|
Name |
Accession |
Description |
Interval |
E-value |
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
114-562 |
0e+00 |
|
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.
Pssm-ID: 273568 [Multi-domain] Cd Length: 460 Bit Score: 584.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVEKSELGGTCLNRGCIPTKTYLHNAEIIENIGHAANRGIVIENpnFTVDMEKLL 193
Cdd:TIGR01350 4 VIVIGGGPGGYVAAIRAAQLGLKVALVEKEYLGGTCLNVGCIPTKALLHSAEVYDEIKHAKDLGIEVEN--VSVDWEKMQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 194 ETKSKVVNTLVGGVAGLLRSYGVTVHKGIGTITKDKNVLVNGS---ELLETKKIILAGGSKVSKINVP-GMESPLVMTSD 269
Cdd:TIGR01350 82 KRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGEngeETLEAKNIIIATGSRPRSLPGPfDFDGKVVITST 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 270 DILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTKLQEIIEEN 349
Cdd:TIGR01350 162 GALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEKND 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 350 GQLRIKVEGKD--DIIASKALLSIGRMPDLEGIG--EVEFELD-RGCIKVNEYMETSVPGIYAPGDINGTKMLAHAAFRM 424
Cdd:TIGR01350 242 DQVTYENKGGEteTLTGEKVLVAVGRKPNTEGLGleKLGVELDeRGRIVVDEYMRTNVPGIYAIGDVIGGPMLAHVASHE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 425 GEVSAENALKGNHAVAKLNLTPAAIYTLPEVAAVGLTEEQAREK-YDVAIGKFNFAANGRAIASDAAQGFVKVIADKKYG 503
Cdd:TIGR01350 322 GIVAAENIAGKEPAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAgYDVKIGKFPFAANGKALALGETDGFVKIIADKKTG 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 892236353 504 EILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSEVMYEAFADVLGMAIH 562
Cdd:TIGR01350 402 EILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEAIKEAALAALGKPIH 460
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
114-558 |
4.07e-176 |
|
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: 505.39 E-value: 4.07e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVEKSELGGTCLNRGCIPTKTYLHNAEIIENIGHAANRGIVIENPnfTVDMEKLL 193
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVEKGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISAGAP--SVDWAALM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 194 ETKSKVVNTLVGGVAGLLRSYGVTVHKGIGTITKDKNVLVNGSELLETKKIILAGGSKVSKINVPGMESPLVMTSDDILE 273
Cdd:COG1249 84 ARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVTGGETLTADHIVIATGSRPRVPPIPGLDEVRVLTSDEALE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 274 MNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTKLQEIIEENGQLR 353
Cdd:COG1249 164 LEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDGVT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 354 IKVEGKDD---IIASKALLSIGRMPDLEGIG--EVEFELD-RGCIKVNEYMETSVPGIYAPGDINGTKMLAHAAFRMGEV 427
Cdd:COG1249 244 VTLEDGGGeeaVEADKVLVATGRRPNTDGLGleAAGVELDeRGGIKVDEYLRTSVPGIYAIGDVTGGPQLAHVASAEGRV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 428 SAENALKGNHAVAKLNLTPAAIYTLPEVAAVGLTEEQAREK-YDVAIGKFNFAANGRAIASDAAQGFVKVIADKKYGEIL 506
Cdd:COG1249 324 AAENILGKKPRPVDYRAIPSVVFTDPEIASVGLTEEEAREAgIDVKVGKFPFAANGRALALGETEGFVKLIADAETGRIL 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 892236353 507 GVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSEVMYEAFADVLG 558
Cdd:COG1249 404 GAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAALALLG 455
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
114-562 |
1.52e-155 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 453.06 E-value: 1.52e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVEKSELGGTCLNRGCIPTKTYLHNAEIIENIGHAANRGIVIENPNFtvDMEKLL 193
Cdd:PRK06416 7 VIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIKAENVGI--DFKKVQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 194 ETKSKVVNTLVGGVAGLLRSYGVTVHKGIGTITKDKNVLVN---GSELLETKKIILAGGSKVskINVPGME--SPLVMTS 268
Cdd:PRK06416 85 EWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMtedGEQTYTAKNIILATGSRP--RELPGIEidGRVIWTS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 269 DDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTKLQEIIEE 348
Cdd:PRK06416 163 DEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPGEDKEISKLAERALKKRGIKIKTGAKAKKVEQT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 349 NGQLRIKVE--GKDDIIASKALLS-IGRMPDLEGIG--EVEFELDRGCIKVNEYMETSVPGIYAPGDINGTKMLAHAAFR 423
Cdd:PRK06416 243 DDGVTVTLEdgGKEETLEADYVLVaVGRRPNTENLGleELGVKTDRGFIEVDEQLRTNVPNIYAIGDIVGGPMLAHKASA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 424 MGEVSAENALKGNHAVAKLNLtPAAIYTLPEVAAVGLTEEQAREK-YDVAIGKFNFAANGRAIASDAAQGFVKVIADKKY 502
Cdd:PRK06416 323 EGIIAAEAIAGNPHPIDYRGI-PAVTYTHPEVASVGLTEAKAKEEgFDVKVVKFPFAGNGKALALGETDGFVKLIFDKKD 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 503 GEILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSEVMYEAFADVLGMAIH 562
Cdd:PRK06416 402 GEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEALGEAALAAAGKPLH 461
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
114-562 |
5.77e-138 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 408.03 E-value: 5.77e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVEKSELGGTCLNRGCIPTKTYLHNAEIIENIGHAANRGIVIENPnfTVDMEKLL 193
Cdd:PRK06292 6 VIVIGAGPAGYVAARRAAKLGKKVALIEKGPLGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHADGP--KIDFKKVM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 194 ETKSKVVNTLVGGV-AGLLRSYGVTVHKGIGTITKDKNVLVNGsELLETKKIILAGGSKVskINVPGMESPL---VMTSD 269
Cdd:PRK06292 84 ARVRRERDRFVGGVvEGLEKKPKIDKIKGTARFVDPNTVEVNG-ERIEAKNIVIATGSRV--PPIPGVWLILgdrLLTSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 270 DILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKgMTILTGTKLQEIiEEN 349
Cdd:PRK06292 161 DAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILSKE-FKIKLGAKVTSV-EKS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 350 GQLRIKVEGKDD----IIASKALLSIGRMPDLEGIG--EVEFELD-RGCIKVNEYMETSVPGIYAPGDINGTKMLAHAAF 422
Cdd:PRK06292 239 GDEKVEELEKGGktetIEADYVLVATGRRPNTDGLGleNTGIELDeRGRPVVDEHTQTSVPGIYAAGDVNGKPPLLHEAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 423 RMGEVSAENALKGNHAVAKLNLTPAAIYTLPEVAAVGLTEEQAREK-YDVAIGKFNFAANGRAIASDAAQGFVKVIADKK 501
Cdd:PRK06292 319 DEGRIAAENAAGDVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAgIDYVVGEVPFEAQGRARVMGKNDGFVKVYADKK 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 892236353 502 YGEILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSEVMYEAFADVLGMAIH 562
Cdd:PRK06292 399 TGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRTALRDLFSKLIH 459
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
114-562 |
8.05e-121 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 364.63 E-value: 8.05e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVE-------KSELGGTCLNRGCIPTKTYLHNAEIIENIGHA-ANRGIVIENpnF 185
Cdd:PRK06327 7 VVVIGAGPGGYVAAIRAAQLGLKVACIEawknpkgKPALGGTCLNVGCIPSKALLASSEEFENAGHHfADHGIHVDG--V 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 186 TVDMEKLLETKSKVVNTLVGGVAGLLRSYGVTVHKGIGTITKDKN------VLVNGSELLETKKIILAGGSKvsKINVPG 259
Cdd:PRK06327 85 KIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVGKTDagyeikVTGEDETVITAKHVIIATGSE--PRHLPG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 260 M--ESPLVMTSDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTIL 337
Cdd:PRK06327 163 VpfDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAAADEQVAKEAAKAFTKQGLDIH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 338 TGTKLQEIIEENGQLRIKVEGKDD----IIASKALLSIGRMPDLEGIG--EVEFELD-RGCIKVNEYMETSVPGIYAPGD 410
Cdd:PRK06327 243 LGVKIGEIKTGGKGVSVAYTDADGeaqtLEVDKLIVSIGRVPNTDGLGleAVGLKLDeRGFIPVDDHCRTNVPNVYAIGD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 411 INGTKMLAHAAFRMGEVSAENAlKGNHAVAKLNLTPAAIYTLPEVAAVGLTEEQAR-EKYDVAIGKFNFAANGRAIASDA 489
Cdd:PRK06327 323 VVRGPMLAHKAEEEGVAVAERI-AGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLKaEGVEYKAGKFPFMANGRALAMGE 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 892236353 490 AQGFVKVIADKKYGEILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSEVMYEAFADVLGMAIH 562
Cdd:PRK06327 402 PDGFVKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEVWHEAALAVDKRPLH 474
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
115-547 |
1.11e-107 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 330.63 E-value: 1.11e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 115 VVIGGGPAGYVAAIKAAQFGGKVALVEKSELGGTCLNRGCIPTKTYLHNAEIIENIGHAANRGIVIENPnFTVDMEKLLE 194
