|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
1-466 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 625.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 1 MAYDVIVVGSGPGGYVAAIRASQLGLKTAIIEKESLGGICLNWGCIPTKALLKSAQVFNDIQHAKDYGIEASG-TPDFGA 79
Cdd:PRK06416 3 FEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIKAENvGIDFKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 80 IVKRSRGVADKMSKGVQFLMKKNKIDVIMGFGTLKAKGQVEVKGTDGKTTLvEGKHVILATGGRSRELPALKQDGKKIIG 159
Cdd:PRK06416 83 VQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDGEQTY-TAKNIILATGSRPRELPGIEIDGRVIWT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 160 YREAMVLPQQPKSIIVVGSGAIGVEFGYFYNSLGTKVTIVEFLPRVVPVEDEDISKELEKNLKKQGITVMTSSEVTSVDT 239
Cdd:PRK06416 162 SDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPGEDKEISKLAERALKKRGIKIKTGAKAKKVEQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 240 SGNGVKAKVKTATGEAILEADVLLSAVGVAANIEGIGLETVGVKTDKGKIVVDKFYKTNVDGVYAIGDCVPGQALAHVAS 319
Cdd:PRK06416 242 TDDGVTVTLEDGGKEETLEADYVLVAVGRRPNTENLGLEELGVKTDRGFIEVDEQLRTNVPNIYAIGDIVGGPMLAHKAS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 320 KEGIICVENIAfGEkkykhqPEALDYGNVPGCTYCYPEIASVGFTEKQAKEAGYEVKVGKFPLSASGKASAAGHTEGFVK 399
Cdd:PRK06416 322 AEGIIAAEAIA-GN------PHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFDVKVVKFPFAGNGKALALGETDGFVK 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517457889 400 VIFDAKYGEWLGTHMIGYNVTEIIAETVVGRKLETTYHEVLNSIHPHPTISESVKDAIEVAYGEAIH 466
Cdd:PRK06416 395 LIFDKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEALGEAALAAAGKPLH 461
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
1-463 |
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: 591.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 1 MAYDVIVVGSGPGGYVAAIRASQLGLKTAIIEKESLGGICLNWGCIPTKALLKSAQVFNDIQHAKDYGIEASG-TPDFGA 79
Cdd:COG1249 2 KDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISAGApSVDWAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 80 IVKRSRGVADKMSKGVQFLMKKNKIDVIMGFGTLKAKGQVEVKGTdgktTLVEGKHVILATGGRSRELPALKQDGKKIIG 159
Cdd:COG1249 82 LMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVTGG----ETLTADHIVIATGSRPRVPPIPGLDEVRVLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 160 YREAMVLPQQPKSIIVVGSGAIGVEFGYFYNSLGTKVTIVEFLPRVVPVEDEDISKELEKNLKKQGITVMTSSEVTSVDT 239
Cdd:COG1249 158 SDEALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 240 SGNGVKAKVKTATGEAILEADVLLSAVGVAANIEGIGLETVGVKTD-KGKIVVDKFYKTNVDGVYAIGDCVPGQALAHVA 318
Cdd:COG1249 238 TGDGVTVTLEDGGGEEAVEADKVLVATGRRPNTDGLGLEAAGVELDeRGGIKVDEYLRTSVPGIYAIGDVTGGPQLAHVA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 319 SKEGIICVENIAfgekkyKHQPEALDYGNVPGCTYCYPEIASVGFTEKQAKEAGYEVKVGKFPLSASGKASAAGHTEGFV 398
Cdd:COG1249 318 SAEGRVAAENIL------GKKPRPVDYRAIPSVVFTDPEIASVGLTEEEAREAGIDVKVGKFPFAANGRALALGETEGFV 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517457889 399 KVIFDAKYGEWLGTHMIGYNVTEIIAETVVGRKLETTYHEVLNSIHPHPTISESVKDAIEVAYGE 463
Cdd:COG1249 392 KLIADAETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAALALLGR 456
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
2-466 |
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: 557.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 2 AYDVIVVGSGPGGYVAAIRASQLGLKTAIIEKESLGGICLNWGCIPTKALLKSAQVFNDIQHAKDYGIEASG-TPDFGAI 80
Cdd:TIGR01350 1 AYDVIVIGGGPGGYVAAIRAAQLGLKVALVEKEYLGGTCLNVGCIPTKALLHSAEVYDEIKHAKDLGIEVENvSVDWEKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 81 VKRSRGVADKMSKGVQFLMKKNKIDVIMGFGTLKAKGQVEVKGTDGKTTLvEGKHVILATGGRSRELP-ALKQDGKKIIG 159
Cdd:TIGR01350 81 QKRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGENGEETL-EAKNIIIATGSRPRSLPgPFDFDGKVVIT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 160 YREAMVLPQQPKSIIVVGSGAIGVEFGYFYNSLGTKVTIVEFLPRVVPVEDEDISKELEKNLKKQGITVMTSSEVTSVDT 239
Cdd:TIGR01350 160 STGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 240 SGNGVKAKVKTATGEAIlEADVLLSAVGVAANIEGIGLETVGVKTDK-GKIVVDKFYKTNVDGVYAIGDCVPGQALAHVA 318
Cdd:TIGR01350 240 NDDQVTYENKGGETETL-TGEKVLVAVGRKPNTEGLGLEKLGVELDErGRIVVDEYMRTNVPGIYAIGDVIGGPMLAHVA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 319 SKEGIICVENIAFGEkkykhqPEALDYGNVPGCTYCYPEIASVGFTEKQAKEAGYEVKVGKFPLSASGKASAAGHTEGFV 398
Cdd:TIGR01350 319 SHEGIVAAENIAGKE------PAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGYDVKIGKFPFAANGKALALGETDGFV 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517457889 399 KVIFDAKYGEWLGTHMIGYNVTEIIAETVVGRKLETTYHEVLNSIHPHPTISESVKDAIEVAYGEAIH 466
Cdd:TIGR01350 393 KIIADKKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEAIKEAALAALGKPIH 460
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
1-466 |
6.51e-167 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 478.13 E-value: 6.51e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 1 MAYDVIVVGSGPGGYVAAIRASQLGLKTAIIEKESLGGICLNWGCIPTKALLKSAQVFNDIQHAKDYGIEASG-TPDFGA 79
Cdd:PRK06292 2 EKYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGPLGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHADGpKIDFKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 80 IVKRSRGVADKMSKGV-QFLMKKNKIDVIMGFGTLKAKGQVEVKGTdgkttLVEGKHVILATGGRSRELPALKQ-DGKKI 157
Cdd:PRK06292 82 VMARVRRERDRFVGGVvEGLEKKPKIDKIKGTARFVDPNTVEVNGE-----RIEAKNIVIATGSRVPPIPGVWLiLGDRL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 158 IGYREAMVLPQQPKSIIVVGSGAIGVEFGYFYNSLGTKVTIVEFLPRVVPVEDEDISKELEKNLKKQgITVMTSSEVTSV 237
Cdd:PRK06292 157 LTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILSKE-FKIKLGAKVTSV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 238 DTSGNGVKAKVKTATGEAILEADVLLSAVGVAANIEGIGLETVGVKTDK-GKIVVDKFYKTNVDGVYAIGDCVPGQALAH 316
Cdd:PRK06292 236 EKSGDEKVEELEKGGKTETIEADYVLVATGRRPNTDGLGLENTGIELDErGRPVVDEHTQTSVPGIYAAGDVNGKPPLLH 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 317 VASKEGIICVENIAFGekkykhQPEALDYGNVPGCTYCYPEIASVGFTEKQAKEAGYEVKVGKFPLSASGKASAAGHTEG 396
Cdd:PRK06292 316 EAADEGRIAAENAAGD------VAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEVPFEAQGRARVMGKNDG 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 397 FVKVIFDAKYGEWLGTHMIGYNVTEIIAETVVGRKLETTYHEVLNSIHPHPTISESVKDAIEVAYGEAIH 466
Cdd:PRK06292 390 FVKVYADKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRTALRDLFSKLIH 459
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
2-467 |
2.32e-160 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 462.09 E-value: 2.32e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 2 AYDVIVVGSGPGGYVAAIRASQLGLKTAIIE-------KESLGGICLNWGCIPTKALLKSAQVFNDIQHA-KDYGIEASG 73
Cdd:PRK06327 4 QFDVVVIGAGPGGYVAAIRAAQLGLKVACIEawknpkgKPALGGTCLNVGCIPSKALLASSEEFENAGHHfADHGIHVDG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 74 -TPDFGAIVKRSRGVADKMSKGVQFLMKKNKIDVIMGFGTLKAKG----QVEVKGTDGKTtlVEGKHVILATGGRSRELP 148
Cdd:PRK06327 84 vKIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVGKTdagyEIKVTGEDETV--ITAKHVIIATGSEPRHLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 149 ALKQDGKKIIGYREAMVLPQQPKSIIVVGSGAIGVEFGYFYNSLGTKVTIVEFLPRVVPVEDEDISKELEKNLKKQGITV 228
Cdd:PRK06327 162 GVPFDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAAADEQVAKEAAKAFTKQGLDI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 229 MTSSEVTSVDTSGNGVKAKVKTATGEA-ILEADVLLSAVGVAANIEGIGLETVGVKTD-KGKIVVDKFYKTNVDGVYAIG 306
Cdd:PRK06327 242 HLGVKIGEIKTGGKGVSVAYTDADGEAqTLEVDKLIVSIGRVPNTDGLGLEAVGLKLDeRGFIPVDDHCRTNVPNVYAIG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 307 DCVPGQALAHVASKEGIICVENIAfgekkykHQPEALDYGNVPGCTYCYPEIASVGFTEKQAKEAGYEVKVGKFPLSASG 386
Cdd:PRK06327 322 DVVRGPMLAHKAEEEGVAVAERIA-------GQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLKAEGVEYKAGKFPFMANG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 387 KASAAGHTEGFVKVIFDAKYGEWLGTHMIGYNVTEIIAETVVGRKLETTYHEVLNSIHPHPTISESVKDAIEVAYGEAIH 466
Cdd:PRK06327 395 RALAMGEPDGFVKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEVWHEAALAVDKRPLH 474
|
.
