|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
1-466 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 641.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 1 MNSYDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKYST------LGGTCLNVGCIPSKALLDSSHHYEDAVKHFEEHGIEV 74
Cdd:PRK06327 2 SKQFDVVVIGAGPGGYVAAIRAAQLGLKVACIEAWKNpkgkpaLGGTCLNVGCIPSKALLASSEEFENAGHHFADHGIHV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 75 pGEVKVNLEKMIARKQAVVDQTTGGIDFLMKKNNIDVYQGLGSFK----DATHITIAGEETTEIEAKNTIIATGSKPSNL 150
Cdd:PRK06327 82 -DGVKIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVgktdAGYEIKVTGEDETVITAKHVIIATGSEPRHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 151 PFIELDKERIITSTEALKLKEIPKHMIVIGGGVIGLELGQVYRRLGAEVTVVEYMDRIIPTMDAGLSKELNKVFKKAKFK 230
Cdd:PRK06327 161 PGVPFDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAAADEQVAKEAAKAFTKQGLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 231 MQVSHKVKSVERKGDEVIVKADNKKGEEVEFKGDYCLVSVGRSPYTDGLNAEAAGVKLDDRGRVEVDAHLQTSASNIYAI 310
Cdd:PRK06327 241 IHLGVKIGEIKTGGKGVSVAYTDADGEAQTLEVDKLIVSIGRVPNTDGLGLEAVGLKLDERGFIPVDDHCRTNVPNVYAI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 311 GDVVKGAMLAHKAEEEGVFVAETIAGQKPHIDYNLIPGVVYTWPEVAAVGKTEEELKEAGIEYKTGSFPMRALGRSRASM 390
Cdd:PRK06327 321 GDVVRGPMLAHKAEEEGVAVAERIAGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLKAEGVEYKAGKFPFMANGRALAMG 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2731058258 391 DLDGFVKILADKTTDEILGVHMIGARAADMIAEAVVAMEYRASAEDVSRMSHAHPTFTEAIKEAALAATEdRALHI 466
Cdd:PRK06327 401 EPDGFVKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEVWHEAALAVDK-RPLHF 475
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
1-458 |
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: 639.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 1 MNSYDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKySTLGGTCLNVGCIPSKALLDSSHHYEDAvKHFEEHGIEVpGEVKV 80
Cdd:COG1249 1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEK-GRLGGTCLNVGCIPSKALLHAAEVAHEA-RHAAEFGISA-GAPSV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 81 NLEKMIARKQAVVDQTTGGIDFLMKKNNIDVYQGLGSFKDATHITIAGEETteIEAKNTIIATGSKPSNLPFIELDKERI 160
Cdd:COG1249 78 DWAALMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVTGGET--LTADHIVIATGSRPRVPPIPGLDEVRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 161 ITSTEALKLKEIPKHMIVIGGGVIGLELGQVYRRLGAEVTVVEYMDRIIPTMDAGLSKELNKVFKKAKFKMQVSHKVKSV 240
Cdd:COG1249 156 LTSDEALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 241 ERKGDEVIVKADNKKGEEVEfKGDYCLVSVGRSPYTDGLNAEAAGVKLDDRGRVEVDAHLQTSASNIYAIGDVVKGAMLA 320
Cdd:COG1249 236 EKTGDGVTVTLEDGGGEEAV-EADKVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRTSVPGIYAIGDVTGGPQLA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 321 HKAEEEGVFVAETIAGQKPH-IDYNLIPGVVYTWPEVAAVGKTEEELKEAGIEYKTGSFPMRALGRSRASMDLDGFVKIL 399
Cdd:COG1249 315 HVASAEGRVAAENILGKKPRpVDYRAIPSVVFTDPEIASVGLTEEEAREAGIDVKVGKFPFAANGRALALGETEGFVKLI 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2731058258 400 ADKTTDEILGVHMIGARAADMIAEAVVAMEYRASAEDVSRMSHAHPTFTEAIKEAALAA 458
Cdd:COG1249 395 ADAETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAALAL 453
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
3-465 |
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: 591.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 3 SYDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKySTLGGTCLNVGCIPSKALLDSSHHYEDAvKHFEEHGIEVPGeVKVNL 82
Cdd:TIGR01350 1 AYDVIVIGGGPGGYVAAIRAAQLGLKVALVEK-EYLGGTCLNVGCIPTKALLHSAEVYDEI-KHAKDLGIEVEN-VSVDW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 83 EKMIARKQAVVDQTTGGIDFLMKKNNIDVYQGLGSFKDATHITIAGEETTE-IEAKNTIIATGSKPSNLPF-IELDKERI 160
Cdd:TIGR01350 78 EKMQKRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGENGEEtLEAKNIIIATGSRPRSLPGpFDFDGKVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 161 ITSTEALKLKEIPKHMIVIGGGVIGLELGQVYRRLGAEVTVVEYMDRIIPTMDAGLSKELNKVFKKAKFKMQVSHKVKSV 240
Cdd:TIGR01350 158 ITSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 241 ERKGDEVIVKadNKKGEEVEFKGDYCLVSVGRSPYTDGLNAEAAGVKLDDRGRVEVDAHLQTSASNIYAIGDVVKGAMLA 320
Cdd:TIGR01350 238 EKNDDQVTYE--NKGGETETLTGEKVLVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDVIGGPMLA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 321 HKAEEEGVFVAETIAGQKP-HIDYNLIPGVVYTWPEVAAVGKTEEELKEAGIEYKTGSFPMRALGRSRASMDLDGFVKIL 399
Cdd:TIGR01350 316 HVASHEGIVAAENIAGKEPaHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGYDVKIGKFPFAANGKALALGETDGFVKII 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2731058258 400 ADKTTDEILGVHMIGARAADMIAEAVVAMEYRASAEDVSRMSHAHPTFTEAIKEAALAATeDRALH 465
Cdd:TIGR01350 396 ADKKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEAIKEAALAAL-GKPIH 460
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
2-466 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 562.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 2 NSYDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKySTLGGTCLNVGCIPSKALLDSSHHYEDAvKHFEEHGIEVpGEVKVN 81
Cdd:PRK06416 3 FEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEK-EKLGGTCLNRGCIPSKALLHAAERADEA-RHSEDFGIKA-ENVGID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 82 LEKMIARKQAVVDQTTGGIDFLMKKNNIDVYQGLGSFKDATHITIAGEETTE-IEAKNTIIATGSKPSNLPFIELDKERI 160
Cdd:PRK06416 80 FKKVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDGEQtYTAKNIILATGSRPRELPGIEIDGRVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 161 ITSTEALKLKEIPKHMIVIGGGVIGLELGQVYRRLGAEVTVVEYMDRIIPTMDAGLSKELNKVFKKAKFKMQVSHKVKSV 240
Cdd:PRK06416 160 WTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPGEDKEISKLAERALKKRGIKIKTGAKAKKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 241 ERKGDEVIVkADNKKGEEVEFKGDYCLVSVGRSPYTDGLNAEAAGVKLDdRGRVEVDAHLQTSASNIYAIGDVVKGAMLA 320
Cdd:PRK06416 240 EQTDDGVTV-TLEDGGKEETLEADYVLVAVGRRPNTENLGLEELGVKTD-RGFIEVDEQLRTNVPNIYAIGDIVGGPMLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 321 HKAEEEGVFVAETIAGQKPHIDYNLIPGVVYTWPEVAAVGKTEEELKEAGIEYKTGSFPMRALGRSRASMDLDGFVKILA 400
Cdd:PRK06416 318 HKASAEGIIAAEAIAGNPHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFDVKVVKFPFAGNGKALALGETDGFVKLIF 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2731058258 401 DKTTDEILGVHMIGARAADMIAEAVVAMEYRASAEDVSRMSHAHPTFTEAIKEAALAAtEDRALHI 466
Cdd:PRK06416 398 DKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEALGEAALAA-AGKPLHA 462
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
1-466 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 553.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 1 MNSYDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKySTLGGTCLNVGCIPSKALLDSSHHYEDAvKHFEEHGIEVPGeVKV 80
Cdd:PRK06292 1 MEKYDVIVIGAGPAGYVAARRAAKLGKKVALIEK-GPLGGTCLNVGCIPSKALIAAAEAFHEA-KHAEEFGIHADG-PKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 81 NLEKMIARKQAVVDQTTGGI-DFLMKKNNIDVYQGLGSFKDATHITIAGEEtteIEAKNTIIATGSKPSNLPFIEL-DKE 158
Cdd:PRK06292 78 DFKKVMARVRRERDRFVGGVvEGLEKKPKIDKIKGTARFVDPNTVEVNGER---IEAKNIVIATGSRVPPIPGVWLiLGD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 159 RIITSTEALKLKEIPKHMIVIGGGVIGLELGQVYRRLGAEVTVVEYMDRIIPTMDAGLSKELNKVFKKaKFKMQVSHKVK 238
Cdd:PRK06292 155 RLLTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILSK-EFKIKLGAKVT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 239 SVERKGDEVIVKADnKKGEEVEFKGDYCLVSVGRSPYTDGLNAEAAGVKLDDRGRVEVDAHLQTSASNIYAIGDVVKGAM 318
Cdd:PRK06292 234 SVEKSGDEKVEELE-KGGKTETIEADYVLVATGRRPNTDGLGLENTGIELDERGRPVVDEHTQTSVPGIYAAGDVNGKPP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 319 LAHKAEEEGVFVAETIAG-QKPHIDYNLIPGVVYTWPEVAAVGKTEEELKEAGIEYKTGSFPMRALGRSRASMDLDGFVK 397
Cdd:PRK06292 313 LLHEAADEGRIAAENAAGdVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEVPFEAQGRARVMGKNDGFVK 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2731058258 398 ILADKTTDEILGVHMIGARAADMIAEAVVAMEYRASAEDVSRMSHAHPTFTEAIKEAALAAtEDRALHI 466
Cdd:PRK06292 393 VYADKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRTALRDL-FSKLIHG 460
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
1-455 |
2.21e-129 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 382.63 E-value: 2.21e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 1 MNSYDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKySTLGGTCLNVGCIPSKALLDSSHHYEDAvKHFEEHGIEVPGEVKV 80
Cdd:PRK06370 3 AQRYDAIVIGAGQAGPPLAARAAGLGMKVALIER-GLLGGTCVNTGCVPTKTLIASARAAHLA-RRAAEYGVSVGGPVSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 81 NLEKMIARKQAVVDQT-TGGIDFLMKKNNIDVYQGLGSFKDATHITIAGEEtteIEAKNTIIATGSKPSNLPFIELDKER 159
Cdd:PRK06370 81 DFKAVMARKRRIRARSrHGSEQWLRGLEGVDVFRGHARFESPNTVRVGGET---LRAKRIFINTGARAAIPPIPGLDEVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 160 IITSTEALKLKEIPKHMIVIGGGVIGLELGQVYRRLGAEVTVVEYMDRIIPTMDAGLSKELNKVFKKAKFKMQVSHKVKS 239
Cdd:PRK06370 158 YLTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILEREGIDVRLNAECIR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 240 VERKGDEVIVKADNKKGEEvEFKGDYCLVSVGRSPYTDGLNAEAAGVKLDDRGRVEVDAHLQTSASNIYAIGDVVKGAML 319
Cdd:PRK06370 238 VERDGDGIAVGLDCNGGAP-EITGSHILVAVGRVPNTDDLGLEAAGVETDARGYIKVDDQLRTTNPGIYAAGDCNGRGAF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 320 AHKAEEEGVFVAETIAGQKPH-IDYNLIPGVVYTWPEVAAVGKTEEELKEAGIEYKTGSFPMRALGRSRASMDLDGFVKI 398
Cdd:PRK06370 317 THTAYNDARIVAANLLDGGRRkVSDRIVPYATYTDPPLARVGMTEAEARKSGRRVLVGTRPMTRVGRAVEKGETQGFMKV 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2731058258 399 LADKTTDEILGVHMIGARAADMIAEAVVAMEYRASAEDVSRMSHAHPTFTEAIKEAA 455
