|
Name |
Accession |
Description |
Interval |
E-value |
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
126-578 |
1.01e-179 |
|
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: 515.27 E-value: 1.01e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 126 EYDMVVVGGGPAGYYAAIRGAQLGGKIAIVEKSEFGGTCLNKGCIPTKTYLKNAEILDGLKIAAGRGINLAstNYTIDMD 205
Cdd:TIGR01350 1 AYDVIVIGGGPGGYVAAIRAAQLGLKVALVEKEYLGGTCLNVGCIPTKALLHSAEVYDEIKHAKDLGIEVE--NVSVDWE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 206 KTVDFKNSVVKTLTGGVQGLLKANKVTIFNGLGQVNPDKTVTI----GSQTIKGRSIVLATGSKVSRINIP-GIDSKLVL 280
Cdd:TIGR01350 79 KMQKRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVtgenGEETLEAKNIIIATGSRPRSLPGPfDFDGKVVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 281 TSDDILDLREIPKTLTVMGGGVVGVELGLVYASYGTEVTVVEMADRIIPGMDREVSVELQKVLSKKGMKFLTSVGVSEII 360
Cdd:TIGR01350 159 TSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTAVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 361 EANNQLTIKLNDGSE--IVSEKALLSIGRVPQL--AGLENLNLEMD-RGRIKVNAYQETSIPGIYAPGDVNGTKMLAHAA 435
Cdd:TIGR01350 239 KNDDQVTYENKGGETetLTGEKVLVAVGRKPNTegLGLEKLGVELDeRGRIVVDEYMRTNVPGIYAIGDVIGGPMLAHVA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 436 YRMGEVAAENAINGNHHKAKLDFTPAAVYTHPEIAMVGLTEDQAREQyGNDILIGKCSFTGNGRAIASNEAHGFVKVIAD 515
Cdd:TIGR01350 319 SHEGIVAAENIAGKEPAHIDYDAVPSVIYTDPEVASVGLTEEQAKEA-GYDVKIGKFPFAANGKALALGETDGFVKIIAD 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1485845380 516 KKYHEILGVHIIGPVAAEMINEAATIMESELTVDDVAASIHGHPTFSEVMYEAFLDVLGVAIH 578
Cdd:TIGR01350 398 KKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEAIKEAALAALGKPIH 460
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
126-574 |
1.77e-174 |
|
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: 501.92 E-value: 1.77e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 126 EYDMVVVGGGPAGYYAAIRGAQLGGKIAIVEKSEFGGTCLNKGCIPTKTYLKNAEILDGLKIAAGRGINLasTNYTIDMD 205
Cdd:COG1249 3 DYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISA--GAPSVDWA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 206 KTVDFKNSVVKTLTGGVQGLLKANKVTIFNGLGQVNPDKTVTI-GSQTIKGRSIVLATGSKVSRINIPGIDSKLVLTSDD 284
Cdd:COG1249 81 ALMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVtGGETLTADHIVIATGSRPRVPPIPGLDEVRVLTSDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 285 ILDLREIPKTLTVMGGGVVGVELGLVYASYGTEVTVVEMADRIIPGMDREVSVELQKVLSKKGMKFLTSVGVSEIIEANN 364
Cdd:COG1249 161 ALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 365 QLTIKLNDGSEIVSEKA---LLSIGRVPQLA--GLENLNLEMD-RGRIKVNAYQETSIPGIYAPGDVNGTKMLAHAAYRM 438
Cdd:COG1249 241 GVTVTLEDGGGEEAVEAdkvLVATGRRPNTDglGLEAAGVELDeRGGIKVDEYLRTSVPGIYAIGDVTGGPQLAHVASAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 439 GEVAAENAINGNHHKAKLDFTPAAVYTHPEIAMVGLTEDQAREQyGNDILIGKCSFTGNGRAIASNEAHGFVKVIADKKY 518
Cdd:COG1249 321 GRVAAENILGKKPRPVDYRAIPSVVFTDPEIASVGLTEEEAREA-GIDVKVGKFPFAANGRALALGETEGFVKLIADAET 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1485845380 519 HEILGVHIIGPVAAEMINEAATIMESELTVDDVAASIHGHPTFSEVMYEAFLDVLG 574
Cdd:COG1249 400 GRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAALALLG 455
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
126-578 |
1.57e-158 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 461.54 E-value: 1.57e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 126 EYDMVVVGGGPAGYYAAIRGAQLGGKIAIVEKSEFGGTCLNKGCIPTKTYLKNAEILDGLKIAAGRGINlaSTNYTIDMD 205
Cdd:PRK06416 4 EYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIK--AENVGIDFK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 206 KTVDFKNSVVKTLTGGVQGLLKANKVTIFNGLGQVNPDKTVTI----GSQTIKGRSIVLATGSKVsrINIPGI--DSKLV 279
Cdd:PRK06416 82 KVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVmtedGEQTYTAKNIILATGSRP--RELPGIeiDGRVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 280 LTSDDILDLREIPKTLTVMGGGVVGVELGLVYASYGTEVTVVEMADRIIPGMDREVSVELQKVLSKKGMKFLTSVGVSEI 359
Cdd:PRK06416 160 WTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPGEDKEISKLAERALKKRGIKIKTGAKAKKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 360 IEANNQLTIKLNDGSE---IVSEKALLSIGRVPQLA--GLENLNLEMDRGRIKVNAYQETSIPGIYAPGDVNGTKMLAHA 434
Cdd:PRK06416 240 EQTDDGVTVTLEDGGKeetLEADYVLVAVGRRPNTEnlGLEELGVKTDRGFIEVDEQLRTNVPNIYAIGDIVGGPMLAHK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 435 AYRMGEVAAENaINGNHHKAKLDFTPAAVYTHPEIAMVGLTEDQAREQyGNDILIGKCSFTGNGRAIASNEAHGFVKVIA 514
Cdd:PRK06416 320 ASAEGIIAAEA-IAGNPHPIDYRGIPAVTYTHPEVASVGLTEAKAKEE-GFDVKVVKFPFAGNGKALALGETDGFVKLIF 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1485845380 515 DKKYHEILGVHIIGPVAAEMINEAATIMESELTVDDVAASIHGHPTFSEVMYEAFLDVLGVAIH 578
Cdd:PRK06416 398 DKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEALGEAALAAAGKPLH 461
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
125-578 |
5.15e-141 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 416.50 E-value: 5.15e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 125 DEYDMVVVGGGPAGYYAAIRGAQLGGKIAIVEKSEFGGTCLNKGCIPTKTYLKNAEILDGLKIAAGRGINlaSTNYTIDM 204
Cdd:PRK06292 2 EKYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGPLGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIH--ADGPKIDF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 205 DKTVDFKNSVVKTLTGGV-QGLLKANKVTIFNGLGQVNPDKTVTIGSQTIKGRSIVLATGSKVsrINIPG---IDSKLVL 280
Cdd:PRK06292 80 KKVMARVRRERDRFVGGVvEGLEKKPKIDKIKGTARFVDPNTVEVNGERIEAKNIVIATGSRV--PPIPGvwlILGDRLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 281 TSDDILDLREIPKTLTVMGGGVVGVELGLVYASYGTEVTVVEMADRIIPGMDREVSVELQKVLSKKgMKFLTSVGVSEII 360
Cdd:PRK06292 158 TSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILSKE-FKIKLGAKVTSVE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 361 EANNQ---LTIKLNDGSEIVSEKALLSIGRVPQLA--GLENLNLEMD-RGRIKVNAYQETSIPGIYAPGDVNGTKMLAHA 434
Cdd:PRK06292 237 KSGDEkveELEKGGKTETIEADYVLVATGRRPNTDglGLENTGIELDeRGRPVVDEHTQTSVPGIYAAGDVNGKPPLLHE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 435 AYRMGEVAAENAINGNHHKAKLDFTPAAVYTHPEIAMVGLTEDQAREQyGNDILIGKCSFTGNGRAIASNEAHGFVKVIA 514
Cdd:PRK06292 317 AADEGRIAAENAAGDVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAA-GIDYVVGEVPFEAQGRARVMGKNDGFVKVYA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1485845380 515 DKKYHEILGVHIIGPVAAEMINEAATIMESELTVDDVAASIHGHPTFSEVMYEAFLDVLGVAIH 578
Cdd:PRK06292 396 DKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRTALRDLFSKLIH 459
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
125-578 |
2.52e-120 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 364.25 E-value: 2.52e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 125 DEYDMVVVGGGPAGYYAAIRGAQLGGKIAIVE-------KSEFGGTCLNKGCIPTKTYLKNAEILDGLKIA-AGRGINLA 196
Cdd:PRK06327 3 KQFDVVVIGAGPGGYVAAIRAAQLGLKVACIEawknpkgKPALGGTCLNVGCIPSKALLASSEEFENAGHHfADHGIHVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 197 stNYTIDMDKTVDFKNSVVKTLTGGVQGLLKANKVTIFNGLGQVNPD-------KTVTIGSQTIKGRSIVLATGSKvSRi 269
Cdd:PRK06327 83 --GVKIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVGKtdagyeiKVTGEDETVITAKHVIIATGSE-PR- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 270 NIPGI--DSKLVLTSDDILDLREIPKTLTVMGGGVVGVELGLVYASYGTEVTVVEMADRIIPGMDREVSVELQKVLSKKG 347
Cdd:PRK06327 159 HLPGVpfDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAAADEQVAKEAAKAFTKQG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 348 MKFLTSVGVSEIIEANNQLTIKLNDGS----EIVSEKALLSIGRVPQLAGL--ENLNLEMD-RGRIKVNAYQETSIPGIY 420
Cdd:PRK06327 239 LDIHLGVKIGEIKTGGKGVSVAYTDADgeaqTLEVDKLIVSIGRVPNTDGLglEAVGLKLDeRGFIPVDDHCRTNVPNVY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 421 APGDVNGTKMLAHAAYRMGEVAAENaINGNHHKAKLDFTPAAVYTHPEIAMVGLTEDQAREQyGNDILIGKCSFTGNGRA 500
Cdd:PRK06327 319 AIGDVVRGPMLAHKAEEEGVAVAER-IAGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLKAE-GVEYKAGKFPFMANGRA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1485845380 501 IASNEAHGFVKVIADKKYHEILGVHIIGPVAAEMINEAATIMESELTVDDVAASIHGHPTFSEVMYEAFLDVLGVAIH 578
Cdd:PRK06327 397 LAMGEPDGFVKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEVWHEAALAVDKRPLH 474
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
125-563 |
1.42e-103 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 320.61 E-value: 1.42e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 125 DEYDMVVVGGGPAGYYAAIRGAQLGGKIAIVEKSEFGGTCLNKGCIPTKTYLKNAEILDGLKIAAGRGINLAStNYTIDM 204
Cdd:PRK06370 4 QRYDAIVIGAGQAGPPLAARAAGLGMKVALIERGLLGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGG-PVSVDF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 205 DKTVDFKNSVV-KTLTGGVQGLLKANKVTIFNGLGQVNPDKTVTIGSQTIKGRSIVLATGSKVSRINIPGIDSKLVLTSD 283
