|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
1-461 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 623.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 1 MKYDILVLGSGPGGYVTAIRASQLGMKVAIVEREALGGICLNWGCIPTKALLKSANVFEYIEHAGDYGINVAKPKVDFTG 80
Cdd:PRK06416 3 FEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIKAENVGIDFKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 81 MVSRSRGVANGMSKGVQFLMKKNKIDVIMGNGKLMPGRKVEVTDADGGQQmVEADHIIIATGARSRQLPNLPQDGKKIMG 160
Cdd:PRK06416 83 VQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDGEQT-YTAKNIILATGSRPRELPGIEIDGRVIWT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 161 YREAMTMEKQPKKLVVVGSGAIGVEFAYFYNAIGTNVTIVEYMPNIVPVEDEEVSKQLARSFKKSGIHIMTSSEVTGVDT 240
Cdd:PRK06416 162 SDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPGEDKEISKLAERALKKRGIKIKTGAKAKKVEQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 241 SGKGCKVHVKTKKGEEVLDADVVLSAVGVVSNIDGIGLEEVGIAADRGKLIVDDFYKTNIPGYYAIGDCVPGPALAHVAS 320
Cdd:PRK06416 242 TDDGVTVTLEDGGKEETLEADYVLVAVGRRPNTENLGLEELGVKTDRGFIEVDEQLRTNVPNIYAIGDIVGGPMLAHKAS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 321 AEGILCVEKIAGHNVePLDYGNIPGCTYCFPEVASVGKTEEDCKKEGIDIKVGKFPFSASGKASAAGHKDGFVKLIFDAK 400
Cdd:PRK06416 322 AEGIIAAEAIAGNPH-PIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFDVKVVKFPFAGNGKALALGETDGFVKLIFDKK 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519712285 401 YGELLGGHMIGANVTEMIAEIVAIRKLETTGHEMIKTVHPHPTLSEAVMEAAAAAYDEVIH 461
Cdd:PRK06416 401 DGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEALGEAALAAAGKPLH 461
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
1-450 |
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: 603.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 1 MKYDILVLGSGPGGYVTAIRASQLGMKVAIVEREALGGICLNWGCIPTKALLKSANVFEYIEHAGDYGINVAKPKVDFTG 80
Cdd:COG1249 2 KDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISAGAPSVDWAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 81 MVSRSRGVANGMSKGVQFLMKKNKIDVIMGNGKLMPGRKVEVTdadgGQQMVEADHIIIATGARSRQLPNLPQDGKKIMG 160
Cdd:COG1249 82 LMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVT----GGETLTADHIVIATGSRPRVPPIPGLDEVRVLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 161 YREAMTMEKQPKKLVVVGSGAIGVEFAYFYNAIGTNVTIVEYMPNIVPVEDEEVSKQLARSFKKSGIHIMTSSEVTGVDT 240
Cdd:COG1249 158 SDEALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 241 SGKGCKVHVKTKKGEEVLDADVVLSAVGVVSNIDGIGLEEVGIAAD-RGKLIVDDFYKTNIPGYYAIGDCVPGPALAHVA 319
Cdd:COG1249 238 TGDGVTVTLEDGGGEEAVEADKVLVATGRRPNTDGLGLEAAGVELDeRGGIKVDEYLRTSVPGIYAIGDVTGGPQLAHVA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 320 SAEGILCVEKIAGHNVEPLDYGNIPGCTYCFPEVASVGKTEEDCKKEGIDIKVGKFPFSASGKASAAGHKDGFVKLIFDA 399
Cdd:COG1249 318 SAEGRVAAENILGKKPRPVDYRAIPSVVFTDPEIASVGLTEEEAREAGIDVKVGKFPFAANGRALALGETEGFVKLIADA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1519712285 400 KYGELLGGHMIGANVTEMIAEIVAIRKLETTGHEMIKTVHPHPTLSEAVME 450
Cdd:COG1249 398 ETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKE 448
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
3-461 |
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: 558.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 3 YDILVLGSGPGGYVTAIRASQLGMKVAIVEREALGGICLNWGCIPTKALLKSANVFEYIEHAGDYGINVAKPKVDFTGMV 82
Cdd:TIGR01350 2 YDVIVIGGGPGGYVAAIRAAQLGLKVALVEKEYLGGTCLNVGCIPTKALLHSAEVYDEIKHAKDLGIEVENVSVDWEKMQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 83 SRSRGVANGMSKGVQFLMKKNKIDVIMGNGKLMPGRKVEVTDaDGGQQMVEADHIIIATGARSRQLPN-LPQDGKKIMGY 161
Cdd:TIGR01350 82 KRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTG-ENGEETLEAKNIIIATGSRPRSLPGpFDFDGKVVITS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 162 REAMTMEKQPKKLVVVGSGAIGVEFAYFYNAIGTNVTIVEYMPNIVPVEDEEVSKQLARSFKKSGIHIMTSSEVTGVDTS 241
Cdd:TIGR01350 161 TGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEKN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 242 GKGCKVHVKtKKGEEVLDADVVLSAVGVVSNIDGIGLEEVGIAAD-RGKLIVDDFYKTNIPGYYAIGDCVPGPALAHVAS 320
Cdd:TIGR01350 241 DDQVTYENK-GGETETLTGEKVLVAVGRKPNTEGLGLEKLGVELDeRGRIVVDEYMRTNVPGIYAIGDVIGGPMLAHVAS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 321 AEGILCVEKIAGHNVEPLDYGNIPGCTYCFPEVASVGKTEEDCKKEGIDIKVGKFPFSASGKASAAGHKDGFVKLIFDAK 400
Cdd:TIGR01350 320 HEGIVAAENIAGKEPAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGYDVKIGKFPFAANGKALALGETDGFVKIIADKK 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519712285 401 YGELLGGHMIGANVTEMIAEIVAIRKLETTGHEMIKTVHPHPTLSEAVMEAAAAAYDEVIH 461
Cdd:TIGR01350 400 TGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEAIKEAALAALGKPIH 460
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
1-450 |
3.04e-167 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 478.90 E-value: 3.04e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 1 MKYDILVLGSGPGGYVTAIRASQLGMKVAIVEREALGGICLNWGCIPTKALLKSANVFEYIEHAGDYGINVAKPKVDFTG 80
Cdd:PRK06292 2 EKYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGPLGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHADGPKIDFKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 81 MVSRSRGVANGMSKGV-QFLMKKNKIDVIMGNGKLMPGRKVEVtdadgGQQMVEADHIIIATGARSRQLPNLPQ-DGKKI 158
Cdd:PRK06292 82 VMARVRRERDRFVGGVvEGLEKKPKIDKIKGTARFVDPNTVEV-----NGERIEAKNIVIATGSRVPPIPGVWLiLGDRL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 159 MGYREAMTMEKQPKKLVVVGSGAIGVEFAYFYNAIGTNVTIVEYMPNIVPVEDEEVSKQLARSFKKSgIHIMTSSEVTGV 238
Cdd:PRK06292 157 LTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILSKE-FKIKLGAKVTSV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 239 DTSGKGCKVHVKTKKGEEVLDADVVLSAVGVVSNIDGIGLEEVGIAAD-RGKLIVDDFYKTNIPGYYAIGDCVPGPALAH 317
Cdd:PRK06292 236 EKSGDEKVEELEKGGKTETIEADYVLVATGRRPNTDGLGLENTGIELDeRGRPVVDEHTQTSVPGIYAAGDVNGKPPLLH 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 318 VASAEGILCVEKIAGHNVEPLDYGNIPGCTYCFPEVASVGKTEEDCKKEGIDIKVGKFPFSASGKASAAGHKDGFVKLIF 397
Cdd:PRK06292 316 EAADEGRIAAENAAGDVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEVPFEAQGRARVMGKNDGFVKVYA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1519712285 398 DAKYGELLGGHMIGANVTEMIAEIVAIRKLETTGHEMIKTVHPHPTLSEAVME 450
Cdd:PRK06292 396 DKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRT 448
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
2-450 |
1.07e-162 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 467.87 E-value: 1.07e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 2 KYDILVLGSGPGGYVTAIRASQLGMKVAIVE-------REALGGICLNWGCIPTKALLKSANVFEYIEHA-GDYGINVAK 73
Cdd:PRK06327 4 QFDVVVIGAGPGGYVAAIRAAQLGLKVACIEawknpkgKPALGGTCLNVGCIPSKALLASSEEFENAGHHfADHGIHVDG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 74 PKVDFTGMVSRSRGVANGMSKGVQFLMKKNKIDVIMGNGKLMP----GRKVEVTDADGgqQMVEADHIIIATGARSRQLP 149
Cdd:PRK06327 84 VKIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVGktdaGYEIKVTGEDE--TVITAKHVIIATGSEPRHLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 150 NLPQDGKKIMGYREAMTMEKQPKKLVVVGSGAIGVEFAYFYNAIGTNVTIVEYMPNIVPVEDEEVSKQLARSFKKSGIHI 229
Cdd:PRK06327 162 GVPFDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAAADEQVAKEAAKAFTKQGLDI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 230 MTSSEVTGVDTSGKGCKVHVKTKKGEE-VLDADVVLSAVGVVSNIDGIGLEEVGIAAD-RGKLIVDDFYKTNIPGYYAIG 307
Cdd:PRK06327 242 HLGVKIGEIKTGGKGVSVAYTDADGEAqTLEVDKLIVSIGRVPNTDGLGLEAVGLKLDeRGFIPVDDHCRTNVPNVYAIG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 308 DCVPGPALAHVASAEGILCVEKIAGHNvEPLDYGNIPGCTYCFPEVASVGKTEEDCKKEGIDIKVGKFPFSASGKASAAG 387
Cdd:PRK06327 322 DVVRGPMLAHKAEEEGVAVAERIAGQK-GHIDYNTIPWVIYTSPEIAWVGKTEQQLKAEGVEYKAGKFPFMANGRALAMG 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1519712285 388 HKDGFVKLIFDAKYGELLGGHMIGANVTEMIAEIVAIRKLETTGHEMIKTVHPHPTLSEAVME 450
Cdd:PRK06327 401 EPDGFVKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEVWHE 463
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
2-448 |
1.75e-114 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 344.49 E-value: 1.75e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 2 KYDILVLGSGPGGYVTAIRASQLGMKVAIVEREALGGICLNWGCIPTKALLKSANVFEYIEHAGDYGINVAKP-KVDFTG 80
Cdd:PRK06370 5 RYDAIVIGAGQAGPPLAARAAGLGMKVALIERGLLGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGGPvSVDFKA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 81 MVSRSRGVANGMSKGV-QFLMKKNKIDVIMGNGKLMPGRKVEVTDADggqqmVEADHIIIATGARSrQLPNLPqdGKKIM 159
