|
Name |
Accession |
Description |
Interval |
E-value |
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
40-453 |
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: 539.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 40 IDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKnETLGGTCLNVGCIPSKALLNNSHYYHMAhgKDFASRGIEMSEVRLN 119
Cdd:COG1249 2 KDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEK-GRLGGTCLNVGCIPSKALLHAAEVAHEA--RHAAEFGISAGAPSVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 120 LDKMMEQKSTAVKALTGGIAHLFKQNKI--------------------------------------------DEDTIVSS 155
Cdd:COG1249 79 WAALMARKDKVVDRLRGGVEELLKKNGVdvirgrarfvdphtvevtggetltadhiviatgsrprvppipglDEVRVLTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 156 TGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGvGIDMEISKNFQRILQKQGFKFKLNTKVTGATK 235
Cdd:COG1249 159 DEALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLP-GEDPEISEALEKALEKEGIDILTGAKVTSVEK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 236 KSDGkidVSIEAASGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPMLA 315
Cdd:COG1249 238 TGDG---VTVTLEDGGGEEAVEADKVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRTSVPGIYAIGDVTGGPQLA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 316 HKAEDEGIICVEGMAGGAVH-IDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMVKIL 394
Cdd:COG1249 315 HVASAEGRVAAENILGKKPRpVDYRAIPSVVFTDPEIASVGLTEEEAREAGIDVKVGKFPFAANGRALALGETEGFVKLI 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 576583544 395 GQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAA 453
Cdd:COG1249 395 ADAETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAALAL 453
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
43-461 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 524.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIE--KNET----LGGTCLNVGCIPSKALLNNSHYYHMAhGKDFASRGIEMSEV 116
Cdd:PRK06327 6 DVVVIGAGPGGYVAAIRAAQLGLKVACIEawKNPKgkpaLGGTCLNVGCIPSKALLASSEEFENA-GHHFADHGIHVDGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 117 RLNLDKMMEQKSTAVKALTGGIAHLFKQNKI------------------------------------------------- 147
Cdd:PRK06327 85 KIDVAKMIARKDKVVKKMTGGIEGLFKKNKItvlkgrgsfvgktdagyeikvtgedetvitakhviiatgseprhlpgvp 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 148 -DEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHVggvgiDMEISKNFQRILQKQGF 222
Cdd:PRK06327 165 fDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEalpaFLAAA-----DEQVAKEAAKAFTKQGL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 223 KFKLNTKVtGATKKSDGKIDVSIEAASGgKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNI 302
Cdd:PRK06327 240 DIHLGVKI-GEIKTGGKGVSVAYTDADG-EAQTLEVDKLIVSIGRVPNTDGLGLEAVGLKLDERGFIPVDDHCRTNVPNV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 303 YAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAK 382
Cdd:PRK06327 318 YAIGDVVRGPMLAHKAEEEGVAVAERIAGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLKAEGVEYKAGKFPFMANGRAL 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 576583544 383 TNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAASfGKSINF 461
Cdd:PRK06327 398 AMGEPDGFVKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEVWHEAALAVD-KRPLHF 475
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
43-460 |
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: 514.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKnETLGGTCLNVGCIPSKALLNNSHYYH-MAHGKDFasrGIEMSEVRLNLD 121
Cdd:TIGR01350 3 DVIVIGGGPGGYVAAIRAAQLGLKVALVEK-EYLGGTCLNVGCIPTKALLHSAEVYDeIKHAKDL---GIEVENVSVDWE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 122 KMMEQKSTAVKALTGGIAHLFKQNKI------------------------------------------------DEDTIV 153
Cdd:TIGR01350 79 KMQKRKNKVVKKLVGGVSGLLKKNKVtvikgeakfldpgtvsvtgengeetleakniiiatgsrprslpgpfdfDGKVVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 154 SSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGvGIDMEISKNFQRILQKQGFKFKLNTKVTGA 233
Cdd:TIGR01350 159 TSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILP-GEDAEVSKVLQKALKKKGVKILTNTKVTAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 234 TKKSDGkidVSIEAaSGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPM 313
Cdd:TIGR01350 238 EKNDDQ---VTYEN-KGGETETLTGEKVLVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDVIGGPM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 314 LAHKAEDEGIICVEGMAGGA-VHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMVK 392
Cdd:TIGR01350 314 LAHVASHEGIVAAENIAGKEpAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGYDVKIGKFPFAANGKALALGETDGFVK 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 576583544 393 ILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAAsFGKSIN 460
Cdd:TIGR01350 394 IIADKKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEAIKEAALAA-LGKPIH 460
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
40-455 |
4.33e-173 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 493.54 E-value: 4.33e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 40 IDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKnETLGGTCLNVGCIPSKALLNNSHYYHMAhgKDFASRGIEMSEVRLN 119
Cdd:PRK06292 2 EKYDVIVIGAGPAGYVAARRAAKLGKKVALIEK-GPLGGTCLNVGCIPSKALIAAAEAFHEA--KHAEEFGIHADGPKID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 120 LDKMMEQKSTAVKALTGGIAH-LFKQNKID--------------------------------------------EDTIVS 154
Cdd:PRK06292 79 FKKVMARVRRERDRFVGGVVEgLEKKPKIDkikgtarfvdpntvevngerieakniviatgsrvppipgvwlilGDRLLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 155 STGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGvGIDMEISKNFQRILQKQgFKFKLNTKVTGAT 234
Cdd:PRK06292 159 SDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILP-LEDPEVSKQAQKILSKE-FKIKLGAKVTSVE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 235 KKSDGKIDVSIEaasGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPML 314
Cdd:PRK06292 237 KSGDEKVEELEK---GGKTETIEADYVLVATGRRPNTDGLGLENTGIELDERGRPVVDEHTQTSVPGIYAAGDVNGKPPL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 315 AHKAEDEGIICVEGMAGG-AVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMVKI 393
Cdd:PRK06292 314 LHEAADEGRIAAENAAGDvAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEVPFEAQGRARVMGKNDGFVKV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 576583544 394 LGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAASF 455
Cdd:PRK06292 394 YADKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRTALRDLFS 455
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
38-461 |
1.05e-171 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 490.04 E-value: 1.05e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 38 QPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKnETLGGTCLNVGCIPSKALLNNSHYYH-MAHGKDFasrGIEMSEV 116
Cdd:PRK06416 1 FAFEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEK-EKLGGTCLNRGCIPSKALLHAAERADeARHSEDF---GIKAENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 117 RLNLDKMMEQKSTAVKALTGGIAHLFKQNKI-----------------------------------------------DE 149
Cdd:PRK06416 77 GIDFKKVQEWKNGVVNRLTGGVEGLLKKNKVdiirgeaklvdpntvrvmtedgeqtytakniilatgsrprelpgieiDG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 150 DTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGvGIDMEISKNFQRILQKQGFKFKLNTK 229
Cdd:PRK06416 157 RVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILP-GEDKEISKLAERALKKRGIKIKTGAK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 230 VTGATKKSDGkIDVSIEAasGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDpRGRIPVNTRFQTKIPNIYAIGDVV 309
Cdd:PRK06416 236 AKKVEQTDDG-VTVTLED--GGKEETLEADYVLVAVGRRPNTENLGLEELGVKTD-RGFIEVDEQLRTNVPNIYAIGDIV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 310 AGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDG 389
Cdd:PRK06416 312 GGPMLAHKASAEGIIAAEAIAGNPHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFDVKVVKFPFAGNGKALALGETDG 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 576583544 390 MVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAASfGKSINF 461
Cdd:PRK06416 392 FVKLIFDKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEALGEAALAAA-GKPLHA 462
