|
Name |
Accession |
Description |
Interval |
E-value |
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
1-432 |
9.60e-124 |
|
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: 367.10 E-value: 9.60e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 1 MKYDIVVIGGGTAGYVAGSILARKGKKVIVIEKEKFGGVCVNFGCVPSIFLFDVTFLLNRFKEIVYYlGLDG---EIEYK 77
Cdd:COG1249 2 KDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEF-GISAgapSVDWA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 78 DLLfSKRNEIVNYLSNAGRRLIEDSGGETELGEAEIISPSEVKV-NRRIVEFDKLIIATGSKPMIPNIDGIED--AISED 154
Cdd:COG1249 81 ALM-ARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVtGGETLTADHIVIATGSRPRVPPIPGLDEvrVLTSD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 155 DAVNLNSIPSSMVVIGGGYAGVEIAQIYSRLGSQVTLLSRSE-ILPTFPEDVRSVVKDSLEFDGVNVVENTRIVKLR--- 230
Cdd:COG1249 160 EALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDrLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEktg 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 231 DGKVIT-----EKGEIEGNVIVYATGRRPQLPK-GIEKLGLEIDECG-INVDKYKQIKN-NAYAIGDVINKeRKTAHSAM 302
Cdd:COG1249 240 DGVTVTledggGEEAVEADKVLVATGRRPNTDGlGLEAAGVELDERGgIKVDEYLRTSVpGIYAIGDVTGG-PQLAHVAS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 303 FDALVASLHILKETTFiPPDNFKIPVVLYTDPQVGVIG-DHKEAK------KFSVFPFAAITRAIINGIKDGYVKIGIN- 374
Cdd:COG1249 319 AEGRVAAENILGKKPR-PVDYRAIPSVVFTDPEIASVGlTEEEAReagidvKVGKFPFAANGRALALGETEGFVKLIADa 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 504325421 375 ERNEIVFGEVIGDKAEELINILTLVVNNRMRIESLALMPFVHPSLSEAIVNAAKGFFD 432
Cdd:COG1249 398 ETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAALALLG 455
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
1-432 |
9.17e-96 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 295.55 E-value: 9.17e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 1 MKYDIVVIGGGTAGYVAGSILARKGKKVIVIEKEKFGGVCVNFGCVPS---IFLFDVTFLLNRFKEIvyylGLDG---EI 74
Cdd:PRK06292 2 EKYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGPLGGTCLNVGCIPSkalIAAAEAFHEAKHAEEF----GIHAdgpKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 75 EYKDLLFSKRNEiVNYLSNAGRRLIEDSGGETEL-GEAEIISPSEVKVNRRIVEFDKLIIATGSKpmIPNIDGIEDA--- 150
Cdd:PRK06292 78 DFKKVMARVRRE-RDRFVGGVVEGLEKKPKIDKIkGTARFVDPNTVEVNGERIEAKNIVIATGSR--VPPIPGVWLIlgd 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 151 --ISEDDAVNLNSIPSSMVVIGGGYAGVEIAQIYSRLGSQVTLLSRSE-ILPTFPEDVRSVVKDSL--EFD---GVNV-- 220
Cdd:PRK06292 155 rlLTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDrILPLEDPEVSKQAQKILskEFKiklGAKVts 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 221 VENTRIVKLRDGKVITEKGEIEGNVIVYATGRRPQLPK-GIEKLGLEIDECG-INVDKY-KQIKNNAYAIGDVINKeRKT 297
Cdd:PRK06292 235 VEKSGDEKVEELEKGGKTETIEADYVLVATGRRPNTDGlGLENTGIELDERGrPVVDEHtQTSVPGIYAAGDVNGK-PPL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 298 AHSAMFDALVASLHILKETtfIPPDNFK-IPVVLYTDPQVGVIGD-HKEAKK----FSV--FPFAAITRAIINGIKDGYV 369
Cdd:PRK06292 314 LHEAADEGRIAAENAAGDV--AGGVRYHpIPSVVFTDPQIASVGLtEEELKAagidYVVgeVPFEAQGRARVMGKNDGFV 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504325421 370 KIGINERNEIVFG-EVIGDKAEELINILTLVVNNRMRIESLALMPFVHPSLSEAIVNAAKGFFD 432
Cdd:PRK06292 392 KVYADKKTGRLLGaHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRTALRDLFS 455
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
3-432 |
5.86e-90 |
|
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: 280.68 E-value: 5.86e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 3 YDIVVIGGGTAGYVAGSILARKGKKVIVIEKEKFGGVCVNFGCVPSIFLFDVTFLLNRFKEIVYYlGLDGE---IEYKDL 79
Cdd:TIGR01350 2 YDVIVIGGGPGGYVAAIRAAQLGLKVALVEKEYLGGTCLNVGCIPTKALLHSAEVYDEIKHAKDL-GIEVEnvsVDWEKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 80 LFSKrNEIVNYLSNAGRRLIEDSGGETELGEAEIISPSEVKVN----RRIVEFDKLIIATGSKPMIPNIDGIEDA---IS 152
Cdd:TIGR01350 81 QKRK-NKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTgengEETLEAKNIIIATGSRPRSLPGPFDFDGkvvIT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 153 EDDAVNLNSIPSSMVVIGGGYAGVEIAQIYSRLGSQVTLLSRSE-ILPTFPEDVRSVVKDSLEFDGVNVVENTRIVKLR- 230
Cdd:TIGR01350 160 STGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDrILPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEk 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 231 --DGKVITEKGE----IEGNVIVYATGRRPQLPK-GIEKLGLEIDECG-INVDKYKQIK-NNAYAIGDVINKErKTAHSA 301
Cdd:TIGR01350 240 ndDQVTYENKGGetetLTGEKVLVAVGRKPNTEGlGLEKLGVELDERGrIVVDEYMRTNvPGIYAIGDVIGGP-MLAHVA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 302 MFDALVASLHILKETTfIPPDNFKIPVVLYTDPQVGVIG-DHKEAK------KFSVFPFAAITRAIINGIKDGYVKIGIN 374
Cdd:TIGR01350 319 SHEGIVAAENIAGKEP-AHIDYDAVPSVIYTDPEVASVGlTEEQAKeagydvKIGKFPFAANGKALALGETDGFVKIIAD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 504325421 375 ER-NEIVFGEVIGDKAEELINILTLVVNNRMRIESLALMPFVHPSLSEAIVNAAKGFFD 432
Cdd:TIGR01350 398 KKtGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEAIKEAALAALG 456
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
3-437 |
8.72e-75 |
|
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: 241.56 E-value: 8.72e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 3 YDIVVIGGGTAGYVAGSILARKGKKVIVIEKEKFGGVCVNFGCVPSIFLFDVTFLLNRFKEIVY-YLGLDGEIEYkDLLF 81
Cdd:TIGR02053 1 YDLVIIGSGAAAFAAAIKAAELGASVAMVERGPLGGTCVNVGCVPSKMLLRAAEVAHYARKPPFgGLAATVAVDF-GELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 82 SKRNEIVNYLSNAG-RRLIEDSGGETELGEAEIISPSEVKVN--RRIVEFDKLIIATGSKPMIPNIDGIEDA--ISEDDA 156
Cdd:TIGR02053 80 EGKREVVEELRHEKyEDVLSSYGVDYLRGRARFKDPKTVKVDlgREVRGAKRFLIATGARPAIPPIPGLKEAgyLTSEEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 157 VNLNSIPSSMVVIGGGYAGVEIAQIYSRLGSQVTLLSRSE-ILPTFPEDVRSVVKDSLEFDGVNVVENT--RIVKLRDGK 233
Cdd:TIGR02053 160 LALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSDrLLPREEPEISAAVEEALAEEGIEVVTSAqvKAVSVRGGG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 234 VITE------KGEIEGNVIVYATGRRPQL-PKGIEKLGLEIDECG-INVDKYKQIKN-NAYAIGDVIN---------KER 295
Cdd:TIGR02053 240 KIITvekpggQGEVEADELLVATGRRPNTdGLGLEKAGVKLDERGgILVDETLRTSNpGIYAAGDVTGglqleyvaaKEG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 296 KTAHSAMFDALVASLhilkettfippDNFKIPVVLYTDPQVGVIG-DHKEAKK------FSVFPFAAITRAIINGIKDGY 368
Cdd:TIGR02053 320 VVAAENALGGANAKL-----------DLLVIPRVVFTDPAVASVGlTEAEAQKagiecdCRTLPLTNVPRARINRDTRGF 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 369 VKIGINERNEIVFG-EVIGDKAEELINILTLVVNNRMRIESLALMPFVHPSLSEAIVNAAKGfFDLDVDR 437
Cdd:TIGR02053 389 IKLVAEPGTGKVLGvQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGLKLAAQT-FYRDVSK 457
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
2-430 |
6.98e-74 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 238.95 E-value: 6.98e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 2 KYDIVVIGGGTAGYVAGSILARKGKKVIVIEKEKFGGVCVNFGCVPSiflfdvtfllnrfKEIV------------YYLG 69
Cdd:PRK06370 5 RYDAIVIGAGQAGPPLAARAAGLGMKVALIERGLLGGTCVNTGCVPT-------------KTLIasaraahlarraAEYG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 70 LDG----EIEYKDLLFSKRNEIVNYLSNAGRRLIEDSGGETELGEAEIISPSEVKVNRRIVEFDKLIIATGSKPMIPNID 145
Cdd:PRK06370 72 VSVggpvSVDFKAVMARKRRIRARSRHGSEQWLRGLEGVDVFRGHARFESPNTVRVGGETLRAKRIFINTGARAAIPPIP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 146 GIEDA--ISEDDAVNLNSIPSSMVVIGGGYAGVEIAQIYSRLGSQVTLLSRSE-ILPTFPEDVRSVVKDSLEFDGVNVVE 222
Cdd:PRK06370 152 GLDEVgyLTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPrLLPREDEDVAAAVREILEREGIDVRL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 223 NTRIVKLR---DGKVIT-----EKGEIEGNVIVYATGRRPQLPK-GIEKLGLEIDECG-INVDKYKQIKN-NAYAIGDVi 291
Cdd:PRK06370 232 NAECIRVErdgDGIAVGldcngGAPEITGSHILVAVGRVPNTDDlGLEAAGVETDARGyIKVDDQLRTTNpGIYAAGDC- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 292 NKERKTAHSAMFDALVASLHIL-----KETTFIppdnfkIPVVLYTDPQVGVIGDH-KEAKK------FSVFPFAAITRA 359
Cdd:PRK06370 311 NGRGAFTHTAYNDARIVAANLLdggrrKVSDRI------VPYATYTDPPLARVGMTeAEARKsgrrvlVGTRPMTRVGRA 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504325421 360 IINGIKDGYVKIGIN-ERNEIVFGEVIGDKAEELINILTLVVNNRMRIESLALMPFVHPSLSEAIVNAAKGF 430
Cdd:PRK06370 385 VEKGETQGFMKVVVDaDTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIPTLAQAL 456
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
