|
Name |
Accession |
Description |
Interval |
E-value |
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
111-562 |
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: 589.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 111 AFDIVVIGGGPAGYVAAIKAAQLGGKVALVEKSELGGTCLNRGCIPTKTYLHNAEIIENIGHAANRGIVIENpnFTVDME 190
Cdd:TIGR01350 1 AYDVIVIGGGPGGYVAAIRAAQLGLKVALVEKEYLGGTCLNVGCIPTKALLHSAEVYDEIKHAKDLGIEVEN--VSVDWE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 191 KLLETKSKVVNTLVVGVAGLLRSYGVTVHKGIGTITKDKNVLVNGS---ELLETKKIILAGGSKVSKINVP-GMESPLVM 266
Cdd:TIGR01350 79 KMQKRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGEngeETLEAKNIIIATGSRPRSLPGPfDFDGKVVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 267 TSDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTKLQEII 346
Cdd:TIGR01350 159 TSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTAVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 347 EENGQLRIKVEGKDN--IIASKALLSIGRMPDLEGIG--EVEFELD-RGCIKVNEYMETSVPGIYAPGDINGTKMLAHAA 421
Cdd:TIGR01350 239 KNDDQVTYENKGGETetLTGEKVLVAVGRKPNTEGLGleKLGVELDeRGRIVVDEYMRTNVPGIYAIGDVIGGPMLAHVA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 422 FRMGEVSAENALKGNHAVAKLNLTPAAIYTLPEVAAVGLTEEQAREK-YDVAIGKFNFAANGRAIASDAAQGFVKVIADK 500
Cdd:TIGR01350 319 SHEGIVAAENIAGKEPAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAgYDVKIGKFPFAANGKALALGETDGFVKIIADK 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447085691 501 KYGEILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSEVMYEAFADVLGMAIH 562
Cdd:TIGR01350 399 KTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEAIKEAALAALGKPIH 460
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
112-558 |
7.23e-178 |
|
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: 509.63 E-value: 7.23e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 112 FDIVVIGGGPAGYVAAIKAAQLGGKVALVEKSELGGTCLNRGCIPTKTYLHNAEIIENIGHAANRGIVIENPnfTVDMEK 191
Cdd:COG1249 4 YDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISAGAP--SVDWAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 192 LLETKSKVVNTLVVGVAGLLRSYGVTVHKGIGTITKDKNVLVNGSELLETKKIILAGGSKVSKINVPGMESPLVMTSDDI 271
Cdd:COG1249 82 LMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVTGGETLTADHIVIATGSRPRVPPIPGLDEVRVLTSDEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 272 LEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTKLQEIIEENGQ 351
Cdd:COG1249 162 LELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 352 LRIKVEGKDN---IIASKALLSIGRMPDLEGIG--EVEFELD-RGCIKVNEYMETSVPGIYAPGDINGTKMLAHAAFRMG 425
Cdd:COG1249 242 VTVTLEDGGGeeaVEADKVLVATGRRPNTDGLGleAAGVELDeRGGIKVDEYLRTSVPGIYAIGDVTGGPQLAHVASAEG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 426 EVSAENALKGNHAVAKLNLTPAAIYTLPEVAAVGLTEEQAREK-YDVAIGKFNFAANGRAIASDAAQGFVKVIADKKYGE 504
Cdd:COG1249 322 RVAAENILGKKPRPVDYRAIPSVVFTDPEIASVGLTEEEAREAgIDVKVGKFPFAANGRALALGETEGFVKLIADAETGR 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 447085691 505 ILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSEVMYEAFADVLG 558
Cdd:COG1249 402 ILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAALALLG 455
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
108-562 |
1.71e-157 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 458.07 E-value: 1.71e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 108 SDDAFDIVVIGGGPAGYVAAIKAAQLGGKVALVEKSELGGTCLNRGCIPTKTYLHNAEIIENIGHAANRGIVIENPNFtv 187
Cdd:PRK06416 1 FAFEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIKAENVGI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 188 DMEKLLETKSKVVNTLVVGVAGLLRSYGVTVHKGIGTITKDKNVLVN---GSELLETKKIILAGGSKVskINVPGME--S 262
Cdd:PRK06416 79 DFKKVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMtedGEQTYTAKNIILATGSRP--RELPGIEidG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 263 PLVMTSDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTKL 342
Cdd:PRK06416 157 RVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPGEDKEISKLAERALKKRGIKIKTGAKA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 343 QEIIEENGQLRIKVEGK---DNIIASKALLSIGRMPDLEGIG--EVEFELDRGCIKVNEYMETSVPGIYAPGDINGTKML 417
Cdd:PRK06416 237 KKVEQTDDGVTVTLEDGgkeETLEADYVLVAVGRRPNTENLGleELGVKTDRGFIEVDEQLRTNVPNIYAIGDIVGGPML 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 418 AHAAFRMGEVSAENALKGNHAVAKLNLtPAAIYTLPEVAAVGLTEEQAREK-YDVAIGKFNFAANGRAIASDAAQGFVKV 496
Cdd:PRK06416 317 AHKASAEGIIAAEAIAGNPHPIDYRGI-PAVTYTHPEVASVGLTEAKAKEEgFDVKVVKFPFAGNGKALALGETDGFVKL 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447085691 497 IADKKYGEILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSEVMYEAFADVLGMAIH 562
Cdd:PRK06416 396 IFDKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEALGEAALAAAGKPLH 461
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
112-562 |
2.52e-139 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 411.49 E-value: 2.52e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 112 FDIVVIGGGPAGYVAAIKAAQLGGKVALVEKSELGGTCLNRGCIPTKTYLHNAEIIENIGHAANRGIVIENPnfTVDMEK 191
Cdd:PRK06292 4 YDVIVIGAGPAGYVAARRAAKLGKKVALIEKGPLGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHADGP--KIDFKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 192 LLETKSKVVNTLVVGV-AGLLRSYGVTVHKGIGTITKDKNVLVNGsELLETKKIILAGGSKVskINVPGMESPL---VMT 267
Cdd:PRK06292 82 VMARVRRERDRFVGGVvEGLEKKPKIDKIKGTARFVDPNTVEVNG-ERIEAKNIVIATGSRV--PPIPGVWLILgdrLLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 268 SDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKgMTILTGTKLQEIiE 347
Cdd:PRK06292 159 SDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILSKE-FKIKLGAKVTSV-E 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 348 ENGQLRIKVEGKDN----IIASKALLSIGRMPDLEGIG--EVEFELD-RGCIKVNEYMETSVPGIYAPGDINGTKMLAHA 420
Cdd:PRK06292 237 KSGDEKVEELEKGGktetIEADYVLVATGRRPNTDGLGleNTGIELDeRGRPVVDEHTQTSVPGIYAAGDVNGKPPLLHE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 421 AFRMGEVSAENALKGNHAVAKLNLTPAAIYTLPEVAAVGLTEEQAREK-YDVAIGKFNFAANGRAIASDAAQGFVKVIAD 499
Cdd:PRK06292 317 AADEGRIAAENAAGDVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAgIDYVVGEVPFEAQGRARVMGKNDGFVKVYAD 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447085691 500 KKYGEILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSEVMYEAFADVLGMAIH 562
Cdd:PRK06292 397 KKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRTALRDLFSKLIH 459
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
110-562 |
8.40e-124 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 372.34 E-value: 8.40e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 110 DAFDIVVIGGGPAGYVAAIKAAQLGGKVALVE-------KSELGGTCLNRGCIPTKTYLHNAEIIENIGHA-ANRGIVIE 181
Cdd:PRK06327 3 KQFDVVVIGAGPGGYVAAIRAAQLGLKVACIEawknpkgKPALGGTCLNVGCIPSKALLASSEEFENAGHHfADHGIHVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 182 NpnFTVDMEKLLETKSKVVNTLVVGVAGLLRSYGVTVHKGIGTITKDKN------VLVNGSELLETKKIILAGGSKvsKI 255
Cdd:PRK06327 83 G--VKIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVGKTDagyeikVTGEDETVITAKHVIIATGSE--PR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 256 NVPGM--ESPLVMTSDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKG 333
Cdd:PRK06327 159 HLPGVpfDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAAADEQVAKEAAKAFTKQG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 334 MTILTGTKLQEIIEENGQLRIKVEGKD----NIIASKALLSIGRMPDLEGIG--EVEFELD-RGCIKVNEYMETSVPGIY 406
Cdd:PRK06327 239 LDIHLGVKIGEIKTGGKGVSVAYTDADgeaqTLEVDKLIVSIGRVPNTDGLGleAVGLKLDeRGFIPVDDHCRTNVPNVY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 407 APGDINGTKMLAHAAFRMGEVSAENAlKGNHAVAKLNLTPAAIYTLPEVAAVGLTEEQAR-EKYDVAIGKFNFAANGRAI 485
Cdd:PRK06327 319 AIGDVVRGPMLAHKAEEEGVAVAERI-AGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLKaEGVEYKAGKFPFMANGRAL 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447085691 486 ASDAAQGFVKVIADKKYGEILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSEVMYEAFADVLGMAIH 562
Cdd:PRK06327 398 AMGEPDGFVKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEVWHEAALAVDKRPLH 474
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
112-555 |
3.92e-110 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 336.79 E-value: 3.92e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 112 FDIVVIGGGPAGYVAAIKAAQLGGKVALVEKSELGGTCLNRGCIPTKTYLHNAEIIENIGHAANRGIVIENPnFTVDMEK 191
Cdd:PRK06370 6 YDAIVIGAGQAGPPLAARAAGLGMKVALIERGLLGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGGP-VSVDFKA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 192 LLETKSKVVNTLVVGVAGLLRSY-GVTVHKGIGTITKDKNVLVNGsELLETKKIILAGGSKVSKINVPGMESPLVMTSDD 270
Cdd:PRK06370 85 VMARKRRIRARSRHGSEQWLRGLeGVDVFRGHARFESPNTVRVGG-ETLRAKRIFINTGARAAIPPIPGLDEVGYLTNET 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 271 ILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTKLQEIIEENG 350
Cdd:PRK06370 164 IFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILEREGIDVRLNAECIRVERDGD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 351 QLRIKVEGKDN---IIASKALLSIGRMPDLEGIG----EVEFElDRGCIKVNEYMETSVPGIYAPGDINGTKMLAHAAFR 423
Cdd:PRK06370 244 GIAVGLDCNGGapeITGSHILVAVGRVPNTDDLGleaaGVETD-ARGYIKVDDQLRTTNPGIYAAGDCNGRGAFTHTAYN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 424 MGEVSAENALKGNHAVAKLNLTPAAIYTLPEVAAVGLTEEQAREK-YDVAIGKFNFAANGRAIASDAAQGFVKVIADKKY 502
Cdd:PRK06370 323 DARIVAANLLDGGRRKVSDRIVPYATYTDPPLARVGMTEAEARKSgRRVLVGTRPMTRVGRAVEKGETQGFMKVVVDADT 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 447085691 503 GEILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSEVMYEAFAD 555
Cdd:PRK06370 403 DRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIPTLAQA 455
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
112-547 |
1.48e-92 |
|
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: 291.63 E-value: 1.48e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 112 FDIVVIGGGPAGYVAAIKAAQLGGKVALVEKSELGGTCLNRGCIPTKTYLHNAEIIENIGHAANRGIVIEnpnFTVDMEK 191
Cdd:TIGR02053 1 YDLVIIGSGAAAFAAAIKAAELGASVAMVERGPLGGTCVNVGCVPSKMLLRAAEVAHYARKPPFGGLAAT---VAVDFGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 192 LLETKSKVVNTL-VVGVAGLLRSYGVTVHKGIGTITKDKNVLVN-GSELLETKKIILAGGSKVSKINVPGMESPLVMTSD 269
Cdd:TIGR02053 78 LLEGKREVVEELrHEKYEDVLSSYGVDYLRGRARFKDPKTVKVDlGREVRGAKRFLIATGARPAIPPIPGLKEAGYLTSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 270 DILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTKLQEIIEEN 349
Cdd:TIGR02053 158 EALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSDRLLPREEPEISAAVEEALAEEGIEVVTSAQVKAVSVRG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 350 GQLRIKVEGKDN---IIASKALLSIGRMPDLEGIG--EVEFELD-RGCIKVNEYMETSVPGIYAPGDINGTKMLAHAAFR 423
Cdd:TIGR02053 238 GGKIITVEKPGGqgeVEADELLVATGRRPNTDGLGleKAGVKLDeRGGILVDETLRTSNPGIYAAGDVTGGLQLEYVAAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 424 MGEVSAENALKGNHAVAKLNLTPAAIYTLPEVAAVGLTEEQAREK-YDVAIGKFNFAANGRAIASDAAQGFVKVIADKKY 502
