|
Name |
Accession |
Description |
Interval |
E-value |
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
11-499 |
0e+00 |
|
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: 906.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 11 YDFDLIIIGGGSGGLAAAKEAAKFDKKVLVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKV 90
Cdd:TIGR01438 1 YDYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPTPLGTRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 91 EDTVKHDWEKMTESVQSHIGSLNWGYRVALREKKVVYENAYGRFIGPHRIVATNNKGKEKIYSAERFLIATGERPRYLGI 170
Cdd:TIGR01438 81 EETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERPRYPGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 171 PGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHMEEHGIKFIRQ 250
Cdd:TIGR01438 161 PGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDCANKVGEHMEEHGVKFKRQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 251 FVPTKIEQIEAgtpgrlRVTAQSTNSEETIEGEFNTVLLAVGRDSCTRTIGLETVGVKINEKTGKIPVTDEEQTNVPYIY 330
Cdd:TIGR01438 241 FVPIKVEQIEA------KVLVEFTDSTNGIEEEYDTVLLAIGRDACTRKLNLENVGVKINKKTGKIPADEEEQTNVPYIY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 331 AIGDILEGKLELTPVAIQAGRLLAQRLYGGSNVKCDYDNVPTTVFTPLEYGCCGLSEEKAVEKFGEENIEVYHSFFWPLE 410
Cdd:TIGR01438 315 AVGDILEDKPELTPVAIQAGRLLAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENVEVFHSYFWPLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 411 WTVPSRDN-NKCYAKIICNLKDDERVVGFHVLGPNAGEVTQGFAAALKCGLTKQQLDSTIGIHPVCAEIFTTLSVTKRSG 489
Cdd:TIGR01438 395 WTIPSRDNhNKCYAKLVCNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTLSVTKRSG 474
|
490
....*....|
gi 110224442 490 GDILQSGCUG 499
Cdd:TIGR01438 475 QDILQQGCCG 484
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
10-499 |
0e+00 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 520.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 10 SYDFDLIIIGGGSGGLAAAKEAAKFDKKVLVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALK-DSRNYGW 88
Cdd:PTZ00052 3 TFMYDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKPSTQGTKWGLGGTCVNVGCVPKKLMHYAANIGSIFHhDSQMYGW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 89 KVEDTvkHDWEKMTESVQSHIGSLNWGYRVALREKKVVYENAYGRFIGPHRiVATNNKGKEKIYSAERFLIATGERPRYL 168
Cdd:PTZ00052 83 KTSSS--FNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHT-VSYGDNSQEETITAKYILIATGGRPSIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 169 -GIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHMEEHGIKF 247
Cdd:PTZ00052 160 eDVPGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRSIPLRGFDRQCSEKVVEYMKEQGTLF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 248 IRQFVPTKIEQIEAgtpgRLRVTAQSTNSEetiegEFNTVLLAVGRDSCTRTIGLETVGVKINeKTGKIPVTDeEQTNVP 327
Cdd:PTZ00052 240 LEGVVPINIEKMDD----KIKVLFSDGTTE-----LFDTVLYATGRKPDIKGLNLNAIGVHVN-KSNKIIAPN-DCTNIP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 328 YIYAIGDILEGKLELTPVAIQAGRLLAQRLYGGSNVKCDYDNVPTTVFTPLEYGCCGLSEEKAVEKFGEENIEVYHSFFW 407
Cdd:PTZ00052 309 NIFAVGDVVEGRPELTPVAIKAGILLARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQEFN 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 408 PLEWTVPSRD--------------NNKCYAKIICNLKDDERVVGFHVLGPNAGEVTQGFAAALKCGLTKQQLDSTIGIHP 473
Cdd:PTZ00052 389 TLEIAAVHREkherarkdeydfdvSSNCLAKLVCVKSEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHP 468
|
490 500
....*....|....*....|....*.
gi 110224442 474 VCAEIFTTLSVTKRSGGDILQSGCUG 499
Cdd:PTZ00052 469 TDAEVFMNLSVTRRSGESFAAKGGCG 494
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
31-482 |
2.26e-138 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 406.46 E-value: 2.26e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 31 AAKFDKKVLVLDfvtptplGTRwgLGGTCVNVGCIPKKLMHQAALLGQALKD-SRNYGWKVEDTvKHDWEKMTESVQSHI 109
Cdd:PRK06116 23 AAMYGAKVALIE-------AKR--LGGTCVNVGCVPKKLMWYGAQIAEAFHDyAPGYGFDVTEN-KFDWAKLIANRDAYI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 110 GSLNWGYRVALREKKVVYENAYGRFIGPHRIVATNNKgkekiYSAERFLIATGERPRYLGIPGdKEYCISSDDLFSLPYC 189
Cdd:PRK06116 93 DRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNGER-----YTADHILIATGGRPSIPDIPG-AEYGITSDGFFALEEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 190 PGKTLVVGASYVALECAGFLAGIGLDVTVMVRSIL-LRGFDQDMANKIGEHMEEHGIKFIRQFVPTKIEQIEAGtpgRLR 268
Cdd:PRK06116 167 PKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDApLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADG---SLT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 269 VTaqsTNSEETIEgeFNTVLLAVGRDSCTRTIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEGKLELTPVAIQ 348
Cdd:PRK06116 244 LT---LEDGETLT--VDCLIWAIGREPNTDGLGLENAGVKLNEK-GYIIVDEYQNTNVPGIYAVGDV-TGRVELTPVAIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 349 AGRLLAQRLYGG-SNVKCDYDNVPTTVFTPLEYGCCGLSEEKAVEKFGEENIEVYHSFFWPLEWTVPSRDNnKCYAKIIC 427
Cdd:PRK06116 317 AGRRLSERLFNNkPDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVKVYRSSFTPMYTALTGHRQ-PCLMKLVV 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 110224442 428 NlKDDERVVGFHVLGPNAGEVTQGFAAALKCGLTKQQLDSTIGIHPVCAEIFTTL 482
Cdd:PRK06116 396 V-GKEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFVTM 449
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
31-482 |
1.04e-117 |
|
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: 353.62 E-value: 1.04e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 31 AAKFDKKVLVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVEDtVKHDWEKMTESVQSHIG 110
Cdd:COG1249 22 AAQLGLKVALVE---------KGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISAGA-PSVDWAALMARKDKVVD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 111 SLNWGYRVALREKKVVYENAYGRFIGPHRIVATNnkgkEKIYSAERFLIATGERPRYLGIPG-DKEYCISSDDLFSLPYC 189
Cdd:COG1249 92 RLRGGVEELLKKNGVDVIRGRARFVDPHTVEVTG----GETLTADHIVIATGSRPRVPPIPGlDEVRVLTSDEALELEEL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 190 PGKTLVVGASYVALECAGFLAGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHGIKFIRQFVPTKIEQIEAGtpgrLR 268
Cdd:COG1249 168 PKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGdRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDG----VT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 269 VTAQSTNSEETIEGEfnTVLLAVGRDSCTRTIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILeGKLELTPVAIQ 348
Cdd:COG1249 244 VTLEDGGGEEAVEAD--KVLVATGRRPNTDGLGLEAAGVELDER-GGIKVDEYLRTSVPGIYAIGDVT-GGPQLAHVASA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 349 AGRLLAQRLYGGSNVKCDYDNVPTTVFTPLEYGCCGLSEEKAVEKFgeENIEVYHSFFWPLEWTVpSRDNNKCYAKIICN 428
Cdd:COG1249 320 EGRVAAENILGKKPRPVDYRAIPSVVFTDPEIASVGLTEEEAREAG--IDVKVGKFPFAANGRAL-ALGETEGFVKLIAD 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 110224442 429 lKDDERVVGFHVLGPNAGEVTQGFAAALKCGLTKQQLDSTIGIHPVCAEIFTTL 482
Cdd:COG1249 397 -AETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEA 449
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
11-482 |
1.49e-109 |
|
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, e.g., for maintaining the cellular thiol/disulfide status and for protecting against reactive oxygen species such as hydrogen peroxide. Glutathione-disulfide reductase regenerates reduced glutathione from oxidized glutathione (glutathione disulfide) + NADPH. This model represents one of two closely related subfamilies of glutathione-disulfide reductase. Both are closely related to trypanothione reductase, and separate models are built so each of the three can describe proteins with conserved function. This model describes glutathione-disulfide reductases of plants and some bacteria, including cyanobacteria. [Energy metabolism, Electron transport]
Pssm-ID: 213618 [Multi-domain] Cd Length: 446 Bit Score: 332.55 E-value: 1.49e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 11 YDFDLIIIGGGSGGLAAAKEAAKFDKKVLV--LDFVtptplgtrwglGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGW 88
Cdd:TIGR01424 1 FDYDLFVIGAGSGGVRAARLAAALGAKVAIaeEFRV-----------GGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGW 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 89 KVEDtVKHDWEKMTESVQSHIGSLNWGYRVALREKKVVYENAYGRFIGPHRiVATNNKGKEkiYSAERFLIATGERPRYL 168
Cdd:TIGR01424 70 TVGK-ARFDWKKLLAAKDQEIARLSGLYRKGLANAGAELLDGRAELVGPNT-VEVLASGKT--YTAEKILIAVGGRPPKP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 169 GIPGdKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVR-SILLRGFDQDMANKIGEHMEEHGIKF 247