1-428 |
6.67e-71 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 231.19 E-value: 6.67e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 1 MKYDIVVIGGGTAGYVAGSILARKGKKVIVIEKEKFGGVCVNFGCVPSIFLFdvtfllnRFKEIVYYL------GL---D 71
Cdd:PRK06416 3 FEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLGGTCLNRGCIPSKALL-------HAAERADEArhsedfGIkaeN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 72 GEIEYKDLLFSKRNeIVNYLSNAGRRLIEDSGGETELGEAEIISPSEVKVNR----RIVEFDKLIIATGSKPM-IPNID- 145
Cdd:PRK06416 76 VGIDFKKVQEWKNG-VVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTedgeQTYTAKNIILATGSRPReLPGIEi 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 146 GIEDAISEDDAVNLNSIPSSMVVIGGGYAGVEIAQIYSRLGSQVTLL-SRSEILPTFPEDVRSVVKDSLEFDGVNVVENT 224
Cdd:PRK06416 155 DGRVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVeALPRILPGEDKEISKLAERALKKRGIKIKTGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 225 RIVKLRDG----KVITEKGE----IEGNVIVYATGRRPQLPK-GIEKLGLEIDECGINVDKYKQiKN--NAYAIGDVINK 293
Cdd:PRK06416 235 KAKKVEQTddgvTVTLEDGGkeetLEADYVLVAVGRRPNTENlGLEELGVKTDRGFIEVDEQLR-TNvpNIYAIGDIVGG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 294 ErKTAHSAMFDALVASLHILKETTfiPPDNFKIPVVLYTDPQVGVIG----DHKEAK---KFSVFPFAAITRAIINGIKD 366
Cdd:PRK06416 314 P-MLAHKASAEGIIAAEAIAGNPH--PIDYRGIPAVTYTHPEVASVGlteaKAKEEGfdvKVVKFPFAGNGKALALGETD 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504325421 367 GYVK-IGINERNEIVFGEVIGDKAEELINILTLVVNNRMRIESLALMPFVHPSLSEAIVNAAK 428
Cdd:PRK06416 391 GFVKlIFDKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEALGEAAL 453
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
3-340 |
9.02e-55 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 188.44 E-value: 9.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 3 YDIVVIGGGTAGYVAGSILARKGKKVIVIEKEKFGGVCVNFGCVP------------------SIFLFDVTflLNRFkei 64
Cdd:PRK06116 5 YDLIVIGGGSGGIASANRAAMYGAKVALIEAKRLGGTCVNVGCVPkklmwygaqiaeafhdyaPGYGFDVT--ENKF--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 65 vyylgldgeiEYKDLLFSKRNEIvNYLSNAGRRLIEDSGGETELGEAEIISPSEVKVNRRIVEFDKLIIATGSKPMIPNI 144
Cdd:PRK06116 80 ----------DWAKLIANRDAYI-DRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNGERYTADHILIATGGRPSIPDI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 145 DGIEDAISEDDAVNLNSIPSSMVVIGGGYAGVEIAQIYSRLGSQVTLLSRSE-ILPTFPEDVRSVVKDSLEFDGVNVVEN 223
Cdd:PRK06116 149 PGAEYGITSDGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDaPLRGFDPDIRETLVEEMEKKGIRLHTN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 224 T---RIVKLRDG--KVITEKGE-IEGNVIVYATGRRPQLPK-GIEKLGLEIDECG-INVDKYKQIK-NNAYAIGDVINKE 294
Cdd:PRK06116 229 AvpkAVEKNADGslTLTLEDGEtLTVDCLIWAIGREPNTDGlGLENAGVKLNEKGyIIVDEYQNTNvPGIYAVGDVTGRV 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 504325421 295 RKTA---HSAMfdALVASLhiLKETTFIPPDNFKIPVVLYTDPQVGVIG 340
Cdd:PRK06116 309 ELTPvaiAAGR--RLSERL--FNNKPDEKLDYSNIPTVVFSHPPIGTVG 353
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
3-305 |
6.67e-53 |
|
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: 179.44 E-value: 6.67e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 3 YDIVVIGGGTAGYVAGSILARKGKKVIVIEKEkfgGVCVNFGCVPSiflfdvtfllnrfKEIVYYLGLDGEIEYKDLLFS 82
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDE---GTCPYGGCVLS-------------KALLGAAEAPEIASLWADLYK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 83 KRNEIVNYLSNAGRRLIEDSGGETELGEAEIISPSEVKVNRRIVEFDKLIIATGSKPMIPNIDGIE-------DAISEDD 155
Cdd:pfam07992 65 RKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELVDGDGETITYDRLVIATGARPRLPPIPGVElnvgflvRTLDSAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 156 AVNLNSIPSSMVVIGGGYAGVEIAQIYSRLGSQVTLLSRSE-ILPTFPEDVRSVVKDSLEFDGVNVVENTRIVKLRDG-- 232
Cdd:pfam07992 145 ALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDrLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDgd 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504325421 233 --KVITEKG-EIEGNVIVYATGRRPQlPKGIEKLGLEIDECG-INVDKYKQIKN-NAYAIGDVINKERKTAHSAMFDA 305
Cdd:pfam07992 225 gvEVILKDGtEIDADLVVVAIGRRPN-TELLEAAGLELDERGgIVVDEYLRTSVpGIYAAGDCRVGGPELAQNAVAQG 301
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
2-421 |
2.68e-50 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 176.48 E-value: 2.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 2 KYDIVVIGGGTAGYVAGSILARKGKKVIVIEKEK--FGGVCVNFGCVPSiflfdVTFLLNRFKEIVYylgldgeieykDL 79
Cdd:PRK07251 3 TYDLIVIGFGKAGKTLAAKLASAGKKVALVEESKamYGGTCINIGCIPT-----KTLLVAAEKNLSF-----------EQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 80 LFSKRNEIVNYLSNAGRRLIEDSGGETELGEAEIISPSEVKV----NRRIVEFDKLIIATGSKPMIPNIDGIEDAISEDD 155
Cdd:PRK07251 67 VMATKNTVTSRLRGKNYAMLAGSGVDLYDAEAHFVSNKVIEVqagdEKIELTAETIVINTGAVSNVLPIPGLADSKHVYD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 156 AV---NLNSIPSSMVVIGGGYAGVEIAQIYSRLGSQVTLL-SRSEILPTFPEDVRSVVKDSLEFDGVNVVENTRI--VKL 229
Cdd:PRK07251 147 STgiqSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLdAASTILPREEPSVAALAKQYMEEDGITFLLNAHTteVKN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 230 RDGKVI--TEKGEIEGNVIVYATGRRPQL-PKGIEKLGLEIDECG-INVDKYKQIK-NNAYAIGDViNKERKTAHSAMFD 304
Cdd:PRK07251 227 DGDQVLvvTEDETYRFDALLYATGRKPNTePLGLENTDIELTERGaIKVDDYCQTSvPGVFAVGDV-NGGPQFTYISLDD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 305 ALVASLHILKETTFIPPDNFKIPVVLYTDPQVGVIG-DHKEAK------KFSVFPFAAITRAIINGIKDGYVKIGIN-ER 376
Cdd:PRK07251 306 FRIVFGYLTGDGSYTLEDRGNVPTTMFITPPLSQVGlTEKEAKeaglpyAVKELLVAAMPRAHVNNDLRGAFKVVVNtET 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 504325421 377 NEIVFGEVIGDKAEELINILTLVVNNRMRIESLALMPFVHPSLSE 421
Cdd:PRK07251 386 KEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAE 430
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
3-340 |
1.78e-47 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 170.38 E-value: 1.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 3 YDIVVIGGGTAGYVAGSILARKGKKVIVIE-------KEKFGGV---CVNFGCVPS-IFLFDVTF--LLNRFKEIVYYLG 69
Cdd:PLN02507 26 FDLFVIGAGSGGVRAARFSANFGAKVGICElpfhpisSESIGGVggtCVIRGCVPKkILVYGATFggEFEDAKNYGWEIN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 70 LDGEIEYKDLLFSKRNEIVNyLSNAGRRLIEDSGGETELGEAEIISPSEVKV-----NRRIVEFDKLIIATGSKPMIPNI 144
Cdd:PLN02507 106 EKVDFNWKKLLQKKTDEILR-LNGIYKRLLANAGVKLYEGEGKIVGPNEVEVtqldgTKLRYTAKHILIATGSRAQRPNI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 145 DGIEDAISEDDAVNLNSIPSSMVVIGGGYAGVEIAQIYSRLGSQVTLLSRSEI-LPTFPEDVRSVVKDSLEFDGVNVVEN 223
Cdd:PLN02507 185 PGKELAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELpLRGFDDEMRAVVARNLEGRGINLHPR 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 224 T---RIVKLRDG-KVITEKG-EIEGNVIVYATGRRPQLPK-GIEKLGLEIDECG-INVDKYKQIK-NNAYAIGDVINKER 295
Cdd:PLN02507 265 TnltQLTKTEGGiKVITDHGeEFVADVVLFATGRAPNTKRlNLEAVGVELDKAGaVKVDEYSRTNiPSIWAIGDVTNRIN 344
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 504325421 296 KTAHSAMFDALVASLHILKETTfiPPDNFKIPVVLYTDPQVGVIG 340
Cdd:PLN02507 345 LTPVALMEGTCFAKTVFGGQPT--KPDYENVACAVFCIPPLSVVG 387
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
3-340 |
4.49e-46 |
|
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: 165.40 E-value: 4.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 3 YDIVVIGGGTAGYVAGSILARKGKKVIVIEKEKFGGVCVNFGCVPSIFLFDVTFLLNRFKEIVYYlGLDGEIEYK---DL 79
Cdd:TIGR01421 3 YDYLVIGGGSGGIASARRAAEHGAKALLVEAKKLGGTCVNVGCVPKKVMWYASDLAERMHDAADY-GFYQNDENTfnwPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 80 LFSKRNEIVNYLSNAGRRLIEDSGGETELGEAEIISPSEVKVNRRIVEFDKLIIATGSKPMIP-NIDGIEDAISEDDAVN 158
Cdd:TIGR01421 82 LKEKRDAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVNGRDYTAPHILIATGGKPSFPeNIPGAELGTDSDGFFA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 159 LNSIPSSMVVIGGGYAGVEIAQIYSRLGSQVTLLSRSE-ILPTFPEDVRSVVKDSLEFDGVNVVENTRIVKLR---DGKV 234
Cdd:TIGR01421 162 LEELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRHErVLRSFDSMISETITEEYEKEGINVHKLSKPVKVEktvEGKL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 235 ITE----KGEIEGNVIVYATGRRPQ-LPKGIEKLGLEIDECG-INVDKYKQ-IKNNAYAIGDVINKERKTAhsamfdALV 307
Cdd:TIGR01421 242 VIHfedgKSIDDVDELIWAIGRKPNtKGLGLENVGIKLNEKGqIIVDEYQNtNVPGIYALGDVVGKVELTP------VAI 315
|
330 340 350
....*....|....*....|....*....|....*...
