKAEDEG 363
Cdd:PRK12770 267 PGSEFVLEADTVVFAIGEIP-TPPFAKECLGIELNRKGEIVVDEKHMTSREGVFAAGDVVTGPSKIGKAIKSG 338
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
37-378 |
1.09e-11 |
|
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 440259 [Multi-domain] Cd Length: 434 Bit Score: 66.70 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 37 VTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTclnvgcipskallnnshyyhLAHGkdfasrgieIPEVRLNlEKM 116
Cdd:COG0493 124 VAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGGL--------------------LRYG---------IPEFRLP-KDV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 117 MEQKRSAVKALtgGIAhlFKQNKVVhvngfgkitGKNqVTATT------AdgstqvigtknILIATGSEV---TPFPGIt 187
Cdd:COG0493 174 LDREIELIEAL--GVE--FRTNVEV---------GKD-ITLDElleefdA-----------VFLATGAGKprdLGIPGE- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 188 iDEDTIVS----------STGALSLKKVPEKLVVIGAG-----VIGVELgsvwqRLGA-DVTAVEFLGHVggigiDM--- 248
Cdd:COG0493 228 -DLKGVHSamdfltavnlGEAPDTILAVGKRVVVIGGGntamdCARTAL-----RLGAeSVTIVYRRTRE-----EMpas 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 249 --EISKnfqriLQKQGFKFKLNTKVTGATKKSDG--------KIDVSVEAASG--------GKAEVITCDVLLVCIGRRP 310
Cdd:COG0493 297 keEVEE-----ALEEGVEFLFLVAPVEIIGDENGrvtglecvRMELGEPDESGrrrpvpieGSEFTLPADLVILAIGQTP 371
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958782340 311 FTQNLgLEELGIELDPKGRIPVNTR-FQTKIPNIFAIGDVVAGPMLAhkaedegiicVEGMAGG---AVHID 378
Cdd:COG0493 372 DPSGL-EEELGLELDKRGTIVVDEEtYQTSLPGVFAGGDAVRGPSLV----------VWAIAEGrkaARAID 432
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
172-349 |
6.13e-11 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 64.18 E-value: 6.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 172 ILIATGSEVTPFPGI-TIDED--TIVSSTGALSLKKV--PEKLVVI-GAGVIGVELGSVWQRLGADVTAVEFLGHVGGIG 245
Cdd:PRK09754 104 LFIATGAAARPLPLLdALGERcfTLRHAGDAARLREVlqPERSVVIvGAGTIGLELAASATQRRCKVTVIELAATVMGRN 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 246 IDMEISKNFQRILQKQGFKFKLNTKVTGATKKSdgkiDVSVEAASGgkaEVITCDVLLVCIGRRpFTQNLGLEElgiELD 325
Cdd:PRK09754 184 APPPVQRYLLQRHQQAGVRILLNNAIEHVVDGE----KVELTLQSG---ETLQADVVIYGIGIS-ANDQLAREA---NLD 252
|
170 180
....*....|....*....|....
gi 1958782340 326 PKGRIPVNTRFQTKIPNIFAIGDV 349
Cdd:PRK09754 253 TANGIVIDEACRTCDPAIFAGGDV 276
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
156-351 |
1.21e-10 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 64.08 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 156 TATTADGSTQVIGTK--------NILIATGSE--VTPFPGI---------TIDE-DTIvsstgaLSLKKVPEKLVVIGAG 215
Cdd:TIGR02374 76 TVIQIDTDQKQVITDagrtlsydKLILATGSYpfILPIPGAdkkgvyvfrTIEDlDAI------MAMAQRFKKAAVIGGG 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 216 VIGVELGSVWQRLGADVTAVEFLGHVGGIGIDMEISKNFQRILQKQGFKFKLNTKVTGATKksDGKIDvSVEAASGgkaE 295
Cdd:TIGR02374 150 LLGLEAAVGLQNLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVG--ATKAD-RIRFKDG---S 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958782340 296 VITCDVLLVCIGRRPFTqnlgleELGIE--LDPKGRIPVNTRFQTKIPNIFAIGDVVA 351
Cdd:TIGR02374 224 SLEADLIVMAAGIRPND------ELAVSagIKVNRGIIVNDSMQTSDPDIYAVGECAE 275
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
295-370 |
7.30e-08 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 54.78 E-value: 7.30e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782340 295 EVITCDVLLVCIGRRPFTQNLgLEELGIELDPKGRIPVNTR-FQTKIPNIFAIGDVVAGPMLAHKAEDEGIICVEGM 370
Cdd:PRK12810 385 FVLPADLVLLAMGFTGPEAGL-LAQFGVELDERGRVAAPDNaYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAI 460
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
20-361 |
2.61e-07 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 53.23 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 20 ASSVPLRTYS---DQPI---DADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTcLNVGcIPSKALLNNshyyhl 93