Cdd:PRK06370 83 KAVMARKRRIRaRSRHGSEQWLRGLEGVDVFRGHARFESPNTVRVGGETLRAKRIFINTGARAAIPPIPGLDEVGYLTNE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 284 DILDLREIPKTLTVMGGGVVGVELGLVYASYGTEVTVVEMADRIIPGMDREVSVELQKVLSKKGMKFLTSVGVSEIIEAN 363
Cdd:PRK06370 163 TIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILEREGIDVRLNAECIRVERDG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 364 NQLTIKLN---DGSEIVSEKALLSIGRVPQlagLENLNLEM------DRGRIKVNAYQETSIPGIYAPGDVNGTKMLAHA 434
Cdd:PRK06370 243 DGIAVGLDcngGAPEITGSHILVAVGRVPN---TDDLGLEAagvetdARGYIKVDDQLRTTNPGIYAAGDCNGRGAFTHT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 435 AYRMGEVAAENAINGNHHKAKLDFTPAAVYTHPEIAMVGLTEDQAReQYGNDILIGKCSFTGNGRAIASNEAHGFVKVIA 514
Cdd:PRK06370 320 AYNDARIVAANLLDGGRRKVSDRIVPYATYTDPPLARVGMTEAEAR-KSGRRVLVGTRPMTRVGRAVEKGETQGFMKVVV 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1485845380 515 DKKYHEILGVHIIGPVAAEMINEAATIMESELTVDDVAASIHGHPTFSE 563
Cdd:PRK06370 399 DADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSE 447
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
127-563 |
1.69e-82 |
|
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: 265.83 E-value: 1.69e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 127 YDMVVVGGGPAGYYAAIRGAQLGGKIAIVEKSEFGGTCLNKGCIPTKTYLKNAEILDGLKIAAGRGInlaSTNYTIDMDK 206
Cdd:TIGR02053 1 YDLVIIGSGAAAFAAAIKAAELGASVAMVERGPLGGTCVNVGCVPSKMLLRAAEVAHYARKPPFGGL---AATVAVDFGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 207 TVDFKNSVVKTL-TGGVQGLLKANKVTIFNGLGQVNPDKTVTI--GSQTIKGRSIVLATGSKVSRINIPGIDSKLVLTSD 283
Cdd:TIGR02053 78 LLEGKREVVEELrHEKYEDVLSSYGVDYLRGRARFKDPKTVKVdlGREVRGAKRFLIATGARPAIPPIPGLKEAGYLTSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 284 DILDLREIPKTLTVMGGGVVGVELGLVYASYGTEVTVVEMADRIIPGMDREVSVELQKVLSKKGMKFLTSVGVSEiIEAN 363
Cdd:TIGR02053 158 EALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSDRLLPREEPEISAAVEEALAEEGIEVVTSAQVKA-VSVR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 364 NQLTIKLNDGS----EIVSEKALLSIGRVPQLA--GLENLNLEMD-RGRIKVNAYQETSIPGIYAPGDVNGTKMLAHAAY 436
Cdd:TIGR02053 237 GGGKIITVEKPggqgEVEADELLVATGRRPNTDglGLEKAGVKLDeRGGILVDETLRTSNPGIYAAGDVTGGLQLEYVAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 437 RMGEVAAENAINGNHHKAKLDFTPAAVYTHPEIAMVGLTEDQA-REQYGNDILIgkCSFTGNGRAIASNEAHGFVKVIAD 515
Cdd:TIGR02053 317 KEGVVAAENALGGANAKLDLLVIPRVVFTDPAVASVGLTEAEAqKAGIECDCRT--LPLTNVPRARINRDTRGFIKLVAE 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1485845380 516 KKYHEILGVHIIGPVAAEMINEAATIMESELTVDDVAASIHGHPTFSE 563
Cdd:TIGR02053 395 PGTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAE 442
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
126-563 |
6.88e-76 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 248.15 E-value: 6.88e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 126 EYDMVVVGGGPAGYYAAIRGAQLGGKIAIVEKSEFGGTCLNKGCIPTKTYLKNAEILDGLK-IAAGRGINLASTNYtiDM 204
Cdd:PRK06116 4 DYDLIVIGGGSGGIASANRAAMYGAKVALIEAKRLGGTCVNVGCVPKKLMWYGAQIAEAFHdYAPGYGFDVTENKF--DW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 205 DKTVDFKNSVVKTLTGGVQGLLKANKVTIFNGLGQVNPDKTVTIGSQTIKGRSIVLATGSKVSRINIPGIDskLVLTSDD 284
Cdd:PRK06116 82 AKLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNGERYTADHILIATGGRPSIPDIPGAE--YGITSDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 285 ILDLREIPKTLTVMGggvvgvelglvyASY------------GTEVTVVEMADRIIPGMDREVSVELQKVLSKKGMKFLT 352
Cdd:PRK06116 160 FFALEELPKRVAVVG------------AGYiavefagvlnglGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 353 SVGVSEII-EANNQLTIKLNDGSEIVSEKALLSIGRVPQLA--GLENLNLEMD-RGRIKVNAYQETSIPGIYAPGDVNGT 428
Cdd:PRK06116 228 NAVPKAVEkNADGSLTLTLEDGETLTVDCLIWAIGREPNTDglGLENAGVKLNeKGYIIVDEYQNTNVPGIYAVGDVTGR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 429 KMLAHAAYRMGEVAAENAINGNHHkAKLDFT--PAAVYTHPEIAMVGLTEDQAREQYGND-ILIGKCSFTGNGRAIASNE 505
Cdd:PRK06116 308 VELTPVAIAAGRRLSERLFNNKPD-EKLDYSniPTVVFSHPPIGTVGLTEEEAREQYGEDnVKVYRSSFTPMYTALTGHR 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1485845380 506 AHGFVKVIADKKYHEILGVHIIGPVAAEMINEAATIMESELTVDDVAASIHGHPTFSE 563
Cdd:PRK06116 387 QPCLMKLVVVGKEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAE 444
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
126-574 |
1.01e-73 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 242.75 E-value: 1.01e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 126 EYDMVVVGGGPAGYYAAIRGAQLGGKIAIVEK-SEFGGTCLNKGCIPTKTylknaeildgLKIAAGRGINLAS----TNY 200
Cdd:PRK05249 5 DYDLVVIGSGPAGEGAAMQAAKLGKRVAVIERyRNVGGGCTHTGTIPSKA----------LREAVLRLIGFNQnplySSY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 201 ----TIDMDKTVDFKNSVVKTLTGGVQGLLKANKVTIFNGLGQ-VNPDkTVTI-----GSQTIKGRSIVLATGSKVSRI- 269
Cdd:PRK05249 75 rvklRITFADLLARADHVINKQVEVRRGQYERNRVDLIQGRARfVDPH-TVEVecpdgEVETLTADKIVIATGSRPYRPp 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 270 NIPgIDSKLVLTSDDILDLREIPKTLTVmgggVVGVELGLVYASY----GTEVTVVEMADRIIPGMDREVSVELQKVLSK 345
Cdd:PRK05249 154 DVD-FDHPRIYDSDSILSLDHLPRSLII----YGAGVIGCEYASIfaalGVKVTLINTRDRLLSFLDDEISDALSYHLRD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 346 KGMKFLTSVGVSEIIEANNQLTIKLNDGSEIVSEKALLSIGRVPQLA--GLENLNLEMD-RGRIKVNAYQETSIPGIYAP 422
Cdd:PRK05249 229 SGVTIRHNEEVEKVEGGDDGVIVHLKSGKKIKADCLLYANGRTGNTDglNLENAGLEADsRGQLKVNENYQTAVPHIYAV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 423 GDVNGTKMLAHAAYRMGEVAAENAInGNHHKAKLDFTPAAVYTHPEIAMVGLTEDQAREQYGnDILIGKCSFTGNGRAIA 502
Cdd:PRK05249 309 GDVIGFPSLASASMDQGRIAAQHAV-GEATAHLIEDIPTGIYTIPEISSVGKTEQELTAAKV-PYEVGRARFKELARAQI 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1485845380 503 SNEAHGFVKVIADKKYHEILGVHIIGPVAAEMINEAATIMESELTVDDVAASIHGHPTFSEVMYEAFLDVLG 574
Cdd:PRK05249 387 AGDNVGMLKILFHRETLEILGVHCFGERATEIIHIGQAIMEQKGTIEYFVNTTFNYPTMAEAYRVAALDGLN 458
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
126-570 |
8.82e-67 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 224.06 E-value: 8.82e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 126 EYDMVVVGGGPAGYYAAIRGAQLggKIAIVEKSEFGGTCLNKGCIPTKTYLKNAEILDGLKIAAGRGINLASTNytidmd 205
Cdd:PRK07846 1 HYDLIIIGTGSGNSILDERFADK--RIAIVEKGTFGGTCLNVGCIPTKMFVYAADVARTIREAARLGVDAELDG------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 206 ktVDFKNSVVKTL-------TGGVQG-LLKANKVTIFNGLGQVNPDKTVTIGS-QTIKGRSIVLATGSkvsRINIPGI-- 274
Cdd:PRK07846 73 --VRWPDIVSRVFgridpiaAGGEEYrGRDTPNIDVYRGHARFIGPKTLRTGDgEEITADQVVIAAGS---RPVIPPVia 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 275 DSKL-VLTSDDILDLREIPKTLTVMGGGVVGVELGLVYASYGTEVTVVEMADRIIPGMDREVSVELQKVLSKKgMKFLTS 353
Cdd:PRK07846 148 DSGVrYHTSDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLDDDISERFTELASKR-WDVRLG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 354 VGVSEIIEANNQLTIKLNDGSEIVSEKALLSIGRVPQ--LAGLENLNLEMDR-GRIKVNAYQETSIPGIYAPGDVNGTKM 430
Cdd:PRK07846 227 RNVVGVSQDGSGVTLRLDDGSTVEADVLLVATGRVPNgdLLDAAAAGVDVDEdGRVVVDEYQRTSAEGVFALGDVSSPYQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 431 LAHAAYRMGEVAAENAINGNH-HKAKLDFTPAAVYTHPEIAMVGLTEDQAREQyGNDILIGKCSFTGNGRAIASNEAHGF 509
Cdd:PRK07846 307 LKHVANHEARVVQHNLLHPDDlIASDHRFVPAAVFTHPQIASVGLTENEARAA-GLDITVKVQNYGDVAYGWAMEDTTGF 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1485845380 510 VKVIADKKYHEILGVHIIGPVAAEMINEAATIMESELTVDDVAAS---IhgHPTFSEVMYEAFL 570
Cdd:PRK07846 386 VKLIADRDTGRLLGAHIIGPQASTLIQPLIQAMSFGLDAREMARGqywI--HPALPEVVENALL 447
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
127-569 |
1.60e-60 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 207.29 E-value: 1.60e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 127 YDMVVVGGGPAGYYAAIRGAQLGGKIAIVEKSE--FGGTCLNKGCIPTKTYLknaeildglkIAAGRGInlastnytiDM 204
Cdd:PRK07251 4 YDLIVIGFGKAGKTLAAKLASAGKKVALVEESKamYGGTCINIGCIPTKTLL----------VAAEKNL---------SF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 205 DKTVDFKNSVVKTLTGGVQGLLKANKVTIFNGLGQVNPDKTVTI----GSQTIKGRSIVLATGSKVSRINIPGI-DSKLV 279
Cdd:PRK07251 65 EQVMATKNTVTSRLRGKNYAMLAGSGVDLYDAEAHFVSNKVIEVqagdEKIELTAETIVINTGAVSNVLPIPGLaDSKHV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 280 LTSDDILDLREIPKTLTVMGGGVVGVELGLVYASYGTEVTVVEMADRIIPGMDREVSVELQKVLSKKGMKFLTSVGVSEI 359
Cdd:PRK07251 145 YDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYMEEDGITFLLNAHTTEV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 360 IEANNQLTIKLNDGSEIVsEKALLSIGRVPQLA--GLENLNLEM-DRGRIKVNAYQETSIPGIYAPGDVNGTKMLAHAA- 435
Cdd:PRK07251 225 KNDGDQVLVVTEDETYRF-DALLYATGRKPNTEplGLENTDIELtERGAIKVDDYCQTSVPGVFAVGDVNGGPQFTYISl 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 436 --YRM--GEVAAENAINGNHHKAkldfTPAAVYTHPEIAMVGLTEDQAREQyGNDILIGKCSFTGNGRAIASNEAHGFVK 511
Cdd:PRK07251 304 ddFRIvfGYLTGDGSYTLEDRGN----VPTTMFITPPLSQVGLTEKEAKEA-GLPYAVKELLVAAMPRAHVNNDLRGAFK 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1485845380 512 VIADKKYHEILGVHIIGPVAAEMINEAATIMESELTVDDVAASIHGHPTFSEVMYEAF 569