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
43-459 |
1.34e-93 |
|
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: 290.86 E-value: 1.34e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNeTLGGTCLNVGCIPSKALLNNSHYYHMAHGkdfASRGIEMSEVRLNLDK 122
Cdd:TIGR02053 2 DLVIIGSGAAAFAAAIKAAELGASVAMVERG-PLGGTCVNVGCVPSKMLLRAAEVAHYARK---PPFGGLAATVAVDFGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 123 MMEQKSTAVKALTG----------------GIAHlFKQNKI-------------------------------DEDTIVSS 155
Cdd:TIGR02053 78 LLEGKREVVEELRHekyedvlssygvdylrGRAR-FKDPKTvkvdlgrevrgakrfliatgarpaippipglKEAGYLTS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 156 TGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHvggvgIDMEISKNFQRILQKQGFKFKLNTKVT 231
Cdd:TIGR02053 157 EEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQrsdrLLPR-----EEPEISAAVEEALAEEGIEVVTSAQVK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 232 GATKKSDGKIDVSIEAASGGKAEVitcDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAG 311
Cdd:TIGR02053 232 AVSVRGGGKIITVEKPGGQGEVEA---DELLVATGRRPNTDGLGLEKAGVKLDERGGILVDETLRTSNPGIYAAGDVTGG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 312 PMLAHKAEDEGIICVEGMAGGA-VHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGM 390
Cdd:TIGR02053 309 LQLEYVAAKEGVVAAENALGGAnAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNVPRARINRDTRGF 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 576583544 391 VKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREAnlAASFGKSI 459
Cdd:TIGR02053 389 IKLVAEPGTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGLKLA--AQTFYRDV 455
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
43-455 |
2.37e-93 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 290.18 E-value: 2.37e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNEtLGGTCLNVGCIPSKALLNNSHYYHMA-HGKDFasrGIEMS-EVRLNL 120
Cdd:PRK06370 7 DAIVIGAGQAGPPLAARAAGLGMKVALIERGL-LGGTCVNTGCVPTKTLIASARAAHLArRAAEY---GVSVGgPVSVDF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 121 DKMMEQKSTAVKALTGGIAHLFKQNK-----------IDEDT------------IVSSTGA------------------- 158
Cdd:PRK06370 83 KAVMARKRRIRARSRHGSEQWLRGLEgvdvfrgharfESPNTvrvggetlrakrIFINTGAraaippipgldevgyltne 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 159 --LSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGvGIDMEISKNFQRILQKQGFKFKLNTKVTGATKK 236
Cdd:PRK06370 163 tiFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLP-REDEDVAAAVREILEREGIDVRLNAECIRVERD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 237 SDGKIdvsIEAASGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPMLAH 316
Cdd:PRK06370 242 GDGIA---VGLDCNGGAPEITGSHILVAVGRVPNTDDLGLEAAGVETDARGYIKVDDQLRTTNPGIYAAGDCNGRGAFTH 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 317 KAEDEGIICVEGMA-GGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMVKILG 395
Cdd:PRK06370 319 TAYNDARIVAANLLdGGRRKVSDRIVPYATYTDPPLARVGMTEAEARKSGRRVLVGTRPMTRVGRAVEKGETQGFMKVVV 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 396 QKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFReaNLAASF 455
Cdd:PRK06370 399 DADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIP--TLAQAL 456
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
38-453 |
6.11e-88 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 275.88 E-value: 6.11e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 38 QPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKAL---------LNNSHYYHMAHGKdfas 108
Cdd:PRK05249 2 HMYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGGGCTHTGTIPSKALreavlrligFNQNPLYSSYRVK---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 109 RGIEMSEVRLNLDKMMEQKstaVKALTG-----------GIAHLFKQNKI------------------------------ 147
Cdd:PRK05249 78 LRITFADLLARADHVINKQ---VEVRRGqyernrvdliqGRARFVDPHTVevecpdgevetltadkiviatgsrpyrppd 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 148 ---DEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVE-------FLghvggvgiDMEISKNFQRIL 217
Cdd:PRK05249 155 vdfDHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINtrdrllsFL--------DDEISDALSYHL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 218 QKQGFKFKLNTKVTGATKKSDGKIdvsIEAASGGKaevITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQT 297
Cdd:PRK05249 227 RDSGVTIRHNEEVEKVEGGDDGVI---VHLKSGKK---IKADCLLYANGRTGNTDGLNLENAGLEADSRGQLKVNENYQT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 298 KIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAA 377
Cdd:PRK05249 301 AVPHIYAVGDVIGFPSLASASMDQGRIAAQHAVGEATAHLIEDIPTGIYTIPEISSVGKTEQELTAAKVPYEVGRARFKE 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 576583544 378 NSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAA 453
Cdd:PRK05249 381 LARAQIAGDNVGMLKILFHRETLEILGVHCFGERATEIIHIGQAIMEQKGTIEYFVNTTFNYPTMAEAYRVAALDG 456
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
41-446 |
1.60e-69 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 227.73 E-value: 1.60e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 41 DADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNEtLGGTCLNVGCIPSKALLNNSHYYHMAH--GKDFasrGIEMSEVRL 118
Cdd:PRK06116 4 DYDLIVIGGGSGGIASANRAAMYGAKVALIEAKR-LGGTCVNVGCVPKKLMWYGAQIAEAFHdyAPGY---GFDVTENKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 119 NLDKMMEQKSTAVKALTGGIAHLFKQNK----------IDEDTI-------------------------------VSSTG 157
Cdd:PRK06116 80 DWAKLIANRDAYIDRLHGSYRNGLENNGvdliegfarfVDAHTVevngerytadhiliatggrpsipdipgaeygITSDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 158 ALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAV----EFLGhvggvGIDMEISKNFQRILQKQGFKFKLNTKVTGA 233
Cdd:PRK06116 160 FFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFvrgdAPLR-----GFDPDIRETLVEEMEKKGIRLHTNAVPKAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 234 TKKSDGKIDVSIEaasggKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPM 313
Cdd:PRK06116 235 EKNADGSLTLTLE-----DGETLTVDCLIWAIGREPNTDGLGLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGDVTGRVE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 314 LAHKAEDEGIICVEGMAGG--AVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEY--KVGKFPFAANSRAKTNADTDG 389
Cdd:PRK06116 310 LTPVAIAAGRRLSERLFNNkpDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDnvKVYRSSFTPMYTALTGHRQPC 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 576583544 390 MVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAF 446
Cdd:PRK06116 390 LMKLVVVGKEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEF 446
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
43-454 |
6.32e-63 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 215.55 E-value: 6.32e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNE-TLGGTCLNVGCIPSKALL----------NNSHYYHMA-------HGK 104
Cdd:PTZ00153 118 DVGIIGCGVGGHAAAINAMERGLKVIIFTGDDdSIGGTCVNVGCIPSKALLyatgkyrelkNLAKLYTYGiytnafkNGK 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 105 DFASRGIEM--SEVRLNLDKMMEQKSTAVKALTGGIAHLFKQNKI----------------------------------- 147
Cdd:PTZ00153 198 NDPVERNQLvaDTVQIDITKLKEYTQSVIDKLRGGIENGLKSKKFcknsehvqviyerghivdkntikseksgkefkvkn 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 148 -----------------DEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGvGIDMEIS 210
Cdd:PTZ00153 278 iiiatgstpnipdnievDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSPQLLP-LLDADVA 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 211 KNFQRILQK-QGFKFKLNTKVT-------------GATKKSDGKIDVSIEAASGGKAevITCDVLLVCIGRRPFTKNLGL 276
Cdd:PTZ00153 357 KYFERVFLKsKPVRVHLNTLIEyvragkgnqpviiGHSERQTGESDGPKKNMNDIKE--TYVDSCLVATGRKPNTNNLGL 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 277 EELGIELDpRGRIPVNTRFQTK------IPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVH-------------ID 337
Cdd:PTZ00153 435 DKLKIQMK-RGFVSVDEHLRVLredqevYDNIFCIGDANGKQMLAHTASHQALKVVDWIEGKGKEnvninvenwaskpII 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 338 YNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFP--FAANSRA----------------------KTNADTDGMVKI 393
Cdd:PTZ00153 514 YKNIPSVCYTTPELAFIGLTEKEAKELYPPDNVGVEIsfYKANSKVlcennisfpnnsknnsynkgkyNTVDNTEGMVKI 593
