|
Name |
Accession |
Description |
Interval |
E-value |
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
4-461 |
0e+00 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 583.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 4 EIKTQVVVLGAGPAGYSAAFRCADLGLETVLVERySTLGGVCLNVGCIPSKALLHVAKVIEEAKALAEHGIVFGEPKTDI 83
Cdd:COG1249 1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEK-GRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISAGAPSVDW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 84 DKVRLWKEKVITQLTGGLAGMAKGRKVNVVNGVGKFTGANTLEVEGEngkTVINFDNAIIAAGSRPIQLPFIPHDDPRVW 163
Cdd:COG1249 80 AALMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVTGG---ETLTADHIVIATGSRPRVPPIPGLDEVRVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 164 DSTDALALTTVPERLLVMGGGIIGLEMGTVYHALGSQIDVVEMFDQVIPAADKDVVKVFTKRISKQ-FNLMLETKVTAVE 242
Cdd:COG1249 157 TSDEALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEgIDILTGAKVTSVE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 243 AKEDGIYVTMEGKKAPSEpQRYDAVLVAIGRVPNGKLLDAGKAGVEVDDRGFIHVDKQLRTNVPHIFAIGDIVGQPMLAH 322
Cdd:COG1249 237 KTGDGVTVTLEDGGGEEA-VEADKVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRTSVPGIYAIGDVTGGPQLAH 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 323 KGVHEGHVAAEVIAGKK-HYFDPKVIPSIAYTEPEVAWVGVTEKEAKEKGISFETATFPWAASGRAIASDCADGMTKLIF 401
Cdd:COG1249 316 VASAEGRVAAENILGKKpRPVDYRAIPSVVFTDPEIASVGLTEEEAREAGIDVKVGKFPFAANGRALALGETEGFVKLIA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 402 DKETHRIIGGAIVGANGGELLGEIGLAIEMGCDAEDIALTIHAHPTLHESVGLAAEIYEG 461
Cdd:COG1249 396 DAETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAALALLG 455
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
9-457 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 518.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 9 VVVLGAGPAGYSAAFRCADLGLETVLVERySTLGGVCLNVGCIPSKALLHVAKVIEEAKALAEHGIVFGEPKTDIDKVRL 88
Cdd:PRK06416 7 VIVIGAGPGGYVAAIRAAQLGLKVAIVEK-EKLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIKAENVGIDFKKVQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 89 WKEKVITQLTGGLAGMAKGRKVNVVNGVGKFTGANTLEVEGENGKTVINFDNAIIAAGSRPIQLPFIPHDDPRVWDSTDA 168
Cdd:PRK06416 86 WKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDGEQTYTAKNIILATGSRPRELPGIEIDGRVIWTSDEA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 169 LALTTVPERLLVMGGGIIGLEMGTVYHALGSQIDVVEMFDQVIPAADKDVVKVFTKRISKQ-FNLMLETKVTAVEAKEDG 247
Cdd:PRK06416 166 LNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPGEDKEISKLAERALKKRgIKIKTGAKAKKVEQTDDG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 248 IYVTMEgKKAPSEPQRYDAVLVAIGRVPNGKLLDAGKAGVEVDdRGFIHVDKQLRTNVPHIFAIGDIVGQPMLAHKGVHE 327
Cdd:PRK06416 246 VTVTLE-DGGKEETLEADYVLVAVGRRPNTENLGLEELGVKTD-RGFIEVDEQLRTNVPNIYAIGDIVGGPMLAHKASAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 328 GHVAAEVIAGKKHYFDPKVIPSIAYTEPEVAWVGVTEKEAKEKGISFETATFPWAASGRAIASDCADGMTKLIFDKETHR 407
Cdd:PRK06416 324 GIIAAEAIAGNPHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFDVKVVKFPFAGNGKALALGETDGFVKLIFDKKDGE 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1812594828 408 IIGGAIVGANGGELLGEIGLAIEMGCDAEDIALTIHAHPTLHESVGLAAE 457
Cdd:PRK06416 404 VLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEALGEAAL 453
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
9-457 |
3.42e-172 |
|
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.
Pssm-ID: 273568 [Multi-domain] Cd Length: 460 Bit Score: 491.77 E-value: 3.42e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 9 VVVLGAGPAGYSAAFRCADLGLETVLVERySTLGGVCLNVGCIPSKALLHVAKVIEEAKALAEHGIVFGEPKTDIDKVRL 88
Cdd:TIGR01350 4 VIVIGGGPGGYVAAIRAAQLGLKVALVEK-EYLGGTCLNVGCIPTKALLHSAEVYDEIKHAKDLGIEVENVSVDWEKMQK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 89 WKEKVITQLTGGLAGMAKGRKVNVVNGVGKFTGANTLEVEGENGKTVINFDNAIIAAGSRPIQLPF-IPHDDPRVWDSTD 167
Cdd:TIGR01350 83 RKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGENGEETLEAKNIIIATGSRPRSLPGpFDFDGKVVITSTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 168 ALALTTVPERLLVMGGGIIGLEMGTVYHALGSQIDVVEMFDQVIPAADKDVVKVFTKRISKQ-FNLMLETKVTAVEAKED 246
Cdd:TIGR01350 163 ALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKgVKILTNTKVTAVEKNDD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 247 GIYVTMEGKKAPSEpqRYDAVLVAIGRVPNGKLLDAGKAGVEVDDRGFIHVDKQLRTNVPHIFAIGDIVGQPMLAHKGVH 326
Cdd:TIGR01350 243 QVTYENKGGETETL--TGEKVLVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDVIGGPMLAHVASH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 327 EGHVAAEVIAGK-KHYFDPKVIPSIAYTEPEVAWVGVTEKEAKEKGISFETATFPWAASGRAIASDCADGMTKLIFDKET 405
Cdd:TIGR01350 321 EGIVAAENIAGKePAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGYDVKIGKFPFAANGKALALGETDGFVKIIADKKT 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1812594828 406 HRIIGGAIVGANGGELLGEIGLAIEMGCDAEDIALTIHAHPTLHESVGLAAE 457
Cdd:TIGR01350 401 GEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEAIKEAAL 452
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
9-456 |
5.77e-157 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 453.61 E-value: 5.77e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 9 VVVLGAGPAGYSAAFRCADLGLETVLVERYST------LGGVCLNVGCIPSKALLHVAKVIEEAK-ALAEHGIVFGEPKT 81
Cdd:PRK06327 7 VVVIGAGPGGYVAAIRAAQLGLKVACIEAWKNpkgkpaLGGTCLNVGCIPSKALLASSEEFENAGhHFADHGIHVDGVKI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 82 DIDKVRLWKEKVITQLTGGLAGMAKGRKVNVVNGVGKFTGA----NTLEVEGEnGKTVINFDNAIIAAGSRPIQLPFIPH 157
Cdd:PRK06327 87 DVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVGKtdagYEIKVTGE-DETVITAKHVIIATGSEPRHLPGVPF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 158 DDPRVWDSTDALALTTVPERLLVMGGGIIGLEMGTVYHALGSQIDVVEMFDQVIPAADKDVVKVFTKRISKQ-FNLMLET 236
Cdd:PRK06327 166 DNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAAADEQVAKEAAKAFTKQgLDIHLGV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 237 KVTAVEAKEDGIYVTMEGKKAPSEPQRYDAVLVAIGRVPNGKLLDAGKAGVEVDDRGFIHVDKQLRTNVPHIFAIGDIVG 316
Cdd:PRK06327 246 KIGEIKTGGKGVSVAYTDADGEAQTLEVDKLIVSIGRVPNTDGLGLEAVGLKLDERGFIPVDDHCRTNVPNVYAIGDVVR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 317 QPMLAHKGVHEGHVAAEVIAGKKHYFDPKVIPSIAYTEPEVAWVGVTEKEAKEKGISFETATFPWAASGRAIASDCADGM 396
Cdd:PRK06327 326 GPMLAHKAEEEGVAVAERIAGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLKAEGVEYKAGKFPFMANGRALAMGEPDGF 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 397 TKLIFDKETHRIIGGAIVGANGGELLGEIGLAIEMGCDAEDIALTIHAHPTLHESVGLAA 456
Cdd:PRK06327 406 VKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEVWHEAA 465
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
5-456 |
4.24e-152 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 440.77 E-value: 4.24e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 5 IKTQVVVLGAGPAGYSAAFRCADLGLETVLVERySTLGGVCLNVGCIPSKALLHVAKVIEEAKALAEHGIVFGEPKTDID 84
Cdd:PRK06292 2 EKYDVIVIGAGPAGYVAARRAAKLGKKVALIEK-GPLGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHADGPKIDFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 85 KVRLWKEKVITQLTGG-LAGMAKGRKVNVVNGVGKFTGANTLEVEGEngktVINFDNAIIAAGSRPIQLP-FIPHDDPRV 162
Cdd:PRK06292 81 KVMARVRRERDRFVGGvVEGLEKKPKIDKIKGTARFVDPNTVEVNGE----RIEAKNIVIATGSRVPPIPgVWLILGDRL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 163 WDSTDALALTTVPERLLVMGGGIIGLEMGTVYHALGSQIDVVEMFDQVIPAADKDVVKVFTKRISKQFNLMLETKVTAVE 242
Cdd:PRK06292 157 LTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILSKEFKIKLGAKVTSVE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 243 aKEDGIYVTMEGKKAPSEPQRYDAVLVAIGRVPNGKLLDAGKAGVEVDDRGFIHVDKQLRTNVPHIFAIGDIVGQPMLAH 322
Cdd:PRK06292 237 -KSGDEKVEELEKGGKTETIEADYVLVATGRRPNTDGLGLENTGIELDERGRPVVDEHTQTSVPGIYAAGDVNGKPPLLH 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 323 KGVHEGHVAAEVIAG-KKHYFDPKVIPSIAYTEPEVAWVGVTEKEAKEKGISFETATFPWAASGRAIASDCADGMTKLIF 401
Cdd:PRK06292 316 EAADEGRIAAENAAGdVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEVPFEAQGRARVMGKNDGFVKVYA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1812594828 402 DKETHRIIGGAIVGANGGELLGEIGLAIEMGCDAEDIALTIHAHPTLHESVGLAA 456
Cdd:PRK06292 396 DKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRTAL 450
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
10-460 |
6.46e-105 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 320.23 E-value: 6.46e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 10 VVLGAGPAGYSAAFRCADLGLETVLVERySTLGGVCLNVGCIPSKALLHVAKVIEEAKALAEHGIVFGEPKT-DIDKVRL 88
Cdd:PRK06370 9 IVIGAGQAGPPLAARAAGLGMKVALIER-GLLGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGGPVSvDFKAVMA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 89 WKEKVITQLTGGLA-GMAKGRKVNVVNGVGKFTGANTLEVEGEngktVINFDNAIIAAGSRPiQLPFIPH-DDPRVWDST 166