Cdd:PRK06370 85 VMARKRRIRARSRHGSeQWLRGLEGVDVFRGHARFESPNTVRVGGET-----LRAKRIFINTGARA-AIPPIP--GLDEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 160 GYR---EAMTMEKQPKKLVVVGSGAIGVEFAYFYNAIGTNVTIVEYMPNIVPVEDEEVSKQLARSFKKSGIHIMTSSEVT 236
Cdd:PRK06370 157 GYLtneTIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILEREGIDVRLNAECI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 237 GVDTSGKGCKVHVKTKKGEEVLDADVVLSAVGVVSNIDGIGLEEVGIAAD-RGKLIVDDFYKTNIPGYYAIGDCVPGPAL 315
Cdd:PRK06370 237 RVERDGDGIAVGLDCNGGAPEITGSHILVAVGRVPNTDDLGLEAAGVETDaRGYIKVDDQLRTTNPGIYAAGDCNGRGAF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 316 AHVASAEGILCVEKIAGHNVEPLDYGNIPGCTYCFPEVASVGKTEEDCKKEGIDIKVGKFPFSASGKASAAGHKDGFVKL 395
Cdd:PRK06370 317 THTAYNDARIVAANLLDGGRRKVSDRIVPYATYTDPPLARVGMTEAEARKSGRRVLVGTRPMTRVGRAVEKGETQGFMKV 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1519712285 396 IFDAKYGELLGGHMIGANVTEMIAEIVAIRKLETTGHEMIKTVHPHPTLSEAV 448
Cdd:PRK06370 397 VVDADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELI 449
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
1-447 |
4.13e-89 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 278.96 E-value: 4.13e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 1 MKYDILVLGSGPGGYVTAIRASQLGMKVAIVERE-ALGGICLNWGCIPTKALLKSA-NVFEYIEHA--GDYGInvaKPKV 76
Cdd:PRK05249 4 YDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYrNVGGGCTHTGTIPSKALREAVlRLIGFNQNPlySSYRV---KLRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 77 DFTGMVSRSRGVANGMSKGVQFLMKKNKIDVIMGNGKLMPGRKVEVTDADGGQQMVEADHIIIATGARSRQLPNLPQDGK 156
Cdd:PRK05249 81 TFADLLARADHVINKQVEVRRGQYERNRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATGSRPYRPPDVDFDHP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 157 KIMGYREAMTMEKQPKKLVVVGSGAIGVEFAYFYNAIGTNVTIVEYMPNIVPVEDEEVSKQLARSFKKSGIHIMTSSEVT 236
Cdd:PRK05249 161 RIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSFLDDEISDALSYHLRDSGVTIRHNEEVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 237 GVDTSGKGCKVHVKTKKgeeVLDADVVLSAVGVVSNIDGIGLEEVGIAAD-RGKLIVDDFYKTNIPGYYAIGDCVPGPAL 315
Cdd:PRK05249 241 KVEGGDDGVIVHLKSGK---KIKADCLLYANGRTGNTDGLNLENAGLEADsRGQLKVNENYQTAVPHIYAVGDVIGFPSL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 316 AHVASAEGILCVEKIAGH-NVEPLDYgnIPGCTYCFPEVASVGKTEEDCKKEGIDIKVGKFPFSASGKASAAGHKDGFVK 394
Cdd:PRK05249 318 ASASMDQGRIAAQHAVGEaTAHLIED--IPTGIYTIPEISSVGKTEQELTAAKVPYEVGRARFKELARAQIAGDNVGMLK 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1519712285 395 LIFDAKYGELLGGHMIGANVTEMIAEIVAIRKLETTGHEMIKTVHPHPTLSEA 447
Cdd:PRK05249 396 ILFHRETLEILGVHCFGERATEIIHIGQAIMEQKGTIEYFVNTTFNYPTMAEA 448
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
3-446 |
5.79e-79 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 252.38 E-value: 5.79e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 3 YDILVLGSGPGGYVTAIRASQLGMKVAIVEREALGGICLNWGCIPTKALLKSANVFEYIEH-AGDYGINVAKPKVDFTGM 81
Cdd:PRK06116 5 YDLIVIGGGSGGIASANRAAMYGAKVALIEAKRLGGTCVNVGCVPKKLMWYGAQIAEAFHDyAPGYGFDVTENKFDWAKL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 82 V-------SRSRGVANGMskgvqflMKKNKIDVIMGNGKLMPGRKVEVTDadggqQMVEADHIIIATGARSrQLPNLPqd 154
Cdd:PRK06116 85 IanrdayiDRLHGSYRNG-------LENNGVDLIEGFARFVDAHTVEVNG-----ERYTADHILIATGGRP-SIPDIP-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 155 GKKimgY----REAMTMEKQPKKLVVVGSGAIGVEFAYFYNAIGTNVTIVEYMPNIVPVEDEEVSKQLARSFKKSGIHIM 230
Cdd:PRK06116 150 GAE---YgitsDGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLH 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 231 TSSEVTGVDTSGKGcKVHVKTKKGEEvLDADVVLSAVGVVSNIDGIGLEEVGIA-ADRGKLIVDDFYKTNIPGYYAIGDC 309
Cdd:PRK06116 227 TNAVPKAVEKNADG-SLTLTLEDGET-LTVDCLIWAIGREPNTDGLGLENAGVKlNEKGYIIVDEYQNTNVPGIYAVGDV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 310 VPGPALAHVASAEGILCVEKIAGHN-VEPLDYGNIPGCTYCFPEVASVGKTEEDCKKEGID--IKVGKFPFsASGKASAA 386
Cdd:PRK06116 305 TGRVELTPVAIAAGRRLSERLFNNKpDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEdnVKVYRSSF-TPMYTALT 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519712285 387 GHKDG-FVKLIFDAKYGELLGGHMIGANVTEMIAEI-VAIrKLETTGHEMIKTVHPHPTLSE 446
Cdd:PRK06116 384 GHRQPcLMKLVVVGKEEKVVGLHGIGFGADEMIQGFaVAI-KMGATKADFDNTVAIHPTAAE 444
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
5-418 |
2.52e-78 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 251.32 E-value: 2.52e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 5 ILVLGSGPGGYVTAIRASQLGMKVAIVEREALGGICLNWGCIPTKALLKSANVFEYIEHAGDYGINVA---KPKVDFTGM 81
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIERDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRFIddgEARVDLPAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 82 VSRSRGVANGMSKGVQFLMKKNKIDVIMGNGKL----MPGRKVEVTDADGGQQMVEADHIIIATGARSRQLPNLPQDGKK 157
Cdd:PRK07845 84 NARVKALAAAQSADIRARLEREGVRVIAGRGRLidpgLGPHRVKVTTADGGEETLDADVVLIATGASPRILPTAEPDGER 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 158 IMGYREAMTMEKQPKKLVVVGSGAIGVEFAYFYNAIGTNVTIVEYMPNIVPVEDEEVSKQLARSFKKSGIHIMTSSEVTG 237
Cdd:PRK07845 164 ILTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPGEDADAAEVLEEVFARRGMTVLKRSRAES 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 238 VDTSGKGckVHVKTKKGEEVlDADVVLSAVGVVSNIDGIGLEEVGIA-ADRGKLIVDDFYKTNIPGYYAIGDCVPGPALA 316
Cdd:PRK07845 244 VERTGDG--VVVTLTDGRTV-EGSHALMAVGSVPNTAGLGLEEAGVElTPSGHITVDRVSRTSVPGIYAAGDCTGVLPLA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 317 HVASAEGILCVEKIAGHNVEPLDYGNIPGCTYCFPEVASVGKTEEDCKKEGIDIKVGKFPFSASGKASAAGHKDGFVKLI 396
Cdd:PRK07845 321 SVAAMQGRIAMYHALGEAVSPLRLKTVASNVFTRPEIATVGVSQAAIDSGEVPARTVMLPLATNPRAKMSGLRDGFVKLF 400
|
410 420
....*....|....*....|..
gi 1519712285 397 FDAKYGELLGGHMIGANVTEMI 418
Cdd:PRK07845 401 CRPGTGVVIGGVVVAPRASELI 422
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
3-448 |
6.63e-74 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 239.47 E-value: 6.63e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 3 YDILVLGSGPGGYVTAIRASqlGMKVAIVEREALGGICLNWGCIPTKALLKSANVFEYIEHAGDYGINVAKPKVDFTGMV 82
Cdd:PRK07846 2 YDLIIIGTGSGNSILDERFA--DKRIAIVEKGTFGGTCLNVGCIPTKMFVYAADVARTIREAARLGVDAELDGVRWPDIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 83 SRSRGVANGMSK-GVQFLMKKN-KIDVIMGNGKLMPGRKVEVTDADggqqMVEADHIIIATGARSRQLPNLPQDGKKIMG 160
Cdd:PRK07846 80 SRVFGRIDPIAAgGEEYRGRDTpNIDVYRGHARFIGPKTLRTGDGE----EITADQVVIAAGSRPVIPPVIADSGVRYHT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 161 YREAMTMEKQPKKLVVVGSGAIGVEFAYFYNAIGTNVTIVEYMPNIVPVEDEEVSKQLARSFKKSGIHIMtSSEVTGVDT 240
Cdd:PRK07846 156 SDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLDDDISERFTELASKRWDVRL-GRNVVGVSQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 241 SGKGCKVhvkTKKGEEVLDADVVLSAVGVVSNIDGIGLEEVGIAADR-GKLIVDDFYKTNIPGYYAIGDcVPGP-ALAHV 318
Cdd:PRK07846 235 DGSGVTL---RLDDGSTVEADVLLVATGRVPNGDLLDAAAAGVDVDEdGRVVVDEYQRTSAEGVFALGD-VSSPyQLKHV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 319 ASAEGilcveKIAGHNV------EPLDYGNIPGCTYCFPEVASVGKTEEDCKKEGIDIKVGKFPFSASGKASAAGHKDGF 392
Cdd:PRK07846 311 ANHEA-----RVVQHNLlhpddlIASDHRFVPAAVFTHPQIASVGLTENEARAAGLDITVKVQNYGDVAYGWAMEDTTGF 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1519712285 393 VKLIFDAKYGELLGGHMIGANVTEMIAEIVAIRKLETTGHEMIKTVH-PHPTLSEAV 448
Cdd:PRK07846 386 VKLIADRDTGRLLGAHIIGPQASTLIQPLIQAMSFGLDAREMARGQYwIHPALPEVV 442
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
3-323 |
7.36e-73 |
|
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: 231.82 E-value: 7.36e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 3 YDILVLGSGPGGYVTAIRASQLGMKVAIVEreaLGGICLNWGCIPTKALLKSANVFEYIEHAGDYginvakpkvdftgmV 82
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIE---DEGTCPYGGCVLSKALLGAAEAPEIASLWADL--------------Y 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 83 SRSRGVANGMSKGVQFLMKKNKIDVIMGNGKLmpgrkVEVTDADGGQQMVEADHIIIATGARSRqLPNLPQD------GK 156
Cdd:pfam07992 64 KRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKV-----VLEELVDGDGETITYDRLVIATGARPR-LPPIPGVelnvgfLV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 157 KIMGYREAMTMEKQPKKLVVVGSGAIGVEFAYFYNAIGTNVTIVEYMPNIVPVEDEEVSKQLARSFKKSGIHIMTSSEVT 236
Cdd:pfam07992 138 RTLDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 237 GVDtsGKGCKVHVKTKKGEEvLDADVVLSAVGVVSNIDgiGLEEVGIAAD-RGKLIVDDFYKTNIPGYYAIGDC-VPGPA 314
Cdd:pfam07992 218 EII--GDGDGVEVILKDGTE-IDADLVVVAIGRRPNTE--LLEAAGLELDeRGGIVVDEYLRTSVPGIYAAGDCrVGGPE 292
|
....*....