Cdd:TIGR02053 318 EGVVAAENALGGANAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAgIECDCRTLPLTNVPRARINRDTRGFIKLVAEPGT 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 447085691 503 GEILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSE 547
Cdd:TIGR02053 398 GKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAE 442
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
112-547 |
3.38e-71 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 235.44 E-value: 3.38e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 112 FDIVVIGGGPAGYVAAIKAAQLGGKVALVEKSELGGTCLNRGCIPTKTYLHNAEIIENIGH-AANRGIVIENPNFtvDME 190
Cdd:PRK06116 5 YDLIVIGGGSGGIASANRAAMYGAKVALIEAKRLGGTCVNVGCVPKKLMWYGAQIAEAFHDyAPGYGFDVTENKF--DWA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 191 KLLETKSKVVNTLVVGVAGLLRSYGVTVHKGIGTITKDKNVLVNGsELLETKKIILAGGSKVSKINVPGMEspLVMTSDD 270
Cdd:PRK06116 83 KLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNG-ERYTADHILIATGGRPSIPDIPGAE--YGITSDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 271 ILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTKLQEII-EEN 349
Cdd:PRK06116 160 FFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEkNAD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 350 GQLRIKVEGKDNIIASKALLSIGRMPDLEGIG----EVEFElDRGCIKVNEYMETSVPGIYAPGDINGTKMLAHAAFRMG 425
Cdd:PRK06116 240 GSLTLTLEDGETLTVDCLIWAIGREPNTDGLGlenaGVKLN-EKGYIIVDEYQNTNVPGIYAVGDVTGRVELTPVAIAAG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 426 EVSAENALKGNhAVAKLN--LTPAAIYTLPEVAAVGLTEEQAREKY---DVAIGKFNFAANGRAIASDAAQGFVKVIADK 500
Cdd:PRK06116 319 RRLSERLFNNK-PDEKLDysNIPTVVFSHPPIGTVGLTEEEAREQYgedNVKVYRSSFTPMYTALTGHRQPCLMKLVVVG 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 447085691 501 KYGEILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSE 547
Cdd:PRK06116 398 KEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAE 444
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
112-547 |
5.42e-67 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 224.65 E-value: 5.42e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 112 FDIVVIGGGPAGYVAAIKAAQLGGKVALVEK-SELGGTCLNRGCIPTKTYLHNA-EIIEnighAANRGIVIEN---PNFT 186
Cdd:PRK05249 6 YDLVVIGSGPAGEGAAMQAAKLGKRVAVIERyRNVGGGCTHTGTIPSKALREAVlRLIG----FNQNPLYSSYrvkLRIT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 187 vdMEKLLETKSKVVNTLVVGVAGLLRSYGVTVHKGIGTITkDKN-VLV----NGSELLETKKIILAGGSKVSKI-NVPgM 260
Cdd:PRK05249 82 --FADLLARADHVINKQVEVRRGQYERNRVDLIQGRARFV-DPHtVEVecpdGEVETLTADKIVIATGSRPYRPpDVD-F 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 261 ESPLVMTSDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGT 340
Cdd:PRK05249 158 DHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSFLDDEISDALSYHLRDSGVTIRHNE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 341 KLQEIIEENGQLRIKVEGKDNIIASKALLSIGRMP-----DLEGIGeveFELD-RGCIKVNEYMETSVPGIYAPGDINGT 414
Cdd:PRK05249 238 EVEKVEGGDDGVIVHLKSGKKIKADCLLYANGRTGntdglNLENAG---LEADsRGQLKVNENYQTAVPHIYAVGDVIGF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 415 KMLAHAAFRMGEVSAENALkGNHAVAKLNLTPAAIYTLPEVAAVGLTEEQAREK---YDVAIGKFNFAANGrAIASDAAq 491
Cdd:PRK05249 315 PSLASASMDQGRIAAQHAV-GEATAHLIEDIPTGIYTIPEISSVGKTEQELTAAkvpYEVGRARFKELARA-QIAGDNV- 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 447085691 492 GFVKVIADKKYGEILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSE 547
Cdd:PRK05249 392 GMLKILFHRETLEILGVHCFGERATEIIHIGQAIMEQKGTIEYFVNTTFNYPTMAE 447
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
112-425 |
4.06e-61 |
|
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: 204.09 E-value: 4.06e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 112 FDIVVIGGGPAGYVAAIKAAQLGGKVALVEkseLGGTCLNRGCIPTKTYLHNAEIIENIGHAAnrgivienpnftvdmeK 191
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIE---DEGTCPYGGCVLSKALLGAAEAPEIASLWA----------------D 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 192 LLETKSKVVNTLVVGVAGLLRSYGVTVHKGIGTITKDKNVLVNGSELlETKKIILAGGSKVSKINVPGMESPL-----VM 266
Cdd:pfam07992 62 LYKRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELVDGDGETI-TYDRLVIATGARPRLPPIPGVELNVgflvrTL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 267 TSDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTKLQEII 346
Cdd:pfam07992 141 DSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEII 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 347 EENGQLRIKVEGKDNIIASKALLSIGRMPDLEGIGEVEFELD-RGCIKVNEYMETSVPGIYAPGDINGTK-MLAHAAFRM 424
Cdd:pfam07992 221 GDGDGVEVILKDGTEIDADLVVVAIGRRPNTELLEAAGLELDeRGGIVVDEYLRTSVPGIYAAGDCRVGGpELAQNAVAQ 300
|
.
gi 447085691 425 G 425
Cdd:pfam07992 301 G 301
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
112-547 |
5.45e-61 |
|
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: 208.13 E-value: 5.45e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 112 FDIVVIGGGPAGYVAAIKAAQLGGKVALVEKSELGGTCLNRGCIPTKTYLHNAEIIENIGHAANRGIVIENPNFtvDMEK 191
Cdd:TIGR01424 3 YDLFVIGAGSGGVRAARLAAALGAKVAIAEEFRVGGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGWTVGKARF--DWKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 192 LLETKSKVVNTLVVGVAGLLRSYGVTVHKGIGTITKDKNVLVNGSELLET-KKIILAGGSKVSKINVPGMEspLVMTSDD 270
Cdd:TIGR01424 81 LLAAKDQEIARLSGLYRKGLANAGAELLDGRAELVGPNTVEVLASGKTYTaEKILIAVGGRPPKPALPGHE--LGITSNE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 271 ILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTKLQEIIE-EN 349
Cdd:TIGR01424 159 AFHLPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRGKEILRGFDDDMRRGLAAALEERGIRILPEDSITSISKdDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 350 GQLRIKVEGKDNIIASKALLSIGRMPDLEGIG--EVEFEL-DRGCIKVNEYMETSVPGIYAPGDINGTKMLAHAAFRMGE 426
Cdd:TIGR01424 239 GRLKATLSKHEEIVADVVLFATGRSPNTNGLGleAAGVRLnDLGAIAVDEYSRTSTPSIYAVGDVTDRINLTPVAIHEAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 427 VSAENALKGNHAVAKLNLTPAAIYTLPEVAAVGLTEEQAREKY-DVAIGKFNFAANGRAIASDAAQGFVKVIADKKYGEI 505
Cdd:TIGR01424 319 CFAETEFGNNPTSFDHDLIATAVFSQPPIGTVGLTEEEARRKFgDIEVYRAEFRPMKATFSGRQEKTLMKLVVDAKDDKV 398
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 447085691 506 LGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSE 547
Cdd:TIGR01424 399 LGAHMVGPDAAEIIQGLAIALKMGATKDDFDSTVAVHPTSAE 440
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
112-548 |
1.30e-60 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 207.50 E-value: 1.30e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 112 FDIVVIGGGPAGYVAAIKAAQLggKVALVEKSELGGTCLNRGCIPTKTYLHNAEIIENIGHAANRGIVIENPNftVDMEK 191
Cdd:PRK07846 2 YDLIIIGTGSGNSILDERFADK--RIAIVEKGTFGGTCLNVGCIPTKMFVYAADVARTIREAARLGVDAELDG--VRWPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 192 LletKSKVVNTLVVGVAGLLRSYG-----VTVHKGIGTITKDKNVLVNGSELLETKKIILAGGSKVSKINVPGMESPLVM 266
Cdd:PRK07846 78 I---VSRVFGRIDPIAAGGEEYRGrdtpnIDVYRGHARFIGPKTLRTGDGEEITADQVVIAAGSRPVIPPVIADSGVRYH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 267 TSDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKgMTILTGTKLQEII 346
Cdd:PRK07846 155 TSDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLDDDISERFTELASKR-WDVRLGRNVVGVS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 347 EENGQLRIKVEGKDNIIASKALLSIGRMP--DLEGIGEVEFELDR-GCIKVNEYMETSVPGIYAPGDINGTKMLAHAAFR 423
Cdd:PRK07846 234 QDGSGVTLRLDDGSTVEADVLLVATGRVPngDLLDAAAAGVDVDEdGRVVVDEYQRTSAEGVFALGDVSSPYQLKHVANH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 424 MGEVSAENALKGNH-AVAKLNLTPAAIYTLPEVAAVGLTEEQAREK-YDVAIGKFNFA--ANGRAIASDaaQGFVKVIAD 499
Cdd:PRK07846 314 EARVVQHNLLHPDDlIASDHRFVPAAVFTHPQIASVGLTENEARAAgLDITVKVQNYGdvAYGWAMEDT--TGFVKLIAD 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 447085691 500 KKYGEILGVHIIGPAAAELINEASSIIEMEITVEEMLKT---IhgHPTYSEV 548
Cdd:PRK07846 392 RDTGRLLGAHIIGPQASTLIQPLIQAMSFGLDAREMARGqywI--HPALPEV 441
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
111-554 |
9.21e-59 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 201.90 E-value: 9.21e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 111 AFDIVVIGGGPAGYVAAIKAAQLGGKVALVEKSEL--GGTCLNRGCIPTKTYLHNAEiienighaanrgiviENPNFtvd 188
Cdd:PRK07251 3 TYDLIVIGFGKAGKTLAAKLASAGKKVALVEESKAmyGGTCINIGCIPTKTLLVAAE---------------KNLSF--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 189 mEKLLETKSKVVNTLVVGVAGLLRSYGVTVHKGIGTITKDKNVLVNG---SELLETKKIILAGGSKVSKINVPGM-ESPL 264
Cdd:PRK07251 65 -EQVMATKNTVTSRLRGKNYAMLAGSGVDLYDAEAHFVSNKVIEVQAgdeKIELTAETIVINTGAVSNVLPIPGLaDSKH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 265 VMTSDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTKLQE 344
Cdd:PRK07251 144 VYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYMEEDGITFLLNAHTTE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 345 IIEENGQLRIKVEGKDniIASKALL-SIGRMPDLEGIG--EVEFEL-DRGCIKVNEYMETSVPGIYAPGDINGTKMLAHA 420
Cdd:PRK07251 224 VKNDGDQVLVVTEDET--YRFDALLyATGRKPNTEPLGleNTDIELtERGAIKVDDYCQTSVPGVFAVGDVNGGPQFTYI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 421 A---FRMgevsAENALKGN--HAVAKLNLTPAAIYTLPEVAAVGLTEEQAREK-YDVAIGKFNFAANGRAIASDAAQGFV 494
Cdd:PRK07251 302 SlddFRI----VFGYLTGDgsYTLEDRGNVPTTMFITPPLSQVGLTEKEAKEAgLPYAVKELLVAAMPRAHVNNDLRGAF 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 495 KVIADKKYGEILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSEVMYEAFA 554
Cdd:PRK07251 378 KVVVNTETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAENLNDLFN 437
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
73-535 |
1.42e-53 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 191.13 E-value: 1.42e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 73 IGYLGEERENIPTAGSASPEASPVPVASTSNDDGKSDDAFDIVVIGGGPAGYVAAIKAAQLGGKVALVEKSELGGTCLNR 152
Cdd:PRK13748 60 LGYRATLADAPPTDNRGGLLDKMRGWLGGADKHSGNERPLHVAVIGSGGAAMAAALKAVEQGARVTLIERGTIGGTCVNV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 153 GCIPTKTYLHNAEIIE-NIGHAANRGIVIENPnfTVDMEKLLETKSKVVNTL-VVGVAGLLRSY-GVTVHKGIGTItKDK 229
Cdd:PRK13748 140 GCVPSKIMIRAAHIAHlRRESPFDGGIAATVP--TIDRSRLLAQQQARVDELrHAKYEGILDGNpAITVLHGEARF-KDD 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 230 NVLV----NGSEL-LETKKIILAGGSKVSKINVPGMESPLVMTSDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKV 304
Cdd:PRK13748 217 QTLIvrlnDGGERvVAFDRCLIATGASPAVPPIPGLKETPYWTSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKV 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 305 TVI---EMMDRIVPAMDAEVSKNLRLilerKGMTILTGTKLQEIIEENGQLRIKVeGKDNIIASKALLSIGRMP-----D 376
Cdd:PRK13748 297 TILarsTLFFREDPAIGEAVTAAFRA----EGIEVLEHTQASQVAHVDGEFVLTT-GHGELRADKLLVATGRAPntrslA 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 377 LEGIGeVEFElDRGCIKVNEYMETSVPGIYAPGDINGTKMLAHAAFRMGEVSAENALKGNhavAKLNLT--PAAIYTLPE 454