Cdd:PRK06370 9 IVIGAGQAGPPLAARAAGLGMKVALIERGLLGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGGP-VSVDFKAVMA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 195 TKSKVVNTLVGGVAGLLRSY-GVTVHKGIGTITKDKNVLVNGsELLETKKIILAGGSKVSKINVPGMESPLVMTSDDILE 273
Cdd:PRK06370 88 RKRRIRARSRHGSEQWLRGLeGVDVFRGHARFESPNTVRVGG-ETLRAKRIFINTGARAAIPPIPGLDEVGYLTNETIFS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 274 MNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTKLQEIIEENGQLR 353
Cdd:PRK06370 167 LDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILEREGIDVRLNAECIRVERDGDGIA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 354 IKVE---GKDDIIASKALLSIGRMPDLEGIG----EVEFElDRGCIKVNEYMETSVPGIYAPGDINGTKMLAHAAFRMGE 426
Cdd:PRK06370 247 VGLDcngGAPEITGSHILVAVGRVPNTDDLGleaaGVETD-ARGYIKVDDQLRTTNPGIYAAGDCNGRGAFTHTAYNDAR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 427 VSAENALKGNHAVAKLNLTPAAIYTLPEVAAVGLTEEQAREK-YDVAIGKFNFAANGRAIASDAAQGFVKVIADKKYGEI 505
Cdd:PRK06370 326 IVAANLLDGGRRKVSDRIVPYATYTDPPLARVGMTEAEARKSgRRVLVGTRPMTRVGRAVEKGETQGFMKVVVDADTDRI 405
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 892236353 506 LGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSE 547
Cdd:PRK06370 406 LGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSE 447
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
114-547 |
1.01e-90 |
|
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: 286.63 E-value: 1.01e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVEKSELGGTCLNRGCIPTKTYLHNAEIIENIGHAANRGIVIEnpnFTVDMEKLL 193
Cdd:TIGR02053 3 LVIIGSGAAAFAAAIKAAELGASVAMVERGPLGGTCVNVGCVPSKMLLRAAEVAHYARKPPFGGLAAT---VAVDFGELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 194 ETKSKVVNTL-VGGVAGLLRSYGVTVHKGIGTITKDKNVLVN-GSELLETKKIILAGGSKVSKINVPGMESPLVMTSDDI 271
Cdd:TIGR02053 80 EGKREVVEELrHEKYEDVLSSYGVDYLRGRARFKDPKTVKVDlGREVRGAKRFLIATGARPAIPPIPGLKEAGYLTSEEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 272 LEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTKLQEIIEENGQ 351
Cdd:TIGR02053 160 LALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSDRLLPREEPEISAAVEEALAEEGIEVVTSAQVKAVSVRGGG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 352 LRIKVEGKD---DIIASKALLSIGRMPDLEGIG--EVEFELD-RGCIKVNEYMETSVPGIYAPGDINGTKMLAHAAFRMG 425
Cdd:TIGR02053 240 KIITVEKPGgqgEVEADELLVATGRRPNTDGLGleKAGVKLDeRGGILVDETLRTSNPGIYAAGDVTGGLQLEYVAAKEG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 426 EVSAENALKGNHAVAKLNLTPAAIYTLPEVAAVGLTEEQAREK-YDVAIGKFNFAANGRAIASDAAQGFVKVIADKKYGE 504
Cdd:TIGR02053 320 VVAAENALGGANAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAgIECDCRTLPLTNVPRARINRDTRGFIKLVAEPGTGK 399
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 892236353 505 ILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSE 547
Cdd:TIGR02053 400 VLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAE 442
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
116-547 |
1.29e-70 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 233.90 E-value: 1.29e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 116 VIGGGPAGYVAAIKAAQFGGKVALVEKSELGGTCLNRGCIPTKTYLHNAEIIENIGH-AANRGIVIENPNFtvDMEKLLE 194
Cdd:PRK06116 9 VIGGGSGGIASANRAAMYGAKVALIEAKRLGGTCVNVGCVPKKLMWYGAQIAEAFHDyAPGYGFDVTENKF--DWAKLIA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 195 TKSKVVNTLVGGVAGLLRSYGVTVHKGIGTITKDKNVLVNGsELLETKKIILAGGSKVSKINVPGMEspLVMTSDDILEM 274
Cdd:PRK06116 87 NRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNG-ERYTADHILIATGGRPSIPDIPGAE--YGITSDGFFAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 275 NEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTKLQEII-EENGQLR 353
Cdd:PRK06116 164 EELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEkNADGSLT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 354 IKVEGKDDIIASKALLSIGRMPDLEGIG----EVEFElDRGCIKVNEYMETSVPGIYAPGDINGTKMLAHAAFRMGEVSA 429
Cdd:PRK06116 244 LTLEDGETLTVDCLIWAIGREPNTDGLGlenaGVKLN-EKGYIIVDEYQNTNVPGIYAVGDVTGRVELTPVAIAAGRRLS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 430 ENALKGNhAVAKLN--LTPAAIYTLPEVAAVGLTEEQAREKY---DVAIGKFNFAANGRAIASDAAQGFVKVIADKKYGE 504
Cdd:PRK06116 323 ERLFNNK-PDEKLDysNIPTVVFSHPPIGTVGLTEEEAREQYgedNVKVYRSSFTPMYTALTGHRQPCLMKLVVVGKEEK 401
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 892236353 505 ILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSE 547
Cdd:PRK06116 402 VVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAE 444
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
114-547 |
3.20e-64 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 217.33 E-value: 3.20e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVEK-SELGGTCLNRGCIPTKTYLHNA-EIIEnighAANRGIVIEN---PNFTvd 188
Cdd:PRK05249 8 LVVIGSGPAGEGAAMQAAKLGKRVAVIERyRNVGGGCTHTGTIPSKALREAVlRLIG----FNQNPLYSSYrvkLRIT-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 189 MEKLLETKSKVVNTLVGGVAGLLRSYGVTVHKGIGTITkDKN-VLV----NGSELLETKKIILAGGSKVSKI-NVPgMES 262
Cdd:PRK05249 82 FADLLARADHVINKQVEVRRGQYERNRVDLIQGRARFV-DPHtVEVecpdGEVETLTADKIVIATGSRPYRPpDVD-FDH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 263 PLVMTSDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGtkl 342
Cdd:PRK05249 160 PRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSFLDDEISDALSYHLRDSGVTIRHN--- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 343 qEIIEengqlriKVEGKDD-----------IIASKALLSIGRMP-----DLEGIGeveFELD-RGCIKVNEYMETSVPGI 405
Cdd:PRK05249 237 -EEVE-------KVEGGDDgvivhlksgkkIKADCLLYANGRTGntdglNLENAG---LEADsRGQLKVNENYQTAVPHI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 406 YAPGDINGTKMLAHAAFRMGEVSAENALkGNHAVAKLNLTPAAIYTLPEVAAVGLTEEQAREK---YDVAIGKFNFAANG 482
Cdd:PRK05249 306 YAVGDVIGFPSLASASMDQGRIAAQHAV-GEATAHLIEDIPTGIYTIPEISSVGKTEQELTAAkvpYEVGRARFKELARA 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 892236353 483 rAIASDAAqGFVKVIADKKYGEILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSE 547
Cdd:PRK05249 385 -QIAGDNV-GMLKILFHRETLEILGVHCFGERATEIIHIGQAIMEQKGTIEYFVNTTFNYPTMAE 447
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
116-547 |
3.77e-60 |
|
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, e.g., for maintaining the cellular thiol/disulfide status and for protecting against reactive oxygen species such as hydrogen peroxide. Glutathione-disulfide reductase regenerates reduced glutathione from oxidized glutathione (glutathione disulfide) + NADPH. This model represents one of two closely related subfamilies of glutathione-disulfide reductase. Both are closely related to trypanothione reductase, and separate models are built so each of the three can describe proteins with conserved function. This model describes glutathione-disulfide reductases of plants and some bacteria, including cyanobacteria. [Energy metabolism, Electron transport]
Pssm-ID: 213618 [Multi-domain] Cd Length: 446 Bit Score: 205.82 E-value: 3.77e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 116 VIGGGPAGYVAAIKAAQFGGKVALVEKSELGGTCLNRGCIPTKTYLHNAEIIENIGHAANRGIVIENPNFtvDMEKLLET 195
Cdd:TIGR01424 7 VIGAGSGGVRAARLAAALGAKVAIAEEFRVGGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGWTVGKARF--DWKKLLAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 196 KSKVVNTLVGGVAGLLRSYGVTVHKGIGTITKDKNVLVNGSELLET-KKIILAGGSKVSKINVPGMEspLVMTSDDILEM 274
Cdd:TIGR01424 85 KDQEIARLSGLYRKGLANAGAELLDGRAELVGPNTVEVLASGKTYTaEKILIAVGGRPPKPALPGHE--LGITSNEAFHL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 275 NEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTKLQEIIE-ENGQLR 353
Cdd:TIGR01424 163 PTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRGKEILRGFDDDMRRGLAAALEERGIRILPEDSITSISKdDDGRLK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 354 IKVEGKDDIIASKALLSIGRMPDLEGIG--EVEFEL-DRGCIKVNEYMETSVPGIYAPGDINGTKMLAHAAFRMGEVSAE 430
Cdd:TIGR01424 243 ATLSKHEEIVADVVLFATGRSPNTNGLGleAAGVRLnDLGAIAVDEYSRTSTPSIYAVGDVTDRINLTPVAIHEATCFAE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 431 NALKGNHAVAKLNLTPAAIYTLPEVAAVGLTEEQAREKY-DVAIGKFNFAANGRAIASDAAQGFVKVIADKKYGEILGVH 509
Cdd:TIGR01424 323 TEFGNNPTSFDHDLIATAVFSQPPIGTVGLTEEEARRKFgDIEVYRAEFRPMKATFSGRQEKTLMKLVVDAKDDKVLGAH 402
|
410 420 430
....*....|....*....|....*....|....*...