Cdd:PRK06370 88 RKRRIRARSRHGSEqWLRGLEGVDVFRGHARFESPNTVRVGGE----TLRAKRIFINTGARA-AIPPIPGlDEVGYLTNE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 167 DALALTTVPERLLVMGGGIIGLEMGTVYHALGSQIDVVEMFDQVIPAADKDVVKVFTKRISKQ-FNLMLETKVTAVEAKE 245
Cdd:PRK06370 163 TIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILEREgIDVRLNAECIRVERDG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 246 DGIYVTMEGKKAPSEpQRYDAVLVAIGRVPNGKLLDAGKAGVEVDDRGFIHVDKQLRTNVPHIFAIGDIVGQPMLAHKGV 325
Cdd:PRK06370 243 DGIAVGLDCNGGAPE-ITGSHILVAVGRVPNTDDLGLEAAGVETDARGYIKVDDQLRTTNPGIYAAGDCNGRGAFTHTAY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 326 HEGHVAAEVIAGKKHY-FDPKVIPSIAYTEPEVAWVGVTEKEAKEKGISFETATFPWAASGRAIASDCADGMTKLIFDKE 404
Cdd:PRK06370 322 NDARIVAANLLDGGRRkVSDRIVPYATYTDPPLARVGMTEAEARKSGRRVLVGTRPMTRVGRAVEKGETQGFMKVVVDAD 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1812594828 405 THRIIGGAIVGANGGELLGEIGLAIEMGCDAEDIALTIHAHPTLHESVGLAAEIYE 460
Cdd:PRK06370 402 TDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIPTLAQALR 457
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
9-467 |
1.45e-93 |
|
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: 291.25 E-value: 1.45e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 9 VVVLGAGPAGYSAAFRCADLGLETVLVERySTLGGVCLNVGCIPSKALLHVAKVIEEAKAlAEHGIVFGEPKTDIDKVRL 88
Cdd:TIGR02053 3 LVIIGSGAAAFAAAIKAAELGASVAMVER-GPLGGTCVNVGCVPSKMLLRAAEVAHYARK-PPFGGLAATVAVDFGELLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 89 WKEKVITQL-TGGLAGMAKGRKVNVVNGVGKFTGANTLEVEGenGKTVINFDNAIIAAGSRPiQLPFIPH-DDPRVWDST 166
Cdd:TIGR02053 81 GKREVVEELrHEKYEDVLSSYGVDYLRGRARFKDPKTVKVDL--GREVRGAKRFLIATGARP-AIPPIPGlKEAGYLTSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 167 DALALTTVPERLLVMGGGIIGLEMGTVYHALGSQIDVVEMFDQVIPAADKDVVKVFTKRISKQ-FNLMLETKVTAVEAKE 245
Cdd:TIGR02053 158 EALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSDRLLPREEPEISAAVEEALAEEgIEVVTSAQVKAVSVRG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 246 DGIYVTMEGKKAPSEpQRYDAVLVAIGRVPNGKLLDAGKAGVEVDDRGFIHVDKQLRTNVPHIFAIGDIVGQPMLAHKGV 325
Cdd:TIGR02053 238 GGKIITVEKPGGQGE-VEADELLVATGRRPNTDGLGLEKAGVKLDERGGILVDETLRTSNPGIYAAGDVTGGLQLEYVAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 326 HEGHVAAE-VIAGKKHYFDPKVIPSIAYTEPEVAWVGVTEKEAKEKGISFETATFPWAASGRAIASDCADGMTKLIFDKE 404
Cdd:TIGR02053 317 KEGVVAAEnALGGANAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNVPRARINRDTRGFIKLVAEPG 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1812594828 405 THRIIGGAIVGANGGELLGEIGLAIEMGCDAEDIALTIHAHPTLHESVGLAAEIYEGSITDLP 467
Cdd:TIGR02053 397 TGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGLKLAAQTFYRDVSKLS 459
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
9-433 |
5.05e-90 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 281.66 E-value: 5.05e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 9 VVVLGAGPAGYSAAFRCADLGLETVLVERYSTLGGVCLNVGCIPSKALLHVAKVIEEAKA---LAEHGIVfgePKTDIDK 85
Cdd:PRK05249 8 LVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGGGCTHTGTIPSKALREAVLRLIGFNQnplYSSYRVK---LRITFAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 86 VRLWKEKVITQLTGGLAGMAKGRKVNVVNGVGKFTGANTLEVEGENG-KTVINFDNAIIAAGSRPIQLPFIPHDDPRVWD 164
Cdd:PRK05249 85 LLARADHVINKQVEVRRGQYERNRVDLIQGRARFVDPHTVEVECPDGeVETLTADKIVIATGSRPYRPPDVDFDHPRIYD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 165 STDALALTTVPERLLVMGGGIIGLEMGTVYHALGSQIDVVEMFDQVIPAADKDVVKVFTKRISKQ-FNLMLETKVTAVEA 243
Cdd:PRK05249 165 SDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSFLDDEISDALSYHLRDSgVTIRHNEEVEKVEG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 244 KEDGIYVTME-GKKAPSepqryDAVLVAIGRVPNGKLLDAGKAGVEVDDRGFIHVDKQLRTNVPHIFAIGDIVGQPMLAH 322
Cdd:PRK05249 245 GDDGVIVHLKsGKKIKA-----DCLLYANGRTGNTDGLNLENAGLEADSRGQLKVNENYQTAVPHIYAVGDVIGFPSLAS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 323 KGVHEGHVAAEVIAGKKHYFDPKVIPSIAYTEPEVAWVGVTEKEAKEKGISFEtatfpwaaSGRA---------IASDCa 393
Cdd:PRK05249 320 ASMDQGRIAAQHAVGEATAHLIEDIPTGIYTIPEISSVGKTEQELTAAKVPYE--------VGRArfkelaraqIAGDN- 390
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1812594828 394 DGMTKLIFDKETHRIIGGAIVGANGGELLgEIGLAIeMGC 433
Cdd:PRK05249 391 VGMLKILFHRETLEILGVHCFGERATEII-HIGQAI-MEQ 428
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
29-452 |
1.70e-72 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 236.00 E-value: 1.70e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 29 GLETVLVERySTLGGVCLNVGCIPSKALLHVAKVIEEAKALAEHGIVFGEPKTDIDKVRlwkEKVITQL----TGGLAGM 104
Cdd:PRK07846 22 DKRIAIVEK-GTFGGTCLNVGCIPTKMFVYAADVARTIREAARLGVDAELDGVRWPDIV---SRVFGRIdpiaAGGEEYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 105 AKGR-KVNVVNGVGKFTGANTLEVEGengKTVINFDNAIIAAGSRPIQLPFIPHDDPRVWDSTDALALTTVPERLLVMGG 183
Cdd:PRK07846 98 GRDTpNIDVYRGHARFIGPKTLRTGD---GEEITADQVVIAAGSRPVIPPVIADSGVRYHTSDTIMRLPELPESLVIVGG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 184 GIIGLEMGTVYHALGSQIDVVEMFDQVIPAADKDVVKVFTKRISKQFNLMLETKVTAVEAKEDGIYVTMEGkkapSEPQR 263
Cdd:PRK07846 175 GFIAAEFAHVFSALGVRVTVVNRSGRLLRHLDDDISERFTELASKRWDVRLGRNVVGVSQDGSGVTLRLDD----GSTVE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 264 YDAVLVAIGRVPNGKLLDAGKAGVEVDDRGFIHVDKQLRTNVPHIFAIGDIVGQPMLAHKGVHEGHV-------AAEVIA 336
Cdd:PRK07846 251 ADVLLVATGRVPNGDLLDAAAAGVDVDEDGRVVVDEYQRTSAEGVFALGDVSSPYQLKHVANHEARVvqhnllhPDDLIA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 337 gkkhyFDPKVIPSIAYTEPEVAWVGVTEKEAKEKGISFETATFPWA--ASGRAIASDcaDGMTKLIFDKETHRIIGGAIV 414
Cdd:PRK07846 331 -----SDHRFVPAAVFTHPQIASVGLTENEARAAGLDITVKVQNYGdvAYGWAMEDT--TGFVKLIADRDTGRLLGAHII 403
|
410 420 430
....*....|....*....|....*....|....*....
gi 1812594828 415 GANGGELLGEIGLAIEMGCDAEDIALTIH-AHPTLHESV 452
Cdd:PRK07846 404 GPQASTLIQPLIQAMSFGLDAREMARGQYwIHPALPEVV 442
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
9-450 |
4.45e-69 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 226.94 E-value: 4.45e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 9 VVVLGAGPAGYSAAFRCADLGLETVLVERYSTL-GGVCLNVGCIPSKALLHVAkvieeakalaEHGIVFgepktdiDKVR 87
Cdd:PRK07251 6 LIVIGFGKAGKTLAAKLASAGKKVALVEESKAMyGGTCINIGCIPTKTLLVAA----------EKNLSF-------EQVM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 88 LWKEKVITQLTGGLAGMAKGRKVNVVNGVGKFTGANTLEVEGENGKTVINFDNAIIAAGSRPIQLPfIP--HDDPRVWDS 165
Cdd:PRK07251 69 ATKNTVTSRLRGKNYAMLAGSGVDLYDAEAHFVSNKVIEVQAGDEKIELTAETIVINTGAVSNVLP-IPglADSKHVYDS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 166 TDALALTTVPERLLVMGGGIIGLEMGTVYHALGSQIDVVEMFDQVIPAADKDVVKVFTKRISKQ-FNLMLETKVTAVEAK 244
Cdd:PRK07251 148 TGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYMEEDgITFLLNAHTTEVKND 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 245 EDGIYVTMEGKKApsepqRYDAVLVAIGRVPNGKLLDAGKAGVEVDDRGFIHVDKQLRTNVPHIFAIGDIVGQPMLAHKG 324
Cdd:PRK07251 228 GDQVLVVTEDETY-----RFDALLYATGRKPNTEPLGLENTDIELTERGAIKVDDYCQTSVPGVFAVGDVNGGPQFTYIS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 325 VHEGHVAAEVIAGKKHYF--DPKVIPSIAYTEPEVAWVGVTEKEAKEKGISFETATFPWAASGRAIASDCADGMTKLIFD 402
Cdd:PRK07251 303 LDDFRIVFGYLTGDGSYTleDRGNVPTTMFITPPLSQVGLTEKEAKEAGLPYAVKELLVAAMPRAHVNNDLRGAFKVVVN 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1812594828 403 KETHRIIGGAIVGANGGELLGEIGLAIEMGCDAEDIALTIHAHPTLHE 450
Cdd:PRK07251 383 TETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAE 430
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
7-328 |
5.95e-69 |
|
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: 222.19 E-value: 5.95e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 7 TQVVVLGAGPAGYSAAFRCADLGLETVLVErystLGGVCLNVGCIPSKALLHVAKVIEEAKALAEhgivfgepktdidkV 86
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIE----DEGTCPYGGCVLSKALLGAAEAPEIASLWAD--------------L 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 87 RLWKEKVITQLTGGLAGMAKGRKVNVVNGVGKFTGANTLEVEGENgktvINFDNAIIAAGSRPIqLPFIP------HDDP 160
Cdd:pfam07992 63 YKRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELVDGDGET----ITYDRLVIATGARPR-LPPIPgvelnvGFLV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 161 RVWDSTDALALTTVPERLLVMGGGIIGLEMGTVYHALGSQIDVVEMFDQVIPAADKDVVKVFTKRISKQ-FNLMLETKVT 239
Cdd:pfam07992 138 RTLDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNgVEVRLGTSVK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 240 AVEAKEDGI-YVTMEGKKAPsepqrYDAVLVAIGRVPNGKLLDAgkAGVEVDDRGFIHVDKQLRTNVPHIFAIGDI-VGQ 317
Cdd:pfam07992 218 EIIGDGDGVeVILKDGTEID-----ADLVVVAIGRRPNTELLEA--AGLELDERGGIVVDEYLRTSVPGIYAAGDCrVGG 290
|
330
....*....|.