gi 504325421 308 ASLHILKETTFIPPDNFK-----IPVVLYTDPQVGVIG 340
Cdd:TIGR01421 316 AAGRKLSERLFNGKTDDKldynnVPTVVFSHPPIGTIG 353
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
5-430 |
1.84e-43 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 160.32 E-value: 1.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 5 IVVIGGGTAGYVAGSILARKGKKVIVIEKEKFGGVCVNFGCVPSIFLFDVTFLLNRFKEIVYYLGLDG---EIEyKDLLF 81
Cdd:PRK13748 101 VAVIGSGGAAMAAALKAVEQGARVTLIERGTIGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDGGIAAtvpTID-RSRLL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 82 SKRNEIVNYLSNAGRRLIEDSG-------GETELGEAEIISPSEVKVNRRIVEFDKLIIATGSKPMIPNIDGIEDA--IS 152
Cdd:PRK13748 180 AQQQARVDELRHAKYEGILDGNpaitvlhGEARFKDDQTLIVRLNDGGERVVAFDRCLIATGASPAVPPIPGLKETpyWT 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 153 EDDAVNLNSIPSSMVVIGGGYAGVEIAQIYSRLGSQVTLLSRSEILptFPED--VRSVVKDSLEFDGVNVVENTRI--VK 228
Cdd:PRK13748 260 STEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILARSTLF--FREDpaIGEAVTAAFRAEGIEVLEHTQAsqVA 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 229 LRDGKVI--TEKGEIEGNVIVYATGRRPQLPK-GIEKLGLEIDECG-INVDKYKQIKN-NAYAIGDVINKER--KTAHSA 301
Cdd:PRK13748 338 HVDGEFVltTGHGELRADKLLVATGRAPNTRSlALDAAGVTVNAQGaIVIDQGMRTSVpHIYAAGDCTDQPQfvYVAAAA 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 302 MFDALV------ASLhilkettfippDNFKIPVVLYTDPQVGVIG-DHKEAKKFS------VFPFAAITRAIINGIKDGY 368
Cdd:PRK13748 418 GTRAAInmtggdAAL-----------DLTAMPAVVFTDPQVATVGySEAEAHHDGietdsrTLTLDNVPRALANFDTRGF 486
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504325421 369 VKIGINERNEIVFG-EVIGDKAEELINILTLVVNNRMRIESLALMPFVHPSLSEAIVNAAKGF 430
Cdd:PRK13748 487 IKLVIEEGSGRLIGvQAVAPEAGELIQTAALAIRNRMTVQELADQLFPYLTMVEGLKLAAQTF 549
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
2-427 |
5.03e-43 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 157.78 E-value: 5.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 2 KYDIVVIGGGTAGYVAGSILARKGKKVIVIEKEK-------FGGVCVNFGCVPSIFL----------------------- 51
Cdd:PRK06327 4 QFDVVVIGAGPGGYVAAIRAAQLGLKVACIEAWKnpkgkpaLGGTCLNVGCIPSKALlasseefenaghhfadhgihvdg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 52 --FDVTFLLNRFKEIVYylGLDGEIEYkdlLFsKRNEIVNYlsnAGR-RLIEDSGGETEL---GEAEiispsevkvnrRI 125
Cdd:PRK06327 84 vkIDVAKMIARKDKVVK--KMTGGIEG---LF-KKNKITVL---KGRgSFVGKTDAGYEIkvtGEDE-----------TV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 126 VEFDKLIIATGSKPM-IPNIDGIEDAISEDD-AVNLNSIPSSMVVIGGGYAGVEIAQIYSRLGSQVTLLsrsEILPTF-- 201
Cdd:PRK06327 144 ITAKHVIIATGSEPRhLPGVPFDNKIILDNTgALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTIL---EALPAFla 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 202 --PEDVRSVVKDSLEFDGVNVVENTRIVKLRDGK--VITEKGEIEGN--------VIVyATGRRPQLPK-GIEKLGLEID 268
Cdd:PRK06327 221 aaDEQVAKEAAKAFTKQGLDIHLGVKIGEIKTGGkgVSVAYTDADGEaqtlevdkLIV-SIGRVPNTDGlGLEAVGLKLD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 269 ECG-INVDKYKQIK-NNAYAIGDVINKErKTAHSAMFDALVASLHILKETTFIppdNFK-IPVVLYTDPQVGVIG-DHKE 344
Cdd:PRK06327 300 ERGfIPVDDHCRTNvPNVYAIGDVVRGP-MLAHKAEEEGVAVAERIAGQKGHI---DYNtIPWVIYTSPEIAWVGkTEQQ 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 345 AK------KFSVFPFAAITRAIINGIKDGYVKIGINERNEIVFG-EVIGDKAEELINILTLVVNNRMRIESLALMPFVHP 417
Cdd:PRK06327 376 LKaegveyKAGKFPFMANGRALAMGEPDGFVKIIADAKTDEILGvHVIGPNASELIAEAVVAMEFKASSEDIARICHAHP 455
|
490
....*....|
gi 504325421 418 SLSEAIVNAA 427
Cdd:PRK06327 456 TLSEVWHEAA 465
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
3-424 |
1.18e-42 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 158.12 E-value: 1.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 3 YDIVVIGGGTAGYVAGSILARKGKKVIVIE-------KEKFGGV---CVNFGCVPSIFLFDVTFLLNRFKE---IVYYLG 69
Cdd:PLN02546 80 FDLFTIGAGSGGVRASRFASNFGASAAVCElpfatisSDTLGGVggtCVLRGCVPKKLLVYASKYSHEFEEsrgFGWKYE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 70 LDGEIEYKDLLFSKRNEI-------VNYLSNAGRRLIEdsggetelGEAEIISPSEVKVNRRIVEFDKLIIATGSKPMIP 142
Cdd:PLN02546 160 TEPKHDWNTLIANKNAELqrltgiyKNILKNAGVTLIE--------GRGKIVDPHTVDVDGKLYTARNILIAVGGRPFIP 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 143 NIDGIEDAISEDDAVNLNSIPSSMVVIGGGYAGVEIAQIYSRLGSQVTLLSRSE-ILPTFPEDVRSVVKDSLEFDGVNV- 220
Cdd:PLN02546 232 DIPGIEHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKkVLRGFDEEVRDFVAEQMSLRGIEFh 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 221 VENT--RIVKLRDG--KVITEKGEIEG-NVIVYATGRRPQLPK-GIEKLGLEIDECG-INVDKYKQIK-NNAYAIGDVIN 292
Cdd:PLN02546 312 TEESpqAIIKSADGslSLKTNKGTVEGfSHVMFATGRKPNTKNlGLEEVGVKMDKNGaIEVDEYSRTSvPSIWAVGDVTD 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 293 KERKTAHSAMFDALVASLHILKETTfiPPDNFKIPVVLYTDP---QVGVIGDHKEAKKFSVFPFAAITR---AIINGIKD 366
Cdd:PLN02546 392 RINLTPVALMEGGALAKTLFGNEPT--KPDYRAVPSAVFSQPpigQVGLTEEQAIEEYGDVDVFTANFRplkATLSGLPD 469
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 367 G-YVKIGINERNEIVFG-EVIGDKAEELINILTLVVNNRMRIESLALMPFVHPSLSEAIV 424
Cdd:PLN02546 470 RvFMKLIVCAKTNKVLGvHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEEFV 529
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
2-423 |
2.60e-39 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 146.70 E-value: 2.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 2 KYDIVVIGGGTAGYVAGSILARKGKKVIVIEKEK--FGGVCVNFGCVPSiflfdvtfllnrfKEIVYYLGLDGEIEykdL 79
Cdd:PRK08010 3 KYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNamYGGTCINIGCIPT-------------KTLVHDAQQHTDFV---R 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 80 LFSKRNEIVNYLSNAGRRLIEDSGGETEL-GEAEIISPSEVKVNR----RIVEFDKLIIATGSKPMIPNIDGIEDAISED 154
Cdd:PRK08010 67 AIQRKNEVVNFLRNKNFHNLADMPNIDVIdGQAEFINNHSLRVHRpegnLEIHGEKIFINTGAQTVVPPIPGITTTPGVY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 155 DA---VNLNSIPSSMVVIGGGYAGVEIAQIYSRLGSQVTLL-SRSEILPTFPEDVRSVVKDSLEFDGVNVVENTRI--VK 228
Cdd:PRK08010 147 DStglLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILeAASLFLPREDRDIADNIATILRDQGVDIILNAHVerIS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 229 LRDG--KVITEKGEIEGNVIVYATGRRPQLPK-GIEKLGLEIDECG-INVDKY-KQIKNNAYAIGDVINKERKTaHSAMF 303
Cdd:PRK08010 227 HHENqvQVHSEHAQLAVDALLIASGRQPATASlHPENAGIAVNERGaIVVDKYlHTTADNIWAMGDVTGGLQFT-YISLD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 304 DALVASLHILKETTFIPPDNFKIPVVLYTDPQVGVIGDHKEAKKFS-------VFPFAAITRAIINGIKDGYVKIGINER 376
Cdd:PRK08010 306 DYRIVRDELLGEGKRSTDDRKNVPYSVFMTPPLSRVGMTEEQARESgadiqvvTLPVAAIPRARVMNDTRGVLKAIVDNK 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 504325421 377 NEIVFG-EVIGDKAEELINILTLVVNNRMRIESLALMPFVHPSLSEAI 423
Cdd:PRK08010 386 TQRILGaSLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESL 433
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
1-422 |
2.65e-39 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 147.23 E-value: 2.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 1 MKYDIVVIGGGTAGYVAGSILARKGKKVIVIEKEK-FGGVCVNFGCVPSIFLFDVTFLLNRFKEIVYY--LGLDGEIEYK 77
Cdd:PRK05249 4 YDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYRnVGGGCTHTGTIPSKALREAVLRLIGFNQNPLYssYRVKLRITFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 78 DLLFSKRNEI---VNYLSNAGRR----LIEdsggetelGEAEIISPSEVKV-----NRRIVEFDKLIIATGSKPMIP--- 142
Cdd:PRK05249 84 DLLARADHVInkqVEVRRGQYERnrvdLIQ--------GRARFVDPHTVEVecpdgEVETLTADKIVIATGSRPYRPpdv 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 143 NIDG--IEDAiseDDAVNLNSIPSSMVVIGGGYAGVEIAQIYSRLGSQVTLLSR---------SEILPTFPEDVRS---V 208
Cdd:PRK05249 156 DFDHprIYDS---DSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTrdrllsfldDEISDALSYHLRDsgvT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 209 VKDSLEFDGVNVVENTRIVKLRDGKVitekgeIEGNVIVYATGRRPQLPK-GIEKLGLEIDECG-INVDKYKQIKN-NAY 285
Cdd:PRK05249 233 IRHNEEVEKVEGGDDGVIVHLKSGKK------IKADCLLYANGRTGNTDGlNLENAGLEADSRGqLKVNENYQTAVpHIY 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 286 AIGDVINKErKTAHSAMFDALVASLHILKETTFIPPDNfkIPVVLYTDPQVGVIGDHKEAKKFSVFP-------FAAITR 358
Cdd:PRK05249 307 AVGDVIGFP-SLASASMDQGRIAAQHAVGEATAHLIED--IPTGIYTIPEISSVGKTEQELTAAKVPyevgrarFKELAR 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504325421 359 AIINGIKDGYVKIGINERNEIVFG-EVIGDKAEELINILTLVVNNRMRIESLALMPFVHPSLSEA 422
Cdd:PRK05249 384 AQIAGDNVGMLKILFHRETLEILGvHCFGERATEIIHIGQAIMEQKGTIEYFVNTTFNYPTMAEA 448
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
3-428 |
3.77e-36 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 140.82 E-value: 3.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 3 YDIVVIGGGTAGYVAGSILARKGKKVIVI--EKEKFGGVCVNFGCVPSIFLFDVTfllNRFKEI-----VYYLGL----- 70
Cdd:PTZ00153 117 YDVGIIGCGVGGHAAAINAMERGLKVIIFtgDDDSIGGTCVNVGCIPSKALLYAT---GKYRELknlakLYTYGIytnaf 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 71 ----DGEIEYKDLLFSKRNEIVNYLSNAGRRLIED--SGGETELGEAEIISPSEVK---------VNRRIVEFDK----- 130