Cdd:PRK13748 372 LDAAG-VTVN-AQGAIVIDQGMRTSVPHIYAAGDCTDQPQFVYVAAAAGTRAAINMTGGD---AALDLTamPAVVFTDPQ 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 455 VAAVGLTEEQAR----EKYDVAIGKFNFAangRAIASDAAQGFVKVIADKKYGEILGVHIIGPAAAELINEASSIIEMEI 530
Cdd:PRK13748 447 VATVGYSEAEAHhdgiETDSRTLTLDNVP---RALANFDTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAALAIRNRM 523
|
....*
gi 447085691 531 TVEEM 535
Cdd:PRK13748 524 TVQEL 528
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
99-562 |
7.08e-52 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 188.20 E-value: 7.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 99 ASTSNDDGKSDDAFDIVVIGGGPAGYVAAIKAAQLGGKVALV--EKSELGGTCLNRGCIPTKTYLHNA---EIIENIGHA 173
Cdd:PTZ00153 104 FATSQSMNFSDEEYDVGIIGCGVGGHAAAINAMERGLKVIIFtgDDDSIGGTCVNVGCIPSKALLYATgkyRELKNLAKL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 174 ANRGI-----------VIENPN-----FTVDMEKLLETKSKVVNTLVVGVAGLLRSYGVTVHKGIGTITK------DKNV 231
Cdd:PTZ00153 184 YTYGIytnafkngkndPVERNQlvadtVQIDITKLKEYTQSVIDKLRGGIENGLKSKKFCKNSEHVQVIYerghivDKNT 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 232 LVNGSELLE--TKKIILAGGSKVSKINVPGMESPLVMTSDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEM 309
Cdd:PTZ00153 264 IKSEKSGKEfkVKNIIIATGSTPNIPDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEY 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 310 MDRIVPAMDAEVSKNL-RLILERKGMTILTGTKLQEIIEENG------QLRIKVEGKDN-----------IIASKALLSI 371
Cdd:PTZ00153 344 SPQLLPLLDADVAKYFeRVFLKSKPVRVHLNTLIEYVRAGKGnqpviiGHSERQTGESDgpkknmndikeTYVDSCLVAT 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 372 GRMPDLEGIG--EVEFELDRGCIKVNEYMETS------VPGIYAPGDINGTKMLAHAAFRMG----------EVSAENAL 433
Cdd:PTZ00153 424 GRKPNTNNLGldKLKIQMKRGFVSVDEHLRVLredqevYDNIFCIGDANGKQMLAHTASHQAlkvvdwiegkGKENVNIN 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 434 KGNHAVAKLNL--TPAAIYTLPEVAAVGLTEEQAREKY---DVAIGKFNFAANGRAIA---------------------- 486
Cdd:PTZ00153 504 VENWASKPIIYknIPSVCYTTPELAFIGLTEKEAKELYppdNVGVEISFYKANSKVLCennisfpnnsknnsynkgkynt 583
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447085691 487 SDAAQGFVKVIADKKYGEILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSEVMYEAFADVLGMAIH 562
Cdd:PTZ00153 584 VDNTEGMVKIVYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDAAFKAIAGVRTH 659
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
114-552 |
1.03e-49 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 178.52 E-value: 1.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 114 IVVIGGGPAGYVAAIKAAQLGGKVALVEKSELGGTCLNRGCIPTKTYLHNAEIIENIGHAANRGI-VIENPNFTVDMEKl 192
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIERDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIrFIDDGEARVDLPA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 193 letkskvVNTLVVGVA---------GLLRSyGVTVHKGIGTITKDK----NVLVN----GSELLETKKIILAGGS--KVS 253
Cdd:PRK07845 83 -------VNARVKALAaaqsadiraRLERE-GVRVIAGRGRLIDPGlgphRVKVTtadgGEETLDADVVLIATGAspRIL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 254 KINVPGMESplVMTSDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKG 333
Cdd:PRK07845 155 PTAEPDGER--ILTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPGEDADAAEVLEEVFARRG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 334 MTILTGTKLQEIIEENGQLRIKVEGKDNIIASKALLSIGRMPDLEGIG--EVEFELDR-GCIKVNEYMETSVPGIYAPGD 410
Cdd:PRK07845 233 MTVLKRSRAESVERTGDGVVVTLTDGRTVEGSHALMAVGSVPNTAGLGleEAGVELTPsGHITVDRVSRTSVPGIYAAGD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 411 INGTKMLAHAAFRMGEVSAENALkgNHAVAKLNLT--PAAIYTLPEVAAVGLTEEQARE-KYDVAIGKFNFAANGRAIAS 487
Cdd:PRK07845 313 CTGVLPLASVAAMQGRIAMYHAL--GEAVSPLRLKtvASNVFTRPEIATVGVSQAAIDSgEVPARTVMLPLATNPRAKMS 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447085691 488 DAAQGFVKVIADKKYGEILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSEVMYEA 552
Cdd:PRK07845 391 GLRDGFVKLFCRPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYPSLSGSITEA 455
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
112-547 |
2.89e-49 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 178.09 E-value: 2.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 112 FDIVVIGGGPAGYVAAIKAAQLGGKVALVE------KSE----LGGTCLNRGCIPTKTYLHNAEIIENIGHAANRGIVIe 181
Cdd:PLN02507 26 FDLFVIGAGSGGVRAARFSANFGAKVGICElpfhpiSSEsiggVGGTCVIRGCVPKKILVYGATFGGEFEDAKNYGWEI- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 182 NPNFTVDMEKLLETKSKVVNTLVVGVAGLLRSYGVTVHKGIGTITKDKNVLV---NGSELLET-KKIILAGGSKVSKINV 257
Cdd:PLN02507 105 NEKVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVtqlDGTKLRYTaKHILIATGSRAQRPNI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 258 PGMEspLVMTSDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTIL 337
Cdd:PLN02507 185 PGKE--LAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRAVVARNLEGRGINLH 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 338 TGTKLQEIIEENGQLRIKVEGKDNIIASKALLSIGRMPDLEGIG--EVEFELDR-GCIKVNEYMETSVPGIYAPGDINGT 414
Cdd:PLN02507 263 PRTNLTQLTKTEGGIKVITDHGEEFVADVVLFATGRAPNTKRLNleAVGVELDKaGAVKVDEYSRTNIPSIWAIGDVTNR 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 415 KMLAHAAFRMGEVSAENALKGNHAVAKLNLTPAAIYTLPEVAAVGLTEEQARE--KYDVAIGKFNFAANGRAIASDAAQG 492
Cdd:PLN02507 343 INLTPVALMEGTCFAKTVFGGQPTKPDYENVACAVFCIPPLSVVGLSEEEAVEqaKGDILVFTSSFNPMKNTISGRQEKT 422
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 447085691 493 FVKVIADKKYGEILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSE 547
Cdd:PLN02507 423 VMKLIVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAE 477
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
111-547 |
4.77e-48 |
|
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: 174.39 E-value: 4.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 111 AFDIVVIGGGPAGYVAAIKAAQLGGK-VALVE---------KSELGGTCLNRGCIPTKTYLHNAEIIENIGHAANRGIVI 180
Cdd:TIGR01423 3 AFDLVVIGAGSGGLEAGWNAATLYKKrVAVVDvqthhgppfYAALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGWEF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 181 ENPNFTVDMEKLLETKSKVVNTLVVGVAGLLR-SYGVTVHKGIGTITKDKNVLVNGS--------ELLETKKIILAGGSK 251
Cdd:TIGR01423 83 DRSSVKANWKALIAAKNKAVLDINKSYEGMFAdTEGLTFFLGWGALEDKNVVLVRESadpksavkERLQAEHILLATGSW 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 252 VSKINVPGMEspLVMTSDDILEMNEVPESLVIIGGGVVGIELGQAFMTF---GSKVTVIEMMDRIVPAMDAEVSKNLRLI 328
Cdd:TIGR01423 163 PQMLGIPGIE--HCISSNEAFYLDEPPRRVLTVGGGFISVEFAGIFNAYkprGGKVTLCYRNNMILRGFDSTLRKELTKQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 329 LERKGMTILTGTKLQEI-IEENGQLRIKVEGKDNIIASKALLSIGRMP---DLEgIGEVEFEL-DRGCIKVNEYMETSVP 403
Cdd:TIGR01423 241 LRANGINIMTNENPAKVtLNADGSKHVTFESGKTLDVDVVMMAIGRVPrtqTLQ-LDKVGVELtKKGAIQVDEFSRTNVP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 404 GIYAPGDINGTKMLAHAAFRMGEVSAENALKGNHAVAKLNLTPAAIYTLPEVAAVGLTEEQAREKYD-VAIGKFNFAANG 482
Cdd:TIGR01423 320 NIYAIGDVTDRVMLTPVAINEGAAFVDTVFGNKPRKTDHTRVASAVFSIPPIGTCGLVEEDAAKKFEkVAVYESSFTPLM 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447085691 483 RAIASDAAQGFV-KVIADKKYGEILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSE 547
Cdd:TIGR01423 400 HNISGSKYKKFVaKIVTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAE 465
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
112-552 |
7.00e-48 |
|
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: 173.02 E-value: 7.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 112 FDIVVIGGGPAGYVAAIKAAqlGGKVALVEKSELGGTCLNRGCIPTKTYLHNAEIIENIGHAANRGIvienpNFTVDMEK 191
Cdd:TIGR03452 3 YDLIIIGTGSGNSIPDPRFA--DKRIAIVEKGTFGGTCLNVGCIPTKMFVYAAEVAQSIGESARLGI-----DAEIDSVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 192 LLETKSKVVNTLVVGVAGLLRSY-------GVTVHKGIGTITKDKNVLVNGSELLETKKIILAGGSKvsKINVPGMESPL 264
Cdd:TIGR03452 76 WPDIVSRVFGDRIDPIAAGGEDYrrgdetpNIDVYDGHARFVGPRTLRTGDGEEITGDQIVIAAGSR--PYIPPAIADSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 265 VM--TSDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKgMTILTGTKL 342
Cdd:TIGR03452 154 VRyhTNEDIMRLPELPESLVIVGGGYIAAEFAHVFSALGTRVTIVNRSTKLLRHLDEDISDRFTEIAKKK-WDIRLGRNV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 343 QEIIEENGQLRIKVEGKDNIIASKALLSIGRMP-----DLEGIGeVEFElDRGCIKVNEYMETSVPGIYAPGDINGTKML 417
Cdd:TIGR03452 233 TAVEQDGDGVTLTLDDGSTVTADVLLVATGRVPngdllDAEAAG-VEVD-EDGRIKVDEYGRTSARGVWALGDVSSPYQL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 418 AHAAFRMGEVSAENAL------KGNHAVaklnlTPAAIYTLPEVAAVGLTEEQAREK-YD--VAIGKFNFAANGRAIASD 488
Cdd:TIGR03452 311 KHVANAEARVVKHNLLhpndlrKMPHDF-----VPSAVFTHPQIATVGLTEQEAREAgHDitVKIQNYGDVAYGWAMEDT 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447085691 489 aaQGFVKVIADKKYGEILGVHIIGPAAAELINEASSIIEMEITVEEML-KTIHGHPTYSEVMYEA 552
Cdd:TIGR03452 386 --TGFCKLIADRDTGKLLGAHIIGPQASSLIQPLITAMAFGLDAREMArKQYWIHPALPEVVENA 448
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
112-556 |
1.19e-46 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 169.57 E-value: 1.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 112 FDIVVIGGGPAGYVAAIKAAQLGGKVALVEKSE--LGGTCLNRGCIPTKTYLHNAEIIENIGHAANR--GIV--IENPNF 185
Cdd:NF040477 4 YQAIIIGFGKAGKTLAATLAKAGWRVAIIEQSAqmYGGTCINIGCIPTKTLVHDAEQHQDFSTAMQRksSVVgfLRDKNY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 186 --TVDMEKLletkskvvnTLVVGVAGLLRSYGVTVHKGigtitkdknvlvNGSELLETKKIILAGGSKVSKINVPGM-ES 262
Cdd:NF040477 84 hnLADLDNV---------DVINGRAEFIDNHTLRVFQA------------DGEQELRGEKIFINTGAQSVLPPIPGLtTT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 263 PLVMTSDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTKL 342
Cdd:NF040477 143 PGVYDSTGLLNLTQLPARLGILGGGYIGVEFASMFARFGSKVTIFEAAELFLPREDRDIAQAIATILQDQGVELILNAQV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 343 QEIIEENGQlrIKVEGKDNIIASKALL-SIGRMPDLEGI----GEVEFElDRGCIKVNEYMETSVPGIYAPGDINGTKML 417
Cdd:NF040477 223 QRVSSHEGE--VQLETAEGVLTVDALLvASGRKPATAGLqlqnAGVAVN-ERGAIVVDKYLRTTADNIWAMGDVTGGLQF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 418 AHAA---FR------MGEVSAENALKGNhavaklnlTPAAIYTLPEVAAVGLTEEQAREK-YDVAIGKFNFAANGRAIAS 487
Cdd:NF040477 300 TYISlddFRivrdslLGEGKRSTDDRQN--------VPYSVFMTPPLSRIGMTEEQARASgADIQVVTLPVAAIPRARVM 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447085691 488 DAAQGFVKVIADKKYGEILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSEVMYEAFADV 556
Cdd:NF040477 372 NDTRGVLKAVVDNKTQRILGVSLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSESLNDLFALI 440
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
112-548 |
5.75e-44 |
|
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: 163.10 E-value: 5.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 112 FDIVVIGGGPAGYVAAIKAAQLGGKVALVEKSE---------LGGTCLNRGCIPtKTYLHNAEII-ENIGHAANRGIVIE 181