Cdd:PRK13984 263 VDNVPVEKYSeilDDEPekkNKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGV-MRYG-IPSYRLPDE------ 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 94 AHGKDFA---SRGIEI-PEVRLNLEKMMEQKRsavkaltggiahlfKQNKVVHVN-GFGKitGKnqvtattadgSTQVIG 168
Cdd:PRK13984 335 ALDKDIAfieALGVKIhLNTRVGKDIPLEELR--------------EKHDAVFLStGFTL--GR----------STRIPG 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 169 T--KNILIAtgsevtpfpgITIDEDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLG------ADVTAV----- 235
Cdd:PRK13984 389 TdhPDVIQA----------LPLLREIRDYLRGEGPKPKIPRSLVVIGGGNVAMDIARSMARLQkmeygeVNVKVTslert 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 236 --EFLGHVGGI------GIDMEISKNFQRIL----QKQGFKFKLNTKVTGATKKSDGKIDVSVEAasggkaeVITCDVLL 303
Cdd:PRK13984 459 feEMPADMEEIeegleeGVVIYPGWGPMEVViendKVKGVKFKKCVEVFDEEGRFNPKFDESDQI-------IVEADMVV 531
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958782340 304 VCIGRRPFTQNLGlEELGIELD-PKGRIPVNTRFQTKIPNIFAIGDVVAGPMLAHKAED 361
Cdd:PRK13984 532 EAIGQAPDYSYLP-EELKSKLEfVRGRILTNEYGQTSIPWLFAGGDIVHGPDIIHGVAD 589
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
33-177 |
3.35e-07 |
|
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: 52.53 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 33 IDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT------CLNVGCIP-SKALLNNS---HYYHLAHGKD---- 98
Cdd:COG1053 2 HEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGGHtaaaqgGINAAGTNvQKAAGEDSpeeHFYDTVKGGDglad 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 99 ------FASRGIEI--------------PEVRLNLEKMMEQKRSAVKALTGG---IAHLFKQNK----VVHVNGF----- 146
Cdd:COG1053 82 qdlveaLAEEAPEAidwleaqgvpfsrtPDGRLPQFGGHSVGRTCYAGDGTGhalLATLYQAALrlgvEIFTETEvldli 161
|
170 180 190
....*....|....*....|....*....|....
gi 1958782340 147 ---GKITGknqVTATTADGSTQVIGTKNILIATG 177
Cdd:COG1053 162 vddGRVVG---VVARDRTGEIVRIRAKAVVLATG 192
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
24-72 |
6.81e-07 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 52.03 E-value: 6.81e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1958782340 24 PLRTYSDQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 72
Cdd:PRK06134 2 PSAAAYPPDLECDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGGT 50
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
36-71 |
6.94e-07 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 51.77 E-value: 6.94e-07
10 20 30
....*....|....*....|....*....|....*.
gi 1958782340 36 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGG 71
Cdd:COG1233 5 DVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
36-72 |
7.08e-07 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 51.46 E-value: 7.08e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1958782340 36 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 72
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGM 37
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
37-352 |
1.46e-06 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 50.56 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 37 VTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGtcLNVGCIPSkallnnshyYHLAhgKDFASRGIEipevrlNLEKM 116
Cdd:PRK11749 143 VAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG--LLRYGIPE---------FRLP--KDIVDREVE------RLLKL 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 117 meqkrsavkaltgGIAhlFKQNKVVhvngfgkitGKNqvtaTTADGSTQviGTKNILIATGSEVTPF---PGIT------ 187
Cdd:PRK11749 204 -------------GVE--IRTNTEV---------GRD----ITLDELRA--GYDAVFIGTGAGLPRFlgiPGENlggvys 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 188 -IDEDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGA-DVTAVEFLGHVggigiDMEISKNFQRILQKQGFKF 265
Cdd:PRK11749 254 aVDFLTRVNQAVADYDLPVGKRVVVIGGGNTAMDAARTAKRLGAeSVTIVYRRGRE-----EMPASEEEVEHAKEEGVEF 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 266 KLNTK---VTGatkksDGKIDVSVEA---------ASG-------GKAEVITCDVLLVCIGRRPFTQNLGLEElGIELDP 326
Cdd:PRK11749 329 EWLAApveILG-----DEGRVTGVEFvrmelgepdASGrrrvpieGSEFTLPADLVIKAIGQTPNPLILSTTP-GLELNR 402
|
330 340
....*....|....*....|....*..