Cdd:PRK07251 379 VVVNTETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAENLNDLF 436
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
127-439 |
2.88e-60 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 202.16 E-value: 2.88e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 127 YDMVVVGGGPAGYYAAIRGAQLGGKIAIVEkseFGGTCLNKGCIPTKTYLKNAEILDGLKIAAgrginlastnytidmdK 206
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIE---DEGTCPYGGCVLSKALLGAAEAPEIASLWA----------------D 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 207 TVDFKNSVVKTLTGGVQGLLKANKVTIFNGLGQVNPDKTVTIGSQTIKGRSIVLATGSKVSRINIPG-----IDSKLVLT 281
Cdd:pfam07992 62 LYKRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELVDGDGETITYDRLVIATGARPRLPPIPGvelnvGFLVRTLD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 282 SDDILDLREIPKTLTVMGGGVVGVELGLVYASYGTEVTVVEMADRIIPGMDREVSVELQKVLSKKGMKFLTSVGVSEIIE 361
Cdd:pfam07992 142 SAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 362 ANNQLTIKLNDGSEIVSEKALLSIGRVPQLAGLENLNLEMD-RGRIKVNAYQETSIPGIYAPGDVNGTK-MLAHAAYRMG 439
Cdd:pfam07992 222 DGDGVEVILKDGTEIDADLVVVAIGRRPNTELLEAAGLELDeRGGIVVDEYLRTSVPGIYAAGDCRVGGpELAQNAVAQG 301
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
127-570 |
5.19e-59 |
|
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: 203.45 E-value: 5.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 127 YDMVVVGGGPAGyyaAIRGAQLGGK-IAIVEKSEFGGTCLNKGCIPTKTYLKNAEILDGLKIAAGRGINlASTNyTIDMD 205
Cdd:TIGR03452 3 YDLIIIGTGSGN---SIPDPRFADKrIAIVEKGTFGGTCLNVGCIPTKMFVYAAEVAQSIGESARLGID-AEID-SVRWP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 206 KTVD--FKNSVVKTLTGGV---QGLLKANkVTIFNGLGQVNPDKTVTIGS-QTIKGRSIVLATGskvSRINIPGI--DSK 277
Cdd:TIGR03452 78 DIVSrvFGDRIDPIAAGGEdyrRGDETPN-IDVYDGHARFVGPRTLRTGDgEEITGDQIVIAAG---SRPYIPPAiaDSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 278 LVL-TSDDILDLREIPKTLTVMGGGVVGVELGLVYASYGTEVTVVEMADRIIPGMDREVSVELQKvLSKKGMKFLTSVGV 356
Cdd:TIGR03452 154 VRYhTNEDIMRLPELPESLVIVGGGYIAAEFAHVFSALGTRVTIVNRSTKLLRHLDEDISDRFTE-IAKKKWDIRLGRNV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 357 SEIIEANNQLTIKLNDGSEIVSEKALLSIGRVPQ--LAGLENLNLEMDR-GRIKVNAYQETSIPGIYAPGDVNGTKMLAH 433
Cdd:TIGR03452 233 TAVEQDGDGVTLTLDDGSTVTADVLLVATGRVPNgdLLDAEAAGVEVDEdGRIKVDEYGRTSARGVWALGDVSSPYQLKH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 434 AAYRMGEVAAENAINGNH-HKAKLDFTPAAVYTHPEIAMVGLTEDQAREQyGNDILIGKCSFTGNGRAIASNEAHGFVKV 512
Cdd:TIGR03452 313 VANAEARVVKHNLLHPNDlRKMPHDFVPSAVFTHPQIATVGLTEQEAREA-GHDITVKIQNYGDVAYGWAMEDTTGFCKL 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1485845380 513 IADKKYHEILGVHIIGPVAAEMINEAATIMESELTVDDVAASIHG-HPTFSEVMYEAFL 570
Cdd:TIGR03452 392 IADRDTGKLLGAHIIGPQASSLIQPLITAMAFGLDAREMARKQYWiHPALPEVVENALL 450
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
125-578 |
3.93e-56 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 200.53 E-value: 3.93e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 125 DEYDMVVVGGGPAGYYAAIRGAQLGGKIAIV--EKSEFGGTCLNKGCIPTKTYL---------KNAEILDGLKIAAGRGI 193
Cdd:PTZ00153 115 EEYDVGIIGCGVGGHAAAINAMERGLKVIIFtgDDDSIGGTCVNVGCIPSKALLyatgkyrelKNLAKLYTYGIYTNAFK 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 194 N----------LASTNYTIDMDKTVDFKNSVVKTLTGGVQGLLKANKVTIFNGLGQVNPDKTVTIGSQTIKG-------- 255
Cdd:PTZ00153 195 NgkndpvernqLVADTVQIDITKLKEYTQSVIDKLRGGIENGLKSKKFCKNSEHVQVIYERGHIVDKNTIKSeksgkefk 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 256 -RSIVLATGSKVsriNIPG---IDSKLVLTSDDILDLREIPKTLTVMGGGVVGVELGLVYASYGTEVTVVEMADRIIPGM 331
Cdd:PTZ00153 275 vKNIIIATGSTP---NIPDnieVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSPQLLPLL 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 332 DREVSVELQKVLSK-KGMKFLTS----------------VGVSEIIEANNQLTIK-LNDGSEIVSEKALLSIGRVP--QL 391
Cdd:PTZ00153 352 DADVAKYFERVFLKsKPVRVHLNtlieyvragkgnqpviIGHSERQTGESDGPKKnMNDIKETYVDSCLVATGRKPntNN 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 392 AGLENLNLEMDRGRIKVNAYQETS------IPGIYAPGDVNGTKMLAHAAYRMGeVAAENAINGNHHKAKLDFT------ 459
Cdd:PTZ00153 432 LGLDKLKIQMKRGFVSVDEHLRVLredqevYDNIFCIGDANGKQMLAHTASHQA-LKVVDWIEGKGKENVNINVenwask 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 460 -------PAAVYTHPEIAMVGLTEDQAREQYGNDILIGKCSF-TGNGRAIASNE----------------------AHGF 509
Cdd:PTZ00153 511 piiykniPSVCYTTPELAFIGLTEKEAKELYPPDNVGVEISFyKANSKVLCENNisfpnnsknnsynkgkyntvdnTEGM 590
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1485845380 510 VKVIADKKYHEILGVHIIGPVAAEMINEAATIMESELTVDDVAASIHGHPTFSEVMYEAFLDVLGVAIH 578
Cdd:PTZ00153 591 VKIVYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDAAFKAIAGVRTH 659
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
126-564 |
2.57e-54 |
|
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: 191.60 E-value: 2.57e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 126 EYDMVVVGGGPAGYYAAIRGAQLGGKIAIVEKSE---------FGGTCLNKGCIPTKTYLKNAEILDGLKIAAGRGINLA 196
Cdd:TIGR01438 2 DYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTptplgtrwgIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 197 STnYTIDMDKTVDFKNSVVKTLTGGVQGLLKANKVTIFNGLGQ-VNPDK---TVTIGSQ-TIKGRSIVLATGSKVSRINI 271
Cdd:TIGR01438 82 ET-VKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEfVDKHRikaTNKKGKEkIYSAERFLIATGERPRYPGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 272 PGiDSKLVLTSDDILDLREIP-KTLTVMGGGVVGVELGLvYASYGTEVTVvemADRIIP--GMDREVSVELQKVLSKKGM 348
Cdd:TIGR01438 161 PG-AKELCITSDDLFSLPYCPgKTLVVGASYVALECAGF-LAGIGLDVTV---MVRSILlrGFDQDCANKVGEHMEEHGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 349 KFLTSVGVSEIIEANNQLTIKLNDGSEIVSEK---ALLSIGRVPQLA--GLENLNLEMDR--GRIKVNAYQETSIPGIYA 421
Cdd:TIGR01438 236 KFKRQFVPIKVEQIEAKVLVEFTDSTNGIEEEydtVLLAIGRDACTRklNLENVGVKINKktGKIPADEEEQTNVPYIYA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 422 PGDV-NGTKMLAHAAYRMGEVAAENAINGNHHKAKLDFTPAAVYTHPEIAMVGLTEDQAREQYGND-ILIGKCSFTGNGR 499
Cdd:TIGR01438 316 VGDIlEDKPELTPVAIQAGRLLAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAVEKFGEEnVEVFHSYFWPLEW 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1485845380 500 AIASNEAHGF--VKVIADKKYHE-ILGVHIIGPVAAEMINEAATIMESELTVDDVAASIHGHPTFSEV 564
Cdd:TIGR01438 396 TIPSRDNHNKcyAKLVCNKKENErVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEV 463
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
126-569 |
6.45e-53 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 186.91 E-value: 6.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 126 EYDMVVVGGGPAGYYAAIRGAQLGGKIAIVEKSE--FGGTCLNKGCIPTKTYLKNAEILDGLKIAAGRginlastnytid 203
Cdd:NF040477 3 HYQAIIIGFGKAGKTLAATLAKAGWRVAIIEQSAqmYGGTCINIGCIPTKTLVHDAEQHQDFSTAMQR------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 204 mdktvdfKNSVVKTL-TGGVQGLLKANKVTIFNGLGQVNPDKTVTI----GSQTIKGRSIVLATGSKVSRINIPGI-DSK 277
Cdd:NF040477 71 -------KSSVVGFLrDKNYHNLADLDNVDVINGRAEFIDNHTLRVfqadGEQELRGEKIFINTGAQSVLPPIPGLtTTP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 278 LVLTSDDILDLREIPKTLTVMGGGVVGVELGLVYASYGTEVTVVEMADRIIPGMDREVSVELQKVLSKKGMKFLTSVGVS 357
Cdd:NF040477 144 GVYDSTGLLNLTQLPARLGILGGGYIGVEFASMFARFGSKVTIFEAAELFLPREDRDIAQAIATILQDQGVELILNAQVQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 358 EIIEANNQLTIKLNDGSEIVsEKALLSIGRVPQLAGL--ENLNLEMD-RGRIKVNAYQETSIPGIYAPGDVNGTKMLAHA 434
Cdd:NF040477 224 RVSSHEGEVQLETAEGVLTV-DALLVASGRKPATAGLqlQNAGVAVNeRGAIVVDKYLRTTADNIWAMGDVTGGLQFTYI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 435 A---YRMgeVAAENAINGNHHKAKLDFTPAAVYTHPEIAMVGLTEDQAREQyGNDILIGKCSFTGNGRAIASNEAHGFVK 511
Cdd:NF040477 303 SlddFRI--VRDSLLGEGKRSTDDRQNVPYSVFMTPPLSRIGMTEEQARAS-GADIQVVTLPVAAIPRARVMNDTRGVLK 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1485845380 512 VIADKKYHEILGVHIIGPVAAEMINEAATIMESELTVDDVAASIHGHPTFSEVMYEAF 569
Cdd:NF040477 380 AVVDNKTQRILGVSLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSESLNDLF 437
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
129-568 |
3.21e-52 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 185.45 E-value: 3.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 129 MVVVGGGPAGYYAAIRGAQLGGKIAIVEKSEFGGTCLNKGCIPTKTYLKNAEILDGLKIAAGRGINLAS-TNYTIDMDKT 207
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIERDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRFIDdGEARVDLPAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 208 vdfkNSVVKTLT----GGVQGLLKANKVTIFNGLGQVNPDK---------TVTIGSQTIKGRSIVLATGSKvSRInIPGI 274
Cdd:PRK07845 84 ----NARVKALAaaqsADIRARLEREGVRVIAGRGRLIDPGlgphrvkvtTADGGEETLDADVVLIATGAS-PRI-LPTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 275 --DSKLVLTSDDILDLREIPKTLTVMGGGVVGVELGLVYASYGTEVTVVEMADRIIPGMDREVSVELQKVLSKKGMKFLT 352