gi 1812594828 318 PMLAHKGVHEG 328
Cdd:pfam07992 291 PELAQNAVAQG 301
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
8-466 |
1.17e-66 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 223.87 E-value: 1.17e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 8 QVVVLGAGPAGYSAAFRCADLGLETVLVERySTLGGVCLNVGCIPSKALLHVAKVieeAKALAEH----GIVFGEPKTD- 82
Cdd:PRK13748 100 HVAVIGSGGAAMAAALKAVEQGARVTLIER-GTIGGTCVNVGCVPSKIMIRAAHI---AHLRRESpfdgGIAATVPTIDr 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 83 ----------IDKVRLWKEKVItqLTGGLAgmakgrkVNVVNGVGKFTGANTLEVE-GENGKTVINFDNAIIAAGSRPiQ 151
Cdd:PRK13748 176 srllaqqqarVDELRHAKYEGI--LDGNPA-------ITVLHGEARFKDDQTLIVRlNDGGERVVAFDRCLIATGASP-A 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 152 LPFIP--HDDPrVWDSTDALALTTVPERLLVMGGGIIGLEMGTVYHALGSQIDVV---EMFDQVIPAADKDVVKVFTKri 226
Cdd:PRK13748 246 VPPIPglKETP-YWTSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILarsTLFFREDPAIGEAVTAAFRA-- 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 227 sKQFNLMLETKVTAVeAKEDGIYV--TMEGKKapsepqRYDAVLVAIGRVPNGKLLDAGKAGVEVDDRGFIHVDKQLRTN 304
Cdd:PRK13748 323 -EGIEVLEHTQASQV-AHVDGEFVltTGHGEL------RADKLLVATGRAPNTRSLALDAAGVTVNAQGAIVIDQGMRTS 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 305 VPHIFAIGDIVGQPMLAHKGVHEGHVAAEVIAGKKHYFDPKVIPSIAYTEPEVAWVGVTEKEAKEKGISFETATFPWAAS 384
Cdd:PRK13748 395 VPHIYAAGDCTDQPQFVYVAAAAGTRAAINMTGGDAALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRTLTLDNV 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 385 GRAIASDCADGMTKLIFDKETHRIIGGAIVGANGGELLGEIGLAIEMGCDAEDIALTIHAHPTLHESVGLAAEIYEGSIT 464
Cdd:PRK13748 475 PRALANFDTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAALAIRNRMTVQELADQLFPYLTMVEGLKLAAQTFNKDVK 554
|
..
gi 1812594828 465 DL 466
Cdd:PRK13748 555 QL 556
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
9-455 |
1.40e-66 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 225.56 E-value: 1.40e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 9 VVVLGAGPAGYSAAFRCADLGLETVLVE-RYSTLGGVCLNVGCIPSKALLHVAKVIEEAKALAE---HGI---------- 74
Cdd:PTZ00153 119 VGIIGCGVGGHAAAINAMERGLKVIIFTgDDDSIGGTCVNVGCIPSKALLYATGKYRELKNLAKlytYGIytnafkngkn 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 75 --------VFGEPKTDIDKVRLWKEKVITQLTGGLAGMAKGRKVN-------VVNGVGKFTGANTleVEGENGKTVINFD 139
Cdd:PTZ00153 199 dpvernqlVADTVQIDITKLKEYTQSVIDKLRGGIENGLKSKKFCknsehvqVIYERGHIVDKNT--IKSEKSGKEFKVK 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 140 NAIIAAGSrpiqLPFIPH----DDPRVWDSTDALALTTVPERLLVMGGGIIGLEMGTVYHALGSQIDVVEMFDQVIPAAD 215
Cdd:PTZ00153 277 NIIIATGS----TPNIPDnievDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSPQLLPLLD 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 216 KDVVKVFTKRI--SKQFNLMLETKVTAVEAKEDGIYVTM------------EGKKAPSEPQRY-DAVLVAIGRVPNGKLL 280
Cdd:PTZ00153 353 ADVAKYFERVFlkSKPVRVHLNTLIEYVRAGKGNQPVIIghserqtgesdgPKKNMNDIKETYvDSCLVATGRKPNTNNL 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 281 DAGKAGVEVdDRGFIHVDKQLRTN------VPHIFAIGDIVGQPMLAHKGVHEGHVAAEVIAGKK---HYFDP------- 344
Cdd:PTZ00153 433 GLDKLKIQM-KRGFVSVDEHLRVLredqevYDNIFCIGDANGKQMLAHTASHQALKVVDWIEGKGkenVNINVenwaskp 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 345 ---KVIPSIAYTEPEVAWVGVTEKEAKE--------KGISFETA----------TFPWAAS------GRAIASDCADGMT 397
Cdd:PTZ00153 512 iiyKNIPSVCYTTPELAFIGLTEKEAKElyppdnvgVEISFYKAnskvlcenniSFPNNSKnnsynkGKYNTVDNTEGMV 591
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1812594828 398 KLIFDKETHRIIGGAIVGANGGELLGEIGLAIEMGCDAEDIALTIHAHPTLHESVGLA 455
Cdd:PTZ00153 592 KIVYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDAA 649
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
11-447 |
1.03e-65 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 218.10 E-value: 1.03e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 11 VLGAGPAGYSAAFRCADLGLETVLVERYStLGGVCLNVGCIPSKALLHVAKVIEEAKALAE-HGIVFGEPKTDIDKVRLW 89
Cdd:PRK06116 9 VIGGGSGGIASANRAAMYGAKVALIEAKR-LGGTCVNVGCVPKKLMWYGAQIAEAFHDYAPgYGFDVTENKFDWAKLIAN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 90 KEKVITQLTGGLAGMAKGRKVNVVNGVGKFTGANTLEVEGENgktvINFDNAIIAAGSRPIqLPFIP---HddprVWDST 166
Cdd:PRK06116 88 RDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNGER----YTADHILIATGGRPS-IPDIPgaeY----GITSD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 167 DALALTTVPERLLVMGGGIIGLEMGTVYHALGSQIDVVEMFDQVIPAADKDVVKVFTKRISKQ-FNLMLETKVTAVEAKE 245
Cdd:PRK06116 159 GFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKgIRLHTNAVPKAVEKNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 246 DGIY-VTMEGkkapSEPQRYDAVLVAIGRVPNGKLLDAGKAGVEVDDRGFIHVDKQLRTNVPHIFAIGDIVGQPMLAHKG 324
Cdd:PRK06116 239 DGSLtLTLED----GETLTVDCLIWAIGREPNTDGLGLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGDVTGRVELTPVA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 325 VHEGHVAAEVIAGKKHY--FDPKVIPSIAYTEPEVAWVGVTEKEAKEKG----ISFETATFpwaASGRAIASDCADGMT- 397
Cdd:PRK06116 315 IAAGRRLSERLFNNKPDekLDYSNIPTVVFSHPPIGTVGLTEEEAREQYgednVKVYRSSF---TPMYTALTGHRQPCLm 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1812594828 398 KLIFDKETHRIIGGAIVGANGGELLGEIGLAIEMGCDAEDIALTIHAHPT 447
Cdd:PRK06116 392 KLVVVGKEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPT 441
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
6-452 |
6.54e-59 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 200.24 E-value: 6.54e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 6 KTQVVVLGAGPAGYSAAFRCADLGLETVLVERYSTL-GGVCLNVGCIPSKALLHVAkvieeakalaehgivfgEPKTDID 84
Cdd:PRK08010 3 KYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNAMyGGTCINIGCIPTKTLVHDA-----------------QQHTDFV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 85 KVRLWKEKVITQLTG-GLAGMAKGRKVNVVNGVGKFTGANTLEVEGENGKTVINFDNAIIAAGSRPIqLPFIP--HDDPR 161
Cdd:PRK08010 66 RAIQRKNEVVNFLRNkNFHNLADMPNIDVIDGQAEFINNHSLRVHRPEGNLEIHGEKIFINTGAQTV-VPPIPgiTTTPG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 162 VWDSTDALALTTVPERLLVMGGGIIGLEMGTVYHALGSQIDVVEMFDQVIPAADKDVVKVFTKRISKQ-FNLMLETKVTA 240
Cdd:PRK08010 145 VYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQgVDIILNAHVER 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 241 VEAKEDGIYVtmegkKAPSEPQRYDAVLVAIGRVPNGKLLDAGKAGVEVDDRGFIHVDKQLRTNVPHIFAIGDIVGQPML 320
Cdd:PRK08010 225 ISHHENQVQV-----HSEHAQLAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKYLHTTADNIWAMGDVTGGLQF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 321 AHKGVHEGHVAAEVI--AGKKHYFDPKVIPSIAYTEPEVAWVGVTEKEAKEKGISFETATFPWAASGRAIASDCADGMTK 398
Cdd:PRK08010 300 TYISLDDYRIVRDELlgEGKRSTDDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDTRGVLK 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1812594828 399 LIFDKETHRIIGGAIVGANGGELLGEIGLAIEMGCDAEDIALTIHAHPTLHESV 452