gi 517457889 467 L 467
Cdd:PRK06327 475 F 475
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
3-454 |
3.38e-119 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 356.43 E-value: 3.38e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 3 YDVIVVGSGPGGYVAAIRASQLGLKTAIIEKESLGGICLNWGCIPTKALLKSAQVFNDIQHAKDYGIEASG--TPDFGAI 80
Cdd:PRK06370 6 YDAIVIGAGQAGPPLAARAAGLGMKVALIERGLLGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGGpvSVDFKAV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 81 VKRSRGVADKMSKGV-QFLMKKNKIDVIMGFGTLKAKGQVEVkgtDGKTtlVEGKHVILATGGRSR--ELPALKQdgkki 157
Cdd:PRK06370 86 MARKRRIRARSRHGSeQWLRGLEGVDVFRGHARFESPNTVRV---GGET--LRAKRIFINTGARAAipPIPGLDE----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 158 IGYR---EAMVLPQQPKSIIVVGSGAIGVEFGYFYNSLGTKVTIVEFLPRVVPVEDEDISKELEKNLKKQGITVMTSSEV 234
Cdd:PRK06370 156 VGYLtneTIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILEREGIDVRLNAEC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 235 TSVDTSGNGVKAKVKTATGEAILEADVLLSAVGVAANIEGIGLETVGVKTDK-GKIVVDKFYKTNVDGVYAIGDCVPGQA 313
Cdd:PRK06370 236 IRVERDGDGIAVGLDCNGGAPEITGSHILVAVGRVPNTDDLGLEAAGVETDArGYIKVDDQLRTTNPGIYAAGDCNGRGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 314 LAHVASKEGIICVENIAFGEkkykhqPEALDYGNVPGCTYCYPEIASVGFTEKQAKEAGYEVKVGKFPLSASGKASAAGH 393
Cdd:PRK06370 316 FTHTAYNDARIVAANLLDGG------RRKVSDRIVPYATYTDPPLARVGMTEAEARKSGRRVLVGTRPMTRVGRAVEKGE 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517457889 394 TEGFVKVIFDAKYGEWLGTHMIGYNVTEIIAETVVGRKLETTYHEVLNSIHPHPTISESVK 454
Cdd:PRK06370 390 TQGFMKVVVDADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIP 450
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
3-423 |
4.87e-81 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 258.16 E-value: 4.87e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 3 YDVIVVGSGPGGYVAAIRASQLGLKTAIIEKES-LGGICLNWGCIPTKALLKSA-QV--FNDIQHAKDYGIeaSGTPDFG 78
Cdd:PRK05249 6 YDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYRnVGGGCTHTGTIPSKALREAVlRLigFNQNPLYSSYRV--KLRITFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 79 AIVKRSRGVADKMSKGVQFLMKKNKIDVIMGFGTLKAKGQVEVKGTDGKTTLVEGKHVILATGGRSRELPALKQDGKKII 158
Cdd:PRK05249 84 DLLARADHVINKQVEVRRGQYERNRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATGSRPYRPPDVDFDHPRIY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 159 GYREAMVLPQQPKSIIVVGSGAIGVEFGYFYNSLGTKVTIVEFLPRVVPVEDEDISKELEKNLKKQGITVMTSSEVTSVD 238
Cdd:PRK05249 164 DSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSFLDDEISDALSYHLRDSGVTIRHNEEVEKVE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 239 TSGNGVKAKVKTatgEAILEADVLLSAVGVAANIEGIGLETVGVKTD-KGKIVVDKFYKTNVDGVYAIGDCVPGQALAHV 317
Cdd:PRK05249 244 GGDDGVIVHLKS---GKKIKADCLLYANGRTGNTDGLNLENAGLEADsRGQLKVNENYQTAVPHIYAVGDVIGFPSLASA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 318 ASKEGIICVENiAFGEKKyKHQPEALDYGnvpgcTYCYPEIASVGFTEKQAKEAG--YEVKVGKFPLSAsgKASAAGHTE 395
Cdd:PRK05249 321 SMDQGRIAAQH-AVGEAT-AHLIEDIPTG-----IYTIPEISSVGKTEQELTAAKvpYEVGRARFKELA--RAQIAGDNV 391
|
410 420
....*....|....*....|....*...
gi 517457889 396 GFVKVIFDAKYGEWLGTHMIGYNVTEII 423
Cdd:PRK05249 392 GMLKILFHRETLEILGVHCFGERATEII 419
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
3-451 |
1.22e-79 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 254.31 E-value: 1.22e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 3 YDVIVVGSGPGGYVAAIRASQLGLKTAIIEKESLGGICLNWGCIPTKALLKSAQVFNDIQH-AKDYGIEaSGTPDFG--- 78
Cdd:PRK06116 5 YDLIVIGGGSGGIASANRAAMYGAKVALIEAKRLGGTCVNVGCVPKKLMWYGAQIAEAFHDyAPGYGFD-VTENKFDwak 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 79 ------AIVKRSRGVADKMskgvqflMKKNKIDVIMGFGTLKAKGQVEVKGtdgktTLVEGKHVILATGGRSReLPALKq 152
Cdd:PRK06116 84 lianrdAYIDRLHGSYRNG-------LENNGVDLIEGFARFVDAHTVEVNG-----ERYTADHILIATGGRPS-IPDIP- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 153 dGKKI-IGYREAMVLPQQPKSIIVVGSGAIGVEFGYFYNSLGTKVTIV----EFLPRVvpveDEDISKELEKNLKKQGIT 227
Cdd:PRK06116 150 -GAEYgITSDGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFvrgdAPLRGF----DPDIRETLVEEMEKKGIR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 228 VMTSSEVTSVDTSGNGvKAKVKTATGEaILEADVLLSAVGVAANIEGIGLETVGVKTD-KGKIVVDKFYKTNVDGVYAIG 306
Cdd:PRK06116 225 LHTNAVPKAVEKNADG-SLTLTLEDGE-TLTVDCLIWAIGREPNTDGLGLENAGVKLNeKGYIIVDEYQNTNVPGIYAVG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 307 DCVPGQALAHVASKEGiicvenIAFGEKKYKHQPEA-LDYGNVPGCTYCYPEIASVGFTEKQAKEAGYE--VKV--GKFp 381
Cdd:PRK06116 303 DVTGRVELTPVAIAAG------RRLSERLFNNKPDEkLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEdnVKVyrSSF- 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517457889 382 lsASGKASAAGHTEG-FVKVIFDAKYGEWLGTHMIGYNVTEIIAETVVGRKLETTYHEVLNSIHPHPTISE 451
Cdd:PRK06116 376 --TPMYTALTGHRQPcLMKLVVVGKEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAE 444
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
3-457 |
3.30e-78 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 250.64 E-value: 3.30e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 3 YDVIVVGSGPGGYVAAIRASqlGLKTAIIEKESLGGICLNWGCIPTKALLKSAQVFNDIQHAKDYGIEAS-GTPDFGAIV 81
Cdd:PRK07846 2 YDLIIIGTGSGNSILDERFA--DKRIAIVEKGTFGGTCLNVGCIPTKMFVYAADVARTIREAARLGVDAElDGVRWPDIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 82 KRSRGVADKMSK-GVQFLMKKN-KIDVIMGFGTLKAKGQVEVkgtdGKTTLVEGKHVILATGGRSRELPALKQDGkkiIG 159
Cdd:PRK07846 80 SRVFGRIDPIAAgGEEYRGRDTpNIDVYRGHARFIGPKTLRT----GDGEEITADQVVIAAGSRPVIPPVIADSG---VR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 160 YR---EAMVLPQQPKSIIVVGSGAIGVEFGYFYNSLGTKVTIVEFLPRVVPVEDEDISKELeKNLKKQGITVMTSSEVTS 236
Cdd:PRK07846 153 YHtsdTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLDDDISERF-TELASKRWDVRLGRNVVG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 237 VDTSGNGVKAkvkTATGEAILEADVLLSAVGVAANIEGIGLETVGVKT-DKGKIVVDKFYKTNVDGVYAIGD-CVPGQaL 314
Cdd:PRK07846 232 VSQDGSGVTL---RLDDGSTVEADVLLVATGRVPNGDLLDAAAAGVDVdEDGRVVVDEYQRTSAEGVFALGDvSSPYQ-L 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 315 AHVASKEGIICVENIAFGEkkykhQPEALDYGNVPGCTYCYPEIASVGFTEKQAKEAGYE--VKVGKFPLSASGkaSAAG 392
Cdd:PRK07846 308 KHVANHEARVVQHNLLHPD-----DLIASDHRFVPAAVFTHPQIASVGLTENEARAAGLDitVKVQNYGDVAYG--WAME 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517457889 393 HTEGFVKVIFDAKYGEWLGTHMIGYNVTEIIAETVVGRKLETTYHEVLNSIH-PHPTISESVKDAI 457
Cdd:PRK07846 381 DTTGFVKLIADRDTGRLLGAHIIGPQASTLIQPLIQAMSFGLDAREMARGQYwIHPALPEVVENAL 446
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
3-322 |
4.20e-76 |
|
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: 240.30 E-value: 4.20e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 3 YDVIVVGSGPGGYVAAIRASQLGLKTAIIEkesLGGICLNWGCIPTKALLKSAQVFNDIQHAKDygieasgtpdfgaIVK 82
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIE---DEGTCPYGGCVLSKALLGAAEAPEIASLWAD-------------LYK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 83 RSRGVADKMSKGVQFLMKKNKIDVIMGFGTLKAKGQVEVKGTDgkttlVEGKHVILATGGRSREL--PALKQ---DGKKI 157
Cdd:pfam07992 65 RKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELVDGDGET-----ITYDRLVIATGARPRLPpiPGVELnvgFLVRT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 158 IGYREAMVLPQQPKSIIVVGSGAIGVEFGYFYNSLGTKVTIVEFLPRVVPVEDEDISKELEKNLKKQGITVMTSSEVTSV 237
Cdd:pfam07992 140 LDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 238 DtsGNGVKAKVKTATGEAIlEADVLLSAVGVAANIEgiGLETVGVKTDK-GKIVVDKFYKTNVDGVYAIGDC-VPGQALA 315
Cdd:pfam07992 220 I--GDGDGVEVILKDGTEI-DADLVVVAIGRRPNTE--LLEAAGLELDErGGIVVDEYLRTSVPGIYAAGDCrVGGPELA 294
|
....*..