Cdd:PRK06370 397 VVDADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIPTLA 453
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
4-461 |
2.50e-113 |
|
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: 341.71 E-value: 2.50e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 4 YDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKySTLGGTCLNVGCIPSKALLDSSHHYEDAVKHFEEhgiEVPGEVKVNLE 83
Cdd:TIGR02053 1 YDLVIIGSGAAAFAAAIKAAELGASVAMVER-GPLGGTCVNVGCVPSKMLLRAAEVAHYARKPPFG---GLAATVAVDFG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 84 KMIARKQAVVDQ-TTGGIDFLMKKNNIDVYQGLGSFKDATHITIAGEETTeIEAKNTIIATGSKPSNLPFIELDKERIIT 162
Cdd:TIGR02053 77 ELLEGKREVVEElRHEKYEDVLSSYGVDYLRGRARFKDPKTVKVDLGREV-RGAKRFLIATGARPAIPPIPGLKEAGYLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 163 STEALKLKEIPKHMIVIGGGVIGLELGQVYRRLGAEVTVVEYMDRIIPTMDAGLSKELNKVFKKAKFKMQVSHKVKSVER 242
Cdd:TIGR02053 156 SEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSDRLLPREEPEISAAVEEALAEEGIEVVTSAQVKAVSV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 243 KGDEVIVKAD-NKKGEEVEfkGDYCLVSVGRSPYTDGLNAEAAGVKLDDRGRVEVDAHLQTSASNIYAIGDVVKGAMLAH 321
Cdd:TIGR02053 236 RGGGKIITVEkPGGQGEVE--ADELLVATGRRPNTDGLGLEKAGVKLDERGGILVDETLRTSNPGIYAAGDVTGGLQLEY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 322 KAEEEGVFVAET-IAGQKPHIDYNLIPGVVYTWPEVAAVGKTEEELKEAGIEYKTGSFPMRALGRSRASMDLDGFVKILA 400
Cdd:TIGR02053 314 VAAKEGVVAAENaLGGANAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNVPRARINRDTRGFIKLVA 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2731058258 401 DKTTDEILGVHMIGARAADMIAEAVVAMEYRASAEDVSRMSHAHPTFTEAIKEAALAATED 461
Cdd:TIGR02053 394 EPGTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGLKLAAQTFYRD 454
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
1-458 |
2.51e-109 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 331.35 E-value: 2.51e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 1 MNSYDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKYSTLGGTCLNVGCIPSKALldsshhyEDAVKHFEE-------HGIE 73
Cdd:PRK05249 3 MYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGGGCTHTGTIPSKAL-------REAVLRLIGfnqnplySSYR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 74 VPGEVKVnlEKMIARKQAVVDQTTGGI-DFLMKkNNIDVYQGLGSFKDATHITIAGE--ETTEIEAKNTIIATGSKPSNL 150
Cdd:PRK05249 76 VKLRITF--ADLLARADHVINKQVEVRrGQYER-NRVDLIQGRARFVDPHTVEVECPdgEVETLTADKIVIATGSRPYRP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 151 PFIELDKERIITSTEALKLKEIPKHMIVIGGGVIGLELGQVYRRLGAEVTVVEYMDRIIPTMDAGLSKELNKVFKKAKFK 230
Cdd:PRK05249 153 PDVDFDHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSFLDDEISDALSYHLRDSGVT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 231 MQVSHKVKSVERKGDEVIVKADNKKgeevEFKGDYCLVSVGRSPYTDGLNAEAAGVKLDDRGRVEVDAHLQTSASNIYAI 310
Cdd:PRK05249 233 IRHNEEVEKVEGGDDGVIVHLKSGK----KIKADCLLYANGRTGNTDGLNLENAGLEADSRGQLKVNENYQTAVPHIYAV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 311 GDVVKGAMLAHKAEEEGVFVAETIAGQKPHIDYNLIPGVVYTWPEVAAVGKTEEELKEAGIEYKTGSFPMRALGRSRASM 390
Cdd:PRK05249 309 GDVIGFPSLASASMDQGRIAAQHAVGEATAHLIEDIPTGIYTIPEISSVGKTEQELTAAKVPYEVGRARFKELARAQIAG 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 391 DLDGFVKILADKTTDEILGVHMIGARAADM--IAEAVvaMEYRASAEDVSRMSHAHPTFTEAIKEAALAA 458
Cdd:PRK05249 389 DNVGMLKILFHRETLEILGVHCFGERATEIihIGQAI--MEQKGTIEYFVNTTFNYPTMAEAYRVAALDG 456
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
4-449 |
1.02e-83 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 264.71 E-value: 1.02e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 4 YDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKYStLGGTCLNVGCIPSKALLDSSHHYEDAVKHFEEHGIEVpGEVKVNLE 83
Cdd:PRK06116 5 YDLIVIGGGSGGIASANRAAMYGAKVALIEAKR-LGGTCVNVGCVPKKLMWYGAQIAEAFHDYAPGYGFDV-TENKFDWA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 84 KMIARKQAVVDQTTGGIDFLMKKNNIDVYQGLGSFKDATHITIAGEETTeieAKNTIIATGSKPS--NLPFIELdkerII 161
Cdd:PRK06116 83 KLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNGERYT---ADHILIATGGRPSipDIPGAEY----GI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 162 TSTEALKLKEIPKHMIVIGGGVIGLELGQVYRRLGAEVTVVEYMDRIIPTMDAGLSKELNKVFKKAKFKMQVSHKVKSVE 241
Cdd:PRK06116 156 TSDGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 242 RKGD-EVIVKADNKKGEEVefkgDYCLVSVGRSPYTDGLNAEAAGVKLDDRGRVEVDAHLQTSASNIYAIGDVVKGAMLA 320
Cdd:PRK06116 236 KNADgSLTLTLEDGETLTV----DCLIWAIGREPNTDGLGLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGDVTGRVELT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 321 HKAEEEGVFVAETIAGQKP--HIDYNLIPGVVYTWPEVAAVGKTEEELKEAGIE-----YKTGSFPMR-ALGRSRASMdl 392
Cdd:PRK06116 312 PVAIAAGRRLSERLFNNKPdeKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEdnvkvYRSSFTPMYtALTGHRQPC-- 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2731058258 393 dgFVKILADKTTDEILGVHMIGARAADMIAEAVVAMEYRASAEDVSRMSHAHPTFTE 449
Cdd:PRK06116 390 --LMKLVVVGKEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAE 444
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
4-457 |
4.07e-82 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 260.66 E-value: 4.07e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 4 YDVAVIGSGPGGYVAAIRCAqlGMKTAIIEKySTLGGTCLNVGCIPSKALLDSSHhYEDAVKHFEEHGI--EVPGevkvn 81
Cdd:PRK07846 2 YDLIIIGTGSGNSILDERFA--DKRIAIVEK-GTFGGTCLNVGCIPTKMFVYAAD-VARTIREAARLGVdaELDG----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 82 lekmiARKQAVVDQTTGGIDFLMKKN---------NIDVYQGLGSFKDatHITIAGEETTEIEAKNTIIATGSKPSNLPF 152
Cdd:PRK07846 73 -----VRWPDIVSRVFGRIDPIAAGGeeyrgrdtpNIDVYRGHARFIG--PKTLRTGDGEEITADQVVIAAGSRPVIPPV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 153 IELDKERIITSTEALKLKEIPKHMIVIGGGVIGLELGQVYRRLGAEVTVVEYMDRIIPTMDAGLSKELNKVFKKaKFKMQ 232
Cdd:PRK07846 146 IADSGVRYHTSDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLDDDISERFTELASK-RWDVR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 233 VSHKVKSVERKGDEVIVKADNkkGEEVEfkGDYCLVSVGRSPYTDGLNAEAAGVKLDDRGRVEVDAHLQTSASNIYAIGD 312
Cdd:PRK07846 225 LGRNVVGVSQDGSGVTLRLDD--GSTVE--ADVLLVATGRVPNGDLLDAAAAGVDVDEDGRVVVDEYQRTSAEGVFALGD 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 313 VVKGAMLAHKAEEEGVFVAETIAGQKPHI--DYNLIPGVVYTWPEVAAVGKTEEELKEAGIEY--KTGSFPMRALGrsRA 388
Cdd:PRK07846 301 VSSPYQLKHVANHEARVVQHNLLHPDDLIasDHRFVPAAVFTHPQIASVGLTENEARAAGLDItvKVQNYGDVAYG--WA 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 389 SMDLDGFVKILADKTTDEILGVHMIGARAADMIAEAVVAMEYRASAEDVSRMSH-AHPTFTEAIKEAALA 457
Cdd:PRK07846 379 MEDTTGFVKLIADRDTGRLLGAHIIGPQASTLIQPLIQAMSFGLDAREMARGQYwIHPALPEVVENALLG 448
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
4-463 |
1.54e-81 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 265.24 E-value: 1.54e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 4 YDVAVIGSGPGGYVAAIRCAQLGMKTAIIE-KYSTLGGTCLNVGCIPSKALLDSS---------HH------YEDAVKHF 67
Cdd:PTZ00153 117 YDVGIIGCGVGGHAAAINAMERGLKVIIFTgDDDSIGGTCVNVGCIPSKALLYATgkyrelknlAKlytygiYTNAFKNG 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 68 EEHGIE----VPGEVKVNLEKMIARKQAVVDQTTGGIDFLMKKNNIDVYQGLGSF-KDATHI----TIAGEET-TEIEAK 137
Cdd:PTZ00153 197 KNDPVErnqlVADTVQIDITKLKEYTQSVIDKLRGGIENGLKSKKFCKNSEHVQViYERGHIvdknTIKSEKSgKEFKVK 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 138 NTIIATGSKPsNLPF-IELDKERIITSTEALKLKEIPKHMIVIGGGVIGLELGQVYRRLGAEVTVVEYMDRIIPTMDAGL 216
Cdd:PTZ00153 277 NIIIATGSTP-NIPDnIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSPQLLPLLDADV 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 217 SKELNKVFKKAK-FKMQVSHKVKSVERKGDE--VIVK-ADNKKGEE----------VEFKGDYCLVSVGRSPYTDGLNAE 282
Cdd:PTZ00153 356 AKYFERVFLKSKpVRVHLNTLIEYVRAGKGNqpVIIGhSERQTGESdgpkknmndiKETYVDSCLVATGRKPNTNNLGLD 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 283 AAGVKLdDRGRVEVDAHLQTSAS------NIYAIGDVVKGAMLAHKAEEEGVFVAETIAGQ--------------KPhID 342
Cdd:PTZ00153 436 KLKIQM-KRGFVSVDEHLRVLREdqevydNIFCIGDANGKQMLAHTASHQALKVVDWIEGKgkenvninvenwasKP-II 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 343 YNLIPGVVYTWPEVAAVGKTEEELKE------AGIE---YKTGS---------FPMRA------LGRSRASMDLDGFVKI 398
Cdd:PTZ00153 514 YKNIPSVCYTTPELAFIGLTEKEAKElyppdnVGVEisfYKANSkvlcennisFPNNSknnsynKGKYNTVDNTEGMVKI 593
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2731058258 399 LADKTTDEILGVHMIGARAADMIAEAVVAMEYRASAEDVSRMSHAHPTFTEAIKEAALAATEDRA 463
Cdd:PTZ00153 594 VYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDAAFKAIAGVRT 658
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
4-327 |
3.57e-80 |
|
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: 250.70 E-value: 3.57e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 4 YDVAVIGSGPGGYVAAIRCAQLGMKTAIIEkystLGGTCLNVGCIPSKALLDSSHHYEDAVkhfeehgievpgevkvNLE 83
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIE----DEGTCPYGGCVLSKALLGAAEAPEIAS----------------LWA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 84 KMIARKQAVVDQTTGGIDFLMKKNNIDVYQGLGSFKDATHItiaGEETTEIEAKNTIIATGSKPsNLPFIELDKE----- 158
Cdd:pfam07992 61 DLYKRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELV---DGDGETITYDRLVIATGARP-RLPPIPGVELnvgfl 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 159 -RIITSTEALKLKEIPKHMIVIGGGVIGLELGQVYRRLGAEVTVVEYMDRIIPTMDAGLSKELNKVFKKAKFKMQVSHKV 237
Cdd:pfam07992 137 vRTLDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 238 KSVERKGDEVIVKADNKKgeevEFKGDYCLVSVGRSPYTDGLnaEAAGVKLDDRGRVEVDAHLQTSASNIYAIGDV-VKG 316
Cdd:pfam07992 217 KEIIGDGDGVEVILKDGT----EIDADLVVVAIGRRPNTELL--EAAGLELDERGGIVVDEYLRTSVPGIYAAGDCrVGG 290
|
330
....*....|.
