|
Name |
Accession |
Description |
Interval |
E-value |
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
137-600 |
0e+00 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 583.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 137 DIECKMVVLGAGLGGYTAAFRAADLGLDTVLIERYAsLGGVCLNVGCIPSKALLHAAAVIDEVAHAGDFGVDFGQPKITL 216
Cdd:COG1249 1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGR-LGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISAGAPSVDW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 217 DKLREYKEKVVGKLTGGLASMAKQRKVRTVTGVASFVSPNELEIVGDdgktQLLRFEHCIIAAGSQAVKLPNFPWDDKRV 296
Cdd:COG1249 80 AALMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVTGG----ETLTADHIVIATGSRPRVPPIPGLDEVRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 297 MDSTDALELHDIPKTLLVVGGGIIGLEMATVYSALGSKVTVVEFMDQLMPGADKDLVKPLADRLKKQGVEVHLKTKATDV 376
Cdd:COG1249 156 LTSDEALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 377 KADKSGITVSFEAavegeKPGLQATAYDRVLVAVGRSPNGKKIGAEKAGVTITERGFIPVDRQMRTNVPHIFAIGDIVGN 456
Cdd:COG1249 236 EKTGDGVTVTLED-----GGGEEAVEADKVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRTSVPGIYAIGDVTGG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 457 PMLAHKATHEGKLAAEVAAGEKKEWV-ARVIPSVAYTNPEIAWVGVTETEAKAKGLKVGVAKFPWAASGRAIGIGRTEGF 535
Cdd:COG1249 311 PQLAHVASAEGRVAAENILGKKPRPVdYRAIPSVVFTDPEIASVGLTEEEAREAGIDVKVGKFPFAANGRALALGETEGF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2746980421 536 TKLIFDEQTHRVIGGAIVGVHAGDLLAEIGLAIEMGAEAEDIGHTIHAHPTLSESVGMAAEVYDG 600
Cdd:COG1249 391 VKLIADAETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAALALLG 455
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
136-601 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 543.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 136 ADIECKMVVLGAGLGGYTAAFRAADLGLDTVLIERyASLGGVCLNVGCIPSKALLHAAAVIDEVAHAGDFGVDFGQPKIT 215
Cdd:PRK06416 1 FAFEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEK-EKLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIKAENVGID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 216 LDKLREYKEKVVGKLTGGLASMAKQRKVRTVTGVASFVSPNELEiVGDDGKTQLLRFEHCIIAAGSQAVKLPNFPWDDKR 295
Cdd:PRK06416 80 FKKVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVR-VMTEDGEQTYTAKNIILATGSRPRELPGIEIDGRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 296 VMDSTDALELHDIPKTLLVVGGGIIGLEMATVYSALGSKVTVVEFMDQLMPGADKDLVKPLADRLKKQGVEVHLKTKATD 375
Cdd:PRK06416 159 IWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPGEDKEISKLAERALKKRGIKIKTGAKAKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 376 VKADKSGITVSFEAAVEGEKpgLQAtayDRVLVAVGRSPNGKKIGAEKAGVTiTERGFIPVDRQMRTNVPHIFAIGDIVG 455
Cdd:PRK06416 239 VEQTDDGVTVTLEDGGKEET--LEA---DYVLVAVGRRPNTENLGLEELGVK-TDRGFIEVDEQLRTNVPNIYAIGDIVG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 456 NPMLAHKATHEGKLAAEVAAGEKKEWVARVIPSVAYTNPEIAWVGVTETEAKAKGLKVGVAKFPWAASGRAIGIGRTEGF 535
Cdd:PRK06416 313 GPMLAHKASAEGIIAAEAIAGNPHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFDVKVVKFPFAGNGKALALGETDGF 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2746980421 536 TKLIFDEQTHRVIGGAIVGVHAGDLLAEIGLAIEMGAEAEDIGHTIHAHPTLSESVGMAAEVYDGT 601
Cdd:PRK06416 393 VKLIFDKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEALGEAALAAAGK 458
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
143-600 |
3.54e-172 |
|
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: 497.17 E-value: 3.54e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 143 VVLGAGLGGYTAAFRAADLGLDTVLIERyASLGGVCLNVGCIPSKALLHAAAVIDEVAHAGDFGVDFGQPKITLDKLREY 222
Cdd:TIGR01350 5 IVIGGGPGGYVAAIRAAQLGLKVALVEK-EYLGGTCLNVGCIPTKALLHSAEVYDEIKHAKDLGIEVENVSVDWEKMQKR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 223 KEKVVGKLTGGLASMAKQRKVRTVTGVASFVSPNELEIVGDDGkTQLLRFEHCIIAAGSQAVKLPN-FPWDDKRVMDSTD 301
Cdd:TIGR01350 84 KNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGENG-EETLEAKNIIIATGSRPRSLPGpFDFDGKVVITSTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 302 ALELHDIPKTLLVVGGGIIGLEMATVYSALGSKVTVVEFMDQLMPGADKDLVKPLADRLKKQGVEVHLKTKATDVKADKS 381
Cdd:TIGR01350 163 ALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEKNDD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 382 GITVSFEaavegeKPGLQATAYDRVLVAVGRSPNGKKIGAEKAGVTITERGFIPVDRQMRTNVPHIFAIGDIVGNPMLAH 461
Cdd:TIGR01350 243 QVTYENK------GGETETLTGEKVLVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDVIGGPMLAH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 462 KATHEGKLAAEVAAGEKKEWV-ARVIPSVAYTNPEIAWVGVTETEAKAKGLKVGVAKFPWAASGRAIGIGRTEGFTKLIF 540
Cdd:TIGR01350 317 VASHEGIVAAENIAGKEPAHIdYDAVPSVIYTDPEVASVGLTEEQAKEAGYDVKIGKFPFAANGKALALGETDGFVKIIA 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 541 DEQTHRVIGGAIVGVHAGDLLAEIGLAIEMGAEAEDIGHTIHAHPTLSESVGMAAEVYDG 600
Cdd:TIGR01350 397 DKKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEAIKEAALAALG 456
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
143-595 |
4.23e-161 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 469.41 E-value: 4.23e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 143 VVLGAGLGGYTAAFRAADLGLDTVLIERY------ASLGGVCLNVGCIPSKALLHAAAVIDEVAHA-GDFGVDFGQPKIT 215
Cdd:PRK06327 8 VVIGAGPGGYVAAIRAAQLGLKVACIEAWknpkgkPALGGTCLNVGCIPSKALLASSEEFENAGHHfADHGIHVDGVKID 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 216 LDKLREYKEKVVGKLTGGLASMAKQRKVRTVTGVASFVS----PNELEIVGDDGKTqlLRFEHCIIAAGSQAVKLPNFPW 291
Cdd:PRK06327 88 VAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVGktdaGYEIKVTGEDETV--ITAKHVIIATGSEPRHLPGVPF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 292 DDKRVMDSTDALELHDIPKTLLVVGGGIIGLEMATVYSALGSKVTVVEFMDQLMPGADKDLVKPLADRLKKQGVEVHLKT 371
Cdd:PRK06327 166 DNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAAADEQVAKEAAKAFTKQGLDIHLGV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 372 KATDVKADKSGITVsfeaAVEGEKPGLQATAYDRVLVAVGRSPNGKKIGAEKAGVTITERGFIPVDRQMRTNVPHIFAIG 451
Cdd:PRK06327 246 KIGEIKTGGKGVSV----AYTDADGEAQTLEVDKLIVSIGRVPNTDGLGLEAVGLKLDERGFIPVDDHCRTNVPNVYAIG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 452 DIVGNPMLAHKATHEGKLAAEVAAGEKKEWVARVIPSVAYTNPEIAWVGVTETEAKAKGLKVGVAKFPWAASGRAIGIGR 531
Cdd:PRK06327 322 DVVRGPMLAHKAEEEGVAVAERIAGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLKAEGVEYKAGKFPFMANGRALAMGE 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2746980421 532 TEGFTKLIFDEQTHRVIGGAIVGVHAGDLLAEIGLAIEMGAEAEDIGHTIHAHPTLSESVGMAA 595
Cdd:PRK06327 402 PDGFVKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEVWHEAA 465
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
143-595 |
2.27e-144 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 426.13 E-value: 2.27e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 143 VVLGAGLGGYTAAFRAADLGLDTVLIERyASLGGVCLNVGCIPSKALLHAAAVIDEVAHAGDFGVDFGQPKITLDKLREY 222
Cdd:PRK06292 7 IVIGAGPAGYVAARRAAKLGKKVALIEK-GPLGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHADGPKIDFKKVMAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 223 KEKVVGKLTGG-LASMAKQRKVRTVTGVASFVSPNELEIvgddgKTQLLRFEHCIIAAGSqavKLPNFP----WDDKRVM 297
Cdd:PRK06292 86 VRRERDRFVGGvVEGLEKKPKIDKIKGTARFVDPNTVEV-----NGERIEAKNIVIATGS---RVPPIPgvwlILGDRLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 298 DSTDALELHDIPKTLLVVGGGIIGLEMATVYSALGSKVTVVEFMDQLMPGADKDLVKPLADRLKKQgVEVHLKTKATDVK 377
Cdd:PRK06292 158 TSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILSKE-FKIKLGAKVTSVE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 378 ADKSGITVSFEaaVEGEKPGLQAtayDRVLVAVGRSPNGKKIGAEKAGVTITERGFIPVDRQMRTNVPHIFAIGDIVGNP 457
Cdd:PRK06292 237 KSGDEKVEELE--KGGKTETIEA---DYVLVATGRRPNTDGLGLENTGIELDERGRPVVDEHTQTSVPGIYAAGDVNGKP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 458 MLAHKATHEGKLAAEVAAGEKKEWVAR-VIPSVAYTNPEIAWVGVTETEAKAKGLKVGVAKFPWAASGRAIGIGRTEGFT 536
Cdd:PRK06292 312 PLLHEAADEGRIAAENAAGDVAGGVRYhPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEVPFEAQGRARVMGKNDGFV 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2746980421 537 KLIFDEQTHRVIGGAIVGVHAGDLLAEIGLAIEMGAEAEDIGHTIHAHPTLSESVGMAA 595
Cdd:PRK06292 392 KVYADKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRTAL 450
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
143-602 |
1.12e-114 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 349.89 E-value: 1.12e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 143 VVLGAGLGGYTAAFRAADLGLDTVLIERyASLGGVCLNVGCIPSKALLHAAAVIDEVAHAGDFGVDFGQP-KITLDKLRE 221
Cdd:PRK06370 9 IVIGAGQAGPPLAARAAGLGMKVALIER-GLLGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGGPvSVDFKAVMA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 222 YKEKVVGKLTGGLAS-MAKQRKVRTVTGVASFVSPNELEiVGDdgktQLLRFEHCIIAAGSQAVKlPNFP-WDDKRVMDS 299
Cdd:PRK06370 88 RKRRIRARSRHGSEQwLRGLEGVDVFRGHARFESPNTVR-VGG----ETLRAKRIFINTGARAAI-PPIPgLDEVGYLTN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 300 TDALELHDIPKTLLVVGGGIIGLEMATVYSALGSKVTVVEFMDQLMPGADKDLVKPLADRLKKQGVEVHLKTKATDVKAD 379