gi 892236353 510 IIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSE 547
Cdd:TIGR01424 403 MVGPDAAEIIQGLAIALKMGATKDDFDSTVAVHPTSAE 440
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
114-548 |
5.58e-60 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 205.57 E-value: 5.58e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 114 IVVIGGGPAGyvaAIKAAQFGGK-VALVEKSELGGTCLNRGCIPTKTYLHNAEIIENIGHAANRGIVIENPNftVDMEKL 192
Cdd:PRK07846 4 LIIIGTGSGN---SILDERFADKrIAIVEKGTFGGTCLNVGCIPTKMFVYAADVARTIREAARLGVDAELDG--VRWPDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 193 letKSKVVNTL----VGGVAGLLR-SYGVTVHKGIGTITKDKNVLVNGSELLETKKIILAGGSKVSKINVPGMESPLVMT 267
Cdd:PRK07846 79 ---VSRVFGRIdpiaAGGEEYRGRdTPNIDVYRGHARFIGPKTLRTGDGEEITADQVVIAAGSRPVIPPVIADSGVRYHT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 268 SDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKgMTILTGTKLQEIIE 347
Cdd:PRK07846 156 SDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLDDDISERFTELASKR-WDVRLGRNVVGVSQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 348 ENGQLRIKVEGKDDIIASKALLSIGRMP--DLEGIGEVEFELDR-GCIKVNEYMETSVPGIYAPGDINGTKMLAHAAFRM 424
Cdd:PRK07846 235 DGSGVTLRLDDGSTVEADVLLVATGRVPngDLLDAAAAGVDVDEdGRVVVDEYQRTSAEGVFALGDVSSPYQLKHVANHE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 425 GEVSAENALKGNH-AVAKLNLTPAAIYTLPEVAAVGLTEEQAREK-YDVAIGKFNFA--ANGRAIASDaaQGFVKVIADK 500
Cdd:PRK07846 315 ARVVQHNLLHPDDlIASDHRFVPAAVFTHPQIASVGLTENEARAAgLDITVKVQNYGdvAYGWAMEDT--TGFVKLIADR 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 892236353 501 KYGEILGVHIIGPAAAELINEASSIIEMEITVEEMLKT---IhgHPTYSEV 548
Cdd:PRK07846 393 DTGRLLGAHIIGPQASTLIQPLIQAMSFGLDAREMARGqywI--HPALPEV 441
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
114-425 |
2.29e-59 |
|
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: 199.47 E-value: 2.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVEkseLGGTCLNRGCIPTKTYLHNAEIIENIGHAAnrgivienpnftvdmeKLL 193
Cdd:pfam07992 3 VVVIGGGPAGLAAALTLAQLGGKVTLIE---DEGTCPYGGCVLSKALLGAAEAPEIASLWA----------------DLY 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 194 ETKSKVVNTLVGGVAGLLRSYGVTVHKGIGTITKDKNVLVNGSELlETKKIILAGGSKVSKINVPGMESPL-----VMTS 268
Cdd:pfam07992 64 KRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELVDGDGETI-TYDRLVIATGARPRLPPIPGVELNVgflvrTLDS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 269 DDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTKLQEIIEE 348
Cdd:pfam07992 143 AEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGD 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 892236353 349 NGQLRIKVEGKDDIIASKALLSIGRMPDLEGIGEVEFELD-RGCIKVNEYMETSVPGIYAPGDINGTK-MLAHAAFRMG 425
Cdd:pfam07992 223 GDGVEVILKDGTEIDADLVVVAIGRRPNTELLEAAGLELDeRGGIVVDEYLRTSVPGIYAAGDCRVGGpELAQNAVAQG 301
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
114-554 |
1.41e-57 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 198.82 E-value: 1.41e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVEKSEL--GGTCLNRGCIPTKTYLHNAEiienighaanrgiviENPNFtvdmEK 191
Cdd:PRK07251 6 LIVIGFGKAGKTLAAKLASAGKKVALVEESKAmyGGTCINIGCIPTKTLLVAAE---------------KNLSF----EQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 192 LLETKSKVVNTLVGGVAGLLRSYGVTVHKGIGTITKDKNVLVNG---SELLETKKIILAGGSKVSKINVPGM-ESPLVMT 267
Cdd:PRK07251 67 VMATKNTVTSRLRGKNYAMLAGSGVDLYDAEAHFVSNKVIEVQAgdeKIELTAETIVINTGAVSNVLPIPGLaDSKHVYD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 268 SDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTKLQEIIE 347
Cdd:PRK07251 147 STGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYMEEDGITFLLNAHTTEVKN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 348 ENGQLRIKVEGKDDIIASkALLSIGRMPDLEGIG--EVEFEL-DRGCIKVNEYMETSVPGIYAPGDINGTKMLAHAA--- 421
Cdd:PRK07251 227 DGDQVLVVTEDETYRFDA-LLYATGRKPNTEPLGleNTDIELtERGAIKVDDYCQTSVPGVFAVGDVNGGPQFTYISldd 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 422 FRMgevsAENALKGN--HAVAKLNLTPAAIYTLPEVAAVGLTEEQAREK-YDVAIGKFNFAANGRAIASDAAQGFVKVIA 498
Cdd:PRK07251 306 FRI----VFGYLTGDgsYTLEDRGNVPTTMFITPPLSQVGLTEKEAKEAgLPYAVKELLVAAMPRAHVNNDLRGAFKVVV 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 892236353 499 DKKYGEILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSEVMYEAFA 554
Cdd:PRK07251 382 NTETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAENLNDLFN 437
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
114-535 |
3.21e-52 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 187.28 E-value: 3.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVEKSELGGTCLNRGCIPTKTYLHNAEIIE-NIGHAANRGIVIENPnfTVDMEKL 192
Cdd:PRK13748 101 VAVIGSGGAAMAAALKAVEQGARVTLIERGTIGGTCVNVGCVPSKIMIRAAHIAHlRRESPFDGGIAATVP--TIDRSRL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 193 LETKSKVVNTL-VGGVAGLLRSY-GVTVHKGIGTItKDKNVLV----NGSEL-LETKKIILAGGSKVSKINVPGMESPLV 265
Cdd:PRK13748 179 LAQQQARVDELrHAKYEGILDGNpAITVLHGEARF-KDDQTLIvrlnDGGERvVAFDRCLIATGASPAVPPIPGLKETPY 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 266 MTSDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVI---EMMDRIVPAMDAEVSKNLRLilerKGMTILTGTKL 342
Cdd:PRK13748 258 WTSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILarsTLFFREDPAIGEAVTAAFRA----EGIEVLEHTQA 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 343 QEIIEENGQLRIKVeGKDDIIASKALLSIGRMP-----DLEGIGeVEFElDRGCIKVNEYMETSVPGIYAPGDINGTKML 417
Cdd:PRK13748 334 SQVAHVDGEFVLTT-GHGELRADKLLVATGRAPntrslALDAAG-VTVN-AQGAIVIDQGMRTSVPHIYAAGDCTDQPQF 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 418 AHAAFRMGEVSAENALKGNhavAKLNLT--PAAIYTLPEVAAVGLTEEQAR----EKYDVAIGKFNFAangRAIASDAAQ 491
Cdd:PRK13748 411 VYVAAAAGTRAAINMTGGD---AALDLTamPAVVFTDPQVATVGYSEAEAHhdgiETDSRTLTLDNVP---RALANFDTR 484
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 892236353 492 GFVKVIADKKYGEILGVHIIGPAAAELINEASSIIEMEITVEEM 535
Cdd:PRK13748 485 GFIKLVIEEGSGRLIGVQAVAPEAGELIQTAALAIRNRMTVQEL 528
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
94-562 |
4.73e-50 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 183.19 E-value: 4.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 94 SSVPVASTSNDDDKSDDAFDIVVIGGGPAGYVAAIKAAQFGGKVALV--EKSELGGTCLNRGCIPTKTYLHNA---EIIE 168
Cdd:PTZ00153 99 LRANGFATSQSMNFSDEEYDVGIIGCGVGGHAAAINAMERGLKVIIFtgDDDSIGGTCVNVGCIPSKALLYATgkyRELK 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 169 NIGHAANRGI-----------VIENPN-----FTVDMEKLLETKSKVVNTLVGGVAGLLRSYGVTVHKGIGTITK----- 227
Cdd:PTZ00153 179 NLAKLYTYGIytnafkngkndPVERNQlvadtVQIDITKLKEYTQSVIDKLRGGIENGLKSKKFCKNSEHVQVIYerghi 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 228 -DKNVLVNGSELLE--TKKIILAGGSKVSKINVPGMESPLVMTSDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKV 304
Cdd:PTZ00153 259 vDKNTIKSEKSGKEfkVKNIIIATGSTPNIPDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEV 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 305 TVIEMMDRIVPAMDAEVSKNL-RLILERKGMTILTGTKLQEIIEENG------QLRIKVEGKDD-----------IIASK 366
Cdd:PTZ00153 339 VSFEYSPQLLPLLDADVAKYFeRVFLKSKPVRVHLNTLIEYVRAGKGnqpviiGHSERQTGESDgpkknmndikeTYVDS 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 367 ALLSIGRMPDLEGIG--EVEFELDRGCIKVNEYMETS------VPGIYAPGDINGTKMLAHAAFRMG----------EVS 428
Cdd:PTZ00153 419 CLVATGRKPNTNNLGldKLKIQMKRGFVSVDEHLRVLredqevYDNIFCIGDANGKQMLAHTASHQAlkvvdwiegkGKE 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 429 AENALKGNHAVAKLNL--TPAAIYTLPEVAAVGLTEEQAREKY---DVAIGKFNFAANGRAIA----------------- 486
Cdd:PTZ00153 499 NVNINVENWASKPIIYknIPSVCYTTPELAFIGLTEKEAKELYppdNVGVEISFYKANSKVLCennisfpnnsknnsynk 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 487 -----SDAAQGFVKVIADKKYGEILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSEVMYEAFADVLGMAI 561
Cdd:PTZ00153 579 gkyntVDNTEGMVKIVYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDAAFKAIAGVRT 658
|
.
gi 892236353 562 H 562
Cdd:PTZ00153 659 H 659
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
116-547 |
5.11e-50 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 180.01 E-value: 5.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 116 VIGGGPAGYVAAIKAAQFGGKVALVE------KSE----LGGTCLNRGCIPTKTYLHNAEIIENIGHAANRGIVIeNPNF 185
Cdd:PLN02507 30 VIGAGSGGVRAARFSANFGAKVGICElpfhpiSSEsiggVGGTCVIRGCVPKKILVYGATFGGEFEDAKNYGWEI-NEKV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 186 TVDMEKLLETKSKVVNTLVGGVAGLLRSYGVTVHKGIGTITKDKNVLV---NGSELLET-KKIILAGGSKVSKINVPGME 261
Cdd:PLN02507 109 DFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVtqlDGTKLRYTaKHILIATGSRAQRPNIPGKE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 262 spLVMTSDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTK 341
Cdd:PLN02507 189 --LAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRAVVARNLEGRGINLHPRTN 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 342 LQEIIEENGQLRIKVEGKDDIIASKALLSIGRMPDLEGIG--EVEFELDR-GCIKVNEYMETSVPGIYAPGDINGTKMLA 418
Cdd:PLN02507 267 LTQLTKTEGGIKVITDHGEEFVADVVLFATGRAPNTKRLNleAVGVELDKaGAVKVDEYSRTNIPSIWAIGDVTNRINLT 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 419 HAAFRMGEVSAENALKGNHAVAKLNLTPAAIYTLPEVAAVGLTEEQARE--KYDVAIGKFNFAANGRAIASDAAQGFVKV 496
Cdd:PLN02507 347 PVALMEGTCFAKTVFGGQPTKPDYENVACAVFCIPPLSVVGLSEEEAVEqaKGDILVFTSSFNPMKNTISGRQEKTVMKL 426
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 892236353 497 IADKKYGEILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSE 547
Cdd:PLN02507 427 IVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAE 477
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
114-552 |
1.27e-48 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 175.43 E-value: 1.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVEKSELGGTCLNRGCIPTKTYLHNAEIIENIGHAANRGI-VIENPNFTVDMEKl 192
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIERDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIrFIDDGEARVDLPA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 193 letkskvVNTLVGGVA---------GLLRSyGVTVHKGIGTITKDK----NVLVN----GSELLETKKIILAGGS--KVS 253
Cdd:PRK07845 83 -------VNARVKALAaaqsadiraRLERE-GVRVIAGRGRLIDPGlgphRVKVTtadgGEETLDADVVLIATGAspRIL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 254 KINVPGMESplVMTSDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKG 333
Cdd:PRK07845 155 PTAEPDGER--ILTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPGEDADAAEVLEEVFARRG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 334 MTILTGTKLQEIIEENGQLRIKVEGKDDIIASKALLSIGRMPDLEGIG--EVEFELDR-GCIKVNEYMETSVPGIYAPGD 410
Cdd:PRK07845 233 MTVLKRSRAESVERTGDGVVVTLTDGRTVEGSHALMAVGSVPNTAGLGleEAGVELTPsGHITVDRVSRTSVPGIYAAGD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 411 INGTKMLAHAAFRMGEVSAENALkgNHAVAKLNLT--PAAIYTLPEVAAVGLTEEQARE-KYDVAIGKFNFAANGRAIAS 487
Cdd:PRK07845 313 CTGVLPLASVAAMQGRIAMYHAL--GEAVSPLRLKtvASNVFTRPEIATVGVSQAAIDSgEVPARTVMLPLATNPRAKMS 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 892236353 488 DAAQGFVKVIADKKYGEILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSEVMYEA 552
Cdd:PRK07845 391 GLRDGFVKLFCRPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYPSLSGSITEA 455
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
114-552 |
1.55e-47 |
|
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and related species, can form a disulfide-linked dimer called mycothione. This enzyme can reduce mycothione to regenerate two mycothiol molecules. The enzyme shows some sequence similarity to glutathione-disulfide reductase, trypanothione-disulfide reductase, and dihydrolipoamide dehydrogenase. The characterized protein from M. tuberculosis, a homodimer, has FAD as a cofactor, one per monomer, and uses NADPH as a substrate.