gi 2731058258 317 AMLAHKAEEEG 327
Cdd:pfam07992 291 PELAQNAVAQG 301
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
1-449 |
3.67e-76 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 245.04 E-value: 3.67e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 1 MNSYDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKYSTL-GGTCLNVGCIPSKALLdsshhyedavkhfeehgieVPGEVK 79
Cdd:PRK07251 1 MLTYDLIVIGFGKAGKTLAAKLASAGKKVALVEESKAMyGGTCINIGCIPTKTLL-------------------VAAEKN 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 80 VNLEKMIARKQAVVDQTTGGIDFLMKKNNIDVYQGLGSFKDATHITI-AGEETTEIEAKNTIIATGSKPSNLPFIEL-DK 157
Cdd:PRK07251 62 LSFEQVMATKNTVTSRLRGKNYAMLAGSGVDLYDAEAHFVSNKVIEVqAGDEKIELTAETIVINTGAVSNVLPIPGLaDS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 158 ERIITSTEALKLKEIPKHMIVIGGGVIGLELGQVYRRLGAEVTVVEYMDRIIPTMDAGLSKELNKVFKKAKFKMQVSHKV 237
Cdd:PRK07251 142 KHVYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYMEEDGITFLLNAHT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 238 KSVERKGDEVIVKADNKKgeeveFKGDYCLVSVGRSPYTDGLNAEAAGVKLDDRGRVEVDAHLQTSASNIYAIGDVVKGA 317
Cdd:PRK07251 222 TEVKNDGDQVLVVTEDET-----YRFDALLYATGRKPNTEPLGLENTDIELTERGAIKVDDYCQTSVPGVFAVGDVNGGP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 318 MLAHKAEEEGVFVAETIAGQKphiDYNL-----IPGVVYTWPEVAAVGKTEEELKEAGIEYKTGSFPMRALGRSRASMDL 392
Cdd:PRK07251 297 QFTYISLDDFRIVFGYLTGDG---SYTLedrgnVPTTMFITPPLSQVGLTEKEAKEAGLPYAVKELLVAAMPRAHVNNDL 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2731058258 393 DGFVKILADKTTDEILGVHMIGARAADMIAEAVVAMEYRASAEDVSRMSHAHPTFTE 449
Cdd:PRK07251 374 RGAFKVVVNTETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAE 430
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
6-461 |
4.24e-76 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 248.14 E-value: 4.24e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 6 VAVIGSGPGGYVAAIRCAQLGMKTAIIEKySTLGGTCLNVGCIPSKALLDSSHHYEDAVKHFEEHGIEvPGEVKVNLEKM 85
Cdd:PRK13748 101 VAVIGSGGAAMAAALKAVEQGARVTLIER-GTIGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDGGIA-ATVPTIDRSRL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 86 IARKQAVVDQTTG----GIdfLMKKNNIDVYQGLGSFKDATHITIAGEETTEIE--AKNTIIATGSKPSNLPFIELDKER 159
Cdd:PRK13748 179 LAQQQARVDELRHakyeGI--LDGNPAITVLHGEARFKDDQTLIVRLNDGGERVvaFDRCLIATGASPAVPPIPGLKETP 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 160 IITSTEALKLKEIPKHMIVIGGGVIGLELGQVYRRLGAEVTVVEyMDRIIPTMDAGLSKELNKVFKKAKFKMQVSHKVKS 239
Cdd:PRK13748 257 YWTSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILA-RSTLFFREDPAIGEAVTAAFRAEGIEVLEHTQASQ 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 240 VERKGDEVIVKADNKkgeevEFKGDYCLVSVGRSPYTDGLNAEAAGVKLDDRGRVEVDAHLQTSASNIYAIGDVVKGAML 319
Cdd:PRK13748 336 VAHVDGEFVLTTGHG-----ELRADKLLVATGRAPNTRSLALDAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQPQF 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 320 AHKAEEEGVFVAETIAGQKPHIDYNLIPGVVYTWPEVAAVGKTEEELKEAGIEYKTGSFPMRALGRSRASMDLDGFVKIL 399
Cdd:PRK13748 411 VYVAAAAGTRAAINMTGGDAALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRTLTLDNVPRALANFDTRGFIKLV 490
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2731058258 400 ADKTTDEILGVHMIGARAADMIAEAVVAMEYRASAEDVSRMSHAHPTFTEAIKEAALAATED 461
Cdd:PRK13748 491 IEEGSGRLIGVQAVAPEAGELIQTAALAIRNRMTVQELADQLFPYLTMVEGLKLAAQTFNKD 552
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
4-457 |
1.69e-73 |
|
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: 238.50 E-value: 1.69e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 4 YDVAVIGSGPGGYVAAIRCAqlGMKTAIIEKySTLGGTCLNVGCIPSKALL---DSSHHYEDAVK---HFEEHGIEVPGE 77
Cdd:TIGR03452 3 YDLIIIGTGSGNSIPDPRFA--DKRIAIVEK-GTFGGTCLNVGCIPTKMFVyaaEVAQSIGESARlgiDAEIDSVRWPDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 78 VKVNLEKMIARKQAvvdqttGGIDFLM--KKNNIDVYQGLGSFKDAThiTIAGEETTEIEAKNTIIATGSKPSNLPFIEL 155
Cdd:TIGR03452 80 VSRVFGDRIDPIAA------GGEDYRRgdETPNIDVYDGHARFVGPR--TLRTGDGEEITGDQIVIAAGSRPYIPPAIAD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 156 DKERIITSTEALKLKEIPKHMIVIGGGVIGLELGQVYRRLGAEVTVVEYMDRIIPTMDAGLSKELNKVFKKaKFKMQVSH 235
Cdd:TIGR03452 152 SGVRYHTNEDIMRLPELPESLVIVGGGYIAAEFAHVFSALGTRVTIVNRSTKLLRHLDEDISDRFTEIAKK-KWDIRLGR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 236 KVKSVERKGDEVIVKADNkkGEEVEfkGDYCLVSVGRSPYTDGLNAEAAGVKLDDRGRVEVDAHLQTSASNIYAIGDVVK 315
Cdd:TIGR03452 231 NVTAVEQDGDGVTLTLDD--GSTVT--ADVLLVATGRVPNGDLLDAEAAGVEVDEDGRIKVDEYGRTSARGVWALGDVSS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 316 GAMLAHKAEEEGVFVAETIAGQKPHI--DYNLIPGVVYTWPEVAAVGKTEEELKEAG--IEYKTGSFPMRALGrsRASMD 391
Cdd:TIGR03452 307 PYQLKHVANAEARVVKHNLLHPNDLRkmPHDFVPSAVFTHPQIATVGLTEQEAREAGhdITVKIQNYGDVAYG--WAMED 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2731058258 392 LDGFVKILADKTTDEILGVHMIGARAADMIAEAVVAMEYRASAEDVSRMSH-AHPTFTEAIKEAALA 457
Cdd:TIGR03452 385 TTGFCKLIADRDTGKLLGAHIIGPQASSLIQPLITAMAFGLDAREMARKQYwIHPALPEVVENALLG 451
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
3-449 |
9.24e-70 |
|
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: 228.57 E-value: 9.24e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 3 SYDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKYStLGGTCLNVGCIPSKALLDSSHHYEdAVKHFEEHGIEVPGEVKVNL 82
Cdd:TIGR01421 2 HYDYLVIGGGSGGIASARRAAEHGAKALLVEAKK-LGGTCVNVGCVPKKVMWYASDLAE-RMHDAADYGFYQNDENTFNW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 83 EKMIARKQAVVDQTTGGIDFLMKKNNIDVYQGLGSFKDATHITIAGEETTeieAKNTIIATG---SKPSNLPFIELDker 159
Cdd:TIGR01421 80 PELKEKRDAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVNGRDYT---APHILIATGgkpSFPENIPGAELG--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 160 iITSTEALKLKEIPKHMIVIGGGVIGLELGQVYRRLGAEVTVVEYMDRIIPTMDAGLSKELNKVFKKAKFKMQVSHKVKS 239
Cdd:TIGR01421 154 -TDSDGFFALEELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRHERVLRSFDSMISETITEEYEKEGINVHKLSKPVK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 240 VER--KGDEVIVKADNKKGEEVefkgDYCLVSVGRSPYTDGLNAEAAGVKLDDRGRVEVDAHLQTSASNIYAIGDVVKGA 317
Cdd:TIGR01421 233 VEKtvEGKLVIHFEDGKSIDDV----DELIWAIGRKPNTKGLGLENVGIKLNEKGQIIVDEYQNTNVPGIYALGDVVGKV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 318 MLAHKAEEEGVFVAETIAGQKP--HIDYNLIPGVVYTWPEVAAVGKTEEE-LKEAGIE----YKTGSFPM-RALGRSRAS 389
Cdd:TIGR01421 309 ELTPVAIAAGRKLSERLFNGKTddKLDYNNVPTVVFSHPPIGTIGLTEKEaIEKYGKEnikvYNSSFTPMyYAMTSEKQK 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 390 MDLdgfvKILADKTTDEILGVHMIGARAADMIAEAVVAMEYRASAEDVSRMSHAHPTFTE 449
Cdd:TIGR01421 389 CRM----KLVCAGKEEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSE 444
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
6-465 |
1.05e-69 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 228.98 E-value: 1.05e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 6 VAVIGSGPGGYVAAIRCAQLGMKTAIIEKySTLGGTCLNVGCIPSKALLDSSHhYEDAVKHFEEHGIEV--PGEVKVNLE 83
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIER-DGLGGAAVLTDCVPSKTLIATAE-VRTELRRAAELGIRFidDGEARVDLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 84 KMIARKQAVVDQTTGGIDFLMKKNNIDVYQGLGSF---KDATH---ITIAGEETTEIEAKNTIIATGSKPSNLPFIELDK 157
Cdd:PRK07845 82 AVNARVKALAAAQSADIRARLEREGVRVIAGRGRLidpGLGPHrvkVTTADGGEETLDADVVLIATGASPRILPTAEPDG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 158 ERIITSTEALKLKEIPKHMIVIGGGVIGLELGQVYRRLGAEVTVVEYMDRIIPTMDAGLSKELNKVFkkAKFKMQV-SH- 235
Cdd:PRK07845 162 ERILTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPGEDADAAEVLEEVF--ARRGMTVlKRs 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 236 KVKSVERKGDEVIVK-ADnkkGEEVEfkGDYCLVSVGRSPYTDGLNAEAAGVKLDDRGRVEVDAHLQTSASNIYAIGDVV 314
Cdd:PRK07845 240 RAESVERTGDGVVVTlTD---GRTVE--GSHALMAVGSVPNTAGLGLEEAGVELTPSGHITVDRVSRTSVPGIYAAGDCT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 315 KGAMLAHKAEEEGvfvaeTIA-------GQKPhIDYNLIPGVVYTWPEVAAVGKTEEELKEAGIEYKTGSFPMRalGRSR 387
Cdd:PRK07845 315 GVLPLASVAAMQG-----RIAmyhalgeAVSP-LRLKTVASNVFTRPEIATVGVSQAAIDSGEVPARTVMLPLA--TNPR 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 388 ASMDL--DGFVKILADKTTDEILGVHMIGARAADMIAEAVVAMEYRASAEDVSRMSHAHPTFTEAIKEAAlaatedRALH 465
Cdd:PRK07845 387 AKMSGlrDGFVKLFCRPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYPSLSGSITEAA------RRLM 460
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
1-453 |
3.80e-64 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 213.87 E-value: 3.80e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 1 MNSYDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKYSTL-GGTCLNVGCIPSKALLdsshhyEDAVKHfeehgievpgevk 79
Cdd:NF040477 1 MNHYQAIIIGFGKAGKTLAATLAKAGWRVAIIEQSAQMyGGTCINIGCIPTKTLV------HDAEQH------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 80 VNLEKMIARKQAVVdqttggiDFLMKKN--------NIDVYQGLGSFKDATHITIAG-EETTEIEAKNTIIATGSKpSNL 150
Cdd:NF040477 62 QDFSTAMQRKSSVV-------GFLRDKNyhnladldNVDVINGRAEFIDNHTLRVFQaDGEQELRGEKIFINTGAQ-SVL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 151 PFIELDKE--RIITSTEALKLKEIPKHMIVIGGGVIGLELGQVYRRLGAEVTVVEYMDRIIPTMDAGLSKELNKVFKKAK 228
Cdd:NF040477 134 PPIPGLTTtpGVYDSTGLLNLTQLPARLGILGGGYIGVEFASMFARFGSKVTIFEAAELFLPREDRDIAQAIATILQDQG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 229 FKMQVSHKVKSVERKGDEVIVKAdnkkgEEVEFKGDYCLVSVGRSPYTDGLNAEAAGVKLDDRGRVEVDAHLQTSASNIY 308