Cdd:PRK06370 162 ETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILEREGIDVRLNAECIRVERD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 380 KSGITVSFEaaVEGEKPGLQAtayDRVLVAVGRSPNGKKIGAEKAGVTITERGFIPVDRQMRTNVPHIFAIGDIVGNPML 459
Cdd:PRK06370 242 GDGIAVGLD--CNGGAPEITG---SHILVAVGRVPNTDDLGLEAAGVETDARGYIKVDDQLRTTNPGIYAAGDCNGRGAF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 460 AHKATHEGKLAAEVAAGEKKEWVA-RVIPSVAYTNPEIAWVGVTETEAKAKGLKVGVAKFPWAASGRAIGIGRTEGFTKL 538
Cdd:PRK06370 317 THTAYNDARIVAANLLDGGRRKVSdRIVPYATYTDPPLARVGMTEAEARKSGRRVLVGTRPMTRVGRAVEKGETQGFMKV 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2746980421 539 IFDEQTHRVIGGAIVGVHAGDLLAEIGLAIEMGAEAEDIGHTIHAHPTLSESVGMAAEVYDGTI 602
Cdd:PRK06370 397 VVDADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIPTLAQALRRTR 460
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
142-595 |
5.02e-97 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 304.39 E-value: 5.02e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 142 MVVLGAGLGGYTAAFRAADLGLDTVLIERYASLGGVCLNVGCIPSKALLHAAAVIDEvAHAGDFGVDFGQPK-ITLDKLR 220
Cdd:PRK05249 8 LVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGGGCTHTGTIPSKALREAVLRLIG-FNQNPLYSSYRVKLrITFADLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 221 EYKEKVVGKLTGGLASMAKQRKVRTVTGVASFVSPNELEIVGDDGKTQLLRFEHCIIAAGSQAVKLPNFPWDDKRVMDST 300
Cdd:PRK05249 87 ARADHVINKQVEVRRGQYERNRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATGSRPYRPPDVDFDHPRIYDSD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 301 DALELHDIPKTLLVVGGGIIGLEMATVYSALGSKVTVVEFMDQLMPGADKDLVKPLADRLKKQGVEVHLKTKATDVKADK 380
Cdd:PRK05249 167 SILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSFLDDEISDALSYHLRDSGVTIRHNEEVEKVEGGD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 381 SGITVSFEAaveGEKpgLQAtayDRVLVAVGRSPNGKKIGAEKAGVTITERGFIPVDRQMRTNVPHIFAIGDIVGNPMLA 460
Cdd:PRK05249 247 DGVIVHLKS---GKK--IKA---DCLLYANGRTGNTDGLNLENAGLEADSRGQLKVNENYQTAVPHIYAVGDVIGFPSLA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 461 HKATHEGKLAAEVAAGEKKEWVARVIPSVAYTNPEIAWVGVTETEAKAKGL--KVGVAKFPWAAsgRAIGIGRTEGFTKL 538
Cdd:PRK05249 319 SASMDQGRIAAQHAVGEATAHLIEDIPTGIYTIPEISSVGKTEQELTAAKVpyEVGRARFKELA--RAQIAGDNVGMLKI 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2746980421 539 IFDEQTHRVIGGAIVGVHAGDLLaEIGLAI-EMGAEAEDIGHTIHAHPTLSESVGMAA 595
Cdd:PRK05249 397 LFHRETLEILGVHCFGERATEII-HIGQAImEQKGTIEYFVNTTFNYPTMAEAYRVAA 453
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
142-605 |
4.17e-86 |
|
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: 276.23 E-value: 4.17e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 142 MVVLGAGLGGYTAAFRAADLGLDTVLIERyASLGGVCLNVGCIPSKALLHAAAVIDeVAHAGDFGVDFGQPKITLDKLRE 221
Cdd:TIGR02053 3 LVIIGSGAAAFAAAIKAAELGASVAMVER-GPLGGTCVNVGCVPSKMLLRAAEVAH-YARKPPFGGLAATVAVDFGELLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 222 YKEKVVGKL-TGGLASMAKQRKVRTVTGVASFVSPNELEIvgdDGKTQLLRFEHCIIAAGSQAVKlPNFP-WDDKRVMDS 299
Cdd:TIGR02053 81 GKREVVEELrHEKYEDVLSSYGVDYLRGRARFKDPKTVKV---DLGREVRGAKRFLIATGARPAI-PPIPgLKEAGYLTS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 300 TDALELHDIPKTLLVVGGGIIGLEMATVYSALGSKVTVVEFMDQLMPGADKDLVKPLADRLKKQGVEVHLKTKATDVKAD 379
Cdd:TIGR02053 157 EEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSDRLLPREEPEISAAVEEALAEEGIEVVTSAQVKAVSVR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 380 KSGITVSFeaavegEKPGLQATA-YDRVLVAVGRSPNGKKIGAEKAGVTITERGFIPVDRQMRTNVPHIFAIGDIVGNPM 458
Cdd:TIGR02053 237 GGGKIITV------EKPGGQGEVeADELLVATGRRPNTDGLGLEKAGVKLDERGGILVDETLRTSNPGIYAAGDVTGGLQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 459 LAHKATHEGKLAAEVA-AGEKKEWVARVIPSVAYTNPEIAWVGVTETEAKAKGLKVGVAKFPWAASGRAIGIGRTEGFTK 537
Cdd:TIGR02053 311 LEYVAAKEGVVAAENAlGGANAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNVPRARINRDTRGFIK 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2746980421 538 LIFDEQTHRVIGGAIVGVHAGDLLAEIGLAIEMGAEAEDIGHTIHAHPTLSESVGMAAEVYDGTITDL 605
Cdd:TIGR02053 391 LVAEPGTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGLKLAAQTFYRDVSKL 458
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
134-594 |
7.39e-81 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 267.94 E-value: 7.39e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 134 KPADIECKMVVLGAGLGGYTAAFRAADLGLDTVLIE-RYASLGGVCLNVGCIPSKALLHAAAVIDEV---AHAGDFGVDF 209
Cdd:PTZ00153 111 NFSDEEYDVGIIGCGVGGHAAAINAMERGLKVIIFTgDDDSIGGTCVNVGCIPSKALLYATGKYRELknlAKLYTYGIYT 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 210 ------------------GQPKITLDKLREYKEKVVGKLTGGLASMAKQRKV-RTVTGVASFVSPNEL---EIVGDDGKT 267
Cdd:PTZ00153 191 nafkngkndpvernqlvaDTVQIDITKLKEYTQSVIDKLRGGIENGLKSKKFcKNSEHVQVIYERGHIvdkNTIKSEKSG 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 268 QLLRFEHCIIAAGSqavkLPNFP----WDDKRVMDSTDALELHDIPKTLLVVGGGIIGLEMATVYSALGSKVTVVEFMDQ 343
Cdd:PTZ00153 271 KEFKVKNIIIATGS----TPNIPdnieVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSPQ 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 344 LMPGADKDLVKpLADR--LKKQGVEVHLKTKATDVKADKSG--ITVSFEAAVEGE--KPGLQATAY-----DRVLVAVGR 412
Cdd:PTZ00153 347 LLPLLDADVAK-YFERvfLKSKPVRVHLNTLIEYVRAGKGNqpVIIGHSERQTGEsdGPKKNMNDIketyvDSCLVATGR 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 413 SPNGKKIGAEKAGVTiTERGFIPVDRQMRTN------VPHIFAIGDIVGNPMLAHKATHEGKLAAEVAAGEKKE------ 480
Cdd:PTZ00153 426 KPNTNNLGLDKLKIQ-MKRGFVSVDEHLRVLredqevYDNIFCIGDANGKQMLAHTASHQALKVVDWIEGKGKEnvninv 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 481 --WVARV-----IPSVAYTNPEIAWVGVTETEAKAKGLK--VGVAKFPWAASGRAI----------------------GI 529
Cdd:PTZ00153 505 enWASKPiiyknIPSVCYTTPELAFIGLTEKEAKELYPPdnVGVEISFYKANSKVLcennisfpnnsknnsynkgkynTV 584
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2746980421 530 GRTEGFTKLIFDEQTHRVIGGAIVGVHAGDLLAEIGLAIEMGAEAEDIGHTIHAHPTLSESVGMA 594
Cdd:PTZ00153 585 DNTEGMVKIVYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDAA 649
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
144-589 |
8.92e-74 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 243.14 E-value: 8.92e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 144 VLGAGLGGYTAAFRAADLGLDTVLIERYAsLGGVCLNVGCIPSKALLHAAAVIDEVAH-AGDFGVDFGQPKITLDKLREY 222
Cdd:PRK06116 9 VIGGGSGGIASANRAAMYGAKVALIEAKR-LGGTCVNVGCVPKKLMWYGAQIAEAFHDyAPGYGFDVTENKFDWAKLIAN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 223 KEKVVGKLTGGLASMAKQRKVRTVTGVASFVSPNELEIVGddgktQLLRFEHCIIAAGSQAVKlPNFPWDDkRVMDSTDA 302
Cdd:PRK06116 88 RDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNG-----ERYTADHILIATGGRPSI-PDIPGAE-YGITSDGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 303 LELHDIPKTLLVVGGGIIGLEMATVYSALGSKVTVVEFMDQLMPGADKDLVKPLADRLKKQGVEVHLKTKATDV-KADKS 381
Cdd:PRK06116 161 FALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVeKNADG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 382 GITVSFEAavegekpGLQATAyDRVLVAVGRSPNGKKIGAEKAGVTITERGFIPVDRQMRTNVPHIFAIGDIVGNPMLAH 461
Cdd:PRK06116 241 SLTLTLED-------GETLTV-DCLIWAIGREPNTDGLGLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGDVTGRVELTP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 462 KATHEGKLAAEVAAGEKKEwvARV----IPSVAYTNPEIAWVGVTETEAKAKG----LKVGVAKFpwAASGRAIGIGRTE 533
Cdd:PRK06116 313 VAIAAGRRLSERLFNNKPD--EKLdysnIPTVVFSHPPIGTVGLTEEEAREQYgednVKVYRSSF--TPMYTALTGHRQP 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2746980421 534 GFTKLIFDEQTHRVIGGAIVGVHAGDLLAEIGLAIEMGAEAEDIGHTIHAHPTLSE 589
Cdd:PRK06116 389 CLMKLVVVGKEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAE 444
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
143-467 |
3.67e-71 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 231.44 E-value: 3.67e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 143 VVLGAGLGGYTAAFRAADLGLDTVLIEryasLGGVCLNVGCIPSKALLHAAAVIDEVAHAGDfgvdfgqpkitldkLREY 222
Cdd:pfam07992 4 VVIGGGPAGLAAALTLAQLGGKVTLIE----DEGTCPYGGCVLSKALLGAAEAPEIASLWAD--------------LYKR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 223 KEKVVGKLTGGLASMAKQRKVRTVTGVASFVSPNEleivgDDGKTQLLRFEHCIIAAGSQAVKLP-----NFPWDDKRVM 297
Cdd:pfam07992 66 KEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEEL-----VDGDGETITYDRLVIATGARPRLPPipgveLNVGFLVRTL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 298 DSTDALELHDIPKTLLVVGGGIIGLEMATVYSALGSKVTVVEFMDQLMPGADKDLVKPLADRLKKQGVEVHLKTKATDVK 377
Cdd:pfam07992 141 DSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEII 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 378 ADKSGITVSFEaavEGEKpglqaTAYDRVLVAVGRSPNgkKIGAEKAGVTITERGFIPVDRQMRTNVPHIFAIGDI-VGN 456
Cdd:pfam07992 221 GDGDGVEVILK---DGTE-----IDADLVVVAIGRRPN--TELLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDCrVGG 290
|
330
....*....|.