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 576583544 394 LGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAAS 454
Cdd:PTZ00153 594 VYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDAAFKAIA 654
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
43-322 |
2.54e-60 |
|
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: 199.08 E-value: 2.54e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEknetLGGTCLNVGCIPSKALLNNSHYYH-MAHGKDFASR----------GI 111
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIE----DEGTCPYGGCVLSKALLGAAEAPEiASLWADLYKRkeevvkklnnGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 112 EM-------------SEVRLNLDKMMEQKSTAVKAL---TGGIAHLF-----KQNKIDEDTIVSSTGALSLKKVPEKMVV 170
Cdd:pfam07992 78 EVllgtevvsidpgaKKVVLEELVDGDGETITYDRLviaTGARPRLPpipgvELNVGFLVRTLDSAEALRLKLLPKRVVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 171 IGAGVIGVELGSVWQRLGADVTAVEFLGHVGGvGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGKidvsieAASG 250
Cdd:pfam07992 158 VGGGYIGVELAAALAKLGKEVTLIEALDRLLR-AFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGV------EVIL 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 576583544 251 GKAEVITCDVLLVCIGRRPftKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDV-VAGPMLAHKAEDEG 322
Cdd:pfam07992 231 KDGTEIDADLVVVAIGRRP--NTELLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDCrVGGPELAQNAVAQG 301
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
43-446 |
2.29e-59 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 200.75 E-value: 2.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETL-GGTCLNVGCIPSKALL-----NNSHYYHMAH---------GKDFA 107
Cdd:PRK07251 5 DLIVIGFGKAGKTLAAKLASAGKKVALVEESKAMyGGTCINIGCIPTKTLLvaaekNLSFEQVMATkntvtsrlrGKNYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 108 ---SRGIEM--SEVRLNLDKMMEQKSTAVKAL---------TGGIAHLFKQNKIDEDT-IVSSTGALSLKKVPEKMVVIG 172
Cdd:PRK07251 85 mlaGSGVDLydAEAHFVSNKVIEVQAGDEKIEltaetivinTGAVSNVLPIPGLADSKhVYDSTGIQSLETLPERLGIIG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 173 AGVIGVELGSVWQRLGADVTAVE----FLGHVggvgiDMEISKNFQRILQKQGFKFKLNTKVTgATKKSDGKIDVSIEaa 248
Cdd:PRK07251 165 GGNIGLEFAGLYNKLGSKVTVLDaastILPRE-----EPSVAALAKQYMEEDGITFLLNAHTT-EVKNDGDQVLVVTE-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 249 sggkAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEG 328
Cdd:PRK07251 237 ----DETYRFDALLYATGRKPNTEPLGLENTDIELTERGAIKVDDYCQTSVPGVFAVGDVNGGPQFTYISLDDFRIVFGY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 329 MAGGA--VHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMVKILGQKSTDRVLGAH 406
Cdd:PRK07251 313 LTGDGsyTLEDRGNVPTTMFITPPLSQVGLTEKEAKEAGLPYAVKELLVAAMPRAHVNNDLRGAFKVVVNTETKEILGAT 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 576583544 407 ILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAF 446
Cdd:PRK07251 393 LFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAENL 432
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
44-460 |
6.14e-58 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 199.99 E-value: 6.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 44 VTVIGSGPGGYVAAIKAAQLGFKTVCIEKNeTLGGTCLNVGCIPSKALLNNSHYYHMAHGKDFASrGIEMSEVRLNLDKM 123
Cdd:PRK13748 101 VAVIGSGGAAMAAALKAVEQGARVTLIERG-TIGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDG-GIAATVPTIDRSRL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 124 MEQKSTAVKAL-----------TGGIAHL-----FKqnkiDEDTIV---------------------------------- 153
Cdd:PRK13748 179 LAQQQARVDELrhakyegildgNPAITVLhgearFK----DDQTLIvrlndggervvafdrcliatgaspavppipglke 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 154 ----SSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHvggvgiDMEISKNFQRILQKQGFKFK 225
Cdd:PRK13748 255 tpywTSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILArstlFFRE------DPAIGEAVTAAFRAEGIEVL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 226 LNTKVTgATKKSDGKIDVSIEAASggkaevITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAI 305
Cdd:PRK13748 329 EHTQAS-QVAHVDGEFVLTTGHGE------LRADKLLVATGRAPNTRSLALDAAGVTVNAQGAIVIDQGMRTSVPHIYAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 306 GDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNA 385
Cdd:PRK13748 402 GDCTDQPQFVYVAAAAGTRAAINMTGGDAALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRTLTLDNVPRALANF 481
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 576583544 386 DTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREAnlAASFGKSIN 460
Cdd:PRK13748 482 DTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAALAIRNRMTVQELADQLFPYLTMVEGLKLA--AQTFNKDVK 554
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
43-446 |
6.37e-58 |
|
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: 197.37 E-value: 6.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNEtLGGTCLNVGCIPSKALLNNSH-------------------------- 96
Cdd:TIGR01421 4 DYLVIGGGSGGIASARRAAEHGAKALLVEAKK-LGGTCVNVGCVPKKVMWYASDlaermhdaadygfyqndentfnwpel 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 97 ------YYHMAHG---KDFASRGIEMSE--VRLNLDKMMEQKSTAVKA-----LTGGIAhLFKQNKIDEDTIVSSTGALS 160
Cdd:TIGR01421 83 kekrdaYVDRLNGiyqKNLEKNKVDVIFghARFTKDGTVEVNGRDYTAphiliATGGKP-SFPENIPGAELGTDSDGFFA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 161 LKKVPEKMVVIGAGVIGVELGSVWQRLGADvTAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGK 240
Cdd:TIGR01421 162 LEELPKRVVIVGAGYIAVELAGVLHGLGSE-THLVIRHERVLRSFDSMISETITEEYEKEGINVHKLSKPVKVEKTVEGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 241 IDVSIEAASggkaEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPMLAHKAED 320
Cdd:TIGR01421 241 LVIHFEDGK----SIDDVDELIWAIGRKPNTKGLGLENVGIKLNEKGQIIVDEYQNTNVPGIYALGDVVGKVELTPVAIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 321 EGIICVEGMAGGA--VHIDYNCVPSVIYTHPEVAWVGKSEEQ-LKEEGIE-YKVGKFPFAANSRAKTNADTDGMVKILGQ 396
Cdd:TIGR01421 317 AGRKLSERLFNGKtdDKLDYNNVPTVVFSHPPIGTIGLTEKEaIEKYGKEnIKVYNSSFTPMYYAMTSEKQKCRMKLVCA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 576583544 397 KSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAF 446
Cdd:TIGR01421 397 GKEEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEEL 446
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
46-448 |
1.05e-57 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 196.54 E-value: 1.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 46 VIGSGPGGYVAAIKAAQLGFKTVCIEKNETL-GGTCLNVGCIPSKALLNNSHYYHmahgkDFASRGIEMSEV-------- 116
Cdd:NF040477 8 IIGFGKAGKTLAATLAKAGWRVAIIEQSAQMyGGTCINIGCIPTKTLVHDAEQHQ-----DFSTAMQRKSSVvgflrdkn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 117 RLNLDKM------------MEQKSTAVKALTGGIahLFKQNKIDEDT-----------------IVSSTGALSLKKVPEK 167
Cdd:NF040477 83 YHNLADLdnvdvingraefIDNHTLRVFQADGEQ--ELRGEKIFINTgaqsvlppipgltttpgVYDSTGLLNLTQLPAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 168 MVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGVGiDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGkidVSIEA 247
Cdd:NF040477 161 LGILGGGYIGVEFASMFARFGSKVTIFEAAELFLPRE-DRDIAQAIATILQDQGVELILNAQVQRVSSHEGE---VQLET 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 248 ASGgkaeVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVE 327
Cdd:NF040477 237 AEG----VLTVDALLVASGRKPATAGLQLQNAGVAVNERGAIVVDKYLRTTADNIWAMGDVTGGLQFTYISLDDFRIVRD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 328 GMAG-GAVHI-DYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMVKILGQKSTDRVLGA 405
Cdd:NF040477 313 SLLGeGKRSTdDRQNVPYSVFMTPPLSRIGMTEEQARASGADIQVVTLPVAAIPRARVMNDTRGVLKAVVDNKTQRILGV 392
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 576583544 406 HILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFRE 448
Cdd:NF040477 393 SLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSESLND 435
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
341-449 |
1.41e-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: 177.36 E-value: 1.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 341 VPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAA 420
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGEVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQEAA 80
|
90 100
....*....|....*....|....*....