Cdd:NF040477 214 VELILNAQVQRVSSHEGEVQLET-----AEGVLTVDALLVASGRKPATAGLQLQNAGVAVNERGAIVVDKYLRTTADNIW 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 309 AIGDVVKGAMLAHKAEEEGVFVAETI--AGQKPHIDYNLIPGVVYTWPEVAAVGKTEEELKEAGIEYKTGSFPMRALGRS 386
Cdd:NF040477 289 AMGDVTGGLQFTYISLDDFRIVRDSLlgEGKRSTDDRQNVPYSVFMTPPLSRIGMTEEQARASGADIQVVTLPVAAIPRA 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2731058258 387 RASMDLDGFVKILADKTTDEILGVHMIGARAADMIAEAVVAMEYRASAEDVSRMSHAHPTFTEAIKE 453
Cdd:NF040477 369 RVMNDTRGVLKAVVDNKTQRILGVSLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSESLND 435
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
4-449 |
1.10e-58 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 200.81 E-value: 1.10e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 4 YDVAVIGSGPGGYVAAIRCAQLGMKTAIIE---------KYSTLGGTCLNVGCIPSKALLDSSH---HYEDAvkhfEEHG 71
Cdd:PLN02507 26 FDLFVIGAGSGGVRAARFSANFGAKVGICElpfhpisseSIGGVGGTCVIRGCVPKKILVYGATfggEFEDA----KNYG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 72 IEVPGEVKVNLEKMIARKQAVVDQTTGGIDFLMKKNNIDVYQGLGSFKDATHITIAGEETTEIE--AKNTIIATGSK--P 147
Cdd:PLN02507 102 WEINEKVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRytAKHILIATGSRaqR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 148 SNLPfielDKERIITSTEALKLKEIPKHMIVIGGGVIGLELGQVYRRLGAEVTVveYMDRIIPTmdAGLSKELNKVFKK- 226
Cdd:PLN02507 182 PNIP----GKELAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDL--FFRKELPL--RGFDDEMRAVVARn 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 227 ---AKFKMQVSHKVKSVERKGDEVIVKADNkkGEEveFKGDYCLVSVGRSPYTDGLNAEAAGVKLDDRGRVEVDAHLQTS 303
Cdd:PLN02507 254 legRGINLHPRTNLTQLTKTEGGIKVITDH--GEE--FVADVVLFATGRAPNTKRLNLEAVGVELDKAGAVKVDEYSRTN 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 304 ASNIYAIGDVVKGAMLAHKAEEEGVFVAETIAGQKP-HIDYNLIPGVVYTWPEVAAVGKTEEELKEAG---IEYKTGSF- 378
Cdd:PLN02507 330 IPSIWAIGDVTNRINLTPVALMEGTCFAKTVFGGQPtKPDYENVACAVFCIPPLSVVGLSEEEAVEQAkgdILVFTSSFn 409
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2731058258 379 PMRAL--GRSRASmdldgFVKILADKTTDEILGVHMIGARAADMIAEAVVAMEYRASAEDVSRMSHAHPTFTE 449
Cdd:PLN02507 410 PMKNTisGRQEKT-----VMKLIVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAE 477
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
3-451 |
1.51e-57 |
|
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: 197.50 E-value: 1.51e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 3 SYDVAVIGSGPGGYVAAIRCAQL-GMKTAIIE--------KYSTLGGTCLNVGCIPSKaLLDSSHHYEDAVKHFEEHGIE 73
Cdd:TIGR01423 3 AFDLVVIGAGSGGLEAGWNAATLyKKRVAVVDvqthhgppFYAALGGTCVNVGCVPKK-LMVTGAQYMDTLRESAGFGWE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 74 VPGE-VKVNLEKMIARK-QAVVDQTTGGIDFLMKKNNIDVYQGLGSFKDATHITIagEETTE--------IEAKNTIIAT 143
Cdd:TIGR01423 82 FDRSsVKANWKALIAAKnKAVLDINKSYEGMFADTEGLTFFLGWGALEDKNVVLV--RESADpksavkerLQAEHILLAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 144 GSKPsNLPFIELDkERIITSTEALKLKEIPKHMIVIGGGVIGLELGQV---YRRLGAEVTVVEYMDRIIPTMDAGLSKEL 220
Cdd:TIGR01423 160 GSWP-QMLGIPGI-EHCISSNEAFYLDEPPRRVLTVGGGFISVEFAGIfnaYKPRGGKVTLCYRNNMILRGFDSTLRKEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 221 NKVFKKAKFKMQVSHKVKSVERKGD---EVIVKAdnkkGEEVEFkgDYCLVSVGRSPYTDGLNAEAAGVKLDDRGRVEVD 297
Cdd:TIGR01423 238 TKQLRANGINIMTNENPAKVTLNADgskHVTFES----GKTLDV--DVVMMAIGRVPRTQTLQLDKVGVELTKKGAIQVD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 298 AHLQTSASNIYAIGDVVKGAMLAHKAEEEGVFVAETIAGQKPH-IDYNLIPGVVYTWPEVAAVGKTEEelkEAGIEYKTG 376
Cdd:TIGR01423 312 EFSRTNVPNIYAIGDVTDRVMLTPVAINEGAAFVDTVFGNKPRkTDHTRVASAVFSIPPIGTCGLVEE---DAAKKFEKV 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2731058258 377 SFPMRA---LGRSRASMDLDGFV-KILADKTTDEILGVHMIGARAADMIAEAVVAMEYRASAEDVSRMSHAHPTFTEAI 451
Cdd:TIGR01423 389 AVYESSftpLMHNISGSKYKKFVaKIVTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAEEL 467
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
1-453 |
6.08e-57 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 194.85 E-value: 6.08e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 1 MNSYDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKYSTL-GGTCLNVGCIPSKALLdsshhyEDAvkhfEEHGievpgevk 79
Cdd:PRK08010 1 MNKYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNAMyGGTCINIGCIPTKTLV------HDA----QQHT-------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 80 vNLEKMIARKQAVVDqttggidFLMKKN--------NIDVYQGLGSFKDATHITI--AGEETtEIEAKNTIIATGSKpSN 149
Cdd:PRK08010 63 -DFVRAIQRKNEVVN-------FLRNKNfhnladmpNIDVIDGQAEFINNHSLRVhrPEGNL-EIHGEKIFINTGAQ-TV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 150 LPFIE--LDKERIITSTEALKLKEIPKHMIVIGGGVIGLELGQVYRRLGAEVTVVEYMDRIIPTMDAGLSKELNKVFKKA 227
Cdd:PRK08010 133 VPPIPgiTTTPGVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQ 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 228 KFKMQVSHKVKSVERKGDEVIVKAdnkkgEEVEFKGDYCLVSVGRSPYTDGLNAEAAGVKLDDRGRVEVDAHLQTSASNI 307
Cdd:PRK08010 213 GVDIILNAHVERISHHENQVQVHS-----EHAQLAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKYLHTTADNI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 308 YAIGDVVKGAMLAHKAEEEGVFVAETI--AGQKPHIDYNLIPGVVYTWPEVAAVGKTEEELKEAGIEYKTGSFPMRALGR 385
Cdd:PRK08010 288 WAMGDVTGGLQFTYISLDDYRIVRDELlgEGKRSTDDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPR 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2731058258 386 SRASMDLDGFVKILADKTTDEILGVHMIGARAADMIAEAVVAMEYRASAEDVSRMSHAHPTFTEAIKE 453
Cdd:PRK08010 368 ARVMNDTRGVLKAIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLND 435
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
2-449 |
6.60e-53 |
|
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: 185.06 E-value: 6.60e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 2 NSYDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKYST--------LGGTCLNVGCIPSKaLLDSSHHYEDAVKHFEEHGIE 73
Cdd:TIGR01438 1 YDYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPtplgtrwgIGGTCVNVGCIPKK-LMHQAALLGQALKDSRNYGWK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 74 VPGEVKVNLEKMIARKQAVVDQTTGGIDFLMKKNNIDVYQGLGSFKDATHITIAGEETTE--IEAKNTIIATGSKPsNLP 151
Cdd:TIGR01438 80 VEETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEkiYSAERFLIATGERP-RYP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 152 FIELDKERIITSTEALKLKEIPKHMIVIGGGVIGLELGQVYRRLGAEVTVveyMDRIIPTmdAGLSKEL-NKVFKK---- 226
Cdd:TIGR01438 159 GIPGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTV---MVRSILL--RGFDQDCaNKVGEHmeeh 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 227 -AKFKMQVshKVKSVERKGDEVIVKADNKKGEEVEfKGDYCLVSVGRSPYTDGLNAEAAGVKLDDR-GRVEVDAHLQTSA 304
Cdd:TIGR01438 234 gVKFKRQF--VPIKVEQIEAKVLVEFTDSTNGIEE-EYDTVLLAIGRDACTRKLNLENVGVKINKKtGKIPADEEEQTNV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 305 SNIYAIGDVVKGAM-LAHKAEEEGVFVAETI-AGQKPHIDYNLIPGVVYTWPEVAAVGKTEEE----LKEAGIEYKTGSF 378
Cdd:TIGR01438 311 PYIYAVGDILEDKPeLTPVAIQAGRLLAQRLfKGSTVICDYENVPTTVFTPLEYGACGLSEEKavekFGEENVEVFHSYF 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2731058258 379 -PMRALGRSRASMDLdGFVKILADKTTDE-ILGVHMIGARAADMIAEAVVAMEYRASAEDVSRMSHAHPTFTE 449
Cdd:TIGR01438 391 wPLEWTIPSRDNHNK-CYAKLVCNKKENErVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAE 462
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
4-449 |
1.23e-47 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 172.37 E-value: 1.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 4 YDVAVIGSGPGGYVAAIRCAQLGMKTAIIE-KYST--------LGGTCLNVGCIPSKALLDSS---HHYEdavkhfEEHG 71
Cdd:PLN02546 80 FDLFTIGAGSGGVRASRFASNFGASAAVCElPFATissdtlggVGGTCVLRGCVPKKLLVYASkysHEFE------ESRG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 72 I--EVPGEVKVNLEKMIARKQAVVDQTTGGIDFLMKKNNIDVYQGLGSFKDATHITIAGEETTeieAKNTIIATGSKPS- 148
Cdd:PLN02546 154 FgwKYETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDVDGKLYT---ARNILIAVGGRPFi 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 149 -NLPFIEldkeRIITSTEALKLKEIPKHMIVIGGGVIGLELGQVYRRLGAEVTVVEYMDRIIPTMDAGLSKELNKVFKKA 227
Cdd:PLN02546 231 pDIPGIE----HAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKKVLRGFDEEVRDFVAEQMSLR 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 228 KFKMQVSHKVKSVERKGDEVIVKADNKkgEEVE-FKgdYCLVSVGRSPYTDGLNAEAAGVKLDDRGRVEVDAHLQTSASN 306
Cdd:PLN02546 307 GIEFHTEESPQAIIKSADGSLSLKTNK--GTVEgFS--HVMFATGRKPNTKNLGLEEVGVKMDKNGAIEVDEYSRTSVPS 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 307 IYAIGDVVKGAMLAHKAEEEGVFVAETIAGQKP-HIDYNLIPGVVYTWPEVAAVGKTEEE-LKEAG-IEYKTGSFpmRAL 383
Cdd:PLN02546 383 IWAVGDVTDRINLTPVALMEGGALAKTLFGNEPtKPDYRAVPSAVFSQPPIGQVGLTEEQaIEEYGdVDVFTANF--RPL 460
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2731058258 384 GRSRASMDLDGFVKILADKTTDEILGVHMIGARAADMIAEAVVAMEYRASAEDVSRMSHAHPTFTE 449
Cdd:PLN02546 461 KATLSGLPDRVFMKLIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAE 526
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
346-454 |
1.20e-45 |
|
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: 154.25 E-value: 1.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 346 IPGVVYTWPEVAAVGKTEEELKEAGIEYKTGSFPMRALGRSRASMDLDGFVKILADKTTDEILGVHMIGARAADMIAEAV 425
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGEVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQEAA 80
|
90 100
....*....|....*....|....*....