gi 2746980421 457 PMLAHKATHEG 467
Cdd:pfam07992 291 PELAQNAVAQG 301
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
141-595 |
8.56e-68 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 227.82 E-value: 8.56e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 141 KMVVLGAGLGGYTAAFRAADLGLDTVLIERyASLGGVCLNVGCIPSKALLHAAAVIDEVAHAGDFGV---DFGQPKITLD 217
Cdd:PRK07845 3 RIVIIGGGPGGYEAALVAAQLGADVTVIER-DGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIrfiDDGEARVDLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 218 KLREYKEKVVGKLTGGLASMAKQRKVRTVTGVASF----VSPNELEIVGDDGKTQLLRFEHCIIAAGSQAVKLPNFPWDD 293
Cdd:PRK07845 82 AVNARVKALAAAQSADIRARLEREGVRVIAGRGRLidpgLGPHRVKVTTADGGEETLDADVVLIATGASPRILPTAEPDG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 294 KRVMDSTDALELHDIPKTLLVVGGGIIGLEMATVYSALGSKVTVVEFMDQLMPGADKDLVKPLADRLKKQGVEVHLKTKA 373
Cdd:PRK07845 162 ERILTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPGEDADAAEVLEEVFARRGMTVLKRSRA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 374 TDVKADKSGITVSFE--AAVEGEkpglqataydRVLVAVGRSPNGKKIGAEKAGVTITERGFIPVDRQMRTNVPHIFAIG 451
Cdd:PRK07845 242 ESVERTGDGVVVTLTdgRTVEGS----------HALMAVGSVPNTAGLGLEEAGVELTPSGHITVDRVSRTSVPGIYAAG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 452 DIVGNPMLAHKATHEGKLAAEVAAGE-----KKEWVArvipSVAYTNPEIAWVGVTETEAKAKGLKVGVAKFPWAASGRA 526
Cdd:PRK07845 312 DCTGVLPLASVAAMQGRIAMYHALGEavsplRLKTVA----SNVFTRPEIATVGVSQAAIDSGEVPARTVMLPLATNPRA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2746980421 527 IGIGRTEGFTKLIFDEQTHRVIGGAIVGVHAGDLLAEIGLAIEMGAEAEDIGHTIHAHPTLSESVGMAA 595
Cdd:PRK07845 388 KMSGLRDGFVKLFCRPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYPSLSGSITEAA 456
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
142-591 |
7.46e-67 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 224.83 E-value: 7.46e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 142 MVVLGAGLGGYTAAFRAADLglDTVLIERyASLGGVCLNVGCIPSKALLHAAAVIDEVAHAGDFGVDFGQPKITLDKLRE 221
Cdd:PRK07846 4 LIIIGTGSGNSILDERFADK--RIAIVEK-GTFGGTCLNVGCIPTKMFVYAADVARTIREAARLGVDAELDGVRWPDIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 222 ykeKVVGKL----TGGLASMAKQRKVRTV-TGVASFVSPNELEiVGDDGktqLLRFEHCIIAAGSQAVKLPNFPWDDKRV 296
Cdd:PRK07846 81 ---RVFGRIdpiaAGGEEYRGRDTPNIDVyRGHARFIGPKTLR-TGDGE---EITADQVVIAAGSRPVIPPVIADSGVRY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 297 MDSTDALELHDIPKTLLVVGGGIIGLEMATVYSALGSKVTVVEFMDQLMPGADKDLVKPLADrLKKQGVEVHLKTKATDV 376
Cdd:PRK07846 154 HTSDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLDDDISERFTE-LASKRWDVRLGRNVVGV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 377 KADKSGITVSF--EAAVEGekpglqatayDRVLVAVGRSPNGKKIGAEKAGVTITERGFIPVDRQMRTNVPHIFAIGDIV 454
Cdd:PRK07846 233 SQDGSGVTLRLddGSTVEA----------DVLLVATGRVPNGDLLDAAAAGVDVDEDGRVVVDEYQRTSAEGVFALGDVS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 455 GNPMLAHKATHEGKLAAE--VAAGEKKEWVARVIPSVAYTNPEIAWVGVTETEAKAKGLK--VGVAKFPWAASGRAigIG 530
Cdd:PRK07846 303 SPYQLKHVANHEARVVQHnlLHPDDLIASDHRFVPAAVFTHPQIASVGLTENEARAAGLDitVKVQNYGDVAYGWA--ME 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2746980421 531 RTEGFTKLIFDEQTHRVIGGAIVGVHAGDLLAEIGLAIEMGAEAEDIGHTIH-AHPTLSESV 591
Cdd:PRK07846 381 DTTGFVKLIADRDTGRLLGAHIIGPQASTLIQPLIQAMSFGLDAREMARGQYwIHPALPEVV 442
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
142-589 |
5.06e-65 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 219.62 E-value: 5.06e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 142 MVVLGAGLGGYTAAFRAADLGLDTVLIERYASL-GGVCLNVGCIPSKALLHAAavidevahagdfgvdfgQPKITLDKLR 220
Cdd:PRK07251 6 LIVIGFGKAGKTLAAKLASAGKKVALVEESKAMyGGTCINIGCIPTKTLLVAA-----------------EKNLSFEQVM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 221 EYKEKVVGKLTGGLASMAKQRKVRTVTGVASFVSPNELEIVGDDGKtQLLRFEHCIIAAGSQAVKLPnFPW--DDKRVMD 298
Cdd:PRK07251 69 ATKNTVTSRLRGKNYAMLAGSGVDLYDAEAHFVSNKVIEVQAGDEK-IELTAETIVINTGAVSNVLP-IPGlaDSKHVYD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 299 STDALELHDIPKTLLVVGGGIIGLEMATVYSALGSKVTVVEFMDQLMPGADKDLVKPLADRLKKQGVEVHLKTKATDVKA 378
Cdd:PRK07251 147 STGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYMEEDGITFLLNAHTTEVKN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 379 DKSGITVSFEAavegekpglQATAYDRVLVAVGRSPNGKKIGAEKAGVTITERGFIPVDRQMRTNVPHIFAIGDIVGNPM 458
Cdd:PRK07251 227 DGDQVLVVTED---------ETYRFDALLYATGRKPNTEPLGLENTDIELTERGAIKVDDYCQTSVPGVFAVGDVNGGPQ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 459 LAHKATHEGKLAAEVAAGEKKEWVA--RVIPSVAYTNPEIAWVGVTETEAKAKGLKVGVAKFPWAASGRAIGIGRTEGFT 536
Cdd:PRK07251 298 FTYISLDDFRIVFGYLTGDGSYTLEdrGNVPTTMFITPPLSQVGLTEKEAKEAGLPYAVKELLVAAMPRAHVNNDLRGAF 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2746980421 537 KLIFDEQTHRVIGGAIVGVHAGDLLAEIGLAIEMGAEAEDIGHTIHAHPTLSE 589
Cdd:PRK07251 378 KVVVNTETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAE 430
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
143-605 |
4.86e-59 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 206.93 E-value: 4.86e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 143 VVLGAGLGGYTAAFRAADLGLDTVLIERyASLGGVCLNVGCIPSKALLHAAavidEVAHAG-----DFGVDFGQPKITLD 217
Cdd:PRK13748 102 AVIGSGGAAMAAALKAVEQGARVTLIER-GTIGGTCVNVGCVPSKIMIRAA----HIAHLRrespfDGGIAATVPTIDRS 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 218 KLREYKEKVV-----GKLTGGLASmakQRKVRTVTGVASFVSPNELEIVGDDGKTQLLRFEHCIIAAGSQAvKLPNFP-W 291
Cdd:PRK13748 177 RLLAQQQARVdelrhAKYEGILDG---NPAITVLHGEARFKDDQTLIVRLNDGGERVVAFDRCLIATGASP-AVPPIPgL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 292 DDKRVMDSTDALELHDIPKTLLVVGGGIIGLEMATVYSALGSKVTVVEfMDQLMPGADKDLVKPLADRLKKQGVEVHLKT 371
Cdd:PRK13748 253 KETPYWTSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILA-RSTLFFREDPAIGEAVTAAFRAEGIEVLEHT 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 372 KATDVKADKSGITVSFEAaveGEkpgLQAtayDRVLVAVGRSPNGKKIGAEKAGVTITERGFIPVDRQMRTNVPHIFAIG 451
Cdd:PRK13748 332 QASQVAHVDGEFVLTTGH---GE---LRA---DKLLVATGRAPNTRSLALDAAGVTVNAQGAIVIDQGMRTSVPHIYAAG 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 452 DIVGNPMLAHKATHEGKLAAEVAAGEKKEWVARVIPSVAYTNPEIAWVGVTETEAKAKGLKVGVAKFPWAASGRAIGIGR 531
Cdd:PRK13748 403 DCTDQPQFVYVAAAAGTRAAINMTGGDAALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRTLTLDNVPRALANFD 482
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2746980421 532 TEGFTKLIFDEQTHRVIGGAIVGVHAGDLLAEIGLAIEMGAEAEDIGHTIHAHPTLSESVGMAAEVYDGTITDL 605
Cdd:PRK13748 483 TRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAALAIRNRMTVQELADQLFPYLTMVEGLKLAAQTFNKDVKQL 556
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
141-591 |
8.72e-59 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 203.32 E-value: 8.72e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 141 KMVVLGAGLGGYTAAFRAADLGLDTVLIERYASL-GGVCLNVGCIPSKALLHAAAvidevaHAGDFGVDFGQPKITLDKL 219
Cdd:PRK08010 5 QAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNAMyGGTCINIGCIPTKTLVHDAQ------QHTDFVRAIQRKNEVVNFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 220 REykekvvgkltGGLASMAKQRKVRTVTGVASFVSPNELEIVGDDGKTQLlRFEHCIIAAGSQAVkLPNFP--WDDKRVM 297
Cdd:PRK08010 79 RN----------KNFHNLADMPNIDVIDGQAEFINNHSLRVHRPEGNLEI-HGEKIFINTGAQTV-VPPIPgiTTTPGVY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 298 DSTDALELHDIPKTLLVVGGGIIGLEMATVYSALGSKVTVVEFMDQLMPGADKDLVKPLADRLKKQGVEVHLKTKATDVK 377
Cdd:PRK08010 147 DSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVERIS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 378 ADKSGITVSFEAAvegekpglqATAYDRVLVAVGRSPNGKKIGAEKAGVTITERGFIPVDRQMRTNVPHIFAIGDIVGNP 457
Cdd:PRK08010 227 HHENQVQVHSEHA---------QLAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKYLHTTADNIWAMGDVTGGL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 458 MLAHKATHEGKLAAEVAAGEKKEWV--ARVIPSVAYTNPEIAWVGVTETEAKAKGLKVGVAKFPWAASGRAIGIGRTEGF 535
Cdd:PRK08010 298 QFTYISLDDYRIVRDELLGEGKRSTddRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDTRGV 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2746980421 536 TKLIFDEQTHRVIGGAIVGVHAGDLLAEIGLAIEMGAEAEDIGHTIHAHPTLSESV 591
Cdd:PRK08010 378 LKAIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESL 433
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
142-590 |
3.07e-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: 191.99 E-value: 3.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 142 MVVLGAGLGGYTAAFRAADLGLDTVLIERYA--------SLGGVCLNVGCIPSKALLHAAAVIDEVAHAGDFGVDF-GQP 212
Cdd:TIGR01438 5 LIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTptplgtrwGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVeETV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 213 KITLDKLREYKEKVVGKLTGGLASMAKQRKVRTVTGVASFVSPNELEIVGDDGKTQLLRFEHCIIAAGSQAvKLPNFPWD 292
Cdd:TIGR01438 85 KHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERP-RYPGIPGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 293 DKRVMDSTDALELHDIPKTLLVVGGGIIGLEMATVYSALGSKVTVVeFMDQLMPGADKDLVKPLADRLKKQGVEVHLKTK 372