gi 1519712285 315 LAHVASAEG 323
Cdd:pfam07992 293 LAQNAVAQG 301
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
2-446 |
1.01e-64 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 215.00 E-value: 1.01e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 2 KYDILVLGSGPGGYVTAIRASQLGMKVAIVEREAL--GGICLNWGCIPTKALLKSAnvfeyiEHAGDYGINVAKPKVdft 79
Cdd:PRK07251 3 TYDLIVIGFGKAGKTLAAKLASAGKKVALVEESKAmyGGTCINIGCIPTKTLLVAA------EKNLSFEQVMATKNT--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 80 gMVSRSRGVANGMSKGvqflmkkNKIDVIMGNGKLMPGRKVEVTDADGGQQMvEADHIIIATGARSRQLPnLP--QDGKK 157
Cdd:PRK07251 74 -VTSRLRGKNYAMLAG-------SGVDLYDAEAHFVSNKVIEVQAGDEKIEL-TAETIVINTGAVSNVLP-IPglADSKH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 158 IMGYREAMTMEKQPKKLVVVGSGAIGVEFAYFYNAIGTNVTIVEYMPNIVPVEDEEVSKQLARSFKKSGIHIMTSSEVTG 237
Cdd:PRK07251 144 VYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYMEEDGITFLLNAHTTE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 238 VdtSGKGCKVHVKTKKGEEVLDAdvVLSAVGVVSNIDGIGLEEVGIA-ADRGKLIVDDFYKTNIPGYYAIGDCVPGPALA 316
Cdd:PRK07251 224 V--KNDGDQVLVVTEDETYRFDA--LLYATGRKPNTEPLGLENTDIElTERGAIKVDDYCQTSVPGVFAVGDVNGGPQFT 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 317 HVASAEGILCVEKIAGHNVEPL-DYGNIPGCTYCFPEVASVGKTEEDCKKEGIDIKVGKFPFSASGKASAAGHKDGFVKL 395
Cdd:PRK07251 300 YISLDDFRIVFGYLTGDGSYTLeDRGNVPTTMFITPPLSQVGLTEKEAKEAGLPYAVKELLVAAMPRAHVNNDLRGAFKV 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1519712285 396 IFDAKYGELLGGHMIGANVTEMIAEI-VAI-RKLETTghEMIKTVHPHPTLSE 446
Cdd:PRK07251 380 VVNTETKEILGATLFGEGSQEIINLItMAMdNKIPYT--YFKKQIFTHPTMAE 430
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
3-446 |
2.42e-62 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 210.44 E-value: 2.42e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 3 YDILVLGSGPGGYVTAIRASQLGMKVAIVE-------REALGGI---CLNWGCIPTKALLKSANVFEYIEHAGDYGINVA 72
Cdd:PLN02507 26 FDLFVIGAGSGGVRAARFSANFGAKVGICElpfhpisSESIGGVggtCVIRGCVPKKILVYGATFGGEFEDAKNYGWEIN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 73 KpKVDFTG---MVSRSRGVA--NGMSKGvqfLMKKNKIDVIMGNGKLMPGRKVEVTDADGGQQMVEADHIIIATGARSrQ 147
Cdd:PLN02507 106 E-KVDFNWkklLQKKTDEILrlNGIYKR---LLANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRYTAKHILIATGSRA-Q 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 148 LPNLPqdGKKI-MGYREAMTMEKQPKKLVVVGSGAIGVEFAYFYNAIGTNVTIVEYMPNIVPVEDEEVSKQLARSFKKSG 226
Cdd:PLN02507 181 RPNIP--GKELaITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRAVVARNLEGRG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 227 IHIMTSSEVTGVDTSGKGCKvhVKTKKGEEVLdADVVLSAVGVVSNIDGIGLEEVGIAADR-GKLIVDDFYKTNIPGYYA 305
Cdd:PLN02507 259 INLHPRTNLTQLTKTEGGIK--VITDHGEEFV-ADVVLFATGRAPNTKRLNLEAVGVELDKaGAVKVDEYSRTNIPSIWA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 306 IGDCVPGPALAHVASAEGIlCVEK--IAGHNVEPlDYGNIPGCTYCFPEVASVGKTEEDCKKEGI-DIKVGKFPFSASGK 382
Cdd:PLN02507 336 IGDVTNRINLTPVALMEGT-CFAKtvFGGQPTKP-DYENVACAVFCIPPLSVVGLSEEEAVEQAKgDILVFTSSFNPMKN 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1519712285 383 ASAAGHKDGFVKLIFDAKYGELLGGHMIGANVTEMIAEIVAIRKLETTGHEMIKTVHPHPTLSE 446
Cdd:PLN02507 414 TISGRQEKTVMKLIVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAE 477
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
3-448 |
2.49e-58 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 203.22 E-value: 2.49e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 3 YDILVLGSGPGGYVTAIRASQLGMKVAIV--EREALGGICLNWGCIPTKALLKSANVFEYIE---HAGDYGI--NVAKP- 74
Cdd:PTZ00153 117 YDVGIIGCGVGGHAAAINAMERGLKVIIFtgDDDSIGGTCVNVGCIPSKALLYATGKYRELKnlaKLYTYGIytNAFKNg 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 75 ---------------KVDFTGMVSRSRGVANGMSKGVQFLMKKNKIDVIMGNGKLM--PGRKVEVTDADGGQQMVE--AD 135
Cdd:PTZ00153 197 kndpvernqlvadtvQIDITKLKEYTQSVIDKLRGGIENGLKSKKFCKNSEHVQVIyeRGHIVDKNTIKSEKSGKEfkVK 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 136 HIIIATGArsrqLPNLP----QDGKKIMGYREAMTMEKQPKKLVVVGSGAIGVEFAYFYNAIGTNVTIVEYMPNIVPVED 211
Cdd:PTZ00153 277 NIIIATGS----TPNIPdnieVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSPQLLPLLD 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 212 EEVSKQLARSFKKSG-IHIMTSSEVTGVDTSGKGCKV---HVKTKKGEE-----------VLDADVVLSAVGVVSNIDGI 276
Cdd:PTZ00153 353 ADVAKYFERVFLKSKpVRVHLNTLIEYVRAGKGNQPViigHSERQTGESdgpkknmndikETYVDSCLVATGRKPNTNNL 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 277 GLEEVGIAADRGKLIVDDFYKTN------IPGYYAIGDCVPGPALAHVASAEGILCVEKIAGHNVE------------PL 338
Cdd:PTZ00153 433 GLDKLKIQMKRGFVSVDEHLRVLredqevYDNIFCIGDANGKQMLAHTASHQALKVVDWIEGKGKEnvninvenwaskPI 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 339 DYGNIPGCTYCFPEVASVGKTEEDCKKEGIDIKVGK------------------FPFSAS------GKASAAGHKDGFVK 394
Cdd:PTZ00153 513 IYKNIPSVCYTTPELAFIGLTEKEAKELYPPDNVGVeisfykanskvlcennisFPNNSKnnsynkGKYNTVDNTEGMVK 592
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1519712285 395 LIFDAKYGELLGGHMIGANVTEMIAEIVAIRKLETTGHEMIKTVHPHPTLSEAV 448
Cdd:PTZ00153 593 IVYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVL 646
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
3-446 |
1.84e-54 |
|
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase.