gi 2731058258 426 VAMEYRASAEDVSRMSHAHPTFTEAIKEA 454
Cdd:pfam02852 81 LAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
4-451 |
3.21e-44 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 162.86 E-value: 3.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 4 YDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKySTLGGTCLNVGCIPSKaLLDSSHHYEDAVKHFEEHGIEVpgEVKVNLE 83
Cdd:PTZ00058 49 YDLIVIGGGSGGMAAARRAARNKAKVALVEK-DYLGGTCVNVGCVPKK-IMFNAASIHDILENSRHYGFDT--QFSFNLP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 84 KMIARKQAVVDQTTGGIDFLMKKNNIDVYQGLGSF----------------------KDATHITIAGEETTE----IEAK 137
Cdd:PTZ00058 125 LLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLlsenqvlikkvsqvdgeadesdDDEVTIVSAGVSQLDdgqvIEGK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 138 NTIIATGSKPSnLPFIElDKERIITSTEALKLKEiPKHMIVIGGGVIGLELGQVYRRLGAEVTVVEYMDRIIPTMDAGLS 217
Cdd:PTZ00058 205 NILIAVGNKPI-FPDVK-GKEFTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLRKFDETII 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 218 KELNKVFKKAKFKMQVSHKVKSVERKGDEVIVKADNKKGEEVEFkgDYCLVSVGRSPYTDGLNAEAAGVKlDDRGRVEVD 297
Cdd:PTZ00058 282 NELENDMKKNNINIITHANVEEIEKVKEKNLTIYLSDGRKYEHF--DYVIYCVGRSPNTEDLNLKALNIK-TPKGYIKVD 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 298 AHLQTSASNIYAIGDVV---------KGAMLAHKAEEEGVFVAETIAGQKPH--------------------------ID 342
Cdd:PTZ00058 359 DNQRTSVKHIYAVGDCCmvkknqeieDLNLLKLYNEEPYLKKKENTSGESYYnvqltpvainagrlladrlfgpfsrtTN 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 343 YNLIPGVVYTWPEVAAVGKTEEELKEAGIEYKTGSFPMRALGRSRASMDLD------GFVKILADKTTDEILGVHMIGAR 416
Cdd:PTZ00058 439 YKLIPSVIFSHPPIGTIGLSEQEAIDIYGKENVKIYESRFTNLFFSVYDMDpaqkekTYLKLVCVGKEELIKGLHIVGLN 518
|
490 500 510
....*....|....*....|....*....|....*
gi 2731058258 417 AADMIAEAVVAMEYRASAEDVSRMSHAHPTFTEAI 451
Cdd:PTZ00058 519 ADEILQGFAVALKMNATKADFDETIPIHPTAAEEF 553
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
4-450 |
1.61e-39 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 148.82 E-value: 1.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 4 YDVAVIGSGPGGYVAAIRCAQLGMKTAIIE--KYST------LGGTCLNVGCIPSKaLLDSSHHYEDAVKH-FEEHGIEV 74
Cdd:PTZ00052 6 YDLVVIGGGSGGMAAAKEAAAHGKKVALFDyvKPSTqgtkwgLGGTCVNVGCVPKK-LMHYAANIGSIFHHdSQMYGWKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 75 PGevKVNLEKMIARKQAVVDQTTGGIDFLMKKNNIDVYQGLGSFKDAThiTIAGEETTEIE---AKNTIIATGSKPSNLP 151
Cdd:PTZ00052 85 SS--SFNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEH--TVSYGDNSQEEtitAKYILIATGGRPSIPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 152 FIELDKERIITSTEALKLKEIPKHMIVIGGGVIGLELGQVYRRLGAEVTVVEymdRIIPT--MDAGLSKELNKVFKKAKF 229
Cdd:PTZ00052 161 DVPGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAV---RSIPLrgFDRQCSEKVVEYMKEQGT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 230 KMQVSHKVKSVERKGDEVIVKADNKKGEEVefkgDYCLVSVGRSPYTDGLNAEAAGVKLDDRGRVEVDAHLqTSASNIYA 309
Cdd:PTZ00052 238 LFLEGVVPINIEKMDDKIKVLFSDGTTELF----DTVLYATGRKPDIKGLNLNAIGVHVNKSNKIIAPNDC-TNIPNIFA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 310 IGDVVKGA-MLAHKAEEEGVFVAETIAGQ-KPHIDYNLIPGVVYTWPEVAAVGKTEE----ELKEAGIEYKTGSF---PM 380
Cdd:PTZ00052 313 VGDVVEGRpELTPVAIKAGILLARRLFKQsNEFIDYTFIPTTIFTPIEYGACGYSSEaaiaKYGEDDIEEYLQEFntlEI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 381 RALGRSRA------SMDLD----GFVKILADKTTDE-ILGVHMIGARAADMIAEAVVAMEYRASAEDVSRMSHAHPTFTE 449
Cdd:PTZ00052 393 AAVHREKHerarkdEYDFDvssnCLAKLVCVKSEDNkVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHPTDAE 472
|
.
gi 2731058258 450 A 450
Cdd:PTZ00052 473 V 473
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
140-339 |
1.55e-32 |
|
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: 126.08 E-value: 1.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 140 IIATGSKPSNLPFIELDKERIITST---EALKLKE-----IPKHMIVIGGGVIGLELGQVYRRLGAEVTVVEYMDRIIPT 211
Cdd:COG0446 83 VLATGARPRPPPIPGLDLPGVFTLRtldDADALREalkefKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 212 MDAGLSKELNKVFKKAKFKMQVSHKVKSVERKGDEVIVKADnkkGEEVEFkgDYCLVSVGRSPYTDgLnAEAAGVKLDDR 291
Cdd:COG0446 163 LDPEMAALLEEELREHGVELRLGETVVAIDGDDKVAVTLTD---GEEIPA--DLVVVAPGVRPNTE-L-AKDAGLALGER 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2731058258 292 GRVEVDAHLQTSASNIYAIGDVV----------KGAMLAHKAEEEGVFVAETIAGQKP 339
Cdd:COG0446 236 GWIKVDETLQTSDPDVYAAGDCAevphpvtgktVYIPLASAANKQGRVAAENILGGPA 293
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
4-316 |
1.05e-26 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 109.44 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 4 YDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKySTLGGTCLNVGCIpskalldssHHY-------------EDAVKHFEEH 70
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEG-GEPGGQLATTKEI---------ENYpgfpegisgpelaERLREQAERF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 71 GIEVpgevkvnlekmiaRKQAVVdqttgGIDflmkknnidvyqglgsfKDATHITIAGEETTEIEAKNTIIATGSKPSNL 150
Cdd:COG0492 71 GAEI-------------LLEEVT-----SVD-----------------KDDGPFRVTTDDGTEYEAKAVIIATGAGPRKL 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 151 PfieLDKERIIT--------STEALKLKEipKHMIVIGGGVIGLELGQVYRRLGAEVTVveymdrIIPTMDAGLSKEL-N 221
Cdd:COG0492 116 G---LPGEEEFEgrgvsycaTCDGFFFRG--KDVVVVGGGDSALEEALYLTKFASKVTL------IHRRDELRASKILvE 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 222 KVFKKAKFKMQVSHKVKSVERKG--DEVIVKaDNKKGEEVEFKGDYCLVSVGRSPYTDGLnaEAAGVKLDDRGRVEVDAH 299
Cdd:COG0492 185 RLRANPKIEVLWNTEVTEIEGDGrvEGVTLK-NVKTGEEKELEVDGVFVAIGLKPNTELL--KGLGLELDEDGYIVVDED 261
|
330
....*....|....*..
gi 2731058258 300 LQTSASNIYAIGDVVKG 316
Cdd:COG0492 262 METSVPGVFAAGDVRDY 278
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
105-337 |
3.14e-26 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 109.85 E-value: 3.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 105 KKNNIDVYQGlgsfKDATHI-----TIAGEETTEIEAKNTIIATGSKPSNLPFIELDKERII---TSTEALKLKEI---P 173
Cdd:COG1251 67 EENGIDLRLG----TRVTAIdraarTVTLADGETLPYDKLVLATGSRPRVPPIPGADLPGVFtlrTLDDADALRAAlapG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 174 KHMIVIGGGVIGLELGQVYRRLGAEVTVVEYMDRIIPT-MDAGLSKELNKVFKKAKFKMQVSHKVKSVErkGDEVIVKAD 252
Cdd:COG1251 143 KRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPRqLDEEAGALLQRLLEALGVEVRLGTGVTEIE--GDDRVTGVR 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 253 NKKGEEVEfkGDYCLVSVGRSPYTDgLnAEAAGVKLdDRGrVEVDAHLQTSASNIYAIGDV--VKGAMLAHK-------A 323
Cdd:COG1251 221 LADGEELP--ADLVVVAIGVRPNTE-L-ARAAGLAV-DRG-IVVDDYLRTSDPDIYAAGDCaeHPGPVYGRRvlelvapA 294
|
250
....*....|....
gi 2731058258 324 EEEGVFVAETIAGQ 337
Cdd:COG1251 295 YEQARVAAANLAGG 308
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
140-427 |
1.73e-21 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 96.65 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 140 IIATGSKPSNLPFIELDKERIITST---------EALKLKEIpKHMIVIGGGVIGLELGQVYRRLGAEVTVVEYMDRIIP 210
Cdd:PRK09564 108 MIATGARPIIPPIKNINLENVYTLKsmedglalkELLKDEEI-KNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRILP 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 211 -TMDAGLSKELNKVFKKAKFKMQVSHKVKSVERKGDEVIVKADNKkgeevEFKGDYCLVSVGRSPYTDGLnaEAAGVKLD 289
Cdd:PRK09564 187 dSFDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEGVVTDKG-----EYEADVVIVATGVKPNTEFL--EDTGLKTL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 290 DRGRVEVDAHLQTSASNIYAIGD------VVKG----AMLAHKAEEEGVFVAETIAGQKPHIDYNLIPGVVYTWP-EVAA 358
Cdd:PRK09564 260 KNGAIIVDEYGETSIENIYAAGDcatiynIVSNknvyVPLATTANKLGRMVGENLAGRHVSFKGTLGSACIKVLDlEAAR 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 359 VGKTEEELKEAGIEYK---------TGSFPmralGRSrasmdlDGFVKILADKTTDEILGVHMIGARAA----DMIAEAV 425
Cdd:PRK09564 340 TGLTEEEAKKLGIDYKtvfikdknhTNYYP----GQE------DLYVKLIYEADTKVILGGQIIGKKGAvlriDALAVAI 409
|
..