gi 517457889 316 HVASKEG 322
Cdd:pfam07992 295 QNAVAQG 301
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
5-401 |
1.41e-74 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 241.69 E-value: 1.41e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 5 VIVVGSGPGGYVAAIRASQLGLKTAIIEKESLGGICLNWGCIPTKALLKSAQVFNDIQHAKDYGIEASGTP----DFGAI 80
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIERDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRFIDDGearvDLPAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 81 VKRSRGVADKMSKGVQFLMKKNKIDVIMGFGTLKAKGQ----VEVKGTDGKTTLVEGKHVILATGGRSRELPALKQDGKK 156
Cdd:PRK07845 84 NARVKALAAAQSADIRARLEREGVRVIAGRGRLIDPGLgphrVKVTTADGGEETLDADVVLIATGASPRILPTAEPDGER 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 157 IIGYREAMVLPQQPKSIIVVGSGAIGVEFGYFYNSLGTKVTIVEFLPRVVPVEDEDISKELEKNLKKQGITVMTSSEVTS 236
Cdd:PRK07845 164 ILTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPGEDADAAEVLEEVFARRGMTVLKRSRAES 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 237 VDTSGNGVkaKVKTATGEAIlEADVLLSAVGVAANIEGIGLETVGVKTDK-GKIVVDKFYKTNVDGVYAIGDCVPGQALA 315
Cdd:PRK07845 244 VERTGDGV--VVTLTDGRTV-EGSHALMAVGSVPNTAGLGLEEAGVELTPsGHITVDRVSRTSVPGIYAAGDCTGVLPLA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 316 HVASKEGIICVENiAFGEKKykhQPeaLDYGNVPGCTYCYPEIASVGFTEKQAKEAGYEVKVGKFPLSASGKASAAGHTE 395
Cdd:PRK07845 321 SVAAMQGRIAMYH-ALGEAV---SP--LRLKTVASNVFTRPEIATVGVSQAAIDSGEVPARTVMLPLATNPRAKMSGLRD 394
|
....*.
gi 517457889 396 GFVKVI 401
Cdd:PRK07845 395 GFVKLF 400
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
2-455 |
1.43e-65 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 217.31 E-value: 1.43e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 2 AYDVIVVGSGPGGYVAAIRASQLGLKTAIIEKESL--GGICLNWGCIPTKALLKSAQ---VFNDIQHAKDygieasgtpd 76
Cdd:PRK07251 3 TYDLIVIGFGKAGKTLAAKLASAGKKVALVEESKAmyGGTCINIGCIPTKTLLVAAEknlSFEQVMATKN---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 77 fgAIVKRSRGVADKMSKGvqflmkkNKIDVIMGFGTLKAKGQVEVKGTDGKTTLvEGKHVILATGGRSRELP--ALKqDG 154
Cdd:PRK07251 73 --TVTSRLRGKNYAMLAG-------SGVDLYDAEAHFVSNKVIEVQAGDEKIEL-TAETIVINTGAVSNVLPipGLA-DS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 155 KKIIGYREAMVLPQQPKSIIVVGSGAIGVEFGYFYNSLGTKVTIVEFLPRVVPVEDEDISKELEKNLKKQGITVMTSSEV 234
Cdd:PRK07251 142 KHVYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYMEEDGITFLLNAHT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 235 TSVDTSGNGVkakVKTATGEAiLEADVLLSAVGVAANIEGIGLETVGVK-TDKGKIVVDKFYKTNVDGVYAIGDCVPGQA 313
Cdd:PRK07251 222 TEVKNDGDQV---LVVTEDET-YRFDALLYATGRKPNTEPLGLENTDIElTERGAIKVDDYCQTSVPGVFAVGDVNGGPQ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 314 LAHVASKEGIIcVENIAFGEKKYKHQpealDYGNVPGCTYCYPEIASVGFTEKQAKEAGYEVKVGKFPLSASGKASAAGH 393
Cdd:PRK07251 298 FTYISLDDFRI-VFGYLTGDGSYTLE----DRGNVPTTMFITPPLSQVGLTEKEAKEAGLPYAVKELLVAAMPRAHVNND 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517457889 394 TEGFVKVIFDAKYGEWLGTHMIGYNVTEIIAETVVGRKLETTYHEVLNSIHPHPTISESVKD 455
Cdd:PRK07251 373 LRGAFKVVVNTETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAENLND 434
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
3-466 |
5.45e-62 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 213.24 E-value: 5.45e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 3 YDVIVVGSGPGGYVAAIRASQLGLKTAII--EKESLGGICLNWGCIPTKALLKSAQVFNDIQ---HAKDYGIEASGTP-- 75
Cdd:PTZ00153 117 YDVGIIGCGVGGHAAAINAMERGLKVIIFtgDDDSIGGTCVNVGCIPSKALLYATGKYRELKnlaKLYTYGIYTNAFKng 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 76 -----------------DFGAIVKRSRGVADKMSKGVQFLMKKNKIDVIMGFGTL-KAKGQVEVKGT-----DGKTTLVe 132
Cdd:PTZ00153 197 kndpvernqlvadtvqiDITKLKEYTQSVIDKLRGGIENGLKSKKFCKNSEHVQViYERGHIVDKNTiksekSGKEFKV- 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 133 gKHVILATGGRSRELPALKQDGKKIIGYREAMVLPQQPKSIIVVGSGAIGVEFGYFYNSLGTKVTIVEFLPRVVPVEDED 212
Cdd:PTZ00153 276 -KNIIIATGSTPNIPDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSPQLLPLLDAD 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 213 ISKELEKN-LKKQGITVMTSSEVTSVDTSGNGV--------------KAKVKTATGEAILEADVLLSAVGVAANIEGIGL 277
Cdd:PTZ00153 355 VAKYFERVfLKSKPVRVHLNTLIEYVRAGKGNQpviighserqtgesDGPKKNMNDIKETYVDSCLVATGRKPNTNNLGL 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 278 ETVGVKTDKGKIVVDKFYKTN------VDGVYAIGDCVPGQALAHVASKEGIICVENIAFGEKK------YKHQPEALDY 345
Cdd:PTZ00153 435 DKLKIQMKRGFVSVDEHLRVLredqevYDNIFCIGDANGKQMLAHTASHQALKVVDWIEGKGKEnvninvENWASKPIIY 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 346 GNVPGCTYCYPEIASVGFTEKQAKEAGYEVKVGK------------------FPLSAS------GKASAAGHTEGFVKVI 401
Cdd:PTZ00153 515 KNIPSVCYTTPELAFIGLTEKEAKELYPPDNVGVeisfykanskvlcennisFPNNSKnnsynkGKYNTVDNTEGMVKIV 594
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517457889 402 FDAKYGEWLGTHMIGYNVTEIIAETVVGRKLETTYHEVLNSIHPHPTISESVKDAIEVAYGEAIH 466
Cdd:PTZ00153 595 YLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDAAFKAIAGVRTH 659
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
3-451 |
2.74e-57 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 196.96 E-value: 2.74e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 3 YDVIVVGSGPGGYVAAIRASQLGLKTAIIE-------KESLGGI---CLNWGCIPTKALLKSAQVFNDIQHAKDYGIEAS 72
Cdd:PLN02507 26 FDLFVIGAGSGGVRAARFSANFGAKVGICElpfhpisSESIGGVggtCVIRGCVPKKILVYGATFGGEFEDAKNYGWEIN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 73 GTPDFG---AIVKRSRGVAdKMSKGVQFLMKKNKIDVIMGFGTLKAKGQVEVKGTDGKTTLVEGKHVILATGGRSRElPA 149
Cdd:PLN02507 106 EKVDFNwkkLLQKKTDEIL-RLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRYTAKHILIATGSRAQR-PN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 150 LKqdGKKI-IGYREAMVLPQQPKSIIVVGSGAIGVEFGYFYNSLGTKVTIveFLPRVVPVE--DEDISKELEKNLKKQGI 226
Cdd:PLN02507 184 IP--GKELaITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDL--FFRKELPLRgfDDEMRAVVARNLEGRGI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 227 TVMTSSEVTSVDTSGNGVKakVKTATGEAILeADVLLSAVGVAANIEGIGLETVGVKTDK-GKIVVDKFYKTNVDGVYAI 305
Cdd:PLN02507 260 NLHPRTNLTQLTKTEGGIK--VITDHGEEFV-ADVVLFATGRAPNTKRLNLEAVGVELDKaGAVKVDEYSRTNIPSIWAI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 306 GDCVPGQALAHVASKEGIiCVENIAFGekkykHQPEALDYGNVPGCTYCYPEIASVGFTEKQA-KEAGYEVKVgkFPLSA 384
Cdd:PLN02507 337 GDVTNRINLTPVALMEGT-CFAKTVFG-----GQPTKPDYENVACAVFCIPPLSVVGLSEEEAvEQAKGDILV--FTSSF 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517457889 385 SG-KASAAGHTE-GFVKVIFDAKYGEWLGTHMIGYNVTEIIAETVVGRKLETTYHEVLNSIHPHPTISE 451
Cdd:PLN02507 409 NPmKNTISGRQEkTVMKLIVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAE 477
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
2-453 |
4.87e-57 |
|
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: 196.35 E-value: 4.87e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 2 AYDVIVVGSGPGGYVAAIRASQL-GLKTAIIEKE---------SLGGICLNWGCIPTKALLKSAQVFNDIQHAKDYGIEA 71
Cdd:TIGR01423 3 AFDLVVIGAGSGGLEAGWNAATLyKKRVAVVDVQthhgppfyaALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGWEF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 72 SGT---PDFGAIVKRSRGVADKMSKGVQFLMKKNK-IDVIMGFGTLKAKGQVEVK-GTDGKTTLVE---GKHVILATGGR 143
Cdd:TIGR01423 83 DRSsvkANWKALIAAKNKAVLDINKSYEGMFADTEgLTFFLGWGALEDKNVVLVReSADPKSAVKErlqAEHILLATGSW 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 144 SrELPALKQDgKKIIGYREAMVLPQQPKSIIVVGSGAIGVEF-GYF--YNSLGTKVTIVEFLPRVVPVEDEDISKELEKN 220
Cdd:TIGR01423 163 P-QMLGIPGI-EHCISSNEAFYLDEPPRRVLTVGGGFISVEFaGIFnaYKPRGGKVTLCYRNNMILRGFDSTLRKELTKQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 221 LKKQGITVMTSSEVTSVDTSGNGVKaKVKTATGeAILEADVLLSAVGVAANIEGIGLETVGVK-TDKGKIVVDKFYKTNV 299
Cdd:TIGR01423 241 LRANGINIMTNENPAKVTLNADGSK-HVTFESG-KTLDVDVVMMAIGRVPRTQTLQLDKVGVElTKKGAIQVDEFSRTNV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 300 DGVYAIGDCVPGQALAHVASKEGIICVENIaFGEKkykhqPEALDYGNVPGCTYCYPEIASVGFTEKQAKEAGYEVKV-- 377
Cdd:TIGR01423 319 PNIYAIGDVTDRVMLTPVAINEGAAFVDTV-FGNK-----PRKTDHTRVASAVFSIPPIGTCGLVEEDAAKKFEKVAVye 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517457889 378 GKF-PLSASgkASAAGHTEGFVKVIFDAKYGEWLGTHMIGYNVTEIIAETVVGRKLETTYHEVLNSIHPHPTISESV 453
Cdd:TIGR01423 393 SSFtPLMHN--ISGSKYKKFVAKIVTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAEEL 467
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
3-452 |
4.52e-54 |
|
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member of the pyridine nucleotide disulfide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly, where SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily, Cys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-term arm of the protein is proposed to allow broad substrate specificity.