Pssm-ID: 200098 [Multi-domain] Cd Length: 486 Bit Score: 189.03 E-value: 1.84e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 3 YDILVLGSGPGGYVTAIRASQL-GMKVAIVERE---------ALGGICLNWGCIPTKALLKSANVFEYIEHAGDYG--IN 70
Cdd:TIGR01423 4 FDLVVIGAGSGGLEAGWNAATLyKKRVAVVDVQthhgppfyaALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGweFD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 71 VAKPKVDFTGMVSRSRGVANGMSKGVQFLMKKNK-IDVIMGNGKLMPGRKVEVTD-ADGGQQMVE---ADHIIIATGARS 145
Cdd:TIGR01423 84 RSSVKANWKALIAAKNKAVLDINKSYEGMFADTEgLTFFLGWGALEDKNVVLVREsADPKSAVKErlqAEHILLATGSWP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 146 rQLPNLPQDGKKIMGyREAMTMEKQPKKLVVVGSGAIGVEFAYFYNA---IGTNVTIVEYMPNIVPVEDEEVSKQLARSF 222
Cdd:TIGR01423 164 -QMLGIPGIEHCISS-NEAFYLDEPPRRVLTVGGGFISVEFAGIFNAykpRGGKVTLCYRNNMILRGFDSTLRKELTKQL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 223 KKSGIHIMTSSEVTGVDTSGKGCKvHVKTKKGEEvLDADVVLSAVGVVSNIDGIGLEEVGI-AADRGKLIVDDFYKTNIP 301
Cdd:TIGR01423 242 RANGINIMTNENPAKVTLNADGSK-HVTFESGKT-LDVDVVMMAIGRVPRTQTLQLDKVGVeLTKKGAIQVDEFSRTNVP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 302 GYYAIGDCVPGPALAHVASAEGILCVEKIAGHNVEPLDYGNIPGCTYCFPEVASVGKTEEDCKKEGIDIKVGKFPFSA-S 380
Cdd:TIGR01423 320 NIYAIGDVTDRVMLTPVAINEGAAFVDTVFGNKPRKTDHTRVASAVFSIPPIGTCGLVEEDAAKKFEKVAVYESSFTPlM 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519712285 381 GKASAAGHKDGFVKLIFDAKYGELLGGHMIGANVTEMIAEIVAIRKLETTGHEMIKTVHPHPTLSE 446
Cdd:TIGR01423 400 HNISGSKYKKFVAKIVTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAE 465
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
5-446 |
2.35e-53 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 187.67 E-value: 2.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 5 ILVLGSGPGGYVTAIRASQLGMKVAIVEREALGGICLNWGCIPTKALLKSANVFEY-IEHAGDYGINVAKPKVDFTGMVS 83
Cdd:PRK13748 101 VAVIGSGGAAMAAALKAVEQGARVTLIERGTIGGTCVNVGCVPSKIMIRAAHIAHLrRESPFDGGIAATVPTIDRSRLLA 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 84 RSRGVANGM--SKGVQFLMKKNKIDVIMGNGKLMPGRKVEVTDADGGQQMVEADHIIIATGArSRQLPNLPqdGKKIMGY 161
Cdd:PRK13748 181 QQQARVDELrhAKYEGILDGNPAITVLHGEARFKDDQTLIVRLNDGGERVVAFDRCLIATGA-SPAVPPIP--GLKETPY 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 162 ---REAMTMEKQPKKLVVVGSGAIGVEFAYFYNAIGTNVTIVEyMPNIVPVEDEEVSKQLARSFKKSGIHIMTSSEVTGV 238
Cdd:PRK13748 258 wtsTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILA-RSTLFFREDPAIGEAVTAAFRAEGIEVLEHTQASQV 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 239 dTSGKGCKVhVKTKKGEevLDADVVLSAVGVVSNIDGIGLEEVGIAAD-RGKLIVDDFYKTNIPGYYAIGDCVPGPALAH 317
Cdd:PRK13748 337 -AHVDGEFV-LTTGHGE--LRADKLLVATGRAPNTRSLALDAAGVTVNaQGAIVIDQGMRTSVPHIYAAGDCTDQPQFVY 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 318 VASAEGILCVEKIAGHNVEpLDYGNIPGCTYCFPEVASVGKTEEDCKKEGIDIKVGKFPFSASGKASAAGHKDGFVKLIF 397
Cdd:PRK13748 413 VAAAAGTRAAINMTGGDAA-LDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRTLTLDNVPRALANFDTRGFIKLVI 491
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1519712285 398 DAKYGELLGGHMIGANVTEMI-AEIVAIRKlETTGHEMIKTVHPHPTLSE 446
Cdd:PRK13748 492 EEGSGRLIGVQAVAPEAGELIqTAALAIRN-RMTVQELADQLFPYLTMVE 540
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
2-449 |
4.55e-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: 185.44 E-value: 4.55e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 2 KYDILVLGSGPGGYVTAIRASQLGMKVAIVE---------REALGGICLNWGCIPTKALLKSANVFEYIEHAGDYGINVA 72
Cdd:TIGR01438 2 DYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDfvtptplgtRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 73 KP-KVDFTGMVSRSRGVANGMSKGVQFLMKKNKIDVIMGNGKLMPGRKVEVTDADGGQQMVEADHIIIATGARSRqLPNL 151
Cdd:TIGR01438 82 ETvKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERPR-YPGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 152 PQDGKKIMGYREAMTMEKQPKKLVVVGSGAIGVEFAYFYNAIGTNVTIveyMPNIVPVE--DEEVSKQLARSFKKSGIHI 229
Cdd:TIGR01438 161 PGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTV---MVRSILLRgfDQDCANKVGEHMEEHGVKF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 230 MTSSEVTGVDTSGKGCKVHVKTKKGEEVLDADVVLSAVGVVSNIDGIGLEEVGIAADR--GKLIVDDFYKTNIPGYYAIG 307
Cdd:TIGR01438 238 KRQFVPIKVEQIEAKVLVEFTDSTNGIEEEYDTVLLAIGRDACTRKLNLENVGVKINKktGKIPADEEEQTNVPYIYAVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 308 DCVPG-PALAHVASAEGILCVEKIAGHNVEPLDYGNIPGCTYCFPEVASVGKTEEDC----KKEGIDIKVGKF-PFSASg 381
Cdd:TIGR01438 318 DILEDkPELTPVAIQAGRLLAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAvekfGEENVEVFHSYFwPLEWT- 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1519712285 382 KASAAGHKDGFVKLIFDAKYGE-LLGGHMIGANVTEMIAEIVAIRKLETTGHEMIKTVHPHPTLSEAVM 449
Cdd:TIGR01438 397 IPSRDNHNKCYAKLVCNKKENErVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFT 465
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
2-448 |
1.86e-48 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 172.12 E-value: 1.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 2 KYDILVLGSGPGGYVTAIRASQLGMKVAIVEREA--LGGICLNWGCIPTKALlksanvfeyiehagdygINVAKPKVDFT 79
Cdd:PRK08010 3 KYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNamYGGTCINIGCIPTKTL-----------------VHDAQQHTDFV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 80 GMVSRSRGVANGM-SKGVQFLMKKNKIDVIMGNGKLMPGRKVEVTDADGgQQMVEADHIIIATGARSrQLPNLP--QDGK 156
Cdd:PRK08010 66 RAIQRKNEVVNFLrNKNFHNLADMPNIDVIDGQAEFINNHSLRVHRPEG-NLEIHGEKIFINTGAQT-VVPPIPgiTTTP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 157 KIMGYREAMTMEKQPKKLVVVGSGAIGVEFAYFYNAIGTNVTIVEYMPNIVPVEDEEVSKQLARSFKKSGIHIMTSSEVT 236
Cdd:PRK08010 144 GVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 237 GVdtSGKGCKVHVKTKKGEEVLDAdvVLSAVGVVSNIDGIGLEEVGIAA-DRGKLIVDDFYKTNIPGYYAIGDCVPGPAL 315
Cdd:PRK08010 224 RI--SHHENQVQVHSEHAQLAVDA--LLIASGRQPATASLHPENAGIAVnERGAIVVDKYLHTTADNIWAMGDVTGGLQF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 316 AHVASAEGILCVEKIAGHNVEPL-DYGNIPGCTYCFPEVASVGKTEEDCKKEGIDIKVGKFPFSASGKASAAGHKDGFVK 394
Cdd:PRK08010 300 TYISLDDYRIVRDELLGEGKRSTdDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDTRGVLK 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1519712285 395 LIFDAKYGELLGGHMIGANVTEMIAEIVAIRKLETTGHEMIKTVHPHPTLSEAV 448
Cdd:PRK08010 380 AIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESL 433
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
1-449 |
2.72e-47 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 171.34 E-value: 2.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 1 MKYDILVLGSGPGGYVTAIRASQLGMKVAIVEREALGGICLNWGCIPTKALLKSANVFEYIEHAGDYGINVAKpKVDFTG 80
Cdd:PTZ00058 47 MVYDLIVIGGGSGGMAAARRAARNKAKVALVEKDYLGGTCVNVGCVPKKIMFNAASIHDILENSRHYGFDTQF-SFNLPL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 81 MVSRSRGVANGMSKGVQFLMKKNKIDVIMGNGKLMPGRKV------------------------EVTDADGGQQMVEADH 136
Cdd:PTZ00058 126 LVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVlikkvsqvdgeadesdddevtivsAGVSQLDDGQVIEGKN 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 137 IIIATGARsrqlPNLPQ-DGKKIMGYREAMTMEKQPKKLVVVGSGAIGVEFAYFYNAIGTNVTIVEYMPNIVPVEDEEVS 215
Cdd:PTZ00058 206 ILIAVGNK----PIFPDvKGKEFTISSDDFFKIKEAKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLRKFDETII 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 216 KQLARSFKKSGIHIMTSSEVTGVD-TSGKGCKVHVKTKKGEEvlDADVVLSAVGVVSNIDGIGLEEVGIAADRGKLIVDD 294
Cdd:PTZ00058 282 NELENDMKKNNINIITHANVEEIEkVKEKNLTIYLSDGRKYE--HFDYVIYCVGRSPNTEDLNLKALNIKTPKGYIKVDD 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 295 FYKTNIPGYYAIGDCVPGPA----------------------------------LAHVASAEGILCVEKIAGHNVEPLDY 340
Cdd:PTZ00058 360 NQRTSVKHIYAVGDCCMVKKnqeiedlnllklyneepylkkkentsgesyynvqLTPVAINAGRLLADRLFGPFSRTTNY 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 341 GNIPGCTYCFPEVASVGKTEEDC----KKEGIDIKVGKFP--FSASGKASAAGHKDGFVKLIFDAKYGELLGGHMIGANV 414
Cdd:PTZ00058 440 KLIPSVIFSHPPIGTIGLSEQEAidiyGKENVKIYESRFTnlFFSVYDMDPAQKEKTYLKLVCVGKEELIKGLHIVGLNA 519
|
490 500 510
....*....|....*....|....*....|....*
gi 1519712285 415 TEMIAEIVAIRKLETTGHEMIKTVHPHPTLSEAVM 449
Cdd:PTZ00058 520 DEILQGFAVALKMNATKADFDETIPIHPTAAEEFV 554
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
3-446 |
6.25e-45 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 164.66 E-value: 6.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 3 YDILVLGSGPGGyVTAIR-ASQLGMKVAIVE-------REALGGI---CLNWGCIPTKALLKSANVFEYIEHAGDYG-IN 70
Cdd:PLN02546 80 FDLFTIGAGSGG-VRASRfASNFGASAAVCElpfatisSDTLGGVggtCVLRGCVPKKLLVYASKYSHEFEESRGFGwKY 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 71 VAKPKVDFTGMVSRSRGVANGMSKGVQFLMKKNKIDVIMGNGKLMPGRKVEVtdaDGgqQMVEADHIIIATGARSrQLPN 150
Cdd:PLN02546 159 ETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDV---DG--KLYTARNILIAVGGRP-FIPD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 151 LPqdGKK-IMGYREAMTMEKQPKKLVVVGSGAIGVEFAYFYNAIGTNVTIVEYMPNIVPVEDEEVSKQLARSFKKSGIHI 229
Cdd:PLN02546 233 IP--GIEhAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKKVLRGFDEEVRDFVAEQMSLRGIEF 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 230 MTSSEVTGVDTSGKGcKVHVKTKKGEeVLDADVVLSAVGVVSNIDGIGLEEVGIAADR-GKLIVDDFYKTNIPGYYAIGD 308
Cdd:PLN02546 311 HTEESPQAIIKSADG-SLSLKTNKGT-VEGFSHVMFATGRKPNTKNLGLEEVGVKMDKnGAIEVDEYSRTSVPSIWAVGD 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 309 CVPGPALAHVASAEGILCVEKIAGHNVEPLDYGNIPGCTYCFPEVASVGKTEEDCKKEGIDIKVGKFPFSASgKASAAGH 388
Cdd:PLN02546 389 VTDRINLTPVALMEGGALAKTLFGNEPTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYGDVDVFTANFRPL-KATLSGL 467
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1519712285 389 KDG-FVKLIFDAKYGELLGGHMIGANVTEMIAEIVAIRKLETTGHEMIKTVHPHPTLSE 446
Cdd:PLN02546 468 PDRvFMKLIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAE 526
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
343-450 |
9.37e-42 |
|
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: 143.85 E-value: 9.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 343 IPGCTYCFPEVASVGKTEEDCKKEGIDIKVGKFPFSASGKASAAGHKDGFVKLIFDAKYGELLGGHMIGANVTEMIAEIV 422
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGEVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQEAA 80
|
90 100
....*....|....*....|....*...