Cdd:PRK07845 158 epDGERILTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPGEDADAAEVLEEVFARRGMTVLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 353 SVGVSEIIEANNQLTIKLNDGSEIVSEKALLSIGRVPQLA--GLENLNLEMDR-GRIKVNAYQETSIPGIYAPGDVNGTK 429
Cdd:PRK07845 238 RSRAESVERTGDGVVVTLTDGRTVEGSHALMAVGSVPNTAglGLEEAGVELTPsGHITVDRVSRTSVPGIYAAGDCTGVL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 430 MLAHAAYRMGEVAAENAINGNHHKAKLDFTPAAVYTHPEIAMVGLTEDQARE-QYGNDILigKCSFTGNGRAIASNEAHG 508
Cdd:PRK07845 318 PLASVAAMQGRIAMYHALGEAVSPLRLKTVASNVFTRPEIATVGVSQAAIDSgEVPARTV--MLPLATNPRAKMSGLRDG 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 509 FVKVIADKKYHEILGVHIIGPVAAEMINEAATIMESELTVDDVAASIHGHPTFSEVMYEA 568
Cdd:PRK07845 396 FVKLFCRPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYPSLSGSITEA 455
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
126-563 |
3.82e-50 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 180.78 E-value: 3.82e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 126 EYDMVVVGGGPAGYYAAIRGAQLGGKIAIVE------KSE----FGGTCLNKGCIPTKTYLKNA----EILDglkiaagr 191
Cdd:PLN02507 25 DFDLFVIGAGSGGVRAARFSANFGAKVGICElpfhpiSSEsiggVGGTCVIRGCVPKKILVYGAtfggEFED-------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 192 ginlaSTNYTIDMDKTVDF--------KNSVVKTLTGGVQGLLKANKVTIFNGLGQVNPDKTVTI-----GSQTIKGRSI 258
Cdd:PLN02507 97 -----AKNYGWEINEKVDFnwkkllqkKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVtqldgTKLRYTAKHI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 259 VLATGSKVSRINIPGidSKLVLTSDDILDLREIPKTLTVMGGGVVGVELGLVYASYGTEVTVVEMADRIIPGMDREVSVE 338
Cdd:PLN02507 172 LIATGSRAQRPNIPG--KELAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRAV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 339 LQKVLSKKGMKFLTSVGVSEIIEANNQLTIKLNDGSEIVSEKALLSIGRVP--QLAGLENLNLEMDR-GRIKVNAYQETS 415
Cdd:PLN02507 250 VARNLEGRGINLHPRTNLTQLTKTEGGIKVITDHGEEFVADVVLFATGRAPntKRLNLEAVGVELDKaGAVKVDEYSRTN 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 416 IPGIYAPGDVNGTKMLAHAAYRMGEVAAENAINGNHHKAKLDFTPAAVYTHPEIAMVGLTEDQAREQYGNDILIGKCSFT 495
Cdd:PLN02507 330 IPSIWAIGDVTNRINLTPVALMEGTCFAKTVFGGQPTKPDYENVACAVFCIPPLSVVGLSEEEAVEQAKGDILVFTSSFN 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1485845380 496 GNGRAIASNEAHGFVKVIADKKYHEILGVHIIGPVAAEMINEAATIMESELTVDDVAASIHGHPTFSE 563
Cdd:PLN02507 410 PMKNTISGRQEKTVMKLIVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAE 477
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
127-563 |
1.00e-46 |
|
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: 170.92 E-value: 1.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 127 YDMVVVGGGPAGYYAAIRGAQLGGK-IAIVE---------KSEFGGTCLNKGCIPTKTYLKNAEILDGLKIAAGRGINLA 196
Cdd:TIGR01423 4 FDLVVIGAGSGGLEAGWNAATLYKKrVAVVDvqthhgppfYAALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGWEFD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 197 STNYTIDMDKTVDFKNSVVKTLTGGVQGLLKANK-VTIFNGLGQVNPDKTVTIGS---------QTIKGRSIVLATGSKV 266
Cdd:TIGR01423 84 RSSVKANWKALIAAKNKAVLDINKSYEGMFADTEgLTFFLGWGALEDKNVVLVREsadpksavkERLQAEHILLATGSWP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 267 SRINIPGIDskLVLTSDDILDLREIPK---TLTVMGGGVVGVELGLVYASYGTEVTVVEMADRIIPGMDREVSVELQKVL 343
Cdd:TIGR01423 164 QMLGIPGIE--HCISSNEAFYLDEPPRrvlTVGGGFISVEFAGIFNAYKPRGGKVTLCYRNNMILRGFDSTLRKELTKQL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 344 SKKGMKFLTSVGVSEI-IEANNQLTIKLNDGSEIVSEKALLSIGRVP--QLAGLENLNLEM-DRGRIKVNAYQETSIPGI 419
Cdd:TIGR01423 242 RANGINIMTNENPAKVtLNADGSKHVTFESGKTLDVDVVMMAIGRVPrtQTLQLDKVGVELtKKGAIQVDEFSRTNVPNI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 420 YAPGDVNGTKMLAHAAYRMGeVAAENAINGNHHKaKLDFT--PAAVYTHPEIAMVGLTEDQAREQYgNDILIGKCSFTGN 497
Cdd:TIGR01423 322 YAIGDVTDRVMLTPVAINEG-AAFVDTVFGNKPR-KTDHTrvASAVFSIPPIGTCGLVEEDAAKKF-EKVAVYESSFTPL 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1485845380 498 GRAIASNEAHGFV-KVIADKKYHEILGVHIIGPVAAEMINEAATIMESELTVDDVAASIHGHPTFSE 563
Cdd:TIGR01423 399 MHNISGSKYKKFVaKIVTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAE 465
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
125-569 |
1.69e-46 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 169.42 E-value: 1.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 125 DEYDMVVVGGGPAGYYAAIRGAQLGGKIAIVEKSE--FGGTCLNKGCIPTKTYLKNAEildglkiaagrginlASTNYTI 202
Cdd:PRK08010 2 NKYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNamYGGTCINIGCIPTKTLVHDAQ---------------QHTDFVR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 203 DMDKtvdfKNSVVKTLTG-GVQGLLKANKVTIFNGLGQVNPDKTVTI----GSQTIKGRSIVLATGSKVSRINIPGIDSK 277
Cdd:PRK08010 67 AIQR----KNEVVNFLRNkNFHNLADMPNIDVIDGQAEFINNHSLRVhrpeGNLEIHGEKIFINTGAQTVVPPIPGITTT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 278 L-VLTSDDILDLREIPKTLTVMGGGVVGVELGLVYASYGTEVTVVEMADRIIPGMDREVSVELQKVLSKKGMKFLTSVGV 356
Cdd:PRK08010 143 PgVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 357 SEIIEANNQLTIKLNDGSEIVsEKALLSIGRVPQLAGLENLNLEM---DRGRIKVNAYQETSIPGIYAPGDVNGTKMLAH 433
Cdd:PRK08010 223 ERISHHENQVQVHSEHAQLAV-DALLIASGRQPATASLHPENAGIavnERGAIVVDKYLHTTADNIWAMGDVTGGLQFTY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 434 AA---YRMgeVAAENAINGNHHKAKLDFTPAAVYTHPEIAMVGLTEDQAREQyGNDILIGKCSFTGNGRAIASNEAHGFV 510
Cdd:PRK08010 302 ISlddYRI--VRDELLGEGKRSTDDRKNVPYSVFMTPPLSRVGMTEEQARES-GADIQVVTLPVAAIPRARVMNDTRGVL 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1485845380 511 KVIADKKYHEILGVHIIGPVAAEMINEAATIMESELTVDDVAASIHGHPTFSEVMYEAF 569
Cdd:PRK08010 379 KAIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLNDLF 437
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
126-563 |
6.39e-46 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 170.06 E-value: 6.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 126 EYDMVVVGGGPAGYYAAIRGAQLGGKIAIVE------KSE----FGGTCLNKGCIPTKTYLKNAEILDGLKIAAGRGINL 195
Cdd:PLN02546 79 DFDLFTIGAGSGGVRASRFASNFGASAAVCElpfatiSSDtlggVGGTCVLRGCVPKKLLVYASKYSHEFEESRGFGWKY 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 196 AsTNYTIDMDKTVDFKNSVVKTLTGGVQGLLKANKVTIFNGLGQVNPDKTVTIGSQTIKGRSIVLATGSKVSRINIPGID 275
Cdd:PLN02546 159 E-TEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDVDGKLYTARNILIAVGGRPFIPDIPGIE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 276 SklVLTSDDILDLREIPKTLTVMGGGVVGVELGLVYASYGTEVTVVEMADRIIPGMDREVSVELQKVLSKKGMKFLTSVG 355
Cdd:PLN02546 238 H--AIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKKVLRGFDEEVRDFVAEQMSLRGIEFHTEES 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 356 VSEIIEANN-QLTIKLNDGSEIVSEKALLSIGRVPQLA--GLENLNLEMDR-GRIKVNAYQETSIPGIYAPGDVNGTKML 431
Cdd:PLN02546 316 PQAIIKSADgSLSLKTNKGTVEGFSHVMFATGRKPNTKnlGLEEVGVKMDKnGAIEVDEYSRTSVPSIWAVGDVTDRINL 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 432 AHAAYRMGEVAAENAINGNHHKAKLDFTPAAVYTHPEIAMVGLTEDQAREQYGnDILIgkcsFTGNGRAIASNEA----H 507
Cdd:PLN02546 396 TPVALMEGGALAKTLFGNEPTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYG-DVDV----FTANFRPLKATLSglpdR 470
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1485845380 508 GFVKVIADKKYHEILGVHIIGPVAAEMINEAATIMESELTVDDVAASIHGHPTFSE 563
Cdd:PLN02546 471 VFMKLIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAE 526
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
130-552 |
1.03e-43 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 164.17 E-value: 1.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 130 VVVGGGPAGYYAAIRGAQLGGKIAIVEKSEFGGTCLNKGCIPTKTYLKNAEILDgLKIAAGRGINLASTNYTIDMDKTVD 209
Cdd:PRK13748 102 AVIGSGGAAMAAALKAVEQGARVTLIERGTIGGTCVNVGCVPSKIMIRAAHIAH-LRRESPFDGGIAATVPTIDRSRLLA 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 210 FKNSVVKTLT-GGVQGLLKAN-KVTIFNGLGQVNPDKTVTI-----GSQTIKGRSIVLATGSKVSRINIPGIDSKLVLTS 282
Cdd:PRK13748 181 QQQARVDELRhAKYEGILDGNpAITVLHGEARFKDDQTLIVrlndgGERVVAFDRCLIATGASPAVPPIPGLKETPYWTS 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 283 DDILDLREIPKTLTVMGGGVVGVELGLVYASYGTEVTVVEMAdRIIPGMDREVSVELQKVLSKKGMKFLTSVGVSEIIEA 362
Cdd:PRK13748 261 TEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILARS-TLFFREDPAIGEAVTAAFRAEGIEVLEHTQASQVAHV 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 363 NNQLTIKLNDGsEIVSEKALLSIGRVPQLAG--LENLNLEMD-RGRIKVNAYQETSIPGIYAPGDVNGTKMLAHAAYRMG 439
Cdd:PRK13748 340 DGEFVLTTGHG-ELRADKLLVATGRAPNTRSlaLDAAGVTVNaQGAIVIDQGMRTSVPHIYAAGDCTDQPQFVYVAAAAG 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 440 EVAAENAINGNhhkAKLDFT--PAAVYTHPEIAMVGLTEDQAREQygnDILIGKCSFTGNG--RAIASNEAHGFVKVIAD 515
Cdd:PRK13748 419 TRAAINMTGGD---AALDLTamPAVVFTDPQVATVGYSEAEAHHD---GIETDSRTLTLDNvpRALANFDTRGFIKLVIE 492
|
410 420 430
....*....|....*....|....*....|....*..