Cdd:TIGR01438 3 YDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTptplgtrwgIGGTCVNVGCIP-KKLMHQAALLgQALKDSRNYGWKVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 182 NpNFTVDMEKLLETKSKVVNTLVVGVAGLLRSYGVTVHKGIGTItKDKNVLV----NGSE-LLETKKIILAGGSKVSKIN 256
Cdd:TIGR01438 82 E-TVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEF-VDKHRIKatnkKGKEkIYSAERFLIATGERPRYPG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 257 VPGmESPLVMTSDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTViemMDRIVP--AMDAEVSKNLRLILERKGM 334
Cdd:TIGR01438 160 IPG-AKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTV---MVRSILlrGFDQDCANKVGEHMEEHGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 335 TILTGTKLQEIIEENGQLRIKVEGKDNIIASK---ALLSIGRMPDLEGIG----EVEFELDRGCIKVNEYMETSVPGIYA 407
Cdd:TIGR01438 236 KFKRQFVPIKVEQIEAKVLVEFTDSTNGIEEEydtVLLAIGRDACTRKLNlenvGVKINKKTGKIPADEEEQTNVPYIYA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 408 PGDI-NGTKMLAHAAFRMGEVSAENALKGNHAVAKLNLTPAAIYTLPEVAAVGLTEEQAREKY-----DVAIGKFNFAAN 481
Cdd:TIGR01438 316 VGDIlEDKPELTPVAIQAGRLLAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAVEKFgeenvEVFHSYFWPLEW 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447085691 482 GRAIASDAAQGFVKVIADKKYGE-ILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSEV 548
Cdd:TIGR01438 396 TIPSRDNHNKCYAKLVCNKKENErVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEV 463
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
112-554 |
1.34e-43 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 160.95 E-value: 1.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 112 FDIVVIGGGPAGYVAAIKAAQLGGKVALVEKSE--LGGTCLNRGCIPTKTYLHNAEIIENIGHAANRGIVI----ENPNF 185
Cdd:PRK08010 4 YQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNamYGGTCINIGCIPTKTLVHDAQQHTDFVRAIQRKNEVvnflRNKNF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 186 --TVDMEKLletkskvvnTLVVGVAGLLRSYGVTVHKGigtitkDKNVLVNGselletKKIILAGGSKVSKINVPGMES- 262
Cdd:PRK08010 84 hnLADMPNI---------DVIDGQAEFINNHSLRVHRP------EGNLEIHG------EKIFINTGAQTVVPPIPGITTt 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 263 PLVMTSDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTKL 342
Cdd:PRK08010 143 PGVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 343 QEIIEENGQlrIKVEGKDNIIASKALL-SIGRMPDLEGIGEVEFEL---DRGCIKVNEYMETSVPGIYAPGDINGTKMLA 418
Cdd:PRK08010 223 ERISHHENQ--VQVHSEHAQLAVDALLiASGRQPATASLHPENAGIavnERGAIVVDKYLHTTADNIWAMGDVTGGLQFT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 419 HAAFRMGEVSAENAL-KGNHAVAKLNLTPAAIYTLPEVAAVGLTEEQAREK-YDVAIGKFNFAANGRAIASDAAQGFVKV 496
Cdd:PRK08010 301 YISLDDYRIVRDELLgEGKRSTDDRKNVPYSVFMTPPLSRVGMTEEQARESgADIQVVTLPVAAIPRARVMNDTRGVLKA 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 447085691 497 IADKKYGEILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSEVMYEAFA 554
Cdd:PRK08010 381 IVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLNDLFS 438
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
94-547 |
1.38e-40 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 155.03 E-value: 1.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 94 SPVPVASTSNDDGKSDDA---FDIVVIGGGPAGYVAAIKAAQLGGKVALVE------KSE----LGGTCLNRGCIPTKTY 160
Cdd:PLN02546 59 RRRSVSRAAAPNGAESERhydFDLFTIGAGSGGVRASRFASNFGASAAVCElpfatiSSDtlggVGGTCVLRGCVPKKLL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 161 LHNAEIIENIGHAANRGIVIE-NPNFtvDMEKLLETKSKVVNTLVVGVAGLLRSYGVTVHKGIGTITKDKNVLVNGsELL 239
Cdd:PLN02546 139 VYASKYSHEFEESRGFGWKYEtEPKH--DWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDVDG-KLY 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 240 ETKKIILAGGSKVSKINVPGMESplVMTSDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTVIEMMDRIVPAMDA 319
Cdd:PLN02546 216 TARNILIAVGGRPFIPDIPGIEH--AIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKKVLRGFDE 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 320 EVSKNLRLILERKGMTILTGTKLQEIIEEN-GQLRIK-----VEGkdniiASKALLSIGRMPDLEGIG--EVEFELDR-G 390
Cdd:PLN02546 294 EVRDFVAEQMSLRGIEFHTEESPQAIIKSAdGSLSLKtnkgtVEG-----FSHVMFATGRKPNTKNLGleEVGVKMDKnG 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 391 CIKVNEYMETSVPGIYAPGDINGTKMLAHAAFRMGEVSAENALKGNHAVAKLNLTPAAIYTLPEVAAVGLTEEQAREKY- 469
Cdd:PLN02546 369 AIEVDEYSRTSVPSIWAVGDVTDRINLTPVALMEGGALAKTLFGNEPTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYg 448
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447085691 470 DVAIGKFNFAANGRAIASDAAQGFVKVIADKKYGEILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSE 547
Cdd:PLN02546 449 DVDVFTANFRPLKATLSGLPDRVFMKLIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAE 526
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
445-552 |
2.42e-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: 141.92 E-value: 2.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 445 TPAAIYTLPEVAAVGLTEEQAREKY-DVAIGKFNFAANGRAIASDAAQGFVKVIADKKYGEILGVHIIGPAAAELINEAS 523
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGgEVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQEAA 80
|
90 100
....*....|....*....|....*....
gi 447085691 524 SIIEMEITVEEMLKTIHGHPTYSEVMYEA 552
Cdd:pfam02852 81 LAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
88-547 |
4.37e-40 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 153.62 E-value: 4.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 88 SASPEASPVPVASTSnddgKSDDAFDIVVIGGGPAGYVAAIKAAQLGGKVALVEKSELGGTCLNRGCIPTKTYLHNAEII 167
Cdd:PTZ00058 29 YHNLEASSAPTHLKK----KPRMVYDLIVIGGGSGGMAAARRAARNKAKVALVEKDYLGGTCVNVGCVPKKIMFNAASIH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 168 ENIGHAANRGIvieNPNFTVDMEKLLETKSKVVNTLVVGVAGLLRSYGVTVHKGIGTITKDKNVLV----------NGSE 237
Cdd:PTZ00058 105 DILENSRHYGF---DTQFSFNLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLIkkvsqvdgeaDESD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 238 ------------------LLETKKIILAGGSKVSKINVPGMEspLVMTSDDILEMNEvPESLVIIGGGVVGIELGQAFMT 299
Cdd:PTZ00058 182 ddevtivsagvsqlddgqVIEGKNILIAVGNKPIFPDVKGKE--FTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 300 FGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTKLQEI--IEENGQLRIKVEGKDNIIASKALLSIGRMPDL 377
Cdd:PTZ00058 259 LGAESYIFARGNRLLRKFDETIINELENDMKKNNINIITHANVEEIekVKEKNLTIYLSDGRKYEHFDYVIYCVGRSPNT 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 378 EGIG--EVEFELDRGCIKVNEYMETSVPGIYAPGDINGTKM----------------------------------LAHAA 421
Cdd:PTZ00058 339 EDLNlkALNIKTPKGYIKVDDNQRTSVKHIYAVGDCCMVKKnqeiedlnllklyneepylkkkentsgesyynvqLTPVA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 422 FRMGEVSAENALKGNHAVAKLNLTPAAIYTLPEVAAVGLTEEQAREKY---DVAIGKFNFAANGRAI----ASDAAQGFV 494
Cdd:PTZ00058 419 INAGRLLADRLFGPFSRTTNYKLIPSVIFSHPPIGTIGLSEQEAIDIYgkeNVKIYESRFTNLFFSVydmdPAQKEKTYL 498
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 447085691 495 KVIADKKYGEILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSE 547
Cdd:PTZ00058 499 KLVCVGKEELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIHPTAAE 551
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
112-548 |
6.42e-34 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 134.95 E-value: 6.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 112 FDIVVIGGGPAGYVAAIKAAQLGGKVALVE---------KSELGGTCLNRGCIPtKTYLHNAEIIENIGH--AANRGIVI 180
Cdd:PTZ00052 6 YDLVVIGGGSGGMAAAKEAAAHGKKVALFDyvkpstqgtKWGLGGTCVNVGCVP-KKLMHYAANIGSIFHhdSQMYGWKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 181 ENpnfTVDMEKLLETKSKVVNTLVVGVAGLLRSYGVTVHKGIGTItKDKNVLVNGS----ELLETKKIILAGGSKVS-KI 255
Cdd:PTZ00052 85 SS---SFNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKL-KDEHTVSYGDnsqeETITAKYILIATGGRPSiPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 256 NVPGMESpLVMTSDDILEMNEVPESLVIIGGGVVGIELGQAFMTFGSKVTViEMMDRIVPAMDAEVSKNLRLILERKGMT 335
Cdd:PTZ00052 161 DVPGAKE-YSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTV-AVRSIPLRGFDRQCSEKVVEYMKEQGTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 336 ILTGTKLQEIieENGQLRIKVEGKDNIIA--SKALLSIGRMPDLEGIG--EVEFELDRGCIKVNEYMETSVPGIYAPGDI 411
Cdd:PTZ00052 239 FLEGVVPINI--EKMDDKIKVLFSDGTTElfDTVLYATGRKPDIKGLNlnAIGVHVNKSNKIIAPNDCTNIPNIFAVGDV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 412 -NGTKMLAHAAFRMGEVSAENALKGNHAVAKLNLTPAAIYTLPEVAAVGLTEEQAREKY-----DVAIGKFN---FAANG 482
Cdd:PTZ00052 317 vEGRPELTPVAIKAGILLARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYgeddiEEYLQEFNtleIAAVH 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447085691 483 R--AIASDAAQG--------FVKVIADKKYGE-ILGVHIIGPAAAELINEASSIIEMEITVEEMLKTIHGHPTYSEV 548
Cdd:PTZ00052 397 RekHERARKDEYdfdvssncLAKLVCVKSEDNkVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHPTDAEV 473
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1-100 |
9.18e-27 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 112.58 E-value: 9.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 1 MALEVIMPKAGVDMTEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVPVTEVIGYLGEER 80
Cdd:PRK11856 1 MMFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEG 80
|
90 100
....*....|....*....|
gi 447085691 81 ENIPTAGSASPEASPVPVAS 100
Cdd:PRK11856 81 EAEAAAAAEAAPEAPAPEPA 100
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
4-76 |
1.07e-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: 1.07e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447085691 4 EVIMPKAGVDMTEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVPVTEVIGYL 76
Cdd:cd06849 2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-76 |
1.33e-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: 1.33e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447085691 1 MALEVIMPKAGVDMTEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVPVTEVIGYL 76
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
112-434 |
2.04e-23 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 100.96 E-value: 2.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 112 FDIVVIGGGPAGYVAAIKAAQLGGKVALVEKSELGGTclnrgciptktyLHNAEIIENIghaanrgivienPNFTVD--- 188
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQ------------LATTKEIENY------------PGFPEGisg 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 189 ---MEKLLEtkskvvntlvvgvagLLRSYGVTVHKG-IGTITKDKN---VLVNGSELLETKKIILAGGSKVSKINVPGME 261
Cdd:COG0492 57 pelAERLRE---------------QAERFGAEILLEeVTSVDKDDGpfrVTTDDGTEYEAKAVIIATGAGPRKLGLPGEE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 262 SPL---VMTS--DDILEM-NE-----------VPESLviigggvvgielgqaFMT-FGSKVTVIemmdriVPAMDAEVSK 323
Cdd:COG0492 122 EFEgrgVSYCatCDGFFFrGKdvvvvgggdsaLEEAL---------------YLTkFASKVTLI------HRRDELRASK 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 324 NL-RLILERKGMTILTGTKLQEIIEENGQLRIKVEGKDN-----IIASKALLSIGRMPDLEGIGEVEFELD-RGCIKVNE 396
Cdd:COG0492 181 ILvERLRANPKIEVLWNTEVTEIEGDGRVEGVTLKNVKTgeekeLEVDGVFVAIGLKPNTELLKGLGLELDeDGYIVVDE 260
|
330 340 350
....*....|....*....|....*....|....*....