gi 1519712285 423 AIRKLETTGHEMIKTVHPHPTLSEAVME 450
Cdd:pfam02852 81 LAIKMGATVEDLANTIHIHPTLSEALVE 108
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
113-362 |
2.69e-36 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 137.97 E-value: 2.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 113 KLMPGRKVE--------VTDADGGQqmVEADHIIIATGARSRQLPNLPQDGKKIMGYReamTME---------KQPKKLV 175
Cdd:COG1251 72 DLRLGTRVTaidraartVTLADGET--LPYDKLVLATGSRPRVPPIPGADLPGVFTLR---TLDdadalraalAPGKRVV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 176 VVGSGAIGVEFAYFYNAIGTNVTIVEYMPNIVP-VEDEEVSKQLARSFKKSGIHIMTSSEVTGVDTSGKGCKVHvkTKKG 254
Cdd:COG1251 147 VIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPrQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVR--LADG 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 255 EEvLDADVVLSAVGVVSNIDgiGLEEVGIAADRGkLIVDDFYKTNIPGYYAIGDC--VPGP-----ALAHVASAE--GIL 325
Cdd:COG1251 225 EE-LPADLVVVAIGVRPNTE--LARAAGLAVDRG-IVVDDYLRTSDPDIYAAGDCaeHPGPvygrrVLELVAPAYeqARV 300
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1519712285 326 CVEKIAGHNVE-----PLDYGNIPGCtycfpEVASVGKTEED 362
Cdd:COG1251 301 AAANLAGGPAAyegsvPSTKLKVFGV-----DVASAGDAEGD 337
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
97-341 |
4.38e-36 |
|
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: 135.71 E-value: 4.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 97 QFLMKKNkIDVIMGngklmpgrkVEVTDADGGQQMVEA--------DHIIIATGARSRQLP----NLP--------QDGK 156
Cdd:COG0446 44 ESFERKG-IDVRTG---------TEVTAIDPEAKTVTLrdgetlsyDKLVLATGARPRPPPipglDLPgvftlrtlDDAD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 157 KImgyREAMTmEKQPKKLVVVGSGAIGVEFAYFYNAIGTNVTIVEYMPNIVPVEDEEVSKQLARSFKKSGIHIMTSSEVT 236
Cdd:COG0446 114 AL---REALK-EFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 237 GVDTSGkgcKVHVKTKKGEEvLDADVVLSAVGVVSNIDgIgLEEVGIAAD-RGKLIVDDFYKTNIPGYYAIGDC--VPGP 313
Cdd:COG0446 190 AIDGDD---KVAVTLTDGEE-IPADLVVVAPGVRPNTE-L-AKDAGLALGeRGWIKVDETLQTSDPDVYAAGDCaeVPHP 263
|
250 260 270
....*....|....*....|....*....|....*.
gi 1519712285 314 --------ALAHVASAEGILCVEKIAGHNVEPLDYG 341
Cdd:COG0446 264 vtgktvyiPLASAANKQGRVAAENILGGPAPFPGLG 299
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
3-449 |
6.96e-34 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 133.03 E-value: 6.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 3 YDILVLGSGPGGYVTAIRASQLGMKVAIVE---------REALGGICLNWGCIPTKALLKSANVFEYIEH-AGDYGINVa 72
Cdd:PTZ00052 6 YDLVVIGGGSGGMAAAKEAAAHGKKVALFDyvkpstqgtKWGLGGTCVNVGCVPKKLMHYAANIGSIFHHdSQMYGWKT- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 73 KPKVDFTGMVSRSRGVANGMSKGVQFLMKKNKIDVIMGNGKLMPGRKVEVTDaDGGQQMVEADHIIIATGARsrqlPNLP 152
Cdd:PTZ00052 85 SSSFNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTVSYGD-NSQEETITAKYILIATGGR----PSIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 153 QDgkkIMGYRE-------AMTMEKQPKKLVVVGSGAIGVEFAYFYNAIGTNVTIVeyMPNIVPVE-DEEVSKQLARSFKK 224
Cdd:PTZ00052 160 ED---VPGAKEysitsddIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVA--VRSIPLRGfDRQCSEKVVEYMKE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 225 SGIHIMTSSEVTGVDTSGKGCKVHVKTKKGEEVldaDVVLSAVGVVSNIDGIGLEEVGIAADRGKLIVDDFYKTNIPGYY 304
Cdd:PTZ00052 235 QGTLFLEGVVPINIEKMDDKIKVLFSDGTTELF---DTVLYATGRKPDIKGLNLNAIGVHVNKSNKIIAPNDCTNIPNIF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 305 AIGDCVPG-PALAHVASAEGILCVEKIAGHNVEPLDYGNIPGCTYCFPEVASVGKTEEDCKKEGIDIKVGKFPFSASGKA 383
Cdd:PTZ00052 312 AVGDVVEGrPELTPVAIKAGILLARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQEFNTLE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 384 SAAGHKDG-----------------FVKLIFDAKYGE-LLGGHMIGANVTEMIAEIVAIRKLETTGHEMIKTVHPHPTLS 445
Cdd:PTZ00052 392 IAAVHREKherarkdeydfdvssncLAKLVCVKSEDNkVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHPTDA 471
|
....
gi 1519712285 446 EAVM 449
Cdd:PTZ00052 472 EVFM 475
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
3-336 |
3.16e-30 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 119.07 E-value: 3.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 3 YDILVLGSGPGGYVTAIRASQLGMKVAIVEREALGGICLNWGCIptkallksANVF---------EYI----EHAGDYGI 69
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQLATTKEI--------ENYPgfpegisgpELAerlrEQAERFGA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 70 NVakpkvdFTGMVsrsrgvangmskgvqflmkkNKIDVImgngklmpGRKVEVTDADGGqqMVEADHIIIATGARSRQLP 149
Cdd:COG0492 73 EI------LLEEV--------------------TSVDKD--------DGPFRVTTDDGT--EYEAKAVIIATGAGPRKLG 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 150 nlpqdgkkIMGYREAM-----------TMEKQPKKLVVVGSGAIGVEFAYFYNAIGTNVTIveympnIVPVEDEEVSKQL 218
Cdd:COG0492 117 --------LPGEEEFEgrgvsycatcdGFFFRGKDVVVVGGGDSALEEALYLTKFASKVTL------IHRRDELRASKIL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 219 A-RSFKKSGIHIMTSSEVTGVDTSGKGCKVHVKTKKG--EEVLDADVVLSAVGVVSN---IDGIGLEevgiAADRGKLIV 292
Cdd:COG0492 183 VeRLRANPKIEVLWNTEVTEIEGDGRVEGVTLKNVKTgeEKELEVDGVFVAIGLKPNtelLKGLGLE----LDEDGYIVV 258
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1519712285 293 DDFYKTNIPGYYAIGDCVPGP-ALAHVASAEGIlcvekIAGHNVE 336
Cdd:COG0492 259 DEDMETSVPGVFAAGDVRDYKyRQAATAAGEGA-----IAALSAA 298
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
118-430 |
5.57e-27 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 112.44 E-value: 5.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 118 RKVEVTDADGGQQMVEA-DHIIIATGARSrQLPNLP-------------QDGKKImgyREAMtMEKQPKKLVVVGSGAIG 183
Cdd:PRK09564 87 KTITVKNLKTGSIFNDTyDKLMIATGARP-IIPPIKninlenvytlksmEDGLAL---KELL-KDEEIKNIVIIGAGFIG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 184 VEFAYFYNAIGTNVTIVEYMPNIVP-VEDEEVSKQLARSFKKSGIHIMTSSEVTGVDTSGKGCKvhVKTKKGEevLDADV 262
Cdd:PRK09564 162 LEAVEAAKHLGKNVRIIQLEDRILPdSFDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEG--VVTDKGE--YEADV 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 263 VLSAVGVVSNIDgiGLEEVGI-AADRGKLIVDDFYKTNIPGYYAIGDC------VPGP----ALAHVASAEGILCVEKIA 331
Cdd:PRK09564 238 VIVATGVKPNTE--FLEDTGLkTLKNGAIIVDEYGETSIENIYAAGDCatiyniVSNKnvyvPLATTANKLGRMVGENLA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 332 GHNVEpldygnIPG-----CTYCFP-EVASVGKTEEDCKKEGIDIKVgKFPFSASGKASAAGHKDGFVKLIFDAKYGELL 405
Cdd:PRK09564 316 GRHVS------FKGtlgsaCIKVLDlEAARTGLTEEEAKKLGIDYKT-VFIKDKNHTNYYPGQEDLYVKLIYEADTKVIL 388
|
330 340
....*....|....*....|....*..