gi 1485845380 516 KKYHEILGVHIIGPVAAEMINEAATIMESELTVDDVA 552
Cdd:PRK13748 493 EGSGRLIGVQAVAPEAGELIQTAALAIRNRMTVQELA 529
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
459-568 |
2.39e-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: 147.70 E-value: 2.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 459 TPAAVYTHPEIAMVGLTEDQAREQYGnDILIGKCSFTGNGRAIASNEAHGFVKVIADKKYHEILGVHIIGPVAAEMINEA 538
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGG-EVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQEA 79
|
90 100 110
....*....|....*....|....*....|
gi 1485845380 539 ATIMESELTVDDVAASIHGHPTFSEVMYEA 568
Cdd:pfam02852 80 ALAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
127-563 |
1.47e-41 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 157.85 E-value: 1.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 127 YDMVVVGGGPAGYYAAIRGAQLGGKIAIVEKSEFGGTCLNKGCIPTKTYLKNAEILDGLKIAAGRGINlasTNYTIDMDK 206
Cdd:PTZ00058 49 YDLIVIGGGSGGMAAARRAARNKAKVALVEKDYLGGTCVNVGCVPKKIMFNAASIHDILENSRHYGFD---TQFSFNLPL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 207 TVDFKNSVVKTLTGGVQGLLKANKVTIFNGLGQV--------------------NPDKTVTIGS---------QTIKGRS 257
Cdd:PTZ00058 126 LVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLlsenqvlikkvsqvdgeadeSDDDEVTIVSagvsqlddgQVIEGKN 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 258 IVLATGSKVSRINIPGIDskLVLTSDDILDLREiPKTLTVMGGGVVGVELGLVYASYGTEVTVVEMADRIIPGMDREVSV 337
Cdd:PTZ00058 206 ILIAVGNKPIFPDVKGKE--FTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLRKFDETIIN 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 338 ELQKVLSKKGMKFLTSVGVSEI--IEANNQLTIKLNDGSEIVSEKALLSIGRVPQLA--GLENLNLEMDRGRIKVNAYQE 413
Cdd:PTZ00058 283 ELENDMKKNNINIITHANVEEIekVKEKNLTIYLSDGRKYEHFDYVIYCVGRSPNTEdlNLKALNIKTPKGYIKVDDNQR 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 414 TSIPGIYAPGDVNGTKM----------------------------------LAHAAYRMGEVAAENAINGNHHKAKLDFT 459
Cdd:PTZ00058 363 TSVKHIYAVGDCCMVKKnqeiedlnllklyneepylkkkentsgesyynvqLTPVAINAGRLLADRLFGPFSRTTNYKLI 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 460 PAAVYTHPEIAMVGLTEDQAREQYGNDIL-IGKCSFTGNGRAI----ASNEAHGFVKVIADKKYHEILGVHIIGPVAAEM 534
Cdd:PTZ00058 443 PSVIFSHPPIGTIGLSEQEAIDIYGKENVkIYESRFTNLFFSVydmdPAQKEKTYLKLVCVGKEELIKGLHIVGLNADEI 522
|
490 500
....*....|....*....|....*....
gi 1485845380 535 INEAATIMESELTVDDVAASIHGHPTFSE 563
Cdd:PTZ00058 523 LQGFAVALKMNATKADFDETIPIHPTAAE 551
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
127-564 |
8.11e-41 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 154.98 E-value: 8.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 127 YDMVVVGGGPAGYYAAIRGAQLGGKIAIVE---------KSEFGGTCLNKGCIPTKTYLKNAEIldglkiaaGRGINLAS 197
Cdd:PTZ00052 6 YDLVVIGGGSGGMAAAKEAAAHGKKVALFDyvkpstqgtKWGLGGTCVNVGCVPKKLMHYAANI--------GSIFHHDS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 198 TNYTIDMDKTVDFKNsVVKTLTGGVQGL-------LKANKVTIFNGLGQVNPDKTVTIGS----QTIKGRSIVLATGSkv 266
Cdd:PTZ00052 78 QMYGWKTSSSFNWGK-LVTTVQNHIRSLnfsyrtgLRSSKVEYINGLAKLKDEHTVSYGDnsqeETITAKYILIATGG-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 267 sRINIPgiDS-----KLVLTSDDILDLREIP-KTLTVMGGGVVGVELGLvYASYGTEVTVvemADRIIP--GMDREVSVE 338
Cdd:PTZ00052 155 -RPSIP--EDvpgakEYSITSDDIFSLSKDPgKTLIVGASYIGLETAGF-LNELGFDVTV---AVRSIPlrGFDRQCSEK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 339 LQKVLSKKGMKFLTSVGVSEIIEANNQLTIKLNDGSEIVSEKALLSIGRVPQLAGL--ENLNLEMDRGRIKVNAYQETSI 416
Cdd:PTZ00052 228 VVEYMKEQGTLFLEGVVPINIEKMDDKIKVLFSDGTTELFDTVLYATGRKPDIKGLnlNAIGVHVNKSNKIIAPNDCTNI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 417 PGIYAPGDV-NGTKMLAHAAYRMGEVAAENAINGNHHKAKLDFTPAAVYTHPEIAMVGLTEDQAREQYG-NDILIGKCSF 494
Cdd:PTZ00052 308 PNIFAVGDVvEGRPELTPVAIKAGILLARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGeDDIEEYLQEF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 495 TGNGRAIASNEAH---------------GFVKVIADKKYHE-ILGVHIIGPVAAEMINEAATIMESELTVDDVAASIHGH 558
Cdd:PTZ00052 388 NTLEIAAVHREKHerarkdeydfdvssnCLAKLVCVKSEDNkVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIH 467
|
....*.
gi 1485845380 559 PTFSEV 564
Cdd:PTZ00052 468 PTDAEV 473
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1-103 |
5.79e-32 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 127.98 E-value: 5.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 1 MAVEIIMPKLGVDMQEGEIIEWKKQEGDVVNEGDVILEMMSDKTSMELEAEDSGILLKIVRGNGETVPVTEVIGYIGAEG 80
Cdd:PRK11856 1 MMFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEG 80
|
90 100
....*....|....*....|...