Pssm-ID: 273624 [Multi-domain] Cd Length: 484 Bit Score: 188.14 E-value: 4.52e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 3 YDVIVVGSGPGGYVAAIRASQLGLKTAIIE---------KESLGGICLNWGCIPTKALLKSAQVFNDIQHAKDYG--IEA 71
Cdd:TIGR01438 3 YDLIVIGGGSGGLAAAKEAAAYGAKVMLLDfvtptplgtRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGwkVEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 72 SGTPDFGAIVKRSRGVADKMSKGVQFLMKKNKIDVIMGFGTLKAKGQVEVKGTDGKTTLVEGKHVILATGGRSReLPALK 151
Cdd:TIGR01438 83 TVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERPR-YPGIP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 152 QDGKKIIGYREAMVLPQQPKSIIVVGSGAIGVEFGYFYNSLGTKVTIvefLPRVVPVE--DEDISKELEKNLKKQGITVM 229
Cdd:TIGR01438 162 GAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTV---MVRSILLRgfDQDCANKVGEHMEEHGVKFK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 230 TSSEVTSVDTSGNGVKAKVKTATGEAILEADVLLSAVGVAANIEGIGLETVGVKTDK--GKIVVDKFYKTNVDGVYAIGD 307
Cdd:TIGR01438 239 RQFVPIKVEQIEAKVLVEFTDSTNGIEEEYDTVLLAIGRDACTRKLNLENVGVKINKktGKIPADEEEQTNVPYIYAVGD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 308 CVPG-QALAHVASKEGIIcveniaFGEKKYKHQPEALDYGNVPGCTYCYPEIASVGFTEKQA----KEAGYEVKVGKF-P 381
Cdd:TIGR01438 319 ILEDkPELTPVAIQAGRL------LAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAvekfGEENVEVFHSYFwP 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517457889 382 LSASgKASAAGHTEGFVKVIFDAKYGE-WLGTHMIGYNVTEIIAETVVGRKLETTYHEVLNSIHPHPTISES 452
Cdd:TIGR01438 393 LEWT-IPSRDNHNKCYAKLVCNKKENErVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEV 463
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
1-453 |
2.55e-52 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 185.20 E-value: 2.55e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 1 MAYDVIVVGSGPGGYVAAIRASQLGLKTAIIEKESLGGICLNWGCIPTKALLKSAQVFNDIQHAKDYGIEASGTPDFGAI 80
Cdd:PTZ00058 47 MVYDLIVIGGGSGGMAAARRAARNKAKVALVEKDYLGGTCVNVGCVPKKIMFNAASIHDILENSRHYGFDTQFSFNLPLL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 81 VKRSRGVADKMSKGVQFLMKKNKIDVIMGFGTLKAKGQVEVKGT-----------DGKTTLV-------------EGKHV 136
Cdd:PTZ00058 127 VERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLIKKVsqvdgeadesdDDEVTIVsagvsqlddgqviEGKNI 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 137 ILATGGRSrELPALKqdGKKIIGYREAMVLPQQPKSIIVVGSGAIGVEFGYFYNSLGTKVTIVEFLPRVVPVEDEDISKE 216
Cdd:PTZ00058 207 LIAVGNKP-IFPDVK--GKEFTISSDDFFKIKEAKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLRKFDETIINE 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 217 LEKNLKKQGITVMTSS---EVTSVDTSGngvkAKVKTATGEAILEADVLLSAVGVAANIEGIGLETVGVKTDKGKIVVDK 293
Cdd:PTZ00058 284 LENDMKKNNINIITHAnveEIEKVKEKN----LTIYLSDGRKYEHFDYVIYCVGRSPNTEDLNLKALNIKTPKGYIKVDD 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 294 FYKTNVDGVYAIGDCV--------PGQALAHVASKEGIICVENIAFGEKKYKHQ--PEAL------------------DY 345
Cdd:PTZ00058 360 NQRTSVKHIYAVGDCCmvkknqeiEDLNLLKLYNEEPYLKKKENTSGESYYNVQltPVAInagrlladrlfgpfsrttNY 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 346 GNVPGCTYCYPEIASVGFTEKQAKEA-GYE-VKV----------GKFPLSASGKASAaghtegFVKVIFDAKYGEWLGTH 413
Cdd:PTZ00058 440 KLIPSVIFSHPPIGTIGLSEQEAIDIyGKEnVKIyesrftnlffSVYDMDPAQKEKT------YLKLVCVGKEELIKGLH 513
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 517457889 414 MIGYNVTEIIAETVVGRKLETTYHEVLNSIHPHPTISESV 453
Cdd:PTZ00058 514 IVGLNADEILQGFAVALKMNATKADFDETIPIHPTAAEEF 553
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
3-455 |
1.00e-51 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 180.98 E-value: 1.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 3 YDVIVVGSGPGGYVAAIRASQLGLKTAIIEKES--LGGICLNWGCIPTKALLKSAQvfndiQHAkdygieasgtpDFGAI 80
Cdd:PRK08010 4 YQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNamYGGTCINIGCIPTKTLVHDAQ-----QHT-----------DFVRA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 81 VKRSRGVadkmskgVQFLMKKN--------KIDVIMGFGTLKAKGQVEVKGTDGKTTLvEGKHVILATGGRSrELPALK- 151
Cdd:PRK08010 68 IQRKNEV-------VNFLRNKNfhnladmpNIDVIDGQAEFINNHSLRVHRPEGNLEI-HGEKIFINTGAQT-VVPPIPg 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 152 -QDGKKIIGYREAMVLPQQPKSIIVVGSGAIGVEFGYFYNSLGTKVTIVEFLPRVVPVEDEDISKELEKNLKKQGITVMT 230
Cdd:PRK08010 139 iTTTPGVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIIL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 231 SSEVTSVDTSGNGVKAKvktaTGEAILEADVLLSAVGVAANIEGIGLETVGVK-TDKGKIVVDKFYKTNVDGVYAIGDCV 309
Cdd:PRK08010 219 NAHVERISHHENQVQVH----SEHAQLAVDALLIASGRQPATASLHPENAGIAvNERGAIVVDKYLHTTADNIWAMGDVT 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 310 PGQALAHVASKEGIIcVENIAFGEKKYKHQpealDYGNVPGCTYCYPEIASVGFTEKQAKEAGYEVKVGKFPLSASGKAS 389
Cdd:PRK08010 295 GGLQFTYISLDDYRI-VRDELLGEGKRSTD----DRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRAR 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517457889 390 AAGHTEGFVKVIFDAKYGEWLGTHMIGYNVTEI--IAETVVGRKLetTYHEVLNSIHPHPTISESVKD 455
Cdd:PRK08010 370 VMNDTRGVLKAIVDNKTQRILGASLLCVDSHEMinIVKMVMDAGL--PYSILRDQIFTHPSMSESLND 435
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
5-454 |
2.00e-49 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 177.27 E-value: 2.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 5 VIVVGSGPGGYVAAIRASQLGLKTAIIEKESLGGICLNWGCIPTKALLKSAQvfndIQHAK-----DYGIEA-SGTPDFG 78
Cdd:PRK13748 101 VAVIGSGGAAMAAALKAVEQGARVTLIERGTIGGTCVNVGCVPSKIMIRAAH----IAHLRrespfDGGIAAtVPTIDRS 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 79 AIVKRSRGVADKM--SKGVQFLMKKNKIDVIMGFGTLKAKGQVEVKGTDGKTTLVEGKHVILATgGRSRELPALkqDGKK 156
Cdd:PRK13748 177 RLLAQQQARVDELrhAKYEGILDGNPAITVLHGEARFKDDQTLIVRLNDGGERVVAFDRCLIAT-GASPAVPPI--PGLK 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 157 IIGY---REAMVLPQQPKSIIVVGSGAIGVEFGYFYNSLGTKVTIV---EFLPRvvpvEDEDISKELEKNLKKQGITVMT 230
Cdd:PRK13748 254 ETPYwtsTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILarsTLFFR----EDPAIGEAVTAAFRAEGIEVLE 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 231 SSEVTSVDTSGNgvKAKVKTATGEaiLEADVLLSAVGVAANIEGIGLETVGVKTDK-GKIVVDKFYKTNVDGVYAIGDCV 309
Cdd:PRK13748 330 HTQASQVAHVDG--EFVLTTGHGE--LRADKLLVATGRAPNTRSLALDAAGVTVNAqGAIVIDQGMRTSVPHIYAAGDCT 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 310 PGQALAHVASKEGIICVENIAFGEKkykhqpeALDYGNVPGCTYCYPEIASVGFTEKQAKEAGYEVKVGKFPLSASGKAS 389
Cdd:PRK13748 406 DQPQFVYVAAAAGTRAAINMTGGDA-------ALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRTLTLDNVPRAL 478
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517457889 390 AAGHTEGFVKVIFDAKYGEWLGTHMIGYNVTEIIAETVVGRKLETTYHEVLNSIHPHPTISESVK 454
Cdd:PRK13748 479 ANFDTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAALAIRNRMTVQELADQLFPYLTMVEGLK 543
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
3-451 |
4.32e-45 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 165.43 E-value: 4.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 3 YDVIVVGSGPGGYVAAIRASQLGLKTAIIE-------KESLGGI---CLNWGCIPTKALLKSAQVFNDIQHAKDYGIEAS 72
Cdd:PLN02546 80 FDLFTIGAGSGGVRASRFASNFGASAAVCElpfatisSDTLGGVggtCVLRGCVPKKLLVYASKYSHEFEESRGFGWKYE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 73 GTP--DFGAIVKRSRGVADKMSKGVQFLMKKNKIDVIMGFGTLKAKGQVEVkgtDGKttLVEGKHVILATGGRSR--ELP 148
Cdd:PLN02546 160 TEPkhDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDV---DGK--LYTARNILIAVGGRPFipDIP 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 149 ALKQdgkkIIGYREAMVLPQQPKSIIVVGSGAIGVEFGYFYNSLGTKVTIVEFLPRVVPVEDEDISKELEKNLKKQGITV 228
Cdd:PLN02546 235 GIEH----AIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKKVLRGFDEEVRDFVAEQMSLRGIEF 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 229 MTSSEVTSVDTSGNGVKAkVKTATGEAILEADVLLsAVGVAANIEGIGLETVGVKTDK-GKIVVDKFYKTNVDGVYAIGD 307
Cdd:PLN02546 311 HTEESPQAIIKSADGSLS-LKTNKGTVEGFSHVMF-ATGRKPNTKNLGLEEVGVKMDKnGAIEVDEYSRTSVPSIWAVGD 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 308 CVPGQALAHVASKEGiicvenIAFGEKKYKHQPEALDYGNVPGCTYCYPEIASVGFTEKQA-KEAG-YEVKVGKF-PLsa 384
Cdd:PLN02546 389 VTDRINLTPVALMEG------GALAKTLFGNEPTKPDYRAVPSAVFSQPPIGQVGLTEEQAiEEYGdVDVFTANFrPL-- 460
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517457889 385 sgKASAAGHTEG-FVKVIFDAKYGEWLGTHMIGYNVTEIIAETVVGRKLETTYHEVLNSIHPHPTISE 451
Cdd:PLN02546 461 --KATLSGLPDRvFMKLIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAE 526
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
96-340 |
1.17e-37 |
|
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: 139.95 E-value: 1.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 96 QFLMKKNkIDVIMgfgtlkakgQVEVKG--TDGKT-TLVEGKHV-----ILATGGRSRELP----------ALK--QDGK 155
Cdd:COG0446 44 ESFERKG-IDVRT---------GTEVTAidPEAKTvTLRDGETLsydklVLATGARPRPPPipgldlpgvfTLRtlDDAD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 156 KIIgyreAMVLPQQPKSIIVVGSGAIGVEFGYFYNSLGTKVTIVEFLPRVVPVEDEDISKELEKNLKKQGITVMTSSEVT 235
Cdd:COG0446 114 ALR----EALKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 236 SVDTSGngvKAKVKTATGEAIlEADVLLSAVGVAANIE---GIGLETvgvkTDKGKIVVDKFYKTNVDGVYAIGDCV--- 309
Cdd:COG0446 190 AIDGDD---KVAVTLTDGEEI-PADLVVVAPGVRPNTElakDAGLAL----GERGWIKVDETLQTSDPDVYAAGDCAevp 261
|
250 260 270
....*....|....*....|....*....|....*...