Cdd:TIGR01424 146 ALPG-HELGITSNEAFHLPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRgKEILRGFDDDMRRGLAAALEERGIRI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 248 IRQfvpTKIEQIEAGTPGRLRVTaqsTNSEETIEGEfnTVLLAVGRDSCTRTIGLETVGVKINEKtGKIPVTDEEQTNVP 327
Cdd:TIGR01424 225 LPE---DSITSISKDDDGRLKAT---LSKHEEIVAD--VVLFATGRSPNTNGLGLEAAGVRLNDL-GAIAVDEYSRTSTP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 328 YIYAIGDILEgKLELTPVAIQAGRLLAQRLYGGSNVKCDYDNVPTTVFTPLEYGCCGLSEEKAVEKFGEenIEVYHSFFW 407
Cdd:TIGR01424 296 SIYAVGDVTD-RINLTPVAIHEATCFAETEFGNNPTSFDHDLIATAVFSQPPIGTVGLTEEEARRKFGD--IEVYRAEFR 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110224442 408 PLEWTVPSRdNNKCYAKIICNLKDDeRVVGFHVLGPNAGEVTQGFAAALKCGLTKQQLDSTIGIHPVCAEIFTTL 482
Cdd:TIGR01424 373 PMKATFSGR-QEKTLMKLVVDAKDD-KVLGAHMVGPDAAEIIQGLAIALKMGATKDDFDSTVAVHPTSAEELVTM 445
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
55-482 |
7.05e-108 |
|
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important reductant, e.g., for maintaining the cellular thiol/disulfide status and for protecting against reactive oxygen species such as hydrogen peroxide. Glutathione-disulfide reductase regenerates reduced glutathione from oxidized glutathione (glutathione disulfide) + NADPH. This model represents one of two closely related subfamilies of glutathione-disulfide reductase. Both are closely related to trypanothione reductase, and separate models are built so each of the three can describe proteins with conserved function. This model describes glutathione-disulfide reductases of animals, yeast, and a number of animal-resident bacteria. [Energy metabolism, Electron transport]
Pssm-ID: 273614 [Multi-domain] Cd Length: 450 Bit Score: 328.34 E-value: 7.05e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 55 LGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVEDTVKHDWEKMTESVQSHIGSLNWGYRVALREKKVVYENAYGRF 134
Cdd:TIGR01421 36 LGGTCVNVGCVPKKVMWYASDLAERMHDAADYGFYQNDENTFNWPELKEKRDAYVDRLNGIYQKNLEKNKVDVIFGHARF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 135 IGPHRIVATNNKgkekiYSAERFLIATGERPRYL-GIPGdKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIG 213
Cdd:TIGR01421 116 TKDGTVEVNGRD-----YTAPHILIATGGKPSFPeNIPG-AELGTDSDGFFALEELPKRVVIVGAGYIAVELAGVLHGLG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 214 LDVTVMVR-SILLRGFDQDMANKIGEHMEEHGIKFIRQFVPTKIEQIeagTPGRLRVTAQSTNSEETIEgefnTVLLAVG 292
Cdd:TIGR01421 190 SETHLVIRhERVLRSFDSMISETITEEYEKEGINVHKLSKPVKVEKT---VEGKLVIHFEDGKSIDDVD----ELIWAIG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 293 RDSCTRTIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILeGKLELTPVAIQAGRLLAQRLYGG-SNVKCDYDNVP 371
Cdd:TIGR01421 263 RKPNTKGLGLENVGIKLNEK-GQIIVDEYQNTNVPGIYALGDVV-GKVELTPVAIAAGRKLSERLFNGkTDDKLDYNNVP 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 372 TTVFTPLEYGCCGLSEEKAVEKFGEENIEVYHSFFWPLEWTVPSRdNNKCYAKIICNLKdDERVVGFHVLGPNAGEVTQG 451
Cdd:TIGR01421 341 TVVFSHPPIGTIGLTEKEAIEKYGKENIKVYNSSFTPMYYAMTSE-KQKCRMKLVCAGK-EEKVVGLHGIGDGVDEMLQG 418
|
410 420 430
....*....|....*....|....*....|.
gi 110224442 452 FAAALKCGLTKQQLDSTIGIHPVCAEIFTTL 482
Cdd:TIGR01421 419 FAVAIKMGATKADFDNTVAIHPTSSEELVTM 449
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
2-487 |
8.85e-104 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 319.45 E-value: 8.85e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 2 NGSKDPPGSYDFDLIIIGGGSGGLAAAKEAAKFDKKVLV--LDFvtpTPLGTRW--GLGGTCVNVGCIPKKLMHQAALLG 77
Cdd:PLN02507 15 NADEANATHYDFDLFVIGAGSGGVRAARFSANFGAKVGIceLPF---HPISSESigGVGGTCVIRGCVPKKILVYGATFG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 78 QALKDSRNYGWKVEDTVKHDWEKMTESVQSHIGSLNWGYRVALREKKV-VYENAyGRFIGPHRIVATNNKGKEKIYSAER 156
Cdd:PLN02507 92 GEFEDAKNYGWEINEKVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVkLYEGE-GKIVGPNEVEVTQLDGTKLRYTAKH 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 157 FLIATGERPRYLGIPGdKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSIL-LRGFDQDMANK 235
Cdd:PLN02507 171 ILIATGSRAQRPNIPG-KELAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELpLRGFDDEMRAV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 236 IGEHMEEHGIKFIRQFVPTKIEQIEAGtpgrLRVTaqSTNSEETIEgefNTVLLAVGRDSCTRTIGLETVGVKInEKTGK 315
Cdd:PLN02507 250 VARNLEGRGINLHPRTNLTQLTKTEGG----IKVI--TDHGEEFVA---DVVLFATGRAPNTKRLNLEAVGVEL-DKAGA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 316 IPVTDEEQTNVPYIYAIGDIlEGKLELTPVAIQAGRLLAQRLYGGSNVKCDYDNVPTTVFTPLEYGCCGLSEEKAVEKfG 395
Cdd:PLN02507 320 VKVDEYSRTNIPSIWAIGDV-TNRINLTPVALMEGTCFAKTVFGGQPTKPDYENVACAVFCIPPLSVVGLSEEEAVEQ-A 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 396 EENIEVYHSFFWPLEWTVPSRdNNKCYAKIICNLKDDeRVVGFHVLGPNAGEVTQGFAAALKCGLTKQQLDSTIGIHPVC 475
Cdd:PLN02507 398 KGDILVFTSSFNPMKNTISGR-QEKTVMKLIVDAETD-KVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSA 475
|
490
....*....|...
gi 110224442 476 AEIFTTL-SVTKR 487
Cdd:PLN02507 476 AEEFVTMrSVTRR 488
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
2-487 |
2.83e-100 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 312.20 E-value: 2.83e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 2 NGSkDPPGSYDFDLIIIGGGSGGLAAAKEAAKFDKKVLV--LDFVTPTPlGTRWGLGGTCVNVGCIPKKLMHQAALLGQA 79
Cdd:PLN02546 70 NGA-ESERHYDFDLFTIGAGSGGVRASRFASNFGASAAVceLPFATISS-DTLGGVGGTCVLRGCVPKKLLVYASKYSHE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 80 LKDSRNYGWKVEDTVKHDWEKMTESVQSHIGSLNWGYRVALREKKVVYENAYGRFIGPHRIVATNnkgkeKIYSAERFLI 159
Cdd:PLN02546 148 FEESRGFGWKYETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDVDG-----KLYTARNILI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 160 ATGERPRYLGIPGdKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSI-LLRGFDQDMANKIGE 238
Cdd:PLN02546 223 AVGGRPFIPDIPG-IEHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKkVLRGFDEEVRDFVAE 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 239 HMEEHGIKFIRQFVPTKIEQIEAGTpgrlrvTAQSTNsEETIEGeFNTVLLAVGRDSCTRTIGLETVGVKINeKTGKIPV 318
Cdd:PLN02546 302 QMSLRGIEFHTEESPQAIIKSADGS------LSLKTN-KGTVEG-FSHVMFATGRKPNTKNLGLEEVGVKMD-KNGAIEV 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 319 TDEEQTNVPYIYAIGDILEgKLELTPVAIQAGRLLAQRLYGGSNVKCDYDNVPTTVFTPLEYGCCGLSEEKAVEKFGEen 398
Cdd:PLN02546 373 DEYSRTSVPSIWAVGDVTD-RINLTPVALMEGGALAKTLFGNEPTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYGD-- 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 399 IEVYHSFFWPLEWTVpSRDNNKCYAKIICNLKDDeRVVGFHVLGPNAGEVTQGFAAALKCGLTKQQLDSTIGIHPVCAEI 478
Cdd:PLN02546 450 VDVFTANFRPLKATL-SGLPDRVFMKLIVCAKTN-KVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEE 527
|
....*....
gi 110224442 479 FTTLSVTKR 487
Cdd:PLN02546 528 FVTMRTPTR 536
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
55-483 |
4.40e-87 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 278.04 E-value: 4.40e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 55 LGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVEDTVkhDWEKMTESVQSHIGSLNWGYRVALREKKVVYENAYGRF 134
Cdd:PTZ00058 82 LGGTCVNVGCVPKKIMFNAASIHDILENSRHYGFDTQFSF--NLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 135 IGPHRIVATNNKG-----------KEKIYS-------------AERFLIATGERPRYLGIPGdKEYCISSDDLFSLPYcP 190
Cdd:PTZ00058 160 LSENQVLIKKVSQvdgeadesdddEVTIVSagvsqlddgqvieGKNILIAVGNKPIFPDVKG-KEFTISSDDFFKIKE-A 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 191 GKTLVVGASYVALECAGFLAGIGLDVTVMVR-SILLRGFDQDMANKIGEHMEEHGIKFIRQFVPTKIEQIEagTPGRLRV 269
Cdd:PTZ00058 238 KRIGIAGSGYIAVELINVVNRLGAESYIFARgNRLLRKFDETIINELENDMKKNNINIITHANVEEIEKVK--EKNLTIY 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 270 TAQSTNSEetiegEFNTVLLAVGRDSCTRTIGLEtvGVKINEKTGKIPVTDEEQTNVPYIYAIGDILEGK---------- 339
Cdd:PTZ00058 316 LSDGRKYE-----HFDYVIYCVGRSPNTEDLNLK--ALNIKTPKGYIKVDDNQRTSVKHIYAVGDCCMVKknqeiedlnl 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 340 -----------------------LELTPVAIQAGRLLAQRLYGGSNVKCDYDNVPTTVFTPLEYGCCGLSEEKAVEKFGE 396
Cdd:PTZ00058 389 lklyneepylkkkentsgesyynVQLTPVAINAGRLLADRLFGPFSRTTNYKLIPSVIFSHPPIGTIGLSEQEAIDIYGK 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 397 ENIEVYHSFFWPLEWTV----PSrDNNKCYAKIICNLKdDERVVGFHVLGPNAGEVTQGFAAALKCGLTKQQLDSTIGIH 472
Cdd:PTZ00058 469 ENVKIYESRFTNLFFSVydmdPA-QKEKTYLKLVCVGK-EELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIH 546
|
490
....*....|.