Cdd:PRK08010 380 AIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESL 433
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
7-456 |
2.77e-58 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 198.93 E-value: 2.77e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 7 TQVVVLGAGPAGYSAAFRCADLGLETVLVERySTLGGVCLNVGCIPSKALLHVAKVIEEAKALAEHGIVF---GEPKTDI 83
Cdd:PRK07845 2 TRIVIIGGGPGGYEAALVAAQLGADVTVIER-DGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRFiddGEARVDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 84 DKV--RLwKEKVITQ---LTGGLAGMAkgrkVNVVNGVGKFT----GANTLEVEGENGKT-VINFDNAIIAAGSRPIQLP 153
Cdd:PRK07845 81 PAVnaRV-KALAAAQsadIRARLEREG----VRVIAGRGRLIdpglGPHRVKVTTADGGEeTLDADVVLIATGASPRILP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 154 FIPHDDPRVWDSTDALALTTVPERLLVMGGGIIGLEMGTVYHALGSQIDVVEMFDQVIPAADKDVVK----VFTKRiskQ 229
Cdd:PRK07845 156 TAEPDGERILTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPGEDADAAEvleeVFARR---G 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 230 FNLMLETKVTAVEAKEDGIYVTM------EGKKApsepqrydavLVAIGRVPNGKLLDAGKAGVEVDDRGFIHVDKQLRT 303
Cdd:PRK07845 233 MTVLKRSRAESVERTGDGVVVTLtdgrtvEGSHA----------LMAVGSVPNTAGLGLEEAGVELTPSGHITVDRVSRT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 304 NVPHIFAIGDIVGQPMLAHKGVHEGHVAAEVIAGKK-HYFDPKVIPSIAYTEPEVAWVGVTEKEAKEKGISFETATFPWA 382
Cdd:PRK07845 303 SVPGIYAAGDCTGVLPLASVAAMQGRIAMYHALGEAvSPLRLKTVASNVFTRPEIATVGVSQAAIDSGEVPARTVMLPLA 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1812594828 383 ASGRAIASDCADGMTKLIFDKETHRIIGGAIVGANGGELLGEIGLAIEMGCDAEDIALTIHAHPTLHESVGLAA 456
Cdd:PRK07845 383 TNPRAKMSGLRDGFVKLFCRPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYPSLSGSITEAA 456
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
10-451 |
3.28e-48 |
|
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: 172.73 E-value: 3.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 10 VVLGAGPAGYSAAFRCADLGlETVLVERYST---------LGGVCLNVGCIPSKALLHVAKVIEEAKALAEHGIVFGEP- 79
Cdd:TIGR01438 6 IVIGGGSGGLAAAKEAAAYG-AKVMLLDFVTptplgtrwgIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVEETv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 80 KTDIDKVRLWKEKVITQLTGGLAGMAKGRKVNVVNGVGKFTGANTLEVEGENGK-TVINFDNAIIAAGSRPiQLPFIPHD 158
Cdd:TIGR01438 85 KHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKeKIYSAERFLIATGERP-RYPGIPGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 159 DPRVWDSTDALALTTVPERLLVMGGGIIGLEMGTVYHALGSQIDV------VEMFDQVIPAADKDVVKVFTKRISKQFnl 232
Cdd:TIGR01438 164 KELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVmvrsilLRGFDQDCANKVGEHMEEHGVKFKRQF-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 233 mLETKVTAVEAKedgIYVTMEGKKAPSEpQRYDAVLVAIGRVPNGKLLDAGKAGVEVDDR-GFIHVDKQLRTNVPHIFAI 311
Cdd:TIGR01438 242 -VPIKVEQIEAK---VLVEFTDSTNGIE-EEYDTVLLAIGRDACTRKLNLENVGVKINKKtGKIPADEEEQTNVPYIYAV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 312 GDIV-GQPMLAHKGVHEGHVAAE-VIAGKKHYFDPKVIPSIAYTEPEVAWVGVTEKEAKEK-GIS------FETATFPWA 382
Cdd:TIGR01438 317 GDILeDKPELTPVAIQAGRLLAQrLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAVEKfGEEnvevfhSYFWPLEWT 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 383 ASGRAIASDCadgMTKLIFD-KETHRIIGGAIVGANGGELLGEIGLAIEMGCDAEDIALTIHAHPTLHES 451
Cdd:TIGR01438 397 IPSRDNHNKC---YAKLVCNkKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEV 463
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
9-452 |
8.19e-47 |
|
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: 169.00 E-value: 8.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 9 VVVLGAGPAGYSAAFRCADLGLETVLV---------ERYSTLGGVCLNVGCIPSKALLHVAKVIEEAKALAEHGIVFGEP 79
Cdd:TIGR01423 6 LVVIGAGSGGLEAGWNAATLYKKRVAVvdvqthhgpPFYAALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGWEFDRS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 80 --KTDIDKVRLWKEKVITQLTGGLAGMAKGRK-VNVVNGVGKFTGANTLEV-EGENGKTVI----NFDNAIIAAGSRPiQ 151
Cdd:TIGR01423 86 svKANWKALIAAKNKAVLDINKSYEGMFADTEgLTFFLGWGALEDKNVVLVrESADPKSAVkerlQAEHILLATGSWP-Q 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 152 LPFIPHDDPRVwDSTDALALTTVPERLLVMGGGIIGLEMGTV---YHALGSQIDVVEMFDQVIPAADKDVVKVFTKRISK 228
Cdd:TIGR01423 165 MLGIPGIEHCI-SSNEAFYLDEPPRRVLTVGGGFISVEFAGIfnaYKPRGGKVTLCYRNNMILRGFDSTLRKELTKQLRA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 229 Q-FNLMLETKVTAVEAKEDGI-YVTMEGKKAPSepqrYDAVLVAIGRVPNGKLLDAGKAGVEVDDRGFIHVDKQLRTNVP 306
Cdd:TIGR01423 244 NgINIMTNENPAKVTLNADGSkHVTFESGKTLD----VDVVMMAIGRVPRTQTLQLDKVGVELTKKGAIQVDEFSRTNVP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 307 HIFAIGDIVGQPMLAHKGVHEGHVAAEVIAGKK-HYFDPKVIPSIAYTEPEVAWVGVTEKEAK---EKGISFETATFPWA 382
Cdd:TIGR01423 320 NIYAIGDVTDRVMLTPVAINEGAAFVDTVFGNKpRKTDHTRVASAVFSIPPIGTCGLVEEDAAkkfEKVAVYESSFTPLM 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1812594828 383 --ASGraiaSDCADGMTKLIFDKETHRIIGGAIVGANGGELLGEIGLAIEMGCDAEDIALTIHAHPTLHESV 452
Cdd:TIGR01423 400 hnISG----SKYKKFVAKIVTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAEEL 467
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
11-450 |
3.44e-45 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 164.60 E-value: 3.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 11 VLGAGPAGYSAAFRCADLGLETVLVE---------RYSTLGGVCLNVGCIPSKALLHVAKV---IEEAKalaEHGIVFGE 78
Cdd:PLN02507 30 VIGAGSGGVRAARFSANFGAKVGICElpfhpisseSIGGVGGTCVIRGCVPKKILVYGATFggeFEDAK---NYGWEINE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 79 pKTDIDKVRLWKEKV--ITQLTGGLAGMAKGRKVNVVNGVGKFTGANTLEVEGENGkTVINF--DNAIIAAGSRPiQLPF 154
Cdd:PLN02507 107 -KVDFNWKKLLQKKTdeILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDG-TKLRYtaKHILIATGSRA-QRPN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 155 IPHDDPRVwDSTDALALTTVPERLLVMGGGIIGLEMGTVYHALGSQIDVVEMFDQVIPAADKDVVKVFTKRI-SKQFNLM 233
Cdd:PLN02507 184 IPGKELAI-TSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRAVVARNLeGRGINLH 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 234 LETKVTAVEAKEDGIYVTMEGKkapsEPQRYDAVLVAIGRVPNGKLLDAGKAGVEVDDRGFIHVDKQLRTNVPHIFAIGD 313
Cdd:PLN02507 263 PRTNLTQLTKTEGGIKVITDHG----EEFVADVVLFATGRAPNTKRLNLEAVGVELDKAGAVKVDEYSRTNIPSIWAIGD 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 314 IVGQPMLAHKGVHEGHVAAE-VIAGKKHYFDPKVIPSIAYTEPEVAWVGVTEKEAKEKG---ISFETATF-PW--AASGR 386
Cdd:PLN02507 339 VTNRINLTPVALMEGTCFAKtVFGGQPTKPDYENVACAVFCIPPLSVVGLSEEEAVEQAkgdILVFTSSFnPMknTISGR 418
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1812594828 387 AIASdcadgMTKLIFDKETHRIIGGAIVGANGGELLGEIGLAIEMGCDAEDIALTIHAHPTLHE 450
Cdd:PLN02507 419 QEKT-----VMKLIVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAE 477
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
347-455 |
1.18e-42 |
|
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases.