gi 517457889 310 -------PGQALAHVASKEGIICVENIAFGEKKYKHQP 340
Cdd:COG0446 262 hpvtgktVYIPLASAANKQGRVAAENILGGPAPFPGLG 299
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
348-456 |
1.36e-37 |
|
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: 133.06 E-value: 1.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 348 VPGCTYCYPEIASVGFTEKQAKEAGYEVKVGKFPLSASGKASAAGHTEGFVKVIFDAKYGEWLGTHMIGYNVTEIIAETV 427
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGEVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQEAA 80
|
90 100
....*....|....*....|....*....
gi 517457889 428 VGRKLETTYHEVLNSIHPHPTISESVKDA 456
Cdd:pfam02852 81 LAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
3-455 |
1.16e-34 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 135.34 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 3 YDVIVVGSGPGGYVAAIRASQLGLKTAIIE---------KESLGGICLNWGCIPTKALLKSAQVFNDIQH-AKDYGIEAS 72
Cdd:PTZ00052 6 YDLVVIGGGSGGMAAAKEAAAHGKKVALFDyvkpstqgtKWGLGGTCVNVGCVPKKLMHYAANIGSIFHHdSQMYGWKTS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 73 GTPDFGAIVKRSRGVADKMSKGVQFLMKKNKIDVIMGFGTLKAKGQVEVkGTDGKTTLVEGKHVILATGGRsrelPALKQ 152
Cdd:PTZ00052 86 SSFNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTVSY-GDNSQEETITAKYILIATGGR----PSIPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 153 DGKKIIGYR----EAMVLPQQPKSIIVVGSGAIGVEFGYFYNSLGTKVTIVEflpRVVPVE--DEDISKELEKNLKKQGi 226
Cdd:PTZ00052 161 DVPGAKEYSitsdDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAV---RSIPLRgfDRQCSEKVVEYMKEQG- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 227 tVMTSSEVTSVDTSGNGVKAKVKTATGeAILEADVLLSAVGVAANIEGIGLETVGVKTDK-GKIVVDKfYKTNVDGVYAI 305
Cdd:PTZ00052 237 -TLFLEGVVPINIEKMDDKIKVLFSDG-TTELFDTVLYATGRKPDIKGLNLNAIGVHVNKsNKIIAPN-DCTNIPNIFAV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 306 GDCVPGQA-LAHVASKEGIIcveniaFGEKKYKHQPEALDYGNVPGCTYCYPEIASVGFTEKQAKEAGYEVKVGKFPLSA 384
Cdd:PTZ00052 314 GDVVEGRPeLTPVAIKAGIL------LARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQEF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 385 SGKASAAGHTEGFVK------------------VIFDAKYGEWLGTHMIGYNVTEIIAETVVGRKLETTYHEVLNSIHPH 446
Cdd:PTZ00052 388 NTLEIAAVHREKHERarkdeydfdvssnclaklVCVKSEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIH 467
|
....*....
gi 517457889 447 PTISESVKD 455
Cdd:PTZ00052 468 PTDAEVFMN 476
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
135-338 |
1.77e-30 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 121.79 E-value: 1.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 135 HVILATGGRSRELPALKQDGKKIIGYR-----EAMV-LPQQPKSIIVVGSGAIGVEFGYFYNSLGTKVTIVEFLPRVVP- 207
Cdd:COG1251 101 KLVLATGSRPRVPPIPGADLPGVFTLRtlddaDALRaALAPGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPr 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 208 VEDEDISKELEKNLKKQGITVMTSSEVTSVDTSGNGVKakVKTATGEAIlEADVLLSAVGVAANIEGigLETVGVKTDKG 287
Cdd:COG1251 181 QLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTG--VRLADGEEL-PADLVVVAIGVRPNTEL--ARAAGLAVDRG 255
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 288 kIVVDKFYKTNVDGVYAIGDC--VPGQ-----ALAHVAS--KEGIICVENIAFGEKKYKH 338
Cdd:COG1251 256 -IVVDDYLRTSDPDIYAAGDCaeHPGPvygrrVLELVAPayEQARVAAANLAGGPAAYEG 314
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
3-330 |
3.25e-29 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 116.37 E-value: 3.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 3 YDVIVVGSGPGGYVAAIRASQLGLKTAIIEKESLGGICLNWGCI------PTK----ALLKSAQvfndiQHAKDYGIEas 72
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQLATTKEIenypgfPEGisgpELAERLR-----EQAERFGAE-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 73 gtpdfgaivkrsrgvadkmskgvqFLMKK-NKIDvimgfgtlKAKGQVEVKGTDGKTtlVEGKHVILATGGRSRELPAlk 151
Cdd:COG0492 74 ------------------------ILLEEvTSVD--------KDDGPFRVTTDDGTE--YEAKAVIIATGAGPRKLGL-- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 152 qDG-KKIIGYR-------EAMVLPQQPksIIVVGSGAIGVEFGYFYNSLGTKVTIVeflprvVPVEDEDISKELEKNLKK 223
Cdd:COG0492 118 -PGeEEFEGRGvsycatcDGFFFRGKD--VVVVGGGDSALEEALYLTKFASKVTLI------HRRDELRASKILVERLRA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 224 -QGITVMTSSEVTSVDTSGNGVKAKVK-TATGEA-ILEADVLLSAVGVAAN---IEGIGLETvgvkTDKGKIVVDKFYKT 297
Cdd:COG0492 189 nPKIEVLWNTEVTEIEGDGRVEGVTLKnVKTGEEkELEVDGVFVAIGLKPNtelLKGLGLEL----DEDGYIVVDEDMET 264
|
330 340 350
....*....|....*....|....*....|....*.
gi 517457889 298 NVDGVYAIGDCVPG---QALahVASKEGIICVENIA 330
Cdd:COG0492 265 SVPGVFAAGDVRDYkyrQAA--TAAGEGAIAALSAA 298
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
120-418 |
5.82e-24 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 103.97 E-value: 5.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 120 EVKGTDGKTTLVEGKHV-------------ILATGGRSReLPALK-------------QDGKKIigyREAMVLPQQpKSI 173
Cdd:PRK09564 78 EVVKVDAKNKTITVKNLktgsifndtydklMIATGARPI-IPPIKninlenvytlksmEDGLAL---KELLKDEEI-KNI 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 174 IVVGSGAIGVEFGYFYNSLGTKVTIVEFLPRVVP-VEDEDISKELEKNLKKQGITVMTSSEVTSVDTSGNGVKakVKTAT 252
Cdd:PRK09564 153 VIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRILPdSFDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEG--VVTDK 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 253 GEaiLEADVLLSAVGVAANIEGigLETVGVKTDK-GKIVVDKFYKTNVDGVYAIGDC------VPGQ----ALAHVASKE 321
Cdd:PRK09564 231 GE--YEADVVIVATGVKPNTEF--LEDTGLKTLKnGAIIVDEYGETSIENIYAAGDCatiyniVSNKnvyvPLATTANKL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 322 GIICVENIAFGEKKYKHQ-----PEALDYgnvpgctycypEIASVGFTEKQAKEAGYEVKVgKFPLSASGKASAAGHTEG 396
Cdd:PRK09564 307 GRMVGENLAGRHVSFKGTlgsacIKVLDL-----------EAARTGLTEEEAKKLGIDYKT-VFIKDKNHTNYYPGQEDL 374
|
330 340
....*....|....*....|..