gi 110224442 473 PVCAEIFTTLS 483
Cdd:PTZ00058 547 PTAAEEFVTMA 557
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
31-477 |
1.43e-78 |
|
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: 253.74 E-value: 1.43e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 31 AAKFDKKVLVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVE-DTVKHDWEKMTESVQSHI 109
Cdd:TIGR01423 23 ATLYKKRVAVVDVQTHHGPPFYAALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGWEFDrSSVKANWKALIAAKNKAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 110 GSLNWGYRVALREKK-VVYENAYGRFIGPHRIVA-----TNNKGKEKIySAERFLIATGERPRYLGIPGDkEYCISSDDL 183
Cdd:TIGR01423 103 LDINKSYEGMFADTEgLTFFLGWGALEDKNVVLVresadPKSAVKERL-QAEHILLATGSWPQMLGIPGI-EHCISSNEA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 184 FSLPYCPGKTLVVGASYVALECAGFLAG---IGLDVTVMVR-SILLRGFDQDMANKIGEHMEEHGIKFIRQFVPTKIEQi 259
Cdd:TIGR01423 181 FYLDEPPRRVLTVGGGFISVEFAGIFNAykpRGGKVTLCYRnNMILRGFDSTLRKELTKQLRANGINIMTNENPAKVTL- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 260 eaGTPGRLRVTAQSTNseetiEGEFNTVLLAVGRDSCTRTIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEGK 339
Cdd:TIGR01423 260 --NADGSKHVTFESGK-----TLDVDVVMMAIGRVPRTQTLQLDKVGVELTKK-GAIQVDEFSRTNVPNIYAIGDV-TDR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 340 LELTPVAIQAGRLLAQRLYGGSNVKCDYDNVPTTVFTPLEYGCCGLSEEKAVEKFgeENIEVYHSFFWPLEWTVPSRDNN 419
Cdd:TIGR01423 331 VMLTPVAINEGAAFVDTVFGNKPRKTDHTRVASAVFSIPPIGTCGLVEEDAAKKF--EKVAVYESSFTPLMHNISGSKYK 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 110224442 420 KCYAKIICNLKDDErVVGFHVLGPNAGEVTQGFAAALKCGLTKQQLDSTIGIHPVCAE 477
Cdd:TIGR01423 409 KFVAKIVTNHADGT-VLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAE 465
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
30-478 |
3.23e-75 |
|
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: 244.09 E-value: 3.23e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 30 EAAKFDKKVLVLDfvtptplgtRWGLGGTCVNVGCIPKK-LMHQAALLGQAlKDSRNYGWKVEdTVKHDWEKMTESVQSH 108
Cdd:TIGR01350 19 RAAQLGLKVALVE---------KEYLGGTCLNVGCIPTKaLLHSAEVYDEI-KHAKDLGIEVE-NVSVDWEKMQKRKNKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 109 IGSLNWGYRVALREKKVVYENAYGRFIGPHRIVATNNKGKEKiYSAERFLIATGERPRYLGIP--GDKEYCISSDDLFSL 186
Cdd:TIGR01350 88 VKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGENGEET-LEAKNIIIATGSRPRSLPGPfdFDGKVVITSTGALNL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 187 PYCPGKTLVVGASYVALECAGFLAGIGLDVTV--MVRSILlRGFDQDMANKIGEHMEEHGIKFIRQfvpTKIEQIEAGtP 264
Cdd:TIGR01350 167 EEVPESLVIIGGGVIGIEFASIFASLGSKVTVieMLDRIL-PGEDAEVSKVLQKALKKKGVKILTN---TKVTAVEKN-D 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 265 GRLRVTaQSTNSEETIEGEFntVLLAVGRDSCTRTIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILeGKLELTP 344
Cdd:TIGR01350 242 DQVTYE-NKGGETETLTGEK--VLVAVGRKPNTEGLGLEKLGVELDER-GRIVVDEYMRTNVPGIYAIGDVI-GGPMLAH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 345 VAIQAGRLLAQRLYGGSNVKCDYDNVPTTVFTPLEYGCCGLSEEKAvekfGEENIEVYHSFFwPLEWTVPSR--DNNKCY 422
Cdd:TIGR01350 317 VASHEGIVAAENIAGKEPAHIDYDAVPSVIYTDPEVASVGLTEEQA----KEAGYDVKIGKF-PFAANGKALalGETDGF 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 110224442 423 AKIICNlKDDERVVGFHVLGPNAGEVTQGFAAALKCGLTKQQLDSTIGIHPVCAEI 478
Cdd:TIGR01350 392 VKIIAD-KKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEA 446
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
30-481 |
1.26e-64 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 216.20 E-value: 1.26e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 30 EAAKFDKKVLVLDfvtPTPLGtrwglgGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVEDtVKHDWEKMTESVQSHI 109
Cdd:PRK06292 21 RAAKLGKKVALIE---KGPLG------GTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHADG-PKIDFKKVMARVRRER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 110 GSLNWGYRVALREK-KVVYENAYGRFIGPHRIVAtnnkgKEKIYSAERFLIATGER-PRYLGI-PGDKEYCISSDDLFSL 186
Cdd:PRK06292 91 DRFVGGVVEGLEKKpKIDKIKGTARFVDPNTVEV-----NGERIEAKNIVIATGSRvPPIPGVwLILGDRLLTSDDAFEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 187 PYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHgIKFIrqfVPTKIEQIEAgtpG 265
Cdd:PRK06292 166 DKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGdRILPLEDPEVSKQAQKILSKE-FKIK---LGAKVTSVEK---S 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 266 RLRVTAQSTNSEETIEGEFNTVLLAVGRDSCTRTIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILeGKLELTPV 345
Cdd:PRK06292 239 GDEKVEELEKGGKTETIEADYVLVATGRRPNTDGLGLENTGIELDER-GRPVVDEHTQTSVPGIYAAGDVN-GKPPLLHE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 346 AIQAGRLLAQRLYGGSNVKCDYDNVPTTVFTPLEYGCCGLSEEKAVEKFGEenievYHSFFWPLEWTVPSR--DNNKCYA 423
Cdd:PRK06292 317 AADEGRIAAENAAGDVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGID-----YVVGEVPFEAQGRARvmGKNDGFV 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 110224442 424 KIICNlKDDERVVGFHVLGPNAGEVTQGFAAALKCGLTKQQLDSTIGIHPVCAEIFTT 481
Cdd:PRK06292 392 KVYAD-KKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRT 448
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
55-499 |
3.00e-63 |
|
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: 213.05 E-value: 3.00e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 55 LGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVEDTVkhDWEKMTESVQSHIGSL-NWGYRVALREKKVVYENAYGR 133
Cdd:TIGR02053 34 LGGTCVNVGCVPSKMLLRAAEVAHYARKPPFGGLAATVAV--DFGELLEGKREVVEELrHEKYEDVLSSYGVDYLRGRAR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 134 FIGPHRIVAtnNKGKEkIYSAERFLIATGERPRYLGIPGDKE--YcISSDDLFSLPYCPGKTLVVGASYVALECAGFLAG 211
Cdd:TIGR02053 112 FKDPKTVKV--DLGRE-VRGAKRFLIATGARPAIPPIPGLKEagY-LTSEEALALDRIPESLAVIGGGAIGVELAQAFAR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 212 IGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHGIKFIRQfvpTKIEQIEAgTPGRLRVTAQSTNSEETIEGEFntVLLA 290
Cdd:TIGR02053 188 LGSEVTILQRSdRLLPREEPEISAAVEEALAEEGIEVVTS---AQVKAVSV-RGGGKIITVEKPGGQGEVEADE--LLVA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 291 VGRDSCTRTIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILeGKLELTPVAIQAGRLLAQRLYGGSNVKCDYDNV 370
Cdd:TIGR02053 262 TGRRPNTDGLGLEKAGVKLDER-GGILVDETLRTSNPGIYAAGDVT-GGLQLEYVAAKEGVVAAENALGGANAKLDLLVI 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 371 PTTVFTPLEYGCCGLSEEKAVEKFGEENIEVYHSFFWPLEWTvpsRDNNKCYAKIICNlKDDERVVGFHVLGPNAGEVTQ 450
Cdd:TIGR02053 340 PRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNVPRARI---NRDTRGFIKLVAE-PGTGKVLGVQVVAPEAAEVIN 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 110224442 451 GFAAALKCGLTKQQLDSTIGIHPVCAEI--FTTLSVTKrsggDILQSGCUG 499
Cdd:TIGR02053 416 EAALAIRAGMTVDDLIDTLHPFPTMAEGlkLAAQTFYR----DVSKLSCCA 462
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
55-478 |
8.78e-63 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 211.54 E-value: 8.78e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 55 LGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVEDtVKHDWEKMTESVQSHIGSLNWGYRVALREKKVVYENAYGRF 134
Cdd:PRK06416 38 LGGTCLNRGCIPSKALLHAAERADEARHSEDFGIKAEN-VGIDFKKVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 135 IGPHRIVATNNKGkEKIYSAERFLIATGERPRYL-GIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIG 213
Cdd:PRK06416 117 VDPNTVRVMTEDG-EQTYTAKNIILATGSRPRELpGIEIDGRVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 214 LDVTV---MVRsiLLRGFDQDMANKIGEHMEEHGIKFIrqfVPTKIEQIEAGTPGrLRVTAQSTNSEETIEGEfnTVLLA 290
Cdd:PRK06416 196 AEVTIveaLPR--ILPGEDKEISKLAERALKKRGIKIK---TGAKAKKVEQTDDG-VTVTLEDGGKEETLEAD--YVLVA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 291 VGRDSCTRTIGLETVGVKINEktGKIPVTDEEQTNVPYIYAIGDILeGKLELTPVAIQAGRLLAQRLyGGSNVKCDYDNV 370
Cdd:PRK06416 268 VGRRPNTENLGLEELGVKTDR--GFIEVDEQLRTNVPNIYAIGDIV-GGPMLAHKASAEGIIAAEAI-AGNPHPIDYRGI 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 371 PTTVFTPLEYGCCGLSEEKAVEKFGEenIEVYHSFFwplewtvpsRDNNKCYA--------KIICNlKDDERVVGFHVLG 442
Cdd:PRK06416 344 PAVTYTHPEVASVGLTEAKAKEEGFD--VKVVKFPF---------AGNGKALAlgetdgfvKLIFD-KKDGEVLGAHMVG 411
|
410 420 430
....*....|....*....|....*....|....*.