Pssm-ID: 132493 [Multi-domain] Cd Length: 452 Bit Score: 172.25 E-value: 1.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 114 IVVIGGGPAGyvaAIKAAQFGGK-VALVEKSELGGTCLNRGCIPTKTYLHNAEIIENIGHAANRGIvienpNFTVDMEKL 192
Cdd:TIGR03452 5 LIIIGTGSGN---SIPDPRFADKrIAIVEKGTFGGTCLNVGCIPTKMFVYAAEVAQSIGESARLGI-----DAEIDSVRW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 193 LETKSKVVNTLVGGVAGLLRSY-------GVTVHKGIGTITKDKNVLVNGSELLETKKIILAGGSKvsKINVPGMESPLV 265
Cdd:TIGR03452 77 PDIVSRVFGDRIDPIAAGGEDYrrgdetpNIDVYDGHARFVGPRTLRTGDGEEITGDQIVIAAGSR--PYIPPAIADSGV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 266 M--TSDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKgMTILTGTKLQ 343
Cdd:TIGR03452 155 RyhTNEDIMRLPELPESLVIVGGGYIAAEFAHVFSALGTRVTIVNRSTKLLRHLDEDISDRFTEIAKKK-WDIRLGRNVT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 344 EIIEENGQLRIKVEGKDDIIASKALLSIGRMP-----DLEGIGeVEFElDRGCIKVNEYMETSVPGIYAPGDINGTKMLA 418
Cdd:TIGR03452 234 AVEQDGDGVTLTLDDGSTVTADVLLVATGRVPngdllDAEAAG-VEVD-EDGRIKVDEYGRTSARGVWALGDVSSPYQLK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 419 HAAFRMGEVSAENAL------KGNHAVaklnlTPAAIYTLPEVAAVGLTEEQAREK-YD--VAIGKFNFAANGRAIASDa 489
Cdd:TIGR03452 312 HVANAEARVVKHNLLhpndlrKMPHDF-----VPSAVFTHPQIATVGLTEQEAREAgHDitVKIQNYGDVAYGWAMEDT- 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 892236353 490 aQGFVKVIADKKYGEILGVHIIGPAAAELINEASSIIEMEITVEEML-KTIHGHPTYSEVMYEA 552
Cdd:TIGR03452 386 -TGFCKLIADRDTGKLLGAHIIGPQASSLIQPLITAMAFGLDAREMArKQYWIHPALPEVVENA 448
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
115-556 |
1.39e-46 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 169.19 E-value: 1.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 115 VVIGGGPAGYVAAIKAAQFGGKVALVEKSE--LGGTCLNRGCIPTKTYLHNAEIIENIGHAANR--GIV--IENPNF--T 186
Cdd:NF040477 7 IIIGFGKAGKTLAATLAKAGWRVAIIEQSAqmYGGTCINIGCIPTKTLVHDAEQHQDFSTAMQRksSVVgfLRDKNYhnL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 187 VDMEKLletkskvvnTLVGGVAGLLRSYGVTVHKGigtitkdknvlvNGSELLETKKIILAGGSKVSKINVPGM-ESPLV 265
Cdd:NF040477 87 ADLDNV---------DVINGRAEFIDNHTLRVFQA------------DGEQELRGEKIFINTGAQSVLPPIPGLtTTPGV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 266 MTSDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTKLQEI 345
Cdd:NF040477 146 YDSTGLLNLTQLPARLGILGGGYIGVEFASMFARFGSKVTIFEAAELFLPREDRDIAQAIATILQDQGVELILNAQVQRV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 346 IEENGQlrIKVEGKDDIIASKALL-SIGRMPDLEGI----GEVEFElDRGCIKVNEYMETSVPGIYAPGDINGTKMLAHA 420
Cdd:NF040477 226 SSHEGE--VQLETAEGVLTVDALLvASGRKPATAGLqlqnAGVAVN-ERGAIVVDKYLRTTADNIWAMGDVTGGLQFTYI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 421 A---FR------MGEVSAENALKGNhavaklnlTPAAIYTLPEVAAVGLTEEQAREK-YDVAIGKFNFAANGRAIASDAA 490
Cdd:NF040477 303 SlddFRivrdslLGEGKRSTDDRQN--------VPYSVFMTPPLSRIGMTEEQARASgADIQVVTLPVAAIPRARVMNDT 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 892236353 491 QGFVKVIADKKYGEILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSEVMYEAFADV 556
Cdd:NF040477 375 RGVLKAVVDNKTQRILGVSLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSESLNDLFALI 440
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
114-547 |
4.95e-45 |
|
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: 165.92 E-value: 4.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGK-VALVE---------KSELGGTCLNRGCIPTKTYLHNAEIIENIGHAANRGIVIENP 183
Cdd:TIGR01423 6 LVVIGAGSGGLEAGWNAATLYKKrVAVVDvqthhgppfYAALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGWEFDRS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 184 NFTVDMEKLLETKSKVVNTLVGGVAGLLR-SYGVTVHKGIGTITKDKNVLVNGS--------ELLETKKIILAGGSKVSK 254
Cdd:TIGR01423 86 SVKANWKALIAAKNKAVLDINKSYEGMFAdTEGLTFFLGWGALEDKNVVLVRESadpksavkERLQAEHILLATGSWPQM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 255 INVPGMEspLVMTSDDILEMNEVPESLVIIGGGVVGIELGQAFMTF---GSKVTVIEMMDRIVPAMDAEVSKNLRLILER 331
Cdd:TIGR01423 166 LGIPGIE--HCISSNEAFYLDEPPRRVLTVGGGFISVEFAGIFNAYkprGGKVTLCYRNNMILRGFDSTLRKELTKQLRA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 332 KGMTILTGTKLQEI-IEENGQLRIKVEGKDDIIASKALLSIGRMP---DLEgIGEVEFEL-DRGCIKVNEYMETSVPGIY 406
Cdd:TIGR01423 244 NGINIMTNENPAKVtLNADGSKHVTFESGKTLDVDVVMMAIGRVPrtqTLQ-LDKVGVELtKKGAIQVDEFSRTNVPNIY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 407 APGDINGTKMLAHAAFRMGEVSAENALKGNHAVAKLNLTPAAIYTLPEVAAVGLTEEQAREKYD-VAIGKFNFAANGRAI 485
Cdd:TIGR01423 323 AIGDVTDRVMLTPVAINEGAAFVDTVFGNKPRKTDHTRVASAVFSIPPIGTCGLVEEDAAKKFEkVAVYESSFTPLMHNI 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 892236353 486 ASDAAQGFV-KVIADKKYGEILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSE 547
Cdd:TIGR01423 403 SGSKYKKFVaKIVTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAE 465
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
115-554 |
1.92e-43 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 160.56 E-value: 1.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 115 VVIGGGPAGYVAAIKAAQFGGKVALVEKSE--LGGTCLNRGCIPTKTYLHNAEIIENIGHAANRGIVI----ENPNF--T 186
Cdd:PRK08010 7 VIIGFGKAGKTLAVTLAKAGWRVALIEQSNamYGGTCINIGCIPTKTLVHDAQQHTDFVRAIQRKNEVvnflRNKNFhnL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 187 VDMEKLletkskvvnTLVGGVAGLLRSYGVTVHKGigtitkDKNVLVNGselletKKIILAGGSKVSKINVPGMES-PLV 265
Cdd:PRK08010 87 ADMPNI---------DVIDGQAEFINNHSLRVHRP------EGNLEIHG------EKIFINTGAQTVVPPIPGITTtPGV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 266 MTSDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTKLQEI 345
Cdd:PRK08010 146 YDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVERI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 346 IEENGQlrIKVEGKDDIIASKALL-SIGRMPDLEGIGEVEFEL---DRGCIKVNEYMETSVPGIYAPGDINGTKMLAHAA 421
Cdd:PRK08010 226 SHHENQ--VQVHSEHAQLAVDALLiASGRQPATASLHPENAGIavnERGAIVVDKYLHTTADNIWAMGDVTGGLQFTYIS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 422 FRMGEVSAENAL-KGNHAVAKLNLTPAAIYTLPEVAAVGLTEEQAREK-YDVAIGKFNFAANGRAIASDAAQGFVKVIAD 499
Cdd:PRK08010 304 LDDYRIVRDELLgEGKRSTDDRKNVPYSVFMTPPLSRVGMTEEQARESgADIQVVTLPVAAIPRARVMNDTRGVLKAIVD 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 892236353 500 KKYGEILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSEVMYEAFA 554
Cdd:PRK08010 384 NKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLNDLFS 438
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
114-548 |
1.23e-41 |
|
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: 156.55 E-value: 1.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVEKSE---------LGGTCLNRGCIPtKTYLHNAEII-ENIGHAANRGIVIENp 183
Cdd:TIGR01438 5 LIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTptplgtrwgIGGTCVNVGCIP-KKLMHQAALLgQALKDSRNYGWKVEE- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 184 NFTVDMEKLLETKSKVVNTLVGGVAGLLRSYGVTVHKGIGTItKDKNVLV----NGSE-LLETKKIILAGGSKVSKINVP 258
Cdd:TIGR01438 83 TVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEF-VDKHRIKatnkKGKEkIYSAERFLIATGERPRYPGIP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 259 GmESPLVMTSDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTViemMDRIVP--AMDAEVSKNLRLILERKGMTI 336
Cdd:TIGR01438 162 G-AKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTV---MVRSILlrGFDQDCANKVGEHMEEHGVKF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 337 LTGTKLQEIIEENGQLRIKVEGKDDIIASK---ALLSIGRMPDLEGIG----EVEFELDRGCIKVNEYMETSVPGIYAPG 409
Cdd:TIGR01438 238 KRQFVPIKVEQIEAKVLVEFTDSTNGIEEEydtVLLAIGRDACTRKLNlenvGVKINKKTGKIPADEEEQTNVPYIYAVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 410 DI-NGTKMLAHAAFRMGEVSAENALKGNHAVAKLNLTPAAIYTLPEVAAVGLTEEQAREKY-----DVAIGKFNFAANGR 483
Cdd:TIGR01438 318 DIlEDKPELTPVAIQAGRLLAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAVEKFgeenvEVFHSYFWPLEWTI 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 892236353 484 AIASDAAQGFVKVIADKKYGE-ILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSEV 548
Cdd:TIGR01438 398 PSRDNHNKCYAKLVCNKKENErVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEV 463
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
117-547 |
7.05e-41 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 155.80 E-value: 7.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 117 IGGGPAGYVAAIKAAQFGGKVALVE------KSE----LGGTCLNRGCIPTKTYLHNAEIIENIGHAANRGIVIE-NPNF 185
Cdd:PLN02546 85 IGAGSGGVRASRFASNFGASAAVCElpfatiSSDtlggVGGTCVLRGCVPKKLLVYASKYSHEFEESRGFGWKYEtEPKH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 186 tvDMEKLLETKSKVVNTLVGGVAGLLRSYGVTVHKGIGTITKDKNVLVNGsELLETKKIILAGGSKVSKINVPGMESplV 265
Cdd:PLN02546 165 --DWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDVDG-KLYTARNILIAVGGRPFIPDIPGIEH--A 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 266 MTSDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTKLQEI 345
Cdd:PLN02546 240 IDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKKVLRGFDEEVRDFVAEQMSLRGIEFHTEESPQAI 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 346 IEEN-GQLRIK-----VEGkddiiASKALLSIGRMPDLEGIG--EVEFELDR-GCIKVNEYMETSVPGIYAPGDINGTKM 416
Cdd:PLN02546 320 IKSAdGSLSLKtnkgtVEG-----FSHVMFATGRKPNTKNLGleEVGVKMDKnGAIEVDEYSRTSVPSIWAVGDVTDRIN 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 417 LAHAAFRMGEVSAENALKGNHAVAKLNLTPAAIYTLPEVAAVGLTEEQAREKY-DVAIGKFNFAANGRAIASDAAQGFVK 495
Cdd:PLN02546 395 LTPVALMEGGALAKTLFGNEPTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYgDVDVFTANFRPLKATLSGLPDRVFMK 474
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 892236353 496 VIADKKYGEILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSE 547
Cdd:PLN02546 475 LIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAE 526
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
445-552 |
4.38e-40 |
|
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: 141.15 E-value: 4.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 445 TPAAIYTLPEVAAVGLTEEQAREKY-DVAIGKFNFAANGRAIASDAAQGFVKVIADKKYGEILGVHIIGPAAAELINEAS 523
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGgEVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQEAA 80
|
90 100
....*....|....*....|....*....