gi 517457889 397 FVKVIFDAKYGEWLGTHMIGYN 418
Cdd:PRK09564 375 YVKLIYEADTKVILGGQIIGKK 396
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
98-330 |
1.12e-22 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 99.44 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 98 LMKKNKIDVIMGfgtlkakgqvEVKG--TDGKT-TLVEGKHV-----ILATGGRSR--ELPALKQDG------------- 154
Cdd:COG1252 65 LLRRAGVRFIQG----------EVTGidPEARTvTLADGRTLsydylVIATGSVTNffGIPGLAEHAlplktledalalr 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 155 KKIIGYREAMvLPQQPKSIIVVGSGAIGVEF-----------GYFYNSLG--TKVTIVEFLPRVVPVEDEDISKELEKNL 221
Cdd:COG1252 135 ERLLAAFERA-ERRRLLTIVVVGGGPTGVELagelaellrklLRYPGIDPdkVRITLVEAGPRILPGLGEKLSEAAEKEL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 222 KKQGITVMTSSEVTSVDtsgngvKAKVKTATGEAIlEADVLLSAVGVAAN--IEGIGLETvgvkTDKGKIVVDKFYKT-N 298
Cdd:COG1252 214 EKRGVEVHTGTRVTEVD------ADGVTLEDGEEI-PADTVIWAAGVKAPplLADLGLPT----DRRGRVLVDPTLQVpG 282
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 517457889 299 VDGVYAIGDC--VPGQ------ALAHVASKEGIICVENIA 330
Cdd:COG1252 283 HPNVFAIGDCaaVPDPdgkpvpKTAQAAVQQAKVLAKNIA 322
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
112-315 |
6.92e-22 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 96.91 E-value: 6.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 112 TLKAKGQVEVKGTDGKTTLVEGK-----HVILATGGRSReLPALKQDGKKII-----GYREAMVLPQQPKSIIVVGSGAI 181
Cdd:PRK04965 74 RLFPHTWVTDIDAEAQVVKSQGNqwqydKLVLATGASAF-VPPIPGRELMLTlnsqqEYRAAETQLRDAQRVLVVGGGLI 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 182 GVEFGYFYNSLGTKVTIVE----FLPRVVPVEdedISKELEKNLKKQGITVMTSSEVTSVDTSGNGVkaKVKTATGEAIl 257
Cdd:PRK04965 153 GTELAMDLCRAGKAVTLVDnaasLLASLMPPE---VSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGI--RATLDSGRSI- 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517457889 258 EADVLLSAVGVAANiegIGLET-VGVKTDKGkIVVDKFYKTNVDGVYAIGDC--VPGQALA 315
Cdd:PRK04965 227 EVDAVIAAAGLRPN---TALARrAGLAVNRG-IVVDSYLQTSAPDIYALGDCaeINGQVLP 283
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
172-249 |
9.90e-21 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 86.10 E-value: 9.90e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517457889 172 SIIVVGSGAIGVEFGYFYNSLGTKVTIVEFLPRVVPVEDEDISKELEKNLKKQGITVMTSSEVTSVDTSGNGVKAKVK 249
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLT 78
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
101-308 |
1.36e-16 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 82.57 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 101 KNKIDVIMGFGTLKAKGQVEVKGTDGKTTLVEGKhVILATGGRSRELPALKQDGKKIIGYRE------AMVLPQQPKSII 174
Cdd:TIGR02374 66 KHGITLYTGETVIQIDTDQKQVITDAGRTLSYDK-LILATGSYPFILPIPGADKKGVYVFRTiedldaIMAMAQRFKKAA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 175 VVGSGAIGVEFGYFYNSLGTKVTIVEFLPRVVPVE-DEDISKELEKNLKKQGITVMTSSEvtSVDTSGNGVKAKVKTATG 253
Cdd:TIGR02374 145 VIGGGLLGLEAAVGLQNLGMDVSVIHHAPGLMAKQlDQTAGRLLQRELEQKGLTFLLEKD--TVEIVGATKADRIRFKDG 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517457889 254 EAIlEADVLLSAVGVAANIEgIGLETvGVKTDKGkIVVDKFYKTNVDGVYAIGDC 308
Cdd:TIGR02374 223 SSL-EADLIVMAAGIRPNDE-LAVSA-GIKVNRG-IIVNDSMQTSDPDIYAVGEC 273
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
5-329 |
5.28e-14 |
|
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: 73.63 E-value: 5.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 5 VIVVGSGPGGYVAAIRASQLGLKTAIIEKES-LGGiclnwgciptkaLLKsaqvfndiqhakdYGIeasgtPDFgaivKR 83
Cdd:COG0493 124 VAVVGSGPAGLAAAYQLARAGHEVTVFEALDkPGG------------LLR-------------YGI-----PEF----RL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 84 SRGVADKmskgvqflmkknKIDVIMGFGtlkakgqVEVK-GTD-GKTTLVEG-----KHVILATG-GRSRELPAlkqDGK 155
Cdd:COG0493 170 PKDVLDR------------EIELIEALG-------VEFRtNVEvGKDITLDElleefDAVFLATGaGKPRDLGI---PGE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 156 KIIGYREAM---------VLPQQP----KSIIVVGSG--AI---------GVEfgyfynslgtKVTIVEFLPRV-VPVED 210
Cdd:COG0493 228 DLKGVHSAMdfltavnlgEAPDTIlavgKRVVVIGGGntAMdcartalrlGAE----------SVTIVYRRTREeMPASK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 211 EDISkelekNLKKQGITVMTSSEVTSVDTSGNGVKAKVKTA------------------TGEA-ILEADVLLSAVGVAAN 271
Cdd:COG0493 298 EEVE-----EALEEGVEFLFLVAPVEIIGDENGRVTGLECVrmelgepdesgrrrpvpiEGSEfTLPADLVILAIGQTPD 372
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 272 IEGIgLETVGVKTDK-GKIVVDKF-YKTNVDGVYAIGDCVPGQALAHVASKEGIICVENI 329
Cdd:COG0493 373 PSGL-EEELGLELDKrGTIVVDEEtYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAI 431
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
2-310 |
1.73e-11 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 65.95 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 2 AYDVIVVGSGPGGYVAAIRASQLGLKTAIIeKESLGGiclnwgciptkallksaQVfNDIQhakdyGIEasgtpDFgaI- 80
Cdd:PRK15317 211 PYDVLVVGGGPAGAAAAIYAARKGIRTGIV-AERFGG-----------------QV-LDTM-----GIE-----NF--Is 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 81 VKRSRGVadKMSKGVQFLMKKNKIDVIMG---FGTLKAKGQVEVKGTDGKTtlVEGKHVILATGGRSREL--PALKQ--- 152
Cdd:PRK15317 260 VPETEGP--KLAAALEEHVKEYDVDIMNLqraSKLEPAAGLIEVELANGAV--LKAKTVILATGARWRNMnvPGEDEyrn 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 153 ---------DGKKIIGyreamvlpqqpKSIIVVGSGAIGVEFGYFYNSLGTKVTIVEFLP--RVVPVedediskeLEKNL 221
Cdd:PRK15317 336 kgvaycphcDGPLFKG-----------KRVAVIGGGNSGVEAAIDLAGIVKHVTVLEFAPelKADQV--------LQDKL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 222 KKQG-ITVMTSSEVTSVDTSGNGVKAKVKT--ATGEailEADVLLSAVGVAaniegIGL--------ETVGVkTDKGKIV 290
Cdd:PRK15317 397 RSLPnVTIITNAQTTEVTGDGDKVTGLTYKdrTTGE---EHHLELEGVFVQ-----IGLvpntewlkGTVEL-NRRGEII 467
|
330 340
....*....|....*....|..
gi 517457889 291 VDKFYKTNVDGVYAIGDC--VP 310
Cdd:PRK15317 468 VDARGATSVPGVFAAGDCttVP 489
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
136-307 |
1.78e-11 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 65.72 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 136 VILATGGRSRELPALKQDGKKIIGYR---EAMVLPQ--QP-KSIIVVGSGAIGVEFGYFYNSLGTKVTIVEFLPRVV--- 206
Cdd:PRK09754 104 LFIATGAAARPLPLLDALGERCFTLRhagDAARLREvlQPeRSVVIVGAGTIGLELAASATQRRCKVTVIELAATVMgrn 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 207 ---PVEDEDISKELEKnlkkqGITVMTSSEVTSVDtsgNGVKAKVKTATGEAiLEADVLLSAVGVAANiEGIGLETvGVK 283
Cdd:PRK09754 184 appPVQRYLLQRHQQA-----GVRILLNNAIEHVV---DGEKVELTLQSGET-LQADVVIYGIGISAN-DQLAREA-NLD 252
|
170 180
....*....|....*....|....
gi 517457889 284 TDKGkIVVDKFYKTNVDGVYAIGD 307
Cdd:PRK09754 253 TANG-IVIDEACRTCDPAIFAGGD 275
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
225-340 |
3.36e-10 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 62.20 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 225 GITVMTSSEVTSVDTSGNGVKA--------KVKTATG--------EAILEADVLLSAVGvaANIEGIGLETV-GVKTDKG 287
Cdd:PRK12771 319 GVEINWLRTPVEIEGDENGATGlrvitvekMELDEDGrpspvtgeEETLEADLVVLAIG--QDIDSAGLESVpGVEVGRG 396
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 517457889 288 KIVVDKFYK-TNVDGVYAIGDCVPGQALAHVASKEGIICVENI-AF-GEKKYKHQP 340
Cdd:PRK12771 397 VVQVDPNFMmTGRPGVFAGGDMVPGPRTVTTAIGHGKKAARNIdAFlGGEPYEHRP 452
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
1-193 |
6.12e-10 |
|
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: 61.00 E-value: 6.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 1 MAYDVIVVGSGPGGYVAAIRASQLGLKTAIIEKESL---------GGIclnwgCIPTKALLKSA------QVFNDIQHAK 65
Cdd:COG1053 2 HEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPrgghtaaaqGGI-----NAAGTNVQKAAgedspeEHFYDTVKGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 66 DY------------------------GIEASGTPDF------GAIVKRSRGVADKMskGVQFL------MKKNKIDVIMG 109
Cdd:COG1053 77 DGladqdlvealaeeapeaidwleaqGVPFSRTPDGrlpqfgGHSVGRTCYAGDGT--GHALLatlyqaALRLGVEIFTE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 110 FGTL-------KAKGqVEVKGTDGKTTLVEGKHVILATGG--RSRELPALKQDGKKII-----------GYREAM----- 164
Cdd:COG1053 155 TEVLdlivddgRVVG-VVARDRTGEIVRIRAKAVVLATGGfgRNYEMRAEYLPEAEGAlstnapgntgdGIAMALragaa 233
|
250 260 270
....*....|....*....|....*....|....*...