gi 110224442 443 PNAGEVTQGFAAALKCGLTKQQLDSTIGIHPVCAEI 478
Cdd:PRK06416 412 ARASELIQEAQLAINWEATPEDLALTIHPHPTLSEA 447
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
55-482 |
4.00e-58 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 199.27 E-value: 4.00e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 55 LGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVEDTVKHDWEKMTESVQSHIGSLNWGYRVALREKK---VVYENAy 131
Cdd:PRK06370 39 LGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGGPVSVDFKAVMARKRRIRARSRHGSEQWLRGLEgvdVFRGHA- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 132 gRFIGPHRIVATNnkgkeKIYSAERFLIATGERPRYLGIPG--DKEYcISSDDLFSLPYCPGKTLVVGASYVALECAGFL 209
Cdd:PRK06370 118 -RFESPNTVRVGG-----ETLRAKRIFINTGARAAIPPIPGldEVGY-LTNETIFSLDELPEHLVIIGGGYIGLEFAQMF 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 210 AGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHGIKFIrqfVPTKIEQIEaGTPGRLRVTAQSTNSEETIEGEfnTVL 288
Cdd:PRK06370 191 RRFGSEVTVIERGpRLLPREDEDVAAAVREILEREGIDVR---LNAECIRVE-RDGDGIAVGLDCNGGAPEITGS--HIL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 289 LAVGRDSCTRTIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEGKLELTPVAIQAGRLLAQRLYGGSNVKCDYD 368
Cdd:PRK06370 265 VAVGRVPNTDDLGLEAAGVETDAR-GYIKVDDQLRTTNPGIYAAGDC-NGRGAFTHTAYNDARIVAANLLDGGRRKVSDR 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 369 NVPTTVFTPLEYGCCGLSEEKAVEKfGEeNIEVYhsffwplewTVPSRD--------NNKCYAKIICNlKDDERVVGFHV 440
Cdd:PRK06370 343 IVPYATYTDPPLARVGMTEAEARKS-GR-RVLVG---------TRPMTRvgravekgETQGFMKVVVD-ADTDRILGATI 410
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 110224442 441 LGPNAGEVTQGFAAALKCGLTKQQLDSTIGIHPVCAEIFTTL 482
Cdd:PRK06370 411 LGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIPTL 452
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
29-350 |
1.62e-53 |
|
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: 182.52 E-value: 1.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 29 KEAAKFDKKVLVLdfvtptplgtrwGLGGTCVNVGCIPKKLMHQAAllgqalkdsrnygwKVEDTVKHdWEKMTESVQSH 108
Cdd:pfam07992 17 LTLAQLGGKVTLI------------EDEGTCPYGGCVLSKALLGAA--------------EAPEIASL-WADLYKRKEEV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 109 IGSLNWGYRVALREKKVVYENAYGRFIGPHRIVatnnkGKEKIYSAERFLIATGERPRYLGIPGDKEYC------ISSDD 182
Cdd:pfam07992 70 VKKLNNGIEVLLGTEVVSIDPGAKKVVLEELVD-----GDGETITYDRLVIATGARPRLPPIPGVELNVgflvrtLDSAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 183 LFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHGIKFIRQFVPTKIEqiea 261
Cdd:pfam07992 145 ALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALdRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEII---- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 262 GTPGRLRVTaqsTNSEETIEGEfnTVLLAVGRDscTRTIGLETVGVKINEkTGKIPVTDEEQTNVPYIYAIGDILEGKLE 341
Cdd:pfam07992 221 GDGDGVEVI---LKDGTEIDAD--LVVVAIGRR--PNTELLEAAGLELDE-RGGIVVDEYLRTSVPGIYAAGDCRVGGPE 292
|
....*....
gi 110224442 342 LTPVAIQAG 350
Cdd:pfam07992 293 LAQNAVAQG 301
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
56-478 |
1.40e-46 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 167.82 E-value: 1.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 56 GGTCVNVGCIPKKLMHQAALLGQALKDSRNYGwkVEDTVKH-DWEKMTESVQSHIGSLNWG---YRVALREKKVVYENAY 131
Cdd:PRK07846 34 GGTCLNVGCIPTKMFVYAADVARTIREAARLG--VDAELDGvRWPDIVSRVFGRIDPIAAGgeeYRGRDTPNIDVYRGHA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 132 gRFIGPHRIVAtnnkGKEKIYSAERFLIATGERPRYLGIPGDKE--YcISSDDLFSLPYCPGKTLVVGASYVALECAGFL 209
Cdd:PRK07846 112 -RFIGPKTLRT----GDGEEITADQVVIAAGSRPVIPPVIADSGvrY-HTSDTIMRLPELPESLVIVGGGFIAAEFAHVF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 210 AGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHgIKFIRQFVPTKIEQieagTPGRLRVTaqsTNSEETIEGEfnTVL 288
Cdd:PRK07846 186 SALGVRVTVVNRSgRLLRHLDDDISERFTELASKR-WDVRLGRNVVGVSQ----DGSGVTLR---LDDGSTVEAD--VLL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 289 LAVGRDSCTRTIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEGKLELTPVAIQAGRLLAQRLYGGSN-VKCDY 367
Cdd:PRK07846 256 VATGRVPNGDLLDAAAAGVDVDED-GRVVVDEYQRTSAEGVFALGDV-SSPYQLKHVANHEARVVQHNLLHPDDlIASDH 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 368 DNVPTTVFTPLEYGCCGLSEEKAVEKfgEENIEVYHSFF------WPLEWTvpsrdnnKCYAKIICNlKDDERVVGFHVL 441
Cdd:PRK07846 334 RFVPAAVFTHPQIASVGLTENEARAA--GLDITVKVQNYgdvaygWAMEDT-------TGFVKLIAD-RDTGRLLGAHII 403
|
410 420 430
....*....|....*....|....*....|....*...
gi 110224442 442 GPNAGEVTQGFAAALKCGLTKQQL-DSTIGIHPVCAEI 478
Cdd:PRK07846 404 GPQASTLIQPLIQAMSFGLDAREMaRGQYWIHPALPEV 441
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
55-488 |
1.11e-44 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 163.56 E-value: 1.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 55 LGGTCVNVGCIPKK-LMHQAALLGQALKDSRNYGWKVEDtVKHDWEKMTESVQSHIGSLNWGYRVALREKKVVYENAYGR 133
Cdd:PRK06327 45 LGGTCLNVGCIPSKaLLASSEEFENAGHHFADHGIHVDG-VKIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 134 FIGPH---RIVATNNKGKEKIySAERFLIATGERPRYL-GIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFL 209
Cdd:PRK06327 124 FVGKTdagYEIKVTGEDETVI-TAKHVIIATGSEPRHLpGVPFDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVW 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 210 AGIGLDVTVM-VRSILLRGFDQDMANKIGEHMEEHGIKFIrqfVPTKIEQIEAGTPGrLRVTAQSTNSEETIEgEFNTVL 288
Cdd:PRK06327 203 RRLGAEVTILeALPAFLAAADEQVAKEAAKAFTKQGLDIH---LGVKIGEIKTGGKG-VSVAYTDADGEAQTL-EVDKLI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 289 LAVGRDSCTRTIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILEGKLeLTPVAIQAGRLLAQRLyGGSNVKCDYD 368
Cdd:PRK06327 278 VSIGRVPNTDGLGLEAVGLKLDER-GFIPVDDHCRTNVPNVYAIGDVVRGPM-LAHKAEEEGVAVAERI-AGQKGHIDYN 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 369 NVPTTVFTPLEYGCCGLSEEKAVekfgEENIEVYHSFFwplewtvPSRDNNKC--------YAKIICNLKDDeRVVGFHV 440
Cdd:PRK06327 355 TIPWVIYTSPEIAWVGKTEQQLK----AEGVEYKAGKF-------PFMANGRAlamgepdgFVKIIADAKTD-EILGVHV 422
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 110224442 441 LGPNAGEVTQGFAAALKCGLTKQQLDSTIGIHPVCAEIF--TTLSVTKRS 488
Cdd:PRK06327 423 IGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEVWheAALAVDKRP 472
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
31-447 |
1.42e-41 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 154.54 E-value: 1.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 31 AAKFDKKVLVLDfvtptplgTRWGLGGTCVNVGCIPKKLMHQAAL-LGQALKDS--RNYGWKVEDTVKhDWEKMTESVQS 107
Cdd:PRK05249 24 AAKLGKRVAVIE--------RYRNVGGGCTHTGTIPSKALREAVLrLIGFNQNPlySSYRVKLRITFA-DLLARADHVIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 108 HigslnwgyRVALREK-----KVVYENAYGRFIGPHRIVATNNKGKEKIYSAERFLIATGERP-RYLGIPGDKEYCISSD 181
Cdd:PRK05249 95 K--------QVEVRRGqyernRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATGSRPyRPPDVDFDHPRIYDSD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 182 DLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVM-VRSILLRGFDQDMANKIGEHMEEHGIKfIRQfvPTKIEQIE 260
Cdd:PRK05249 167 SILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLInTRDRLLSFLDDEISDALSYHLRDSGVT-IRH--NEEVEKVE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 261 AGTPGRLRVTAqstnSEETIEGEfnTVLLAVGRDSCTRTIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILeGKL 340
Cdd:PRK05249 244 GGDDGVIVHLK----SGKKIKAD--CLLYANGRTGNTDGLNLENAGLEADSR-GQLKVNENYQTAVPHIYAVGDVI-GFP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 341 ELTPVAIQAGRLLAQRLYGGSNVKCdYDNVPTTVFTPLEYGCCGLSEEKAVekfgEENI--EVYHSFFWPLewtvpSR-- 416
Cdd:PRK05249 316 SLASASMDQGRIAAQHAVGEATAHL-IEDIPTGIYTIPEISSVGKTEQELT----AAKVpyEVGRARFKEL-----ARaq 385
|
410 420 430
....*....|....*....|....*....|....