Cdd:PTZ00153 194 kngkNDPVERNQLVADTVQIDITKLKEYTQSVIDKlrGGIENGLKSKKFCKNSEHVqviyerghiVDKNTIKSEKsgkef 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 131 ----LIIATGSKPMIPNIDGIED--AISEDDAVNLNSIPSSMVVIGGGYAGVEIAQIYSRLGSQVTLLSRS-EILPTFPE 203
Cdd:PTZ00153 274 kvknIIIATGSTPNIPDNIEVDQksVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSpQLLPLLDA 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 204 DV-----RSVVKDSlefdGVNVVENTRIVKLRDGK----VI---TEKGEIEGNVIVY---------------ATGRRPQL 256
Cdd:PTZ00153 354 DVakyfeRVFLKSK----PVRVHLNTLIEYVRAGKgnqpVIighSERQTGESDGPKKnmndiketyvdsclvATGRKPNT 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 257 PK-GIEKLGLEIDECGINVDKYKQIK-------NNAYAIGDViNKERKTAHSAMFDALVASLHIL---KETTFIPPDNF- 324
Cdd:PTZ00153 430 NNlGLDKLKIQMKRGFVSVDEHLRVLredqevyDNIFCIGDA-NGKQMLAHTASHQALKVVDWIEgkgKENVNINVENWa 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 325 -------KIPVVLYTDPQVGVIGD-HKEAKKF--------SVFPFAAITRAI----------------------INGIKD 366
Cdd:PTZ00153 509 skpiiykNIPSVCYTTPELAFIGLtEKEAKELyppdnvgvEISFYKANSKVLcennisfpnnsknnsynkgkynTVDNTE 588
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504325421 367 GYVKI-GINERNEIVFGEVIGDKAEELINILTLVVNNRMRIESLALMPFVHPSLSEAIVNAAK 428
Cdd:PTZ00153 589 GMVKIvYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDAAFK 651
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
3-423 |
3.99e-34 |
|
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: 133.17 E-value: 3.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 3 YDIVVIGGGTAGYVAGSILAR-KGKKVIVIEKEK---------FGGVCVNFGCVPSIFLFDVTFLLNRFKEIVYY-LGLD 71
Cdd:TIGR01423 4 FDLVVIGAGSGGLEAGWNAATlYKKRVAVVDVQThhgppfyaaLGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFgWEFD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 72 GEI---EYKDLLFSKrNEIVNYLSNAGRRLIEDSGG-ETELGEAEIISPSEVKVN---------RRIVEFDKLIIATGSK 138
Cdd:TIGR01423 84 RSSvkaNWKALIAAK-NKAVLDINKSYEGMFADTEGlTFFLGWGALEDKNVVLVResadpksavKERLQAEHILLATGSW 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 139 PMIPNIDGIEDAISEDDAVNLNSIPSSMVVIGGGYAGVEIAQI---YSRLGSQVTLLSRSE-ILPTFPEDVRSVVKDSLE 214
Cdd:TIGR01423 163 PQMLGIPGIEHCISSNEAFYLDEPPRRVLTVGGGFISVEFAGIfnaYKPRGGKVTLCYRNNmILRGFDSTLRKELTKQLR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 215 FDGVNVVEN---TRIVKLRDGK--VITEKG-EIEGNVIVYATGRRPQLPK-GIEKLGLEI-DECGINVDKYKQIK-NNAY 285
Cdd:TIGR01423 243 ANGINIMTNenpAKVTLNADGSkhVTFESGkTLDVDVVMMAIGRVPRTQTlQLDKVGVELtKKGAIQVDEFSRTNvPNIY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 286 AIGDVINKERKTA-----HSAMFDALVASLHilKETtfippDNFKIPVVLYTDPQVGVIGDHKE--AKKF-SVFPFAAIT 357
Cdd:TIGR01423 323 AIGDVTDRVMLTPvaineGAAFVDTVFGNKP--RKT-----DHTRVASAVFSIPPIGTCGLVEEdaAKKFeKVAVYESSF 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504325421 358 RAIINGI-----KDGYVKIGINERNEIVFG-EVIGDKAEELINILTLVVNNRMRIESLALMPFVHPSLSEAI 423
Cdd:TIGR01423 396 TPLMHNIsgskyKKFVAKIVTNHADGTVLGvHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAEEL 467
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
2-425 |
8.88e-34 |
|
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: 132.28 E-value: 8.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 2 KYDIVVIGGGTAGYVAGSILARKGKKVIVIE---------KEKFGGVCVNFGCVPSIFLFDVTFLLNRFKEIVYYlGLDG 72
Cdd:TIGR01438 2 DYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDfvtptplgtRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNY-GWKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 73 EIEYK---DLLFSKRNEIVNYLSNAGRRLIEDSGGETELGEAEIISPSEVKV-----NRRIVEFDKLIIATGSKPMIPNI 144
Cdd:TIGR01438 81 EETVKhdwKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKAtnkkgKEKIYSAERFLIATGERPRYPGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 145 DG-IEDAISEDDAVNLNSIPSSMVVIGGGYAGVEIAQIYSRLGSQVTLLSRSEILPTFPEDVRSVVKDSLEFDGVNVVEN 223
Cdd:TIGR01438 161 PGaKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDCANKVGEHMEEHGVKFKRQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 224 TRIVKLR--DGKVI------TEKGEIEGNVIVYATGRRPQLPK-GIEKLGLEIDECG--INVDKYKQIK-NNAYAIGDVI 291
Cdd:TIGR01438 241 FVPIKVEqiEAKVLveftdsTNGIEEEYDTVLLAIGRDACTRKlNLENVGVKINKKTgkIPADEEEQTNvPYIYAVGDIL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 292 NKERKTAHSAMFDALVASLHILKETTFIpPDNFKIPVVLYTDPQVGVIG--DHKEAKKF-----SVF--PFAAITRAIIN 362
Cdd:TIGR01438 321 EDKPELTPVAIQAGRLLAQRLFKGSTVI-CDYENVPTTVFTPLEYGACGlsEEKAVEKFgeenvEVFhsYFWPLEWTIPS 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504325421 363 GIKDG--YVKI--GINERNEIVFGEVIGDKAEELINILTLVVNNRMRIESLALMPFVHPSLSEAIVN 425
Cdd:TIGR01438 400 RDNHNkcYAKLvcNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTT 466
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
5-428 |
1.68e-33 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 131.14 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 5 IVVIGGGTAGYVAGSILARKGKKVIVIEKEKFGGVCVNFGCVPS---IFLFDVTFLLNRFKEIVYYLGLDGEIEY----- 76
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIERDGLGGAAVLTDCVPSktlIATAEVRTELRRAAELGIRFIDDGEARVdlpav 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 77 ----KDLLFSKRNEIVNYLSNAGRRLIEDSGGETELGEAeiisPSEVKVNR-----RIVEFDKLIIATGSKP-MIPNI-- 144
Cdd:PRK07845 84 narvKALAAAQSADIRARLEREGVRVIAGRGRLIDPGLG----PHRVKVTTadggeETLDADVVLIATGASPrILPTAep 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 145 DGiEDAISEDDAVNLNSIPSSMVVIGGGYAGVEIAQIYSRLGSQVTLL-SRSEILPTFPEDVRSVVKDSLEFDGVNVVEN 223
Cdd:PRK07845 160 DG-ERILTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVsSRDRVLPGEDADAAEVLEEVFARRGMTVLKR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 224 TR-----------IVKLRDGKvitekgEIEGNVIVYATGRRPQLPK-GIEKLGLEIDECG-INVDKYKQIK-NNAYAIGD 289
Cdd:PRK07845 239 SRaesvertgdgvVVTLTDGR------TVEGSHALMAVGSVPNTAGlGLEEAGVELTPSGhITVDRVSRTSvPGIYAAGD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 290 VinkerkT-----AHSAMFDALVASLHILKETtfIPPDNFK-IPVVLYTDPQVGVIG------DHKEAKKFSV-FPFAAI 356
Cdd:PRK07845 313 C------TgvlplASVAAMQGRIAMYHALGEA--VSPLRLKtVASNVFTRPEIATVGvsqaaiDSGEVPARTVmLPLATN 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504325421 357 TRAIINGIKDGYVKIGINERNEIVFGEVI-GDKAEELINILTLVVNNRMRIESLALMPFVHPSLSEAIVNAAK 428
Cdd:PRK07845 385 PRAKMSGLRDGFVKLFCRPGTGVVIGGVVvAPRASELILPIALAVQNRLTVDDLAQTFTVYPSLSGSITEAAR 457
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
3-426 |
2.57e-33 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 130.46 E-value: 2.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 3 YDIVVIGGGTAGYVAGSILArkGKKVIVIEKEKFGGVCVNFGCVPS-IFLFDVTFLLNrFKEIVYYlGLDGEIE------ 75
Cdd:PRK07846 2 YDLIIIGTGSGNSILDERFA--DKRIAIVEKGTFGGTCLNVGCIPTkMFVYAADVART-IREAARL-GVDAELDgvrwpd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 76 YKDLLFSKRNEIvnylSNAGRRLIEDSGGETEL--GEAEIISPSEVKV-NRRIVEFDKLIIATGSKPMIPNIDGIEDAI- 151
Cdd:PRK07846 78 IVSRVFGRIDPI----AAGGEEYRGRDTPNIDVyrGHARFIGPKTLRTgDGEEITADQVVIAAGSRPVIPPVIADSGVRy 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 152 -SEDDAVNLNSIPSSMVVIGGGYAGVEIAQIYSRLGSQVTLLSRS---------EILPTFPEDVRSVVKDSLEFDGVNVV 221
Cdd:PRK07846 154 hTSDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSgrllrhlddDISERFTELASKRWDVRLGRNVVGVS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 222 ENTRIVKLR--DGKVitekgeIEGNVIVYATGRRP---QLpkGIEKLGLEIDECG-INVDKYKQIK-NNAYAIGDVINK- 293
Cdd:PRK07846 234 QDGSGVTLRldDGST------VEADVLLVATGRVPngdLL--DAAAAGVDVDEDGrVVVDEYQRTSaEGVFALGDVSSPy 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 294 ERKtaHSAMFDALVASLHILKETTFIPPDNFKIPVVLYTDPQVGVIG-DHKEAKK------FSVFPFAAITRAIINGIKD 366
Cdd:PRK07846 306 QLK--HVANHEARVVQHNLLHPDDLIASDHRFVPAAVFTHPQIASVGlTENEARAaglditVKVQNYGDVAYGWAMEDTT 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504325421 367 GYVK-IGINERNEIVFGEVIGDKAEELINILTLVVNNRMRIESLALMPF-VHPSLSEAIVNA 426
Cdd:PRK07846 384 GFVKlIADRDTGRLLGAHIIGPQASTLIQPLIQAMSFGLDAREMARGQYwIHPALPEVVENA 445
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
1-296 |
2.65e-31 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 126.27 E-value: 2.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 1 MKYDIVVIGGGTAGYVAGSILARKGKKVIVIEKEKFGGVCVNFGCVPSIFLFDVTFLLNRFKEIVYYlGLDGE------- 73
Cdd:PTZ00058 47 MVYDLIVIGGGSGGMAAARRAARNKAKVALVEKDYLGGTCVNVGCVPKKIMFNAASIHDILENSRHY-GFDTQfsfnlpl 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 74 -IEYKDLLFSKRNEIV-NYLSNAGRRLIEDSG--------------------GETELGEAEIISPSEVKV-NRRIVEFDK 130
Cdd:PTZ00058 126 lVERRDKYIRRLNDIYrQNLKKDNVEYFEGKGsllsenqvlikkvsqvdgeaDESDDDEVTIVSAGVSQLdDGQVIEGKN 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 131 LIIATGSKPMIPNIDGIEDAISEDDAVNLNSiPSSMVVIGGGYAGVEIAQIYSRLGSQVTLLSR-SEILPTFPEDVRSVV 209
Cdd:PTZ00058 206 ILIAVGNKPIFPDVKGKEFTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARgNRLLRKFDETIINEL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 210 KDSLEFDGVNVVEN---TRIVKLRDGKVIT----EKGEIEGNVIVYATGRRPQLPK-GIEKLGLEIDECGINVDKYKQIK 281
Cdd:PTZ00058 285 ENDMKKNNINIITHanvEEIEKVKEKNLTIylsdGRKYEHFDYVIYCVGRSPNTEDlNLKALNIKTPKGYIKVDDNQRTS 364
|
330
....*....|....*.