Cdd:TIGR01438 164 KELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVM-VRSILLRGFDQDCANKVGEHMEEHGVKFKRQFV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 373 ATDVKADKSGITVSF---EAAVEGEkpglqataYDRVLVAVGRSPNGKKIGAEKAGVTITER-GFIPVDRQMRTNVPHIF 448
Cdd:TIGR01438 243 PIKVEQIEAKVLVEFtdsTNGIEEE--------YDTVLLAIGRDACTRKLNLENVGVKINKKtGKIPADEEEQTNVPYIY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 449 AIGDIVGN-PMLAHKATHEGKLAAEVAAGEKKEWVA-RVIPSVAYTNPEIAWVGVTETEAKAKGLKVGVAKF-------P 519
Cdd:TIGR01438 315 AVGDILEDkPELTPVAIQAGRLLAQRLFKGSTVICDyENVPTTVFTPLEYGACGLSEEKAVEKFGEENVEVFhsyfwplE 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2746980421 520 WAASGRAigiGRTEGFTKLIFD-EQTHRVIGGAIVGVHAGDLLAEIGLAIEMGAEAEDIGHTIHAHPTLSES 590
Cdd:TIGR01438 395 WTIPSRD---NHNKCYAKLVCNkKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEV 463
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
133-589 |
1.06e-53 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 190.80 E-value: 1.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 133 GKPADIECKMVVLGAGLGGYTAAFRAADLGLDTVLIE---------RYASLGGVCLNVGCIPSKALLHAAAVIDEVAHAG 203
Cdd:PLN02507 19 ANATHYDFDLFVIGAGSGGVRAARFSANFGAKVGICElpfhpisseSIGGVGGTCVIRGCVPKKILVYGATFGGEFEDAK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 204 DFGVDFGQpKITLD--KLREYKEKVVGKLTGGLASMAKQRKVRTVTGVASFVSPNELEIVGDDGKTQLLRFEHCIIAAGS 281
Cdd:PLN02507 99 NYGWEINE-KVDFNwkKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRYTAKHILIATGS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 282 QAVKlPNFPWDDKRVMdSTDALELHDIPKTLLVVGGGIIGLEMATVYSALGSKVTVVEFMDQLMPGADKDLVKPLADRLK 361
Cdd:PLN02507 178 RAQR-PNIPGKELAIT-SDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRAVVARNLE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 362 KQGVEVHLKTKATDVKADKSGITVSFEAAVEGEKpglqatayDRVLVAVGRSPNGKKIGAEKAGVTITERGFIPVDRQMR 441
Cdd:PLN02507 256 GRGINLHPRTNLTQLTKTEGGIKVITDHGEEFVA--------DVVLFATGRAPNTKRLNLEAVGVELDKAGAVKVDEYSR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 442 TNVPHIFAIGDIVGNPMLAHKATHEGK-LAAEVAAGEKKEWVARVIPSVAYTNPEIAWVGVTETEA--KAKGlKVGVAKF 518
Cdd:PLN02507 328 TNIPSIWAIGDVTNRINLTPVALMEGTcFAKTVFGGQPTKPDYENVACAVFCIPPLSVVGLSEEEAveQAKG-DILVFTS 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2746980421 519 PWAASGRAIGiGRTE-GFTKLIFDEQTHRVIGGAIVGVHAGDLLAEIGLAIEMGAEAEDIGHTIHAHPTLSE 589
Cdd:PLN02507 407 SFNPMKNTIS-GRQEkTVMKLIVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAE 477
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
142-591 |
1.65e-50 |
|
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: 182.09 E-value: 1.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 142 MVVLGAGLGGYTAAFRAADLGLDTVLI---------ERYASLGGVCLNVGCIPSKALLHAAAVIDEVAHAGDFGVDFGQP 212
Cdd:TIGR01423 6 LVVIGAGSGGLEAGWNAATLYKKRVAVvdvqthhgpPFYAALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGWEFDRS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 213 KITLD--KLREYKEKVVGKLTGGLASMAKQRKVRTV-TGVASFVSPNELEI-VGDDGKTQL---LRFEHCIIAAGS--QA 283
Cdd:TIGR01423 86 SVKANwkALIAAKNKAVLDINKSYEGMFADTEGLTFfLGWGALEDKNVVLVrESADPKSAVkerLQAEHILLATGSwpQM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 284 VKLPNfpwdDKRVMDSTDALELHDIPKTLLVVGGGIIGLEMATV---YSALGSKVTVVEFMDQLMPGADKDLVKPLADRL 360
Cdd:TIGR01423 166 LGIPG----IEHCISSNEAFYLDEPPRRVLTVGGGFISVEFAGIfnaYKPRGGKVTLCYRNNMILRGFDSTLRKELTKQL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 361 KKQGVEVHLKTKATDVKADKSGIT-VSFEAAVEGEkpglqataYDRVLVAVGRSPNGKKIGAEKAGVTITERGFIPVDRQ 439
Cdd:TIGR01423 242 RANGINIMTNENPAKVTLNADGSKhVTFESGKTLD--------VDVVMMAIGRVPRTQTLQLDKVGVELTKKGAIQVDEF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 440 MRTNVPHIFAIGDIVGNPMLAHKATHEGKLAAEVAAGEKKEWVARV-IPSVAYTNPEIAWVGVTETEAKAKGLKVGVAKF 518
Cdd:TIGR01423 314 SRTNVPNIYAIGDVTDRVMLTPVAINEGAAFVDTVFGNKPRKTDHTrVASAVFSIPPIGTCGLVEEDAAKKFEKVAVYES 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2746980421 519 PWAASGRAIGIGRTEGF-TKLIFDEQTHRVIGGAIVGVHAGDLLAEIGLAIEMGAEAEDIGHTIHAHPTLSESV 591
Cdd:TIGR01423 394 SFTPLMHNISGSKYKKFvAKIVTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAEEL 467
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
145-589 |
2.78e-46 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 171.60 E-value: 2.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 145 LGAGLGGYTAAFRAADLG---------LDTVLIERYASLGGVCLNVGCIPSKALLHAAAVIDEVAHAGDFGVDFG-QPKI 214
Cdd:PLN02546 85 IGAGSGGVRASRFASNFGasaavcelpFATISSDTLGGVGGTCVLRGCVPKKLLVYASKYSHEFEESRGFGWKYEtEPKH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 215 TLDKLREYKEKVVGKLTGGLASMAKQRKVRTVTGVASFVSPNELEIvgdDGKTQLLRfeHCIIAAGSQAVKlPNFPwDDK 294
Cdd:PLN02546 165 DWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDV---DGKLYTAR--NILIAVGGRPFI-PDIP-GIE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 295 RVMDSTDALELHDIPKTLLVVGGGIIGLEMATVYSALGSKVTVVEFMDQLMPGADKDLVKPLADRLKKQGVEVHLK---- 370
Cdd:PLN02546 238 HAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKKVLRGFDEEVRDFVAEQMSLRGIEFHTEespq 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 371 --TKATD----VKADKSgitvsfeaAVEGekpglqataYDRVLVAVGRSPNGKKIGAEKAGVTITERGFIPVDRQMRTNV 444
Cdd:PLN02546 318 aiIKSADgslsLKTNKG--------TVEG---------FSHVMFATGRKPNTKNLGLEEVGVKMDKNGAIEVDEYSRTSV 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 445 PHIFAIGDIVGNPMLAHKATHE-GKLAAEVAAGEKKEWVARVIPSVAYTNPEIAWVGVTETEAKAK--GLKVGVAKF-PW 520
Cdd:PLN02546 381 PSIWAVGDVTDRINLTPVALMEgGALAKTLFGNEPTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEygDVDVFTANFrPL 460
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2746980421 521 AASGRAIgigRTEGFTKLIFDEQTHRVIGGAIVGVHAGDLLAEIGLAIEMGAEAEDIGHTIHAHPTLSE 589
Cdd:PLN02546 461 KATLSGL---PDRVFMKLIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAE 526
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
132-591 |
1.50e-45 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 169.80 E-value: 1.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 132 SGKPADIECKMVVLGAGLGGYTAAFRAADLGLDTVLIERyASLGGVCLNVGCIPSKALLHAAAVIDEVAHAGDFGVDfGQ 211
Cdd:PTZ00058 41 LKKKPRMVYDLIVIGGGSGGMAAARRAARNKAKVALVEK-DYLGGTCVNVGCVPKKIMFNAASIHDILENSRHYGFD-TQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 212 PKITLDKLREYKEKVVGKLTGGLASMAKQRKVRTVTGVASFVSPNELEI------------VGDDGKT------------ 267
Cdd:PTZ00058 119 FSFNLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLIkkvsqvdgeadeSDDDEVTivsagvsqlddg 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 268 QLLRFEHCIIAAGSQavklPNFPwDDK---RVMDSTDALELHDiPKTLLVVGGGIIGLEMATVYSALGSKVTVVEFMDQL 344
Cdd:PTZ00058 199 QVIEGKNILIAVGNK----PIFP-DVKgkeFTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 345 MPGADKDLVKPLADRLKKQGVEVHLKTKATDVKADKS-GITVSFEaavEGEKpglqATAYDRVLVAVGRSPNGKKIGAeK 423
Cdd:PTZ00058 273 LRKFDETIINELENDMKKNNINIITHANVEEIEKVKEkNLTIYLS---DGRK----YEHFDYVIYCVGRSPNTEDLNL-K 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 424 AGVTITERGFIPVDRQMRTNVPHIFAIGDIVG----------------------------------NPMLAHKATHEGKL 469
Cdd:PTZ00058 345 ALNIKTPKGYIKVDDNQRTSVKHIYAVGDCCMvkknqeiedlnllklyneepylkkkentsgesyyNVQLTPVAINAGRL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 470 AAEVAAGEKKEWVA-RVIPSVAYTNPEIAWVGVTETEAKAKGLKVGVAKFPWAASGRAIGIGRTE------GFTKLIFDE 542
Cdd:PTZ00058 425 LADRLFGPFSRTTNyKLIPSVIFSHPPIGTIGLSEQEAIDIYGKENVKIYESRFTNLFFSVYDMDpaqkekTYLKLVCVG 504
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2746980421 543 QTHRVIGGAIVGVHAGDLLAEIGLAIEMGAEAEDIGHTIHAHPTLSESV 591
Cdd:PTZ00058 505 KEELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIHPTAAEEF 553
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
486-594 |
1.92e-41 |
|
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: 145.39 E-value: 1.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 486 IPSVAYTNPEIAWVGVTETEAKAKGLKVGVAKFPWAASGRAIGIGRTEGFTKLIFDEQTHRVIGGAIVGVHAGDLLAEIG 565
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGEVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQEAA 80
|
90 100
....*....|....*....|....*....
gi 2746980421 566 LAIEMGAEAEDIGHTIHAHPTLSESVGMA 594
Cdd:pfam02852 81 LAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
235-478 |
2.02e-40 |
|
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: 149.96 E-value: 2.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 235 ASMAKQR-KVRTVTGVASfVSPNELEIVGDDGKTqlLRFEHCIIAAGSQAVKLPNFPWDDKRVMDST---DALELHD--- 307
Cdd:COG0446 44 ESFERKGiDVRTGTEVTA-IDPEAKTVTLRDGET--LSYDKLVLATGARPRPPPIPGLDLPGVFTLRtldDADALREalk 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 308 --IPKTLLVVGGGIIGLEMATVYSALGSKVTVVEFMDQLMPGADKDLVKPLADRLKKQGVEVHLKTKATDVKADKsGITV 385
Cdd:COG0446 121 efKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAIDGDD-KVAV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 386 SFEaavEGEKpglqaTAYDRVLVAVGRSPNgkkIG-AEKAGVTITERGFIPVDRQMRTNVPHIFAIGDIVGNP------- 457
Cdd:COG0446 200 TLT---DGEE-----IPADLVVVAPGVRPN---TElAKDAGLALGERGWIKVDETLQTSDPDVYAAGDCAEVPhpvtgkt 268
|
250 260
....*....|....*....|....