gi 517457889 165 -VLPQQ--------PKSIIVVGSGAIGVEFGYFYNSLG 193
Cdd:COG1053 234 lADMEFvqfhptglPGDGGLISEGARGKPGGILVNKEG 271
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
4-148 |
9.38e-10 |
|
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: 60.38 E-value: 9.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 4 DVIVVGSGPGGYVAAIRASQLGLKTAIIEKESLGGICLNW--GCIPTKALLKSAQVFNDIQHAKDYGIEAsgtpDFGAIV 81
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGATAWssGGIDALGNPPQGGIDSPELHPTDTLKGL----DELADH 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517457889 82 KRSRGVADKMSKGVQFLMK---------KNKIDVImGFGTLKAKGQVEVKGTDGKTTLVEGKHVILATGGRSRELP 148
Cdd:pfam00890 77 PYVEAFVEAAPEAVDWLEAlgvpfsrteDGHLDLR-PLGGLSATWRTPHDAADRRRGLGTGHALLARLLEGLRKAG 151
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
5-329 |
3.11e-09 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 59.02 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 5 VIVVGSGPGGYVAAIRASQLGLKTAIIEKES-LGGiclnwgciptkaLLKsaqvfndiqhakdYGIeasgtPDFgaivkr 83
Cdd:PRK12810 146 VAVVGSGPAGLAAADQLARAGHKVTVFERADrIGG------------LLR-------------YGI-----PDF------ 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 84 srgvadKMSKGVqflMKKnKIDVIMGFGTlKAKGQVEVKGTDGKTTLVEgKH--VILATG-GRSRELPAlkqDGKKIIGY 160
Cdd:PRK12810 190 ------KLEKEV---IDR-RIELMEAEGI-EFRTNVEVGKDITAEELLA-EYdaVFLGTGaYKPRDLGI---PGRDLDGV 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 161 REAM-VLPQQPKSI----------------IVVGSGAIGVEfgyfynSLGT-------KVTIVEFLPRvvPVEDEDIS-- 214
Cdd:PRK12810 255 HFAMdFLIQNTRRVlgdetepfisakgkhvVVIGGGDTGMD------CVGTairqgakSVTQRDIMPM--PPSRRNKNnp 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 215 -----KELE-KNLKKQGIT----VMTSS---------EVTSVDTSGNGVKAKVKTATgEAILEADVLLSAVGVAANIEGI 275
Cdd:PRK12810 327 wpywpMKLEvSNAHEEGVErefnVQTKEfegengkvtGVKVVRTELGEGDFEPVEGS-EFVLPADLVLLAMGFTGPEAGL 405
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 517457889 276 gLETVGVKTDK-GKIVVDKF-YKTNVDGVYAIGDCVPGQALAHVASKEGIICVENI 329
Cdd:PRK12810 406 -LAQFGVELDErGRVAAPDNaYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAI 460
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
172-322 |
1.52e-08 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 56.70 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 172 SIIVVGSGAIGVEFGY------------FYNSL--GTKVTIVEFLPRVVPVEDEDISKELEKNLKKQGITVMTSSEVTSV 237
Cdd:PTZ00318 175 HFVVVGGGPTGVEFAAeladffrddvrnLNPELveECKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEV 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 238 dtsgngVKAKVKTATGEAILEADVLLSA-VGVAANIEGIGLEtvgvKTDKGKIVVDKFYKT-NVDGVYAIGDC-----VP 310
Cdd:PTZ00318 255 ------LDKEVVLKDGEVIPTGLVVWSTgVGPGPLTKQLKVD----KTSRGRISVDDHLRVkPIPNVFALGDCaaneeRP 324
|
170
....*....|..
gi 517457889 311 GQALAHVASKEG 322
Cdd:PTZ00318 325 LPTLAQVASQQG 336
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
3-145 |
2.46e-08 |
|
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: 55.40 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 3 YDVIVVGSGPGGYVAAIRASQLGLKTAIIEKESLGGICLNWGCIPTKALLK----SAQVFNDIQHAKDYG-----IEASG 73
Cdd:TIGR02032 1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPRYKPCGGALSPRALEEldlpGELIVNLVRGARFFSpngdsVEIPI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517457889 74 TPDFGAIVKRS---RGVADK-MSKGVQFLMKKNKIDVIMGfgtlkaKGQVEVKGTDGKTTlVEGKHVILATGGRSR 145
Cdd:TIGR02032 81 ETELAYVIDRDafdEQLAERaQEAGAELRLGTRVLDVEIH------DDRVVVIVRGSEGT-VTAKIVIGADGSRSI 149
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
152-330 |
6.03e-08 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 54.79 E-value: 6.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 152 QDGKKIIGYREAMvlpqQPKSIIVVGSGAIGVEFGYFYNSLGTKVTIVEFLPRVVPVEDEDISKELEKNLKKQGITVMTS 231
Cdd:PRK13512 134 EDTDAIDQFIKAN----QVDKALVVGAGYISLEVLENLYERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLN 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 232 SEVTSVDtsGNGVKAKV-KTATGEAILEAdvllsaVGVAANIEGIglETVGVK-TDKGKIVVDKFYKTNVDGVYAIGDCV 309
Cdd:PRK13512 210 EEIDAIN--GNEVTFKSgKVEHYDMIIEG------VGTHPNSKFI--ESSNIKlDDKGFIPVNDKFETNVPNIYAIGDII 279
|
170 180 190
....*....|....*....|....*....|.
gi 517457889 310 ---------PGQ-ALAHVASKEGIICVENIA 330
Cdd:PRK13512 280 tshyrhvdlPASvPLAWGAHRAASIVAEQIA 310
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
3-67 |
6.94e-08 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 54.66 E-value: 6.94e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517457889 3 YDVIVVGSGPGGYVAAIRASQLGLKTAIIEK---------ESLGGIclnWgcIPTKALLKSAQVFNDIQHAKDY 67
Cdd:PRK07843 8 YDVVVVGSGAAGMVAALTAAHRGLSTVVVEKaphyggstaRSGGGV---W--IPNNEVLKRAGVPDTPEAARTY 76
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
1-38 |
1.52e-07 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 53.70 E-value: 1.52e-07
10 20 30
....*....|....*....|....*....|....*....
gi 517457889 1 MAYDVIVVGSGPGGYVAAIRASQLGLKTAIIEK-ESLGG 38
Cdd:COG1233 2 MMYDVVVIGAGIGGLAAAALLARAGYRVTVLEKnDTPGG 40
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
4-38 |
2.52e-07 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 52.61 E-value: 2.52e-07
10 20 30
....*....|....*....|....*....|....*.
gi 517457889 4 DVIVVGSGPGGYVAAIRASQLGLKTAIIEKES-LGG 38
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRGfLGG 36
|
|
| PRK12844 |
PRK12844 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
2-88 |
3.05e-07 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 183787 [Multi-domain] Cd Length: 557 Bit Score: 52.83 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 2 AYDVIVVGSGPGGYVAAIRASQLGLKTAIIEKESL--------GGIClnWgcIPTKALLKSAQVFNDIQHAKDYGIEASG 73
Cdd:PRK12844 6 TYDVVVVGSGGGGMCAALAAADSGLEPLIVEKQDKvggstamsGGVL--W--LPNNPLMKAAGVPDSHEDALAYLDAVVG 81
|
90
....*....|....*
gi 517457889 74 tpDFGAIVKRSRGVA 88
Cdd:PRK12844 82 --DQGPASSPERREA 94
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
11-189 |
3.74e-07 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 51.51 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 11 GPGGYVAAIRASQLGLKTAIIEKESLGGICLNWGCIPTKALLK------SAQVFNDIQHAK-----DYGIEASGTPDFGA 79
Cdd:COG0644 2 GPAGSAAARRLARAGLSVLLLEKGSFPGDKICGGGLLPRALEEleplglDEPLERPVRGARfyspgGKSVELPPGRGGGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 80 IVkrSRGVADK------MSKGVQFLMKKNKIDVIMGfgtlkaKGQVEVKGTDGKTtlVEGKHVILATGGRS---RELPAL 150
Cdd:COG0644 82 VV--DRARFDRwlaeqaEEAGAEVRTGTRVTDVLRD------DGRVVVRTGDGEE--IRADYVVDADGARSllaRKLGLK 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 517457889 151 KQDGKK---IIGYREAMVLP-----QQPKSIIVVGSGAIGvefGYFY 189
Cdd:COG0644 152 RRSDEPqdyALAIKEHWELPplegvDPGAVEFFFGEGAPG---GYGW 195
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
5-316 |
2.10e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 50.15 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 5 VIVVGSGPGGYVAAIRASQLGLKTAIIEKESLGGICLNWGcIPTKALLKSAqVFNDIQHakdygIEASGtpdfgaiVKRS 84
Cdd:PRK13984 286 VAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGVMRYG-IPSYRLPDEA-LDKDIAF-----IEALG-------VKIH 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 85 RGVadKMSKGVQFLMKKNKIDVIM---GFGTlkakgqvevkgtdGKTTLVEG---KHVILAtggrsreLPALKQ------ 152
Cdd:PRK13984 352 LNT--RVGKDIPLEELREKHDAVFlstGFTL-------------GRSTRIPGtdhPDVIQA-------LPLLREirdylr 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 153 -DGKKiigyreamvlPQQPKSIIVVGSGAIGVEFGYF--------YNSLGTKVTIVEFLPRVVPVEDEDISKELEknlkk 223
Cdd:PRK13984 410 gEGPK----------PKIPRSLVVIGGGNVAMDIARSmarlqkmeYGEVNVKVTSLERTFEEMPADMEEIEEGLE----- 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 224 QGITVMTS---SEVTSVDTSGNGVKAKVKTA--------------TGEAILEADVLLSAVGVAANIEGIGLE-TVGVKTD 285
Cdd:PRK13984 475 EGVVIYPGwgpMEVVIENDKVKGVKFKKCVEvfdeegrfnpkfdeSDQIIVEADMVVEAIGQAPDYSYLPEElKSKLEFV 554
|
330 340 350
....*....|....*....|....*....|.
gi 517457889 286 KGKIVVDKFYKTNVDGVYAIGDCVPGQALAH 316
Cdd:PRK13984 555 RGRILTNEYGQTSIPWLFAGGDIVHGPDIIH 585
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
3-67 |
3.15e-06 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 49.72 E-value: 3.15e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517457889 3 YDVIVVGSGPGGYVAAIRASQLGLKTAIIEKES-LGGICL---NWGCIPTKALLKSAQVFNDIQHAKDY 67
Cdd:PRK06134 13 CDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPvFGGTTAwsgGWMWIPRNPLARRAGIVEDIEQPRTY 81
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
238-329 |
4.56e-06 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 49.02 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 238 DTSGNGvkaKVKTATGEAILEADVLLSAVG------VAANIEGIGLETVGvktdkGKIVVDKFYKTNVDGVYAIGDCVPG 311
Cdd:PRK11749 358 DASGRR---RVPIEGSEFTLPADLVIKAIGqtpnplILSTTPGLELNRWG-----TIIADDETGRTSLPGVFAGGDIVTG 429
|
90
....*....|....*...
gi 517457889 312 QALAHVASKEGIICVENI 329
Cdd:PRK11749 430 AATVVWAVGDGKDAAEAI 447
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
199-322 |
6.17e-06 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 48.06 E-value: 6.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 199 VEFLPRVVPVEDedISKELEKNLKkqgitvMTSSEVTSVDTSGNgvKAKVKTATGEAILEADVLLSAVGVAA----NIEG 274
Cdd:PRK12770 225 VEFLELVTPVRI--IGEGRVEGVE------LAKMRLGEPDESGR--PRPVPIPGSEFVLEADTVVFAIGEIPtppfAKEC 294
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 517457889 275 IGLETVgvktDKGKIVVDKFYKTNVDGVYAIGDCVPGQALAHVASKEG 322
Cdd:PRK12770 295 LGIELN----RKGEIVVDEKHMTSREGVFAAGDVVTGPSKIGKAIKSG 338
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
84-318 |
1.26e-05 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 47.81 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 84 SRGVADKMSKGVQFLMKKNKIDVIMGFGTLKAKGQVEVKGTDGKTTLVEGKhVILATGGRSRELPALKQDGKKIIGYREA 163
Cdd:PRK14989 54 SHHTAEELSLVREGFYEKHGIKVLVGERAITINRQEKVIHSSAGRTVFYDK-LIMATGSYPWIPPIKGSETQDCFVYRTI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 164 MVL------PQQPKSIIVVGSGAIGVEFGYFYNSLGTKVTIVEFLPRVVPVE-DEDISKELEKNLKKQGITVMTSSEVTS 236
Cdd:PRK14989 133 EDLnaieacARRSKRGAVVGGGLLGLEAAGALKNLGVETHVIEFAPMLMAEQlDQMGGEQLRRKIESMGVRVHTSKNTLE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 237 VDTSGNGVKAKVKTATGEAiLEADVLLSAVGVAAN---IEGIGLETvgvkTDKGKIVVDKFYKTNVDGVYAIGDC----- 308
Cdd:PRK14989 213 IVQEGVEARKTMRFADGSE-LEVDFIVFSTGIRPQdklATQCGLAV----APRGGIVINDSCQTSDPDIYAIGECaswnn 287
|
250
....*....|....*.