gi 110224442 417 ---DNNKCYaKIICNLkDDERVVGFHVLGPNAGE 447
Cdd:PRK05249 386 iagDNVGML-KILFHR-ETLEILGVHCFGERATE 417
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
55-498 |
3.34e-40 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 152.61 E-value: 3.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 55 LGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVEDTVKHDWEKMTESVQShigslnwgyRV-ALREKKvvYEN---- 129
Cdd:PRK13748 132 IGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDGGIAATVPTIDRSRLLAQQQA---------RVdELRHAK--YEGildg 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 130 --------AYGRFIGPHRIVATNNKGKEKIYSAERFLIATGERPRYLGIPGDKE--YCISSDDLFSlPYCPGKTLVVGAS 199
Cdd:PRK13748 201 npaitvlhGEARFKDDQTLIVRLNDGGERVVAFDRCLIATGASPAVPPIPGLKEtpYWTSTEALVS-DTIPERLAVIGSS 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 200 YVALECAGFLAGIGLDVTVMVRSILLrgFDQDMAnkIGEHM----EEHGIKFIRQfvpTKIEQIeAGTPGRLRVTaqstn 275
Cdd:PRK13748 280 VVALELAQAFARLGSKVTILARSTLF--FREDPA--IGEAVtaafRAEGIEVLEH---TQASQV-AHVDGEFVLT----- 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 276 seeTIEGEF--NTVLLAVGRDSCTRTIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILEgKLELTPVAIQAGRLL 353
Cdd:PRK13748 347 ---TGHGELraDKLLVATGRAPNTRSLALDAAGVTVNAQ-GAIVIDQGMRTSVPHIYAAGDCTD-QPQFVYVAAAAGTRA 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 354 AQRLYGGsNVKCDYDNVPTTVFTPLEYGCCGLSEEKAvekfGEENIEVyHSFFWPLEwTVPSRDNN---KCYAKIICNlK 430
Cdd:PRK13748 422 AINMTGG-DAALDLTAMPAVVFTDPQVATVGYSEAEA----HHDGIET-DSRTLTLD-NVPRALANfdtRGFIKLVIE-E 493
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110224442 431 DDERVVGFHVLGPNAGEVTQGFAAALKCGLTKQQLDSTI--------GIHpVCAEIFTTlsvtkrsggDILQSGCU 498
Cdd:PRK13748 494 GSGRLIGVQAVAPEAGELIQTAALAIRNRMTVQELADQLfpyltmveGLK-LAAQTFNK---------DVKQLSCC 559
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
56-478 |
8.70e-40 |
|
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and related species, can form a disulfide-linked dimer called mycothione. This enzyme can reduce mycothione to regenerate two mycothiol molecules. The enzyme shows some sequence similarity to glutathione-disulfide reductase, trypanothione-disulfide reductase, and dihydrolipoamide dehydrogenase. The characterized protein from M. tuberculosis, a homodimer, has FAD as a cofactor, one per monomer, and uses NADPH as a substrate.
Pssm-ID: 132493 [Multi-domain] Cd Length: 452 Bit Score: 149.52 E-value: 8.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 56 GGTCVNVGCIPKKLMHQAALLGQALKDSRNYGwkVEDTVKH-DWEKMTESVQSH----IGSLNWGYRVALREKKVVYENA 130
Cdd:TIGR03452 35 GGTCLNVGCIPTKMFVYAAEVAQSIGESARLG--IDAEIDSvRWPDIVSRVFGDridpIAAGGEDYRRGDETPNIDVYDG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 131 YGRFIGPHRIvatnNKGKEKIYSAERFLIATGERPR---YLGIPGDKEYciSSDDLFSLPYCPGKTLVVGASYVALECAG 207
Cdd:TIGR03452 113 HARFVGPRTL----RTGDGEEITGDQIVIAAGSRPYippAIADSGVRYH--TNEDIMRLPELPESLVIVGGGYIAAEFAH 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 208 FLAGIGLDVTVMVRS-ILLRGFDQDMANKIGE----HMEEHGIKFIrqfvpTKIEQIEAGtpgrlrvTAQSTNSEETIEG 282
Cdd:TIGR03452 187 VFSALGTRVTIVNRStKLLRHLDEDISDRFTEiakkKWDIRLGRNV-----TAVEQDGDG-------VTLTLDDGSTVTA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 283 EfnTVLLAVGRDSCTRTIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEGKLELTPVAIQAGRLLAQRLYGGSN 362
Cdd:TIGR03452 255 D--VLLVATGRVPNGDLLDAEAAGVEVDED-GRIKVDEYGRTSARGVWALGDV-SSPYQLKHVANAEARVVKHNLLHPND 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 363 -VKCDYDNVPTTVFTPLEYGCCGLSEEKAVEKFGEENIEVYH----SFFWPLEWTvpsrdnnKCYAKIICNlKDDERVVG 437
Cdd:TIGR03452 331 lRKMPHDFVPSAVFTHPQIATVGLTEQEAREAGHDITVKIQNygdvAYGWAMEDT-------TGFCKLIAD-RDTGKLLG 402
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 110224442 438 FHVLGPNAGEVTQGFAAALKCGLTKQQL-DSTIGIHPVCAEI 478
Cdd:TIGR03452 403 AHIIGPQASSLIQPLITAMAFGLDAREMaRKQYWIHPALPEV 444
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
370-482 |
1.88e-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: 1.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 370 VPTTVFTPLEYGCCGLSEEKAVEKFGEenIEVYHSFFWPLEWTVPSRDNnKCYAKIICNlKDDERVVGFHVLGPNAGEVT 449
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGE--VKVGKFPFAANGRALAYGDT-DGFVKLVAD-RETGKILGAHIVGPNAGELI 76
|
90 100 110
....*....|....*....|....*....|...
gi 110224442 450 QGFAAALKCGLTKQQLDSTIGIHPVCAEIFTTL 482
Cdd:pfam02852 77 QEAALAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
56-393 |
1.54e-32 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 129.10 E-value: 1.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 56 GGTCVNVGCIPKKLMHQAAllgqalkdsrNYGWKVEDTVKHdwekmTESVQSHIGSLNWGyrvALREKKVVYENAYGRFI 135
Cdd:PRK07251 40 GGTCINIGCIPTKTLLVAA----------EKNLSFEQVMAT-----KNTVTSRLRGKNYA---MLAGSGVDLYDAEAHFV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 136 GPHRIVATnnKGKEKI-YSAERFLIATGERPRYLGIPG--DKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGI 212
Cdd:PRK07251 102 SNKVIEVQ--AGDEKIeLTAETIVINTGAVSNVLPIPGlaDSKHVYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 213 GLDVTVM-VRSILLRGFDQDMANKIGEHMEEHGIKFIRQfvpTKIEQIEAgTPGRLRVTaqsTNSEETIegeFNTVLLAV 291
Cdd:PRK07251 180 GSKVTVLdAASTILPREEPSVAALAKQYMEEDGITFLLN---AHTTEVKN-DGDQVLVV---TEDETYR---FDALLYAT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 292 GRDSCTRTIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEGKLELTPVAIQAGRLLAQRLYGGS--NVKcDYDN 369
Cdd:PRK07251 250 GRKPNTEPLGLENTDIELTER-GAIKVDDYCQTSVPGVFAVGDV-NGGPQFTYISLDDFRIVFGYLTGDGsyTLE-DRGN 326
|
330 340
....*....|....*....|....