gi 447085691 397 YMETSVPGIYAPGDINGTKM-LAHAAFRMGEVSAENALK 434
Cdd:COG0492 261 DMETSVPGVFAAGDVRDYKYrQAATAAGEGAIAALSAAR 299
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
211-459 |
1.03e-21 |
|
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: 96.03 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 211 LRSYGVTVHKG---IGTITKDKNVLVNGSELLETKKIILAGGSKVSKINVPGMESPLVMTSDDILEMNEVPESLVIIGGG 287
Cdd:COG0446 46 FERKGIDVRTGtevTAIDPEAKTVTLRDGETLSYDKLVLATGARPRPPPIPGLDLPGVFTLRTLDDADALREALKEFKGK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 288 VVG--------IELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTKLQEiIEENGQLRIKVEGK 359
Cdd:COG0446 126 RAVvigggpigLELAEALRKRGLKVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVVA-IDGDDKVAVTLTDG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 360 DNIIASKALLSIGRMPDLEGIGEVEFELD-RGCIKVNEYMETSVPGIYAPGD-------INGTKM---LAHAAFRMGEVS 428
Cdd:COG0446 205 EEIPADLVVVAPGVRPNTELAKDAGLALGeRGWIKVDETLQTSDPDVYAAGDcaevphpVTGKTVyipLASAANKQGRVA 284
|
250 260 270
....*....|....*....|....*....|.
gi 447085691 429 AENALKGNHAVAKLNLTPAAIYTLpEVAAVG 459
Cdd:COG0446 285 AENILGGPAPFPGLGTFISKVFDL-CIASTG 314
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
1-102 |
1.64e-20 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 93.75 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 1 MALEVIMPKAGVDMTEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVPVTEVIGYLGEER 80
Cdd:PRK05704 1 MMVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGA 80
|
90 100
....*....|....*....|..
gi 447085691 81 ENIPTAGSASPEASPVPVASTS 102
Cdd:PRK05704 81 AAGAAAAAAAAAAAAAAAPAQA 102
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
4-103 |
1.06e-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: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 4 EVIMPKAGVDMTEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVPVTEVIGYLGEEreni 83
Cdd:TIGR01347 2 EIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEG---- 77
|
90 100
....*....|....*....|
gi 447085691 84 PTAGSASPEASPVPVASTSN 103
Cdd:TIGR01347 78 NDATAAPPAKSGEEKEETPA 97
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
4-97 |
1.25e-18 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 89.14 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 4 EVIMPKAGVDMTEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDG-ETVPVTEVIGYLGEEREN 82
Cdd:PLN02744 114 EIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGaKEIKVGEVIAITVEEEED 193
|
90 100
....*....|....*....|....
gi 447085691 83 I---------PTAGSASPEASPVP 97
Cdd:PLN02744 194 IgkfkdykpsSSAAPAAPKAKPSP 217
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
113-433 |
3.19e-18 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 86.73 E-value: 3.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 113 DIVVIGGGPAGYVAAIKAAQLGGKVALVekselggtclnrgciptktylhnaeIIENIGHAA-NRgivienpnftVDMEK 191
Cdd:COG1251 3 RIVIIGAGMAGVRAAEELRKLDPDGEIT-------------------------VIGAEPHPPyNR----------PPLSK 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 192 LLETKSKVvNTLVVGVAGLLRSYGVTVHKGIgTITK----DKNVLVNGSELLETKKIILAGGSKVSKINVPGMESPLVM- 266
Cdd:COG1251 48 VLAGETDE-EDLLLRPADFYEENGIDLRLGT-RVTAidraARTVTLADGETLPYDKLVLATGSRPRVPPIPGADLPGVFt 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 267 --TSDDILEMNEvpeSLVIIGGG------VVGIELGQAFMTFGSKVTVIEMMDRIVP-AMDAEVSKNLRLILERKGMTIL 337
Cdd:COG1251 126 lrTLDDADALRA---ALAPGKRVvvigggLIGLEAAAALRKRGLEVTVVERAPRLLPrQLDEEAGALLQRLLEALGVEVR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 338 TGTKLQEIIEENGQLRIKVEGKDNIIASKALLSIGRMPDLE-----GIgevefELDRGcIKVNEYMETSVPGIYAPGD-- 410
Cdd:COG1251 203 LGTGVTEIEGDDRVTGVRLADGEELPADLVVVAIGVRPNTElaraaGL-----AVDRG-IVVDDYLRTSDPDIYAAGDca 276
|
330 340 350
....*....|....*....|....*....|
gi 447085691 411 -----INGTKMLAH--AAFRMGEVSAENAL 433
Cdd:COG1251 277 ehpgpVYGRRVLELvaPAYEQARVAAANLA 306
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
1-79 |
1.77e-16 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 81.14 E-value: 1.77e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447085691 1 MALEVIMPKAGVDMTEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVPVTEVIGYLGEE 79
Cdd:PRK14875 1 SITPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADA 79
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
288-535 |
2.50e-16 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 81.63 E-value: 2.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 288 VVGIELGQAFMTFGSKVTVIEMMDRIVP-AMDAEVSKNLRLILERKGMTILTGTKLQEIIEENgqlriKVEG----KDNI 362
Cdd:PRK09564 159 FIGLEAVEAAKHLGKNVRIIQLEDRILPdSFDKEITDVMEEELRENGVELHLNEFVKSLIGED-----KVEGvvtdKGEY 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 363 IASKALLSIGRMPDLEGIGEVEFE-LDRGCIKVNEYMETSVPGIYAPGD-------INGTKM---LAHAAFRMGEVSAEN 431
Cdd:PRK09564 234 EADVVIVATGVKPNTEFLEDTGLKtLKNGAIIVDEYGETSIENIYAAGDcatiyniVSNKNVyvpLATTANKLGRMVGEN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 432 aLKGNHAVAKLNLTPAAIYTLP-EVAAVGLTEEQARE---KYDVAIGK----FNFAANGRAIasdaaqgFVKVIADKKYG 503
Cdd:PRK09564 314 -LAGRHVSFKGTLGSACIKVLDlEAARTGLTEEEAKKlgiDYKTVFIKdknhTNYYPGQEDL-------YVKLIYEADTK 385
|
250 260 270
....*....|....*....|....*....|...
gi 447085691 504 EILGVHIIGPAAAEL-INEASSIIEMEITVEEM 535
Cdd:PRK09564 386 VILGGQIIGKKGAVLrIDALAVAIYAKLTTQEL 418
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
1-102 |
2.97e-16 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 81.50 E-value: 2.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 1 MALEVIMPKAGVDMTEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDG-ETVPVTEVIGYLGEE 79
Cdd:PRK11892 1 MAIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTPIAVLLEE 80
|
90 100
....*....|....*....|...
gi 447085691 80 RENIPTAGSASPEASPVPVASTS 102
Cdd:PRK11892 81 GESASDAGAAPAAAAEAAAAAPA 103
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
4-76 |
1.51e-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: 68.78 E-value: 1.51e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447085691 4 EVIMPKAGVDMTEGqIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVPVTEVIGYL 76
Cdd:pfam00364 2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
303-435 |
4.56e-14 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 74.01 E-value: 4.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 303 KVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTKLQEiIEENGqlrIKVEGKDNIIASKALLSIG-RMPDLegIG 381
Cdd:COG1252 187 RITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTE-VDADG---VTLEDGEEIPADTVIWAAGvKAPPL--LA 260
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447085691 382 EVEFELDR-GCIKVNEYMET-SVPGIYAPGDI--------NGTKMLAHAAFRMGEVSAEN---ALKG 435
Cdd:COG1252 261 DLGLPTDRrGRVLVDPTLQVpGHPNVFAIGDCaavpdpdgKPVPKTAQAAVQQAKVLAKNiaaLLRG 327
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1-120 |
9.60e-12 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 67.72 E-value: 9.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 1 MALEVIMPKAGVDmtEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVPVTEVIGYLGEEr 80
Cdd:PRK11854 1 MAIEIKVPDIGAD--EVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESA- 77
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 447085691 81 eniPTAGSASPEASPVPVASTSNDDGKSDDAFDIVV--IGGG 120
Cdd:PRK11854 78 ---DGAADAAPAQAEEKKEAAPAAAPAAAAAKDVHVpdIGSD 116
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
8-99 |
1.64e-11 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 66.24 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 8 PKAGVDMTEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVPVtevigylGEERENIPTAG 87
Cdd:PTZ00144 50 PTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEV-------GAPLSEIDTGG 122
|
90
....*....|..
gi 447085691 88 SASPEASPVPVA 99
Cdd:PTZ00144 123 APPAAAPAAAAA 134
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
4-140 |
4.80e-11 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 65.23 E-value: 4.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 4 EVIMPKAGvDMTEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVPVTEVIGYLGEERENI 83
Cdd:PRK11855 121 EVKVPDIG-EITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAAP 199
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 447085691 84 PTAGSASPEASPVPVASTSNDDGKSddafdivviggGPAGYVAAIKAAQLGGKVALV 140
Cdd:PRK11855 200 AAAAAPAAAAPAAAAAAAPAPAPAA-----------AAAPAAAAPAAAAAPGKAPHA 245
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
215-435 |
7.10e-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: 7.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 215 GVTVHKGIGTITKD---KNVLVNGSELLETKKIILAGGSKVSKINVPGMESPLVM---TSDD---ILEMNEVPESLVIIG 285
Cdd:TIGR02374 68 GITLYTGETVIQIDtdqKQVITDAGRTLSYDKLILATGSYPFILPIPGADKKGVYvfrTIEDldaIMAMAQRFKKAAVIG 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 286 GGVVGIELGQAFMTFGSKVTVIEMMDRIVP-AMDAEVSKNLRLILERKGMTILTGTKLQEIIEENGQLRIKVEGKDNIIA 364
Cdd:TIGR02374 148 GGLLGLEAAVGLQNLGMDVSVIHHAPGLMAkQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVGATKADRIRFKDGSSLEA 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447085691 365 SKALLSIGRMPDLEGIGEVEFELDRGCIkVNEYMETSVPGIYAPGD---INGTKM-LAHAAFRMGEVSAENALKG 435
Cdd:TIGR02374 228 DLIVMAAGIRPNDELAVSAGIKVNRGII-VNDSMQTSDPDIYAVGEcaeHNGRVYgLVAPLYEQAKVLADHICGV 301
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
4-120 |
7.79e-11 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 64.64 E-value: 7.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 4 EVIMPKAGVDmtEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVPVTEVIGYLGEERENI 83
Cdd:PRK11854 107 DVHVPDIGSD--EVEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFEVAGEAP 184
|
90 100 110
....*....|....*....|....*....|....*....