gi 576583544 421 LALEYGASCEDIARVCHAHPTLSEAFREA 449
Cdd:pfam02852 81 LAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
43-455 |
1.91e-50 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 177.45 E-value: 1.91e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 43 DVTVIGSGPGGyvaAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLnnsHYYHMAH--------GKDFASRGIEMS 114
Cdd:PRK07846 3 DLIIIGTGSGN---SILDERFADKRIAIVEKGTFGGTCLNVGCIPTKMFV---YAADVARtireaarlGVDAELDGVRWP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 115 EVR----------------------LNLDKMMEQKS-TAVKALTGGIAHLfkqnkIDEDTIVSSTG---------ALS-- 160
Cdd:PRK07846 77 DIVsrvfgridpiaaggeeyrgrdtPNIDVYRGHARfIGPKTLRTGDGEE-----ITADQVVIAAGsrpvippviADSgv 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 161 ----------LKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVE----FLGHvggvgIDMEISKNFQRILQKQgFKFKL 226
Cdd:PRK07846 152 ryhtsdtimrLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNrsgrLLRH-----LDDDISERFTELASKR-WDVRL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 227 NTKVTGATKKSDGkidVSIEAASGgkaEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIG 306
Cdd:PRK07846 226 GRNVVGVSQDGSG---VTLRLDDG---STVEADVLLVATGRVPNGDLLDAAAAGVDVDEDGRVVVDEYQRTSAEGVFALG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 307 DVVAGPMLAHKAEDEGIICVEGMAGGA--VHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTN 384
Cdd:PRK07846 300 DVSSPYQLKHVANHEARVVQHNLLHPDdlIASDHRFVPAAVFTHPQIASVGLTENEARAAGLDITVKVQNYGDVAYGWAM 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 576583544 385 ADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCH-AHPTLSEAFREANLAASF 455
Cdd:PRK07846 380 EDTTGFVKLIADRDTGRLLGAHIIGPQASTLIQPLIQAMSFGLDAREMARGQYwIHPALPEVVENALLGLDL 451
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
46-448 |
9.79e-48 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 170.19 E-value: 9.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 46 VIGSGPGGYVAAIKAAQLGFKTVCIEK-NETLGGTCLNVGCIPSKALLNNSHyyhmAHGkDFaSRGIEMSEVRLNL--DK 122
Cdd:PRK08010 8 IIGFGKAGKTLAVTLAKAGWRVALIEQsNAMYGGTCINIGCIPTKTLVHDAQ----QHT-DF-VRAIQRKNEVVNFlrNK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 123 MMEQ-----------------KSTAVKALTGGIAHLFKQNKIDEDT-----------------IVSSTGALSLKKVPEKM 168
Cdd:PRK08010 82 NFHNladmpnidvidgqaefiNNHSLRVHRPEGNLEIHGEKIFINTgaqtvvppipgitttpgVYDSTGLLNLKELPGHL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 169 VVIGAGVIGVELGSVWQRLGADVTAVE----FLGHVggvgiDMEISKNFQRILQKQGFKFKLNTKVTGATKKsDGKIDVS 244
Cdd:PRK08010 162 GILGGGYIGVEFASMFANFGSKVTILEaaslFLPRE-----DRDIADNIATILRDQGVDIILNAHVERISHH-ENQVQVH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 245 IEAASggkaevITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPMLAHKAEDEGII 324
Cdd:PRK08010 236 SEHAQ------LAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKYLHTTADNIWAMGDVTGGLQFTYISLDDYRI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 325 CVEGMAGGAVHI--DYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMVKILGQKSTDRV 402
Cdd:PRK08010 310 VRDELLGEGKRStdDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDTRGVLKAIVDNKTQRI 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 576583544 403 LGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFRE 448
Cdd:PRK08010 390 LGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLND 435
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
44-449 |
6.38e-47 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 168.50 E-value: 6.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 44 VTVIGSGPGGYVAAIKAAQLGFKTVCIEkNETLGGTCLNVGCIPSKALLNNSHYyhMAHGKDFASRGIE---MSEVRLNL 120
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIE-RDGLGGAAVLTDCVPSKTLIATAEV--RTELRRAAELGIRfidDGEARVDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 121 DKMMEQkstaVKALT-------------------GGIAHLFKQN----------------KIDEDTIVSSTGA------- 158
Cdd:PRK07845 81 PAVNAR----VKALAaaqsadirarleregvrviAGRGRLIDPGlgphrvkvttadggeeTLDADVVLIATGAsprilpt 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 159 --------------LSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGvGIDMEISKNFQRILQKQGFKF 224
Cdd:PRK07845 157 aepdgeriltwrqlYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLP-GEDADAAEVLEEVFARRGMTV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 225 KLNTKVTGATKKSDGkidVSIEAASGGKAEVITCdvlLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYA 304
Cdd:PRK07845 236 LKRSRAESVERTGDG---VVVTLTDGRTVEGSHA---LMAVGSVPNTAGLGLEEAGVELTPSGHITVDRVSRTSVPGIYA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 305 IGDVVAGPMLAHKAEDEGIICVEGMAGGAVH-IDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKT 383
Cdd:PRK07845 310 AGDCTGVLPLASVAAMQGRIAMYHALGEAVSpLRLKTVASNVFTRPEIATVGVSQAAIDSGEVPARTVMLPLATNPRAKM 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 576583544 384 NADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREA 449
Cdd:PRK07845 390 SGLRDGFVKLFCRPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYPSLSGSITEA 455
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
41-459 |
6.86e-46 |
|
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: 166.18 E-value: 6.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 41 DADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNET--------LGGTCLNVGCIPSKALLNNSHY-YHMAHGKDFASRGI 111
Cdd:TIGR01438 2 DYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPtplgtrwgIGGTCVNVGCIPKKLMHQAALLgQALKDSRNYGWKVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 112 EmsEVRLNLDKMMEQKSTAVKALTGGIAHLFKQNKI----------DEDTI----------------------------- 152
Cdd:TIGR01438 82 E--TVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVkyenayaefvDKHRIkatnkkgkekiysaerfliatgerprypg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 153 --------VSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVeflghVGGV---GIDMEISKNFQRILQKQG 221
Cdd:TIGR01438 160 ipgakelcITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVM-----VRSIllrGFDQDCANKVGEHMEEHG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 222 FKFKLNTKVTGATKKSDGKIDVSIEAASGGKAEVitcDVLLVCIGRRPFTKNLGLEELGIELDPR-GRIPVNTRFQTKIP 300
Cdd:TIGR01438 235 VKFKRQFVPIKVEQIEAKVLVEFTDSTNGIEEEY---DTVLLAIGRDACTRKLNLENVGVKINKKtGKIPADEEEQTNVP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 301 NIYAIGDVVAG-PMLAHKAEDEGIICVEGMAGGAVHI-DYNCVPSVIYTHPEVAWVGKSEEQ----LKEEGIEYKVGKF- 373
Cdd:TIGR01438 312 YIYAVGDILEDkPELTPVAIQAGRLLAQRLFKGSTVIcDYENVPTTVFTPLEYGACGLSEEKavekFGEENVEVFHSYFw 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 374 PFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAA 453
Cdd:TIGR01438 392 PLEWTIPSRDNHNKCYAKLVCNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTLSVTK 471
|
....*.