gi 2746980421 458 ---MLAHKATHEGKLAAEVAAGEK 478
Cdd:COG0446 269 vyiPLASAANKQGRVAAENILGGP 292
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
235-574 |
3.82e-33 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 131.42 E-value: 3.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 235 ASMAKQRKVRTVTGV-ASFVSPNELEIVGDDGKTqlLRFEHCIIAAGSQAVKLPNFPWDDKRV-----MDSTDALELH-D 307
Cdd:COG1251 63 ADFYEENGIDLRLGTrVTAIDRAARTVTLADGET--LPYDKLVLATGSRPRVPPIPGADLPGVftlrtLDDADALRAAlA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 308 IPKTLLVVGGGIIGLEMATVYSALGSKVTVVEFMDQLMPGA-DKDLVKPLADRLKKQGVEVHLKTKATDVKADKSGITVS 386
Cdd:COG1251 141 PGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPRQlDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVR 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 387 FEaavEGEKpgLQAtayDRVLVAVGRSPNgkkIG-AEKAGVTItERGfIPVDRQMRTNVPHIFAIGDIV-------GNPM 458
Cdd:COG1251 221 LA---DGEE--LPA---DLVVVAIGVRPN---TElARAAGLAV-DRG-IVVDDYLRTSDPDIYAAGDCAehpgpvyGRRV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 459 LAH--KATHEGKLAAEVAAGEKkewvARVIPSVAYTnpeiaWVgvteteaKAKGLKVGVAKFPWAASGRAIGIGRTEG-F 535
Cdd:COG1251 288 LELvaPAYEQARVAAANLAGGP----AAYEGSVPST-----KL-------KVFGVDVASAGDAEGDEEVVVRGDPARGvY 351
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2746980421 536 TKLIFDEQthRVIGGAIVG--VHAGDLLAEIGLAIEMGAEA 574
Cdd:COG1251 352 KKLVLRDG--RLVGAVLVGdtSDAGALRQLIKNGRPLPPRA 390
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
142-592 |
7.01e-33 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 132.25 E-value: 7.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 142 MVVLGAGLGGYTAAFRAADLGLDTVLIERYA--------SLGGVCLNVGCIPSKaLLHAAAVIDEVAH--AGDFGVDFGQ 211
Cdd:PTZ00052 8 LVVIGGGSGGMAAAKEAAAHGKKVALFDYVKpstqgtkwGLGGTCVNVGCVPKK-LMHYAANIGSIFHhdSQMYGWKTSS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 212 pKITLDKLREYKEKVVGKLTGGLASMAKQRKVRTVTGVASFVSPNELEIvGDDGKTQLLRFEHCIIAAGSQavklPNFPW 291
Cdd:PTZ00052 87 -SFNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTVSY-GDNSQEETITAKYILIATGGR----PSIPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 292 DDKRVMD----STDALELHDIPKTLLVVGGGIIGLEMATVYSALGSKVTVVeFMDQLMPGADKDLVKPLADRLKKQGVEV 367
Cdd:PTZ00052 161 DVPGAKEysitSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVA-VRSIPLRGFDRQCSEKVVEYMKEQGTLF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 368 HLKTKATDVKADKSGITVSFEAAVEGEkpglqataYDRVLVAVGRSPNGKKIGAEKAGVTITERGFIPVDRQMrTNVPHI 447
Cdd:PTZ00052 240 LEGVVPINIEKMDDKIKVLFSDGTTEL--------FDTVLYATGRKPDIKGLNLNAIGVHVNKSNKIIAPNDC-TNIPNI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 448 FAIGDIV-GNPMLAHKATHEGKLAAEVAAGEKKEWVA-RVIPSVAYTNPEIAWVGVTETEAKAKGLKVGVAKFPWAASGR 525
Cdd:PTZ00052 311 FAVGDVVeGRPELTPVAIKAGILLARRLFKQSNEFIDyTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQEFNTL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 526 AIGIGRTEG-----------------FTKLI-FDEQTHRVIGGAIVGVHAGDLLAEIGLAIEMGAEAEDIGHTIHAHPTL 587
Cdd:PTZ00052 391 EIAAVHREKherarkdeydfdvssncLAKLVcVKSEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHPTD 470
|
....*
gi 2746980421 588 SESVG 592
Cdd:PTZ00052 471 AEVFM 475
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1-80 |
2.23e-32 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 131.48 E-value: 2.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 1 MAvIEIKVPDIGDYSDVPVIEVLVAVGDSVAKDQGLVTLESDKATLEVPSSAAGVVKELKVKVGDTLSEGALVLLLETEG 80
Cdd:PRK11855 1 MA-IEFKVPDIGEVVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIEAAG 79
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
2-80 |
8.64e-32 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 129.94 E-value: 8.64e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2746980421 2 AVIEIKVPDIGDYSDVPVIEVLVAVGDSVAKDQGLVTLESDKATLEVPSSAAGVVKELKVKVGDTLSEGALVLLLETEG 80
Cdd:PRK11855 118 GVVEVKVPDIGEITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAA 196
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
4-80 |
5.64e-29 |
|
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: 121.52 E-value: 5.64e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2746980421 4 IEIKVPDIGDYSDVPVIEVLVAVGDSVAKDQGLVTLESDKATLEVPSSAAGVVKELKVKVGDTLSEGALVLLLETEG 80
Cdd:TIGR01348 1 TEIKVPDIGDNEEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLEVGA 77
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
140-471 |
9.08e-29 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 116.37 E-value: 9.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 140 CKMVVLGAGLGGYTAAFRAADLGLDTVLIERYAsLGGVCLNVGCI------PSKalLHAAAVIDE-VAHAGDFGVDFgqp 212
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGE-PGGQLATTKEIenypgfPEG--ISGPELAERlREQAERFGAEI--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 213 kitldklreykekvvgkltgglasmakqrKVRTVTGVasFVSPNELEIVGDDGKTqlLRFEHCIIAAGSQAVKLPnFP-W 291
Cdd:COG0492 75 -----------------------------LLEEVTSV--DKDDGPFRVTTDDGTE--YEAKAVIIATGAGPRKLG-LPgE 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 292 DD---KRVMDS--TDALELHDipKTLLVVGGGIIGLEMATVYSALGSKVTVVEFMDQLMpgADKDLVkplaDRLKK-QGV 365
Cdd:COG0492 121 EEfegRGVSYCatCDGFFFRG--KDVVVVGGGDSALEEALYLTKFASKVTLIHRRDELR--ASKILV----ERLRAnPKI 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 366 EVHLKTKATDVKADKSGITVSFEAAVEGEKpglQATAYDRVLVAVGRSPNGKkiGAEKAGVTITERGFIPVDRQMRTNVP 445
Cdd:COG0492 193 EVLWNTEVTEIEGDGRVEGVTLKNVKTGEE---KELEVDGVFVAIGLKPNTE--LLKGLGLELDEDGYIVVDEDMETSVP 267
|
330 340
....*....|....*....|....*..
gi 2746980421 446 HIFAIGDIVGNPM-LAHKATHEGKLAA 471
Cdd:COG0492 268 GVFAAGDVRDYKYrQAATAAGEGAIAA 294
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
3-80 |
3.05e-28 |
|
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: 119.21 E-value: 3.05e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2746980421 3 VIEIKVPDIGDYSDVPVIEVLVAVGDSVAKDQGLVTLESDKATLEVPSSAAGVVKELKVKVGDTLSEGALVLLLETEG 80
Cdd:TIGR01348 116 VQEVTVPDIGDIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAG 193
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1-80 |
1.95e-23 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 104.70 E-value: 1.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 1 MAvIEIKVPDIGdYSDVPVIEVLVAVGDSVAKDQGLVTLESDKATLEVPSSAAGVVKELKVKVGDTLSEGALVLLLETEG 80
Cdd:PRK11854 1 MA-IEIKVPDIG-ADEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESAD 78
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
310-578 |
2.03e-22 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 100.50 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 310 KTLLVVGGGIIGLEMATVYSALGSKVTVVEFMDQLMPGA-DKDLVKPLADRLKKQGVEVHLKTKATDVKADKSGItvsfe 388
Cdd:PRK09564 150 KNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRILPDSfDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVE----- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 389 aAVEGEKPGLQAtayDRVLVAVGRSPNGKKIgaEKAGVTITERGFIPVDRQMRTNVPHIFAIGD-------IVGNPM--- 458
Cdd:PRK09564 225 -GVVTDKGEYEA---DVVIVATGVKPNTEFL--EDTGLKTLKNGAIIVDEYGETSIENIYAAGDcatiyniVSNKNVyvp 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 459 LAHKATHEGKLAAEVAAGEKKEWVARV-IPSVAYTNPEIAWVGVTETEAKAKGLKVGV---------AKFPwaasgraig 528
Cdd:PRK09564 299 LATTANKLGRMVGENLAGRHVSFKGTLgSACIKVLDLEAARTGLTEEEAKKLGIDYKTvfikdknhtNYYP--------- 369
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2746980421 529 iGRTEGFTKLIFDEQTHRVIGGAIVG----VHAGDLLAeigLAIEMGAEAEDIG 578
Cdd:PRK09564 370 -GQEDLYVKLIYEADTKVILGGQIIGkkgaVLRIDALA---VAIYAKLTTQELG 419
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
4-76 |
4.88e-22 |
|
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: 90.13 E-value: 4.88e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2746980421 4 IEIKVPDIGD-YSDVPVIEVLVAVGDSVAKDQGLVTLESDKATLEVPSSAAGVVKELKVKVGDTLSEGALVLLL 76
Cdd:COG0508 3 IEIKMPDLGEsMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
2-80 |
1.55e-21 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 98.92 E-value: 1.55e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2746980421 2 AVIEIKVPDIGdYSDVPVIEVLVAVGDSVAKDQGLVTLESDKATLEVPSSAAGVVKELKVKVGDTLSEGALVLLLETEG 80
Cdd:PRK11854 205 GVKDVNVPDIG-GDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEG 282
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
2-80 |
3.22e-21 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 97.77 E-value: 3.22e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2746980421 2 AVIEIKVPDIGdYSDVPVIEVLVAVGDSVAKDQGLVTLESDKATLEVPSSAAGVVKELKVKVGDTLSEGALVLLLETEG 80
Cdd:PRK11854 104 AAKDVHVPDIG-SDEVEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFEVAG 181
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
312-388 |
3.54e-21 |
|
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: 87.64 E-value: 3.54e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2746980421 312 LLVVGGGIIGLEMATVYSALGSKVTVVEFMDQLMPGADKDLVKPLADRLKKQGVEVHLKTKATDVKADKSGITVSFE 388
Cdd:pfam00070 2 VVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLT 78
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
143-490 |
3.94e-20 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 92.50 E-value: 3.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 143 VVLGAGLGGYTAAFRAADL---GLDTVLIERYASLggvclnvgciPSKALLHaaavidEVAhAGdfGVDFGQpkITLDkl 219
Cdd:COG1252 5 VIVGGGFAGLEAARRLRKKlggDAEVTLIDPNPYH----------LFQPLLP------EVA-AG--TLSPDD--IAIP-- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 220 reykekvvgkltggLASMAKQRKVRTVTGVASFVSPNELEIVGDDGKTqlLRFEHCIIAAGSQavklPNFP----WDDKR 295
Cdd:COG1252 62 --------------LRELLRRAGVRFIQGEVTGIDPEARTVTLADGRT--LSYDYLVIATGSV----TNFFgipgLAEHA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 296 V-MDST-DALELHDI------------PKTLLVVGGGIIGLEMA----------TVYSALGS---KVTVVEFMDQLMPGA 348
Cdd:COG1252 122 LpLKTLeDALALRERllaaferaerrrLLTIVVVGGGPTGVELAgelaellrklLRYPGIDPdkvRITLVEAGPRILPGL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 349 DKDLVKPLADRLKKQGVEVHLKTKATDVKADksGITVSfeaavEGEKpglqaTAYDRVLVAVGRSPNGkkiGAEKAGVTI 428
Cdd:COG1252 202 GEKLSEAAEKELEKRGVEVHTGTRVTEVDAD--GVTLE-----DGEE-----IPADTVIWAAGVKAPP---LLADLGLPT 266
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2746980421 429 TERGFIPVDRQMRT-NVPHIFAIGDIV--------GNPMLAHKATHEGK-----LAAEVAAGEKKEWVARVIPSVA 490
Cdd:COG1252 267 DRRGRVLVDPTLQVpGHPNVFAIGDCAavpdpdgkPVPKTAQAAVQQAKvlaknIAALLRGKPLKPFRYRDKGCLA 342
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
4-76 |
9.13e-19 |
|
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: 80.53 E-value: 9.13e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2746980421 4 IEIKVPDIGD-YSDVPVIEVLVAVGDSVAKDQGLVTLESDKATLEVPSSAAGVVKELKVKVGDTLSEGALVLLL 76
Cdd:cd06849 1 TEIKMPDLGEsMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
272-456 |
2.24e-18 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 87.92 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 272 FEHCIIAAGSQAVKLpNFPWD---DKRVMDSTDALEL----HDIpKTLLVVGGGIIGLEMATVYSALGSKVTVVEFMDQL 344
Cdd:PRK13512 106 YDKLILSPGASANSL-GFESDitfTLRNLEDTDAIDQfikaNQV-DKALVVGAGYISLEVLENLYERGLHPTLIHRSDKI 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 345 MPGADKDLVKPLADRLKKQGVEVHLKTKATDVKadksGITVSFeaavegeKPGLQATaYDRVLVAVGRSPNGKKIgaEKA 424
Cdd:PRK13512 184 NKLMDADMNQPILDELDKREIPYRLNEEIDAIN----GNEVTF-------KSGKVEH-YDMIIEGVGTHPNSKFI--ESS 249
|
170 180 190
....*....|....*....|....*....|..