gi 110224442 370 VPTTVFTPLEYGCCGLSEEKAVEK 393
Cdd:PRK07251 327 VPTTMFITPPLSQVGLTEKEAKEA 350
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
55-481 |
4.41e-30 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 124.26 E-value: 4.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 55 LGGTCVNVGCIPKKLMHQAA----------------LLGQALKDSRNYGWK----VEDTVKHDWEKMTESVQSHIGSLNW 114
Cdd:PTZ00153 152 IGGTCVNVGCIPSKALLYATgkyrelknlaklytygIYTNAFKNGKNDPVErnqlVADTVQIDITKLKEYTQSVIDKLRG 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 115 GYRVALREKKVVYENAYGRFIGPH-RIVATNNKGKEK---IYSAERFLIATGERPRY-LGIPGDKEYCISSDDLFSLPYC 189
Cdd:PTZ00153 232 GIENGLKSKKFCKNSEHVQVIYERgHIVDKNTIKSEKsgkEFKVKNIIIATGSTPNIpDNIEVDQKSVFTSDTAVKLEGL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 190 PGKTLVVGASYVALECAGFLAGIGLDVT-VMVRSILLRGFDQDMANkigeHMEEHGIKF--IRQFVPTKIEQIEAG---T 263
Cdd:PTZ00153 312 QNYMGIVGMGIIGLEFMDIYTALGSEVVsFEYSPQLLPLLDADVAK----YFERVFLKSkpVRVHLNTLIEYVRAGkgnQ 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 264 PGRLRVTAQSTNSEETIEGEFNTV--------LLAVGRDSCTRTIGLETVGVKINEktGKIPVTD------EEQTNVPYI 329
Cdd:PTZ00153 388 PVIIGHSERQTGESDGPKKNMNDIketyvdscLVATGRKPNTNNLGLDKLKIQMKR--GFVSVDEhlrvlrEDQEVYDNI 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 330 YAIGDIlEGKLELTPV----AIQAGRLLAQRlyGGSNVKCD----------YDNVPTTVFTPLEYGCCGLSEEKAVEKFG 395
Cdd:PTZ00153 466 FCIGDA-NGKQMLAHTashqALKVVDWIEGK--GKENVNINvenwaskpiiYKNIPSVCYTTPELAFIGLTEKEAKELYP 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 396 EENIEVYHSFF-------WPLEWTVPSRDNNKCYAKIICN-------------LKDDERVVGFHVLGPNAGEVTQGFAAA 455
Cdd:PTZ00153 543 PDNVGVEISFYkanskvlCENNISFPNNSKNNSYNKGKYNtvdntegmvkivyLKDTKEILGMFIVGSYASILIHEGVLA 622
|
490 500
....*....|....*....|....*.
gi 110224442 456 LKCGLTKQQLDSTIGIHPVCAEIFTT 481
Cdd:PTZ00153 623 INLKLSVKDLAHMVHSHPTISEVLDA 648
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
56-390 |
1.09e-29 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 121.04 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 56 GGTCVNVGCIP-KKLMHQAALlgqalkdsrnygwkvedtvKHDWEKMTESvQSHIGSLnwgyrvaLREK---------KV 125
Cdd:NF040477 40 GGTCINIGCIPtKTLVHDAEQ-------------------HQDFSTAMQR-KSSVVGF-------LRDKnyhnladldNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 126 VYENAYGRFIGPHRIVATNNKGKEKIYsAERFLIATGERPRYLGIPGDKEY--CISSDDLFSLPYCPGKTLVVGASYVAL 203
Cdd:NF040477 93 DVINGRAEFIDNHTLRVFQADGEQELR-GEKIFINTGAQSVLPPIPGLTTTpgVYDSTGLLNLTQLPARLGILGGGYIGV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 204 ECAGFLAGIGLDVTVM-VRSILLRGFDQDMANKIGEHMEEHGIKFIRQFVPTKIEQIEAgtpgrlRVTAQSTNSEETieg 282
Cdd:NF040477 172 EFASMFARFGSKVTIFeAAELFLPREDRDIAQAIATILQDQGVELILNAQVQRVSSHEG------EVQLETAEGVLT--- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 283 eFNTVLLAVGRDSCTRTIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEGKLELTPVAIQAGRLLAQRLYG-GS 361
Cdd:NF040477 243 -VDALLVASGRKPATAGLQLQNAGVAVNER-GAIVVDKYLRTTADNIWAMGDV-TGGLQFTYISLDDFRIVRDSLLGeGK 319
|
330 340
....*....|....*....|....*....
gi 110224442 362 NVKCDYDNVPTTVFTPLEYGCCGLSEEKA 390
Cdd:NF040477 320 RSTDDRQNVPYSVFMTPPLSRIGMTEEQA 348
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
56-482 |
3.87e-24 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 104.71 E-value: 3.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 56 GGTCVNVGCIPKKlmhqaallgqalkdsrnygwkvedTVKHDWEKMTE---SVQSHIGSLNWgyrvaLREKK-------- 124
Cdd:PRK08010 40 GGTCINIGCIPTK------------------------TLVHDAQQHTDfvrAIQRKNEVVNF-----LRNKNfhnladmp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 125 -VVYENAYGRFIGPHRIvATNNKGKEKIYSAERFLIATGERPRYLGIPG--DKEYCISSDDLFSLPYCPGKTLVVGASYV 201
Cdd:PRK08010 91 nIDVIDGQAEFINNHSL-RVHRPEGNLEIHGEKIFINTGAQTVVPPIPGitTTPGVYDSTGLLNLKELPGHLGILGGGYI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 202 ALECAGFLAGIGLDVTVM-VRSILLRGFDQDMANKIGEHMEEHGIKFIR----QFVPTKIEQIEAGTP-GRLRVTAqstn 275
Cdd:PRK08010 170 GVEFASMFANFGSKVTILeAASLFLPREDRDIADNIATILRDQGVDIILnahvERISHHENQVQVHSEhAQLAVDA---- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 276 seetiegefntVLLAVGRDSCTRTIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEGKLELTPVAIQAGRLLAQ 355
Cdd:PRK08010 246 -----------LLIASGRQPATASLHPENAGIAVNER-GAIVVDKYLHTTADNIWAMGDV-TGGLQFTYISLDDYRIVRD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 356 RLYG-GSNVKCDYDNVPTTVFTPLEYGCCGLSEEKAVEKFGEENIEVYhsffwPLEWTVPSR--DNNKCYAKIICNLKdD 432
Cdd:PRK08010 313 ELLGeGKRSTDDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTL-----PVAAIPRARvmNDTRGVLKAIVDNK-T 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 110224442 433 ERVVGFHVLGPNAGEVTQGFAAALKCGLTKQQLDSTIGIHPVCAEIFTTL 482
Cdd:PRK08010 387 QRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLNDL 436
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
31-473 |
4.20e-24 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 104.94 E-value: 4.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 31 AAKFDKKVLVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVED--TVKHDWEKMTESV--- 105
Cdd:PRK07845 20 AAQLGADVTVIE---------RDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRFIDdgEARVDLPAVNARVkal 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 106 ---QSHigslnwGYRVALREKKVVYENAYGRFI----GPHRIVATNNKGKEKIYSAERFLIATGERPRYLgiPG---DKE 175
Cdd:PRK07845 91 aaaQSA------DIRARLEREGVRVIAGRGRLIdpglGPHRVKVTTADGGEETLDADVVLIATGASPRIL--PTaepDGE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 176 YCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVT-VMVRSILLRGFDQDMANKIGEHMEEHGIKFIRQFVPT 254
Cdd:PRK07845 163 RILTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTlVSSRDRVLPGEDADAAEVLEEVFARRGMTVLKRSRAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 255 KIEQIEAGtpgrLRVTaqsTNSEETIEGefNTVLLAVGRDSCTRTIGLETVGVKINEkTGKIPVTDEEQTNVPYIYAIGD 334
Cdd:PRK07845 243 SVERTGDG----VVVT---LTDGRTVEG--SHALMAVGSVPNTAGLGLEEAGVELTP-SGHITVDRVSRTSVPGIYAAGD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 335 IlEGKLELTPVAIQAGRL-LAQRLygGSNVK-CDYDNVPTTVFTPLEYGCCGLSeEKAVEKfGEENIEVYhsffwplewT 412
Cdd:PRK07845 313 C-TGVLPLASVAAMQGRIaMYHAL--GEAVSpLRLKTVASNVFTRPEIATVGVS-QAAIDS-GEVPARTV---------M 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110224442 413 VPSRDNNKC--------YAKIICNlKDDERVVGFHVLGPNAGEVTQGFAAALKCGLTKQQLDSTIGIHP 473
Cdd:PRK07845 379 LPLATNPRAkmsglrdgFVKLFCR-PGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYP 446
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
124-352 |
1.38e-23 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 100.96 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 124 KVVYENAYG-RFIGPHRIVATNNkgkEKIYSAERFLIATGERPRYLGIPGDKE-------YCISSDdlfsLPYCPGKT-L 194
Cdd:COG0492 73 EILLEEVTSvDKDDGPFRVTTDD---GTEYEAKAVIIATGAGPRKLGLPGEEEfegrgvsYCATCD----GFFFRGKDvV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 195 VVGASYVALECAGFLAGIGLDVTVMVRSILLRGfDQDMANKIGEHmeeHGIKFIRQFVPTKIEqieaGTPGRLRVTAQST 274
Cdd:COG0492 146 VVGGGDSALEEALYLTKFASKVTLIHRRDELRA-SKILVERLRAN---PKIEVLWNTEVTEIE----GDGRVEGVTLKNV 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110224442 275 NSEETIEGEFNTVLLAVGRDSCTRTigLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILEGKLELTPVAIQAGRL 352
Cdd:COG0492 218 KTGEEKELEVDGVFVAIGLKPNTEL--LKGLGLELDED-GYIVVDEDMETSVPGVFAAGDVRDYKYRQAATAAGEGAI 292
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
158-383 |
1.28e-21 |
|
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];
Pssm-ID: 440215 [Multi-domain] Cd Length: 322 Bit Score: 95.65 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 158 LIATGERPRYLGIPGdkeycISSDDLFSL------PYC--------PGKTLVVGASYVALECAGFLAGIGLDVTVMVRS- 222
Cdd:COG0446 83 VLATGARPRPPPIPG-----LDLPGVFTLrtlddaDALrealkefkGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAp 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 223 ILLRGFDQDMANKIGEHMEEHGIKFIRQFVPTKIEqieagtpGRLRVTAQSTNSEETiegEFNTVLLAVG--------RD 294
Cdd:COG0446 158 RLLGVLDPEMAALLEEELREHGVELRLGETVVAID-------GDDKVAVTLTDGEEI---PADLVVVAPGvrpntelaKD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 295 SctrtigletvGVKINEkTGKIPVTDEEQTNVPYIYAIGDILE------GK---LELTPVAIQAGRLLAQRLYGGsnvKC 365
Cdd:COG0446 228 A----------GLALGE-RGWIKVDETLQTSDPDVYAAGDCAEvphpvtGKtvyIPLASAANKQGRVAAENILGG---PA 293
|
250
....*....|....*...