gi 447085691 84 PTAGSASPEASPVPVASTsnddgkSDDAFDIVV--IGGG 120
Cdd:PRK11854 185 AAAPAAAEAAAPAAAPAA------AAGVKDVNVpdIGGD 217
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1-102 |
7.82e-11 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 64.46 E-value: 7.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 1 MALEVIMPKAGvDMTEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVPVTEVIGYLGEER 80
Cdd:PRK11855 1 MAIEFKVPDIG-EVVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIEAAG 79
|
90 100
....*....|....*....|..
gi 447085691 81 EnipTAGSASPEASPVPVASTS 102
Cdd:PRK11855 80 A---AAAAAAPAAAAAPAAAAA 98
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
288-359 |
1.85e-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: 57.21 E-value: 1.85e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447085691 288 VVGIELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTILTGTKLQEIIEENGQLRIKVEGK 359
Cdd:pfam00070 9 YIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLTDG 80
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
289-418 |
5.00e-09 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 58.39 E-value: 5.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 289 VGIELGQAFMTFGSKVTVIEMMDRIVPA-MDAEVSKNLRLILERKGMTILTGTKLQEIIEENGQLRIKVEGKDNIIASKA 367
Cdd:PRK04965 152 IGTELAMDLCRAGKAVTLVDNAASLLASlMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRATLDSGRSIEVDAV 231
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 447085691 368 LLSIGRMPDLEGIGEVEFELDRGcIKVNEYMETSVPGIYAPGD---INGtKMLA 418
Cdd:PRK04965 232 IAAAGLRPNTALARRAGLAVNRG-IVVDSYLQTSAPDIYALGDcaeING-QVLP 283
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
4-68 |
5.53e-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: 5.53e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447085691 4 EVIMPKAGVDMTEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVP 68
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVE 65
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
2-100 |
6.15e-09 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 58.86 E-value: 6.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 2 ALEVIMPKAGVDmtEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVPVTEVIGYLGeere 81
Cdd:PRK11854 206 VKDVNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFE---- 279
|
90
....*....|....*....
gi 447085691 82 nipTAGSAsPEASPVPVAS 100
Cdd:PRK11854 280 ---VEGAA-PAAAPAKQEA 294
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
68-411 |
1.69e-08 |
|
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: 57.07 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 68 PVTevIGYLgeERENIPTAGSASPEASPVPVASTsnddGKSddafdIVVIGGGPAGYVAAIKAAQLGGKVALVEK-SELG 146
Cdd:COG0493 91 PVA--IGAL--ERFIADKAFEEGWVKPPPPAPRT----GKK-----VAVVGSGPAGLAAAYQLARAGHEVTVFEAlDKPG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 147 GtcLNRgciptktYlhnaeiienighaanrGIvienPNFTvdMEKlletksKVVNTLVvgvaGLLRSYGVTVHKGIgTIT 226
Cdd:COG0493 158 G--LLR-------Y----------------GI----PEFR--LPK------DVLDREI----ELIEALGVEFRTNV-EVG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 227 KDKNVlvngSELLET-KKIILAGGS-KVSKINVPGMESPLVMTSDDILEMNEvpeslviigggvvGIELGQAFMTFG--- 301
Cdd:COG0493 196 KDITL----DELLEEfDAVFLATGAgKPRDLGIPGEDLKGVHSAMDFLTAVN-------------LGEAPDTILAVGkrv 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 302 ---------------------SKVTVIEMMDRI-VPAMDAEVSKnlrliLERKGMTILTGTKLQEII-EENGQLR----- 353
Cdd:COG0493 259 vvigggntamdcartalrlgaESVTIVYRRTREeMPASKEEVEE-----ALEEGVEFLFLVAPVEIIgDENGRVTglecv 333
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447085691 354 ---------------IKVEGKDNII-ASKALLSIGRMPDLEGIGEV-EFELD-RGCIKVNE-YMETSVPGIYAPGDI 411
Cdd:COG0493 334 rmelgepdesgrrrpVPIEGSEFTLpADLVILAIGQTPDPSGLEEElGLELDkRGTIVVDEeTYQTSLPGVFAGGDA 410
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
113-148 |
1.89e-08 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 56.85 E-value: 1.89e-08
10 20 30
....*....|....*....|....*....|....*..
gi 447085691 113 DIVVIGGGPAGYVAAIKAAQLGGKVALVEKS-ELGGT 148
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRgFLGGM 37
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
113-158 |
4.60e-08 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 55.25 E-value: 4.60e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 447085691 113 DIVVIGGGPAGYVAAIKAAQLGGKVALVekSELGGTCLNRGCIPTK 158
Cdd:pfam01134 1 DVIVIGGGHAGCEAALAAARMGAKVLLI--THNTDTIAELSCNPSI 44
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
109-147 |
6.04e-08 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 55.22 E-value: 6.04e-08
10 20 30
....*....|....*....|....*....|....*....
gi 447085691 109 DDAFDIVVIGGGPAGYVAAIKAAQLGGKVALVEKSELGG 147
Cdd:COG1053 1 DHEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRG 39
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
112-251 |
7.18e-08 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 54.89 E-value: 7.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 112 FDIVVIGGGPAGYVAAIKAAQLGGKVALVEKSEL---------GGTC-LNRGCIPTKTYLHNaeIIEN------------ 169
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKlgrkilisgGGRCnVTNLSEEPDNFLSR--YPGNpkflksalsrft 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 170 ----IGHAANRGI-VIENPN---FTVDMeklletKSK-VVNTLVvgvaGLLRSYGVTVH-----KGIgTITKDKNVLVN- 234
Cdd:pfam03486 79 pwdfIAFFESLGVpLKEEDHgrlFPDSD------KASdIVDALL----NELKELGVKIRlrtrvLSV-EKDDDGRFRVKt 147
|
170
....*....|....*..
gi 447085691 235 GSELLETKKIILAGGSK 251
Cdd:pfam03486 148 GGEELEADSLVLATGGL 164
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
217-467 |
1.19e-07 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 54.40 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 217 TVHKGIGTITKDKNVLVNGSELLET-----KKIILAGGSKVskiNVPGMESPLVMT------SDDI---LEMNEVPESLV 282
Cdd:PRK13512 77 TYHEVIAINDERQTVTVLNRKTNEQfeesyDKLILSPGASA---NSLGFESDITFTlrnledTDAIdqfIKANQVDKALV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 283 IIGGGVVGiELGQAFMTFGSKVTVIEMMDRIVPAMDAEVSKNLRLILERKGMTIltgtKL-QEIIEENGQLRI----KVE 357
Cdd:PRK13512 154 VGAGYISL-EVLENLYERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPY----RLnEEIDAINGNEVTfksgKVE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 358 GKDNIIASkallsIGRMPDLEGIGEVEFELDR-GCIKVNEYMETSVPGIYAPGDI----------NGTKMLAHAAFRMGE 426
Cdd:PRK13512 229 HYDMIIEG-----VGTHPNSKFIESSNIKLDDkGFIPVNDKFETNVPNIYAIGDIitshyrhvdlPASVPLAWGAHRAAS 303
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 447085691 427 VSAENaLKGNHAVAKLNLTPAAI-----YTLpevAAVGLTEEQARE 467
Cdd:PRK13512 304 IVAEQ-IAGNDTIEFKGFLGNNIvkffdYTF---ASVGVKPNELKQ 345
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
109-148 |
1.81e-07 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 53.97 E-value: 1.81e-07
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 447085691 109 DDAFDIVVIGGGPAGYVAAIKAAQLGGKVALVEKSE-LGGT 148
Cdd:PRK12843 14 DAEFDVIVIGAGAAGMSAALFAAIAGLKVLLVERTEyVGGT 54
|
|
| TIGR00275 |
TIGR00275 |
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ... |
115-251 |
1.97e-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: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 115 VVIGGGPAGYVAAIKAAQLGGKVALVEKSEL---------GGTClNrgciptktyLHNAEIIENIghAANRGiviENPNF 185
Cdd:TIGR00275 1 IIIGGGAAGLMAAITAARAGLSVLLLEKNKKigkkllisgGGRC-N---------LTNSCPTPEF--VAYYP---RNGKF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 186 ------------TVD-MEKL-LETKSK--------------VVNTLvvgvAGLLRSYGVTVHKG--IGTITKDKN--VLV 233
Cdd:TIGR00275 66 lrsalsrfsnkdLIDfFESLgLELKVEedgrvfpcsdsaadVLDAL----LNELKELGVEILTNskVKSIEKEDGgfGVE 141
|
170
....*....|....*...
gi 447085691 234 NGSELLETKKIILAGGSK 251
Cdd:TIGR00275 142 TSGGEYEADKVIIATGGL 159
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
114-411 |
1.99e-07 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 54.00 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 114 IVVIGGGPAGYVAAIKAAQLGGKVALVEKSELGGTCLNRGcIPTKTYLHNAeiienighaanrgivienpnftvdMEKLL 193
Cdd:PRK13984 286 VAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGVMRYG-IPSYRLPDEA------------------------LDKDI 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 194 EtkskvvntlvvgvagLLRSYGVTVHKGIgTITKDknvlVNGSELLETKKIIL--AGGSKVSKINVPGMESPLVMTSDDI 271
Cdd:PRK13984 341 A---------------FIEALGVKIHLNT-RVGKD----IPLEELREKHDAVFlsTGFTLGRSTRIPGTDHPDVIQALPL 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 272 LEM-----------NEVPESLVIIGGGVVGIELGQA-----FMTFG-SKVTVI-------EM---MDRIVPAMDAEVSKN 324
Cdd:PRK13984 401 LREirdylrgegpkPKIPRSLVVIGGGNVAMDIARSmarlqKMEYGeVNVKVTslertfeEMpadMEEIEEGLEEGVVIY 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 325 -----LRLILERKGMTILTGTKLQEIIEENGQLRIKVEGKDNII--ASKALLSIGRMPDLEGIGE---VEFELDRGCIKV 394
Cdd:PRK13984 481 pgwgpMEVVIENDKVKGVKFKKCVEVFDEEGRFNPKFDESDQIIveADMVVEAIGQAPDYSYLPEelkSKLEFVRGRILT 560
|
330
....*....|....*..
gi 447085691 395 NEYMETSVPGIYAPGDI 411
Cdd:PRK13984 561 NEYGQTSIPWLFAGGDI 577
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
113-150 |
4.64e-07 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 52.29 E-value: 4.64e-07
10 20 30
....*....|....*....|....*....|....*...
gi 447085691 113 DIVVIGGGPAGYVAAIKAAQLGGKVALVEKSELGGTCL 150
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGAT 38
|
|
| GlpB |
COG3075 |
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism]; |
112-140 |
2.59e-06 |
|
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 442309 Cd Length: 415 Bit Score: 49.79 E-value: 2.59e-06
10 20
....*....|....*....|....*....