gi 1519712285 406 GGHMIGAN--VTEMIAEIVAIRKLETT 430
Cdd:PRK09564 389 GGQIIGKKgaVLRIDALAVAIYAKLTT 415
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
122-309 |
2.34e-22 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 98.07 E-value: 2.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 122 VTDADGGQQMVEA-------DHIIIATGARSRqLPNLPQDGKKI-----MGYREAMTMEKQPKKLVVVGSGAIGVEFAYF 189
Cdd:PRK04965 81 VTDIDAEAQVVKSqgnqwqyDKLVLATGASAF-VPPIPGRELMLtlnsqQEYRAAETQLRDAQRVLVVGGGLIGTELAMD 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 190 YNAIGTNVTIVE----YMPNIVPvedEEVSKQLARSFKKSGIHIMTSSEVTGVDTSGKGckVHVKTKKGEEvLDADVVLS 265
Cdd:PRK04965 160 LCRAGKAVTLVDnaasLLASLMP---PEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSG--IRATLDSGRS-IEVDAVIA 233
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1519712285 266 AVGVVSNidgIGL-EEVGIAADRGkLIVDDFYKTNIPGYYAIGDC 309
Cdd:PRK04965 234 AAGLRPN---TALaRRAGLAVNRG-IVVDSYLQTSAPDIYALGDC 274
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
99-359 |
2.06e-21 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 95.58 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 99 LMKKNKIDVIMGN-GKLMPGRKVeVTDADGGQqmVEADHIIIATGARSRqLPNLPQDGKKIMGYR---EAMTM------- 167
Cdd:COG1252 65 LLRRAGVRFIQGEvTGIDPEART-VTLADGRT--LSYDYLVIATGSVTN-FFGIPGLAEHALPLKtleDALALrerllaa 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 168 -----EKQPKKLVVVGSGAIGVEFA----------YFYNAIGT---NVTIVEYMPNIVPVEDEEVSKQLARSFKKSGIHI 229
Cdd:COG1252 141 feraeRRRLLTIVVVGGGPTGVELAgelaellrklLRYPGIDPdkvRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEV 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 230 MTSSEVTGVDTSGkgckvhVKTKKGEEvLDADVVLSAVGVVSN--IDGIGLEevgiAADRGKLIVDDFYKTniPGY---Y 304
Cdd:COG1252 221 HTGTRVTEVDADG------VTLEDGEE-IPADTVIWAAGVKAPplLADLGLP----TDRRGRVLVDPTLQV--PGHpnvF 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1519712285 305 AIGDC--VPG------PALAHVASAEGILCVE----KIAGHNVEPLDYGNIpGCtycfpeVASVGKT 359
Cdd:COG1252 288 AIGDCaaVPDpdgkpvPKTAQAAVQQAKVLAKniaaLLRGKPLKPFRYRDK-GC------LASLGRG 347
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
119-309 |
1.20e-19 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 92.20 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 119 KVEVTDADggqQMVEADHIIIATGARSRQLPNLPQDGKKIMGYRE------AMTMEKQPKKLVVVGSGAIGVEFAYFYNA 192
Cdd:TIGR02374 85 KQVITDAG---RTLSYDKLILATGSYPFILPIPGADKKGVYVFRTiedldaIMAMAQRFKKAAVIGGGLLGLEAAVGLQN 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 193 IGTNVTIVEYMPNIVPVE-DEEVSKQLARSFKKSGIHIMTSSEVtgVDTSGKGCKVHVKTKKGEEvLDADVVLSAVGVVS 271
Cdd:TIGR02374 162 LGMDVSVIHHAPGLMAKQlDQTAGRLLQRELEQKGLTFLLEKDT--VEIVGATKADRIRFKDGSS-LEADLIVMAAGIRP 238
|
170 180 190
....*....|....*....|....*....|....*...
gi 1519712285 272 NIDgIGLEeVGIAADRGkLIVDDFYKTNIPGYYAIGDC 309
Cdd:TIGR02374 239 NDE-LAVS-AGIKVNRG-IIVNDSMQTSDPDIYAVGEC 273
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
173-250 |
5.03e-19 |
|
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: 81.10 E-value: 5.03e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1519712285 173 KLVVVGSGAIGVEFAYFYNAIGTNVTIVEYMPNIVPVEDEEVSKQLARSFKKSGIHIMTSSEVTGVDTSGKGCKVHVK 250
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLT 78
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
102-308 |
6.64e-15 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 76.12 E-value: 6.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 102 KNKIDVIMGN--GKLMPGRKvEVTDADGGQqmVEADHIIIATGARSRQLPNLPQDGKKIMGYREAMTME------KQPKK 173
Cdd:PRK09754 70 ENNVHLHSGVtiKTLGRDTR-ELVLTNGES--WHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAArlrevlQPERS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 174 LVVVGSGAIGVEFAYFYNAIGTNVTIVEYMPNIV------PVEDeevskQLARSFKKSGIHIMTSsevTGVDTSGKGCKV 247
Cdd:PRK09754 147 VVIVGAGTIGLELAASATQRRCKVTVIELAATVMgrnappPVQR-----YLLQRHQQAGVRILLN---NAIEHVVDGEKV 218
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519712285 248 HVKTKKGEEVLdADVVLSAVGVVSNiDGIGLeEVGIAADRGkLIVDDFYKTNIPGYYAIGD 308
Cdd:PRK09754 219 ELTLQSGETLQ-ADVVIYGIGISAN-DQLAR-EANLDTANG-IVIDEACRTCDPAIFAGGD 275
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
118-310 |
3.20e-13 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 71.35 E-value: 3.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 118 RKVEVTDADGGQQMVEA-DHIIIATGARSRQLP----------NLpQDGKKIMGYREAMtmekQPKKLVVVGSGAIGVEF 186
Cdd:PRK13512 89 QTVTVLNRKTNEQFEESyDKLILSPGASANSLGfesditftlrNL-EDTDAIDQFIKAN----QVDKALVVGAGYISLEV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 187 AYFYNAIGTNVTIVEYMPNIVPVEDEEVSKQLARSFKKSGIHIMTSSEVTGVDtsgkGCKVHVKTKKGEevlDADVVLSA 266
Cdd:PRK13512 164 LENLYERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDAIN----GNEVTFKSGKVE---HYDMIIEG 236
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1519712285 267 VGVVSN---IDGIGLEEvgiaADRGKLIVDDFYKTNIPGYYAIGDCV 310
Cdd:PRK13512 237 VGTHPNskfIESSNIKL----DDKGFIPVNDKFETNVPNIYAIGDII 279
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
135-330 |
1.09e-12 |
|
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 440259 [Multi-domain] Cd Length: 434 Bit Score: 69.39 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 135 DHIIIATGA-RSRQLP----NLPqdgkkimGYREAM-------------TMEKQPKKLVVVGSGAIGVefayfyNAIGT- 195
Cdd:COG0493 208 DAVFLATGAgKPRDLGipgeDLK-------GVHSAMdfltavnlgeapdTILAVGKRVVVIGGGNTAM------DCARTa 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 196 ------NVTIVEYMP-NIVPVEDEEVSKqlArsfKKSGIHIMTSS---EVTGvDTSGKGCKVH-VKTKKG---------- 254
Cdd:COG0493 275 lrlgaeSVTIVYRRTrEEMPASKEEVEE--A---LEEGVEFLFLVapvEIIG-DENGRVTGLEcVRMELGepdesgrrrp 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 255 ------EEVLDADVVLSAVGVVSNIDGIgLEEVGIAAD-RGKLIVDDF-YKTNIPGYYAIGDCVPGPALAHVASAEGILC 326
Cdd:COG0493 349 vpiegsEFTLPADLVILAIGQTPDPSGL-EEELGLELDkRGTIVVDEEtYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKA 427
|
....
gi 1519712285 327 VEKI 330
Cdd:COG0493 428 ARAI 431
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
175-332 |
5.44e-11 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 64.40 E-value: 5.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 175 VVVGSGAIGVEFAY----FYNAIGTN----------VTIVEYMPNIVPVEDEEVSKQLARSFKKSGIHIMTSSEVTGVDt 240
Cdd:PTZ00318 177 VVVGGGPTGVEFAAeladFFRDDVRNlnpelveeckVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEVL- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 241 sgkgcKVHVKTKKGEEVLDADVVLSAvgvvsnidGIGLEEVGIAAD-----RGKLIVDDFYKT-NIPGYYAIGDC----- 309
Cdd:PTZ00318 256 -----DKEVVLKDGEVIPTGLVVWST--------GVGPGPLTKQLKvdktsRGRISVDDHLRVkPIPNVFALGDCaanee 322
|
170 180
....*....|....*....|...
gi 1519712285 310 VPGPALAHVASAEGILCVEKIAG 332
Cdd:PTZ00318 323 RPLPTLAQVASQQGVYLAKEFNN 345
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
135-330 |
1.14e-10 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 63.26 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 135 DHIIIATGARS--------RQLPN-------LPQDGKKIMGYREAMTMEKQPKKLVVVGSGAIGVEfayfynAIGT---- 195
Cdd:PRK12810 230 DAVFLGTGAYKprdlgipgRDLDGvhfamdfLIQNTRRVLGDETEPFISAKGKHVVVIGGGDTGMD------CVGTairq 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 196 ---NVTIVEYMPniVPVEDEE---VSKQLARSFKKSGIH---------IMTSsEVTGVDtsGKGCKVH-VKTKKG----- 254
Cdd:PRK12810 304 gakSVTQRDIMP--MPPSRRNknnPWPYWPMKLEVSNAHeegverefnVQTK-EFEGEN--GKVTGVKvVRTELGegdfe 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 255 -----EEVLDADVVLSAVGVVSNIDGIgLEEVGIAAD-RGKLIVDDF-YKTNIPGYYAIGDCVPGPALAHVASAEGILCV 327
Cdd:PRK12810 379 pvegsEFVLPADLVLLAMGFTGPEAGL-LAQFGVELDeRGRVAAPDNaYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAA 457
|
...