gi 110224442 366 DYDNVPTTVFTPleYGCC 383
Cdd:COG0446 294 PFPGLGTFISKV--FDLC 309
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
138-360 |
1.23e-20 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 93.67 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 138 HRIVATNNkGKEkiYSAERFLIATGERPRYLGIPG-DKEYCI---SSDDLFSL-PYCPGKT--LVVGASYVALECAGFLA 210
Cdd:COG1251 86 ARTVTLAD-GET--LPYDKLVLATGSRPRVPPIPGaDLPGVFtlrTLDDADALrAALAPGKrvVVIGGGLIGLEAAAALR 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 211 GIGLDVTVMVRS--ILLRGFDQDMANKIGEHMEEHGIKFIRQfvpTKIEQIEagtpGRLRVTAQSTNSEETIEGEFntVL 288
Cdd:COG1251 163 KRGLEVTVVERAprLLPRQLDEEAGALLQRLLEALGVEVRLG---TGVTEIE----GDDRVTGVRLADGEELPADL--VV 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 289 LAVG---RDSCTRTIGLETV-GVKINEKTgkipvtdeeQTNVPYIYAIGDILE------GK--LELTPVAIQAGRLLAQR 356
Cdd:COG1251 234 VAIGvrpNTELARAAGLAVDrGIVVDDYL---------RTSDPDIYAAGDCAEhpgpvyGRrvLELVAPAYEQARVAAAN 304
|
....
gi 110224442 357 LYGG 360
Cdd:COG1251 305 LAGG 308
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
192-268 |
1.14e-19 |
|
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: 83.02 E-value: 1.14e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110224442 192 KTLVVGASYVALECAGFLAGIGLDVTVMVRSI-LLRGFDQDMANKIGEHMEEHGIKFIRQFVPTKIEQIEAGTPGRLR 268
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDrLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLT 78
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
192-363 |
9.93e-15 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 75.97 E-value: 9.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 192 KTLVVGASYVALECAGFLAGIGLDVTVMVRSI-LLRGFDQDMANKIGEHMEEHGIkfirqfvPTKIEQIEAGTPGRLrVT 270
Cdd:PRK13512 150 KALVVGAGYISLEVLENLYERGLHPTLIHRSDkINKLMDADMNQPILDELDKREI-------PYRLNEEIDAINGNE-VT 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 271 AQSTNSEEtiegeFNTVLLAVGRDSCTRTIglETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILEG------KLELTP 344
Cdd:PRK13512 222 FKSGKVEH-----YDMIIEGVGTHPNSKFI--ESSNIKLDDK-GFIPVNDKFETNVPNIYAIGDIITShyrhvdLPASVP 293
|
170 180
....*....|....*....|..
gi 110224442 345 VAIQAGR---LLAQRLYGGSNV 363
Cdd:PRK13512 294 LAWGAHRaasIVAEQIAGNDTI 315
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
194-465 |
3.01e-12 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 68.53 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 194 LVVGASYVALECAGFLAGIGLDVTVMVRS--ILLRGFDQDMANKIGEHMEEHGIKFIRQFVPTKIEqieagtpGRLRVTA 271
Cdd:PRK09564 153 VIIGAGFIGLEAVEAAKHLGKNVRIIQLEdrILPDSFDKEITDVMEEELRENGVELHLNEFVKSLI-------GEDKVEG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 272 QSTNSEETiegEFNTVLLAVGRDSCTRTI---GLETVgvkineKTGKIPVTDEEQTNVPYIYAIGD------ILEGKLEL 342
Cdd:PRK09564 226 VVTDKGEY---EADVVIVATGVKPNTEFLedtGLKTL------KNGAIIVDEYGETSIENIYAAGDcatiynIVSNKNVY 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 343 TPVAIQA---GRLLAQRLYGGSNV-KCDYDNVPTTVFTpLEYGCCGLSEEKAVEKfgeeNIEVYHSFFWPLEWTVPSRDN 418
Cdd:PRK09564 297 VPLATTAnklGRMVGENLAGRHVSfKGTLGSACIKVLD-LEAARTGLTEEEAKKL----GIDYKTVFIKDKNHTNYYPGQ 371
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 110224442 419 NKCYAKIICNlKDDERVVGFHVLGPNaGEV--TQGFAAALKCGLTKQQL 465
Cdd:PRK09564 372 EDLYVKLIYE-ADTKVILGGQIIGKK-GAVlrIDALAVAIYAKLTTQEL 418
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
159-391 |
3.40e-11 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 64.77 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 159 IATGERPRYLGIPGDKEYCI---SSDDLFSL------------PYCPGKTLVVGASYVALECAGFLA----------GIG 213
Cdd:COG1252 103 IATGSVTNFFGIPGLAEHALplkTLEDALALrerllaaferaeRRRLLTIVVVGGGPTGVELAGELAellrkllrypGID 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 214 LD------VTVMVRsiLLRGFDQDMANKIGEHMEEHGIKFIRQfvpTKIEQIEAGTpgrlrVTaqsTNSEETIEgeFNTV 287
Cdd:COG1252 183 PDkvritlVEAGPR--ILPGLGEKLSEAAEKELEKRGVEVHTG---TRVTEVDADG-----VT---LEDGEEIP--ADTV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 288 LLAVG-------RDSctrtiGLETvgvkinEKTGKIPVTDEEQT-NVPYIYAIGDI--LEGKLELT-----PVAIQAGRL 352
Cdd:COG1252 248 IWAAGvkappllADL-----GLPT------DRRGRVLVDPTLQVpGHPNVFAIGDCaaVPDPDGKPvpktaQAAVQQAKV 316
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 110224442 353 LAQrlyggsNVKCDYDNVPTTVFTPLEYGC-CGLSEEKAV 391
Cdd:COG1252 317 LAK------NIAALLRGKPLKPFRYRDKGClASLGRGAAV 350
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
139-337 |
6.46e-09 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 58.30 E-value: 6.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 139 RIVATNNKGKEKIYSAER------FLIATGERPRYLGIPG-DKEYCI---SSDDLFSLPYCPGKTL---VVGASYVALEC 205
Cdd:TIGR02374 76 TVIQIDTDQKQVITDAGRtlsydkLILATGSYPFILPIPGaDKKGVYvfrTIEDLDAIMAMAQRFKkaaVIGGGLLGLEA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 206 AGFLAGIGLDVTV--MVRSILLRGFDQDMANKIGEHMEEHGIKFIRQfvPTKIEQIEAGTPGRLRVTaqstnSEETIEGE 283
Cdd:TIGR02374 156 AVGLQNLGMDVSVihHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLE--KDTVEIVGATKADRIRFK-----DGSSLEAD 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 110224442 284 FntVLLAVG---RDSCTRTIGLetvgvKINektGKIPVTDEEQTNVPYIYAIGDILE 337
Cdd:TIGR02374 229 L--IVMAAGirpNDELAVSAGI-----KVN---RGIIVNDSMQTSDPDIYAVGECAE 275
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
158-351 |
7.97e-09 |
|
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 440259 [Multi-domain] Cd Length: 434 Bit Score: 57.84 E-value: 7.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 158 LIATG-ERPRYLGIPG-DKEYCIS----------SDDLFSLPYCPGKTLVVGASYVALECAGFLAGIG-LDVTVMVRsil 224
Cdd:COG0493 211 FLATGaGKPRDLGIPGeDLKGVHSamdfltavnlGEAPDTILAVGKRVVVIGGGNTAMDCARTALRLGaESVTIVYR--- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 225 lRGFDqDMANKIGE--HMEEHGIKFIRQFVPTKI-------------EQIEAGTP---GRLRVTAqSTNSEETIEgeFNT 286
Cdd:COG0493 288 -RTRE-EMPASKEEveEALEEGVEFLFLVAPVEIigdengrvtglecVRMELGEPdesGRRRPVP-IEGSEFTLP--ADL 362
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110224442 287 VLLAVGRDSCTRTIgLETVGVKINEKtGKIpVTDEE--QTNVPYIYAIGDILEGklELTPV-AIQAGR 351
Cdd:COG0493 363 VILAIGQTPDPSGL-EEELGLELDKR-GTI-VVDEEtyQTSLPGVFAGGDAVRG--PSLVVwAIAEGR 425
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
148-355 |
1.14e-08 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 57.34 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 148 KEKIYSAerFLIATGE-RPRYLGIPGdkeycISSDDLFSL-----------PYCPG---------KTLVVGASYVALECA 206
Cdd:PRK12831 225 EEEGFDA--VFIGSGAgLPKFMGIPG-----ENLNGVFSAnefltrvnlmkAYKPEydtpikvgkKVAVVGGGNVAMDAA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 207 GFLAGIGLDVTVMVRsillRGfDQDMANKIGE--HMEEHGIKFIRQFVPTKI-------------EQIEAGTP---GRlR 268
Cdd:PRK12831 298 RTALRLGAEVHIVYR----RS-EEELPARVEEvhHAKEEGVIFDLLTNPVEIlgdengwvkgmkcIKMELGEPdasGR-R 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 269 VTAQSTNSEETIegEFNTVLLAVGRdSCTRTIGLETVGVKINEKtGKIpVTDEE--QTNVPYIYAIGDILEGklELTPV- 345