gi 447085691 112 FDIVVIGGGPAGYVAAIKAAQLGGKVALV 140
Cdd:COG3075 3 FDVVVIGGGLAGLTAAIRAAEAGLRVAIV 31
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
112-169 |
2.75e-06 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 49.85 E-value: 2.75e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 447085691 112 FDIVVIGGGPAGYVAAIKAAQLGGKVALVEKSElGGTCLNRGCIPTKTYLHNAEIIEN 169
Cdd:PRK05329 3 FDVLVIGGGLAGLTAALAAAEAGKRVALVAKGQ-GALHFSSGSIDLLGYLPDGQPVSD 59
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
4-141 |
3.59e-06 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 49.87 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 4 EVIMPKAGvDMTEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVPVTEVIGYL----GEE 79
Cdd:TIGR01348 2 EIKVPDIG-DNEEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLevgaGAQ 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447085691 80 RENIPTAGSASPEASPVPVASTSNDDGKSDdafdivviggGPAGYVAAIKAAQLG--GKVALVE 141
Cdd:TIGR01348 81 AQAEAKKEAAPAPTAGAPAPAAQAQAAPAA----------GQSSGVQEVTVPDIGdiEKVTVIE 134
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
110-259 |
6.85e-06 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 48.62 E-value: 6.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 110 DAFDIVVIGGGPAGYVAAIKAAQLGGKVALVEkselggtclnrgciptktylhnaeiiENIGhaanrGIVIEnpnfTVDM 189
Cdd:PRK15317 210 DPYDVLVVGGGPAGAAAAIYAARKGIRTGIVA--------------------------ERFG-----GQVLD----TMGI 254
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447085691 190 EKLLETKSKVVNTLVVGVAGLLRSYGVTV---------HKGIGTITkdknVLVNGSELLETKKIILAGGSKVSKINVPG 259
Cdd:PRK15317 255 ENFISVPETEGPKLAAALEEHVKEYDVDImnlqrasklEPAAGLIE----VELANGAVLKAKTVILATGARWRNMNVPG 329
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
113-147 |
1.00e-05 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 48.32 E-value: 1.00e-05
10 20 30
....*....|....*....|....*....|....*.
gi 447085691 113 DIVVIGGGPAGYVAAIKAAQLGGKVALVEKS-ELGG 147
Cdd:COG1148 142 RALVIGGGIAGMTAALELAEQGYEVYLVEKEpELGG 177
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
115-249 |
2.65e-05 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 46.58 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 115 VVIGGGPAGYVAAIKAAQLGGKVALVEKSE------L---GGTC--LNRGCIPtktylhnaEIIENIGhaanrgiviENP 183
Cdd:COG2081 1 IVIGAGAAGLMAAITAAERGARVLLLEKNPkvgrkiLisgGGRCnfTNSEPLP--------EFLNYYG---------GNP 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 184 NF------------TVDM-EKL-LETKSK--------------VVNTLVvgvaGLLRSYGVTVHKG--IGTITKDKNVLV 233
Cdd:COG2081 64 HFlksalsrftpedLIAFfEGLgIETKEEssgrvfpdsskasdILRALL----AELREAGVEIRLRtrVTGIEKEDGGFG 139
|
170 180
....*....|....*....|
gi 447085691 234 ---NGSELLETKKIILA-GG 249
Cdd:COG2081 140 vetPDGETVRADAVVLAtGG 159
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
112-147 |
3.10e-05 |
|
geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 273936 [Multi-domain] Cd Length: 295 Bit Score: 46.16 E-value: 3.10e-05
10 20 30
....*....|....*....|....*....|....*.
gi 447085691 112 FDIVVIGGGPAGYVAAIKAAQLGGKVALVEKSELGG 147
Cdd:TIGR02032 1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPR 36
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
112-147 |
4.07e-05 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 46.38 E-value: 4.07e-05
10 20 30
....*....|....*....|....*....|....*..
gi 447085691 112 FDIVVIGGGPAGYVAAIKAAQLGGKVALVEK-SELGG 147
Cdd:COG1233 4 YDVVVIGAGIGGLAAAALLARAGYRVTVLEKnDTPGG 40
|
|
| PRK07494 |
PRK07494 |
UbiH/UbiF family hydroxylase; |
107-140 |
4.21e-05 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181001 [Multi-domain] Cd Length: 388 Bit Score: 46.05 E-value: 4.21e-05
10 20 30
....*....|....*....|....*....|....
gi 447085691 107 KSDDAFDIVVIGGGPAGYVAAIKAAQLGGKVALV 140
Cdd:PRK07494 3 MEKEHTDIAVIGGGPAGLAAAIALARAGASVALV 36
|
|
| sdhA |
PRK07803 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
111-146 |
9.23e-05 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 236101 [Multi-domain] Cd Length: 626 Bit Score: 45.41 E-value: 9.23e-05
10 20 30
....*....|....*....|....*....|....*.
gi 447085691 111 AFDIVVIGGGPAGYVAAIKAAQLGGKVALVEKSELG 146
Cdd:PRK07803 8 SYDVVVIGAGGAGLRAAIEARERGLRVAVVCKSLFG 43
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
94-148 |
9.40e-05 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 45.10 E-value: 9.40e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 447085691 94 SPVPVASTSNDDgksddaFDIVVIGGGPAGYVAAIKAAQLGGKVALVEKS-ELGGT 148
Cdd:PRK06134 1 TPSAAAYPPDLE------CDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDpVFGGT 50
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
114-430 |
2.29e-04 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 44.01 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 114 IVVIGGGPAGYVAAIKAAQLGGKVALVEK-SELGGtcLNRgciptktYlhnaeiienighaanrGIvienPNFtvdmeKL 192
Cdd:PRK11749 143 VAVIGAGPAGLTAAHRLARKGYDVTIFEArDKAGG--LLR-------Y----------------GI----PEF-----RL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 193 leTKSkVVNTLVvgvaGLLRSYGVTVHKG--IG-TITKDknvlvngsELLET-KKIILA-GGSKVSKINVPGMESPLVMT 267
Cdd:PRK11749 189 --PKD-IVDREV----ERLLKLGVEIRTNteVGrDITLD--------ELRAGyDAVFIGtGAGLPRFLGIPGENLGGVYS 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 268 SDDILEMNEVPESLVIIGGgvvgielgqafmtfGSKVTVIEMMDrivPAMDAEVSKnLRL------ILERK--------- 332
Cdd:PRK11749 254 AVDFLTRVNQAVADYDLPV--------------GKRVVVIGGGN---TAMDAARTA-KRLgaesvtIVYRRgreempase 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 333 ---------GMTILTGTKLQEIIEENGQL-------------------RIKVEGKDNII-ASKALLSIG---RMPDLEGI 380
Cdd:PRK11749 316 eevehakeeGVEFEWLAAPVEILGDEGRVtgvefvrmelgepdasgrrRVPIEGSEFTLpADLVIKAIGqtpNPLILSTT 395
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 447085691 381 GEVEFELDRGCIKVNEYMETSVPGIYAPGDI-NGTKMLAHAAfRMGEVSAE 430
Cdd:PRK11749 396 PGLELNRWGTIIADDETGRTSLPGVFAGGDIvTGAATVVWAV-GDGKDAAE 445
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
3-72 |
2.55e-04 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 43.59 E-value: 2.55e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447085691 3 LEVIMPKAGVDMTEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETV-PVTEV 72
Cdd:PLN02226 92 VEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVePGTKV 162
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
105-148 |
2.80e-04 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 43.87 E-value: 2.80e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 447085691 105 DGKSDDAFDIVVIGGGPAGYVAAIKAAQLGGKVALVEKSE-LGGT 148
Cdd:PRK07843 1 MAMTVQEYDVVVVGSGAAGMVAALTAAHRGLSTVVVEKAPhYGGS 45
|
|
| NadB |
COG0029 |
Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the ... |
112-148 |
3.03e-04 |
|
Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 439800 [Multi-domain] Cd Length: 521 Bit Score: 43.56 E-value: 3.03e-04
10 20 30
....*....|....*....|....*....|....*..
gi 447085691 112 FDIVVIGGGPAGYVAAIKAAQLgGKVALVEKSELGGT 148
Cdd:COG0029 5 TDVLVIGSGIAGLSAALKLAER-GRVTLLTKGELGES 40
|
|
| PRK08275 |
PRK08275 |
putative oxidoreductase; Provisional |
394-466 |
3.20e-04 |
|
putative oxidoreductase; Provisional
Pssm-ID: 181346 [Multi-domain] Cd Length: 554 Bit Score: 43.50 E-value: 3.20e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447085691 394 VNEYMETSVPGIYAPGDINGTK---MLahAAFRMGEVSAEnalkgnHAVAKLNLTPAAIYTLPEVAAvglteEQAR 466
Cdd:PRK08275 361 VNEKAETTVPGLYAAGDMASVPhnyML--GAFTYGWFAGE------NAAEYVAGRDLPEVDAAQVEA-----ERAR 423
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
108-148 |
3.39e-04 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 43.53 E-value: 3.39e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 447085691 108 SDDAFDIVVIGGGPAGYVAAIKAAQLGGKVALVEKSE-LGGT 148
Cdd:PRK12842 6 NELTCDVLVIGSGAGGLSAAITARKLGLDVVVLEKEPvFGGT 47
|
|
| PRK13800 |
PRK13800 |
fumarate reductase/succinate dehydrogenase flavoprotein subunit; |
113-179 |
3.49e-04 |
|
fumarate reductase/succinate dehydrogenase flavoprotein subunit;
Pssm-ID: 237512 [Multi-domain] Cd Length: 897 Bit Score: 43.69 E-value: 3.49e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447085691 113 DIVVIGGGPAGYVAAIKAAQLGGKVALVEKSE--------LGGTCLNRGCIPTKT----YLhnAEIIEnighaANRGIV 179
Cdd:PRK13800 15 DVLVIGGGTAGTMAALTAAEHGANVLLLEKAHvrhsgalaMGMDGVNNAVIPGKAepedYV--AEITR-----ANDGIV 86
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
17-67 |
3.51e-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: 3.51e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 447085691 17 GQIVQWNKKVGEFVKEGEIL--LEIMtdKVSMELEAEEDGYLIAILKGDGETV 67
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLavLEAM--KMENEVTAPVAGVVKEILVKEGDQV 58
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
301-406 |
3.55e-04 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 42.60 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 301 GSKVTVIemmDR--IVPAMDAEVSKNLR-LILER-------KGMTILTGTKLQEIIEENGQLRIKVE-GKDNIIASKALL 369
Cdd:pfam13738 178 GARVTVL---YRgsEWEDRDSDPSYSLSpDTLNRleelvknGKIKAHFNAEVKEITEVDVSYKVHTEdGRKVTSNDDPIL 254
|
90 100 110
....*....|....*....|....*....|....*....
gi 447085691 370 SIGRMPDLEGIGEVEFELDR-GCIKVN-EYMETSVPGIY 406
Cdd:pfam13738 255 ATGYHPDLSFLKKGLFELDEdGRPVLTeETESTNVPGLF 293
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
113-149 |
3.68e-04 |
|
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: 43.28 E-value: 3.68e-04
10 20 30
....*....|....*....|....*....|....*...
gi 447085691 113 DIVVIGGGPAGYVAAIKAAQLGGKVALVEKSE-LGGTC 149
Cdd:COG1232 3 RVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDrVGGLI 40
|
|
| PRK08275 |
PRK08275 |
putative oxidoreductase; Provisional |
104-186 |
4.80e-04 |
|
putative oxidoreductase; Provisional
Pssm-ID: 181346 [Multi-domain] Cd Length: 554 Bit Score: 43.12 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 104 DDGKSDDAFDIVVIGGGPAGYVAAIKAAQL--GGKVALVEKSEL---GGTC-----LNRGCIPtktylhnaeiieniGHA 173
Cdd:PRK08275 2 AMNTQEVETDILVIGGGTAGPMAAIKAKERnpALRVLLLEKANVkrsGAISmgmdgLNNAVIP--------------GHA 67
|
90 100
....*....|....*....|....
gi 447085691 174 -----------ANRGIVIENPNFT 186
Cdd:PRK08275 68 tpeqytkeitiANDGIVDQKAVYA 91
|
|
| glycerol3P_GlpB |
TIGR03378 |
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are ... |
112-140 |
5.15e-04 |
|
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are the B subunit, product of the glpB gene, of a three-subunit, membrane-anchored, FAD-dependent anaerobic glycerol-3-phosphate dehydrogenase. [Energy metabolism, Anaerobic]
Pssm-ID: 213807 Cd Length: 419 Bit Score: 42.70 E-value: 5.15e-04
10 20
....*....|....*....|....*....
gi 447085691 112 FDIVVIGGGPAGYVAAIKAAQLGGKVALV 140
Cdd:TIGR03378 1 FDVIIIGGGLAGLSCALRLAEAGKKCAII 29
|
|
| PRK09126 |
PRK09126 |
FAD-dependent hydroxylase; |
112-145 |
7.06e-04 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236385 [Multi-domain] Cd Length: 392 Bit Score: 42.24 E-value: 7.06e-04
10 20 30
....*....|....*....|....*....|....