gi 1485845380 81 EVVDAGAAPKADVAQATADLKAA 103
Cdd:PRK11856 81 EAEAAAAAEAAPEAPAPEPAPAA 103
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
244-445 |
2.33e-27 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 114.47 E-value: 2.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 244 KTVTIGSqtikGRSI-----VLATGSKVSRINIPGIDSKLVL---TSDDILDLR-------------------EIPKTLt 296
Cdd:COG1251 87 RTVTLAD----GETLpydklVLATGSRPRVPPIPGADLPGVFtlrTLDDADALRaalapgkrvvvigggliglEAAAAL- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 297 vmgggvvgvelglvyASYGTEVTVVEMADRIIPG-MDREVSVELQKVLSKKGMKFLTSVGVSEIIEANNQLTIKLNDGSE 375
Cdd:COG1251 162 ---------------RKRGLEVTVVERAPRLLPRqLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRLADGEE 226
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1485845380 376 IVSEKALLSIGRVPQLAGLENLNLEMDRGrIKVNAYQETSIPGIYAPGDV-------NGTKMLAH--AAYRMGEVAAEN 445
Cdd:COG1251 227 LPADLVVVAIGVRPNTELARAAGLAVDRG-IVVDDYLRTSDPDIYAAGDCaehpgpvYGRRVLELvaPAYEQARVAAAN 304
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
240-473 |
2.43e-27 |
|
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: 112.60 E-value: 2.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 240 VNPD-KTVTIGS-QTIKGRSIVLATGSKVSRINIPGIDSKLVLTSDDILDLREIPKTLTVMGGGVVG--------VELGL 309
Cdd:COG0446 62 IDPEaKTVTLRDgETLSYDKLVLATGARPRPPPIPGLDLPGVFTLRTLDDADALREALKEFKGKRAVvigggpigLELAE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 310 VYASYGTEVTVVEMADRIIPGMDREVSVELQKVLSKKGMKFLTSVGVSEiIEANNQLTIKLNDGSEIVSEKALLSIGRVP 389
Cdd:COG0446 142 ALRKRGLKVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVVA-IDGDDKVAVTLTDGEEIPADLVVVAPGVRP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 390 QLAGLENLNLEMD-RGRIKVNAYQETSIPGIYAPGDVNGTK----------MLAHAAYRMGEVAAENAINGNHHKAKLDF 458
Cdd:COG0446 221 NTELAKDAGLALGeRGWIKVDETLQTSDPDVYAAGDCAEVPhpvtgktvyiPLASAANKQGRVAAENILGGPAPFPGLGT 300
|
250
....*....|....*
gi 1485845380 459 TPAAVYTHpEIAMVG 473
Cdd:COG0446 301 FISKVFDL-CIASTG 314
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-76 |
1.04e-26 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 103.22 E-value: 1.04e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1485845380 1 MAVEIIMPKLGVDMQEGEIIEWKKQEGDVVNEGDVILEMMSDKTSMELEAEDSGILLKIVRGNGETVPVTEVIGYI 76
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
3-76 |
1.43e-25 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 99.79 E-value: 1.43e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1485845380 3 VEIIMPKLGVDMQEGEIIEWKKQEGDVVNEGDVILEMMSDKTSMELEAEDSGILLKIVRGNGETVPVTEVIGYI 76
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
1-104 |
2.93e-20 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 92.70 E-value: 2.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 1 MAVEIIMPKLGVDMQEGEIIEWKKQEGDVVNEGDVILEMMSDKTSMELEAEDSGILLKIVRGNGETVPVTEVIGYIgAEG 80
Cdd:PRK14875 1 SITPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVV-ADA 79
|
90 100
....*....|....*....|....*....
gi 1485845380 81 EV----VDAGAAP-KADVAQATADLKAAG 104
Cdd:PRK14875 80 EVsdaeIDAFIAPfARRFAPEGIDEEDAG 108
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
1-103 |
3.14e-20 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 93.83 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 1 MAVEIIMPKLGVDMQEGEIIEWKKQEGDVVNEGDVILEMMSDKTSMELEAEDSGILLKIVRGNG-ETVPVTEVIGYIGAE 79
Cdd:PRK11892 1 MAIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTPIAVLLEE 80
|
90 100
....*....|....*....|....
gi 1485845380 80 GEVVDAGAAPKADVAQATADLKAA 103
Cdd:PRK11892 81 GESASDAGAAPAAAAEAAAAAPAA 104
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
1-103 |
1.26e-18 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 88.35 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 1 MAVEIIMPKLGVDMQEGEIIEWKKQEGDVVNEGDVILEMMSDKTSMELEAEDSGILLKIVRGNGETVPVTEVIGYIGAEG 80
Cdd:PRK05704 1 MMVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGA 80
|
90 100
....*....|....*....|...
gi 1485845380 81 EVVDAGAAPKADVAQATADLKAA 103
Cdd:PRK05704 81 AAGAAAAAAAAAAAAAAAPAQAQ 103
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
127-448 |
4.23e-18 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 85.17 E-value: 4.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 127 YDMVVVGGGPAGYYAAIRGAQLGGKIAIVEKSEFGGTClnkgcipTKTYlknaEILDGLKIAAG-RGINLastnytidMD 205
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQL-------ATTK----EIENYPGFPEGiSGPEL--------AE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 206 KTVD-FKNSVVKTLTGGVQGLLKANKVtifnglgqvnpdKTVTIGS-QTIKGRSIVLATGSKVSRINIPGIDS------- 276
Cdd:COG0492 62 RLREqAERFGAEILLEEVTSVDKDDGP------------FRVTTDDgTEYEAKAVIIATGAGPRKLGLPGEEEfegrgvs 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 277 ------------K--LVLTSDDI-----LDLREIpktltvmgggvvgvelglvyasyGTEVTVVEMADRIipgmdREVSV 337
Cdd:COG0492 130 ycatcdgfffrgKdvVVVGGGDSaleeaLYLTKF-----------------------ASKVTLIHRRDEL-----RASKI 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 338 ELQKVLSKKGMKFLTSVGVSEIIEAN--NQLTIKLNDGSEIVSEKA---LLSIGRVPQLAGLENLNLEMD-RGRIKVNAY 411
Cdd:COG0492 182 LVERLRANPKIEVLWNTEVTEIEGDGrvEGVTLKNVKTGEEKELEVdgvFVAIGLKPNTELLKGLGLELDeDGYIVVDED 261
|
330 340 350
....*....|....*....|....*....|....*...
gi 1485845380 412 QETSIPGIYAPGDVNGTKM-LAHAAYRMGEVAAENAIN 448
Cdd:COG0492 262 METSVPGVFAAGDVRDYKYrQAATAAGEGAIAALSAAR 299
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1-103 |
1.20e-17 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 86.42 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 1 MAVEIIMPKLGvDMQEGEIIEWKKQEGDVVNEGDVILEMMSDKTSMELEAEDSGILLKIVRGNGETVPVTEVIGYIGAEG 80
Cdd:PRK11855 1 MAIEFKVPDIG-EVVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIEAAG 79
|
90 100
....*....|....*....|...
gi 1485845380 81 EVVDAGAAPKADVAQATADLKAA 103
Cdd:PRK11855 80 AAAAAAAPAAAAAPAAAAAAAPA 102
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
317-460 |
8.47e-17 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 82.49 E-value: 8.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 317 EVTVVEMADRIIPGMDREVSVELQKVLSKKGMKFLTSVGVSEiIEANnqlTIKLNDGSEIVSEKALLSIG-RVPQLagLE 395
Cdd:COG1252 187 RITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTE-VDAD---GVTLEDGEEIPADTVIWAAGvKAPPL--LA 260
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1485845380 396 NLNLEMDR-GRIKVNAYQET-SIPGIYAPGDV--------NGTKMLAHAAYRMGEVAAEN---AINGnhhKAKLDFTP 460
Cdd:COG1252 261 DLGLPTDRrGRVLVDPTLQVpGHPNVFAIGDCaavpdpdgKPVPKTAQAAVQQAKVLAKNiaaLLRG---KPLKPFRY 335
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
4-101 |
1.45e-16 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model represents one of several closely related clades of the dihydrolipoamide acetyltransferase subunit of the pyruvate dehydrogenase complex. It includes sequences from mitochondria and from alpha and beta branches of the proteobacteria, as well as from some other bacteria. Sequences from Gram-positive bacteria are not included. The non-enzymatic homolog protein X, which serves as an E3 component binding protein, falls within the clade phylogenetically but is rejected by its low score. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273567 [Multi-domain] Cd Length: 436 Bit Score: 82.15 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 4 EIIMPKLGVDMQEGEIIEWKKQEGDVVNEGDVILEMMSDKTSMELEAEDSGILLKI-VRGNGETVPVTEVIGYIGAEGEv 82
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKIlVPEGTKDVPVNKPIAVLVEEKE- 79
|
90
....*....|....*....
gi 1485845380 83 vdagaapkaDVAQATADLK 101
Cdd:TIGR01349 80 ---------DVADAFKNYK 89
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1-107 |
1.60e-15 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 79.66 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 1 MAVEIIMPKLGVDmqEGEIIEWKKQEGDVVNEGDVILEMMSDKTSMELEAEDSGILLKIVRGNGETVPVTEVIGYIGAEG 80
Cdd:PRK11854 1 MAIEIKVPDIGAD--EVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESAD 78
|
90 100
....*....|....*....|....*..
gi 1485845380 81 EVVDAGAAPKADVAQATADLKAAGLEV 107
Cdd:PRK11854 79 GAADAAPAQAEEKKEAAPAAAPAAAAA 105
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
3-76 |
7.48e-15 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 69.55 E-value: 7.48e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1485845380 3 VEIIMPKLGVDMQEGeIIEWKKQEGDVVNEGDVILEMMSDKTSMELEAEDSGILLKIVRGNGETVPVTEVIGYI 76
Cdd:pfam00364 1 TEIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
2-98 |
1.16e-13 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 73.70 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 2 AVEIIMPKLGvDMQEGEIIEWKKQEGDVVNEGDVILEMMSDKTSMELEAEDSGILLKIVRGNGETVPVTEVIGYIGAEGe 81
Cdd:PRK11855 119 VVEVKVPDIG-EITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAA- 196
|
90
....*....|....*..
gi 1485845380 82 vvDAGAAPKADVAQATA 98
Cdd:PRK11855 197 --AAPAAAAAPAAAAPA 211
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
315-552 |
2.87e-13 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 72.00 E-value: 2.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 315 GTEVTVVEMADRIIPG-MDREVSVELQKVLSKKGMKFLTSVGVSEIIeANNQLTIKLNDGSEIVSEKALLSIGRVPQLAG 393
Cdd:PRK09564 172 GKNVRIIQLEDRILPDsFDKEITDVMEEELRENGVELHLNEFVKSLI-GEDKVEGVVTDKGEYEADVVIVATGVKPNTEF 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 394 LENLNLE-MDRGRIKVNAYQETSIPGIYAPGD-------VNGTKM---LAHAAYRMGEVAAENaINGNHHKAKLDFTPAA 462
Cdd:PRK09564 251 LEDTGLKtLKNGAIIVDEYGETSIENIYAAGDcatiyniVSNKNVyvpLATTANKLGRMVGEN-LAGRHVSFKGTLGSAC 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 463 VYTHP-EIAMVGLTEDQARE---QYGNDILIGKC--SFTGNGRAIasneahgFVKVIADKKYHEILGVHIIGPV-AAEMI 535
Cdd:PRK09564 330 IKVLDlEAARTGLTEEEAKKlgiDYKTVFIKDKNhtNYYPGQEDL-------YVKLIYEADTKVILGGQIIGKKgAVLRI 402
|
250
....*....|....*..
gi 1485845380 536 NEAATIMESELTVDDVA 552
Cdd:PRK09564 403 DALAVAIYAKLTTQELG 419
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
3-103 |
5.77e-13 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]
Pssm-ID: 273565 [Multi-domain] Cd Length: 403 Bit Score: 70.92 E-value: 5.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 3 VEIIMPKLGVDMQEGEIIEWKKQEGDVVNEGDVILEMMSDKTSMELEAEDSGILLKIVRGNGETVPVTEVIGYIgAEGEV 82
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAIL-EEGND 79
|
90 100
....*....|....*....|.
gi 1485845380 83 VDAGAAPKADVAQATADLKAA 103
Cdd:TIGR01347 80 ATAAPPAKSGEEKEETPAASA 100
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
4-97 |
9.48e-13 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 70.65 E-value: 9.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 4 EIIMPKLGVDMQEGEIIEWKKQEGDVVNEGDVILEMMSDKTSMELEAEDSGILLKIVRGNG-ETVPVTEVIGYIGAEGEV 82
Cdd:PLN02744 114 EIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGaKEIKVGEVIAITVEEEED 193
|
90 100
....*....|....*....|...