gi 1958782340 327 KG-RIPVNTRFQTKIPNIFAIGDVVAG 352
Cdd:PRK11749 403 WGtIIADDETGRTSLPGVFAGGDIVTG 429
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
36-85 |
2.06e-06 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 49.86 E-value: 2.06e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1958782340 36 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNetlGGTCLNVGCIPSKALL 85
Cdd:pfam01134 1 DVIVIGGGHAGCEAALAAARMGAKVLLITHN---TDTIAELSCNPSIGGI 47
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
31-72 |
6.70e-06 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 48.54 E-value: 6.70e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1958782340 31 QPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 72
Cdd:PRK12842 6 NELTCDVLVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGGT 47
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
36-72 |
1.16e-05 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 47.72 E-value: 1.16e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1958782340 36 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 72
Cdd:PRK07843 9 DVVVVGSGAAGMVAALTAAHRGLSTVVVEKAPHYGGS 45
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
36-72 |
1.19e-05 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 47.67 E-value: 1.19e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1958782340 36 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 72
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGA 37
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
210-363 |
1.21e-05 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 47.45 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 210 VVIGAGVIGVELGSVWQRLGAD--------------VTAVEFLGHVGGiGIDMEISKNFQRILQKQGFKFKLNTKVTGAT 275
Cdd:PTZ00318 177 VVVGGGPTGVEFAAELADFFRDdvrnlnpelveeckVTVLEAGSEVLG-SFDQALRKYGQRRLRRLGVDIRTKTAVKEVL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 276 KKSdgkidvsVEAASGgkaEVITCDVLL--VCIGRRPFTQNLGleelgIELDPKGRIPVNTRFQTK-IPNIFAIGDVVAG 352
Cdd:PTZ00318 256 DKE-------VVLKDG---EVIPTGLVVwsTGVGPGPLTKQLK-----VDKTSRGRISVDDHLRVKpIPNVFALGDCAAN 320
|
170
....*....|....*.
gi 1958782340 353 -----PMLAHKAEDEG 363
Cdd:PTZ00318 321 eerplPTLAQVASQQG 336
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
29-71 |
1.40e-05 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 47.52 E-value: 1.40e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1958782340 29 SDQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGG 71
Cdd:PRK12839 3 PSMTHTYDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKASTCGG 45
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
29-72 |
3.00e-05 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 46.65 E-value: 3.00e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1958782340 29 SDQPIDA--DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 72
Cdd:PRK12843 9 SPERWDAefDVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGT 54
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
39-73 |
4.29e-05 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 41.36 E-value: 4.29e-05
10 20 30
....*....|....*....|....*....|....*
gi 1958782340 39 VIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTC 73
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNA 35
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
20-177 |
6.02e-05 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 45.62 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 20 ASSVPLRTYSdQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGtclnvgcipsKAllnnSHYYHLAHGKDF 99
Cdd:COG1148 127 KLLEPLEPIK-VPVNKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGG----------RA----AQLHKTFPGLDC 191
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958782340 100 ASrgieipevrlnleKMMEQKRSAVKAlTGGIaHLFKQNKVVHVNGFGkitGKNQVTATTADGSTQVIGTKNILIATG 177
Cdd:COG1148 192 PQ-------------CILEPLIAEVEA-NPNI-TVYTGAEVEEVSGYV---GNFTVTIKKGPREEIEIEVGAIVLATG 251
|
|
| PRK12835 |
PRK12835 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
36-79 |
6.52e-05 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237221 [Multi-domain] Cd Length: 584 Bit Score: 45.57 E-value: 6.52e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1958782340 36 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGG-TCLNVGCI 79
Cdd:PRK12835 13 DVLVVGSGGGGMTAALTAAARGLDTLVVEKSAHFGGsTALSGGGI 57