gi 576583544 454 SFGKSI 459
Cdd:TIGR01438 472 RSGQDI 477
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
41-446 |
1.25e-45 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 165.76 E-value: 1.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 41 DADVTVIGSGPGGYVAAIKAAQLG---------FKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYyhMAHGKDFASRGI 111
Cdd:PLN02507 25 DFDLFVIGAGSGGVRAARFSANFGakvgicelpFHPISSESIGGVGGTCVIRGCVPKKILVYGATF--GGEFEDAKNYGW 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 112 EMSE-VRLNLDKMMEQKSTAVKALTG---------------GIAHLFKQNKID--------------------------- 148
Cdd:PLN02507 103 EINEkVDFNWKKLLQKKTDEILRLNGiykrllanagvklyeGEGKIVGPNEVEvtqldgtklrytakhiliatgsraqrp 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 149 ----EDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVeFLGHVGGVGIDMEISKNFQRILQKQGFKF 224
Cdd:PLN02507 183 nipgKELAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLF-FRKELPLRGFDDEMRAVVARNLEGRGINL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 225 KLNTKVTGATKKSDGkIDVSIEaasggKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYA 304
Cdd:PLN02507 262 HPRTNLTQLTKTEGG-IKVITD-----HGEEFVADVVLFATGRAPNTKRLNLEAVGVELDKAGAVKVDEYSRTNIPSIWA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 305 IGDVVAGPMLAHKAEDEGIICVEGMAGG-AVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEG---IEYKVGKFPFAANSR 380
Cdd:PLN02507 336 IGDVTNRINLTPVALMEGTCFAKTVFGGqPTKPDYENVACAVFCIPPLSVVGLSEEEAVEQAkgdILVFTSSFNPMKNTI 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 576583544 381 AKTNADTdgMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAF 446
Cdd:PLN02507 416 SGRQEKT--VMKLIVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEF 479
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
43-452 |
2.41e-44 |
|
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: 161.08 E-value: 2.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 43 DVTVIGSGPGGyvaAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLnnsHYYHMAHGKDFASR-GI--EMSEVRL- 118
Cdd:TIGR03452 4 DLIIIGTGSGN---SIPDPRFADKRIAIVEKGTFGGTCLNVGCIPTKMFV---YAAEVAQSIGESARlGIdaEIDSVRWp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 119 ----------------------------NLDkMMEQKSTAV--KALTGGIAhlfkqNKIDEDTIVSSTGA---------- 158
Cdd:TIGR03452 78 divsrvfgdridpiaaggedyrrgdetpNID-VYDGHARFVgpRTLRTGDG-----EEITGDQIVIAAGSrpyippaiad 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 159 -----------LSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAV----EFLGHvggvgIDMEISKNFQRILQKQgFK 223
Cdd:TIGR03452 152 sgvryhtnediMRLPELPESLVIVGGGYIAAEFAHVFSALGTRVTIVnrstKLLRH-----LDEDISDRFTEIAKKK-WD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 224 FKLNTKVTGATKKSDGkidVSIEAASGgkaEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIY 303
Cdd:TIGR03452 226 IRLGRNVTAVEQDGDG---VTLTLDDG---STVTADVLLVATGRVPNGDLLDAEAAGVEVDEDGRIKVDEYGRTSARGVW 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 304 AIGDVVAGPMLAHKAEDEGIICVEGMA--GGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEG--IEYKVGKFPFAANS 379
Cdd:TIGR03452 300 ALGDVSSPYQLKHVANAEARVVKHNLLhpNDLRKMPHDFVPSAVFTHPQIATVGLTEQEAREAGhdITVKIQNYGDVAYG 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 576583544 380 RAKtnADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCH-AHPTLSEAFREANLA 452
Cdd:TIGR03452 380 WAM--EDTTGFCKLIADRDTGKLLGAHIIGPQASSLIQPLITAMAFGLDAREMARKQYwIHPALPEVVENALLG 451
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
41-458 |
7.31e-43 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 158.06 E-value: 7.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 41 DADVTVIGSGPGGYVAAIKAAQLGFKTVCIE--KNET------LGGTCLNVGCIPSKALlnnsHY-------YHM---AH 102
Cdd:PTZ00052 5 MYDLVVIGGGSGGMAAAKEAAAHGKKVALFDyvKPSTqgtkwgLGGTCVNVGCVPKKLM----HYaanigsiFHHdsqMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 103 GKDFASR---GIEMSEVR-----LNLDKMMEQKSTAVKALTGgIAHLFKQNKI------DEDTI---------------- 152
Cdd:PTZ00052 81 GWKTSSSfnwGKLVTTVQnhirsLNFSYRTGLRSSKVEYING-LAKLKDEHTVsygdnsQEETItakyiliatggrpsip 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 153 ----------VSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVT-AVEflgHVGGVGIDMEISKNFQRILQKQG 221
Cdd:PTZ00052 160 edvpgakeysITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTvAVR---SIPLRGFDRQCSEKVVEYMKEQG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 222 FKFKlNTKVTGATKKSDGKIDVSIeaaSGGKAEVItcDVLLVCIGRRPFTKNLGLEELGIELDPRGRIpVNTRFQTKIPN 301
Cdd:PTZ00052 237 TLFL-EGVVPINIEKMDDKIKVLF---SDGTTELF--DTVLYATGRKPDIKGLNLNAIGVHVNKSNKI-IAPNDCTNIPN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 302 IYAIGDVVAG-PMLAHKAEDEGIICVEGMAGGAVHI-DYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANS 379
Cdd:PTZ00052 310 IFAVGDVVEGrPELTPVAIKAGILLARRLFKQSNEFiDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQEFNT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 380 ------------RAKTNA-DTD----GMVKILGQKSTD-RVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPT 441
Cdd:PTZ00052 390 leiaavhrekheRARKDEyDFDvssnCLAKLVCVKSEDnKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHPT 469
|
490
....*....|....*..
gi 576583544 442 LSEAFREANLAASFGKS 458
Cdd:PTZ00052 470 DAEVFMNLSVTRRSGES 486
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
43-444 |
1.06e-42 |
|
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: 157.44 E-value: 1.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNET---------LGGTCLNVGCIPSKALLNNSHYyhMAHGKDFASRGIEM 113
Cdd:TIGR01423 5 DLVVIGAGSGGLEAGWNAATLYKKRVAVVDVQThhgppfyaaLGGTCVNVGCVPKKLMVTGAQY--MDTLRESAGFGWEF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 114 --SEVRLNLDKMMEQKSTAVKALTGGIAHLFK--------------------------------QNKIDEDTIVSSTG-- 157
Cdd:TIGR01423 83 drSSVKANWKALIAAKNKAVLDINKSYEGMFAdtegltfflgwgaledknvvlvresadpksavKERLQAEHILLATGsw 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 158 -----------------ALSLKKVPEKMVVIGAGVIGVELGSV---WQRLGADVTaVEFLGHVGGVGIDMEISKNFQRIL 217
Cdd:TIGR01423 163 pqmlgipgiehcissneAFYLDEPPRRVLTVGGGFISVEFAGIfnaYKPRGGKVT-LCYRNNMILRGFDSTLRKELTKQL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 218 QKQGFKFKLNTKVTGATKKSDGKIDVSIEaaSGGKAEVitcDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQT 297
Cdd:TIGR01423 242 RANGINIMTNENPAKVTLNADGSKHVTFE--SGKTLDV---DVVMMAIGRVPRTQTLQLDKVGVELTKKGAIQVDEFSRT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 298 KIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVH-IDYNCVPSVIYTHPEVAWVGKSEEQL--KEEGIEYKVGKF- 373
Cdd:TIGR01423 317 NVPNIYAIGDVTDRVMLTPVAINEGAAFVDTVFGNKPRkTDHTRVASAVFSIPPIGTCGLVEEDAakKFEKVAVYESSFt 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 576583544 374 PFAANSRAKTNADTdgMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSE 444
Cdd:TIGR01423 397 PLMHNISGSKYKKF--VAKIVTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAE 465
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
41-446 |
5.33e-38 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 145.40 E-value: 5.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 41 DADVTVIGSGPGG---------YVAAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHmahgkDF-ASRG 110
Cdd:PLN02546 79 DFDLFTIGAGSGGvrasrfasnFGASAAVCELPFATISSDTLGGVGGTCVLRGCVPKKLLVYASKYSH-----EFeESRG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 111 IEM---SEVRLNLDKMMEQKSTAVKALTGGIAHLFK---------QNKI-DEDTI------------------------- 152
Cdd:PLN02546 154 FGWkyeTEPKHDWNTLIANKNAELQRLTGIYKNILKnagvtliegRGKIvDPHTVdvdgklytarniliavggrpfipdi 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 153 ------VSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVtaveflgHV----GGV--GIDMEISKNFQRILQKQ 220
Cdd:PLN02546 234 pgiehaIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDV-------HVfirqKKVlrGFDEEVRDFVAEQMSLR 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 221 GFKFKLNTKVTGATKKSDGKIDVSIEAAS-GGKAEVitcdvlLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKI 299
Cdd:PLN02546 307 GIEFHTEESPQAIIKSADGSLSLKTNKGTvEGFSHV------MFATGRKPNTKNLGLEEVGVKMDKNGAIEVDEYSRTSV 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 300 PNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGG-AVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVgkfpFAAN 378
Cdd:PLN02546 381 PSIWAVGDVTDRINLTPVALMEGGALAKTLFGNePTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYGDVDV----FTAN 456
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 576583544 379 SRAkTNADTDGM-----VKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAF 446
Cdd:PLN02546 457 FRP-LKATLSGLpdrvfMKLIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEEF 528
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
21-446 |
1.56e-31 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 127.04 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 21 SHGLQGlSAVPLRTYADQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKnETLGGTCLNVGCIPSK----------A 90
Cdd:PTZ00058 29 YHNLEA-SSAPTHLKKKPRMVYDLIVIGGGSGGMAAARRAARNKAKVALVEK-DYLGGTCVNVGCVPKKimfnaasihdI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 91 LLNNSHY---------------------------YHMAHGKD----FASRGIEMSEVRLNLDKMMEQ----------KST 129
Cdd:PTZ00058 107 LENSRHYgfdtqfsfnlpllverrdkyirrlndiYRQNLKKDnveyFEGKGSLLSENQVLIKKVSQVdgeadesdddEVT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 130 AV----------KALTGG---IA----HLFKQNKIDEDTIvSSTGALSLKKvPEKMVVIGAGVIGVELGSVWQRLGADvT 192
Cdd:PTZ00058 187 IVsagvsqlddgQVIEGKnilIAvgnkPIFPDVKGKEFTI-SSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAE-S 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 193 AVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKksDGKIDVSIEAASGGKAEVITCdvLLVCIGRRPFTK 272
Cdd:PTZ00058 264 YIFARGNRLLRKFDETIINELENDMKKNNINIITHANVEEIEK--VKEKNLTIYLSDGRKYEHFDY--VIYCVGRSPNTE 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 273 NLGLEELGIeLDPRGRIPVNTRFQTKIPNIYAIGDVVAGP---------MLAHKAEDEGIICVEGMAGGAVH-------- 335
Cdd:PTZ00058 340 DLNLKALNI-KTPKGYIKVDDNQRTSVKHIYAVGDCCMVKknqeiedlnLLKLYNEEPYLKKKENTSGESYYnvqltpva 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 336 ------------------IDYNCVPSVIYTHPEVAWVGKSEEQL-----KEEGIEYK-------VGKFPFAANSRAKTna 385
Cdd:PTZ00058 419 inagrlladrlfgpfsrtTNYKLIPSVIFSHPPIGTIGLSEQEAidiygKENVKIYEsrftnlfFSVYDMDPAQKEKT-- 496
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 576583544 386 dtdgMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAF 446
Cdd:PTZ00058 497 ----YLKLVCVGKEELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIHPTAAEEF 553
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
165-345 |
2.14e-28 |
|
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];
Pssm-ID: 440215 [Multi-domain] Cd Length: 322 Bit Score: 114.52 E-value: 2.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 165 PEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGVgIDMEISKNFQRILQKQGFKFKLNTKVTGAtkksDGKIDVS 244
Cdd:COG0446 124 GKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGV-LDPEMAALLEEELREHGVELRLGETVVAI----DGDDKVA 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 245 IEAASGgkaEVITCDVLLVCIGRRPftkNLGL-EELGIELDPRGRIPVNTRFQTKIPNIYAIGDVV----------AGPM 313
Cdd:COG0446 199 VTLTDG---EEIPADLVVVAPGVRP---NTELaKDAGLALGERGWIKVDETLQTSDPDVYAAGDCAevphpvtgktVYIP 272
|
170 180 190
....*....|....*....|....*....|..