gi 447085691 112 FDIVVIGGGPAGYVAAIKAAQLGGKVALVEKSEL 145
Cdd:PRK09126 4 SDIVVVGAGPAGLSFARSLAGSGLKVTLIERQPL 37
|
|
| PRK07121 |
PRK07121 |
FAD-binding protein; |
109-148 |
7.95e-04 |
|
FAD-binding protein;
Pssm-ID: 180854 [Multi-domain] Cd Length: 492 Bit Score: 42.18 E-value: 7.95e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 447085691 109 DDAFDIVVIGGGPAGYVAAIKAAQLGGKVALVEK-SELGGT 148
Cdd:PRK07121 18 DDEADVVVVGFGAAGACAAIEAAAAGARVLVLERaAGAGGA 58
|
|
| PRK08274 |
PRK08274 |
FAD-dependent tricarballylate dehydrogenase TcuA; |
108-142 |
8.67e-04 |
|
FAD-dependent tricarballylate dehydrogenase TcuA;
Pssm-ID: 236214 [Multi-domain] Cd Length: 466 Bit Score: 42.17 E-value: 8.67e-04
10 20 30
....*....|....*....|....*....|....*
gi 447085691 108 SDDAFDIVVIGGGPAGYVAAIKAAQLGGKVALVEK 142
Cdd:PRK08274 1 MASMVDVLVIGGGNAALCAALAAREAGASVLLLEA 35
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
112-147 |
8.74e-04 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 42.12 E-value: 8.74e-04
10 20 30
....*....|....*....|....*....|....*..
gi 447085691 112 FDIVVIGGGPAGYVAAIKAAQLGGKVALVEKSE-LGG 147
Cdd:PRK12839 9 YDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKAStCGG 45
|
|
| COG3573 |
COG3573 |
Predicted oxidoreductase [General function prediction only]; |
113-147 |
1.04e-03 |
|
Predicted oxidoreductase [General function prediction only];
Pssm-ID: 442794 [Multi-domain] Cd Length: 551 Bit Score: 41.70 E-value: 1.04e-03
10 20 30
....*....|....*....|....*....|....*...
gi 447085691 113 DIVVIGGGPAGYVAAIKAAQLGGKVALVE---KSELGG 147
Cdd:COG3573 7 DVIVVGAGLAGLVAAAELADAGRRVLLLDqepEANLGG 44
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
108-148 |
1.05e-03 |
|
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];
Pssm-ID: 441675 [Multi-domain] Cd Length: 414 Bit Score: 41.77 E-value: 1.05e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 447085691 108 SDDAFDIVVIGGGPAGYVAAIKAAQLGGKVALVEK-SELGGT 148
Cdd:COG2072 3 ATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKaDDVGGT 44
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
96-466 |
1.06e-03 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 41.78 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 96 VPVASTSNDDGKSddafdIVVIGGGPAGYVAAIKAAQLGGKVALVEK-SELGGTCLnrgciptktYlhnaeiienighaa 174
Cdd:PRK12771 127 WKFPAPAPDTGKR-----VAVIGGGPAGLSAAYHLRRMGHAVTIFEAgPKLGGMMR---------Y-------------- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 175 nrGIvienPNFTVDMEKLLETKSKVVNTlvvgvagllrsyGVTVHKG--IGT-ITKDKnvlvngselLETK--KIILAGG 249
Cdd:PRK12771 179 --GI----PAYRLPREVLDAEIQRILDL------------GVEVRLGvrVGEdITLEQ---------LEGEfdAVFVAIG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 250 SKVSK-INVPGMESPLVMTSDDILEmnevpeslviigggvvGIELGQAFMTfGSKVTVI----EMMD------------- 311
Cdd:PRK12771 232 AQLGKrLPIPGEDAAGVLDAVDFLR----------------AVGEGEPPFL-GKRVVVIgggnTAMDaartarrlgaeev 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 312 RIV--------PAMDAEVSKNLRlilerKGMTILTGTKLQEIIEENG--------QLRIKVEGKDN-----------IIA 364
Cdd:PRK12771 295 TIVyrrtredmPAHDEEIEEALR-----EGVEINWLRTPVEIEGDENgatglrviTVEKMELDEDGrpspvtgeeetLEA 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 365 SKALLSIGRMPDLEGIGEV-EFELDRGCIKVNE-YMETSVPGIYAPGDI-----NGTKMLAHA--------AFRMGEVSA 429
Cdd:PRK12771 370 DLVVLAIGQDIDSAGLESVpGVEVGRGVVQVDPnFMMTGRPGVFAGGDMvpgprTVTTAIGHGkkaarnidAFLGGEPYE 449
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 447085691 430 ENALKGNHAVAKLNL-----TPAAIYTLPEVAAV---------GLTEEQAR 466
Cdd:PRK12771 450 HRPKREIVKFDKLNLwyftdAPRAQRPELDADERvgdfdevlgGLTEEEAR 500
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
112-144 |
1.08e-03 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 41.46 E-value: 1.08e-03
10 20 30
....*....|....*....|....*....|...
gi 447085691 112 FDIVVIGGGPAGYVAAIKAAQLGGKVALVEKSE 144
Cdd:COG0654 4 TDVLIVGGGPAGLALALALARAGIRVTVVERAP 36
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
4-104 |
1.31e-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: 41.40 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447085691 4 EVIMPKAGvDMTEGQIVQWNKKVGEFVKEGEILLEIMTDKVSMELEAEEDGYLIAILKGDGETVPVTEVIGYLGEERENI 83
Cdd:TIGR01348 118 EVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGSTP 196
|
90 100
....*....|....*....|.
gi 447085691 84 PTAgsASPEASPVPVASTSND 104
Cdd:TIGR01348 197 ATA--PAPASAQPAAQSPAAT 215
|
|
| Ubi-OHases |
TIGR01988 |
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a ... |
113-146 |
1.45e-03 |
|
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a family of FAD-dependent hydroxylases (monooxygenases) which are all believed to act in the aerobic ubiquinone biosynthesis pathway. A separate set of hydroxylases, as yet undiscovered, are believed to be active under anaerobic conditions. In E. coli three enzyme activities have been described, UbiB (which acts first at position 6, see TIGR01982), UbiH (which acts at position 4) and UbiF (which acts at position 5). UbiH and UbiF are similar to one another and form the basis of this subfamily. Interestingly, E. coli contains another hydroxylase gene, called visC, that is highly similar to UbiF, adjacent to UbiH and, when mutated, results in a phenotype similar to that of UbiH (which has also been named visB). Several other species appear to have three homologs in this family, although they assort themselves differently on phylogenetic trees (e.g. Xylella and Mesorhizobium) making it difficult to ascribe a specific activity to each one. Eukaryotes appear to have only a single homolog in this subfamily (COQ6) which complements UbiH, but also possess a non-orthologous gene, COQ7 which complements UbiF. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 273913 [Multi-domain] Cd Length: 385 Bit Score: 41.03 E-value: 1.45e-03
10 20 30
....*....|....*....|....*....|....
gi 447085691 113 DIVVIGGGPAGYVAAIKAAQLGGKVALVEKSELG 146
Cdd:TIGR01988 1 DIVIVGGGMVGLALALALARSGLKVALIEATPLP 34
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
116-149 |
1.50e-03 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 37.13 E-value: 1.50e-03
10 20 30
....*....|....*....|....*....|....*
gi 447085691 116 VIGGGPAGYVAAIKAAQLGGKVALVEK-SELGGTC 149
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKrDRLGGNA 35
|
|
| Trp_halogenase |
pfam04820 |
Tryptophan halogenase; Tryptophan halogenase catalyzes the chlorination of tryptophan to form ... |
113-163 |
1.56e-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: 41.16 E-value: 1.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 447085691 113 DIVVIGGGPAGYVAAIK-AAQLGGKVA--LVEKSELGGTCLNRGCIPTKTYLHN 163
Cdd:pfam04820 1 KIVIVGGGTAGWMAAAAlARALKGGLDvtLVESEEIGTVGVGEATIPSIRTFNR 54
|
|
| PRK06481 |
PRK06481 |
flavocytochrome c; |
88-147 |
1.80e-03 |
|
flavocytochrome c;
Pssm-ID: 180584 [Multi-domain] Cd Length: 506 Bit Score: 40.97 E-value: 1.80e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447085691 88 SASPEASPVPVASTSNDDGKSD-----DAFDIVVIGGGPAGYVAAIKAAQLGGKVALVEKSELGG 147
Cdd:PRK06481 33 SSSKESEKTEVTSGASKTSYTDpselkDKYDIVIVGAGGAGMSAAIEAKDAGMNPVILEKMPVAG 97
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
114-147 |
3.35e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 40.26 E-value: 3.35e-03
10 20 30
....*....|....*....|....*....|....*
gi 447085691 114 IVVIGGGPAGYVAAIKAAQLGGKVALVEKSE-LGG 147
Cdd:PRK07233 2 IAIVGGGIAGLAAAYRLAKRGHEVTVFEADDqLGG 36
|
|
| PRK12834 |
PRK12834 |
putative FAD-binding dehydrogenase; Reviewed |
113-147 |
3.55e-03 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 183782 [Multi-domain] Cd Length: 549 Bit Score: 40.27 E-value: 3.55e-03
10 20 30
....*....|....*....|....*....|....*...
gi 447085691 113 DIVVIGGGPAGYVAAIKAAQLGGKVALVEK---SELGG 147
Cdd:PRK12834 6 DVIVVGAGLAGLVAAAELADAGKRVLLLDQeneANLGG 43
|
|
| PTZ00306 |
PTZ00306 |
NADH-dependent fumarate reductase; Provisional |
114-147 |
3.58e-03 |
|
NADH-dependent fumarate reductase; Provisional
Pssm-ID: 140327 [Multi-domain] Cd Length: 1167 Bit Score: 40.53 E-value: 3.58e-03
10 20 30
....*....|....*....|....*....|....*
gi 447085691 114 IVVIGGGPAGYVAAIKAAQLGGKVALVEK-SELGG 147
Cdd:PTZ00306 412 VIVVGGGLAGCSAAIEAASCGAQVILLEKeAKLGG 446
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
113-147 |
6.28e-03 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 39.12 E-value: 6.28e-03
10 20 30
....*....|....*....|....*....|....*
gi 447085691 113 DIVVIGGGPAGYVAAIKAAQLGGKVALVEKSELGG 147
Cdd:COG0665 4 DVVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGS 38
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
113-147 |
7.04e-03 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 38.92 E-value: 7.04e-03
10 20 30
....*....|....*....|....*....|....*
gi 447085691 113 DIVVIGGGPAGYVAAIKAAQLGGKVALVEKSELGG 147
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPG 35
|
|
| PRK08849 |
PRK08849 |
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional |
112-144 |
7.33e-03 |
|
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
Pssm-ID: 181564 [Multi-domain] Cd Length: 384 Bit Score: 38.98 E-value: 7.33e-03
10 20 30
....*....|....*....|....*....|...
gi 447085691 112 FDIVVIGGGPAGYVAAIKAAQLGGKVALVEKSE 144
Cdd:PRK08849 4 YDIAVVGGGMVGAATALGFAKQGRSVAVIEGGE 36
|
|
| MnmG |
COG0445 |
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ... |
112-140 |
8.01e-03 |
|
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440214 [Multi-domain] Cd Length: 626 Bit Score: 39.22 E-value: 8.01e-03
10 20
....*....|....*....|....*....
gi 447085691 112 FDIVVIGGGPAGYVAAIKAAQLGGKVALV 140
Cdd:COG0445 7 YDVIVVGGGHAGCEAALAAARMGAKTLLL 35
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
110-147 |
8.16e-03 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 38.71 E-value: 8.16e-03
10 20 30
....*....|....*....|....*....|....*....
gi 447085691 110 DAFDIVVIGGGPAGYVAAIKAAQLGGKVALVEKS-ELGG 147
Cdd:COG3380 2 SMPDIAIIGAGIAGLAAARALQDAGHEVTVFEKSrGVGG 40
|
|
| PLN02697 |
PLN02697 |
lycopene epsilon cyclase |
109-140 |
8.37e-03 |
|
lycopene epsilon cyclase
Pssm-ID: 215375 [Multi-domain] Cd Length: 529 Bit Score: 39.03 E-value: 8.37e-03
10 20 30
....*....|....*....|....*....|..
gi 447085691 109 DDAFDIVVIGGGPAGYVAAIKAAQLGGKVALV 140
Cdd:PLN02697 106 DGTLDLVVIGCGPAGLALAAESAKLGLNVGLI 137
|
|
| |