gi 2731058258 426 VA 427
Cdd:PRK09564 410 YA 411
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
175-254 |
5.27e-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: 72.62 E-value: 5.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 175 HMIVIGGGVIGLELGQVYRRLGAEVTVVEYMDRIIPTMDAGLSKELNKVFKKAKFKMQVSHKVKSVERKGDEVIVKADNK 254
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLTDG 80
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
6-334 |
7.87e-16 |
|
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: 79.41 E-value: 7.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 6 VAVIGSGPGGYVAAIRCAQLGMKTAIIEKYSTLGGTcLNVGcIPS----KALLDsshhYEdaVKHFEEHGIEVPGEVKV- 80
Cdd:COG0493 124 VAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGGL-LRYG-IPEfrlpKDVLD----RE--IELIEALGVEFRTNVEVg 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 81 ---NLEKMIARKQAVvdqttggidFLmkknnidvyqGLGSFKDaTHITIAGEEtteieAKNTIIAtgskpsnLPFIEldk 157
Cdd:COG0493 196 kdiTLDELLEEFDAV---------FL----------ATGAGKP-RDLGIPGED-----LKGVHSA-------MDFLT--- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 158 eRIITSTEALKLKEIPKHMIVIGGG-----VIGlelgqVYRRLGAE-VTVVEYMDR---------IIPTMDAG------- 215
Cdd:COG0493 241 -AVNLGEAPDTILAVGKRVVVIGGGntamdCAR-----TALRLGAEsVTIVYRRTReempaskeeVEEALEEGveflflv 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 216 -----LSKELNKVfKKAKF-KMQVSHKVKSVERKGDEVivkadnkKGEEVEFKGDYCLVSVGRSPYTDGLnAEAAGVKLD 289
Cdd:COG0493 315 apveiIGDENGRV-TGLECvRMELGEPDESGRRRPVPI-------EGSEFTLPADLVILAIGQTPDPSGL-EEELGLELD 385
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2731058258 290 DRGRVEVDA-HLQTSASNIYAIGDVVKGAMLAHKAEEEGVFVAETI 334
Cdd:COG0493 386 KRGTIVVDEeTYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAI 431
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
140-312 |
9.03e-16 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 78.81 E-value: 9.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 140 IIATGSKPSnLPFIELDkERIIT--STEALKLKEIP----KHMIVIGGGVIGLELGQVYRRLGAEVTVVEYMDRIIPT-M 212
Cdd:PRK04965 104 VLATGASAF-VPPIPGR-ELMLTlnSQQEYRAAETQlrdaQRVLVVGGGLIGTELAMDLCRAGKAVTLVDNAASLLASlM 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 213 DAGLSKELNKVFKKAKFKMQVSHKVKSVERKGDEVIVKADNKKGEEVefkgDYCLVSVGRSPYTdGLnAEAAGVKLDdRG 292
Cdd:PRK04965 182 PPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRATLDSGRSIEV----DAVIAAAGLRPNT-AL-ARRAGLAVN-RG 254
|
170 180
....*....|....*....|
gi 2731058258 293 rVEVDAHLQTSASNIYAIGD 312
Cdd:PRK04965 255 -IVVDSYLQTSAPDIYALGD 273
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
140-335 |
5.73e-14 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 73.24 E-value: 5.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 140 IIATGSKPS--NLP--------------FIELdKERIITSTEALKLKEiPKHMIVIGGGVIGLEL-GQVYRRLG------ 196
Cdd:COG1252 102 VIATGSVTNffGIPglaehalplktledALAL-RERLLAAFERAERRR-LLTIVVVGGGPTGVELaGELAELLRkllryp 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 197 ------AEVTVVEYMDRIIPTMDAGLSKELNKVFKKAKFKMQVSHKVKSVErkGDEVIVKadnkKGEEVEFkgDYCLVSV 270
Cdd:COG1252 180 gidpdkVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVD--ADGVTLE----DGEEIPA--DTVIWAA 251
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2731058258 271 GRSPYTDglnAEAAGVKLDDRGRVEVDAHLQT-SASNIYAIGDVV-------KG-AMLAHKAEEEGVFVAETIA 335
Cdd:COG1252 252 GVKAPPL---LADLGLPTDRRGRVLVDPTLQVpGHPNVFAIGDCAavpdpdgKPvPKTAQAAVQQAKVLAKNIA 322
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
140-313 |
2.77e-13 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 71.11 E-value: 2.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 140 IIATGSKPSNLPFIELDKERIIT---STEALKLKEI---PKHMIVIGGGVIGLELGQVYRRLGAEVTVVE----YMDRII 209
Cdd:PRK09754 105 FIATGAAARPLPLLDALGERCFTlrhAGDAARLREVlqpERSVVIVGAGTIGLELAASATQRRCKVTVIElaatVMGRNA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 210 PTMdagLSKELNKVFKKAKFKMQVSHKVKSVErKGDEVIVKADNkkGEEVEfkGDYCLVSVGRSpYTDGLNAEAAgvkLD 289
Cdd:PRK09754 185 PPP---VQRYLLQRHQQAGVRILLNNAIEHVV-DGEKVELTLQS--GETLQ--ADVVIYGIGIS-ANDQLAREAN---LD 252
|
170 180
....*....|....*....|....
gi 2731058258 290 DRGRVEVDAHLQTSASNIYAIGDV 313
Cdd:PRK09754 253 TANGIVIDEACRTCDPAIFAGGDV 276
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
174-368 |
1.40e-12 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 69.43 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 174 KHMIVIGGGVIGLE-LGQVYRRlGAEVTVVEYMDRIIPTMDAGLSKELNKVFKKAKFKMQVSHKVKSVerkgdevivkad 252
Cdd:PRK13512 149 DKALVVGAGYISLEvLENLYER-GLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDAI------------ 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 253 nkKGEEVEFKG------DYCLVSVGRSPYTDGLnaEAAGVKLDDRGRVEVDAHLQTSASNIYAIGDVVKG---------- 316
Cdd:PRK13512 216 --NGNEVTFKSgkvehyDMIIEGVGTHPNSKFI--ESSNIKLDDKGFIPVNDKFETNVPNIYAIGDIITShyrhvdlpas 291
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2731058258 317 AMLAHKAEEEGVFVAETIAGQ-----KPHIDYNLIPGVVYTWpevAAVGKTEEELKE 368
Cdd:PRK13512 292 VPLAWGAHRAASIVAEQIAGNdtiefKGFLGNNIVKFFDYTF---ASVGVKPNELKQ 345
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
106-313 |
1.68e-11 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 66.39 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 106 KNNIDVYQGlgsfkdATHITIAGEETTEI-EAKNT------IIATGSKPSNLPFIELDKE-----RIITSTEALK-LKEI 172
Cdd:TIGR02374 66 KHGITLYTG------ETVIQIDTDQKQVItDAGRTlsydklILATGSYPFILPIPGADKKgvyvfRTIEDLDAIMaMAQR 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 173 PKHMIVIGGGVIGLELGQVYRRLGAEVTVVEYMDRIIP-TMDAGLSKELNKvfKKAKFKMQVSHKVKSVERKGDEVIVKA 251
Cdd:TIGR02374 140 FKKAAVIGGGLLGLEAAVGLQNLGMDVSVIHHAPGLMAkQLDQTAGRLLQR--ELEQKGLTFLLEKDTVEIVGATKADRI 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2731058258 252 DNKKGEEVEfkGDYCLVSVGRSPYTDglNAEAAGVKLDdrGRVEVDAHLQTSASNIYAIGDV 313
Cdd:TIGR02374 218 RFKDGSSLE--ADLIVMAAGIRPNDE--LAVSAGIKVN--RGIIVNDSMQTSDPDIYAVGEC 273
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
1-40 |
1.37e-09 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 59.86 E-value: 1.37e-09
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2731058258 1 MNSYDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKYSTLGG 40
Cdd:COG1233 1 MMMYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
129-336 |
1.54e-09 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 59.78 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 129 EETTEIEAKNTIIATGSKPS--NLPFI--------ELDKERIITS------------TEALKLKEIPKHMIVIGGGVIGL 186
Cdd:PTZ00318 107 VNTFSVPYDKLVVAHGARPNtfNIPGVeerafflkEVNHARGIRKrivqcieraslpTTSVEERKRLLHFVVVGGGPTGV 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 187 E--------LGQVYRRLGAE------VTVVEYMDRIIPTMDAGLSKELNKVFKKAKFKMQVSHKVKSVerKGDEVIVKAd 252
Cdd:PTZ00318 187 EfaaeladfFRDDVRNLNPElveeckVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEV--LDKEVVLKD- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 253 nkkGEEVEfkgdYCLV----SVGRSPYTDGLNAEAagvklDDRGRVEVDAHLQTS-ASNIYAIGDV-----VKGAMLAHK 322
Cdd:PTZ00318 264 ---GEVIP----TGLVvwstGVGPGPLTKQLKVDK-----TSRGRISVDDHLRVKpIPNVFALGDCaaneeRPLPTLAQV 331
|
250
....*....|....
gi 2731058258 323 AEEEGVFVAETIAG 336
Cdd:PTZ00318 332 ASQQGVYLAKEFNN 345
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
6-334 |
1.06e-08 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 57.10 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 6 VAVIGSGPGGYVAAIRCAQLGMKTAIIEKYSTLGGtclnvgcipskaLLdsshhyedavkhfeEHGIevPgEVKvnLEKM 85
Cdd:PRK12810 146 VAVVGSGPAGLAAADQLARAGHKVTVFERADRIGG------------LL--------------RYGI--P-DFK--LEKE 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 86 IARKQavVDQTTG-GIDFLMKKN---NIDVYQGLGSFkDAThitiageetteieakntIIATGS-KPSNLPFIELDKERI 160
Cdd:PRK12810 195 VIDRR--IELMEAeGIEFRTNVEvgkDITAEELLAEY-DAV-----------------FLGTGAyKPRDLGIPGRDLDGV 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 161 -------ITSTEALkLKEIP--------KHMIVIGGGVIGLELGQVYRRLGAE-VTVVEYMDRiiptmdAGLSKELNKVF 224
Cdd:PRK12810 255 hfamdflIQNTRRV-LGDETepfisakgKHVVVIGGGDTGMDCVGTAIRQGAKsVTQRDIMPM------PPSRRNKNNPW 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 225 KKAKFKMQVSH----------------------KVKSVE------RKGDEVIVKadnkkGEEVEFKGDYCLVSVGRSPYT 276
Cdd:PRK12810 328 PYWPMKLEVSNaheegverefnvqtkefegengKVTGVKvvrtelGEGDFEPVE-----GSEFVLPADLVLLAMGFTGPE 402
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2731058258 277 DGLnAEAAGVKLDDRGRVEV-DAHLQTSASNIYAIGDVVKGAMLAHKAEEEGVFVAETI 334
Cdd:PRK12810 403 AGL-LAQFGVELDERGRVAApDNAYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAI 460
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
5-41 |
1.69e-08 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 56.46 E-value: 1.69e-08
10 20 30
....*....|....*....|....*....|....*..
gi 2731058258 5 DVAVIGSGPGGYVAAIRCAQLGMKTAIIEKYSTLGGT 41
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGM 37
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
174-335 |
2.15e-08 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 55.77 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 174 KHMIVIGGGVIGLELGQVYRRLGAEVTVVEYMdRIIPTMDAGlSKELNKVFKK-AKFKMQVS-------HKVKSVE---- 241
Cdd:PRK12770 173 KKVVVVGAGLTAVDAALEAVLLGAEKVYLAYR-RTINEAPAG-KYEIERLIARgVEFLELVTpvriigeGRVEGVElakm 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 242 --RKGDEVIVKADNK-KGEEVEFKGDYCLVSVGRSPyTDGLNAEAAGVKLDDRGRVEVDAHLQTSASNIYAIGDVVKGAM 318
Cdd:PRK12770 251 rlGEPDESGRPRPVPiPGSEFVLEADTVVFAIGEIP-TPPFAKECLGIELNRKGEIVVDEKHMTSREGVFAAGDVVTGPS 329
|
170
....*....|....*..