gi 576583544 314 LAHKAEDEGIICVEGMAGGAvhIDYNCVPSVI 345
Cdd:COG0446 273 LASAANKQGRVAAENILGGP--APFPGLGTFI 302
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
43-313 |
9.09e-24 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 100.96 E-value: 9.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNEtLGGTCLNVGCIpskallNNshYYHMAH---GKDFASRGIEMSEvRLN 119
Cdd:COG0492 2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEGGE-PGGQLATTKEI------EN--YPGFPEgisGPELAERLREQAE-RFG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 120 LDKMMEQ-----KSTAVKALTGGiahlfKQNKIDEDTIVSSTGAlSLKKVP-------------------------EKMV 169
Cdd:COG0492 72 AEILLEEvtsvdKDDGPFRVTTD-----DGTEYEAKAVIIATGA-GPRKLGlpgeeefegrgvsycatcdgfffrgKDVV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 170 VIGAGVIGVELGSVWQRLGADVTAVeflgHVGGvgiDMEISKNFQ-RILQKQGFKFKLNTKVTGAtkKSDGKID-VSIEA 247
Cdd:COG0492 146 VVGGGDSALEEALYLTKFASKVTLI----HRRD---ELRASKILVeRLRANPKIEVLWNTEVTEI--EGDGRVEgVTLKN 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 576583544 248 ASGGKAEVITCDVLLVCIGRRPftkNLGL-EELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPM 313
Cdd:COG0492 217 VKTGEEKELEVDGVFVAIGLKP---NTELlKGLGLELDEDGYIVVDEDMETSVPGVFAAGDVRDYKY 280
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
167-334 |
8.55e-22 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 96.75 E-value: 8.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 167 KMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGKidvSIE 246
Cdd:COG1251 144 RVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVT---GVR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 247 AASGgkaEVITCDVLLVCIGRRPftkNLGL-EELGIELDpRGrIPVNTRFQTKIPNIYAIGDVVA-------GPMLAH-- 316
Cdd:COG1251 221 LADG---EELPADLVVVAIGVRP---NTELaRAAGLAVD-RG-IVVDDYLRTSDPDIYAAGDCAEhpgpvygRRVLELva 292
|
170
....*....|....*...
gi 576583544 317 KAEDEGIICVEGMAGGAV 334
Cdd:COG1251 293 PAYEQARVAAANLAGGPA 310
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
167-240 |
1.77e-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: 74.16 E-value: 1.77e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 576583544 167 KMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGvGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGK 240
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLP-GFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGV 73
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
162-440 |
2.62e-15 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 77.77 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 162 KKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVtgatKKSDGKI 241
Cdd:PRK09564 146 DEEIKNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHLNEFV----KSLIGED 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 242 DVSIEAASGGKAEVitcDVLLVCIGRRPFTKnlGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGD-------VVAGPM- 313
Cdd:PRK09564 222 KVEGVVTDKGEYEA---DVVIVATGVKPNTE--FLEDTGLKTLKNGAIIVDEYGETSIENIYAAGDcatiyniVSNKNVy 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 314 --LAHKAEDEGIICVEGMAGGAVH----IDYNCVPSVIYthpEVAWVGKSEEQLKEEGIEYKVgKFPFAANSRAKTNADT 387
Cdd:PRK09564 297 vpLATTANKLGRMVGENLAGRHVSfkgtLGSACIKVLDL---EAARTGLTEEEAKKLGIDYKT-VFIKDKNHTNYYPGQE 372
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 576583544 388 DGMVKILGQKSTDRVLGAHILGP-GAGEMVNEAALALEYGASCEDIARV--CHAHP 440
Cdd:PRK09564 373 DLYVKLIYEADTKVILGGQIIGKkGAVLRIDALAVAIYAKLTTQELGMMdfCYAPP 428
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
144-309 |
6.07e-15 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 76.36 E-value: 6.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 144 QNKIDEDTIVSSTGALSLKKVPekmvVIGAGVIGVE-LGSVWQRlGADVTAVEFLGHVGGVgIDMEISKNFQRILQKQGF 222
Cdd:PRK13512 131 RNLEDTDAIDQFIKANQVDKAL----VVGAGYISLEvLENLYER-GLHPTLIHRSDKINKL-MDADMNQPILDELDKREI 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 223 KFKLNTKVTgatkksdgKIDVSIEAASGGKAEviTCDVLLVCIGRRPFTKNLglEELGIELDPRGRIPVNTRFQTKIPNI 302
Cdd:PRK13512 205 PYRLNEEID--------AINGNEVTFKSGKVE--HYDMIIEGVGTHPNSKFI--ESSNIKLDDKGFIPVNDKFETNVPNI 272
|
....*..