gi 504325421 282 -NNAYAIGDVINKERK 296
Cdd:PTZ00058 365 vKHIYAVGDCCMVKKN 380
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
2-313 |
1.38e-27 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 113.30 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 2 KYDIVVIGGGTAGYVAGSILARKGKK---VIVIEKEKFggvcvnfgcvpsiFLFdVTFLlnrfkeivYYLgLDGEIEYKD 78
Cdd:COG1252 1 MKRIVIVGGGFAGLEAARRLRKKLGGdaeVTLIDPNPY-------------HLF-QPLL--------PEV-AAGTLSPDD 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 79 LLFSkrneIVNYLSNAGRRLIedsggeteLGEAEIISPSEVKV---NRRIVEFDKLIIATGSKPMIPNIDGIED-AI--- 151
Cdd:COG1252 58 IAIP----LRELLRRAGVRFI--------QGEVTGIDPEARTVtlaDGRTLSYDYLVIATGSVTNFFGIPGLAEhALplk 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 152 SEDDAVNLN----------SIPSSM--VVIGGGYAGVEIA-QIYSRLGS------------QVTLLSRS-EILPTFPEDV 205
Cdd:COG1252 126 TLEDALALRerllaaferaERRRLLtiVVVGGGPTGVELAgELAELLRKllrypgidpdkvRITLVEAGpRILPGLGEKL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 206 RSVVKDSLEFDGVNVVENTRIVKLRDGKVITEKGE-IEGNVIVYATGRRPqlPKGIEKLGLEIDECG-INVDKYKQIKN- 282
Cdd:COG1252 206 SEAAEKELEKRGVEVHTGTRVTEVDADGVTLEDGEeIPADTVIWAAGVKA--PPLLADLGLPTDRRGrVLVDPTLQVPGh 283
|
330 340 350
....*....|....*....|....*....|....*....
gi 504325421 283 -NAYAIGD---VINKER----KTAHSAMFDALVASLHIL 313
Cdd:COG1252 284 pNVFAIGDcaaVPDPDGkpvpKTAQAAVQQAKVLAKNIA 322
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
124-292 |
7.34e-26 |
|
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: 107.20 E-value: 7.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 124 RIVEFDKLIIATGSKPMIPNIDGI-----------EDAISEDDAVNlNSIPSSMVVIGGGYAGVEIAQIYSRLGSQVTLL 192
Cdd:COG0446 75 ETLSYDKLVLATGARPRPPPIPGLdlpgvftlrtlDDADALREALK-EFKGKRAVVIGGGPIGLELAEALRKRGLKVTLV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 193 SRSE-ILPTFPEDVRSVVKDSLEFDGVNVVENTRIVKLR-DGKV---ITEKGEIEGNVIVYATGRRP--QLPKGiekLGL 265
Cdd:COG0446 154 ERAPrLLGVLDPEMAALLEEELREHGVELRLGETVVAIDgDDKVavtLTDGEEIPADLVVVAPGVRPntELAKD---AGL 230
|
170 180
....*....|....*....|....*....
gi 504325421 266 EIDECG-INVDKYKQIKN-NAYAIGDVIN 292
Cdd:COG0446 231 ALGERGwIKVDETLQTSDpDVYAAGDCAE 259
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
3-345 |
1.25e-25 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 109.14 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 3 YDIVVIGGGTAGYVAGSILARKGKKVIVIE---------KEKFGGVCVNFGCVPsiflfdvtfllnrfKEIVYYLGLDGE 73
Cdd:PTZ00052 6 YDLVVIGGGSGGMAAAKEAAAHGKKVALFDyvkpstqgtKWGLGGTCVNVGCVP--------------KKLMHYAANIGS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 74 I----------------EYKDLLFSKRNEI--VNYLSNAGRRlieDSGGETELGEAEIISPSEVKVNR----RIVEFDKL 131
Cdd:PTZ00052 72 IfhhdsqmygwktsssfNWGKLVTTVQNHIrsLNFSYRTGLR---SSKVEYINGLAKLKDEHTVSYGDnsqeETITAKYI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 132 IIATGSKPMIP-NIDG-IEDAISEDDAVNLNSIPSSMVVIGGGYAGVEIAQIYSRLGSQVTLLSRSEILPTFPEDVRSVV 209
Cdd:PTZ00052 149 LIATGGRPSIPeDVPGaKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRSIPLRGFDRQCSEKV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 210 KDSLEFDGVNVVENTRIVKLRDG----KVITEKGEIEG-NVIVYATGRRPQLPkgieklGLEIDECGINVDKY--KQIKN 282
Cdd:PTZ00052 229 VEYMKEQGTLFLEGVVPINIEKMddkiKVLFSDGTTELfDTVLYATGRKPDIK------GLNLNAIGVHVNKSnkIIAPN 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504325421 283 ------NAYAIGDVINKERKTAHSAMFDALVASLHILKETTFIPPDNFkIPVVLYTDPQVGVIGDHKEA 345
Cdd:PTZ00052 303 dctnipNIFAVGDVVEGRPELTPVAIKAGILLARRLFKQSNEFIDYTF-IPTTIFTPIEYGACGYSSEA 370
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
3-314 |
1.94e-21 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 94.03 E-value: 1.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 3 YDIVVIGGGTAGYVAGSILARKGKKVIVIEKEKFGGvcvnfgcvpsiflfdvtfLLNRFKEIVYYLGLDGEIEYKDLLfs 82
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGG------------------QLATTKEIENYPGFPEGISGPELA-- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 83 krneivnylsNAGRRLIEDSGGETELGEAEIISPSE----VKV-NRRIVEFDKLIIATGSKPMIPNIDGIEDA----IS- 152
Cdd:COG0492 61 ----------ERLREQAERFGAEILLEEVTSVDKDDgpfrVTTdDGTEYEAKAVIIATGAGPRKLGLPGEEEFegrgVSy 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 153 ---------EDDAVnlnsipssmVVIGGGYAGVEIAQIYSRLGSQVTLLSRSEILPTFPEDVRSVvkdsLEFDGVNVVEN 223
Cdd:COG0492 131 catcdgfffRGKDV---------VVVGGGDSALEEALYLTKFASKVTLIHRRDELRASKILVERL----RANPKIEVLWN 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 224 TRI-----------VKLRDGKVITEKgEIEGNVIVYATGRRPQLpKGIEKLGLEIDECGinvdkykQIKNNA-------- 284
Cdd:COG0492 198 TEVteiegdgrvegVTLKNVKTGEEK-ELEVDGVFVAIGLKPNT-ELLKGLGLELDEDG-------YIVVDEdmetsvpg 268
|
330 340 350
....*....|....*....|....*....|.
gi 504325421 285 -YAIGDVINKERKTAHSAMFDALVASLHILK 314
Cdd:COG0492 269 vFAAGDVRDYKYRQAATAAGEGAIAALSAAR 299
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
2-290 |
2.68e-19 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 89.43 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 2 KYDIVVIGGGTAGYVAGSILARKGK--KVIVIEKEKfggvcvnfgcvpsiflfdvtfllnrfkEIVYY---L--GLDGEI 74
Cdd:COG1251 1 KMRIVIIGAGMAGVRAAEELRKLDPdgEITVIGAEP---------------------------HPPYNrppLskVLAGET 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 75 EYKDLL-----FSKRNEIVNYLS------NAGRRLIEDSGGETelgeaeiispsevkvnrriVEFDKLIIATGSKPMIPN 143
Cdd:COG1251 54 DEEDLLlrpadFYEENGIDLRLGtrvtaiDRAARTVTLADGET-------------------LPYDKLVLATGSRPRVPP 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 144 IDGIE-DAI----SEDDAVNLNSI---PSSMVVIGGGYAGVEIAQIYSRLGSQVTLLSRSE-ILPT-FPEDVRSVVKDSL 213
Cdd:COG1251 115 IPGADlPGVftlrTLDDADALRAAlapGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPrLLPRqLDEEAGALLQRLL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 214 EFDGVNVVENTRIVKLRDG----KVITEKGE-IEGNVIVYATGRRP--QLPKGIeklGLEIDEcGINVDKYKQ-----Ik 281
Cdd:COG1251 195 EALGVEVRLGTGVTEIEGDdrvtGVRLADGEeLPADLVVVAIGVRPntELARAA---GLAVDR-GIVVDDYLRtsdpdI- 269
|
....*....
gi 504325421 282 nnaYAIGDV 290
Cdd:COG1251 270 ---YAAGDC 275
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
326-426 |
1.03e-18 |
|
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: 81.06 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 326 IPVVLYTDPQVGVIG-DHKEAKKFSV------FPFAAITRAIINGIKDGYVKIGINERNEIVFG-EVIGDKAEELINILT 397
Cdd:pfam02852 1 IPSVVFTDPEIASVGlTEEEAKEKGGevkvgkFPFAANGRALAYGDTDGFVKLVADRETGKILGaHIVGPNAGELIQEAA 80
|
90 100
....*....|....*....|....*....
gi 504325421 398 LVVNNRMRIESLALMPFVHPSLSEAIVNA 426
Cdd:pfam02852 81 LAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
1-289 |
1.45e-15 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 78.54 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 1 MKydIVVIGGGTAGYVAGSILAR--KGKKVIVIEKEKFggvcVNFG-CVPSIFL---FDVT-FLLNRFKEIVYYLGLDGE 73
Cdd:PRK09564 1 MK--IIIIGGTAAGMSAAAKAKRlnKELEITVYEKTDI----VSFGaCGLPYFVggfFDDPnTMIARTPEEFIKSGIDVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 74 IEYkdllfskrnEIVNYLSNAGRRLIEDsggeteLGEAEIISPSevkvnrriveFDKLIIATGSKPMIPNIDGI------ 147
Cdd:PRK09564 75 TEH---------EVVKVDAKNKTITVKN------LKTGSIFNDT----------YDKLMIATGARPIIPPIKNInlenvy 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 148 -----EDAISEDDAVNLNSIPsSMVVIGGGYAGVEIAQIYSRLGSQVTLLSRSE-ILP-TFPEDVRSVVKDSLEFDGVNV 220
Cdd:PRK09564 130 tlksmEDGLALKELLKDEEIK-NIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDrILPdSFDKEITDVMEEELRENGVEL 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504325421 221 VENTRIVKLrDGK-----VITEKGEIEGNVIVYATGRRPQlPKGIEKLGLEIDECG-INVDKY-KQIKNNAYAIGD 289
Cdd:PRK09564 209 HLNEFVKSL-IGEdkvegVVTDKGEYEADVVIVATGVKPN-TEFLEDTGLKTLKNGaIIVDEYgETSIENIYAAGD 282
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
165-236 |
4.43e-14 |
|
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: 67.23 E-value: 4.43e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504325421 165 SMVVIGGGYAGVEIAQIYSRLGSQVTLLSRS-EILPTFPEDVRSVVKDSLEFDGVNVVENTRIVKLR---DGKVIT 236
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRdRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEgngDGVVVV 76
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
119-289 |
4.56e-14 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 73.41 E-value: 4.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 119 VKVNRRIVEFDKLIIATGSKPMIPNIDGIEDAISeddavnLNSI------------PSSMVVIGGGYAGVEIAQIYSRLG 186
Cdd:PRK04965 91 VKSQGNQWQYDKLVLATGASAFVPPIPGRELMLT------LNSQqeyraaetqlrdAQRVLVVGGGLIGTELAMDLCRAG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 187 SQVTLLSR-SEILPTF-PEDVRSVVKDSLEFDGVNVVENT---RIVKLRDG-KVITEKGE-IEGNVIVYATGRRP--QLP 257
Cdd:PRK04965 165 KAVTLVDNaASLLASLmPPEVSSRLQHRLTEMGVHLLLKSqlqGLEKTDSGiRATLDSGRsIEVDAVIAAAGLRPntALA 244
|
170 180 190
....*....|....*....|....*....|...