gi 892236353 524 SIIEMEITVEEMLKTIHGHPTYSEVMYEA 552
Cdd:pfam02852 81 LAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
90-547 |
9.65e-39 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 149.77 E-value: 9.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 90 SPEASSVPVASTSNDDDKSDdafdIVVIGGGPAGYVAAIKAAQFGGKVALVEKSELGGTCLNRGCIPTKTYLHNAEIIEN 169
Cdd:PTZ00058 31 NLEASSAPTHLKKKPRMVYD----LIVIGGGSGGMAAARRAARNKAKVALVEKDYLGGTCVNVGCVPKKIMFNAASIHDI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 170 IGHAANRGIvieNPNFTVDMEKLLETKSKVVNTLVGGVAGLLRSYGVTVHKGIGTITKDKNVLV----------NGSE-- 237
Cdd:PTZ00058 107 LENSRHYGF---DTQFSFNLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLIkkvsqvdgeaDESDdd 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 238 ----------------LLETKKIILAGGSKVSKINVPGMEspLVMTSDDILEMNEvPESLVIIGGGVVGIELGQAFMTFG 301
Cdd:PTZ00058 184 evtivsagvsqlddgqVIEGKNILIAVGNKPIFPDVKGKE--FTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 302 SKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTKLQEI--IEENGQLRIKVEGKDDIIASKALLSIGRMPDLEG 379
Cdd:PTZ00058 261 AESYIFARGNRLLRKFDETIINELENDMKKNNINIITHANVEEIekVKEKNLTIYLSDGRKYEHFDYVIYCVGRSPNTED 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 380 IG--EVEFELDRGCIKVNEYMETSVPGIYAPGDINGTKM----------------------------------LAHAAFR 423
Cdd:PTZ00058 341 LNlkALNIKTPKGYIKVDDNQRTSVKHIYAVGDCCMVKKnqeiedlnllklyneepylkkkentsgesyynvqLTPVAIN 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 424 MGEVSAENALKGNHAVAKLNLTPAAIYTLPEVAAVGLTEEQAREKY---DVAIGKFNFAANGRAI----ASDAAQGFVKV 496
Cdd:PTZ00058 421 AGRLLADRLFGPFSRTTNYKLIPSVIFSHPPIGTIGLSEQEAIDIYgkeNVKIYESRFTNLFFSVydmdPAQKEKTYLKL 500
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 892236353 497 IADKKYGEILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSE 547
Cdd:PTZ00058 501 VCVGKEELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIHPTAAE 551
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
115-548 |
4.20e-32 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 129.56 E-value: 4.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 115 VVIGGGPAGYVAAIKAAQFGGKVALVE---------KSELGGTCLNRGCIPtKTYLHNAEIIENIGH--AANRGIVIENp 183
Cdd:PTZ00052 9 VVIGGGSGGMAAAKEAAAHGKKVALFDyvkpstqgtKWGLGGTCVNVGCVP-KKLMHYAANIGSIFHhdSQMYGWKTSS- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 184 nfTVDMEKLLETKSKVVNTLVGGVAGLLRSYGVTVHKGIGTItKDKNVLVNGS----ELLETKKIILAGGSKVS-KINVP 258
Cdd:PTZ00052 87 --SFNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKL-KDEHTVSYGDnsqeETITAKYILIATGGRPSiPEDVP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 259 GMESpLVMTSDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTViEMMDRIVPAMDAEVSKNLRLILERKGMTILT 338
Cdd:PTZ00052 164 GAKE-YSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTV-AVRSIPLRGFDRQCSEKVVEYMKEQGTLFLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 339 GTKLQEIieENGQLRIKVEGKDDIIA--SKALLSIGRMPDLEGIG--EVEFELDRGCIKVNEYMETSVPGIYAPGDI-NG 413
Cdd:PTZ00052 242 GVVPINI--EKMDDKIKVLFSDGTTElfDTVLYATGRKPDIKGLNlnAIGVHVNKSNKIIAPNDCTNIPNIFAVGDVvEG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 414 TKMLAHAAFRMGEVSAENALKGNHAVAKLNLTPAAIYTLPEVAAVGLTEEQAREKY-----DVAIGKFN---FAANGR-- 483
Cdd:PTZ00052 320 RPELTPVAIKAGILLARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYgeddiEEYLQEFNtleIAAVHRek 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 892236353 484 AIASDAAQG--------FVKVIADKKYGE-ILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSEV 548
Cdd:PTZ00052 400 HERARKDEYdfdvssncLAKLVCVKSEDNkVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHPTDAEV 473
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1-100 |
1.29e-26 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 112.19 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 1 MALEVIMPKAGVDMTEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVPVTEVIGYLGEER 80
Cdd:PRK11856 1 MMFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEG 80
|
90 100
....*....|....*....|
gi 892236353 81 ENIPTAGAASPEASSVPVAS 100
Cdd:PRK11856 81 EAEAAAAAEAAPEAPAPEPA 100
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
4-76 |
1.14e-24 |
|
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: 97.48 E-value: 1.14e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 892236353 4 EVIMPKAGVDMTEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVPVTEVIGYL 76
Cdd:cd06849 2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-76 |
1.47e-24 |
|
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: 97.06 E-value: 1.47e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 892236353 1 MALEVIMPKAGVDMTEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVPVTEVIGYL 76
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
114-434 |
4.71e-22 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 96.73 E-value: 4.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVEKSELGGTclnrgciptktyLHNAEIIENIghaanrgivienPNFTVD----- 188
Cdd:COG0492 3 VVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQ------------LATTKEIENY------------PGFPEGisgpe 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 189 -MEKLLEtkskvvntlvggvagLLRSYGVTVHKG-IGTITKDKN---VLVNGSELLETKKIILAGGSKVSKINVPGMESP 263
Cdd:COG0492 59 lAERLRE---------------QAERFGAEILLEeVTSVDKDDGpfrVTTDDGTEYEAKAVIIATGAGPRKLGLPGEEEF 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 264 L---VMTS--DDILEM-NE-----------VPESLviigggvvgielgqaFMT-FGSKVTVIemmdriVPAMDAEVSKNL 325
Cdd:COG0492 124 EgrgVSYCatCDGFFFrGKdvvvvgggdsaLEEAL---------------YLTkFASKVTLI------HRRDELRASKIL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 326 -RLILERKGMTILTGTKLQEIIEENGQLRIKVEGKDD-----IIASKALLSIGRMPDLEGIGEVEFELD-RGCIKVNEYM 398
Cdd:COG0492 183 vERLRANPKIEVLWNTEVTEIEGDGRVEGVTLKNVKTgeekeLEVDGVFVAIGLKPNTELLKGLGLELDeDGYIVVDEDM 262
|
330 340 350
....*....|....*....|....*....|....*..
gi 892236353 399 ETSVPGIYAPGDINGTKM-LAHAAFRMGEVSAENALK 434
Cdd:COG0492 263 ETSVPGVFAAGDVRDYKYrQAATAAGEGAIAALSAAR 299
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
211-459 |
4.82e-22 |
|
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: 97.19 E-value: 4.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 211 LRSYGVTVHKG---IGTITKDKNVLVNGSELLETKKIILAGGSKVSKINVPGMESPLVMTSDDILEMNEVPESLVIIGGG 287
Cdd:COG0446 46 FERKGIDVRTGtevTAIDPEAKTVTLRDGETLSYDKLVLATGARPRPPPIPGLDLPGVFTLRTLDDADALREALKEFKGK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 288 VVG--------IELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTKLQEiIEENGQLRIKVEGK 359
Cdd:COG0446 126 RAVvigggpigLELAEALRKRGLKVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVVA-IDGDDKVAVTLTDG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 360 DDIIASKALLSIGRMPDLEGIGEVEFELD-RGCIKVNEYMETSVPGIYAPGD-------INGTKM---LAHAAFRMGEVS 428
Cdd:COG0446 205 EEIPADLVVVAPGVRPNTELAKDAGLALGeRGWIKVDETLQTSDPDVYAAGDcaevphpVTGKTVyipLASAANKQGRVA 284
|
250 260 270
....*....|....*....|....*....|.
gi 892236353 429 AENALKGNHAVAKLNLTPAAIYTLpEVAAVG 459
Cdd:COG0446 285 AENILGGPAPFPGLGTFISKVFDL-CIASTG 314
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
1-102 |
1.14e-20 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 94.52 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 1 MALEVIMPKAGVDMTEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVPVTEVIGYLGEER 80
Cdd:PRK05704 1 MMVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGA 80
|
90 100
....*....|....*....|..