gi 2746980421 425 GVTITERGFIPVDRQMRTNVPHIFAIGDIVGN 456
Cdd:PRK13512 250 NIKLDDKGFIPVNDKFETNVPNIYAIGDIITS 281
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
5-76 |
3.04e-18 |
|
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: 79.18 E-value: 3.04e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2746980421 5 EIKVPDIGDYSDVPVIEVLVAVGDSVAKDQGLVTLESDKATLEVPSSAAGVVKELKVKVGDTLSEGALVLLL 76
Cdd:pfam00364 2 EIKSPMIGESVREGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
310-452 |
2.02e-17 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 84.20 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 310 KTLLVVGGGIIGLEMATVYSALGSKVTVVEFMDQLMPGADKDLVK-PLADRLKKQGVEVHLKTKATDVKADKSGITVSFE 388
Cdd:PRK04965 142 QRVLVVGGGLIGTELAMDLCRAGKAVTLVDNAASLLASLMPPEVSsRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRATLD 221
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2746980421 389 AAvegekpglQATAYDRVLVAVGRSPNGKKigAEKAGVTItERGfIPVDRQMRTNVPHIFAIGD 452
Cdd:PRK04965 222 SG--------RSIEVDAVIAAAGLRPNTAL--ARRAGLAV-NRG-IVVDSYLQTSAPDIYALGD 273
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
2-80 |
5.02e-17 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 83.69 E-value: 5.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 2 AVIEIKVPDIG-DYSDVPVIEVLVAVGDSVAKDQGLVTLESDKATLEVPSSAAGVVKELKVKVGDTLSEGALVLLLETEG 80
Cdd:PRK11856 1 MMFEFKMPDLGeGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEG 80
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
4-80 |
4.52e-15 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 77.57 E-value: 4.52e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2746980421 4 IEIKVPDIGD-YSDVPVIEVLVAVGDSVAKDQGLVTLESDKATLEVPSSAAGVVKELKVKVGDTLSEGALVLLLETEG 80
Cdd:PRK05704 3 VEIKVPTLPEsVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGA 80
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
260-543 |
1.32e-13 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 74.09 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 260 IVGDDGKTQllRFEHCIIAAGSQAVKLPnFPWDDK------RVMDSTDALE-LHDIPKTLLVVGGGIIGLEMATVYSALG 332
Cdd:TIGR02374 87 VITDAGRTL--SYDKLILATGSYPFILP-IPGADKkgvyvfRTIEDLDAIMaMAQRFKKAAVIGGGLLGLEAAVGLQNLG 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 333 SKVTVVEFMDQLMPGA-DKDLVKPLADRLKKQGVEVHLKTKATDVKADKSGITVSFEaavEGEKpgLQAtayDRVLVAVG 411
Cdd:TIGR02374 164 MDVSVIHHAPGLMAKQlDQTAGRLLQRELEQKGLTFLLEKDTVEIVGATKADRIRFK---DGSS--LEA---DLIVMAAG 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 412 RSPNGKKigAEKAGVTITeRGFIpVDRQMRTNVPHIFAIGDIvgnpmlahkATHEGKLAAEVAAGEKKewvARVIPSVAY 491
Cdd:TIGR02374 236 IRPNDEL--AVSAGIKVN-RGII-VNDSMQTSDPDIYAVGEC---------AEHNGRVYGLVAPLYEQ---AKVLADHIC 299
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2746980421 492 TNPEIAWVGvTETEAKAKGLKVGVAKFpwaasGRAIgigRTEGFTKL-IFDEQ 543
Cdd:TIGR02374 300 GVECEEYEG-SDLSAKLKLLGVDVWSA-----GDAQ---ETERTTSIkIYDEQ 343
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
251-453 |
1.56e-13 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 72.65 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 251 SFVSPNELEIVGDDGKTqlLRFEHCIIAAGSQAVKLPNFPWDDKRVMD---STDALELHDI---PKTLLVVGGGIIGLEM 324
Cdd:PRK09754 82 KTLGRDTRELVLTNGES--WHWDQLFIATGAAARPLPLLDALGERCFTlrhAGDAARLREVlqpERSVVIVGAGTIGLEL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 325 ATVYSALGSKVTVVEFMDQLMPGADKDLVKP-LADRLKKQGVEVHLKTKATDV-KADKSGITVSfeaavEGEKpgLQAta 402
Cdd:PRK09754 160 AASATQRRCKVTVIELAATVMGRNAPPPVQRyLLQRHQQAGVRILLNNAIEHVvDGEKVELTLQ-----SGET--LQA-- 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2746980421 403 yDRVLVAVGRSPNGKKigAEKAGVTITerGFIPVDRQMRTNVPHIFAIGDI 453
Cdd:PRK09754 231 -DVVIYGIGISANDQL--AREANLDTA--NGIVIDEACRTCDPAIFAGGDV 276
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
4-80 |
3.57e-12 |
|
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: 68.61 E-value: 3.57e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2746980421 4 IEIKVPDIGD-YSDVPVIEVLVAVGDSVAKDQGLVTLESDKATLEVPSSAAGVVKELKVKVGDTLSEGALVLLLETEG 80
Cdd:TIGR01347 1 IEIKVPELAEsITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGN 78
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
144-472 |
2.00e-11 |
|
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 440259 [Multi-domain] Cd Length: 434 Bit Score: 66.31 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 144 VLGAGLGGYTAAFRAADLGLDTVLIERYASLGGVcLNVGcIPskallhaaavidevahagdfgvDFGQPKITLDKLREYk 223
Cdd:COG0493 126 VVGSGPAGLAAAYQLARAGHEVTVFEALDKPGGL-LRYG-IP----------------------EFRLPKDVLDREIEL- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 224 ekvvgkltggLASMAkqrkVRTVTGVAsfvspneleiVGDDGKTQLLR--FEHCIIAAGSQAVKLPNFPWDD-KRVMDST 300
Cdd:COG0493 181 ----------IEALG----VEFRTNVE----------VGKDITLDELLeeFDAVFLATGAGKPRDLGIPGEDlKGVHSAM 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 301 D---ALELHDIPKTLL-------VVGGGIIGleMATVYSA--LGSK-VTVVEFMDQL-MPGAD-------------KDLV 353
Cdd:COG0493 237 DfltAVNLGEAPDTILavgkrvvVIGGGNTA--MDCARTAlrLGAEsVTIVYRRTREeMPASKeeveealeegvefLFLV 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 354 KPLADRLKKQGVEVHLKTKATD-VKADKSGiTVSFEAaVEGEKPGLQAtayDRVLVAVGRSPNGKKIGAEKaGVTITERG 432
Cdd:COG0493 315 APVEIIGDENGRVTGLECVRMElGEPDESG-RRRPVP-IEGSEFTLPA---DLVILAIGQTPDPSGLEEEL-GLELDKRG 388
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2746980421 433 FIPVD-RQMRTNVPHIFAIGDIVGNPMLAHKATHEGKLAAE 472
Cdd:COG0493 389 TIVVDeETYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAAR 429
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
19-76 |
2.77e-10 |
|
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: 56.27 E-value: 2.77e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2746980421 19 VIEVLVAVGDSVAKDQGLVTLESDKATLEVPSSAAGVVKELKVKVGDTLSEGALVLLL 76
Cdd:cd06850 10 VVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
314-452 |
2.07e-09 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 60.17 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 314 VVGGGIIGLEMATVYSALGSKVTVVEFMDQLMpgADKDLVkplaDRLKKQG-VEVHLKTKATDVKADKSGIT-VSFEAAV 391
Cdd:PRK15317 356 VIGGGNSGVEAAIDLAGIVKHVTVLEFAPELK--ADQVLQ----DKLRSLPnVTIITNAQTTEVTGDGDKVTgLTYKDRT 429
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2746980421 392 EGEkpgLQATAYDRVLVAVGRSPNGKKIgaeKAGVTITERGFIPVDRQMRTNVPHIFAIGD 452
Cdd:PRK15317 430 TGE---EHHLELEGVFVQIGLVPNTEWL---KGTVELNRRGEIIVDARGATSVPGVFAAGD 484
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
310-472 |
1.28e-08 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 57.82 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 310 KTLLVVGGGIIGLEMATVYSALG-SKVTVV-EFMDQLMPGADKDLVKPLAdrlkkQGVEVHLKTKATDVKADKSGITVSF 387
Cdd:PRK12814 324 KKVVVIGGGNTAIDAARTALRLGaESVTILyRRTREEMPANRAEIEEALA-----EGVSLRELAAPVSIERSEGGLELTA 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 388 EA---------------AVEGEKPGLQAtayDRVLVAVGRSPNGKKigAEKAGVTITERGFIPVDRQ-MRTNVPHIFAIG 451
Cdd:PRK12814 399 IKmqqgepdesgrrrpvPVEGSEFTLQA---DTVISAIGQQVDPPI--AEAAGIGTSRNGTVKVDPEtLQTSVAGVFAGG 473
|
170 180
....*....|....*....|.