gi 576583544 303 YAIGDVV 309
Cdd:PRK13512 273 YAIGDII 279
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
170-307 |
2.43e-14 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 74.18 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 170 VIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGkidVSIEAAS 249
Cdd:PRK04965 146 VVGGGLIGTELAMDLCRAGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSG---IRATLDS 222
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 576583544 250 GgkaEVITCDVLLVCIGRRPftkNLGL-EELGIELDpRGrIPVNTRFQTKIPNIYAIGD 307
Cdd:PRK04965 223 G---RSIEVDAVIAAAGLRP---NTALaRRAGLAVN-RG-IVVDSYLQTSAPDIYALGD 273
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
42-327 |
4.22e-14 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 73.63 E-value: 4.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 42 ADVTVIGSGPGGYVAAIKAAQLGFKTVCIekneTLggtclnvgcIpSKallNNSHYY-HMAHGkdFASRGIEMSEVRLNL 120
Cdd:COG1252 2 KRIVIVGGGFAGLEAARRLRKKLGGDAEV----TL---------I-DP---NPYHLFqPLLPE--VAAGTLSPDDIAIPL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 121 DKMMEQKSTAVkaLTGGIAHLFKQNK---------IDEDTIVSSTG--------------ALSLKKVPE----------- 166
Cdd:COG1252 63 RELLRRAGVRF--IQGEVTGIDPEARtvtladgrtLSYDYLVIATGsvtnffgipglaehALPLKTLEDalalrerllaa 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 167 ----------KMVVIGAGVIGVEL-GSVWQRLG------------ADVTAVEFLGHVGGvGIDMEISKNFQRILQKQGFK 223
Cdd:COG1252 141 feraerrrllTIVVVGGGPTGVELaGELAELLRkllrypgidpdkVRITLVEAGPRILP-GLGEKLSEAAEKELEKRGVE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 224 FKLNTKVTGATKKSdgkidvsIEAASGgkaEVITCDVLLVCIGRR--PFTKNLGLEelgieLDPRGRIPVNTRFQTK-IP 300
Cdd:COG1252 220 VHTGTRVTEVDADG-------VTLEDG---EEIPADTVIWAAGVKapPLLADLGLP-----TDRRGRVLVDPTLQVPgHP 284
|
330 340 350
....*....|....*....|....*....|....*
gi 576583544 301 NIYAIGDVVAG--------PMLAHKAEDEGIICVE 327
Cdd:COG1252 285 NVFAIGDCAAVpdpdgkpvPKTAQAAVQQAKVLAK 319
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
44-337 |
4.13e-12 |
|
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: 67.85 E-value: 4.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 44 VTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTcLNVGcIPS----KALLNNSHYYhmahgkdFASRGIEmseVRLN 119
Cdd:COG0493 124 VAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGGL-LRYG-IPEfrlpKDVLDREIEL-------IEALGVE---FRTN 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 120 --------LDKMMEQ-----------KSTAVK----ALTG---GIAHLFKQNKIDEDTIVSSTGalslKKVpekmVVIGA 173
Cdd:COG0493 192 vevgkditLDELLEEfdavflatgagKPRDLGipgeDLKGvhsAMDFLTAVNLGEAPDTILAVG----KRV----VVIGG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 174 G-----VIGVELgsvwqRLGA-DVTAVEFLGHVggvgiDM-----EISKnfqriLQKQGFKFKLNTKVTGATKKSDG--- 239
Cdd:COG0493 264 GntamdCARTAL-----RLGAeSVTIVYRRTRE-----EMpaskeEVEE-----ALEEGVEFLFLVAPVEIIGDENGrvt 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 240 -----KIDVSIEAASG--------GKAEVITCDVLLVCIGRRPFTKNLgLEELGIELDPRGRIPVNTR-FQTKIPNIYAI 305
Cdd:COG0493 329 glecvRMELGEPDESGrrrpvpieGSEFTLPADLVILAIGQTPDPSGL-EEELGLELDKRGTIVVDEEtYQTSLPGVFAG 407
|
330 340 350
....*....|....*....|....*....|....*
gi 576583544 306 GDVVAGPMLAhkaedegiicVEGMAGG---AVHID 337
Cdd:COG0493 408 GDAVRGPSLV----------VWAIAEGrkaARAID 432
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
250-322 |
7.37e-12 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 66.55 E-value: 7.37e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 576583544 250 GGKAEVITCDVLLVCIGRRPfTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPMLAHKAEDEG 322
Cdd:PRK12770 267 PGSEFVLEADTVVFAIGEIP-TPPFAKECLGIELNRKGEIVVDEKHMTSREGVFAAGDVVTGPSKIGKAIKSG 338
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
167-310 |
9.06e-10 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 61.00 E-value: 9.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 167 KMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKksDGKIDvSIE 246
Cdd:TIGR02374 142 KAAVIGGGLLGLEAAVGLQNLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVG--ATKAD-RIR 218
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 576583544 247 AASGgkaEVITCDVLLVCIGRRPFTknlgleELGIE--LDPRGRIPVNTRFQTKIPNIYAIGDVVA 310
Cdd:TIGR02374 219 FKDG---SSLEADLIVMAAGIRPND------ELAVSagIKVNRGIIVNDSMQTSDPDIYAVGECAE 275
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
165-308 |
6.15e-09 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 57.63 E-value: 6.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 165 PEKMVVI-GAGVIGVELGSVWQRLGADVTAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSdgkiDV 243
Cdd:PRK09754 143 PERSVVIvGAGTIGLELAASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGE----KV 218
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 576583544 244 SIEAASGgkaEVITCDVLLVCIGRRpFTKNLGLEElgiELDPRGRIPVNTRFQTKIPNIYAIGDV 308
Cdd:PRK09754 219 ELTLQSG---ETLQADVVIYGIGIS-ANDQLAREA---NLDTANGIVIDEACRTCDPAIFAGGDV 276
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
30-320 |
1.12e-08 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 57.47 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 30 VPLRTY---ADQPI---DADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTcLNVGcIPSKALLNNshyyhmAHG 103
Cdd:PRK13984 266 VPVEKYseiLDDEPekkNKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGV-MRYG-IPSYRLPDE------ALD 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 104 KDFA---SRGIEM-SEVRLNLDKMMEQ---KSTAVKALTGgiAHLFKQNKIDEDTIVSSTGALSL--------------K 162
Cdd:PRK13984 338 KDIAfieALGVKIhLNTRVGKDIPLEElreKHDAVFLSTG--FTLGRSTRIPGTDHPDVIQALPLlreirdylrgegpkP 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 163 KVPEKMVVIGAGVIGVELGSVWQRLG------ADVTAVEFLGHVGGVGIDM-EISKNF------------QRIL----QK 219
Cdd:PRK13984 416 KIPRSLVVIGGGNVAMDIARSMARLQkmeygeVNVKVTSLERTFEEMPADMeEIEEGLeegvviypgwgpMEVViendKV 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 220 QGFKFKLNTKVTGATKKSDGKIDVSIEAasggkaeVITCDVLLVCIGRRPFTKNLGlEELGIELD-PRGRIPVNTRFQTK 298
Cdd:PRK13984 496 KGVKFKKCVEVFDEEGRFNPKFDESDQI-------IVEADMVVEAIGQAPDYSYLP-EELKSKLEfVRGRILTNEYGQTS 567
|
330 340
....*....|....*....|..
gi 576583544 299 IPNIYAIGDVVAGPMLAHKAED 320
Cdd:PRK13984 568 IPWLFAGGDIVHGPDIIHGVAD 589
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
44-329 |
5.42e-08 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 54.78 E-value: 5.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 44 VTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGtcLNVGCIPSkallnnshyYHMahGKDFASRGIE-MS----EVRL 118
Cdd:PRK12810 146 VAVVGSGPAGLAAADQLARAGHKVTVFERADRIGG--LLRYGIPD---------FKL--EKEVIDRRIElMEaegiEFRT 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 119 N--------LDKMMEQ--------KSTAVKALtgGIA-------H-----LFKQNKIDEDTIVSSTGALSLKKVpekmVV 170
Cdd:PRK12810 213 NvevgkditAEELLAEydavflgtGAYKPRDL--GIPgrdldgvHfamdfLIQNTRRVLGDETEPFISAKGKHV----VV 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 171 IGAGVIGVE-LG-SVwqRLGA-DVTAVEFLghvggvgiDMEISK--------NFQRIL-----QKQG--FKFKLNTK--- 229
Cdd:PRK12810 287 IGGGDTGMDcVGtAI--RQGAkSVTQRDIM--------PMPPSRrnknnpwpYWPMKLevsnaHEEGveREFNVQTKefe 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 230 -----VTG----ATKKSDGKIDVsIEaasgGKAEVITCDVLLVCIGRRPFTKNLgLEELGIELDPRGRIPVNTR-FQTKI 299
Cdd:PRK12810 357 gengkVTGvkvvRTELGEGDFEP-VE----GSEFVLPADLVLLAMGFTGPEAGL-LAQFGVELDERGRVAAPDNaYQTSN 430
|
330 340 350
....*....|....*....|....*....|
gi 576583544 300 PNIYAIGDVVAGPMLAHKAEDEGIICVEGM 329
Cdd:PRK12810 431 PKVFAAGDMRRGQSLVVWAIAEGRQAARAI 460
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
43-78 |
5.61e-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: 5.61e-07
10 20 30
....*....|....*....|....*....|....*.
gi 576583544 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGG 78
Cdd:COG1233 5 DVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
43-79 |
6.05e-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: 6.05e-07
10 20 30
....*....|....*....|....*....|....*..
gi 576583544 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 79
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGM 37
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
31-79 |
6.71e-07 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 51.64 E-value: 6.71e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 576583544 31 PLRTYADQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 79
Cdd:PRK06134 2 PSAAAYPPDLECDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGGT 50
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
43-92 |
1.53e-06 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 50.24 E-value: 1.53e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 576583544 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNetlGGTCLNVGCIPSKALL 92
Cdd:pfam01134 1 DVIVIGGGHAGCEAALAAARMGAKVLLITHN---TDTIAELSCNPSIGGI 47
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
40-79 |
3.83e-06 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 49.06 E-value: 3.83e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 576583544 40 IDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 79
Cdd:COG1053 2 HEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGGH 41
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
38-79 |
4.90e-06 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 48.92 E-value: 4.90e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 576583544 38 QPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 79
Cdd:PRK12842 6 NELTCDVLVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGGT 47
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
43-79 |
9.16e-06 |
|
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: 9.16e-06
10 20 30
....*....|....*....|....*....|....*..
gi 576583544 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 79
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGA 37
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
43-79 |
9.32e-06 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 48.11 E-value: 9.32e-06
10 20 30
....*....|....*....|....*....|....*..