gi 892236353 81 ENIPTAGAASPEASSVPVASTS 102
Cdd:PRK05704 81 AAGAAAAAAAAAAAAAAAPAQA 102
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
114-433 |
8.29e-19 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 88.66 E-value: 8.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 114 IVVIGGGPAGY--VAAIKAAQFGGKVALVekSELGGTCLNRgcIPTKTYLHnaeiieniGHAANRGIVIENPNFtvdmek 191
Cdd:COG1251 4 IVIIGAGMAGVraAEELRKLDPDGEITVI--GAEPHPPYNR--PPLSKVLA--------GETDEEDLLLRPADF------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 192 lletkskvvntlvggvaglLRSYGVTVHKGIgTITK----DKNVLVNGSELLETKKIILAGGSKVSKINVPGMESPLVM- 266
Cdd:COG1251 66 -------------------YEENGIDLRLGT-RVTAidraARTVTLADGETLPYDKLVLATGSRPRVPPIPGADLPGVFt 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 267 --TSDDILEMNEvpeSLVIIGGG------VVGIELGQAFMTFGSKVTVIEMMDRIVP-AMDAEVSKNLRLILERKGMTIL 337
Cdd:COG1251 126 lrTLDDADALRA---ALAPGKRVvvigggLIGLEAAAALRKRGLEVTVVERAPRLLPrQLDEEAGALLQRLLEALGVEVR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 338 TGTKLQEIIEENGQLRIKVEGKDDIIASKALLSIGRMPDLE-----GIgevefELDRGcIKVNEYMETSVPGIYAPGD-- 410
Cdd:COG1251 203 LGTGVTEIEGDDRVTGVRLADGEELPADLVVVAIGVRPNTElaraaGL-----AVDRG-IVVDDYLRTSDPDIYAAGDca 276
|
330 340 350
....*....|....*....|....*....|
gi 892236353 411 -----INGTKMLAH--AAFRMGEVSAENAL 433
Cdd:COG1251 277 ehpgpVYGRRVLELvaPAYEQARVAAANLA 306
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
4-101 |
1.24e-18 |
|
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: 88.25 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 4 EVIMPKAGVDMTEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVPVTEVIGYLGEERENI 83
Cdd:TIGR01347 2 EIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDAT 81
|
90
....*....|....*...
gi 892236353 84 PTAGAASPEASSVPVAST 101
Cdd:TIGR01347 82 AAPPAKSGEEKEETPAAS 99
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
4-97 |
3.17e-18 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 87.99 E-value: 3.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 4 EVIMPKAGVDMTEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDG-ETVPVTEVIGYLGEEREN 82
Cdd:PLN02744 114 EIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGaKEIKVGEVIAITVEEEED 193
|
90 100
....*....|....*....|....
gi 892236353 83 I---------PTAGAASPEASSVP 97
Cdd:PLN02744 194 IgkfkdykpsSSAAPAAPKAKPSP 217
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
1-79 |
1.80e-16 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 81.14 E-value: 1.80e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 892236353 1 MALEVIMPKAGVDMTEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVPVTEVIGYLGEE 79
Cdd:PRK14875 1 SITPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADA 79
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
1-102 |
6.07e-16 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 80.35 E-value: 6.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 1 MALEVIMPKAGVDMTEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDG-ETVPVTEVIGYLGEE 79
Cdd:PRK11892 1 MAIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTPIAVLLEE 80
|
90 100
....*....|....*....|...
gi 892236353 80 RENIPTAGAASPEASSVPVASTS 102
Cdd:PRK11892 81 GESASDAGAAPAAAAEAAAAAPA 103
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
288-535 |
6.17e-16 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 80.08 E-value: 6.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 288 VVGIELGQAFMTFGSKVTVIEMMDRIVP-AMDAEVSKNLRLILERKGMTILTGTKLQEIIEENgqlriKVEG----KDDI 362
Cdd:PRK09564 159 FIGLEAVEAAKHLGKNVRIIQLEDRILPdSFDKEITDVMEEELRENGVELHLNEFVKSLIGED-----KVEGvvtdKGEY 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 363 IASKALLSIGRMPDLEGIGEVEFE-LDRGCIKVNEYMETSVPGIYAPGD-------INGTKM---LAHAAFRMGEVSAEN 431
Cdd:PRK09564 234 EADVVIVATGVKPNTEFLEDTGLKtLKNGAIIVDEYGETSIENIYAAGDcatiyniVSNKNVyvpLATTANKLGRMVGEN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 432 aLKGNHAVAKLNLTPAAIYTLP-EVAAVGLTEEQARE---KYDVAIGK----FNFAANGRAIasdaaqgFVKVIADKKYG 503
Cdd:PRK09564 314 -LAGRHVSFKGTLGSACIKVLDlEAARTGLTEEEAKKlgiDYKTVFIKdknhTNYYPGQEDL-------YVKLIYEADTK 385
|
250 260 270
....*....|....*....|....*....|...
gi 892236353 504 EILGVHIIGPAAAEL-INEASSIIEMEITVEEM 535
Cdd:PRK09564 386 VILGGQIIGKKGAVLrIDALAVAIYAKLTTQEL 418
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
4-76 |
1.65e-14 |
|
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: 68.40 E-value: 1.65e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 892236353 4 EVIMPKAGVDMTEGqIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVPVTEVIGYL 76
Cdd:pfam00364 2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
303-435 |
3.64e-14 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 74.40 E-value: 3.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 303 KVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTKLQEiIEENGqlrIKVEGkDDIIASKALLSIG--RMPDLegI 380
Cdd:COG1252 187 RITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTE-VDADG---VTLED-GEEIPADTVIWAAgvKAPPL--L 259
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 892236353 381 GEVEFELDR-GCIKVNEYMET-SVPGIYAPGDI--------NGTKMLAHAAFRMGEVSAEN---ALKG 435
Cdd:COG1252 260 ADLGLPTDRrGRVLVDPTLQVpGHPNVFAIGDCaavpdpdgKPVPKTAQAAVQQAKVLAKNiaaLLRG 327
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
8-99 |
4.46e-12 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 68.17 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 8 PKAGVDMTEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVPVtevigylGEERENIPTAG 87
Cdd:PTZ00144 50 PTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEV-------GAPLSEIDTGG 122
|
90
....*....|..
gi 892236353 88 AASPEASSVPVA 99
Cdd:PTZ00144 123 APPAAAPAAAAA 134
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1-100 |
1.16e-11 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 67.33 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 1 MALEVIMPKAGVDmtEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVPVTEVIGYLGEER 80
Cdd:PRK11854 1 MAIEIKVPDIGAD--EVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESAD 78
|
90 100
....*....|....*....|
gi 892236353 81 ENIPTAGAASPEASSVPVAS 100
Cdd:PRK11854 79 GAADAAPAQAEEKKEAAPAA 98
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1-102 |
5.19e-11 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 65.23 E-value: 5.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 1 MALEVIMPKAGvDMTEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVPVTEVIGYLGEER 80
Cdd:PRK11855 1 MAIEFKVPDIG-EVVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIEAAG 79
|
90 100
....*....|....*....|..
gi 892236353 81 EnipTAGAASPEASSVPVASTS 102
Cdd:PRK11855 80 A---AAAAAAPAAAAAPAAAAA 98
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
215-435 |
7.22e-11 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 65.23 E-value: 7.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 215 GVTVHKGIGTITKD---KNVLVNGSELLETKKIILAGGSKVSKINVPGMESPLVM---TSDD---ILEMNEVPESLVIIG 285
Cdd:TIGR02374 68 GITLYTGETVIQIDtdqKQVITDAGRTLSYDKLILATGSYPFILPIPGADKKGVYvfrTIEDldaIMAMAQRFKKAAVIG 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 286 GGVVGIELGQAFMTFGSKVTVIEMMDRIVP-AMDAEVSKNLRLILERKGMTILTGTKLQEIIEENGQLRIKVEGKDDIIA 364
Cdd:TIGR02374 148 GGLLGLEAAVGLQNLGMDVSVIHHAPGLMAkQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVGATKADRIRFKDGSSLEA 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 892236353 365 SKALLSIGRMPDLEGIGEVEFELDRGCIkVNEYMETSVPGIYAPGD---INGTKM-LAHAAFRMGEVSAENALKG 435
Cdd:TIGR02374 228 DLIVMAAGIRPNDELAVSAGIKVNRGII-VNDSMQTSDPDIYAVGEcaeHNGRVYgLVAPLYEQAKVLADHICGV 301
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
4-102 |
1.63e-10 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 63.69 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 4 EVIMPKAGvDMTEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVPVTEVIGYLGEERENI 83
Cdd:PRK11855 121 EVKVPDIG-EITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAAP 199
|
90
....*....|....*....
gi 892236353 84 PTAGAASPEASSVPVASTS 102
Cdd:PRK11855 200 AAAAAPAAAAPAAAAAAAP 218
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
288-359 |
2.19e-10 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 56.83 E-value: 2.19e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 892236353 288 VVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTKLQEIIEENGQLRIKVEGK 359
Cdd:pfam00070 9 YIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLTDG 80
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
4-102 |
3.74e-10 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 62.71 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 4 EVIMPKAGVDmtEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVPVTEVIGYLGEERENI 83
Cdd:PRK11854 107 DVHVPDIGSD--EVEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFEVAGEAP 184
|
90
....*....|....*....
gi 892236353 84 PTAGAASPEASSVPVASTS 102
Cdd:PRK11854 185 AAAPAAAEAAAPAAAPAAA 203
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
2-99 |
4.91e-09 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 58.86 E-value: 4.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 2 ALEVIMPKAGVDmtEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVPVTEVIGYLGEerE 81
Cdd:PRK11854 206 VKDVNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEV--E 281
|
90
....*....|....*...