Pssm-ID: 427019 [Multi-domain] Cd Length: 109 Bit Score: 146.54 E-value: 1.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 347 IPSIAYTEPEVAWVGVTEKEAKEKGISFETATFPWAASGRAIASDCADGMTKLIFDKETHRIIGGAIVGANGGELLGEIG 426
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGEVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQEAA 80
|
90 100
....*....|....*....|....*....
gi 1812594828 427 LAIEMGCDAEDIALTIHAHPTLHESVGLA 455
Cdd:pfam02852 81 LAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
12-450 |
2.58e-41 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 155.03 E-value: 2.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 12 LGAGPAG---------YSAAFRCADLGLETVLVERYSTLGGVCLNVGCIPSKALLHVAKVIEEAKALAEHGIVFG-EPKT 81
Cdd:PLN02546 85 IGAGSGGvrasrfasnFGASAAVCELPFATISSDTLGGVGGTCVLRGCVPKKLLVYASKYSHEFEESRGFGWKYEtEPKH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 82 DIDKVRLWKEKVITQLTGGLAGMAKGRKVNVVNGVGKFTGANTLEVEGEngktVINFDNAIIAAGSRPIqLPFIPHDDpR 161
Cdd:PLN02546 165 DWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDVDGK----LYTARNILIAVGGRPF-IPDIPGIE-H 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 162 VWDSTDALALTTVPERLLVMGGGIIGLEMGTVYHALGSQIDVVEMFDQVIPAADKDVVKVFTKRIS-KQFNLMLETKVTA 240
Cdd:PLN02546 239 AIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKKVLRGFDEEVRDFVAEQMSlRGIEFHTEESPQA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 241 VEAKEDGIYV------TMEGkkapsepqrYDAVLVAIGRVPNGKLLDAGKAGVEVDDRGFIHVDKQLRTNVPHIFAIGDI 314
Cdd:PLN02546 319 IIKSADGSLSlktnkgTVEG---------FSHVMFATGRKPNTKNLGLEEVGVKMDKNGAIEVDEYSRTSVPSIWAVGDV 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 315 VGQPMLAHKGVHEGHVAAEVIAGKKHYF-DPKVIPSIAYTEPEVAWVGVTEKEAKEK--GISFETATFpwaASGRAIASD 391
Cdd:PLN02546 390 TDRINLTPVALMEGGALAKTLFGNEPTKpDYRAVPSAVFSQPPIGQVGLTEEQAIEEygDVDVFTANF---RPLKATLSG 466
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 392 CADGM-TKLIFDKETHRIIGGAIVGANGGELLGEIGLAIEMGCDAEDIALTIHAHPTLHE 450
Cdd:PLN02546 467 LPDRVfMKLIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAE 526
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
10-453 |
4.79e-36 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 139.57 E-value: 4.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 10 VVLGAGPAGYSAAFRCADLGLETVLVE--RYST------LGGVCLNVGCIPSKaLLHVAKVIeeAKALAEHGIVFGEPKT 81
Cdd:PTZ00052 9 VVIGGGSGGMAAAKEAAAHGKKVALFDyvKPSTqgtkwgLGGTCVNVGCVPKK-LMHYAANI--GSIFHHDSQMYGWKTS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 82 DIDKvrlWKEKVIT-----------QLTGGLAGmakgrKVNVVNGVGKFTGANTLEVEGENGKTVINFDNAIIAAGSRPi 150
Cdd:PTZ00052 86 SSFN---WGKLVTTvqnhirslnfsYRTGLRSS-----KVEYINGLAKLKDEHTVSYGDNSQEETITAKYILIATGGRP- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 151 qlpFIPHDDPRVWD----STDALALTTVPERLLVMGGGIIGLEMGTVYHALGsqidvvemFDqVIPAADKDVVKVFTKRI 226
Cdd:PTZ00052 157 ---SIPEDVPGAKEysitSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELG--------FD-VTVAVRSIPLRGFDRQC 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 227 SKQFNLMLETKVT---------AVEAKEDGIYVTMEGKKApsepQRYDAVLVAIGRVPNGKLLDAGKAGVEVDDRGFIHV 297
Cdd:PTZ00052 225 SEKVVEYMKEQGTlflegvvpiNIEKMDDKIKVLFSDGTT----ELFDTVLYATGRKPDIKGLNLNAIGVHVNKSNKIIA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 298 DKQLrTNVPHIFAIGDIV-GQPMLAHKGVHEGHV-AAEVIAGKKHYFDPKVIPSIAYTEPEVAWVGVTEKEAKEK-GIS- 373
Cdd:PTZ00052 301 PNDC-TNIPNIFAVGDVVeGRPELTPVAIKAGILlARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKyGEDd 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 374 -----FETATFPWAASGR-------------AIASDCadgMTKLIFDK-ETHRIIGGAIVGANGGELLGEIGLAIEMGCD 434
Cdd:PTZ00052 380 ieeylQEFNTLEIAAVHRekherarkdeydfDVSSNC---LAKLVCVKsEDNKVVGFHFVGPNAGEITQGFSLALKLGAK 456
|
490
....*....|....*....
gi 1812594828 435 AEDIALTIHAHPTLHESVG 453
Cdd:PTZ00052 457 KSDFDSMIGIHPTDAEVFM 475
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
126-344 |
1.16e-35 |
|
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: 134.55 E-value: 1.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 126 EVEGENGKTvINFDNAIIAAGSRPIQLPFIPHDDPRVW--------DSTDALALTTVPERLLVMGGGIIGLEMGTVYHAL 197
Cdd:COG0446 68 TVTLRDGET-LSYDKLVLATGARPRPPPIPGLDLPGVFtlrtlddaDALREALKEFKGKRAVVIGGGPIGLELAEALRKR 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 198 GSQIDVVEMFDQVIPAADKDVVKVFTKRI-SKQFNLMLETKVTAVEAKEDGIYVTMEGKKAPsepqrYDAVLVAIGRVPN 276
Cdd:COG0446 147 GLKVTLVERAPRLLGVLDPEMAALLEEELrEHGVELRLGETVVAIDGDDKVAVTLTDGEEIP-----ADLVVVAPGVRPN 221
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812594828 277 GKLldAGKAGVEVDDRGFIHVDKQLRTNVPHIFAIGDIVGQP----------MLAHKGVHEGHVAAEVIAGKKHYFDP 344
Cdd:COG0446 222 TEL--AKDAGLALGERGWIKVDETLQTSDPDVYAAGDCAEVPhpvtgktvyiPLASAANKQGRVAAENILGGPAPFPG 297
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
10-452 |
7.75e-30 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 122.42 E-value: 7.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 10 VVLGAGPAGYSAAFRCADLGLETVLVERySTLGGVCLNVGCIPSKALLHVAKVIEEAKALAEHGIVFGEpKTDIDKVRLW 89
Cdd:PTZ00058 52 IVIGGGSGGMAAARRAARNKAKVALVEK-DYLGGTCVNVGCVPKKIMFNAASIHDILENSRHYGFDTQF-SFNLPLLVER 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 90 KEKVITQLTGGLAGMAKGRKVNVVNGVGKFTGANTL-------------------------EVEGENGKTVINFDNAIIA 144
Cdd:PTZ00058 130 RDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVlikkvsqvdgeadesdddevtivsaGVSQLDDGQVIEGKNILIA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 145 AGSRPIqLPFIPHDDPRVwDSTDALALTTvPERLLVMGGGIIGLEMGTVYHALGSQIDVVEMFDQVIPAADKDVVKVFTK 224
Cdd:PTZ00058 210 VGNKPI-FPDVKGKEFTI-SSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLRKFDETIINELEN 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 225 RISK-------QFNLmleTKVTAVEAKEDGIYVTMEGKKapsepQRYDAVLVAIGRVPNGKLLDAgKAGVEVDDRGFIHV 297
Cdd:PTZ00058 287 DMKKnniniitHANV---EEIEKVKEKNLTIYLSDGRKY-----EHFDYVIYCVGRSPNTEDLNL-KALNIKTPKGYIKV 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 298 DKQLRTNVPHIFAIGDIVG------------------QPMLAHKGVHEGH-----------------VAAEVIAGKKHYF 342
Cdd:PTZ00058 358 DDNQRTSVKHIYAVGDCCMvkknqeiedlnllklyneEPYLKKKENTSGEsyynvqltpvainagrlLADRLFGPFSRTT 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 343 DPKVIPSIAYTEPEVAWVGVTEKEAKEK------GISFETATFPWAASGRAIASDCADGMTKLIFDKETHRIIGGAIVGA 416
Cdd:PTZ00058 438 NYKLIPSVIFSHPPIGTIGLSEQEAIDIygkenvKIYESRFTNLFFSVYDMDPAQKEKTYLKLVCVGKEELIKGLHIVGL 517
|
490 500 510
....*....|....*....|....*....|....*.
gi 1812594828 417 NGGELLGEIGLAIEMGCDAEDIALTIHAHPTLHESV 452
Cdd:PTZ00058 518 NADEILQGFAVALKMNATKADFDETIPIHPTAAEEF 553
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
6-346 |
2.71e-29 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 118.71 E-value: 2.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 6 KTQVVVLGAGPAGYSAA--FRCADLGLETVLV--ERYSTLGGVCLnvgcipSKALLHVAK----VIEEAKALAEHGI--V 75
Cdd:COG1251 1 KMRIVIIGAGMAGVRAAeeLRKLDPDGEITVIgaEPHPPYNRPPL------SKVLAGETDeedlLLRPADFYEENGIdlR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 76 FGEPKTDIDkvrlwkekvitqltgglagmAKGRKVNVVNGvgkftgantlevegengkTVINFDNAIIAAGSRPIQLPFI 155
Cdd:COG1251 75 LGTRVTAID--------------------RAARTVTLADG------------------ETLPYDKLVLATGSRPRVPPIP 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 156 PHDDPRV---WDSTDALALTTV---PERLLVMGGGIIGLEMGTVYHALGSQIDVVEMFDQVIPAA-DKDVVKVFTKRISK 228
Cdd:COG1251 117 GADLPGVftlRTLDDADALRAAlapGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPRQlDEEAGALLQRLLEA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 229 Q-FNLMLETKVTAVEAKEDGIYVTME-GKKAPSepqryDAVLVAIGRVPNGKLLDAgkAGVEVDdRGfIHVDKQLRTNVP 306
Cdd:COG1251 197 LgVEVRLGTGVTEIEGDDRVTGVRLAdGEELPA-----DLVVVAIGVRPNTELARA--AGLAVD-RG-IVVDDYLRTSDP 267
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1812594828 307 HIFAIGDIV-------GQPMLAH--KGVHEGHVAAEVIAGKKHYFDPKV 346
Cdd:COG1251 268 DIYAAGDCAehpgpvyGRRVLELvaPAYEQARVAAANLAGGPAAYEGSV 316
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
122-432 |
1.06e-26 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 112.06 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 122 ANTLEVEGENGKTVIN--FDNAIIAAGSRPIqLPFIPHDDPR----VWDSTDALAL-----TTVPERLLVMGGGIIGLEM 190
Cdd:PRK09564 86 NKTITVKNLKTGSIFNdtYDKLMIATGARPI-IPPIKNINLEnvytLKSMEDGLALkellkDEEIKNIVIIGAGFIGLEA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 191 GTVYHALGSQIDVVEMFDQVIPAA-DKDVVKVFTKRISKQ-FNLMLETKVTAVEAkEDGIYVTMEGKKapsepqRYDA-- 266
Cdd:PRK09564 165 VEAAKHLGKNVRIIQLEDRILPDSfDKEITDVMEEELRENgVELHLNEFVKSLIG-EDKVEGVVTDKG------EYEAdv 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 267 VLVAIGRVPNGKLLDagKAGVEVDDRGFIHVDKQLRTNVPHIFAIGD-------IVGQPM---LAHKGVHEGHVAAEVIA 336
Cdd:PRK09564 238 VIVATGVKPNTEFLE--DTGLKTLKNGAIIVDEYGETSIENIYAAGDcatiyniVSNKNVyvpLATTANKLGRMVGENLA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 337 GKKHYFdPKVIPS--IAYTEPEVAWVGVTEKEAKEKGISFETATfpwaasgraIASDC--------ADGMTKLIFDKETH 406
Cdd:PRK09564 316 GRHVSF-KGTLGSacIKVLDLEAARTGLTEEEAKKLGIDYKTVF---------IKDKNhtnyypgqEDLYVKLIYEADTK 385
|
330 340
....*....|....*....|....*..