gi 2746980421 452 DIVGNPMLAHKATHEGKLAAE 472
Cdd:PRK12814 474 DCVTGADIAINAVEQGKRAAH 494
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
144-472 |
2.67e-08 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 56.34 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 144 VLGAGLGGYTAAFRAADLGLDTVLIERYASLGGVclNVGCIPS----KALLHAaavidEVAHAGDFGVDF------GqPK 213
Cdd:PRK11749 145 VIGAGPAGLTAAHRLARKGYDVTIFEARDKAGGL--LRYGIPEfrlpKDIVDR-----EVERLLKLGVEIrtntevG-RD 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 214 ITLDKLRE-YKEKVVGkltgglasmakqrkvrtvTGVASfvsPNELEIVGDDgktqllrfehciiaagsqavkLPNfpwd 292
Cdd:PRK11749 217 ITLDELRAgYDAVFIG------------------TGAGL---PRFLGIPGEN---------------------LGG---- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 293 dkrVMDSTDAL-------ELHDIP--KTLLVVGGGIIGLEMATVYSALGSK-VTVVEFMDQL-MPGADKDLvkplaDRLK 361
Cdd:PRK11749 251 ---VYSAVDFLtrvnqavADYDLPvgKRVVVIGGGNTAMDAARTAKRLGAEsVTIVYRRGREeMPASEEEV-----EHAK 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 362 KQGVEVHLKTKATDVKADKSGIT-VSFE--AAVEGEKPGLQATAY---------DRVLVAVGRSPNGKKI-GAEKAGVTi 428
Cdd:PRK11749 323 EEGVEFEWLAAPVEILGDEGRVTgVEFVrmELGEPDASGRRRVPIegseftlpaDLVIKAIGQTPNPLILsTTPGLELN- 401
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2746980421 429 TERGFIPVDRQMRTNVPHIFAIGDIVGNPMLAHKATHEGKLAAE 472
Cdd:PRK11749 402 RWGTIIADDETGRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAE 445
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
239-451 |
7.68e-08 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 54.15 E-value: 7.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 239 KQRKVRTVTGVASFVSPNELEIVGDDGKTqlLRFEHCIIAAGS-QAVKLPNFPwdDKRVMDSTDAlELHDIPKT-LLVVG 316
Cdd:pfam13738 88 FELPINLFEEVTSVKKEDDGFVVTTSKGT--YQARYVIIATGEfDFPNKLGVP--ELPKHYSYVK-DFHPYAGQkVVVIG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 317 GGIIGLEMATVYSALGSKVTVV---EFMDQlmPGADKDL-VKP-----LADRLKKQGVEVHLKTKATDVKADKSGITVSF 387
Cdd:pfam13738 163 GYNSAVDAALELVRKGARVTVLyrgSEWED--RDSDPSYsLSPdtlnrLEELVKNGKIKAHFNAEVKEITEVDVSYKVHT 240
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2746980421 388 EaavEGEKpglqATAYDRVLVAVGRSPNGKKIgaEKAGVTITERGFIPVDRQ-MRTNVPHIFAIG 451
Cdd:pfam13738 241 E---DGRK----VTSNDDPILATGYHPDLSFL--KKGLFELDEDGRPVLTEEtESTNVPGLFLAG 296
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
19-77 |
3.45e-07 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 47.86 E-value: 3.45e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2746980421 19 VIEVLVAVGDSVAKDQGLVTLESDKATLEVPSSAAGVVKELKVKVGDTLSEGALVLLLE 77
Cdd:PRK08225 12 VWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
141-471 |
1.16e-06 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 51.67 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 141 KMVVLGAGLGGYTAAFRAADLGLDTVLIERYASLGGVcLNVGcIPsKALLHAAAVIDEVAHAGDFGVDFgqpkitldklr 220
Cdd:PRK12778 433 KVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGGV-LKYG-IP-EFRLPKKIVDVEIENLKKLGVKF----------- 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 221 eYKEKVVGKLtgglasmakqrkvrtvtgvasfVSPNELEIVGddgktqllrFEHCIIAAGSqavKLPNF---PWDDK-RV 296
Cdd:PRK12778 499 -ETDVIVGKT----------------------ITIEELEEEG---------FKGIFIASGA---GLPNFmniPGENSnGV 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 297 MDSTDAL----------ELHDIP----KTLLVVGGGIIGLEMATVYSALGS-KVTVV-EFMDQLMPgADKDLVKpladRL 360
Cdd:PRK12778 544 MSSNEYLtrvnlmdaasPDSDTPikfgKKVAVVGGGNTAMDSARTAKRLGAeRVTIVyRRSEEEMP-ARLEEVK----HA 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 361 KKQGVEVHLKTKATDVKADKSG-----ITVSFE------------AAVEGEKPGLQAtayDRVLVAVGRSPNgKKIGAEK 423
Cdd:PRK12778 619 KEEGIEFLTLHNPIEYLADEKGwvkqvVLQKMElgepdasgrrrpVAIPGSTFTVDV---DLVIVSVGVSPN-PLVPSSI 694
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2746980421 424 AGVTITERGFIPVDRQMRTNVPHIFAIGDIVGNPMLAHKATHEGKLAA 471
Cdd:PRK12778 695 PGLELNRKGTIVVDEEMQSSIPGIYAGGDIVRGGATVILAMGDGKRAA 742
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
277-472 |
1.17e-06 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 51.41 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 277 IAAGSQAVKLPNFPWDD-KRVMDSTDAL------ELHDIPKTLLVVGGGIIGLEMATVYSALG-SKVTVV---------- 338
Cdd:PRK12771 228 VAIGAQLGKRLPIPGEDaAGVLDAVDFLravgegEPPFLGKRVVVIGGGNTAMDAARTARRLGaEEVTIVyrrtredmpa 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 339 ---EFMDQLMPGAD-KDLVKPLADRLKKQGVEVHLKTKATDVKADKSGitvsFEAAVEGEKPGLQAtayDRVLVAVGRSP 414
Cdd:PRK12771 308 hdeEIEEALREGVEiNWLRTPVEIEGDENGATGLRVITVEKMELDEDG----RPSPVTGEEETLEA---DLVVLAIGQDI 380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2746980421 415 NGKkiGAEKAGVTITERGFIPVDR-QMRTNVPHIFAIGDIVGNPMLAHKATHEGKLAAE 472
Cdd:PRK12771 381 DSA--GLESVPGVEVGRGVVQVDPnFMMTGRPGVFAGGDMVPGPRTVTTAIGHGKKAAR 437
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
3-78 |
1.38e-06 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 51.29 E-value: 1.38e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2746980421 3 VIEIKVPDIGD-YSDVPVIEVLVAVGDSVAKDQGLVTLESDKATLEVPSSAAGVVKELKVKVGDTLSEGALVLLLET 78
Cdd:PLN02226 91 TVEAVVPHMGEsITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISK 167
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
19-77 |
1.39e-06 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 51.38 E-value: 1.39e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2746980421 19 VIEVLVAVGDSVAKDQGLVTLESDKATLEVPSSAAGVVKELKVKVGDTLSEGALVLLLE 77
Cdd:PRK09282 533 VVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
314-561 |
1.62e-06 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 51.27 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 314 VVGGGIIGLEMATVYSALGSKVTVVEFMDQLMP------GADKdlvkpLADRLKKQGVEVHL--KTKATDVKADKSGITV 385
Cdd:PRK14989 150 VVGGGLLGLEAAGALKNLGVETHVIEFAPMLMAeqldqmGGEQ-----LRRKIESMGVRVHTskNTLEIVQEGVEARKTM 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 386 SFEAAVEGEkpglqataYDRVLVAVGRSPNGKKigAEKAGVTITERGFIPVDRQMRTNVPHIFAIGDIvgnpmlahkATH 465
Cdd:PRK14989 225 RFADGSELE--------VDFIVFSTGIRPQDKL--ATQCGLAVAPRGGIVINDSCQTSDPDIYAIGEC---------ASW 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 466 EGKLAAEVAAGEKkewVARVIPSVAYTNpEIAWVGvTETEAKAK--GLKVGvakfpwaasgrAIGI--GRTEG------- 534
Cdd:PRK14989 286 NNRVFGLVAPGYK---MAQVAVDHLLGS-ENAFEG-ADLSAKLKllGVDVG-----------GIGDahGRTPGarsyvyl 349
|
250 260 270
....*....|....*....|....*....|....*
gi 2746980421 535 ------FTKLIFDEQTHRVIGGAIVGVHA--GDLL 561
Cdd:PRK14989 350 deskeiYKRLIVSEDNKTLLGAVLVGDTSdyGNLL 384
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
2-71 |
2.16e-06 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 50.45 E-value: 2.16e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2746980421 2 AVIEIKVPDIGD-YSDVPVIEVLVAVGDSVAKDQGLVTLESDKATLEVPSSAAGVVKELKVKVGDTLSEGA 71
Cdd:PTZ00144 43 SIKVIKVPTMGDsISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGA 113
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
294-492 |
2.85e-06 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 50.15 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 294 KRVMDSTDALELHDIP----KTLL---VVGGGIIGLEMATVYSALGS--------------KVTVVEFMDQLMPGADKDL 352
Cdd:PTZ00318 151 KRIVQCIERASLPTTSveerKRLLhfvVVGGGPTGVEFAAELADFFRddvrnlnpelveecKVTVLEAGSEVLGSFDQAL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 353 VKPLADRLKKQGVEVHLKTKATDVKAD----KSGITVSFEAAVEGekpglqataydrvlVAVGRSPNGKKIGAEKagvti 428
Cdd:PTZ00318 231 RKYGQRRLRRLGVDIRTKTAVKEVLDKevvlKDGEVIPTGLVVWS--------------TGVGPGPLTKQLKVDK----- 291
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2746980421 429 TERGFIPVDRQMRT-NVPHIFAIGDIVGN-----PMLAHKATHEGK-LAAEVAAGEK-----KEWVARVIPSVAYT 492
Cdd:PTZ00318 292 TSRGRISVDDHLRVkPIPNVFALGDCAANeerplPTLAQVASQQGVyLAKEFNNELKgkpmsKPFVYRSLGSLAYL 367
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
5-70 |
3.08e-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: 45.13 E-value: 3.08e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2746980421 5 EIKVPDIGDY-SDVPVIEVLVAVGDSVAKDQGLVTLESDKATLEVPSSAAGVVKELKVKVGDTLSEG 70
Cdd:cd06663 1 TILIPDLAQHlGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGD 67
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
19-70 |
3.79e-06 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 47.16 E-value: 3.79e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2746980421 19 VIEVLVAVGDSVAKDQGLVTLESDKATLEVPSSAAGVVKELKVKVGDTLSEG 70
Cdd:PRK05641 95 ILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTG 146
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
19-76 |
5.11e-06 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 49.69 E-value: 5.11e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2746980421 19 VIEVLVAVGDSVAKDQGLVTLESDKATLEVPSSAAGVVKELKVKVGDTLSEGALVLLL 76
Cdd:COG1038 1087 VVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK12844 |
PRK12844 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
137-252 |
6.50e-06 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 183787 [Multi-domain] Cd Length: 557 Bit Score: 48.98 E-value: 6.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 137 DIECKMVVLGAGLGGYTAAFRAADLGLDTVLIERYASLGGVCLNVGC---IPSKALLHAAAVIDevahagdfgvdfgqpk 213
Cdd:PRK12844 4 DETYDVVVVGSGGGGMCAALAAADSGLEPLIVEKQDKVGGSTAMSGGvlwLPNNPLMKAAGVPD---------------- 67
|
90 100 110
....*....|....*....|....*....|....*....
gi 2746980421 214 iTLDKLREYKEKVVGKLTGGLASMAKQRKVRTVTGVASF 252
Cdd:PRK12844 68 -SHEDALAYLDAVVGDQGPASSPERREAYLRAGPAMVSF 105
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
143-176 |
9.39e-06 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 48.37 E-value: 9.39e-06
10 20 30
....*....|....*....|....*....|....
gi 2746980421 143 VVLGAGLGGYTAAFRAADLGLDTVLIERYASLGG 176
Cdd:pfam12831 3 VVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGG 36
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
23-80 |
1.02e-05 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 48.02 E-value: 1.02e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2746980421 23 LVAVGDSVAKDQGLVTLESDKATLEVPSSAAGVVKELKVKVGDTLSEGALVLLLETEG 80
Cdd:PRK14875 23 LVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAE 80
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
18-77 |
1.09e-05 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 45.27 E-value: 1.09e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 18 PVIEVLVAVGDSVAKDQGLVTLESDKATLEVPSSAAGVVKELKVKVGDTLSEGALVLLLE 77
Cdd:COG0511 77 PGAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
310-472 |
1.49e-05 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 47.29 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 310 KTLLVVGGGIIGLEMATVYSALGS-KVTV-----------------------VEFMDQLMPgadkdlVKPLADRlKKQGV 365
Cdd:PRK12770 173 KKVVVVGAGLTAVDAALEAVLLGAeKVYLayrrtineapagkyeierliargVEFLELVTP------VRIIGEG-RVEGV 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 366 EVhLKTKAtdVKADKSGITVSfeAAVEGEKPGLQAtayDRVLVAVGRSPNgKKIGAEKAGVTITERGFIPVDRQMRTNVP 445
Cdd:PRK12770 246 EL-AKMRL--GEPDESGRPRP--VPIPGSEFVLEA---DTVVFAIGEIPT-PPFAKECLGIELNRKGEIVVDEKHMTSRE 316
|
170 180
....*....|....*....|....*..