gi 892236353 82 NIPTAGAASPEASSVPVA 99
Cdd:PRK11854 282 GAAPAAAPAKQEAAAPAP 299
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
4-68 |
5.97e-09 |
|
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: 52.83 E-value: 5.97e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 892236353 4 EVIMPKAGVDMTEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVP 68
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVE 65
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
289-418 |
8.66e-09 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 57.62 E-value: 8.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 289 VGIELGQAFMTFGSKVTVIEMMDRIVPA-MDAEVSKNLRLILERKGMTILTGTKLQEIIEENGQLRIKVEGKDDIIASKA 367
Cdd:PRK04965 152 IGTELAMDLCRAGKAVTLVDNAASLLASlMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRATLDSGRSIEVDAV 231
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 892236353 368 LLSIGRMPDLEGIGEVEFELDRGcIKVNEYMETSVPGIYAPGD---INGtKMLA 418
Cdd:PRK04965 232 IAAAGLRPNTALARRAGLAVNRG-IVVDSYLQTSAPDIYALGDcaeING-QVLP 283
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
217-467 |
8.30e-08 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 54.79 E-value: 8.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 217 TVHKGIGTITKDKNVLVNGSELLET-----KKIILAGGSKVskiNVPGMESPLVMT------SDDI---LEMNEVPESLV 282
Cdd:PRK13512 77 TYHEVIAINDERQTVTVLNRKTNEQfeesyDKLILSPGASA---NSLGFESDITFTlrnledTDAIdqfIKANQVDKALV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 283 IIGGGVVGiELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTIltgtKL-QEIIEENGQLRI----KVE 357
Cdd:PRK13512 154 VGAGYISL-EVLENLYERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPY----RLnEEIDAINGNEVTfksgKVE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 358 GKDDIIASkallsIGRMPDLEGIGEVEFELDR-GCIKVNEYMETSVPGIYAPGDI----------NGTKMLAHAAFRMGE 426
Cdd:PRK13512 229 HYDMIIEG-----VGTHPNSKFIESSNIKLDDkGFIPVNDKFETNVPNIYAIGDIitshyrhvdlPASVPLAWGAHRAAS 303
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 892236353 427 VSAENaLKGNHAVAKLNLTPAAI-----YTLpevAAVGLTEEQARE 467
Cdd:PRK13512 304 IVAEQ-IAGNDTIEFKGFLGNNIvkffdYTF---ASVGVKPNELKQ 345
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
116-411 |
1.48e-07 |
|
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: 53.99 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 116 VIGGGPAGYVAAIKAAQFGGKVALVEK-SELGGtcLNRgciptktYlhnaeiienighaanrGIvienPNFTvdMEKlle 194
Cdd:COG0493 126 VVGSGPAGLAAAYQLARAGHEVTVFEAlDKPGG--LLR-------Y----------------GI----PEFR--LPK--- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 195 tksKVVNTLVGgvagLLRSYGVTVHKGIgTITKDKNVlvngSELLET-KKIILAGGS-KVSKINVPGMESPLVMTSDDIL 272
Cdd:COG0493 172 ---DVLDREIE----LIEALGVEFRTNV-EVGKDITL----DELLEEfDAVFLATGAgKPRDLGIPGEDLKGVHSAMDFL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 273 EMNEvpeslviigggvvGIELGQAFMTFG------------------------SKVTVIEMMDRI-VPAMDAEVSKnlrl 327
Cdd:COG0493 240 TAVN-------------LGEAPDTILAVGkrvvvigggntamdcartalrlgaESVTIVYRRTREeMPASKEEVEE---- 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 328 iLERKGMTILTGTKLQEII-EENGQLR--------------------IKVEGKDDII-ASKALLSIGRMPDLEGIGEV-E 384
Cdd:COG0493 303 -ALEEGVEFLFLVAPVEIIgDENGRVTglecvrmelgepdesgrrrpVPIEGSEFTLpADLVILAIGQTPDPSGLEEElG 381
|
330 340
....*....|....*....|....*....
gi 892236353 385 FELD-RGCIKVNE-YMETSVPGIYAPGDI 411
Cdd:COG0493 382 LELDkRGTIVVDEeTYQTSLPGVFAGGDA 410
|
|
| TIGR00275 |
TIGR00275 |
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ... |
115-251 |
2.08e-07 |
|
flavoprotein, HI0933 family; The model when searched with a partial length search brings in proteins with a dinucleotide-binding motif (Rossman fold) over the initial 40 residues of the model, including oxidoreductases and dehydrogenases. Partially characterized members include an FAD-binding protein from Bacillus cereus and flavoprotein HI0933 from Haemophilus influenzae. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 272992 [Multi-domain] Cd Length: 400 Bit Score: 53.37 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 115 VVIGGGPAGYVAAIKAAQFGGKVALVEKSEL---------GGTClNrgciptktyLHNAEIIENIghAANRGiviENPNF 185
Cdd:TIGR00275 1 IIIGGGAAGLMAAITAARAGLSVLLLEKNKKigkkllisgGGRC-N---------LTNSCPTPEF--VAYYP---RNGKF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 186 ------------TVD-MEKL-LETKSK--------------VVNTLvggvAGLLRSYGVTVHKG--IGTITKDKN--VLV 233
Cdd:TIGR00275 66 lrsalsrfsnkdLIDfFESLgLELKVEedgrvfpcsdsaadVLDAL----LNELKELGVEILTNskVKSIEKEDGgfGVE 141
|
170
....*....|....*...
gi 892236353 234 NGSELLETKKIILAGGSK 251
Cdd:TIGR00275 142 TSGGEYEADKVIIATGGL 159
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
211-411 |
3.53e-07 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 53.23 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 211 LRSYGVTVHKGIgTITKDknvlVNGSELLETKKIIL--AGGSKVSKINVPGMESPLVMTSDDILEM-----------NEV 277
Cdd:PRK13984 343 IEALGVKIHLNT-RVGKD----IPLEELREKHDAVFlsTGFTLGRSTRIPGTDHPDVIQALPLLREirdylrgegpkPKI 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 278 PESLVIIGGGVVGIELGQA-----FMTFG-SKVTVI-------EM---MDRIVPAMDAEVSKN-----LRLILERKGMTI 336
Cdd:PRK13984 418 PRSLVVIGGGNVAMDIARSmarlqKMEYGeVNVKVTslertfeEMpadMEEIEEGLEEGVVIYpgwgpMEVVIENDKVKG 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 337 LTGTKLQEIIEENGQLRIKVEGKDDII--ASKALLSIGRMPDLEGIGE---VEFELDRGCIKVNEYMETSVPGIYAPGDI 411
Cdd:PRK13984 498 VKFKKCVEVFDEEGRFNPKFDESDQIIveADMVVEAIGQAPDYSYLPEelkSKLEFVRGRILTNEYGQTSIPWLFAGGDI 577
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
114-158 |
1.05e-06 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 51.01 E-value: 1.05e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVekSELGGTCLNRGCIPTK 158
Cdd:pfam01134 2 VIVIGGGHAGCEAALAAARMGAKVLLI--THNTDTIAELSCNPSI 44
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
114-148 |
1.88e-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: 50.30 E-value: 1.88e-06
10 20 30
....*....|....*....|....*....|....*.
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVEKS-ELGGT 148
Cdd:pfam12831 2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRgFLGGM 37
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
114-251 |
4.87e-06 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 49.12 E-value: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVEKSEL---------GGTC-LNRGCIPTKTYLHNaeIIEN-------------- 169
Cdd:pfam03486 3 VIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKlgrkilisgGGRCnVTNLSEEPDNFLSR--YPGNpkflksalsrftpw 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 170 --IGHAANRGI-VIENPN---FTVDMeklletKSK-VVNTLVggvaGLLRSYGVTVH-----KGIgTITKDKNVLVN-GS 236
Cdd:pfam03486 81 dfIAFFESLGVpLKEEDHgrlFPDSD------KASdIVDALL----NELKELGVKIRlrtrvLSV-EKDDDGRFRVKtGG 149
|
170
....*....|....*
gi 892236353 237 ELLETKKIILAGGSK 251
Cdd:pfam03486 150 EELEADSLVLATGGL 164
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
114-150 |
1.31e-05 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 47.67 E-value: 1.31e-05
10 20 30
....*....|....*....|....*....|....*..
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVEKSELGGTCL 150
Cdd:pfam00890 2 VLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGAT 38
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
4-103 |
1.83e-05 |
|
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: 47.56 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 4 EVIMPKAGvDMTEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVPVTEVIGYL----GEE 79
Cdd:TIGR01348 2 EIKVPDIG-DNEEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLevgaGAQ 80
|
90 100
....*....|....*....|....
gi 892236353 80 RENIPTAGAASPEASSVPVASTSN 103
Cdd:TIGR01348 81 AQAEAKKEAAPAPTAGAPAPAAQA 104
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
114-147 |
2.53e-05 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 46.75 E-value: 2.53e-05
10 20 30
....*....|....*....|....*....|....
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVEKSELGG 147
Cdd:COG1053 6 VVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRG 39
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
114-147 |
2.55e-05 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 47.16 E-value: 2.55e-05
10 20 30
....*....|....*....|....*....|....*
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVEKS-ELGG 147
Cdd:COG1148 143 ALVIGGGIAGMTAALELAEQGYEVYLVEKEpELGG 177
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
115-249 |
7.30e-05 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 45.43 E-value: 7.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 115 VVIGGGPAGYVAAIKAAQFGGKVALVEKSE------L---GGTC--LNRGCIPtktylhnaEIIENIGhaanrgiviENP 183
Cdd:COG2081 1 IVIGAGAAGLMAAITAAERGARVLLLEKNPkvgrkiLisgGGRCnfTNSEPLP--------EFLNYYG---------GNP 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 184 NF------------TVDM-EKL-LETKSK--------------VVNTLVggvaGLLRSYGVTVHKG--IGTITKDKNVLV 233
Cdd:COG2081 64 HFlksalsrftpedLIAFfEGLgIETKEEssgrvfpdsskasdILRALL----AELREAGVEIRLRtrVTGIEKEDGGFG 139
|
170 180
....*....|....*....|
gi 892236353 234 ---NGSELLETKKIILA-GG 249
Cdd:COG2081 140 vetPDGETVRADAVVLAtGG 159
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
301-406 |
1.36e-04 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 44.14 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 301 GSKVTVIemmDR--IVPAMDAEVSKNLR-LILER-------KGMTILTGTKLQEIIEENGQLRIKVE-GKDDIIASKALL 369
Cdd:pfam13738 178 GARVTVL---YRgsEWEDRDSDPSYSLSpDTLNRleelvknGKIKAHFNAEVKEITEVDVSYKVHTEdGRKVTSNDDPIL 254
|
90 100 110
....*....|....*....|....*....|....*....
gi 892236353 370 SIGRMPDLEGIGEVEFELDR-GCIKVN-EYMETSVPGIY 406
Cdd:pfam13738 255 ATGYHPDLSFLKKGLFELDEdGRPVLTeETESTNVPGLF 293
|
|
| GlpB |
COG3075 |
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism]; |
114-140 |
1.51e-04 |
|
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 442309 Cd Length: 415 Bit Score: 44.40 E-value: 1.51e-04
10 20
....*....|....*....|....*..
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALV 140
Cdd:COG3075 5 VVVIGGGLAGLTAAIRAAEAGLRVAIV 31
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
3-72 |
2.40e-04 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 43.98 E-value: 2.40e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 892236353 3 LEVIMPKAGVDMTEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETV-PVTEV 72
Cdd:PLN02226 92 VEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVePGTKV 162
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
114-148 |
2.77e-04 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 43.57 E-value: 2.77e-04
10 20 30
....*....|....*....|....*....|....*.