gi 1519712285 328 EKI 330
Cdd:PRK12810 458 RAI 460
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
226-335 |
3.26e-10 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 62.20 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 226 GIHIMTSSEVTGVDTSGKGC------KVHVKTK----------KGEEVLDADVVLSAVGvvSNIDGIGLEEV-GIAADRG 288
Cdd:PRK12771 319 GVEINWLRTPVEIEGDENGAtglrviTVEKMELdedgrpspvtGEEETLEADLVVLAIG--QDIDSAGLESVpGVEVGRG 396
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1519712285 289 KLIVDDFYK-TNIPGYYAIGDCVPGPALAHVASAEGilcveKIAGHNV 335
Cdd:PRK12771 397 VVQVDPNFMmTGRPGVFAGGDMVPGPRTVTTAIGHG-----KKAARNI 439
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
102-319 |
7.02e-09 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 58.21 E-value: 7.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 102 KNKIDVIMGNGKLMPGRKVEVTDADGGQQmVEADHIIIATGARSRQLPNLPQDGKKIMGYReamTME---------KQPK 172
Cdd:PRK14989 71 KHGIKVLVGERAITINRQEKVIHSSAGRT-VFYDKLIMATGSYPWIPPIKGSETQDCFVYR---TIEdlnaieacaRRSK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 173 KLVVVGSGAIGVEFAYFYNAIGTNVTIVEYMPNIVPVE-DEEVSKQLARSFKKSGIHIMTSSEVTGVDTSGKGCKVHVKT 251
Cdd:PRK14989 147 RGAVVGGGLLGLEAAGALKNLGVETHVIEFAPMLMAEQlDQMGGEQLRRKIESMGVRVHTSKNTLEIVQEGVEARKTMRF 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 252 KKGEEvLDADVVLSAVGVVSNiDGIGlEEVGIA-ADRGKLIVDDFYKTNIPGYYAIGDC-----------VPGPALAHVA 319
Cdd:PRK14989 227 ADGSE-LEVDFIVFSTGIRPQ-DKLA-TQCGLAvAPRGGIVINDSCQTSDPDIYAIGECaswnnrvfglvAPGYKMAQVA 303
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
3-311 |
3.77e-08 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 55.55 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 3 YDILVLGSGPGGYVTAIRASQLGMKVAIV-EReaLGGICL------NWGCIPTKALLKSANVFEyiEHAGDYGINVakpk 75
Cdd:PRK15317 212 YDVLVVGGGPAGAAAAIYAARKGIRTGIVaER--FGGQVLdtmgieNFISVPETEGPKLAAALE--EHVKEYDVDI---- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 76 vdftgmvsrsrgvangmskgvqflMKKNKIDVIMGNGKLmpgrkVEVTDADGGQqmVEADHIIIATGARSRQLpNLPQ-- 153
Cdd:PRK15317 284 ------------------------MNLQRASKLEPAAGL-----IEVELANGAV--LKAKTVILATGARWRNM-NVPGed 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 154 -------------DGKKIMGyreamtmekqpKKLVVVGSGAIGVEFAYFYNAIGTNVTIVEYMPNIvpvEDEEVSKQLAR 220
Cdd:PRK15317 332 eyrnkgvaycphcDGPLFKG-----------KRVAVIGGGNSGVEAAIDLAGIVKHVTVLEFAPEL---KADQVLQDKLR 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 221 SFKKsgIHIMTSSEVTGVdtSGKGCKV---HVKTKKGEEV--LDADVVLSAVGVVSNIDGigLEEVGIAADRGKLIVDDF 295
Cdd:PRK15317 398 SLPN--VTIITNAQTTEV--TGDGDKVtglTYKDRTTGEEhhLELEGVFVQIGLVPNTEW--LKGTVELNRRGEIIVDAR 471
|
330
....*....|....*...
gi 1519712285 296 YKTNIPGYYAIGDC--VP 311
Cdd:PRK15317 472 GATSVPGVFAAGDCttVP 489
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
1-142 |
4.18e-08 |
|
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: 55.22 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 1 MKYDILVLGSGPGGYVTAIRASQLGMKVAIVEREAL---------GGIclnwgCIPTKALLKSANV------FEYIEHAG 65
Cdd:COG1053 2 HEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPrgghtaaaqGGI-----NAAGTNVQKAAGEdspeehFYDTVKGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 66 DYGIN---------------------------VAKPKVDFTGMVSRSRGVANGMSKGVQFL------MKKNKIDV----- 107
Cdd:COG1053 77 DGLADqdlvealaeeapeaidwleaqgvpfsrTPDGRLPQFGGHSVGRTCYAGDGTGHALLatlyqaALRLGVEIftete 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 1519712285 108 ----IMGNGKLmpgRKVEVTDADGGQQMVEADHIIIATG 142
Cdd:COG1053 157 vldlIVDDGRV---VGVVARDRTGEIVRIRAKAVVLATG 192
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
11-146 |
2.24e-07 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 52.28 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 11 GPGGYVTAIRASQLGMKVAIVEREALGGICLNWGCIPTKAL--LKSANVFEYIEHA--GDYGINVAKPKVDFTG------ 80
Cdd:COG0644 2 GPAGSAAARRLARAGLSVLLLEKGSFPGDKICGGGLLPRALeeLEPLGLDEPLERPvrGARFYSPGGKSVELPPgrgggy 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519712285 81 MVSRS------RGVAngMSKGVQFLMKKNKIDVIMGNGklmpgrKVEVTDADGGQqmVEADHIIIATGARSR 146
Cdd:COG0644 82 VVDRArfdrwlAEQA--EEAGAEVRTGTRVTDVLRDDG------RVVVRTGDGEE--IRADYVVDADGARSL 143
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
7-324 |
7.38e-07 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 51.69 E-value: 7.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 7 VLGSGPGGYVTAIRASQLGMKVAIVEREALGGICLNWGC----IPTKALLKSANVFEYIehagdyGINVakpkvdFTGMv 82
Cdd:PRK13984 288 IVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGVMRYGIpsyrLPDEALDKDIAFIEAL------GVKI------HLNT- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 83 srsrgvanGMSKGVQFLMKKNKIDVIMGNGKLMPGRKVEVTDADGgQQMVEADHIIiatgarsRQLPN-LPQDGKKImgy 161
Cdd:PRK13984 355 --------RVGKDIPLEELREKHDAVFLSTGFTLGRSTRIPGTDH-PDVIQALPLL-------REIRDyLRGEGPKP--- 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 162 reamtmeKQPKKLVVVGSGAIGVEFAYF--------YNAIGTNVTIVEYMPNIVPVEDEEVskqlaRSFKKSGIHIMTS- 232
Cdd:PRK13984 416 -------KIPRSLVVIGGGNVAMDIARSmarlqkmeYGEVNVKVTSLERTFEEMPADMEEI-----EEGLEEGVVIYPGw 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 233 --SEVTGVDTSGKGckvhVKTKKGEEVLD------------------ADVVLSAVGVVSNIDGIGlEEV--GIAADRGKL 290
Cdd:PRK13984 484 gpMEVVIENDKVKG----VKFKKCVEVFDeegrfnpkfdesdqiiveADMVVEAIGQAPDYSYLP-EELksKLEFVRGRI 558
|
330 340 350
....*....|....*....|....*....|....*....
gi 1519712285 291 IVDDFYKTNIPGYYAIGDCVPGPALAH-VA----SAEGI 324
Cdd:PRK13984 559 LTNEYGQTSIPWLFAGGDIVHGPDIIHgVAdgywAAEGI 597
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
3-274 |
3.19e-06 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 49.44 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 3 YDILVLGSGPGGYVTAIRASQLGMKVAIVER-EALGGICL---NWGCIPTKALLKSANVFE-------YIEHAgdYGINV 71
Cdd:PRK12839 9 YDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKaSTCGGATAwsgGWMWTPGNSLARADGVVEdkeeprtYLEHR--LGENY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 72 AKPKVDftgmvsrsrGVANGMSKGVQFLMKKNKIdvimgngKLMPGRKVevtdADggqqmVEADHIIIATGARSrqLPNL 151
Cdd:PRK12839 87 DADKVD---------ALLDGAPEMVDFFEKKTAL-------QFVPGAKI----AD-----IYGDLPGAGTGHRS--VGPK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 152 PQDGKKImGYREAMTMEKQPKKLVVVGSGAI-GVEFAYFYNA-------------IGTNV-TIVEYMPNIVPVEDEEVSK 216
Cdd:PRK12839 140 PVNLRKL-GPDVAALLRHQLYETSFLGMGIMaGPDLQAFLHAtqdpkgfvhaarrVIVHMwDLATHRRGMQLVNGTALTG 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519712285 217 QLARSFKKSGIHIMTSSEVTGV--DTSGKGCKVHVKTKKGEEVLDA--DVVLSAVGVVSNID 274
Cdd:PRK12839 219 RLLRSADDLGVDLRVSTSATSLttDKNGRVTGVRVQGPDGAVTVEAtrGVVLATGGFPNDVD 280
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
1-38 |
4.55e-06 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 49.08 E-value: 4.55e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1519712285 1 MKYDILVLGSGPGGYVTAIRASQLGMKVAIVEREA-LGG 38
Cdd:COG1233 2 MMYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDtPGG 40
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
172-315 |
5.63e-06 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 48.64 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 172 KKLVVVGSG--AI---------GVEfayfynaigtNVTIV-----EYMPnivpVEDEEVskQLArsfKKSGIHIMTSS-- 233
Cdd:PRK11749 274 KRVVVIGGGntAMdaartakrlGAE----------SVTIVyrrgrEEMP----ASEEEV--EHA---KEEGVEFEWLAap 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 234 -EVTGVDTSGKGCKVhVKTKKGEE---------------VLDADVVLSAVG------VVSNIDGIGLEEvgiaadRGKLI 291
Cdd:PRK11749 335 vEILGDEGRVTGVEF-VRMELGEPdasgrrrvpiegsefTLPADLVIKAIGqtpnplILSTTPGLELNR------WGTII 407
|
170 180
....*....|....*....|....*
gi 1519712285 292 VDDF-YKTNIPGYYAIGDCVPGPAL 315
Cdd:PRK11749 408 ADDEtGRTSLPGVFAGGDIVTGAAT 432
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
133-331 |
8.34e-06 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 47.68 E-value: 8.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 133 EADHIIIATGA-RSRQLpNLPQDGKK-----------IMGYREA-MTMEKQP----KKLVVVGSGAIGVEFAYFYNAIGT 195
Cdd:PRK12770 118 KYDAVLIATGTwKSRKL-GIPGEDLPgvysaleylfrIRAAKLGyLPWEKVPpvegKKVVVVGAGLTAVDAALEAVLLGA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 196 -NVTI-----------------------VEYMPNIVPVE---DEEVSK-QLARSfkksgihimtssEVTGVDTSGKgcKV 247
Cdd:PRK12770 197 eKVYLayrrtineapagkyeierliargVEFLELVTPVRiigEGRVEGvELAKM------------RLGEPDESGR--PR 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 248 HVKTKKGEEVLDADVVLSAVGVVSNiDGIGLEEVGIAADR-GKLIVDDFYKTNIPGYYAIGDCVPGPALAHVASAEGILC 326
Cdd:PRK12770 263 PVPIPGSEFVLEADTVVFAIGEIPT-PPFAKECLGIELNRkGEIVVDEKHMTSREGVFAAGDVVTGPSKIGKAIKSGLRA 341
|
....*
gi 1519712285 327 VEKIA 331
Cdd:PRK12770 342 AQSIH 346
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
3-67 |
7.11e-05 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 45.10 E-value: 7.11e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1519712285 3 YDILVLGSGPGGYVTAIRASQLGMKVAIVEREA-LGGICL---NWGCIPTKALLKSANVFEYIEHAGDY 67
Cdd:PRK06134 13 CDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPvFGGTTAwsgGWMWIPRNPLARRAGIVEDIEQPRTY 81
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
132-307 |
1.09e-04 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 44.14 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 132 VEADHIIIATGarSRQLPNLPQDGKKIMGY---REAMTMEKQpkKLVVVGSGAIGVEFAYFYNAIGTNVTIVeYMPNIVP 208
Cdd:pfam13738 117 YQARYVIIATG--EFDFPNKLGVPELPKHYsyvKDFHPYAGQ--KVVVIGGYNSAVDAALELVRKGARVTVL-YRGSEWE 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 209 VEDEEVSK--------QLARSFKKSGIHIMTSSEVTGVDTSGKGckVHVKTKKGEEVLDADVVLSAVGVVSNIDgiGLEE 280
Cdd:pfam13738 192 DRDSDPSYslspdtlnRLEELVKNGKIKAHFNAEVKEITEVDVS--YKVHTEDGRKVTSNDDPILATGYHPDLS--FLKK 267
|
170 180
....*....|....*....|....*....