gi 504325421 258 KGIeklGLEIDEcGINVDKYKQIK-NNAYAIGD 289
Cdd:PRK04965 245 RRA---GLAVNR-GIVVDSYLQTSaPDIYALGD 273
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
100-402 |
1.67e-11 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 66.30 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 100 EDSGGETELGEAEIISPSEVKV----NRRIVEFDKLIIATGSKPMIPNIDGIEdaiSEDDAV-----NLNSIPS------ 164
Cdd:PRK14989 70 EKHGIKVLVGERAITINRQEKVihssAGRTVFYDKLIMATGSYPWIPPIKGSE---TQDCFVyrtieDLNAIEAcarrsk 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 165 SMVVIGGGYAGVEIAQIYSRLGSQVTLLSRSEILPTFPEDVR--SVVKDSLEFDGVNV--VENTR-IV----KLRDGKVI 235
Cdd:PRK14989 147 RGAVVGGGLLGLEAAGALKNLGVETHVIEFAPMLMAEQLDQMggEQLRRKIESMGVRVhtSKNTLeIVqegvEARKTMRF 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 236 TEKGEIEGNVIVYATGRRPQlPKGIEKLGLEIDE-CGINVDKYKQIKN-NAYAIGdvinkERKTAHSAMFD--------A 305
Cdd:PRK14989 227 ADGSELEVDFIVFSTGIRPQ-DKLATQCGLAVAPrGGIVINDSCQTSDpDIYAIG-----ECASWNNRVFGlvapgykmA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 306 LVASLHILK-ETTFIPPDNFKIPVVLYTDpqVGVIGD---HKEAKKFSVFpfaaitraiINGIKDGYVKIGINERNEIVF 381
Cdd:PRK14989 301 QVAVDHLLGsENAFEGADLSAKLKLLGVD--VGGIGDahgRTPGARSYVY---------LDESKEIYKRLIVSEDNKTLL 369
|
330 340
....*....|....*....|.
gi 504325421 382 GEVIGDKAEELINILTLVVNN 402
Cdd:PRK14989 370 GAVLVGDTSDYGNLLQLVLNA 390
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
116-296 |
2.06e-11 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 65.56 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 116 PSEVKVNRRIVEFDKLIIATGSKPMIPNIDGIED------AISED-----------DAVNLNSIPS-------SMVVIGG 171
Cdd:PTZ00318 102 SNNANVNTFSVPYDKLVVAHGARPNTFNIPGVEErafflkEVNHArgirkrivqciERASLPTTSVeerkrllHFVVVGG 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 172 GYAGVE------------IAQIYSRLGS--QVTLL-SRSEILPTFPEDVRSVVKDSLEFDGVNVVENTRIVKLRDGKVIT 236
Cdd:PTZ00318 182 GPTGVEfaaeladffrddVRNLNPELVEecKVTVLeAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEVLDKEVVL 261
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504325421 237 EKGE-IEGNVIVYATGRRPQlpKGIEKLGLEIDECG-INVDKYKQIKN--NAYAIGDVINKERK 296
Cdd:PTZ00318 262 KDGEvIPTGLVVWSTGVGPG--PLTKQLKVDKTSRGrISVDDHLRVKPipNVFALGDCAANEER 323
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
7-292 |
8.10e-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: 63.62 E-value: 8.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 7 VIGGGTAGYVAGSILARKGKKVIVIEK-EKFGGVcVNFGcVPSiflfdvtFLLNrfKEIVyylglDGEIEYkdllfskrn 85
Cdd:COG0493 126 VVGSGPAGLAAAYQLARAGHEVTVFEAlDKPGGL-LRYG-IPE-------FRLP--KDVL-----DREIEL--------- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 86 eivnylsnagrrlIEDSGGETELGeaeiispseVKVNRRIV------EFDKLIIATGS-KPMIPNI-----DGIEDAIse 153
Cdd:COG0493 181 -------------IEALGVEFRTN---------VEVGKDITldelleEFDAVFLATGAgKPRDLGIpgedlKGVHSAM-- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 154 dD---AVNLNSIPSSM-------VVIGGGYAGVEIAQIYSRLG-SQVTLLSRS--EILPTFPEDvrsvVKDSLEfDGVNV 220
Cdd:COG0493 237 -DfltAVNLGEAPDTIlavgkrvVVIGGGNTAMDCARTALRLGaESVTIVYRRtrEEMPASKEE----VEEALE-EGVEF 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 221 VENT---RIVKLRDGKVI------TEKGE-----------IEGN--------VIVyATGRRPQLPKGIEKLGLEIDECG- 271
Cdd:COG0493 311 LFLVapvEIIGDENGRVTglecvrMELGEpdesgrrrpvpIEGSeftlpadlVIL-AIGQTPDPSGLEEELGLELDKRGt 389
|
330 340
....*....|....*....|...
gi 504325421 272 INVDKYKQIKNNA--YAIGDVIN 292
Cdd:COG0493 390 IVVDEETYQTSLPgvFAGGDAVR 412
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
1-79 |
8.47e-11 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 63.72 E-value: 8.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 1 MKYDIVVIGGGTAGYVAGSILARKGKKVIVIEK-EKFGGVCVNF---GcvpsiFLFDV--TFL--LNRFKEIVYYLGLDG 72
Cdd:COG1233 2 MMYDVVVIGAGIGGLAAAALLARAGYRVTVLEKnDTPGGRARTFerpG-----FRFDVgpSVLtmPGVLERLFRELGLED 76
|
....*..
gi 504325421 73 EIEYKDL 79
Cdd:COG1233 77 YLELVPL 83
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
124-311 |
9.94e-11 |
|
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: 9.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 124 RIVEFDKLIIATGSKPMIPNIDG--IEDAISEDDAVNLNSIPSSM------VVIGGGYAGVEIAQIYSRLGSQVTLLSRS 195
Cdd:TIGR02374 93 RTLSYDKLILATGSYPFILPIPGadKKGVYVFRTIEDLDAIMAMAqrfkkaAVIGGGLLGLEAAVGLQNLGMDVSVIHHA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 196 -------------EILPTFPEDVRSVV---KDSLEFDGVNVVENTRivkLRDGKvitekgEIEGNVIVYATGRRPQLPKG 259
Cdd:TIGR02374 173 pglmakqldqtagRLLQRELEQKGLTFlleKDTVEIVGATKADRIR---FKDGS------SLEADLIVMAAGIRPNDELA 243
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504325421 260 IEKlGLEIDEcGINVDKYKQIKN-NAYAIGDVinkerkTAHSAMFDALVASLH 311
Cdd:TIGR02374 244 VSA-GIKVNR-GIIVNDSMQTSDpDIYAVGEC------AEHNGRVYGLVAPLY 288
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
128-291 |
2.72e-10 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 62.11 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 128 FDKLIIATGSKPMIPNID--------GIEDAISEDDAVNLNSIPSSMVViGGGYAGVEIAQ-IYSRlGSQVTLLSRSE-I 197
Cdd:PRK13512 106 YDKLILSPGASANSLGFEsditftlrNLEDTDAIDQFIKANQVDKALVV-GAGYISLEVLEnLYER-GLHPTLIHRSDkI 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 198 LPTFPEDVRSVVKDSLEFDGVNVVENTRIVKLRDGKVITEKGEIEG-NVIVYATGRRPQlPKGIEKLGLEIDECG-INVD 275
Cdd:PRK13512 184 NKLMDADMNQPILDELDKREIPYRLNEEIDAINGNEVTFKSGKVEHyDMIIEGVGTHPN-SKFIESSNIKLDDKGfIPVN 262
|
170
....*....|....*..
gi 504325421 276 KYKQIKN-NAYAIGDVI 291
Cdd:PRK13512 263 DKFETNVpNIYAIGDII 279
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
5-312 |
7.56e-10 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 60.39 E-value: 7.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 5 IVVIGGGTAGYVAGSILARKGKKVIVIEKEKFGGVCVNFGcVPsiflfDVTFLLNRFKEIVYylgldgEIEYKDLLFSKR 84
Cdd:PRK12770 21 VAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLMLFG-IP-----EFRIPIERVREGVK------ELEEAGVVFHTR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 85 NEIVnylsnAGRRLIEDSGgeTELGEaEIISPSEVkvnrrIVEFDKLIIATGS----KPMIP--NIDGIEDAIS---EDD 155
Cdd:PRK12770 89 TKVC-----CGEPLHEEEG--DEFVE-RIVSLEEL-----VKKYDAVLIATGTwksrKLGIPgeDLPGVYSALEylfRIR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 156 AVNLNSIPSS---------MVVIGGGYAGVEIAQIYSRLGSQ-VTLLSRSEI--LPTFPEDVRSVVKDSLEF-------- 215
Cdd:PRK12770 156 AAKLGYLPWEkvppvegkkVVVVGAGLTAVDAALEAVLLGAEkVYLAYRRTIneAPAGKYEIERLIARGVEFlelvtpvr 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 216 -DGVNVVENTRIVKLRDGK----------VIT-EKGEIEGNVIVYATGRRPQLPKGIEKLGLEIDECG-INVDKYKQIKN 282
Cdd:PRK12770 236 iIGEGRVEGVELAKMRLGEpdesgrprpvPIPgSEFVLEADTVVFAIGEIPTPPFAKECLGIELNRKGeIVVDEKHMTSR 315
|
330 340 350
....*....|....*....|....*....|.
gi 504325421 283 -NAYAIGDVINKERKTAhSAMFDALVASLHI 312
Cdd:PRK12770 316 eGVFAAGDVVTGPSKIG-KAIKSGLRAAQSI 345
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
3-241 |
9.65e-08 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 53.74 E-value: 9.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 3 YDIVVIGGGTAGYVAGSILARKGKKVIVIEK-----EKF----GGVCvNF--GCVPSIFLFD-----VTFL---LNRFK- 62
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKgkklgRKIlisgGGRC-NVtnLSEEPDNFLSrypgnPKFLksaLSRFTp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 63 ----EIVYYLGLDGEIEYKDLLFSKRN---EIVNYLSNAgrrlIEDSGGE----TELGEAEIISPS--EVKVNRRIVEFD 129
Cdd:pfam03486 80 wdfiAFFESLGVPLKEEDHGRLFPDSDkasDIVDALLNE----LKELGVKirlrTRVLSVEKDDDGrfRVKTGGEELEAD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 130 KLIIATGSKpmipnidgiedaiseddavnlnSIPSsmvvIGGGYAGVEIAQiysRLGsqvtllsrSEILPTFPEDVRSVV 209
Cdd:pfam03486 156 SLVLATGGL----------------------SWPK----TGSTGFGYPLAE---QFG--------HTIIPLRPALVPFTI 198
|
250 260 270
....*....|....*....|....*....|....*.