gi 2746980421 446 HIFAIGDIVGNPMLAHKATHEGKLAAE 472
Cdd:PRK12770 317 GVFAAGDVVTGPSKIGKAIKSGLRAAQ 343
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
19-77 |
3.08e-05 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 47.06 E-value: 3.08e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2746980421 19 VIEVLVAVGDSVAKDQGLVTLESDK--ATLEVPssAAGVVKELKVKVGDTLSEGALVLLLE 77
Cdd:PRK12999 1087 VVTVLVKEGDEVKAGDPLAVIEAMKmeTTITAP--VDGTVKRVLVKAGDQVEAGDLLVELE 1145
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
144-472 |
3.09e-05 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 46.70 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 144 VLGAGLGGYTAAFRAADLGLDTVLIERYASLGGvcLNVGCIPS----KAllHAAAVIDEVAHAG-DF------GVDfgqp 212
Cdd:PRK12810 148 VVGSGPAGLAAADQLARAGHKVTVFERADRIGG--LLRYGIPDfkleKE--VIDRRIELMEAEGiEFrtnvevGKD---- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 213 kITLDKLREYKEKVVgkLTGGLASmakqrkvrtvtgvasfvsPNELEIVGDDgktqllrfehciiAAG-SQAvkLPNFPW 291
Cdd:PRK12810 220 -ITAEELLAEYDAVF--LGTGAYK------------------PRDLGIPGRD-------------LDGvHFA--MDFLIQ 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 292 DDKRVMDSTDALELHDIPKTLLVVGGGIIGleMATVYSAL--GSK-VTVVEFMDqlMPGA--DKDLVKPLADRLKKQ--- 363
Cdd:PRK12810 264 NTRRVLGDETEPFISAKGKHVVVIGGGDTG--MDCVGTAIrqGAKsVTQRDIMP--MPPSrrNKNNPWPYWPMKLEVsna 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 364 ---GVEVH--LKTKATDVKADK-SGITVS--------FEAaVEGEKPGLQAtayDRVLVAVGRSPNGKKIgAEKAGVTIT 429
Cdd:PRK12810 340 heeGVEREfnVQTKEFEGENGKvTGVKVVrtelgegdFEP-VEGSEFVLPA---DLVLLAMGFTGPEAGL-LAQFGVELD 414
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2746980421 430 ERGFIPV-DRQMRTNVPHIFAIGDIVGNPMLAHKATHEGKLAAE 472
Cdd:PRK12810 415 ERGRVAApDNAYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAAR 458
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
132-176 |
4.28e-05 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 46.61 E-value: 4.28e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2746980421 132 SGKPADIECKMVVLGAGLGGYTAAFRAADLGLDTVLIERYASLGG 176
Cdd:PRK12842 2 ECMTNELTCDVLVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGG 46
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
19-73 |
5.93e-05 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 41.33 E-value: 5.93e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2746980421 19 VIEVLVAVGDSVAKDQGLVTLESDKATLEVPSSAAGVVKELKVKVGDTLSEGALV 73
Cdd:PRK05889 13 VLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLI 67
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
143-202 |
9.62e-05 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 45.41 E-value: 9.62e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2746980421 143 VVLGAGLGGYTAAFRAADLGLDTVLIERYASLGGVCLNVGC---IPSKALLHAAAVIDEVAHA 202
Cdd:PRK07843 11 VVVGSGAAGMVAALTAAHRGLSTVVVEKAPHYGGSTARSGGgvwIPNNEVLKRAGVPDTPEAA 73
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
22-76 |
1.03e-04 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 45.31 E-value: 1.03e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2746980421 22 VLVAVGDSVAKDQGLVTLESDKATLEVPSSAAGVVKELKVKVGDTLSEGALVLLL 76
Cdd:PRK14040 538 VIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTL 592
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
144-495 |
1.45e-04 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 44.85 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 144 VLGAGLGGYTAAFRAADLGLDTVLIERYASLGGVCLNVGCI-----PSKALLhaAAVIDEVAhagdfgvdfGQPKITLdk 218
Cdd:COG1148 145 VIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAQLHKTfpgldCPQCIL--EPLIAEVE---------ANPNITV-- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 219 lreykekvvgkLTGGlasmakqrkvrTVTGVASFVSPNELEIVGDDGKTQLLRFEHCIIAAGSQ---AVKLPNFPWD-DK 294
Cdd:COG1148 212 -----------YTGA-----------EVEEVSGYVGNFTVTIKKGPREEIEIEVGAIVLATGFKpydPTKLGEYGYGkYP 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 295 RVMDSTDALELHDIPKTLLVVGGGI----------------IGLE-------MATVYSAL-------GSKVTVVeFMDQL 344
Cdd:COG1148 270 NVITNLELERLLAAGKILRPSDGKEpksvafiqcvgsrdeeNGLPycsrvccMYALKQALylkeknpDADVYIF-YRDIR 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 345 MPGADKDLVKpladRLKKQGVeVHLKTKATDVKADKSG-ITVSFEAAVEGEKpglQATAYDRVLVAVG-RSPNGKKIGAE 422
Cdd:COG1148 349 TYGKYEEFYR----RAREDGV-RFIRGRVAEIEEDEGGkLVVTVEDTLLGEP---VEIEADLVVLATGmVPSEDNEELAK 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 423 KAGVTITERGFI--------PVDrqmrTNVPHIFAIGdIVGNPMLAHKATHEGKLAAEVAAG--EKKEWVarVIPSVAYT 492
Cdd:COG1148 421 LLKLPLDQDGFFleahpklrPVE----TATDGIFLAG-AAHGPKDIPESIAQATAAAARAIQllSKGELG--VEPSVAEV 493
|
...
gi 2746980421 493 NPE 495
Cdd:COG1148 494 DPE 496
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
137-176 |
3.58e-04 |
|
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: 43.28 E-value: 3.58e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2746980421 137 DIECKMVVLGAGLGGYTAAFRAADLGLDTVLIERYASLGG 176
Cdd:COG1053 1 DHEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
135-176 |
4.25e-04 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 43.17 E-value: 4.25e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2746980421 135 PADIECKMVVLGAGLGGYTAAFRAADLGLDTVLIERYASLGG 176
Cdd:PRK06134 8 PPDLECDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGG 49
|
|
| PRK12835 |
PRK12835 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
137-242 |
5.28e-04 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237221 [Multi-domain] Cd Length: 584 Bit Score: 42.87 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 137 DIECKMVVLGAGLGGYTAAFRAADLGLDTVLIERYASLGG-VCLNVGCI--PSKALLHAAAVIDEVahagdfgvdfgqpk 213
Cdd:PRK12835 9 DREVDVLVVGSGGGGMTAALTAAARGLDTLVVEKSAHFGGsTALSGGGIwvPGAPAQRREGYVPDP-------------- 74
|
90 100
....*....|....*....|....*....
gi 2746980421 214 itlDKLREYKEkvvgKLTGGLASMAKQRK 242
Cdd:PRK12835 75 ---EDVRRYLK----QITGGLVSAARLRA 96
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
141-176 |
5.28e-04 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 42.91 E-value: 5.28e-04
10 20 30
....*....|....*....|....*....|....*.
gi 2746980421 141 KMVVLGAGLGGYTAAFRAADLGLDTVLIERYASLGG 176
Cdd:COG1233 5 DVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
314-454 |
7.98e-04 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 41.97 E-value: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 314 VVGGGIIGLEMATVYSALGSKVTVVEFMDQLMpgADKDLVKPLADRLKKQGVEVHLKTKATDVKADKSGITvSFEAAVEG 393
Cdd:PRK10262 151 VIGGGNTAVEEALYLSNIASEVHLIHRRDGFR--AEKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVT-GVRLRDTQ 227
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2746980421 394 EKPGLQATAYDRVLVAVGRSPNgkkiGAEKAGVTITERGFIPVDRQM-----RTNVPHIFAIGDIV 454
Cdd:PRK10262 228 NSDNIESLDVAGLFVAIGHSPN----TAIFEGQLELENGYIKVQSGIhgnatQTSIPGVFAAGDVM 289
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
19-70 |
8.65e-04 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 39.80 E-value: 8.65e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2746980421 19 VIEVLVAVGDSVAKDQGLVTLESDKATLEVPSSAAGVVKELKVKVGDTLSEG 70
Cdd:PRK06549 72 ILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPG 123
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
144-178 |
1.16e-03 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 37.51 E-value: 1.16e-03
10 20 30
....*....|....*....|....*....|....*
gi 2746980421 144 VLGAGLGGYTAAFRAADLGLDTVLIERYASLGGVC 178
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNA 35
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
10-80 |
1.34e-03 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 41.63 E-value: 1.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2746980421 10 DIGD-YSDVPVIEVLVAVGDSVAKDQGLVTLESDKATLEVPSSAAGVVKELKVKVGDTLSEGALVLLLETEG 80
Cdd:PLN02528 5 QTGEgIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVED 76
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
143-176 |
1.41e-03 |
|
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: 41.50 E-value: 1.41e-03
10 20 30
....*....|....*....|....*....|....
gi 2746980421 143 VVLGAGLGGYTAAFRAADLGLDTVLIERYASLGG 176
Cdd:pfam00890 3 LVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGG 36
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
308-472 |
1.97e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 41.16 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 308 IPKTLLVVGGGIIGLEMATVYSALGSKVTVV-EFMDQLMPgADKDLVKpladRLKKQGVEVHLKTKATDVKADKSG--IT 384
Cdd:PRK12831 280 VGKKVAVVGGGNVAMDAARTALRLGAEVHIVyRRSEEELP-ARVEEVH----HAKEEGVIFDLLTNPVEILGDENGwvKG 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 385 VSFE---------------AAVEGEKPGLQAtayDRVLVAVGRSPNgKKIGAEKAGVTITERGFIPVDRQM-RTNVPHIF 448
Cdd:PRK12831 355 MKCIkmelgepdasgrrrpVEIEGSEFVLEV---DTVIMSLGTSPN-PLISSTTKGLKINKRGCIVADEETgLTSKEGVF 430
|
170 180
....*....|....*....|....
gi 2746980421 449 AIGDIVGNPMLAHKATHEGKLAAE 472
Cdd:PRK12831 431 AGGDAVTGAATVILAMGAGKKAAK 454
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
307-377 |
3.01e-03 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 40.61 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 307 DIPKTLLVVGGGIIGLEMATVYSALGSKVTVVE----------FMDQLMPGAD--KDLVKPLADRLKKQ-GVEVHLKTKA 373
Cdd:COG1148 138 PVNKRALVIGGGIAGMTAALELAEQGYEVYLVEkepelggraaQLHKTFPGLDcpQCILEPLIAEVEANpNITVYTGAEV 217
|
....
gi 2746980421 374 TDVK 377
Cdd:COG1148 218 EEVS 221
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
141-178 |
3.03e-03 |
|
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];
Pssm-ID: 442577 [Multi-domain] Cd Length: 445 Bit Score: 40.22 E-value: 3.03e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2746980421 141 KMVVLGAGLGGYTAAFRAADLGLDTVLIERYASLGGVC 178
Cdd:COG3349 5 RVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGGRA 42
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
143-178 |
3.59e-03 |
|
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440845 [Multi-domain] Cd Length: 443 Bit Score: 40.20 E-value: 3.59e-03
10 20 30
....*....|....*....|....*....|....*.
gi 2746980421 143 VVLGAGLGGYTAAFRAADLGLDTVLIERYASLGGVC 178
Cdd:COG1232 5 AVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLI 40
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
19-77 |
4.64e-03 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 40.09 E-value: 4.64e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2746980421 19 VIEVLVAVGDSVAKDQGLVTLESDKATLEVPSSAAGVVKELKVKVGDTLSEGALVLLLE 77
Cdd:PRK14042 536 IIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
138-221 |
7.42e-03 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 39.06 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2746980421 138 IECKMVVLGAGLGGYTAAFRAADLGLDTVLIERYASlggvclnvgcipskALLHAAAVIDEVAHAGDfGVDFGQPKITLD 217
Cdd:PRK05329 1 MKFDVLVIGGGLAGLTAALAAAEAGKRVALVAKGQG--------------ALHFSSGSIDLLGYLPD-GQPVSDPFEALA 65
|
....
gi 2746980421 218 KLRE 221
Cdd:PRK05329 66 ALAE 69
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
138-176 |
7.83e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 39.04 E-value: 7.83e-03
10 20 30
....*....|....*....|....*....|....*....
gi 2746980421 138 IECKMVVLGAGLGGYTAAFRAADLGLDTVLIERYASLGG 176
Cdd:PRK12839 7 HTYDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKASTCGG 45
|
|
| |