gi 1519712285 281 VGIAADRGKLIV--DDFYKTNIPGYYAIG 307
Cdd:pfam13738 268 GLFELDEDGRPVltEETESTNVPGLFLAG 296
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
4-43 |
1.17e-04 |
|
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: 44.20 E-value: 1.17e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1519712285 4 DILVLGSGPGGYVTAIRASQLGMKVAIVEREALGGICLNW 43
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGATAW 40
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
1-146 |
1.50e-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: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 1 MKYDILVLGSGPGGYVTAIRASQLGMKVAIVEREALG-----GICLN---------WGCIPtkALLKSANVFEYIE-HAG 65
Cdd:COG0654 2 MRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPrpdgrGIALSprslellrrLGLWD--RLLARGAPIRGIRvRDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 66 DYG-----INVAKPKVDFTGMVSRSRgVANGMSKGVQFLmkknKIDVIMGN---GKLMPGRKVEVTDADGgqQMVEADHI 137
Cdd:COG0654 80 SDGrvlarFDAAETGLPAGLVVPRAD-LERALLEAARAL----GVELRFGTevtGLEQDADGVTVTLADG--RTLRADLV 152
|
....*....
gi 1519712285 138 IIATGARSR 146
Cdd:COG0654 153 VGADGARSA 161
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
5-323 |
1.69e-04 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 43.96 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 5 ILVLGSGPGGYVTAIRASQLGMKVAIVEreAL---GGIcLNWGcIPTKALLKsanvfeyiehagdygiNVAKPKVDftgm 81
Cdd:PRK12778 434 VAVIGSGPAGLSFAGDLAKRGYDVTVFE--ALheiGGV-LKYG-IPEFRLPK----------------KIVDVEIE---- 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 82 vsrsrgvaNGMSKGVQFlmkknKIDVIMGNgklmpgrkvEVTDADGGQQMVEAdhIIIATGARSRQLPNLP-QDGKKIMG 160
Cdd:PRK12778 490 --------NLKKLGVKF-----ETDVIVGK---------TITIEELEEEGFKG--IFIASGAGLPNFMNIPgENSNGVMS 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 161 YREAMT----ME----------KQPKKLVVVGSGAIGVEFAYFYNAIGTNVTIVEYMPNIV--PVEDEEVskqlaRSFKK 224
Cdd:PRK12778 546 SNEYLTrvnlMDaaspdsdtpiKFGKKVAVVGGGNTAMDSARTAKRLGAERVTIVYRRSEEemPARLEEV-----KHAKE 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 225 SGIHIMT-----------SSEVTGV----------DTSGKGCKVHVKTKkgEEVLDADVVLSAVGVVSN------IDGIG 277
Cdd:PRK12778 621 EGIEFLTlhnpieyladeKGWVKQVvlqkmelgepDASGRRRPVAIPGS--TFTVDVDLVIVSVGVSPNplvpssIPGLE 698
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1519712285 278 LEEvgiaadRGKLIVDDFYKTNIPGYYAIGDCVPGPALAHVASAEG 323
Cdd:PRK12778 699 LNR------KGTIVVDEEMQSSIPGIYAGGDIVRGGATVILAMGDG 738
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
4-38 |
1.76e-04 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 43.75 E-value: 1.76e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1519712285 4 DILVLGSGPGGYVTAIRASQLGMKVAIVEREA-LGG 38
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRGfLGG 36
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
1-38 |
1.92e-04 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 43.91 E-value: 1.92e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1519712285 1 MKYDILVLGSGPGGYVTAIRASQLGMKVAIVEREA-LGG 38
Cdd:PRK12842 8 LTCDVLVIGSGAGGLSAAITARKLGLDVVVLEKEPvFGG 46
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
3-38 |
4.98e-04 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 42.42 E-value: 4.98e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1519712285 3 YDILVLGSGPGGYVTAIRASQLGMKVAIVER-EALGG 38
Cdd:PRK12843 17 FDVIVIGAGAAGMSAALFAAIAGLKVLLVERtEYVGG 53
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
1-31 |
5.64e-04 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 42.14 E-value: 5.64e-04
10 20 30
....*....|....*....|....*....|.
gi 1519712285 1 MKYDILVLGSGPGGYVTAIRASQLGMKVAIV 31
Cdd:PRK05329 1 MKFDVLVIGGGLAGLTAALAAAEAGKRVALV 31
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
258-331 |
6.78e-04 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 42.24 E-value: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 258 LDADVVLSAVGVVSN------IDGIGLEEVG-IAADRGKLivDDFYKTNIPGYYAIGDCVPGPALAHVASAEGILCVEKI 330
Cdd:PRK12775 673 LECDTVIYALGTKANpiitqsTPGLALNKWGnIAADDGKL--ESTQSTNLPGVFAGGDIVTGGATVILAMGAGRRAARSI 750
|
.
gi 1519712285 331 A 331
Cdd:PRK12775 751 A 751
|
|
| Lys_Orn_oxgnase |
pfam13434 |
L-lysine 6-monooxygenase/L-ornithine 5-monooxygenase; This is a family of Rossmann fold ... |
88-268 |
9.05e-04 |
|
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: 41.42 E-value: 9.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 88 VANGMSKGVQFLMKKNKIDVIMGNGKlmPGRKVEVTDADGGQQMVEADHIIIATGARsrqlPNLP---QDGKKIMGYREA 164
Cdd:pfam13434 104 AASHLPNRLRFGQEVESVEPDAERGE--PLLRVRVRDADGEETTFLARNLVLGTGGE----PYIPecaRGGERVFHSSEY 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 165 MTME---KQPKKLVVVGSGAIGVEFayFYNAIG----TNVTIVEYMPNIVPVED--------------------EEVSKQ 217
Cdd:pfam13434 178 LERIdrlAAKKRIAVVGSGQSAAEI--FRDLLRrgpaYELTWVTRSPNFFPLDDspfvneifspeyvdyfyslpEDTRRA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 218 LARSFKK---SGI-----------------------HIMTSSEVTGVDTSGKGcKVHVKT----KKGEEVLDADVVLSAV 267
Cdd:pfam13434 256 LLREQKGtnyDGIdpslieeiyrllyeqrvdgdprhRLLPNREVQSAERVGDG-GVELTLrdgeQGREETLETDVVVLAT 334
|
.
gi 1519712285 268 G 268
Cdd:pfam13434 335 G 335
|
|
| PRK09126 |
PRK09126 |
FAD-dependent hydroxylase; |
1-36 |
2.37e-03 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236385 [Multi-domain] Cd Length: 392 Bit Score: 39.92 E-value: 2.37e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1519712285 1 MKYDILVLGSGPGGYVTAIRASQLGMKVAIVEREAL 36
Cdd:PRK09126 2 MHSDIVVVGAGPAGLSFARSLAGSGLKVTLIERQPL 37
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
171-283 |
2.75e-03 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 39.73 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519712285 171 PKKLVVVGSGAIGVEFAY-FYNAIGTNVTIV--------EYMP-------NIVPVEDEEVSkqLARSFKKSGIHIMTsSE 234
Cdd:COG1252 1 MKRIVIVGGGFAGLEAARrLRKKLGGDAEVTlidpnpyhLFQPllpevaaGTLSPDDIAIP--LRELLRRAGVRFIQ-GE 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1519712285 235 VTGVDTSGKgckvHVKTKKGEEvLDADVVLSAVGVVSNIDGI-GLEEVGI 283
Cdd:COG1252 78 VTGIDPEAR----TVTLADGRT-LSYDYLVIATGSVTNFFGIpGLAEHAL 122
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
3-67 |
2.98e-03 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 40.02 E-value: 2.98e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1519712285 3 YDILVLGSGPGGYVTAIRASQLGMKVAIVEREAL---------GGIclnWgcIPTKALLKSANVFEYIEHAGDY 67
Cdd:PRK07843 8 YDVVVVGSGAAGMVAALTAAHRGLSTVVVEKAPHyggstarsgGGV---W--IPNNEVLKRAGVPDTPEAARTY 76
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
1-38 |
4.36e-03 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 39.12 E-value: 4.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1519712285 1 MKYDILVLGsgpGGYV---TAIRASQLGMKVAIVEREALGG 38
Cdd:COG0665 1 ATADVVVIG---GGIAglsTAYHLARRGLDVTVLERGRPGS 38
|
|
| LhgO |
COG0579 |
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism]; |
213-269 |
8.71e-03 |
|
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
Pssm-ID: 440344 [Multi-domain] Cd Length: 418 Bit Score: 38.20 E-value: 8.71e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1519712285 213 EVSKQLARSFKKSGIHIMTSSEVTGVDTSGKGckVHVKTKKGEevLDADVVLSAVGV 269
Cdd:COG0579 154 ALTRALAENAEANGVELLLNTEVTGIEREGDG--WEVTTNGGT--IRARFVINAAGL 206
|
|
| |