gi 1485845380 83 VD--------AGAAPKADVAQAT 97
Cdd:PLN02744 194 IGkfkdykpsSSAAPAAPKAKPS 216
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
5-103 |
1.71e-12 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 69.33 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 5 IIMPKLGVDMQEGEIIEWKKQEGDVVNEGDVILEMMSDKTSMELEAEDSGILLKIVRGNGETVPVtevigyiGAEGEVVD 84
Cdd:PTZ00144 47 IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEV-------GAPLSEID 119
|
90
....*....|....*....
gi 1485845380 85 AGAAPKADVAQATADLKAA 103
Cdd:PTZ00144 120 TGGAPPAAAPAAAAAAKAE 138
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
239-444 |
1.12e-11 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 67.93 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 239 QVNPDKTVTIGS--QTIKGRSIVLATGSKVSRINIPGIDSKLVLTSDDILDLREI------PKTLTVMGGGVVGVELGLV 310
Cdd:TIGR02374 79 QIDTDQKQVITDagRTLSYDKLILATGSYPFILPIPGADKKGVYVFRTIEDLDAImamaqrFKKAAVIGGGLLGLEAAVG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 311 YASYGTEVTVVEMADRIIP-GMDREVSVELQKVLSKKGMKFLTSVGVSEIIEANNQLTIKLNDGSEIVSEKALLSIGRVP 389
Cdd:TIGR02374 159 LQNLGMDVSVIHHAPGLMAkQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVGATKADRIRFKDGSSLEADLIVMAAGIRP 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1485845380 390 QLAGLENLNLEMDRGrIKVNAYQETSIPGIYAPGDV---NGTKM-LAHAAYRMGEVAAE 444
Cdd:TIGR02374 239 NDELAVSAGIKVNRG-IIVNDSMQTSDPDIYAVGECaehNGRVYgLVAPLYEQAKVLAD 296
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
2-104 |
2.73e-11 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 66.18 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 2 AVEIIMPKLGVDmqEGEIIEWKKQEGDVVNEGDVILEMMSDKTSMELEAEDSGILLKIVRGNGETVPVTEVIGYIGAEGE 81
Cdd:PRK11854 105 AKDVHVPDIGSD--EVEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFEVAGE 182
|
90 100
....*....|....*....|...
gi 1485845380 82 VVDAGAAPKADVAQATADLKAAG 104
Cdd:PRK11854 183 APAAAPAAAEAAAPAAAPAAAAG 205
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
244-432 |
2.82e-11 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 65.32 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 244 KTVTIGSQTIKGRSIVLATGSKVSRINIPGidSKLVLTSDDILDLREIPKTLTVMGGGV------VGVELGLVYASYGTE 317
Cdd:PRK04965 89 QVVKSQGNQWQYDKLVLATGASAFVPPIPG--RELMLTLNSQQEYRAAETQLRDAQRVLvvggglIGTELAMDLCRAGKA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 318 VTVVEMADRIIPG-MDREVSVELQKVLSKKGMKFLTSVGVSEIIEANNQLTIKLNDGSEIVSEKALLSIGRVPQLAGLEN 396
Cdd:PRK04965 167 VTLVDNAASLLASlMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRATLDSGRSIEVDAVIAAAGLRPNTALARR 246
|
170 180 190
....*....|....*....|....*....|....*....
gi 1485845380 397 LNLEMDRGrIKVNAYQETSIPGIYAPGD---VNGtKMLA 432
Cdd:PRK04965 247 AGLAVNRG-IVVDSYLQTSAPDIYALGDcaeING-QVLP 283
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
2-103 |
2.84e-10 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 63.10 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 2 AVEIIMPKLGVDmqEGEIIEWKKQEGDVVNEGDVILEMMSDKTSMELEAEDSGILLKIVRGNGETVPVTEVIGYIGAEGE 81
Cdd:PRK11854 206 VKDVNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEGA 283
|
90 100
....*....|....*....|..
gi 1485845380 82 VVDAGAAPKADVAQATADLKAA 103
Cdd:PRK11854 284 APAAAPAKQEAAAPAPAAAKAE 305
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
311-373 |
5.44e-10 |
|
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: 56.06 E-value: 5.44e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1485845380 311 YASYGTEVTVVEMADRIIPGMDREVSVELQKVLSKKGMKFLTSVGVSEIIEANNQLTIKLNDG 373
Cdd:pfam00070 18 LARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLTDG 80
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
315-562 |
4.46e-09 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 59.03 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 315 GTEVTVVEMADRIIPGMDREVSVELQKVLSKKGMKFLTSVGVSEIIEANNQLTIKLNDGSEIVSEkallSIGRVPQLAGL 394
Cdd:PRK13512 171 GLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDAINGNEVTFKSGKVEHYDMIIE----GVGTHPNSKFI 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 395 ENLNLEMDR-GRIKVNAYQETSIPGIYAPGDV----------NGTKMLAHAAYRMGEVAAENaINGN---HHKAKL---- 456
Cdd:PRK13512 247 ESSNIKLDDkGFIPVNDKFETNVPNIYAIGDIitshyrhvdlPASVPLAWGAHRAASIVAEQ-IAGNdtiEFKGFLgnni 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 457 ----DFTPAAV------YTHPEIAMVGLTEDQAREQY-GNDILIGKCSFTGNGRAIASNEAHGfvKVIADKKyheilgvh 525
Cdd:PRK13512 326 vkffDYTFASVgvkpneLKQFDYKMVEVTQGAHANYYpGNSPLHLRVYYDTSNRKILRAAAVG--KEGADKR-------- 395
|
250 260 270
....*....|....*....|....*....|....*...
gi 1485845380 526 iigpvaaemINEAATIMESELTVDDVAA-SIHGHPTFS 562
Cdd:PRK13512 396 ---------IDVLSMAMMNQLTVDELTEfEVAYAPPYS 424
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
4-103 |
5.27e-07 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 52.57 E-value: 5.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 4 EIIMPKLGvDMQEGEIIEWKKQEGDVVNEGDVILEMMSDKTSMELEAEDSGILLKIVRGNGETVPVTEVIGYIGAEGEVV 83
Cdd:TIGR01348 2 EIKVPDIG-DNEEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLEVGAGAQ 80
|
90 100
....*....|....*....|....*.
gi 1485845380 84 D-----AGAAPKADV-AQATADLKAA 103
Cdd:TIGR01348 81 AqaeakKEAAPAPTAgAPAPAAQAQA 106
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
127-265 |
1.29e-06 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 51.04 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 127 YDMVVVGGGPAGYYAAIRGAQLGGKIAIVEK-----SEF----GGTC-LNKGCIPTKTYLKNaeildglkiAAGRGINLA 196
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKgkklgRKIlisgGGRCnVTNLSEEPDNFLSR---------YPGNPKFLK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 197 STNYTIDMDKTVDF--KNSV-VKTLTGG------------VQGLL---KANKVTIFNG---LG-QVNPD--KTVTIGSQT 252
Cdd:pfam03486 72 SALSRFTPWDFIAFfeSLGVpLKEEDHGrlfpdsdkasdiVDALLnelKELGVKIRLRtrvLSvEKDDDgrFRVKTGGEE 151
|
170
....*....|...
gi 1485845380 253 IKGRSIVLATGSK 265
Cdd:pfam03486 152 LEADSLVLATGGL 164
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
125-425 |
5.06e-06 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 49.39 E-value: 5.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 125 DEYDMVVVGGGPAGYYAAIRGAQLGGKIAIV-EKseFGGtclnkgciptktylknaEILDGLKIAagrgiNLASTNYTiD 203
Cdd:PRK15317 210 DPYDVLVVGGGPAGAAAAIYAARKGIRTGIVaER--FGG-----------------QVLDTMGIE-----NFISVPET-E 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 204 MDKTVDFKNSVVKTLTGGVQGLLKANKVTIFNGLgqvnpdKTVTIGS-QTIKGRSIVLATGSKVSRINIPGID------- 275
Cdd:PRK15317 265 GPKLAAALEEHVKEYDVDIMNLQRASKLEPAAGL------IEVELANgAVLKAKTVILATGARWRNMNVPGEDeyrnkgv 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 276 ------------SKLVLTsddI----------LDLREIPKtltvmgggvvgvelglvyasygtEVTVVEMADRIipgmdR 333
Cdd:PRK15317 339 aycphcdgplfkGKRVAV---IgggnsgveaaIDLAGIVK-----------------------HVTVLEFAPEL-----K 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 334 EVSVELQKVLSKKGMKFLTSVGVSEIIEANNQLT-IKLND-GSEIVSEKAL----LSIGRVPQ---LAGLENLNlemDRG 404
Cdd:PRK15317 388 ADQVLQDKLRSLPNVTIITNAQTTEVTGDGDKVTgLTYKDrTTGEEHHLELegvfVQIGLVPNtewLKGTVELN---RRG 464
|
330 340
....*....|....*....|.
gi 1485845380 405 RIKVNAYQETSIPGIYAPGDV 425
Cdd:PRK15317 465 EIIVDARGATSVPGVFAAGDC 485
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
131-427 |
6.95e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 48.99 E-value: 6.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 131 VVGGGPAGYYAAIRGAQLGGKIAIVEKSEFGGTCLNKGcIPTKTYLKNAeildglkiaagrginlastnytidMDKTVDF 210
Cdd:PRK13984 288 IVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGVMRYG-IPSYRLPDEA------------------------LDKDIAF 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 211 KNSV-VKTLTGGVQGllkankvtifnglgqvnpdKTVTIGSQTIKGRSIVLATGSKVSR-INIPGIDSKLVLTSDDILD- 287
Cdd:PRK13984 343 IEALgVKIHLNTRVG-------------------KDIPLEELREKHDAVFLSTGFTLGRsTRIPGTDHPDVIQALPLLRe 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 288 ----LR------EIPKTLTVMGGGVVGVELGLVYA-----SYGT-EVTVV-------EM-AD------------RIIPGM 331
Cdd:PRK13984 404 irdyLRgegpkpKIPRSLVVIGGGNVAMDIARSMArlqkmEYGEvNVKVTslertfeEMpADmeeieegleegvVIYPGW 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 332 D-REVSVELQKVlskKGMKFLTSVgvsEIIEANNQLTIKLNDGSEIVSEKALLS--IGRVPQLAGL-ENL--NLEMDRGR 405
Cdd:PRK13984 484 GpMEVVIENDKV---KGVKFKKCV---EVFDEEGRFNPKFDESDQIIVEADMVVeaIGQAPDYSYLpEELksKLEFVRGR 557
|
330 340
....*....|....*....|...