gi 1812594828 407 RIIGGAIVGANGGEL-LGEIGLAIEMG 432
Cdd:PRK09564 386 VILGGQIIGKKGAVLrIDALAVAIYAK 412
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
7-332 |
3.75e-21 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 93.65 E-value: 3.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 7 TQVVVLGAGPAGYSAAFRCADLGLETVLVERySTLGGVCLNVGCI---PSkallhVAKVI---EEAKALAEHGIVFGepk 80
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEG-GEPGGQLATTKEIenyPG-----FPEGIsgpELAERLREQAERFG--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 81 tdidkVRLWKEKVItqltgglagmakgrKVNVVNGVGKFTGANTLEVEGengKTVInfdnaiIAAGSRPIQLPfIPHDDP 160
Cdd:COG0492 72 -----AEILLEEVT--------------SVDKDDGPFRVTTDDGTEYEA---KAVI------IATGAGPRKLG-LPGEEE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 161 RVWDS------TDALALTTvpERLLVMGGGIIGLEMGTVYHALGSQIDVVEMFDQvIPAADKDVVKVF-TKRIskqfNLM 233
Cdd:COG0492 123 FEGRGvsycatCDGFFFRG--KDVVVVGGGDSALEEALYLTKFASKVTLIHRRDE-LRASKILVERLRaNPKI----EVL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 234 LETKVTAVEAKE--DGIYVTmEGKKAPSEPQRYDAVLVAIGRVPNGKLLDagKAGVEVDDRGFIHVDKQLRTNVPHIFAI 311
Cdd:COG0492 196 WNTEVTEIEGDGrvEGVTLK-NVKTGEEKELEVDGVFVAIGLKPNTELLK--GLGLELDEDGYIVVDEDMETSVPGVFAA 272
|
330 340
....*....|....*....|..
gi 1812594828 312 GDIVGQPM-LAHKGVHEGHVAA 332
Cdd:COG0492 273 GDVRDYKYrQAATAAGEGAIAA 294
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
123-418 |
9.41e-18 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 85.22 E-value: 9.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 123 NTLEVEGENGKTVI--NFDNAIIAAGSRPIQLPFiphDDPRVW--------DSTDALALTTVPERLLVMGGGIIGLEMGT 192
Cdd:PRK13512 89 QTVTVLNRKTNEQFeeSYDKLILSPGASANSLGF---ESDITFtlrnledtDAIDQFIKANQVDKALVVGAGYISLEVLE 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 193 VYHALGSQIDVVEMFDQVIPAADKDVVKVFTKRISK-QFNLMLETKVTAVeakeDGIYVTMEGKKApsepQRYDAVLVAI 271
Cdd:PRK13512 166 NLYERGLHPTLIHRSDKINKLMDADMNQPILDELDKrEIPYRLNEEIDAI----NGNEVTFKSGKV----EHYDMIIEGV 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 272 GRVPNGKLLDAgkAGVEVDDRGFIHVDKQLRTNVPHIFAIGDIV----------GQPMLAHkGVHEG-HVAAEVIAGK-- 338
Cdd:PRK13512 238 GTHPNSKFIES--SNIKLDDKGFIPVNDKFETNVPNIYAIGDIItshyrhvdlpASVPLAW-GAHRAaSIVAEQIAGNdt 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 339 ---KHYFDPKVIPSIAYTepeVAWVGVTEKEAKEKGISFETATFPWAASgraiasdCADGMTKL----IFDKETHRIIGG 411
Cdd:PRK13512 315 iefKGFLGNNIVKFFDYT---FASVGVKPNELKQFDYKMVEVTQGAHAN-------YYPGNSPLhlrvYYDTSNRKILRA 384
|
....*..
gi 1812594828 412 AIVGANG 418
Cdd:PRK13512 385 AAVGKEG 391
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
177-255 |
2.06e-15 |
|
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: 71.08 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 177 RLLVMGGGIIGLEMGTVYHALGSQIDVVEMFDQVIPAADKDVVKVFTKRISKQ-FNLMLETKVTAVEAKEDGIYVTMEGK 255
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNgIEFLLNTTVEAIEGNGDGVVVVLTDG 80
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
101-336 |
1.16e-14 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 75.55 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 101 LAGMAKGRKVNVVngVGKFTG----ANTleVEGENGKTvINFDNAIIAAGSRP----IQ------LPFIPHDD-PRVWDS 165
Cdd:COG1252 62 LRELLRRAGVRFI--QGEVTGidpeART--VTLADGRT-LSYDYLVIATGSVTnffgIPglaehaLPLKTLEDaLALRER 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 166 TDALALTTVPERLL---VMGGGIIGLEM-GTVYHALGS------------QIDVVEMFDQVIPAADKDVVKVFTKRISKQ 229
Cdd:COG1252 137 LLAAFERAERRRLLtivVVGGGPTGVELaGELAELLRKllrypgidpdkvRITLVEAGPRILPGLGEKLSEAAEKELEKR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 230 -FNLMLETKVTAVEAkeDGIYVTmEGKKAPsepqrYDAVLVAIGRVPNGkllDAGKAGVEVDDRGFIHVDKQLRT-NVPH 307
Cdd:COG1252 217 gVEVHTGTRVTEVDA--DGVTLE-DGEEIP-----ADTVIWAAGVKAPP---LLADLGLPTDRRGRVLVDPTLQVpGHPN 285
|
250 260 270
....*....|....*....|....*....|....*..
gi 1812594828 308 IFAIGDIV--------GQPMLAHKGVHEGHVAAEVIA 336
Cdd:COG1252 286 VFAIGDCAavpdpdgkPVPKTAQAAVQQAKVLAKNIA 322
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
176-319 |
1.13e-13 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 72.26 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 176 ERLLVMGGGIIGLEMGTVYHALGSQIDVVEMFDQVIPAADKDVV--KVFTKRISKQFNLMLETKVTAVEAKEDGIYVTMe 253
Cdd:PRK04965 142 QRVLVVGGGLIGTELAMDLCRAGKAVTLVDNAASLLASLMPPEVssRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRATL- 220
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1812594828 254 gkkAPSEPQRYDAVLVAIGRVPNGKLldAGKAGVEVDdRGfIHVDKQLRTNVPHIFAIGD---IVGQPM 319
Cdd:PRK04965 221 ---DSGRSIEVDAVIAAAGLRPNTAL--ARRAGLAVN-RG-IVVDSYLQTSAPDIYALGDcaeINGQVL 282
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
9-335 |
9.89e-13 |
|
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 440259 [Multi-domain] Cd Length: 434 Bit Score: 69.78 E-value: 9.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 9 VVVLGAGPAGYSAAFRCADLGLETVLVERYSTLGGVcLNVGcIPS----KALlhvakVIEEAKALAEHGIVFgEPKTDID 84
Cdd:COG0493 124 VAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGGL-LRYG-IPEfrlpKDV-----LDREIELIEALGVEF-RTNVEVG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 85 KV----RLWKE--KVItqltggLA-GMAKGRKvnvvngvgkftgantLEVEGENGKTVINfdnAIiaagsrpiqlPFIPh 157
Cdd:COG0493 196 KDitldELLEEfdAVF------LAtGAGKPRD---------------LGIPGEDLKGVHS---AM----------DFLT- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 158 ddpRVWDSTDALALTTVPERLLVMGGGIIGLEMGTVYHALG-SQIDVVEMFDQV-IPAADKDVVKVFTKRISKQFNLMle 235
Cdd:COG0493 241 ---AVNLGEAPDTILAVGKRVVVIGGGNTAMDCARTALRLGaESVTIVYRRTREeMPASKEEVEEALEEGVEFLFLVA-- 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 236 tkVTAVEAKEDG-----IYVTMEGKKAPSEPQRY-------------DAVLVAIGRVPNGKLLDAgKAGVEVDDRGFIHV 297
Cdd:COG0493 316 --PVEIIGDENGrvtglECVRMELGEPDESGRRRpvpiegseftlpaDLVILAIGQTPDPSGLEE-ELGLELDKRGTIVV 392
|
330 340 350
....*....|....*....|....*....|....*....