Cdd:PRK12831 372 RPVEIEGSEFVL--EVDTVIMSLGT-SPNPLISSTTKGLKINKR-GCI-VADEEtgLTSKEGVFAGGDAVTG--AATVIl 444
|
250
....*....|
gi 110224442 346 AIQAGRLLAQ 355
Cdd:PRK12831 445 AMGAGKKAAK 454
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
158-355 |
3.06e-08 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 55.96 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 158 LIATG-ERPRYLGIPGDK--------EYCISS---DDLFSLPycPGKTLVV-GASYVALECAGFLAGIGL-DVTVMVRsi 223
Cdd:PRK11749 230 FIGTGaGLPRFLGIPGENlggvysavDFLTRVnqaVADYDLP--VGKRVVViGGGNTAMDAARTAKRLGAeSVTIVYR-- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 224 llRGFDqDMANKIGE--HMEEHGIKFIRQFVPTKIEQIEAGTPG------RLRVTAQSTNSEETIEGEF-----NTVLLA 290
Cdd:PRK11749 306 --RGRE-EMPASEEEveHAKEEGVEFEWLAAPVEILGDEGRVTGvefvrmELGEPDASGRRRVPIEGSEftlpaDLVIKA 382
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110224442 291 VGRDScTRTIGLETVGVKINEKTGKIPVTDEEQTNVPYIYAIGDILEGKlELTPVAIQAGRLLAQ 355
Cdd:PRK11749 383 IGQTP-NPLILSTTPGLELNRWGTIIADDETGRTSLPGVFAGGDIVTGA-ATVVWAVGDGKDAAE 445
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
158-357 |
3.33e-08 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 55.38 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 158 LIATGE-RPRYLGIPG-DKEYCISS-DDLFS-----LPYCP---------GKTLVVGASYVALECA--GFLAGiGLDVTV 218
Cdd:PRK12770 123 LIATGTwKSRKLGIPGeDLPGVYSAlEYLFRiraakLGYLPwekvppvegKKVVVVGAGLTAVDAAleAVLLG-AEKVYL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 219 MVRsillRGFDQDMANKIG-EHMEEHGIKFIRQFVPTKI--------------EQIEAGTPGRLRvTAQSTNSEETIegE 283
Cdd:PRK12770 202 AYR----RTINEAPAGKYEiERLIARGVEFLELVTPVRIigegrvegvelakmRLGEPDESGRPR-PVPIPGSEFVL--E 274
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110224442 284 FNTVLLAVGrDSCTRTIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILEGKLELTPvAIQAGRLLAQRL 357
Cdd:PRK12770 275 ADTVVFAIG-EIPTPPFAKECLGIELNRK-GEIVVDEKHMTSREGVFAAGDVVTGPSKIGK-AIKSGLRAAQSI 345
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
154-338 |
5.11e-08 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 55.52 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 154 AERF---LIATGE-RPRYLGIPGDKEYCISS--------------DDLFSLPYCPGK-TLVVGASYVALECAGFLAGIGL 214
Cdd:PRK12778 515 EEGFkgiFIASGAgLPNFMNIPGENSNGVMSsneyltrvnlmdaaSPDSDTPIKFGKkVAVVGGGNTAMDSARTAKRLGA 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 215 DvTVMvrsILLRGFDQDMANKIGE--HMEEHGIKF----------------IRQFVPTKIEQIEAGTPGRLRVTAqSTNS 276
Cdd:PRK12778 595 E-RVT---IVYRRSEEEMPARLEEvkHAKEEGIEFltlhnpieyladekgwVKQVVLQKMELGEPDASGRRRPVA-IPGS 669
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110224442 277 EETIEgeFNTVLLAVGRdSCTRTIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILEG 338
Cdd:PRK12778 670 TFTVD--VDLVIVSVGV-SPNPLVPSSIPGLELNRK-GTIVVDEEMQSSIPGIYAGGDIVRG 727
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
140-333 |
2.56e-07 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 52.23 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 140 IVATNnKGKekiYSAERFLIATGE--RPRYLGIPgdkEYCISSDDLFSL-PYCPGKTLVVGASYVALECAGFLAGIGLDV 216
Cdd:pfam13738 109 VVTTS-KGT---YQARYVIIATGEfdFPNKLGVP---ELPKHYSYVKDFhPYAGQKVVVIGGYNSAVDAALELVRKGARV 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 217 TVMVRSILLRGFDQDMA--------NKIGEHMEEHGIKFIRQFVPTKIEQIEAGtpgrlrVTAQSTNSEETIegEFNTVL 288
Cdd:pfam13738 182 TVLYRGSEWEDRDSDPSyslspdtlNRLEELVKNGKIKAHFNAEVKEITEVDVS------YKVHTEDGRKVT--SNDDPI 253
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 110224442 289 LAVGRDSctrTIGLETVGVKINEKTGKIPVTDE-EQTNVPYIYAIG 333
Cdd:pfam13738 254 LATGYHP---DLSFLKKGLFELDEDGRPVLTEEtESTNVPGLFLAG 296
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
144-357 |
3.90e-07 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 53.02 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 144 NNKGKEKIysaerFLIATGERPRYLGIPGDKEYCISSDDLF---------------SLPYCPGKTLVV-GASYVALECAG 207
Cdd:PRK12775 514 NDKGFDAV-----FLGVGAGAPTFLGIPGEFAGQVYSANEFltrvnlmggdkfpflDTPISLGKSVVViGAGNTAMDCLR 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 208 FLAGIGldvTVMVRSILLRGfDQDMANKIGE--HMEEHGIKFIRQFVPT-------------KIEQIEAGTP---GRLRV 269
Cdd:PRK12775 589 VAKRLG---APTVRCVYRRS-EAEAPARIEEirHAKEEGIDFFFLHSPVeiyvdaegsvrgmKVEEMELGEPdekGRRKP 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 270 TAqstnSEETIEGEFNTVLLAVGRDScTRTIGLETVGVKINeKTGKIPVTDE-----EQTNVPYIYAIGDILEGKLELTp 344
Cdd:PRK12775 665 MP----TGEFKDLECDTVIYALGTKA-NPIITQSTPGLALN-KWGNIAADDGklestQSTNLPGVFAGGDIVTGGATVI- 737
|
250
....*....|...
gi 110224442 345 VAIQAGRLLAQRL 357
Cdd:PRK12775 738 LAMGAGRRAARSI 750
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
152-337 |
5.75e-06 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 48.13 E-value: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 152 YSAERFLIATGERPRYLGIPGDKEY-------CISSDDLFslpYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSIL 224
Cdd:PRK10262 104 YTCDALIIATGASARYLGLPSEEAFkgrgvsaCATCDGFF---YRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 225 LRGfDQDMANKIGEHMEEHGIKFIRQFVPTKIEQIEAGTPG-RLRVTaQSTNSEETIegEFNTVLLAVGRDSCTR----T 299
Cdd:PRK10262 181 FRA-EKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGvRLRDT-QNSDNIESL--DVAGLFVAIGHSPNTAifegQ 256
|
170 180 190
....*....|....*....|....*....|....*...
gi 110224442 300 IGLETVGVKINEKTGKipvtDEEQTNVPYIYAIGDILE 337
Cdd:PRK10262 257 LELENGYIKVQSGIHG----NATQTSIPGVFAAGDVMD 290
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
155-335 |
5.59e-04 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 42.22 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 155 ERFLIATGERPR---YLGIPGDKEYCI-SSDDLFSLPYC--PGKT-LVVGASYVALECAGFLAGIGLDVTVM--VRSILL 225
Cdd:PRK09754 102 DQLFIATGAAARplpLLDALGERCFTLrHAGDAARLREVlqPERSvVIVGAGTIGLELAASATQRRCKVTVIelAATVMG 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 226 RGFDQDMANKIGEHMEEHGIKFirqFVPTKIEQIEAGTPGRLRVtaqstNSEETIEGEFntVLLAVG---RDSCTRTIGL 302
Cdd:PRK09754 182 RNAPPPVQRYLLQRHQQAGVRI---LLNNAIEHVVDGEKVELTL-----QSGETLQADV--VIYGIGisaNDQLAREANL 251
|
170 180 190
....*....|....*....|....*....|...
gi 110224442 303 ETvgvkinekTGKIPVTDEEQTNVPYIYAIGDI 335
Cdd:PRK09754 252 DT--------ANGIVIDEACRTCDPAIFAGGDV 276
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
255-355 |
3.66e-03 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 39.76 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110224442 255 KIEQIEAGTPGRLRVTaqstNSEETIEGEFntVLLAVGRDSCTRTIgLETVGVKINEKtGKIPVTDEE-QTNVPYIYAIG 333
Cdd:PRK12810 366 KVVRTELGEGDFEPVE----GSEFVLPADL--VLLAMGFTGPEAGL-LAQFGVELDER-GRVAAPDNAyQTSNPKVFAAG 437
|
90 100
....*....|....*....|..
gi 110224442 334 DILEGKlELTPVAIQAGRLLAQ 355
Cdd:PRK12810 438 DMRRGQ-SLVVWAIAEGRQAAR 458
|
|
| |