gi 576583544 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 79
Cdd:PRK07843 9 DVVVVGSGAAGMVAALTAAHRGLSTVVVEKAPHYGGS 45
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
44-311 |
1.03e-05 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 47.87 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 44 VTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGtcLNVGCIPSkallnnshyYHMAhgKDFASRGIEM-----SEVRL 118
Cdd:PRK11749 143 VAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG--LLRYGIPE---------FRLP--KDIVDREVERllklgVEIRT 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 119 NldkmmeqksTAV-KALTggIAHLFKQNkideDTIVSSTGA-------------------------LSLKK------VPE 166
Cdd:PRK11749 210 N---------TEVgRDIT--LDELRAGY----DAVFIGTGAglprflgipgenlggvysavdfltrVNQAVadydlpVGK 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 167 KMVVIGAGVIGVELGSVWQRLGA-DVTAVEFLGHVggvgiDMEISKNFQRILQKQGFKFKLNTK---VTGatkksDGKID 242
Cdd:PRK11749 275 RVVVIGGGNTAMDAARTAKRLGAeSVTIVYRRGRE-----EMPASEEEVEHAKEEGVEFEWLAApveILG-----DEGRV 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 243 VSIEA---------ASG-------GKAEVITCDVLLVCIGRRPFTKNLGLEElGIELDPRG-RIPVNTRFQTKIPNIYAI 305
Cdd:PRK11749 345 TGVEFvrmelgepdASGrrrvpieGSEFTLPADLVIKAIGQTPNPLILSTTP-GLELNRWGtIIADDETGRTSLPGVFAG 423
|
....*.
gi 576583544 306 GDVVAG 311
Cdd:PRK11749 424 GDIVTG 429
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
169-322 |
1.04e-05 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 47.45 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 169 VVIGAGVIGVELGSVWQRLGAD--------------VTAVEFLGHVGGVgIDMEISKNFQRILQKQGFKFKLNTKVTGAT 234
Cdd:PTZ00318 177 VVVGGGPTGVEFAAELADFFRDdvrnlnpelveeckVTVLEAGSEVLGS-FDQALRKYGQRRLRRLGVDIRTKTAVKEVL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 235 KKSdgkidvsIEAASGgkaEVITCDVLL--VCIGRRPFTKNLGleelgIELDPRGRIPVNTRFQTK-IPNIYAIGDVVAG 311
Cdd:PTZ00318 256 DKE-------VVLKDG---EVIPTGLVVwsTGVGPGPLTKQLK-----VDKTSRGRISVDDHLRVKpIPNVFALGDCAAN 320
|
170
....*....|....*.
gi 576583544 312 -----PMLAHKAEDEG 322
Cdd:PTZ00318 321 eerplPTLAQVASQQG 336
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
39-78 |
1.31e-05 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 47.52 E-value: 1.31e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 576583544 39 PIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGG 78
Cdd:PRK12839 6 THTYDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKASTCGG 45
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
169-307 |
2.55e-05 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 46.65 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 169 VVIGAGVIGVELGSVWQRLGADVTAVEF--------LGHVGG---------VGIDMEISKNFQRILQkQGfkfklntkvT 231
Cdd:PRK14989 149 AVVGGGLLGLEAAGALKNLGVETHVIEFapmlmaeqLDQMGGeqlrrkiesMGVRVHTSKNTLEIVQ-EG---------V 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 576583544 232 GATKksdgkidvSIEAASGGKAEVitcDVLLVCIGRRPFTKnLGlEELGIELDPRGRIPVNTRFQTKIPNIYAIGD 307
Cdd:PRK14989 219 EARK--------TMRFADGSELEV---DFIVFSTGIRPQDK-LA-TQCGLAVAPRGGIVINDSCQTSDPDIYAIGE 281
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
43-79 |
3.15e-05 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 46.27 E-value: 3.15e-05
10 20 30
....*....|....*....|....*....|....*..
gi 576583544 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 79
Cdd:PRK12843 18 DVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGT 54
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
46-80 |
3.46e-05 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 41.75 E-value: 3.46e-05
10 20 30
....*....|....*....|....*....|....*
gi 576583544 46 VIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTC 80
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNA 35
|
|
| PRK12835 |
PRK12835 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
43-86 |
5.72e-05 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237221 [Multi-domain] Cd Length: 584 Bit Score: 45.57 E-value: 5.72e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 576583544 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGG-TCLNVGCI 86
Cdd:PRK12835 13 DVLVVGSGGGGMTAALTAAARGLDTLVVEKSAHFGGsTALSGGGI 57
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
39-78 |
1.19e-04 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 44.47 E-value: 1.19e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 576583544 39 PIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGG 78
Cdd:COG1148 138 PVNKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGG 177
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
43-79 |
1.61e-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: 1.61e-04
10 20 30
....*....|....*....|....*....|....*..
gi 576583544 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 79
Cdd:COG2072 8 DVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGT 44
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
43-77 |
1.97e-04 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 43.72 E-value: 1.97e-04
10 20 30
....*....|....*....|....*....|....*
gi 576583544 43 DVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLG 77
Cdd:pfam03486 2 DVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
|
|
| PRK12844 |
PRK12844 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
42-79 |
1.98e-04 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 183787 [Multi-domain] Cd Length: 557 Bit Score: 43.59 E-value: 1.98e-04
10 20 30
....*....|....*....|....*....|....*...
gi 576583544 42 ADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGT 79
Cdd:PRK12844 7 YDVVVVGSGGGGMCAALAAADSGLEPLIVEKQDKVGGS 44
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
44-311 |
7.12e-04 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 42.04 E-value: 7.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 44 VTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTcLNVGcIPSKALLNNSHYYHMahgKDFASRGIE-MSEV----RL 118
Cdd:PRK12778 434 VAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGGV-LKYG-IPEFRLPKKIVDVEI---ENLKKLGVKfETDVivgkTI 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 119 NLDKMMEQKSTAVKALTG---------------GI---------AHLFKQNKIDEDTIVsstgalslkKVPEKMVVIGAG 174
Cdd:PRK12778 509 TIEELEEEGFKGIFIASGaglpnfmnipgensnGVmssneyltrVNLMDAASPDSDTPI---------KFGKKVAVVGGG 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 175 VIGVELGSVWQRLGAD-VTAV------------EFLGHVGGVGIDMEISKNFQRIL-QKQGF-------KFKLntkvtGA 233
Cdd:PRK12778 580 NTAMDSARTAKRLGAErVTIVyrrseeemparlEEVKHAKEEGIEFLTLHNPIEYLaDEKGWvkqvvlqKMEL-----GE 654
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 576583544 234 TKKSDGKIDVSIEaasgGKAEVITCDVLLVCIGRRPfTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAG 311
Cdd:PRK12778 655 PDASGRRRPVAIP----GSTFTVDVDLVIVSVGVSP-NPLVPSSIPGLELNRKGTIVVDEEMQSSIPGIYAGGDIVRG 727
|
|
| PRK07494 |
PRK07494 |
UbiH/UbiF family hydroxylase; |
36-70 |
2.13e-03 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181001 [Multi-domain] Cd Length: 388 Bit Score: 40.27 E-value: 2.13e-03
10 20 30
....*....|....*....|....*....|....*
gi 576583544 36 ADQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCI 70
Cdd:PRK07494 2 LMEKEHTDIAVIGGGPAGLAAAIALARAGASVALV 36
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
276-330 |
4.65e-03 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 39.34 E-value: 4.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 576583544 276 LEELGIELDPRGRIPVNT----RFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMA 330
Cdd:PRK12769 590 LESHGVTVDKWGRIIADVesqyRYQTSNPKIFAGGDAVRGADLVVTAMAEGRHAAQGII 648
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
163-311 |
4.80e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 39.23 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 163 KVPEKMVVIGAGVIGVELGSVWQRLGADVTAV------------EFLGHVGGVGIDMEISKNFQRILQKQgfkfklNTKV 230
Cdd:PRK12831 279 KVGKKVAVVGGGNVAMDAARTALRLGAEVHIVyrrseeelparvEEVHHAKEEGVIFDLLTNPVEILGDE------NGWV 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576583544 231 TGAT--KKSDGKIDvsieaASG--------GKAEVITCDVLLVCIGRRPfTKNLGLEELGIELDPRGRIPVNTRF-QTKI 299
Cdd:PRK12831 353 KGMKciKMELGEPD-----ASGrrrpveieGSEFVLEVDTVIMSLGTSP-NPLISSTTKGLKINKRGCIVADEETgLTSK 426
|
170
....*....|..
gi 576583544 300 PNIYAIGDVVAG 311
Cdd:PRK12831 427 EGVFAGGDAVTG 438
|
|
| |