gi 1485845380 406 IKVNAYQETSIPGIYAPGD-VNG 427
Cdd:PRK13984 558 ILTNEYGQTSIPWLFAGGDiVHG 580
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
4-68 |
7.38e-06 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 43.97 E-value: 7.38e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1485845380 4 EIIMPKLGVDMQEGEIIEWKKQEGDVVNEGDVILEMMSDKTSMELEAEDSGILLKIVRGNGETVP 68
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVE 65
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
4-98 |
8.69e-06 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 48.72 E-value: 8.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 4 EIIMPKLGvDMQEGEIIEWKKQEGDVVNEGDVILEMMSDKTSMELEAEDSGILLKIVRGNGETVPVTEVIGYIGAEGEVV 83
Cdd:TIGR01348 118 EVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGSTP 196
|
90
....*....|....*
gi 1485845380 84 DAGAAPKADVAQATA 98
Cdd:TIGR01348 197 ATAPAPASAQPAAQS 211
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
125-163 |
1.17e-05 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 48.19 E-value: 1.17e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1485845380 125 DEYDMVVVGGGPAGYYAAIRGAQLGGKIAIVEKSEF-GGT 163
Cdd:PRK12843 15 AEFDVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYvGGT 54
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
372-448 |
1.33e-05 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 47.87 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 372 DGSEIV--SEKALLSIGRVPQLAGLEN---LNLEMDRGRIKVNAYQETSIPGIYAPGD-VNGTKMLAHAAyRMGEVAAEn 445
Cdd:PRK11749 368 EGSEFTlpADLVIKAIGQTPNPLILSTtpgLELNRWGTIIADDETGRTSLPGVFAGGDiVTGAATVVWAV-GDGKDAAE- 445
|
...
gi 1485845380 446 AIN 448
Cdd:PRK11749 446 AIH 448
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
128-163 |
2.99e-05 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 46.51 E-value: 2.99e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1485845380 128 DMVVVGGGPAGYYAAIRGAQLGGKIAIVEKSE-FGGT 163
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQpFGGA 37
|
|
| sdhA |
PRK07803 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
126-161 |
4.67e-05 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 236101 [Multi-domain] Cd Length: 626 Bit Score: 46.18 E-value: 4.67e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1485845380 126 EYDMVVVGGGPAGYYAAIRGAQLGGKIAIVEKSEFG 161
Cdd:PRK07803 8 SYDVVVIGAGGAGLRAAIEARERGLRVAVVCKSLFG 43
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
126-162 |
5.02e-05 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 45.98 E-value: 5.02e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1485845380 126 EYDMVVVGGGPAGYYAAIRGAQLGGKIAIVEKSEFGG 162
Cdd:COG1053 3 EYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRG 39
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
17-67 |
5.61e-05 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 41.25 E-value: 5.61e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1485845380 17 GEIIEWKKQEGDVVNEGDVILEMMSDKTSMELEAEDSGILLKIVRGNGETV 67
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQV 58
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
127-162 |
5.70e-05 |
|
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: 45.39 E-value: 5.70e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1485845380 127 YDMVVVGGGPAGYYAAIRGAQLGGKIAIVEKSEFGG 162
Cdd:TIGR02032 1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPR 36
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
125-183 |
1.20e-04 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 45.03 E-value: 1.20e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1485845380 125 DEYDMVVVGGGPAGYYAAIRGAQLGGKIAIVEKSE-FGGTCLNKGC---IPTKTYLKNAEILD 183
Cdd:PRK07843 6 QEYDVVVVGSGAAGMVAALTAAHRGLSTVVVEKAPhYGGSTARSGGgvwIPNNEVLKRAGVPD 68
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
128-264 |
1.28e-04 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 44.46 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 128 DMVVVGGGPAGYYAAIRGAQLGGKIAIVekSEFGGTCLNKGCIPT-----KTYLKnAEI--LDGL--------------- 185
Cdd:pfam01134 1 DVIVIGGGHAGCEAALAAARMGAKVLLI--THNTDTIAELSCNPSiggiaKGHLV-REIdaLGGLmgkaadktgiqfrml 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 186 ---KIAAGRGINLAstnytIDMDKtvdFKNSVVKTLTGgvqgllkANKVTIFNGLGQ---VNPDKT---VTIGSQTIKGR 256
Cdd:pfam01134 78 ntsKGPAVRALRAQ-----VDRDL---YSKEMTETLEN-------HPNLTLIQGEVTdliPENGKVkgvVTEDGEEYKAK 142
|
....*...
gi 1485845380 257 SIVLATGS 264
Cdd:pfam01134 143 AVVLATGT 150
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
317-448 |
1.38e-04 |
|
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: 44.74 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 317 EVTVVEMADRI-IPGMDREVSvelqkvLSKK-GMKFLTSVGVSEII-EANNQLT-IKLND------------------GS 374
Cdd:COG0493 281 SVTIVYRRTREeMPASKEEVE------EALEeGVEFLFLVAPVEIIgDENGRVTgLECVRmelgepdesgrrrpvpieGS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 375 EIV--SEKALLSIGRVPQLAGLEN-LNLEMD-RGRIKVNA-YQETSIPGIYAPGD-VNGTKMLAHAAyRMGEVAAEnAIN 448
Cdd:COG0493 355 EFTlpADLVILAIGQTPDPSGLEEeLGLELDkRGTIVVDEeTYQTSLPGVFAGGDaVRGPSLVVWAI-AEGRKAAR-AID 432
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
128-163 |
2.43e-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: 2.43e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1485845380 128 DMVVVGGGPAGYYAAIRGAQLGGKIAIVEKSEF-GGT 163
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRGFlGGM 37
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
126-163 |
6.30e-04 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 42.79 E-value: 6.30e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1485845380 126 EYDMVVVGGGPAGYYAAIRGAQLGGKIAIVEKS-EFGGT 163
Cdd:PRK06134 12 ECDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDpVFGGT 50
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
251-456 |
8.13e-04 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 42.41 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 251 QTIKGRSIVLATGSKVSRINIPGIDSKLVLTSDDILDLREIPKTLTVMGGGV------VGVELGLVYASYGTEVTVVEMA 324
Cdd:PRK14989 98 RTVFYDKLIMATGSYPWIPPIKGSETQDCFVYRTIEDLNAIEACARRSKRGAvvggglLGLEAAGALKNLGVETHVIEFA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 325 DRIIP-GMDREVSVELQKVLSKKGMKFLTSVGVSEII----EANNqlTIKLNDGSEIVSEKALLSIGRVPQ--LAGLENL 397
Cdd:PRK14989 178 PMLMAeQLDQMGGEQLRRKIESMGVRVHTSKNTLEIVqegvEARK--TMRFADGSELEVDFIVFSTGIRPQdkLATQCGL 255
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1485845380 398 NLEmDRGRIKVNAYQETSIPGIYAPGDV----NGTKMLAHAAYRMGEVAA------ENAINGNHHKAKL 456
Cdd:PRK14989 256 AVA-PRGGIVINDSCQTSDPDIYAIGECaswnNRVFGLVAPGYKMAQVAVdhllgsENAFEGADLSAKL 323
|
|
| TIGR00275 |
TIGR00275 |
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ... |
130-157 |
9.59e-04 |
|
flavoprotein, HI0933 family; The model when searched with a partial length search brings in proteins with a dinucleotide-binding motif (Rossman fold) over the initial 40 residues of the model, including oxidoreductases and dehydrogenases. Partially characterized members include an FAD-binding protein from Bacillus cereus and flavoprotein HI0933 from Haemophilus influenzae. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 272992 [Multi-domain] Cd Length: 400 Bit Score: 41.81 E-value: 9.59e-04
10 20
....*....|....*....|....*...
gi 1485845380 130 VVVGGGPAGYYAAIRGAQLGGKIAIVEK 157
Cdd:TIGR00275 1 IIIGGGAAGLMAAITAARAGLSVLLLEK 28
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
125-163 |
1.04e-03 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 41.99 E-value: 1.04e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1485845380 125 DEYDMVVVGGGPAGYYAAIRGAQLGGKIAIVEKSE-FGGT 163
Cdd:PRK12842 8 LTCDVLVIGSGAGGLSAAITARKLGLDVVVLEKEPvFGGT 47
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
125-163 |
1.04e-03 |
|
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: 41.77 E-value: 1.04e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1485845380 125 DEYDMVVVGGGPAGYYAAIRGAQLGGKIAIVEK-SEFGGT 163
Cdd:COG2072 5 EHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKaDDVGGT 44
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
126-170 |
1.11e-03 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 41.76 E-value: 1.11e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1485845380 126 EYDMVVVGGGPAGYYAAIRGAQLGGKIAIVEKSEfGGTCLNKGCI 170
Cdd:PRK05329 2 KFDVLVIGGGLAGLTAALAAAEAGKRVALVAKGQ-GALHFSSGSI 45
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
281-500 |
2.04e-03 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 40.68 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 281 TSDDILDLREI---PKTLTVMGGGVVGVELGLVYASYGTEVTVVEMADRIipgMDREVSVELQKVL----SKKGMKFLTS 353
Cdd:PRK09754 130 HAGDAARLREVlqpERSVVIVGAGTIGLELAASATQRRCKVTVIELAATV---MGRNAPPPVQRYLlqrhQQAGVRILLN 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 354 VGVSEIIEAnNQLTIKLNDGSEIVSEKALLSIGRV--PQLAglENLNLEMDRGrIKVNAYQETSIPGIYAPGDVNGTKML 431
Cdd:PRK09754 207 NAIEHVVDG-EKVELTLQSGETLQADVVIYGIGISanDQLA--REANLDTANG-IVIDEACRTCDPAIFAGGDVAITRLD 282
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1485845380 432 AHAAYRmgevaAENAINGNHHkakldftpAAVYTHpeiAMVGLTEDQA------REQYGNDIligkcSFTGNGRA 500
Cdd:PRK09754 283 NGALHR-----CESWENANNQ--------AQIAAA---AMLGLPLPLLpppwfwSDQYSDNL-----QFIGDMRG 336
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
17-39 |
3.18e-03 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 36.69 E-value: 3.18e-03
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
3-98 |
3.47e-03 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 40.12 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845380 3 VEIIMPKLGVDMQEGEIIEWKKQEGDVVNEGDVILEMMSDKTSMELEAEDSGILLKIVRGNGETVPVTEVIGYIGAEGEV 82
Cdd:PLN02226 92 VEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSEDA 171
|
90
....*....|....*.
gi 1485845380 83 VdAGAAPKADVAQATA 98
Cdd:PLN02226 172 A-SQVTPSQKIPETTD 186
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
126-162 |
3.49e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 40.20 E-value: 3.49e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1485845380 126 EYDMVVVGGGPAGYYAAIRGAQLGGKIAIVEKSEFGG 162
Cdd:PRK12839 8 TYDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKASTCG 44
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
14-73 |
3.84e-03 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 40.21 E-value: 3.84e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1485845380 14 MQeGEIIEWKKQEGDVVNEGDV--ILEMMsdKTSMELEAEDSGILLKIVRGNGETVPVTEVI 73
Cdd:PRK09282 529 MP-GTVVKVKVKEGDKVKAGDTvlVLEAM--KMENEIQAPVDGTVKEILVKEGDRVNPGDVL 587
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
24-78 |
9.69e-03 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 35.37 E-value: 9.69e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1485845380 24 KQEGDVVNEGDVI--LEMMsdKTSMELEAEDSGILLKIVRGNGETVPVTEVIGYIGA 78
Cdd:PRK07051 26 VEVGDAVAAGDVVglIEVM--KQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIEE 80
|
|
| |