gi 504325421 210 KDSLEFD----GVNvVENtrIVKLRDGKVITEKGEI 241
Cdd:pfam03486 199 DEPFLFLkrlsGIS-LKN--VVLSNGKGGITFRGEL 231
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
1-31 |
1.18e-06 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 50.62 E-value: 1.18e-06
10 20 30
....*....|....*....|....*....|.
gi 504325421 1 MKYDIVVIGGGTAGYVAGSILARKGKKVIVI 31
Cdd:PRK05329 1 MKFDVLVIGGGLAGLTAALAAAEAGKRVALV 31
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
114-403 |
1.29e-06 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 50.31 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 114 ISPSE---VKVNRRIVEFDKLIIATGSKPM-IPNIDGIEDAI----SEDDAVNLNSI---PSSMVVIGGGYAGVEIAQIY 182
Cdd:PRK09754 84 LGRDTrelVLTNGESWHWDQLFIATGAAARpLPLLDALGERCftlrHAGDAARLREVlqpERSVVIVGAGTIGLELAASA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 183 SRLGSQVTLLSRSEIL--PTFPEDVRSVVKDSLEFDGVNVVENTRIVKLRDGK---VITEKGE-IEGNVIVYATGR--RP 254
Cdd:PRK09754 164 TQRRCKVTVIELAATVmgRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEkveLTLQSGEtLQADVVIYGIGIsaND 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 255 QLPKgieKLGLEIDEcGINVDKYKQIKNNA-YAIGDV-INKE-------RKTAHSAMFDALVASLHILKETTFIPPdnfk 325
Cdd:PRK09754 244 QLAR---EANLDTAN-GIVIDEACRTCDPAiFAGGDVaITRLdngalhrCESWENANNQAQIAAAAMLGLPLPLLP---- 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 326 iPVVLYTDpQVGV----IGDHKeAKKFsvfpfaaitraIINGIKDGYVKIGINERNEIVFGEVIGDKAEELINILTLVVN 401
Cdd:PRK09754 316 -PPWFWSD-QYSDnlqfIGDMR-GDDW-----------LCRGNPETQKAIWFNLQNGVLIGAVTLNQGREIRPIRKWIQS 381
|
..
gi 504325421 402 NR 403
Cdd:PRK09754 382 GK 383
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
4-38 |
2.37e-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: 49.59 E-value: 2.37e-06
10 20 30
....*....|....*....|....*....|....*.
gi 504325421 4 DIVVIGGGTAGYVAGSILARKGKKVIVIEKE-KFGG 38
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGqPFGG 36
|
|
| GlpB |
COG3075 |
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism]; |
1-31 |
2.51e-06 |
|
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 442309 Cd Length: 415 Bit Score: 49.41 E-value: 2.51e-06
10 20 30
....*....|....*....|....*....|.
gi 504325421 1 MKYDIVVIGGGTAGYVAGSILARKGKKVIVI 31
Cdd:COG3075 1 MKFDVVVIGGGLAGLTAAIRAAEAGLRVAIV 31
|
|
| COG3573 |
COG3573 |
Predicted oxidoreductase [General function prediction only]; |
1-38 |
3.86e-06 |
|
Predicted oxidoreductase [General function prediction only];
Pssm-ID: 442794 [Multi-domain] Cd Length: 551 Bit Score: 49.02 E-value: 3.86e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 504325421 1 MKYDIVVIGGGTAGYVAGSILARKGKKVIVIEKE---KFGG 38
Cdd:COG3573 4 MDADVIVVGAGLAGLVAAAELADAGRRVLLLDQEpeaNLGG 44
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
3-39 |
4.32e-06 |
|
geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 273936 [Multi-domain] Cd Length: 295 Bit Score: 48.08 E-value: 4.32e-06
10 20 30
....*....|....*....|....*....|....*..
gi 504325421 3 YDIVVIGGGTAGYVAGSILARKGKKVIVIEKEKFGGV 39
Cdd:TIGR02032 1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPRY 37
|
|
| Trp_halogenase |
pfam04820 |
Tryptophan halogenase; Tryptophan halogenase catalyzes the chlorination of tryptophan to form ... |
4-71 |
5.82e-06 |
|
Tryptophan halogenase; Tryptophan halogenase catalyzes the chlorination of tryptophan to form 7-chlorotryptophan. This is the first step in the biosynthesis of pyrrolnitrin, an antibiotic with broad-spectrum anti-fungal activity. Tryptophan halogenase is NADH-dependent.
Pssm-ID: 398475 [Multi-domain] Cd Length: 457 Bit Score: 48.48 E-value: 5.82e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504325421 4 DIVVIGGGTAGYVAGSILARKGKK---VIVIEKEKFGGVCVNFGCVPSIflfdVTFllNRFkeivyyLGLD 71
Cdd:pfam04820 1 KIVIVGGGTAGWMAAAALARALKGgldVTLVESEEIGTVGVGEATIPSI----RTF--NRM------LGID 59
|
|
| PRK12834 |
PRK12834 |
putative FAD-binding dehydrogenase; Reviewed |
1-34 |
7.20e-06 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 183782 [Multi-domain] Cd Length: 549 Bit Score: 48.36 E-value: 7.20e-06
10 20 30
....*....|....*....|....*....|....
gi 504325421 1 MKYDIVVIGGGTAGYVAGSILARKGKKVIVIEKE 34
Cdd:PRK12834 3 MDADVIVVGAGLAGLVAAAELADAGKRVLLLDQE 36
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
118-272 |
1.50e-05 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 46.45 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 118 EVKVNRRIVEFDKLIIATG--SKPMIPNIDGIEDAISEDDavnlNSIPSSM---VVIGGGYAGVEIAQIYSRLGSQVTLL 192
Cdd:pfam13738 109 VVTTSKGTYQARYVIIATGefDFPNKLGVPELPKHYSYVK----DFHPYAGqkvVVIGGYNSAVDAALELVRKGARVTVL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 193 SRSEILPTFPEDVRSVVK-DSLEFdgVNVVENTRIVKLRDGKVITEKGEIEGNVIV---------------YATGRRPQL 256
Cdd:pfam13738 185 YRGSEWEDRDSDPSYSLSpDTLNR--LEELVKNGKIKAHFNAEVKEITEVDVSYKVhtedgrkvtsnddpiLATGYHPDL 262
|
170
....*....|....*.
gi 504325421 257 pKGIEKLGLEIDECGI 272
Cdd:pfam13738 263 -SFLKKGLFELDEDGR 277
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
1-38 |
1.80e-05 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 46.75 E-value: 1.80e-05
10 20 30
....*....|....*....|....*....|....*...
gi 504325421 1 MKYDIVVIGGGTAGYVAGSILARKGKKVIVIEKEKFGG 38
Cdd:COG1053 2 HEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRG 39
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
1-251 |
3.80e-05 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 45.67 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 1 MKYDIVVIGGGtagyVAG-SI---LARKGKKVIVIEKEKFGGVC--VNFGCVPSIFLFDVTFLLNRfkeivyyLGLDGei 74
Cdd:COG0665 1 ATADVVVIGGG----IAGlSTayhLARRGLDVTVLERGRPGSGAsgRNAGQLRPGLAALADRALVR-------LAREA-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 75 eyKDLLfskrneivnylsnagRRLIEDSGGETELGEAEII----SPSEVKVNRRIVEfdkliiatgskpmIPNIDGIE-D 149
Cdd:COG0665 68 --LDLW---------------RELAAELGIDCDFRRTGVLylarTEAELAALRAEAE-------------ALRALGLPvE 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 150 AISEDDAVNLNSIPSSMVVIGGgyagveiaqIYSRLGSQVtllsrseilptfpeDVRSVVK---DSLEFDGVNVVENTRI 226
Cdd:COG0665 118 LLDAAELREREPGLGSPDYAGG---------LYDPDDGHV--------------DPAKLVRalaRAARAAGVRIREGTPV 174
|
250 260 270
....*....|....*....|....*....|
gi 504325421 227 VKL-RDGK----VITEKGEIEGNVIVYATG 251
Cdd:COG0665 175 TGLeREGGrvtgVRTERGTVRADAVVLAAG 204
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
4-38 |
6.21e-05 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 44.91 E-value: 6.21e-05
10 20 30
....*....|....*....|....*....|....*.
gi 504325421 4 DIVVIGGGTAGYVAGSILARKGKKVIVIEKEKF-GG 38
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRGFlGG 36
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
162-292 |
9.98e-05 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 44.76 E-value: 9.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 162 IPSSMVVIGGGYAGVEIAQIYSRLGSQ------VTLLSRSEILPTFPEDVRSVVkDSLEfDGVN----------VVENTR 225
Cdd:PRK13984 417 IPRSLVVIGGGNVAMDIARSMARLQKMeygevnVKVTSLERTFEEMPADMEEIE-EGLE-EGVViypgwgpmevVIENDK 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 226 IVKLRDGKVI---------------TEKGEIEGNVIVYATGRRPQ---LPKGIeKLGLEIDECGINVDKYKQIKNN-AYA 286
Cdd:PRK13984 495 VKGVKFKKCVevfdeegrfnpkfdeSDQIIVEADMVVEAIGQAPDysyLPEEL-KSKLEFVRGRILTNEYGQTSIPwLFA 573
|
....*.
gi 504325421 287 IGDVIN 292
Cdd:PRK13984 574 GGDIVH 579
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
5-77 |
1.31e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 44.11 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 5 IVVIGGGTAGYVAGSILARKGKKVIVIEK-EKFGGV--CVNFGCVP------SIFLFDVTfLLNRFKEivyyLGLDGEIE 75
Cdd:PRK07233 2 IAIVGGGIAGLAAAYRLAKRGHEVTVFEAdDQLGGLaaSFEFGGLPierfyhHIFKSDEA-LLELLDE----LGLEDKLR 76
|
..
gi 504325421 76 YK 77
Cdd:PRK07233 77 WR 78
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
4-49 |
1.46e-04 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 43.69 E-value: 1.46e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 504325421 4 DIVVIGGGTAGYVAGSILARKGKKV--IVIEKEKFGGVcvnfGCVPSI 49
Cdd:pfam01134 1 DVIVIGGGHAGCEAALAAARMGAKVllITHNTDTIAEL----SCNPSI 44
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
3-38 |
1.88e-04 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 43.94 E-value: 1.88e-04
10 20 30
....*....|....*....|....*....|....*..
gi 504325421 3 YDIVVIGGGTAGYVAGSILARKGKKVIVIEKE-KFGG 38
Cdd:PRK06134 13 CDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDpVFGG 49
|
|
| PTZ00367 |
PTZ00367 |
squalene epoxidase; Provisional |
3-36 |
1.89e-04 |
|
squalene epoxidase; Provisional
Pssm-ID: 240384 [Multi-domain] Cd Length: 567 Bit Score: 43.69 E-value: 1.89e-04
10 20 30
....*....|....*....|....*....|....
gi 504325421 3 YDIVVIGGGTAGYVAGSILARKGKKVIVIEKEKF 36
Cdd:PTZ00367 34 YDVIIVGGSIAGPVLAKALSKQGRKVLMLERDLF 67
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
3-38 |
2.21e-04 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 43.49 E-value: 2.21e-04
10 20 30
....*....|....*....|....*....|....*..
gi 504325421 3 YDIVVIGGGTAGYVAGSILARKGKKVIVIEK-EKFGG 38
Cdd:PRK07843 8 YDVVVVGSGAAGMVAALTAAHRGLSTVVVEKaPHYGG 44
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
1-33 |
2.44e-04 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 43.00 E-value: 2.44e-04
10 20 30
....*....|....*....|....*....|...