gi 517457889 309 ------VPGQALAHVA 318
Cdd:PRK14989 288 rvfglvAPGYKMAQVA 303
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
3-67 |
1.94e-05 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 47.13 E-value: 1.94e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517457889 3 YDVIVVGSGPGGYVAAIRASQLGLKTAIIEK-ESLGGICL---NWGCIPTKALLKSAQVFNDIQHAKDY 67
Cdd:PRK12839 9 YDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKaSTCGGATAwsgGWMWTPGNSLARADGVVEDKEEPRTY 77
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
4-141 |
4.55e-05 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 45.62 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 4 DVIVVGSGPGGYVAAIRASQLGLKTAIIeKESLGGIClNWGCIPTKALLKSAQVFNDIQHAkdyGIEASGTPDFGAIVKR 83
Cdd:pfam01134 1 DVIVIGGGHAGCEAALAAARMGAKVLLI-THNTDTIA-ELSCNPSIGGIAKGHLVREIDAL---GGLMGKAADKTGIQFR 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517457889 84 S------------RGVADKM--SKGVQFLMKKNK-IDVIMGFGT--LKAKGQVE-VKGTDGKTtlVEGKHVILATG 141
Cdd:pfam01134 76 MlntskgpavralRAQVDRDlySKEMTETLENHPnLTLIQGEVTdlIPENGKVKgVVTEDGEE--YKAKAVVLATG 149
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
3-33 |
5.09e-05 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 45.26 E-value: 5.09e-05
10 20 30
....*....|....*....|....*....|.
gi 517457889 3 YDVIVVGSGPGGYVAAIRASQLGLKTAIIEK 33
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEK 31
|
|
| sdhA |
PRK07803 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
2-37 |
7.47e-05 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 236101 [Multi-domain] Cd Length: 626 Bit Score: 45.03 E-value: 7.47e-05
10 20 30
....*....|....*....|....*....|....*.
gi 517457889 2 AYDVIVVGSGPGGYVAAIRASQLGLKTAIIEKESLG 37
Cdd:PRK07803 8 SYDVVVIGAGGAGLRAAIEARERGLRVAVVCKSLFG 43
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
1-31 |
8.52e-05 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 44.84 E-value: 8.52e-05
10 20 30
....*....|....*....|....*....|.
gi 517457889 1 MAYDVIVVGSGPGGYVAAIRASQLGLKTAII 31
Cdd:PRK05329 1 MKFDVLVIGGGLAGLTAALAAAEAGKRVALV 31
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
1-38 |
1.10e-04 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 44.68 E-value: 1.10e-04
10 20 30
....*....|....*....|....*....|....*....
gi 517457889 1 MAYDVIVVGSGPGGYVAAIRASQLGLKTAIIEKES-LGG 38
Cdd:PRK12842 8 LTCDVLVIGSGAGGLSAAITARKLGLDVVVLEKEPvFGG 46
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
2-38 |
1.60e-04 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 43.96 E-value: 1.60e-04
10 20 30
....*....|....*....|....*....|....*...
gi 517457889 2 AYDVIVVGSGPGGYVAAIRASQLGLKTAIIEK-ESLGG 38
Cdd:PRK12843 16 EFDVIVIGAGAAGMSAALFAAIAGLKVLLVERtEYVGG 53
|
|
| PRK12835 |
PRK12835 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
3-38 |
1.73e-04 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237221 [Multi-domain] Cd Length: 584 Bit Score: 44.03 E-value: 1.73e-04
10 20 30
....*....|....*....|....*....|....*..
gi 517457889 3 YDVIVVGSGPGGYVAAIRASQLGLKTAIIEKES-LGG 38
Cdd:PRK12835 12 VDVLVVGSGGGGMTAALTAAARGLDTLVVEKSAhFGG 48
|
|
| PRK12834 |
PRK12834 |
putative FAD-binding dehydrogenase; Reviewed |
1-38 |
2.39e-04 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 183782 [Multi-domain] Cd Length: 549 Bit Score: 43.35 E-value: 2.39e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 517457889 1 MAYDVIVVGSGPGGYVAAIRASQLGLKTAIIEKE---SLGG 38
Cdd:PRK12834 3 MDADVIVVGAGLAGLVAAAELADAGKRVLLLDQEneaNLGG 43
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
1-35 |
3.61e-04 |
|
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: 42.62 E-value: 3.61e-04
10 20 30
....*....|....*....|....*....|....*
gi 517457889 1 MAYDVIVVGSGPGGYVAAIRASQLGLKTAIIEKES 35
Cdd:COG0654 2 MRTDVLIVGGGPAGLALALALARAGIRVTVVERAP 36
|
|
| COG3573 |
COG3573 |
Predicted oxidoreductase [General function prediction only]; |
1-38 |
7.95e-04 |
|
Predicted oxidoreductase [General function prediction only];
Pssm-ID: 442794 [Multi-domain] Cd Length: 551 Bit Score: 41.70 E-value: 7.95e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 517457889 1 MAYDVIVVGSGPGGYVAAIRASQLGLKTAIIEKE---SLGG 38
Cdd:COG3573 4 MDADVIVVGAGLAGLVAAAELADAGRRVLLLDQEpeaNLGG 44
|
|
| glycerol3P_GlpB |
TIGR03378 |
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are ... |
3-31 |
1.28e-03 |
|
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: 41.16 E-value: 1.28e-03
10 20
....*....|....*....|....*....
gi 517457889 3 YDVIVVGSGPGGYVAAIRASQLGLKTAII 31
Cdd:TIGR03378 1 FDVIIIGGGLAGLSCALRLAEAGKKCAII 29
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
3-38 |
1.38e-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: 41.00 E-value: 1.38e-03
10 20 30
....*....|....*....|....*....|....*..
gi 517457889 3 YDVIVVGSGPGGYVAAIRASQLGLKTAIIEKES-LGG 38
Cdd:COG2072 7 VDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADdVGG 43
|
|
| Lys_Orn_oxgnase |
pfam13434 |
L-lysine 6-monooxygenase/L-ornithine 5-monooxygenase; This is a family of Rossmann fold ... |
119-193 |
1.53e-03 |
|
L-lysine 6-monooxygenase/L-ornithine 5-monooxygenase; This is a family of Rossmann fold oxidoreductases that catalyze NADPH-dependent hydroxylation and are involved in siderophore biosynthesis. This family includes L-ornithine 5-monooxygenase, which catalyzes the hydroxylation of L-ornithine at the N5 position, and L-lysine 6-monooxygenase, which catalyzes the hydroxylation of lysine at the N6 position (EC:1.14.13.59).
Pssm-ID: 433204 [Multi-domain] Cd Length: 338 Bit Score: 40.65 E-value: 1.53e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517457889 119 VEVKGTDGKTTLVEGKHVILATGGRSReLPALKQDGKKII---GYREAMVLPQQPKSIIVVGSGAIGVEFgyFYNSLG 193
Cdd:pfam13434 134 VRVRDADGEETTFLARNLVLGTGGEPY-IPECARGGERVFhssEYLERIDRLAAKKRIAVVGSGQSAAEI--FRDLLR 208
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
114-306 |
2.77e-03 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 39.51 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 114 KAKGQVEVKgTDGKTtlVEGKHVILATGGRSR-ELPALKQDGKKIIGYREAMVLPQQPksIIVVGSGAIGVEFGYFYNSL 192
Cdd:pfam13738 103 KEDDGFVVT-TSKGT--YQARYVIIATGEFDFpNKLGVPELPKHYSYVKDFHPYAGQK--VVVIGGYNSAVDAALELVRK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517457889 193 GTKVTIV-----------EFLPRVVPvedeDISKELEKNLKKQGITVMTSSEVTSVDTSGNGVkaKVKTATGEAILEADV 261
Cdd:pfam13738 178 GARVTVLyrgsewedrdsDPSYSLSP----DTLNRLEELVKNGKIKAHFNAEVKEITEVDVSY--KVHTEDGRKVTSNDD 251
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517457889 262 LLSAVGVAAN---IEGIGLETvgvkTDKGKIVVDKFY-KTNVDGVYAIG 306
Cdd:pfam13738 252 PILATGYHPDlsfLKKGLFEL----DEDGRPVLTEETeSTNVPGLFLAG 296
|
|
| PRK06481 |
PRK06481 |
flavocytochrome c; |
3-38 |
2.88e-03 |
|
flavocytochrome c;
Pssm-ID: 180584 [Multi-domain] Cd Length: 506 Bit Score: 40.20 E-value: 2.88e-03
10 20 30
....*....|....*....|....*....|....*.
gi 517457889 3 YDVIVVGSGPGGYVAAIRASQLGLKTAIIEKESLGG 38
Cdd:PRK06481 62 YDIVIVGAGGAGMSAAIEAKDAGMNPVILEKMPVAG 97
|
|
| PRK12845 |
PRK12845 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
4-67 |
4.03e-03 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237226 [Multi-domain] Cd Length: 564 Bit Score: 39.75 E-value: 4.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517457889 4 DVIVVGSGPGgYVAAIRASQLGLKTAIIEKES-LGGICLNWG---CIPTKALLKSAQVFNDIQHAKDY 67
Cdd:PRK12845 18 DLLVVGSGTG-MAAALAAHELGLSVLIVEKSSyVGGSTARSGgafWLPASPVLDEAGAGDTLERARTY 84
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
7-38 |
4.12e-03 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 35.58 E-value: 4.12e-03
10 20 30
....*....|....*....|....*....|...
gi 517457889 7 VVGSGPGGYVAAIRASQLGLKTAIIEKES-LGG 38
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDrLGG 33
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
1-38 |
8.32e-03 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 38.35 E-value: 8.32e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 517457889 1 MAYDVIVVGsgpGGYV---AAIRASQLGLKTAIIEKESLGG 38
Cdd:COG0665 1 ATADVVVIG---GGIAglsTAYHLARRGLDVTVLERGRPGS 38
|
|
| |