gi 1812594828 298 DKQ-LRTNVPHIFAIGDIVGQPMLAHKGVHEGHVAAEVI 335
Cdd:COG0493 393 DEEtYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAI 431
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
61-336 |
2.94e-11 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 65.62 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 61 KVIEEAKALAEHG---IVFG-EPKTDIDKVRL-------WKEKVITQLTGGLAGMakgrkvnvvNGVGKFTGANTLEVEG 129
Cdd:TIGR02374 12 RCIEEVLKLNRHMfeiTIFGeEPHPNYNRILLssvlqgeADLDDITLNSKDWYEK---------HGITLYTGETVIQIDT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 130 ENgKTVIN-------FDNAIIAAGSRPIQLPFIPHDDP-----RVWDSTDAL-ALTTVPERLLVMGGGIIGLEMGTVYHA 196
Cdd:TIGR02374 83 DQ-KQVITdagrtlsYDKLILATGSYPFILPIPGADKKgvyvfRTIEDLDAImAMAQRFKKAAVIGGGLLGLEAAVGLQN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 197 LGSQIDVVEMfdqvipaADKDVVKVFTKRISKQFNLMLETKVTAVEAKEDGIYVTMEGKK-----APSEPQRYDAVLVAI 271
Cdd:TIGR02374 162 LGMDVSVIHH-------APGLMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVGATKAdrirfKDGSSLEADLIVMAA 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 272 GRVPNGKLldAGKAGVEVdDRGFIhVDKQLRTNVPHIFAIGDIVgqpmlAHKGVHEGHVA-----AEVIA 336
Cdd:TIGR02374 235 GIRPNDEL--AVSAGIKV-NRGII-VNDSMQTSDPDIYAVGECA-----EHNGRVYGLVAplyeqAKVLA 295
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
121-314 |
2.50e-09 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 59.17 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 121 GANTLEVEGENGKTvINFDNAIIAAGSRPIQLPFIPHDDPRVWD---STDALALTTV--PE-RLLVMGGGIIGLEMGTVY 194
Cdd:PRK09754 85 GRDTRELVLTNGES-WHWDQLFIATGAAARPLPLLDALGERCFTlrhAGDAARLREVlqPErSVVIVGAGTIGLELAASA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 195 HALGSQIDVVEMFDQVIPAADKDVVK--VFTKRISKQFNLMLETKVTAVEAKEDGIYVTMEGKKAPSepqryDAVLVAIG 272
Cdd:PRK09754 164 TQRRCKVTVIELAATVMGRNAPPPVQryLLQRHQQAGVRILLNNAIEHVVDGEKVELTLQSGETLQA-----DVVIYGIG 238
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1812594828 273 RVPNGKLldAGKAGVEVDdrGFIHVDKQLRTNVPHIFAIGDI 314
Cdd:PRK09754 239 ISANDQL--AREANLDTA--NGIVIDEACRTCDPAIFAGGDV 276
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
9-335 |
2.75e-08 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 55.94 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 9 VVVLGAGPAGYSAAFRCADLGLETVLVERYSTLGGvcLNVGCIPS----KAllHVAKVIEEakaLAEHGIVF---GEPKT 81
Cdd:PRK12810 146 VAVVGSGPAGLAAADQLARAGHKVTVFERADRIGG--LLRYGIPDfkleKE--VIDRRIEL---MEAEGIEFrtnVEVGK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 82 DIDKVRLWKE--KVItqLTGGLagmakgrkvnvvngvgkfTGANTLEVEGENGKTVinfDNAiiaagsrpiqLPFIPHDD 159
Cdd:PRK12810 219 DITAEELLAEydAVF--LGTGA------------------YKPRDLGIPGRDLDGV---HFA----------MDFLIQNT 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 160 PRVWDSTDALALTTVPERLLVMGGGIIGLEMGTVYHALG----SQIDVVEMfdqviPAADKDVVKVF-----TKRIS--- 227
Cdd:PRK12810 266 RRVLGDETEPFISAKGKHVVVIGGGDTGMDCVGTAIRQGaksvTQRDIMPM-----PPSRRNKNNPWpywpmKLEVSnah 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 228 -----KQFNLM------LETKVTAVEAkedgIYVTMEGKKA---PSEPQRY--DAVLVAIG-RVPNGKLLDAGkaGVEVD 290
Cdd:PRK12810 341 eegveREFNVQtkefegENGKVTGVKV----VRTELGEGDFepvEGSEFVLpaDLVLLAMGfTGPEAGLLAQF--GVELD 414
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1812594828 291 DRGFI-HVDKQLRTNVPHIFAIGDIV-GQPmLAHKGVHEGHVAAEVI 335
Cdd:PRK12810 415 ERGRVaAPDNAYQTSNPKVFAAGDMRrGQS-LVVWAIAEGRQAARAI 460
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
9-43 |
1.57e-06 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 50.30 E-value: 1.57e-06
10 20 30
....*....|....*....|....*....|....*
gi 1812594828 9 VVVLGAGPAGYSAAFRCADLGLETVLVERYSTLGG 43
Cdd:pfam12831 2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGG 36
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
8-335 |
3.91e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 49.38 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 8 QVVVLGAGPAGYSAAFRCADLGLETVLVERYSTLGGVcLNVGcIPSKALlhvakvieeakalaehgivfgePKTDIDKvr 87
Cdd:PRK13984 285 KVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGV-MRYG-IPSYRL----------------------PDEALDK-- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 88 lwKEKVITQLtgglagmakGRKVNVVNGVGKFTGANTLEVEgengktvinFDNAIIAAG---SRPIQLPFIPHddPRVWD 164
Cdd:PRK13984 339 --DIAFIEAL---------GVKIHLNTRVGKDIPLEELREK---------HDAVFLSTGftlGRSTRIPGTDH--PDVIQ 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 165 STDALALTT-----------VPERLLVMGGGIIG------------LEMGTV-YHALGSQIDVVEM---FDQVIPAADKD 217
Cdd:PRK13984 397 ALPLLREIRdylrgegpkpkIPRSLVVIGGGNVAmdiarsmarlqkMEYGEVnVKVTSLERTFEEMpadMEEIEEGLEEG 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 218 VVkvFTKRISKQFNLMLETKVTAVEAKEDGIYVTMEGKKAPS---EPQRY---DAVLVAIGRVPNGKLL-DAGKAGVEVD 290
Cdd:PRK13984 477 VV--IYPGWGPMEVVIENDKVKGVKFKKCVEVFDEEGRFNPKfdeSDQIIveaDMVVEAIGQAPDYSYLpEELKSKLEFV 554
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1812594828 291 dRGFIHVDKQLRTNVPHIFAIGDIVGQPMLAHkGVHEGHVAAEVI 335
Cdd:PRK13984 555 -RGRILTNEYGQTSIPWLFAGGDIVHGPDIIH-GVADGYWAAEGI 597
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
9-335 |
4.63e-06 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 49.02 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 9 VVVLGAGPAGYSAAFRCADLGLETVLVERYSTLGGVclNVGCIPSKALlhvAKVI--EEAKALAEHGIVFgEPKTDIdkv 86
Cdd:PRK11749 143 VAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGGL--LRYGIPEFRL---PKDIvdREVERLLKLGVEI-RTNTEV--- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 87 rlwkEKVIT--QLtgglagMAKGRKVNVVNGVGKftgANTLEVEGENGKTVINfdnAIiaagsrpiqlPFIPhddpRVwD 164
Cdd:PRK11749 214 ----GRDITldEL------RAGYDAVFIGTGAGL---PRFLGIPGENLGGVYS---AV----------DFLT----RV-N 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 165 STDALALTTVPERLLVMGGGIIGLEMGTVYHALGSQ---I----DVVEMfdqviPAADKDVVkvFTKriSKQFNLMLETK 237
Cdd:PRK11749 263 QAVADYDLPVGKRVVVIGGGNTAMDAARTAKRLGAEsvtIvyrrGREEM-----PASEEEVE--HAK--EEGVEFEWLAA 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 238 VTAVEAKEDG----IYVTME--------GKKAPSEPQRY----DAVLVAIGRVPNGKLLDAGKaGVEVDDRG-FIHVDKQ 300
Cdd:PRK11749 334 PVEILGDEGRvtgvEFVRMElgepdasgRRRVPIEGSEFtlpaDLVIKAIGQTPNPLILSTTP-GLELNRWGtIIADDET 412
|
330 340 350
....*....|....*....|....*....|....*...
gi 1812594828 301 LRTNVPHIFAIGDIV-GQPM--LAhkgVHEGHVAAEVI 335
Cdd:PRK11749 413 GRTSLPGVFAGGDIVtGAATvvWA---VGDGKDAAEAI 447
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
9-69 |
5.08e-06 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 48.70 E-value: 5.08e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1812594828 9 VVVLGAGPAGYSAAFRCADLGLETVLV-ERYSTLGgvclNVGCIPSKALLHVAKVIEEAKAL 69
Cdd:pfam01134 2 VIVIGGGHAGCEAALAAARMGAKVLLItHNTDTIA----ELSCNPSIGGIAKGHLVREIDAL 59
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
6-45 |
1.63e-05 |
|
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: 47.13 E-value: 1.63e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1812594828 6 KTQVVVLGAGPAGYSAAFRCADLGLETVLVERYSTLGGVC 45
Cdd:COG1232 1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLI 40
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
2-149 |
4.25e-05 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 46.01 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 2 STEIKTQVVVLGAGPAGYSAAFRCADLGLETVLVERYSTLGGVCLNVGC-IPSkaLLHVAKVIEE-AKALAEHgivfgep 79
Cdd:COG1148 136 KVPVNKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAQLHKtFPG--LDCPQCILEPlIAEVEAN------- 206
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 80 ktdiDKVRLWKEKVITQLTGglagmakgrkvnvvnGVGKFTGanTLEVEGEnGKTVINFDNAIIAAGSRP 149
Cdd:COG1148 207 ----PNITVYTGAEVEEVSG---------------YVGNFTV--TIKKGPR-EEIEIEVGAIVLATGFKP 254
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
265-335 |
4.88e-05 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 45.64 E-value: 4.88e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1812594828 265 DAVLVAIGRVPNGKLLDaGKAGVEVDdRGFIHVDKQLR-TNVPHIFAIGDIVGQPMLAHKGVHEGHVAAEVI 335
Cdd:PRK12771 370 DLVVLAIGQDIDSAGLE-SVPGVEVG-RGVVQVDPNFMmTGRPGVFAGGDMVPGPRTVTTAIGHGKKAARNI 439
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
235-336 |
7.83e-05 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 44.60 E-value: 7.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 235 ETKVTAVEAKEDGIYVTMEGKKAPSEPQ-------RYDAVLVAIGRVPNGKLlDAGKAGVEVDDRGFIHVDKQLRTNVPH 307
Cdd:PRK12770 239 EGRVEGVELAKMRLGEPDESGRPRPVPIpgsefvlEADTVVFAIGEIPTPPF-AKECLGIELNRKGEIVVDEKHMTSREG 317
|
90 100
....*....|....*....|....*....
gi 1812594828 308 IFAIGDIVGQPMLAHKGVHEGHVAAEVIA 336
Cdd:PRK12770 318 VFAAGDVVTGPSKIGKAIKSGLRAAQSIH 346
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
6-332 |
9.72e-05 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 45.02 E-value: 9.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 6 KTQVVVLGAGPAGYSAAFRCADLGLETVLVERYSTLGGVcLNVGCIPSKALLHVAKVIEEakALAEHGIVFG---EPKTD 82
Cdd:PRK12809 310 SEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGM-LTFGIPPFKLDKTVLSQRRE--IFTAMGIDFHlncEIGRD 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 83 IDKVRLWKEKVITQLTGGLAGMAKGrkvnvvngvgkftgantlEVEGENGKTVINFDNAIIAAGSRPIQLPfiphddprv 162
Cdd:PRK12809 387 ITFSDLTSEYDAVFIGVGTYGMMRA------------------DLPHEDAPGVIQALPFLTAHTRQLMGLP--------- 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 163 wdSTDALALTTVP-ERLLVMGGGIIGLE-MGTVYHALGSQIDVVEMFDQV-IPAADKDVVKVFTKRISKQFNLMLET--- 236
Cdd:PRK12809 440 --ESEEYPLTDVEgKRVVVLGGGDTTMDcLRTSIRLNAASVTCAYRRDEVsMPGSRKEVVNAREEGVEFQFNVQPQYiac 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 237 ----KVTAVeakedGIYVTMEGKKAPSEPQR------------YDAVLVAIGRVPNGKLLDAGkAGVEVDDRGFIHVDKQ 300
Cdd:PRK12809 518 dedgRLTAV-----GLIRTAMGEPGPDGRRRprpvagsefelpADVLIMAFGFQAHAMPWLQG-SGIKLDKWGLIQTGDV 591
|
330 340 350
....*....|....*....|....*....|....*.