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
36-72 |
2.11e-04 |
|
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];
Pssm-ID: 441675 [Multi-domain] Cd Length: 414 Bit Score: 43.70 E-value: 2.11e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1958782340 36 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 72
Cdd:COG2072 8 DVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGT 44
|
|
| PRK12844 |
PRK12844 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
35-72 |
2.13e-04 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 183787 [Multi-domain] Cd Length: 557 Bit Score: 43.97 E-value: 2.13e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1958782340 35 ADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 72
Cdd:PRK12844 7 YDVVVVGSGGGGMCAALAAADSGLEPLIVEKQDKVGGS 44
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
37-363 |
2.34e-04 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 43.95 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 37 VTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTclnvgcipskallnnshyyhLAHGkdfasrgieIPEVRLNlEKM 116
Cdd:PRK12814 196 VAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGM--------------------MRYG---------IPRFRLP-ESV 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 117 MEQKRSAVKALTGGiahlFKQNKVvhvngFGK-ITGKNQVTATTAdgstqvigtknILIATGSEVTPFPGITIDEDTIVS 195
Cdd:PRK12814 246 IDADIAPLRAMGAE----FRFNTV-----FGRdITLEELQKEFDA-----------VLLAVGAQKASKMGIPGEELPGVI 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 196 StGALSLKKVPE--------KLVVIGAGVIGVELGSVWQRLGAdvTAVEFLGHVGgigiDMEISKNFQRILQ--KQGFKF 265
Cdd:PRK12814 306 S-GIDFLRNVALgtalhpgkKVVVIGGGNTAIDAARTALRLGA--ESVTILYRRT----REEMPANRAEIEEalAEGVSL 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 266 KLNTKVTgATKKSDGKIDVSVEA-------ASGGKAEV--------ITCDVLLVCIGRRpftQNLGLEEL-GIELDPKGR 329
Cdd:PRK12814 379 RELAAPV-SIERSEGGLELTAIKmqqgepdESGRRRPVpvegseftLQADTVISAIGQQ---VDPPIAEAaGIGTSRNGT 454
|
330 340 350
....*....|....*....|....*....|....*
gi 1958782340 330 IPVN-TRFQTKIPNIFAIGDVVAGPMLAHKAEDEG 363
Cdd:PRK12814 455 VKVDpETLQTSVAGVFAGGDCVTGADIAINAVEQG 489
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
36-70 |
2.64e-04 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 43.34 E-value: 2.64e-04
10 20 30
....*....|....*....|....*....|....*
gi 1958782340 36 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLG 70
Cdd:pfam03486 2 DVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
210-348 |
3.63e-04 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 43.18 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 210 VVIGAGVIGVELGSVWQRLGADVTAVEF--------LGHVGG---------IGIDMEISKNFQRILQkQGfkfklntkvT 272
Cdd:PRK14989 149 AVVGGGLLGLEAAGALKNLGVETHVIEFapmlmaeqLDQMGGeqlrrkiesMGVRVHTSKNTLEIVQ-EG---------V 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958782340 273 GATKksdgkidvSVEAASGGKAEVitcDVLLVCIGRRPftQNLGLEELGIELDPKGRIPVNTRFQTKIPNIFAIGD 348
Cdd:PRK14989 219 EARK--------TMRFADGSELEV---DFIVFSTGIRP--QDKLATQCGLAVAPRGGIVINDSCQTSDPDIYAIGE 281
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
317-371 |
1.07e-03 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 41.66 E-value: 1.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958782340 317 LEELGIELDPKGRIPVNT----RFQTKIPNIFAIGDVVAGPMLAHKAEDEGIICVEGMA 371
Cdd:PRK12769 590 LESHGVTVDKWGRIIADVesqyRYQTSNPKIFAGGDAVRGADLVVTAMAEGRHAAQGII 648
|
|
| LhgO |
COG0579 |
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism]; |
242-332 |
1.70e-03 |
|
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
Pssm-ID: 440344 [Multi-domain] Cd Length: 418 Bit Score: 40.90 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782340 242 GGIgID-MEISKNFQRILQKQGFKFKLNTKVTGATKKSDGkidVSVEAASGgkaeVITCDVLLVCIGrrpftqnLG---- 316
Cdd:COG0579 147 TGI-VDpGALTRALAENAEANGVELLLNTEVTGIEREGDG---WEVTTNGG----TIRARFVINAAG-------LYadrl 211
|
90
....*....|....*.
gi 1958782340 317 LEELGIELDPKGrIPV 332
Cdd:COG0579 212 AQMAGIGKDFGI-FPV 226
|
|
| PRK07494 |
PRK07494 |
UbiH/UbiF family hydroxylase; |
31-63 |
3.41e-03 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181001 [Multi-domain] Cd Length: 388 Bit Score: 39.89 E-value: 3.41e-03
10 20 30
....*....|....*....|....*....|...
gi 1958782340 31 QPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCI 63
Cdd:PRK07494 4 EKEHTDIAVIGGGPAGLAAAIALARAGASVALV 36
|
|
| |