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVEKSE-LGGT 148
Cdd:PRK12843 19 VIVIGAGAAGMSAALFAAIAGLKVLLVERTEyVGGT 54
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
350-430 |
2.87e-04 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 43.63 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 350 GQLRIKVEGKDDII-ASKALLSIG---RMPDLEGIGEVEFELDRGCIKVNEYMETSVPGIYAPGDI-NGTKMLAHAAfRM 424
Cdd:PRK11749 361 GRRRVPIEGSEFTLpADLVIKAIGqtpNPLILSTTPGLELNRWGTIIADDETGRTSLPGVFAGGDIvTGAATVVWAV-GD 439
|
....*.
gi 892236353 425 GEVSAE 430
Cdd:PRK11749 440 GKDAAE 445
|
|
| PRK08275 |
PRK08275 |
putative oxidoreductase; Provisional |
394-466 |
3.40e-04 |
|
putative oxidoreductase; Provisional
Pssm-ID: 181346 [Multi-domain] Cd Length: 554 Bit Score: 43.50 E-value: 3.40e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 892236353 394 VNEYMETSVPGIYAPGDINGTK---MLahAAFRMGEVSAEnalkgnHAVAKLNLTPAAIYTLPEVAAvglteEQAR 466
Cdd:PRK08275 361 VNEKAETTVPGLYAAGDMASVPhnyML--GAFTYGWFAGE------NAAEYVAGRDLPEVDAAQVEA-----ERAR 423
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
114-169 |
3.69e-04 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 43.30 E-value: 3.69e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVEKSElGGTCLNRGCIPTKTYLHNAEIIEN 169
Cdd:PRK05329 5 VLVIGGGLAGLTAALAAAEAGKRVALVAKGQ-GALHFSSGSIDLLGYLPDGQPVSD 59
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
17-67 |
3.99e-04 |
|
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: 38.94 E-value: 3.99e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 892236353 17 GQIVQWNKKVGEFVKEGEIL--LEIMtdKVSMELEAEEDGYLIAILKGDGETV 67
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLavLEAM--KMENEVTAPVAGVVKEILVKEGDQV 58
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
114-147 |
1.21e-03 |
|
geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 273936 [Multi-domain] Cd Length: 295 Bit Score: 41.15 E-value: 1.21e-03
10 20 30
....*....|....*....|....*....|....
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVEKSELGG 147
Cdd:TIGR02032 3 VVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPR 36
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
114-259 |
1.49e-03 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 41.30 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVEkselggtclnrgciptktylhnaeiiENIGhaanrGIVIEnpnfTVDMEKLL 193
Cdd:PRK15317 214 VLVVGGGPAGAAAAIYAARKGIRTGIVA--------------------------ERFG-----GQVLD----TMGIENFI 258
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 892236353 194 ETKSKVVNTLVGGVAGLLRSYGVTV---------HKGIGTITkdknVLVNGSELLETKKIILAGGSKVSKINVPG 259
Cdd:PRK15317 259 SVPETEGPKLAAALEEHVKEYDVDImnlqrasklEPAAGLIE----VELANGAVLKAKTVILATGARWRNMNVPG 329
|
|
| PRK13800 |
PRK13800 |
fumarate reductase/succinate dehydrogenase flavoprotein subunit; |
114-179 |
1.84e-03 |
|
fumarate reductase/succinate dehydrogenase flavoprotein subunit;
Pssm-ID: 237512 [Multi-domain] Cd Length: 897 Bit Score: 41.37 E-value: 1.84e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVEKSE--------LGGTCLNRGCIPTKT----YLhnAEIIEnighaANRGIV 179
Cdd:PRK13800 16 VLVIGGGTAGTMAALTAAEHGANVLLLEKAHvrhsgalaMGMDGVNNAVIPGKAepedYV--AEITR-----ANDGIV 86
|
|
| Trp_halogenase |
pfam04820 |
Tryptophan halogenase; Tryptophan halogenase catalyzes the chlorination of tryptophan to form ... |
114-163 |
1.91e-03 |
|
Tryptophan halogenase; Tryptophan halogenase catalyzes the chlorination of tryptophan to form 7-chlorotryptophan. This is the first step in the biosynthesis of pyrrolnitrin, an antibiotic with broad-spectrum anti-fungal activity. Tryptophan halogenase is NADH-dependent.
Pssm-ID: 398475 [Multi-domain] Cd Length: 457 Bit Score: 40.78 E-value: 1.91e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 892236353 114 IVVIGGGPAGYVAAI---KAAQFGGKVALVEKSELGGTCLNRGCIPTKTYLHN 163
Cdd:pfam04820 2 IVIVGGGTAGWMAAAalaRALKGGLDVTLVESEEIGTVGVGEATIPSIRTFNR 54
|
|
| sdhA |
PRK07803 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
114-146 |
2.12e-03 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 236101 [Multi-domain] Cd Length: 626 Bit Score: 40.79 E-value: 2.12e-03
10 20 30
....*....|....*....|....*....|...
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVEKSELG 146
Cdd:PRK07803 11 VVVIGAGGAGLRAAIEARERGLRVAVVCKSLFG 43
|
|
| PRK07494 |
PRK07494 |
UbiH/UbiF family hydroxylase; |
114-140 |
2.20e-03 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181001 [Multi-domain] Cd Length: 388 Bit Score: 40.66 E-value: 2.20e-03
10 20
....*....|....*....|....*..
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALV 140
Cdd:PRK07494 10 IAVIGGGPAGLAAAIALARAGASVALV 36
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
114-147 |
2.62e-03 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 40.60 E-value: 2.62e-03
10 20 30
....*....|....*....|....*....|....*
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVEK-SELGG 147
Cdd:COG1233 6 VVVIGAGIGGLAAAALLARAGYRVTVLEKnDTPGG 40
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
114-148 |
2.73e-03 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 40.47 E-value: 2.73e-03
10 20 30
....*....|....*....|....*....|....*.
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVEKS-ELGGT 148
Cdd:PRK06134 15 VLVIGSGAAGLSAAVTAAWHGLKVIVVEKDpVFGGT 50
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
4-99 |
3.17e-03 |
|
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: 40.24 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 4 EVIMPKAGvDMTEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVPVTEVIGYLGEERENI 83
Cdd:TIGR01348 118 EVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGSTP 196
|
90
....*....|....*...
gi 892236353 84 PTAG--AASPEASSVPVA 99
Cdd:TIGR01348 197 ATAPapASAQPAAQSPAA 214
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
114-147 |
3.41e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 39.87 E-value: 3.41e-03
10 20 30
....*....|....*....|....*....|....*
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVEKSE-LGG 147
Cdd:PRK07233 2 IAIVGGGIAGLAAAYRLAKRGHEVTVFEADDqLGG 36
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
116-149 |
3.47e-03 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 36.36 E-value: 3.47e-03
10 20 30
....*....|....*....|....*....|....*
gi 892236353 116 VIGGGPAGYVAAIKAAQFGGKVALVEK-SELGGTC 149
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKrDRLGGNA 35
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
114-149 |
3.58e-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: 39.82 E-value: 3.58e-03
10 20 30
....*....|....*....|....*....|....*..
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVEKSE-LGGTC 149
Cdd:COG1232 4 VAVIGGGIAGLTAAYRLAKAGHEVTVLEASDrVGGLI 40
|
|
| PTZ00306 |
PTZ00306 |
NADH-dependent fumarate reductase; Provisional |
114-147 |
4.95e-03 |
|
NADH-dependent fumarate reductase; Provisional
Pssm-ID: 140327 [Multi-domain] Cd Length: 1167 Bit Score: 39.76 E-value: 4.95e-03
10 20 30
....*....|....*....|....*....|....*
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVEK-SELGG 147
Cdd:PTZ00306 412 VIVVGGGLAGCSAAIEAASCGAQVILLEKeAKLGG 446
|
|
| PRK08275 |
PRK08275 |
putative oxidoreductase; Provisional |
114-186 |
6.17e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 181346 [Multi-domain] Cd Length: 554 Bit Score: 39.27 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 114 IVVIGGGPAGYVAAIKAAQF--GGKVALVEKSEL---GGTC-----LNRGCIPtktylhnaeiieniGHA---------- 173
Cdd:PRK08275 12 ILVIGGGTAGPMAAIKAKERnpALRVLLLEKANVkrsGAISmgmdgLNNAVIP--------------GHAtpeqytkeit 77
|
90
....*....|....
gi 892236353 174 -ANRGIVIENPNFT 186
Cdd:PRK08275 78 iANDGIVDQKAVYA 91
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
114-466 |
8.48e-03 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 39.09 E-value: 8.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVEK-SELGGTCLnrgciptktYlhnaeiienighaanrGIvienPNFTVDMEKL 192
Cdd:PRK12771 140 VAVIGGGPAGLSAAYHLRRMGHAVTIFEAgPKLGGMMR---------Y----------------GI----PAYRLPREVL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 193 LETKSKVVNTlvggvagllrsyGVTVHKG--IGT-ITKDKnvlvngselLETK--KIILAGGSKVSK-INVPGMESPLVM 266
Cdd:PRK12771 191 DAEIQRILDL------------GVEVRLGvrVGEdITLEQ---------LEGEfdAVFVAIGAQLGKrLPIPGEDAAGVL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 267 TSDDILEmnevpeslviigggvvGIELGQAFMTfGSKVTVI----EMMD-------------RIV--------PAMDAEV 321
Cdd:PRK12771 250 DAVDFLR----------------AVGEGEPPFL-GKRVVVIgggnTAMDaartarrlgaeevTIVyrrtredmPAHDEEI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 322 SKNLRlilerKGMTILTGTKLQEIIEENG--------QLRIKVEGKD-----------DIIASKALLSIGRMPDLEGIGE 382
Cdd:PRK12771 313 EEALR-----EGVEINWLRTPVEIEGDENgatglrviTVEKMELDEDgrpspvtgeeeTLEADLVVLAIGQDIDSAGLES 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236353 383 V-EFELDRGCIKVNE-YMETSVPGIYAPGDI-----NGTKMLAHA--------AFRMGEVSAENALKGNHAVAKLNL--- 444
Cdd:PRK12771 388 VpGVEVGRGVVQVDPnFMMTGRPGVFAGGDMvpgprTVTTAIGHGkkaarnidAFLGGEPYEHRPKREIVKFDKLNLwyf 467
|
410 420 430
....*....|....*....|....*....|...
gi 892236353 445 --TPAAIYTLPEVAAV---------GLTEEQAR 466
Cdd:PRK12771 468 tdAPRAQRPELDADERvgdfdevlgGLTEEEAR 500
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
114-147 |
8.50e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 39.04 E-value: 8.50e-03
10 20 30
....*....|....*....|....*....|....*
gi 892236353 114 IVVIGGGPAGYVAAIKAAQFGGKVALVEKSE-LGG 147
Cdd:PRK12839 11 VVVVGSGAGGLSAAVAAAYGGAKVLVVEKAStCGG 45
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
354-411 |
9.64e-03 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 38.95 E-value: 9.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 892236353 354 IKVEGKDDII-ASKALLSIGRMPD-LEGIGEVEFELDR-GCIKVNEYMETSVPGIYAPGDI 411
Cdd:PRK12778 664 VAIPGSTFTVdVDLVIVSVGVSPNpLVPSSIPGLELNRkGTIVVDEEMQSSIPGIYAGGDI 724
|
|
| |