gi 1812594828 301 LR----TNVPHIFAIGDIVGQPMLAHKGVHEGHVAA 332
Cdd:PRK12809 592 GYlptqTHLKKVFAGGDAVHGADLVVTAMAAGRQAA 627
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
265-313 |
1.19e-04 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 44.38 E-value: 1.19e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1812594828 265 DAVLVAIGRVPNGKLLdagKAGVEVDDRGFIHVDKQLRTNVPHIFAIGD 313
Cdd:PRK15317 439 EGVFVQIGLVPNTEWL---KGTVELNRRGEIIVDARGATSVPGVFAAGD 484
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
9-43 |
1.46e-04 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 44.07 E-value: 1.46e-04
10 20 30
....*....|....*....|....*....|....*
gi 1812594828 9 VVVLGAGPAGYSAAFRCADLGLETVLVERYSTLGG 43
Cdd:COG1233 6 VVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
6-45 |
1.78e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 43.72 E-value: 1.78e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1812594828 6 KTQVVVLGAGPAGYSAAFRCADLGLETVLVERYSTLGGVC 45
Cdd:PRK07208 4 KKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGIS 43
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
265-335 |
3.01e-04 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 43.18 E-value: 3.01e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1812594828 265 DAVLVAIGRVPNGKLLDAgkAGVEVDDRGFIHVDKQ-LRTNVPHIFAIGDIVGQPMLAHKGVHEGHVAAEVI 335
Cdd:PRK12814 427 DTVISAIGQQVDPPIAEA--AGIGTSRNGTVKVDPEtLQTSVAGVFAGGDCVTGADIAINAVEQGKRAAHAI 496
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
7-45 |
3.29e-04 |
|
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];
Pssm-ID: 442577 [Multi-domain] Cd Length: 445 Bit Score: 42.92 E-value: 3.29e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1812594828 7 TQVVVLGAGPAGYSAAFRCADLGLETVLVERYSTLGGVC 45
Cdd:COG3349 4 PRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGGRA 42
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
127-313 |
3.36e-04 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 43.18 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 127 VEGENGKTViNFDNAIIAAGSrpiqLPFIP------HDDPRVWDSTDAL----ALTTVPERLLVMGGGIIGLEMGTVYHA 196
Cdd:PRK14989 92 IHSSAGRTV-FYDKLIMATGS----YPWIPpikgseTQDCFVYRTIEDLnaieACARRSKRGAVVGGGLLGLEAAGALKN 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 197 LGSQIDVVEmFDQVIPAADKDVVKvftkriSKQFNLMLETKVTAVEAKEDGIYVTMEGKKAPSEPQ-------RYDAVLV 269
Cdd:PRK14989 167 LGVETHVIE-FAPMLMAEQLDQMG------GEQLRRKIESMGVRVHTSKNTLEIVQEGVEARKTMRfadgselEVDFIVF 239
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1812594828 270 AIGRVPNGKLldAGKAGVEVDDRGFIHVDKQLRTNVPHIFAIGD 313
Cdd:PRK14989 240 STGIRPQDKL--ATQCGLAVAPRGGIVINDSCQTSDPDIYAIGE 281
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
9-75 |
5.19e-04 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 42.33 E-value: 5.19e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1812594828 9 VVVLGAGPAGYSAAFRCADLGLETVLVERYSTLGGVCLNVGC---IPSKALLHVAKVIEEAKALAE--HGIV 75
Cdd:PRK07843 10 VVVVGSGAAGMVAALTAAHRGLSTVVVEKAPHYGGSTARSGGgvwIPNNEVLKRAGVPDTPEAARTylHSIV 81
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
4-43 |
5.68e-04 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 42.13 E-value: 5.68e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1812594828 4 EIKTQVVVLGAGPAGYSAAFRCADLGLETVLVERYSTLGG 43
Cdd:COG1053 1 DHEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
|
|
| PRK12844 |
PRK12844 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
1-43 |
6.31e-04 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 183787 [Multi-domain] Cd Length: 557 Bit Score: 42.05 E-value: 6.31e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1812594828 1 MSTEIKTQVVVLGAGPAGYSAAFRCADLGLETVLVERYSTLGG 43
Cdd:PRK12844 1 ATWDETYDVVVVGSGGGGMCAALAAADSGLEPLIVEKQDKVGG 43
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
265-315 |
8.89e-04 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 42.04 E-value: 8.89e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1812594828 265 DAVLVAIGRVPNgKLLDAGKAGVEVDDRGFIHVDKQLRTNVPHIFAIGDIV 315
Cdd:PRK12778 676 DLVIVSVGVSPN-PLVPSSIPGLELNRKGTIVVDEEMQSSIPGIYAGGDIV 725
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
9-37 |
1.15e-03 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 41.12 E-value: 1.15e-03
10 20
....*....|....*....|....*....
gi 1812594828 9 VVVLGAGPAGYSAAFRCADLGLETVLVER 37
Cdd:pfam00890 2 VLVIGGGLAGLAAALAAAEAGLKVAVVEK 30
|
|
| COG2509 |
COG2509 |
FAD-dependent dehydrogenase [General function prediction only]; |
6-37 |
1.41e-03 |
|
FAD-dependent dehydrogenase [General function prediction only];
Pssm-ID: 441999 [Multi-domain] Cd Length: 466 Bit Score: 40.87 E-value: 1.41e-03
10 20 30
....*....|....*....|....*....|..
gi 1812594828 6 KTQVVVLGAGPAGYSAAFRCADLGLETVLVER 37
Cdd:COG2509 30 KYDVVIVGAGPAGLFAALELAEAGLKPLVLER 61
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
1-82 |
1.43e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 40.97 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 1 MSTEIKTQ--VVVLGAGPAGYSAAFRCADLGLETVLVERYSTLGGVCLNVG---CIPSKALLHVAKVIE---EAKALAEH 72
Cdd:PRK12839 1 MTPSMTHTydVVVVGSGAGGLSAAVAAAYGGAKVLVVEKASTCGGATAWSGgwmWTPGNSLARADGVVEdkeEPRTYLEH 80
|
90
....*....|..
gi 1812594828 73 --GIVFGEPKTD 82
Cdd:PRK12839 81 rlGENYDADKVD 92
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
9-37 |
2.31e-03 |
|
geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 273936 [Multi-domain] Cd Length: 295 Bit Score: 39.99 E-value: 2.31e-03
10 20
....*....|....*....|....*....
gi 1812594828 9 VVVLGAGPAGYSAAFRCADLGLETVLVER 37
Cdd:TIGR02032 3 VVVVGAGPAGASAAYRLADKGLRVLLLEK 31
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
7-43 |
2.48e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 40.49 E-value: 2.48e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1812594828 7 TQVVVLGAGPAGYSAAFRCADLGLETVLVERYSTLGG 43
Cdd:PRK12843 17 FDVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGG 53
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
11-45 |
2.74e-03 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 36.36 E-value: 2.74e-03
10 20 30
....*....|....*....|....*....|....*
gi 1812594828 11 VLGAGPAGYSAAFRCADLGLETVLVERYSTLGGVC 45
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNA 35
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
1-43 |
2.85e-03 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 40.06 E-value: 2.85e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1812594828 1 MSTEIKTQVVVLGAGPAGYSAAFRCADLGLETVLVERYSTLGG 43
Cdd:PRK12842 4 MTNELTCDVLVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGG 46
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
9-43 |
2.98e-03 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 40.09 E-value: 2.98e-03
10 20 30
....*....|....*....|....*....|....*
gi 1812594828 9 VVVLGAGPAGYSAAFRCADLGLETVLVERYSTLGG 43
Cdd:PRK06134 15 VLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGG 49
|
|
| FAD_binding_3 |
pfam01494 |
FAD binding domain; This domain is involved in FAD binding in a number of enzymes. |
6-40 |
3.01e-03 |
|
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
Pssm-ID: 396193 [Multi-domain] Cd Length: 348 Bit Score: 39.62 E-value: 3.01e-03
10 20 30
....*....|....*....|....*....|....*
gi 1812594828 6 KTQVVVLGAGPAGYSAAFRCADLGLETVLVERYST 40
Cdd:pfam01494 1 ETDVLIVGGGPAGLMLALLLARAGVRVVLVERHAT 35
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
6-44 |
3.47e-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: 39.54 E-value: 3.47e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1812594828 6 KTQVVVLGAGPAGYSAAFRCADLGLETVLVERYSTLGGV 44
Cdd:COG0654 3 RTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPD 41
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
9-43 |
4.54e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 39.48 E-value: 4.54e-03
10 20 30
....*....|....*....|....*....|....*
gi 1812594828 9 VVVLGAGPAGYSAAFRCADLGLETVLVERYSTLGG 43
Cdd:PRK07233 2 IAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGG 36
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
7-44 |
5.05e-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: 39.08 E-value: 5.05e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1812594828 7 TQVVVLGAGPAGYSAAFRCADLGLETVLVERYSTLGGV 44
Cdd:COG2072 7 VDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGT 44
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
265-339 |
5.49e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 39.23 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594828 265 DAVLVAIGRVPNGKLLDAGKaGVEVDDRGFIHVDKQ-LRTNVPHIFAIGDIVgqpmlahKGvheghvAAEVI----AGKK 339
Cdd:PRK12831 386 DTVIMSLGTSPNPLISSTTK-GLKINKRGCIVADEEtGLTSKEGVFAGGDAV-------TG------AATVIlamgAGKK 451
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
7-42 |
7.02e-03 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 38.72 E-value: 7.02e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1812594828 7 TQVVVLGAGPAGYSAAFRCADLGLETVLVERYSTLG 42
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
|
|
| PLN00093 |
PLN00093 |
geranylgeranyl diphosphate reductase; Provisional |
6-37 |
7.38e-03 |
|
geranylgeranyl diphosphate reductase; Provisional
Pssm-ID: 177713 [Multi-domain] Cd Length: 450 Bit Score: 38.58 E-value: 7.38e-03
10 20 30
....*....|....*....|....*....|..
gi 1812594828 6 KTQVVVLGAGPAGYSAAFRCADLGLETVLVER 37
Cdd:PLN00093 39 KLRVAVIGGGPAGACAAETLAKGGIETFLIER 70
|
|
| |