gi 2731058258 319 LAHKAEEEGVFVAETIA 335
Cdd:PRK12770 330 KIGKAIKSGLRAAQSIH 346
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
5-196 |
4.47e-08 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 54.86 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 5 DVAVIGSGPGGYVAAIRCAQLGMKTAIIekySTLGGTCLNVGCIPSKALLDSSH-HYE-DAV-----KHFEEHGIEVPGe 77
Cdd:pfam01134 1 DVIVIGGGHAGCEAALAAARMGAKVLLI---THNTDTIAELSCNPSIGGIAKGHlVREiDALgglmgKAADKTGIQFRM- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 78 vkVNLEKMIA----RKQAVVDQTTGGI-DFLMKKNNIDVYQGLGS---FKDATHITIAGEETTEIEAKNTIIATGSKPSN 149
Cdd:pfam01134 77 --LNTSKGPAvralRAQVDRDLYSKEMtETLENHPNLTLIQGEVTdliPENGKVKGVVTEDGEEYKAKAVVLATGTFLNG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2731058258 150 LPFIELDKE---RI--ITSTE-ALKLKEIPKHMIVIGGGV------IGLELGQVYRRLG 196
Cdd:pfam01134 155 KIHIGLKCYpagRLgeLTSEGlSESLKELGFELGRFKTGTppridkDSIDFSKLEEQPG 213
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
2-317 |
2.69e-07 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 53.21 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 2 NSYDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKYSTLGGTcLNVGcIPSKALLDsshhyeDAVKHfeehgiEVPGEVKVN 81
Cdd:PRK12778 430 NGKKVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGGV-LKYG-IPEFRLPK------KIVDV------EIENLKKLG 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 82 LEKMiarKQAVVDQTTGgIDFLMKKNNIDVY----QGLGSFkdathITIAGEETTEIEAKNTIIATgskpSNL--PFIEL 155
Cdd:PRK12778 496 VKFE---TDVIVGKTIT-IEELEEEGFKGIFiasgAGLPNF-----MNIPGENSNGVMSSNEYLTR----VNLmdAASPD 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 156 DKERIITStealklkeipKHMIVIGGGVIGLELGQVYRRLGAEVTVVEYMdRIIPTMDAGLSKELNKVFKKAKF------ 229
Cdd:PRK12778 563 SDTPIKFG----------KKVAVVGGGNTAMDSARTAKRLGAERVTIVYR-RSEEEMPARLEEVKHAKEEGIEFltlhnp 631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 230 -----------------KMQVSHKVKSVERKGDEVivkadnkKGEEVEFKGDYCLVSVGRSPyTDGLNAEAAGVKLDDRG 292
Cdd:PRK12778 632 ieyladekgwvkqvvlqKMELGEPDASGRRRPVAI-------PGSTFTVDVDLVIVSVGVSP-NPLVPSSIPGLELNRKG 703
|
330 340
....*....|....*....|....*
gi 2731058258 293 RVEVDAHLQTSASNIYAIGDVVKGA 317
Cdd:PRK12778 704 TIVVDEEMQSSIPGIYAGGDIVRGG 728
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
6-334 |
3.37e-07 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 52.81 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 6 VAVIGSGPGGYVAAIRCAQLGMKTAIIEKYSTLGGTcLNVGcIPS----KALLDSShhyedaVKHFEEHGIEVpgevkvN 81
Cdd:PRK12814 196 VAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGM-MRYG-IPRfrlpESVIDAD------IAPLRAMGAEF------R 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 82 LEKMIARkqavvDQTTGGIdflmkKNNID-VYQGLGSFKdATHITIAGEETTEIEakntiiatgskpSNLPFIeldkeRI 160
Cdd:PRK12814 262 FNTVFGR-----DITLEEL-----QKEFDaVLLAVGAQK-ASKMGIPGEELPGVI------------SGIDFL-----RN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 161 ITSTEALklkEIPKHMIVIGGGVIGLELGQVYRRLGAEVTVVEYMdRIIPTMDAGLSkELNKVFKKAkFKMQVSHKVKSV 240
Cdd:PRK12814 314 VALGTAL---HPGKKVVVIGGGNTAIDAARTALRLGAESVTILYR-RTREEMPANRA-EIEEALAEG-VSLRELAAPVSI 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 241 ERKGDEVIVKADNKKGEEVEFKGDYCLVSVGRSPYT--------------DGLNAEAAGVKLDDRGRVEVD-AHLQTSAS 305
Cdd:PRK12814 388 ERSEGGLELTAIKMQQGEPDESGRRRPVPVEGSEFTlqadtvisaigqqvDPPIAEAAGIGTSRNGTVKVDpETLQTSVA 467
|
330 340
....*....|....*....|....*....
gi 2731058258 306 NIYAIGDVVKGAMLAHKAEEEGVFVAETI 334
Cdd:PRK12814 468 GVFAGGDCVTGADIAINAVEQGKRAAHAI 496
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
6-334 |
5.46e-07 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 51.72 E-value: 5.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 6 VAVIGSGPGGYVAAIRCAQLGMKTAIIEKYSTLGGtcLNVGCIPS----KALLDsshhYEdaVKHFEEHGIEV-PGEV-- 78
Cdd:PRK11749 143 VAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG--LLRYGIPEfrlpKDIVD----RE--VERLLKLGVEIrTNTEvg 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 79 -KVNLEKMIARKQAVVdqttggidflmkknnIDVyqGLGSFKDathITIAGEEtteieAKNTIIATgskpsnlpfieldk 157
Cdd:PRK11749 215 rDITLDELRAGYDAVF---------------IGT--GAGLPRF---LGIPGEN-----LGGVYSAV-------------- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 158 ERIITSTEALKLKEIP--KHMIVIGGGVIGLELGQVYRRLGAE-VTVVEYMDRiiPTMDAglSKE------LNKVfkkaK 228
Cdd:PRK11749 256 DFLTRVNQAVADYDLPvgKRVVVIGGGNTAMDAARTAKRLGAEsVTIVYRRGR--EEMPA--SEEevehakEEGV----E 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 229 FKMQVS--------HKVKSVE------RKGDEVIVKADNKKGEEVEFKGDYCLVSVGRSPYTDGLNAeAAGVKLDDRG-R 293
Cdd:PRK11749 328 FEWLAApveilgdeGRVTGVEfvrmelGEPDASGRRRVPIEGSEFTLPADLVIKAIGQTPNPLILST-TPGLELNRWGtI 406
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2731058258 294 VEVDAHLQTSASNIYAIGDVVKGAMLAHKAEEEGVFVAETI 334
Cdd:PRK11749 407 IADDETGRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAEAI 447
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
6-334 |
5.48e-07 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 52.08 E-value: 5.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 6 VAVIGSGPGGYVAAIRCAQLGMKTAIIEKYSTLGGTcLNVGcIPSKALLDSShhYEDAVKHFEEHGIEVPGEVKVN---- 81
Cdd:PRK13984 286 VAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGV-MRYG-IPSYRLPDEA--LDKDIAFIEALGVKIHLNTRVGkdip 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 82 LEKMIARKQAVVDQTTGGidfLMKKNNI------DVYQGLGSFKdathitiageetteiEAKNTIIATGSKPsnlpfiel 155
Cdd:PRK13984 362 LEELREKHDAVFLSTGFT---LGRSTRIpgtdhpDVIQALPLLR---------------EIRDYLRGEGPKP-------- 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 156 dkeriitstealklkEIPKHMIVIGGGVIGLELGQVYRRL----GAEVTV-VEYMDRIIPTMDAGL-----SKELNKVFK 225
Cdd:PRK13984 416 ---------------KIPRSLVVIGGGNVAMDIARSMARLqkmeYGEVNVkVTSLERTFEEMPADMeeieeGLEEGVVIY 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 226 KAKFKMQV---SHKVKSVERKGDEVIVKADNK------KGEEVEFKGDYCLVSVGRSPYTDGLNAEAAGvKLD-DRGRVE 295
Cdd:PRK13984 481 PGWGPMEVvieNDKVKGVKFKKCVEVFDEEGRfnpkfdESDQIIVEADMVVEAIGQAPDYSYLPEELKS-KLEfVRGRIL 559
|
330 340 350
....*....|....*....|....*....|....*....
gi 2731058258 296 VDAHLQTSASNIYAIGDVVKGAMLAHkAEEEGVFVAETI 334
Cdd:PRK13984 560 TNEYGQTSIPWLFAGGDIVHGPDIIH-GVADGYWAAEGI 597
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
4-313 |
6.01e-07 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 51.70 E-value: 6.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 4 YDVAVIGSGPGGYVAAIRCAQLGMKTAII-EKYstlGGTCLnvgcipskalldsshhyeDAVkhfeehGIEvpgevkvNL 82
Cdd:PRK15317 212 YDVLVVGGGPAGAAAAIYAARKGIRTGIVaERF---GGQVL------------------DTM------GIE-------NF 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 83 ekmIArkqavVDQTTG-----GIDFLMKKNNIDVYQG-----LGSFKDATHITIAGEETteIEAKNTIIATGSKPSNL-- 150
Cdd:PRK15317 258 ---IS-----VPETEGpklaaALEEHVKEYDVDIMNLqraskLEPAAGLIEVELANGAV--LKAKTVILATGARWRNMnv 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 151 -------------------PFIEldkeriitstealklkeiPKHMIVIGGGVIGLEL-----GQVyrrlgAEVTVVEYMd 206
Cdd:PRK15317 328 pgedeyrnkgvaycphcdgPLFK------------------GKRVAVIGGGNSGVEAaidlaGIV-----KHVTVLEFA- 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 207 riiPTM--DAGLSKELN-----KVFKKAKfkmqvshkVKSVERKGDEV--IVKADNKKGEEVEFKGDYCLVSVGRSPYTD 277
Cdd:PRK15317 384 ---PELkaDQVLQDKLRslpnvTIITNAQ--------TTEVTGDGDKVtgLTYKDRTTGEEHHLELEGVFVQIGLVPNTE 452
|
330 340 350
....*....|....*....|....*....|....*.
gi 2731058258 278 GLNAEaagVKLDDRGRVEVDAHLQTSASNIYAIGDV 313
Cdd:PRK15317 453 WLKGT---VELNRRGEIIVDARGATSVPGVFAAGDC 485
|
|
| PRK12844 |
PRK12844 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
3-68 |
6.10e-07 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 183787 [Multi-domain] Cd Length: 557 Bit Score: 51.68 E-value: 6.10e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2731058258 3 SYDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKYSTLGG-TCLNVGC--IPSKALL------DSshhYEDAVKHFE 68
Cdd:PRK12844 6 TYDVVVVGSGGGGMCAALAAADSGLEPLIVEKQDKVGGsTAMSGGVlwLPNNPLMkaagvpDS---HEDALAYLD 77
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
57-312 |
6.25e-07 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 52.04 E-value: 6.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 57 SHHYEDA---VKH--FEEHGIEV-PGEVKVNlekmIARKQAVVDQTTGgidflmkknnidvyqglgsfkdathitiagee 130
Cdd:PRK14989 54 SHHTAEElslVREgfYEKHGIKVlVGERAIT----INRQEKVIHSSAG-------------------------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 131 tTEIEAKNTIIATGSKPSnLPFIELDKER---IITSTEALKLKEI----PKHMIVIGGGVIGLELGQVYRRLGAEVTVVE 203
Cdd:PRK14989 98 -RTVFYDKLIMATGSYPW-IPPIKGSETQdcfVYRTIEDLNAIEAcarrSKRGAVVGGGLLGLEAAGALKNLGVETHVIE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 204 YMDRIIP-TMDAGLSKELNKVFKKAKFKMQVSHKVKSVERKGDE---VIVKADnkkGEEVEFkgDYCLVSVGRSPyTDGL 279
Cdd:PRK14989 176 FAPMLMAeQLDQMGGEQLRRKIESMGVRVHTSKNTLEIVQEGVEarkTMRFAD---GSELEV--DFIVFSTGIRP-QDKL 249
|
250 260 270
....*....|....*....|....*....|...
gi 2731058258 280 nAEAAGVKLDDRGRVEVDAHLQTSASNIYAIGD 312
Cdd:PRK14989 250 -ATQCGLAVAPRGGIVINDSCQTSDPDIYAIGE 281
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
5-41 |
8.43e-07 |
|
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: 51.13 E-value: 8.43e-07
10 20 30
....*....|....*....|....*....|....*..