gi 504325421 1 MKYDIVVIGGGTAGYVAGSILARKGKKVIVIEK 33
Cdd:COG0654 2 MRTDVLIVGGGPAGLALALALARAGIRVTVVER 34
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
2-76 |
2.46e-04 |
|
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440845 [Multi-domain] Cd Length: 443 Bit Score: 43.28 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 2 KYDIVVIGGGTAGYVAGSILARKGKKVIVIEKE-KFGGVC--VNFGcvpsIFLFDV---TFLLNR--FKEIVYYLGLDGE 73
Cdd:COG1232 1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASdRVGGLIrtVEVD----GFRIDRgphSFLTRDpeVLELLRELGLGDE 76
|
...
gi 504325421 74 IEY 76
Cdd:COG1232 77 LVW 79
|
|
| PRK06185 |
PRK06185 |
FAD-dependent oxidoreductase; |
1-64 |
3.32e-04 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 235729 [Multi-domain] Cd Length: 407 Bit Score: 42.92 E-value: 3.32e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 1 MKYDIVVIGGGTAGYVAGSILARKGKKVIVIEKEK-----FGGVCVNfgcvPS-IFLFDVTFLLNRFKEI 64
Cdd:PRK06185 5 ETTDCCIVGGGPAGMMLGLLLARAGVDVTVLEKHAdflrdFRGDTVH----PStLELMDELGLLERFLEL 70
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
7-40 |
3.35e-04 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 38.67 E-value: 3.35e-04
10 20 30
....*....|....*....|....*....|....*
gi 504325421 7 VIGGGTAGYVAGSILARKGKKVIVIEK-EKFGGVC 40
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKrDRLGGNA 35
|
|
| glycerol3P_GlpB |
TIGR03378 |
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are ... |
3-31 |
3.51e-04 |
|
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are the B subunit, product of the glpB gene, of a three-subunit, membrane-anchored, FAD-dependent anaerobic glycerol-3-phosphate dehydrogenase. [Energy metabolism, Anaerobic]
Pssm-ID: 213807 Cd Length: 419 Bit Score: 42.70 E-value: 3.51e-04
10 20
....*....|....*....|....*....
gi 504325421 3 YDIVVIGGGTAGYVAGSILARKGKKVIVI 31
Cdd:TIGR03378 1 FDVIIIGGGLAGLSCALRLAEAGKKCAII 29
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
2-32 |
7.36e-04 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 41.83 E-value: 7.36e-04
10 20 30
....*....|....*....|....*....|.
gi 504325421 2 KYDIVVIGGGTAGYVAGSILARKGKKVIVIE 32
Cdd:COG1231 7 GKDVVIVGAGLAGLAAARELRKAGLDVTVLE 37
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
1-38 |
1.26e-03 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 41.22 E-value: 1.26e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 504325421 1 MKYDIVVIGGGTAGyVAGSILARK-GKKVIVIEKEK-FGG 38
Cdd:PRK12842 8 LTCDVLVIGSGAGG-LSAAITARKlGLDVVVLEKEPvFGG 46
|
|
| PRK10015 |
PRK10015 |
oxidoreductase; Provisional |
2-38 |
1.49e-03 |
|
oxidoreductase; Provisional
Pssm-ID: 182194 [Multi-domain] Cd Length: 429 Bit Score: 40.73 E-value: 1.49e-03
10 20 30
....*....|....*....|....*....|....*..
gi 504325421 2 KYDIVVIGGGTAGYVAGSILARKGKKVIVIEKEKFGG 38
Cdd:PRK10015 5 KFDAIVVGAGVAGSVAALVMARAGLDVLVIERGDSAG 41
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
1-44 |
1.69e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 40.64 E-value: 1.69e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 504325421 1 MKYDIVVIGGGTAGYVAGSILARKGKKVIVIEKE-KFGGVC--VNFG 44
Cdd:PRK07208 3 NKKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADpVVGGISrtVTYK 49
|
|
| PRK08849 |
PRK08849 |
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional |
2-32 |
1.92e-03 |
|
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
Pssm-ID: 181564 [Multi-domain] Cd Length: 384 Bit Score: 40.14 E-value: 1.92e-03
10 20 30
....*....|....*....|....*....|.
gi 504325421 2 KYDIVVIGGGTAGYVAGSILARKGKKVIVIE 32
Cdd:PRK08849 3 KYDIAVVGGGMVGAATALGFAKQGRSVAVIE 33
|
|
| FAD_binding_3 |
pfam01494 |
FAD binding domain; This domain is involved in FAD binding in a number of enzymes. |
2-33 |
2.08e-03 |
|
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
Pssm-ID: 396193 [Multi-domain] Cd Length: 348 Bit Score: 40.00 E-value: 2.08e-03
10 20 30
....*....|....*....|....*....|..
gi 504325421 2 KYDIVVIGGGTAGYVAGSILARKGKKVIVIEK 33
Cdd:pfam01494 1 ETDVLIVGGGPAGLMLALLLARAGVRVVLVER 32
|
|
| BetA |
COG2303 |
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General ... |
1-32 |
2.32e-03 |
|
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General function prediction only]; Choline dehydrogenase or related flavoprotein is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 441878 [Multi-domain] Cd Length: 531 Bit Score: 40.20 E-value: 2.32e-03
10 20 30
....*....|....*....|....*....|...
gi 504325421 1 MKYDIVVIGGGTAGYVAGSILAR-KGKKVIVIE 32
Cdd:COG2303 3 EEYDYVIVGAGSAGCVLANRLSEdAGLRVLLLE 35
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
4-38 |
2.69e-03 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 39.69 E-value: 2.69e-03
10 20 30
....*....|....*....|....*....|....*....
gi 504325421 4 DIVVIGGGtagyVAG-SI---LARKGKKVIVIEKEKFGG 38
Cdd:pfam01266 1 DVVVIGGG----IVGlSTayeLARRGLSVTLLERGDDPG 35
|
|
| solA |
PRK11259 |
N-methyl-L-tryptophan oxidase; |
1-33 |
2.93e-03 |
|
N-methyl-L-tryptophan oxidase;
Pssm-ID: 236887 [Multi-domain] Cd Length: 376 Bit Score: 39.82 E-value: 2.93e-03
10 20 30
....*....|....*....|....*....|...
gi 504325421 1 MKYDIVVIGGGTAGYVAGSILARKGKKVIVIEK 33
Cdd:PRK11259 2 MRYDVIVIGLGSMGSAAGYYLARRGLRVLGLDR 34
|
|
| PRK08274 |
PRK08274 |
FAD-dependent tricarballylate dehydrogenase TcuA; |
1-33 |
3.15e-03 |
|
FAD-dependent tricarballylate dehydrogenase TcuA;
Pssm-ID: 236214 [Multi-domain] Cd Length: 466 Bit Score: 39.86 E-value: 3.15e-03
10 20 30
....*....|....*....|....*....|...
gi 504325421 1 MKYDIVVIGGGTAGYVAGSILARKGKKVIVIEK 33
Cdd:PRK08274 3 SMVDVLVIGGGNAALCAALAAREAGASVLLLEA 35
|
|
| PRK10157 |
PRK10157 |
putative oxidoreductase FixC; Provisional |
3-38 |
3.56e-03 |
|
putative oxidoreductase FixC; Provisional
Pssm-ID: 182273 [Multi-domain] Cd Length: 428 Bit Score: 39.51 E-value: 3.56e-03
10 20 30
....*....|....*....|....*....|....*.
gi 504325421 3 YDIVVIGGGTAGYVAGSILARKGKKVIVIEKEKFGG 38
Cdd:PRK10157 6 FDAIIVGAGLAGSVAALVLAREGAQVLVIERGNSAG 41
|
|
| LhgO |
COG0579 |
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism]; |
1-34 |
3.76e-03 |
|
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
Pssm-ID: 440344 [Multi-domain] Cd Length: 418 Bit Score: 39.36 E-value: 3.76e-03
10 20 30
....*....|....*....|....*....|....*....
gi 504325421 1 MKYDIVVIGGGtagyVAGSILAR-----KGKKVIVIEKE 34
Cdd:COG0579 3 EMYDVVIIGAG----IVGLALARelsryEDLKVLVLEKE 37
|
|
| PRK07608 |
PRK07608 |
UbiH/UbiF family hydroxylase; |
1-32 |
3.80e-03 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181057 [Multi-domain] Cd Length: 388 Bit Score: 39.55 E-value: 3.80e-03
10 20 30
....*....|....*....|....*....|..
gi 504325421 1 MKYDIVVIGGGTAGYVAGSILARKGKKVIVIE 32
Cdd:PRK07608 4 MKFDVVVVGGGLVGASLALALAQSGLRVALLA 35
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
10-159 |
4.98e-03 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 38.80 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 10 GGTAGYVAGSILARKGKKVIVIEKEKFGGVCVNFGCVPS-----IFLFDVT-FLLNRFKEIVYYLGLDGEIEYKDllfsk 83
Cdd:COG0644 1 AGPAGSAAARRLARAGLSVLLLEKGSFPGDKICGGGLLPraleeLEPLGLDePLERPVRGARFYSPGGKSVELPP----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504325421 84 rNEIVNYLSNAG------RRLIEDSGGETELGEA--EII-SPSEVKV---NRRIVEFDKLIIATGSKPMIPNIDGIEDAI 151
Cdd:COG0644 76 -GRGGGYVVDRArfdrwlAEQAEEAGAEVRTGTRvtDVLrDDGRVVVrtgDGEEIRADYVVDADGARSLLARKLGLKRRS 154
|
....*...
gi 504325421 152 SEDDAVNL 159
Cdd:COG0644 155 DEPQDYAL 162
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
4-38 |
6.12e-03 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 39.07 E-value: 6.12e-03
10 20 30
....*....|....*....|....*....|....*.
gi 504325421 4 DIVVIGGGTAGYVAGSILARKGKKVIVIEKEKF-GG 38
Cdd:COG1148 142 RALVIGGGIAGMTAALELAEQGYEVYLVEKEPElGG 177
|
|
| PRK07494 |
PRK07494 |
UbiH/UbiF family hydroxylase; |
3-31 |
6.21e-03 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181001 [Multi-domain] Cd Length: 388 Bit Score: 38.73 E-value: 6.21e-03
10 20
....*....|....*....|....*....
gi 504325421 3 YDIVVIGGGTAGYVAGSILARKGKKVIVI 31
Cdd:PRK07494 8 TDIAVIGGGPAGLAAAIALARAGASVALV 36
|
|
| PRK09126 |
PRK09126 |
FAD-dependent hydroxylase; |
1-33 |
7.05e-03 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236385 [Multi-domain] Cd Length: 392 Bit Score: 38.38 E-value: 7.05e-03
10 20 30
....*....|....*....|....*....|...
gi 504325421 1 MKYDIVVIGGGTAGYVAGSILARKGKKVIVIEK 33
Cdd:PRK09126 2 MHSDIVVVGAGPAGLSFARSLAGSGLKVTLIER 34
|
|
| PRK08244 |
PRK08244 |
monooxygenase; |
1-35 |
7.10e-03 |
|
monooxygenase;
Pssm-ID: 236199 [Multi-domain] Cd Length: 493 Bit Score: 38.57 E-value: 7.10e-03
10 20 30
....*....|....*....|....*....|....*
gi 504325421 1 MKYDIVVIGGGTAGYVAGSILARKGKKVIVIEKEK 35
Cdd:PRK08244 1 MKYEVIIIGGGPVGLMLASELALAGVKTCVIERLK 35
|
|
| |