gi 2731058258 5 DVAVIGSGPGGYVAAIRCAQLGMKTAIIEKYSTLGGT 41
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGA 37
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
119-311 |
1.84e-06 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 49.53 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 119 KDATHITIageETT--EIEAKNTIIATG--SKPsNLPFIeldkeriitstealklKEIPKH--------------MIVIG 180
Cdd:pfam13738 103 KEDDGFVV---TTSkgTYQARYVIIATGefDFP-NKLGV----------------PELPKHysyvkdfhpyagqkVVVIG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 181 G---GV-IGLELGqvyrRLGAEVTVVeYMDRIIPTMDAGLSK--------ELNKVFKKAKFKMQVSHKVKSVERKGDEVI 248
Cdd:pfam13738 163 GynsAVdAALELV----RKGARVTVL-YRGSEWEDRDSDPSYslspdtlnRLEELVKNGKIKAHFNAEVKEITEVDVSYK 237
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2731058258 249 VKADNkkGEEVEFKGDYcLVSVGRSPYTDGLnaEAAGVKLDDRGRVEVDAHLQ-TSASNIYAIG 311
Cdd:pfam13738 238 VHTED--GRKVTSNDDP-ILATGYHPDLSFL--KKGLFELDEDGRPVLTEETEsTNVPGLFLAG 296
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
1-41 |
3.13e-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: 49.45 E-value: 3.13e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2731058258 1 MNSYDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKYSTLGGT 41
Cdd:COG1053 1 DHEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGGH 41
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
4-146 |
6.28e-06 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 48.35 E-value: 6.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 4 YDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKYSTLG--------GTClNV--GCIPSKALLD-------------SSHHY 60
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLGrkilisggGRC-NVtnLSEEPDNFLSrypgnpkflksalSRFTP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 61 EDAVKHFEEHGIEVpgEVKvNLEKM--IARKQAVVdqttggIDFL---MKKNNIDVY-----QGLGSFKDATHITIAGEE 130
Cdd:pfam03486 80 WDFIAFFESLGVPL--KEE-DHGRLfpDSDKASDI------VDALlneLKELGVKIRlrtrvLSVEKDDDGRFRVKTGGE 150
|
170
....*....|....*.
gi 2731058258 131 ttEIEAKNTIIATGSK 146
Cdd:pfam03486 151 --ELEADSLVLATGGL 164
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
3-40 |
7.78e-06 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 48.29 E-value: 7.78e-06
10 20 30
....*....|....*....|....*....|....*...
gi 2731058258 3 SYDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKYSTLGG 40
Cdd:PRK12839 8 TYDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKASTCGG 45
|
|
| glycerol3P_GlpB |
TIGR03378 |
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are ... |
4-32 |
2.35e-05 |
|
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: 46.55 E-value: 2.35e-05
10 20
....*....|....*....|....*....
gi 2731058258 4 YDVAVIGSGPGGYVAAIRCAQLGMKTAII 32
Cdd:TIGR03378 1 FDVIIIGGGLAGLSCALRLAEAGKKCAII 29
|
|
| GlpB |
COG3075 |
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism]; |
4-32 |
4.57e-05 |
|
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 442309 Cd Length: 415 Bit Score: 45.56 E-value: 4.57e-05
10 20
....*....|....*....|....*....
gi 2731058258 4 YDVAVIGSGPGGYVAAIRCAQLGMKTAII 32
Cdd:COG3075 3 FDVVVIGGGLAGLTAAIRAAEAGLRVAIV 31
|
|
| PRK12835 |
PRK12835 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
4-48 |
4.76e-05 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237221 [Multi-domain] Cd Length: 584 Bit Score: 45.95 E-value: 4.76e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2731058258 4 YDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKYSTLGG-TCLNVGCI 48
Cdd:PRK12835 12 VDVLVVGSGGGGMTAALTAAARGLDTLVVEKSAHFGGsTALSGGGI 57
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
3-41 |
4.94e-05 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 45.80 E-value: 4.94e-05
10 20 30
....*....|....*....|....*....|....*....
gi 2731058258 3 SYDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKYSTLGGT 41
Cdd:PRK07843 7 EYDVVVVGSGAAGMVAALTAAHRGLSTVVVEKAPHYGGS 45
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
4-41 |
5.85e-05 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 45.48 E-value: 5.85e-05
10 20 30
....*....|....*....|....*....|....*...
gi 2731058258 4 YDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKYSTLGGT 41
Cdd:PRK06134 13 CDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGGT 50
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
8-42 |
1.18e-04 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 40.21 E-value: 1.18e-04
10 20 30
....*....|....*....|....*....|....*
gi 2731058258 8 VIGSGPGGYVAAIRCAQLGMKTAIIEKYSTLGGTC 42
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNA 35
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
1-39 |
1.48e-04 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 43.77 E-value: 1.48e-04
10 20 30
....*....|....*....|....*....|....*....
gi 2731058258 1 MNSYDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKYSTLG 39
Cdd:COG0654 1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPR 39
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
3-41 |
1.49e-04 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 44.34 E-value: 1.49e-04
10 20 30
....*....|....*....|....*....|....*....
gi 2731058258 3 SYDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKYSTLGGT 41
Cdd:PRK12843 16 EFDVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGT 54
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
4-32 |
1.55e-04 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 44.07 E-value: 1.55e-04
10 20
....*....|....*....|....*....
gi 2731058258 4 YDVAVIGSGPGGYVAAIRCAQLGMKTAII 32
Cdd:PRK05329 3 FDVLVIGGGLAGLTAALAAAEAGKRVALV 31
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
4-41 |
1.66e-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: 1.66e-04
10 20 30
....*....|....*....|....*....|....*...
gi 2731058258 4 YDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKYSTLGGT 41
Cdd:COG2072 7 VDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGT 44
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
3-41 |
2.36e-04 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 43.53 E-value: 2.36e-04
10 20 30
....*....|....*....|....*....|....*....
gi 2731058258 3 SYDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKYSTLGGT 41
Cdd:PRK12842 9 TCDVLVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGGT 47
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
5-165 |
3.78e-04 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 42.92 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 5 DVAVIGSGPGGYVAAIRCAQLGMKTAIIEKYSTLGGTCLNVGCI-----PSKALLDSshHYEDAVKHfeeHGIEVpgevk 79
Cdd:COG1148 142 RALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAQLHKTfpgldCPQCILEP--LIAEVEAN---PNITV----- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 80 vnlekmiaRKQAVVDQTTGGIdflmkknnidvyqglGSFKdaTHITIAGEETTEIEAKNTIIATGSK---PSNLPFIELD 156
Cdd:COG1148 212 --------YTGAEVEEVSGYV---------------GNFT--VTIKKGPREEIEIEVGAIVLATGFKpydPTKLGEYGYG 266
|
170
....*....|
gi 2731058258 157 K-ERIITSTE 165
Cdd:COG1148 267 KyPNVITNLE 276
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
282-335 |
9.80e-04 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 41.66 E-value: 9.80e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2731058258 282 EAAGVKLDDRGR----VEVDAHLQTSASNIYAIGDVVKGAMLAHKAEEEGVFVAETIA 335
Cdd:PRK12769 591 ESHGVTVDKWGRiiadVESQYRYQTSNPKIFAGGDAVRGADLVVTAMAEGRHAAQGII 648
|
|
| PRK07494 |
PRK07494 |
UbiH/UbiF family hydroxylase; |
1-32 |
1.59e-03 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181001 [Multi-domain] Cd Length: 388 Bit Score: 40.66 E-value: 1.59e-03
10 20 30
....*....|....*....|....*....|..
gi 2731058258 1 MNSYDVAVIGSGPGGYVAAIRCAQLGMKTAII 32
Cdd:PRK07494 5 KEHTDIAVIGGGPAGLAAAIALARAGASVALV 36
|
|
| sdhA |
PRK07803 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
3-39 |
2.16e-03 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 236101 [Multi-domain] Cd Length: 626 Bit Score: 40.40 E-value: 2.16e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2731058258 3 SYDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKySTLG 39
Cdd:PRK07803 8 SYDVVVIGAGGAGLRAAIEARERGLRVAVVCK-SLFG 43
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
6-197 |
2.50e-03 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 40.31 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 6 VAVIGSGPGGYVAAIRCAQLGMKTAIIEKYSTLGGTcLNVGcIPS----KALLDSShhyedaVKHFEEHGievpgeVKVN 81
Cdd:PRK12775 433 VAICGSGPAGLAAAADLVKYGVDVTVYEALHVVGGV-LQYG-IPSfrlpRDIIDRE------VQRLVDIG------VKIE 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 82 LEKMIARkqavvdqtTGGIDFLMKKNNID-VYQGLGSfKDATHITIAGEETTEIEAKNTIIATGSKPSNLPFIELDKEri 160
Cdd:PRK12775 499 TNKVIGK--------TFTVPQLMNDKGFDaVFLGVGA-GAPTFLGIPGEFAGQVYSANEFLTRVNLMGGDKFPFLDTP-- 567
|
170 180 190
....*....|....*....|....*....|....*..
gi 2731058258 161 ITstealklkeIPKHMIVIGGGVIGLELGQVYRRLGA 197
Cdd:PRK12775 568 IS---------LGKSVVVIGAGNTAMDCLRVAKRLGA 595
|
|
| PRK08849 |
PRK08849 |
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional |
1-33 |
2.52e-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: 2.52e-03
10 20 30
....*....|....*....|....*....|...
gi 2731058258 1 MNSYDVAVIGSGPGGYVAAIRCAQLGMKTAIIE 33
Cdd:PRK08849 1 MNKYDIAVVGGGMVGAATALGFAKQGRSVAVIE 33
|
|
| PRK06481 |
PRK06481 |
flavocytochrome c; |
2-43 |
2.56e-03 |
|
flavocytochrome c;
Pssm-ID: 180584 [Multi-domain] Cd Length: 506 Bit Score: 40.20 E-value: 2.56e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2731058258 2 NSYDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKYSTLGGTCL 43
Cdd:PRK06481 60 DKYDIVIVGAGGAGMSAAIEAKDAGMNPVILEKMPVAGGNTM 101
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
4-146 |
3.57e-03 |
|
geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 273936 [Multi-domain] Cd Length: 295 Bit Score: 39.22 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731058258 4 YDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKYSTLG-GTClnVGCIPSKALLDSSHHYEDAVKHFEEHGIEVPGEVKVNL 82
Cdd:TIGR02032 1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPRyKPC--GGALSPRALEELDLPGELIVNLVRGARFFSPNGDSVEI 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2731058258 83 EK------MIARK---QAVVDQTTG-GIDFLMKKNNIDVYQGlgsfKDATHITIAGEETTeIEAKNTIIATGSK 146
Cdd:TIGR02032 79 PIetelayVIDRDafdEQLAERAQEaGAELRLGTRVLDVEIH----DDRVVVIVRGSEGT-VTAKIVIGADGSR 147
|
|
| Lys_Orn_oxgnase |
pfam13434 |
L-lysine 6-monooxygenase/L-ornithine 5-monooxygenase; This is a family of Rossmann fold ... |
130-182 |
6.30e-03 |
|
L-lysine 6-monooxygenase/L-ornithine 5-monooxygenase; This is a family of Rossmann fold oxidoreductases that catalyze NADPH-dependent hydroxylation and are involved in siderophore biosynthesis. This family includes L-ornithine 5-monooxygenase, which catalyzes the hydroxylation of L-ornithine at the N5 position, and L-lysine 6-monooxygenase, which catalyzes the hydroxylation of lysine at the N6 position (EC:1.14.13.59).
Pssm-ID: 433204 [Multi-domain] Cd Length: 338 Bit Score: 38.72 E-value: 6.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2731058258 130 ETTEIEAKNTIIATGSKPSnLPFIELDKERIITSTEALKLKEI---PKHMIVIGGG 182
Cdd:pfam13434 142 EETTFLARNLVLGTGGEPY-IPECARGGERVFHSSEYLERIDRlaaKKRIAVVGSG 196
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
3-42 |
8.46e-03 |
|
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: 38.27 E-value: 8.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2731058258 3 SYDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKYSTLGGTC 42
Cdd:COG1232 1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLI 40
|
|
| |
