|
Name |
Accession |
Description |
Interval |
E-value |
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
41-526 |
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: 700.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 41 NFDLLVIGGGSGGLACAKEAAQLGRKVAVADYVEPSPRGTKWGLGGTCVNVGCIPKKLMHQAALLGGMIRDAQHYGWEVA 120
Cdd:TIGR01438 2 DYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPTPLGTRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 121 QPVQHNWKAMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVNEHTVHGVDKAGKVTQLSAKHIVIATGGRPKYPtQV 200
Cdd:TIGR01438 82 ETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERPRYP-GI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 201 KGALEHGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVMMRSVPLRGFDQQMASLVTEHMESHGTRFLKG 280
Cdd:TIGR01438 161 PGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDCANKVGEHMEEHGVKFKRQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 281 CVPSLIRKLPTNQLqVTWEDLASGKEdvGTFDTVLWAIGRVPETRNLNLEKAGVNTNPKNQKIIVDAQEATSVPHIYAIG 360
Cdd:TIGR01438 241 FVPIKVEQIEAKVL-VEFTDSTNGIE--EEYDTVLLAIGRDACTRKLNLENVGVKINKKTGKIPADEEEQTNVPYIYAVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 361 DVAEGRPELTPTAIKAGKLLAQRLFGKSSTLMNYSNVPTTVFTPLEYGCVGLSEEEAVALHGQEHIEVYHAYYKPLEFTV 440
Cdd:TIGR01438 318 DILEDKPELTPVAIQAGRLLAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENVEVFHSYFWPLEWTI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 441 ADRD-ASQCYIKMVCMREPPQLVLGLHFLGPNAGEVTQGFALGIQCGASYAQVMQTVGIHPTCSEEVVKLHISKRSGLDP 519
Cdd:TIGR01438 398 PSRDnHNKCYAKLVCNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTLSVTKRSGQDI 477
|
....*..
gi 55250718 520 TVTGCUG 526
Cdd:TIGR01438 478 LQQGCCG 484
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
42-526 |
0e+00 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 566.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 42 FDLLVIGGGSGGLACAKEAAQLGRKVAVADYVEPSPRGTKWGLGGTCVNVGCIPKKLMHQAALLGGMIR-DAQHYGWEVA 120
Cdd:PTZ00052 6 YDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKPSTQGTKWGLGGTCVNVGCVPKKLMHYAANIGSIFHhDSQMYGWKTS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 121 QpvQHNWKAMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVNEHTVHGVDKaGKVTQLSAKHIVIATGGRPKYPTQV 200
Cdd:PTZ00052 86 S--SFNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTVSYGDN-SQEETITAKYILIATGGRPSIPEDV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 201 KGALEHGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVMMRSVPLRGFDQQMASLVTEHMESHGTRFLKG 280
Cdd:PTZ00052 163 PGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRSIPLRGFDRQCSEKVVEYMKEQGTLFLEG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 281 CVPSLIRKLpTNQLQVTWEDlasgkEDVGTFDTVLWAIGRVPETRNLNLEKAGVNTNPKNQKIIVDaqEATSVPHIYAIG 360
Cdd:PTZ00052 243 VVPINIEKM-DDKIKVLFSD-----GTTELFDTVLYATGRKPDIKGLNLNAIGVHVNKSNKIIAPN--DCTNIPNIFAVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 361 DVAEGRPELTPTAIKAGKLLAQRLFGKSSTLMNYSNVPTTVFTPLEYGCVGLSEEEAVALHGQEHIEVYHAYYKPLEFTV 440
Cdd:PTZ00052 315 DVVEGRPELTPVAIKAGILLARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQEFNTLEIAA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 441 ADRD--------------ASQCYIKMVCMREPPQLVLGLHFLGPNAGEVTQGFALGIQCGASYAQVMQTVGIHPTCSEEV 506
Cdd:PTZ00052 395 VHREkherarkdeydfdvSSNCLAKLVCVKSEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHPTDAEVF 474
|
490 500
....*....|....*....|
gi 55250718 507 VKLHISKRSGLDPTVTGCUG 526
Cdd:PTZ00052 475 MNLSVTRRSGESFAAKGGCG 494
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
42-507 |
6.15e-153 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 444.60 E-value: 6.15e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 42 FDLLVIGGGSGGLACAKEAAQLGRKVAVADYVEpsprgtkwgLGGTCVNVGCIPKKLMHQAALLGGMIRD-AQHYGWEVA 120
Cdd:PRK06116 5 YDLIVIGGGSGGIASANRAAMYGAKVALIEAKR---------LGGTCVNVGCVPKKLMWYGAQIAEAFHDyAPGYGFDVT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 121 QPvQHNWKAMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVNEHTVHgVDKagkvTQLSAKHIVIATGGRPKYPTqV 200
Cdd:PRK06116 76 EN-KFDWAKLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVE-VNG----ERYTADHILIATGGRPSIPD-I 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 201 KGAlEHGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVMMRS-VPLRGFDQQMASLVTEHMESHGTRFLK 279
Cdd:PRK06116 149 PGA-EYGITSDGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGdAPLRGFDPDIRETLVEEMEKKGIRLHT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 280 GCVPSLIRKLPTNQLQVTWEDlasGKEDvgTFDTVLWAIGRVPETRNLNLEKAGVNTNpKNQKIIVDAQEATSVPHIYAI 359
Cdd:PRK06116 228 NAVPKAVEKNADGSLTLTLED---GETL--TVDCLIWAIGREPNTDGLGLENAGVKLN-EKGYIIVDEYQNTNVPGIYAV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 360 GDVaEGRPELTPTAIKAGKLLAQRLF-GKSSTLMNYSNVPTTVFTPLEYGCVGLSEEEAVALHGQEHIEVYHAYYKPLEF 438
Cdd:PRK06116 302 GDV-TGRVELTPVAIAAGRRLSERLFnNKPDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVKVYRSSFTPMYT 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55250718 439 TVADRDAsQCYIKMVCMREPPQlVLGLHFLGPNAGEVTQGFALGIQCGASYAQVMQTVGIHPTCSEEVV 507
Cdd:PRK06116 381 ALTGHRQ-PCLMKLVVVGKEEK-VVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFV 447
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
40-507 |
6.87e-131 |
|
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: 388.29 E-value: 6.87e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 40 QNFDLLVIGGGSGGLACAKEAAQLGRKVAVADyvepsprgtKWGLGGTCVNVGCIPKKLMHQAALLGGMIRDAQHYGWEV 119
Cdd:COG1249 2 KDYDLVVIGAGPGGYVAAIRAAQLGLKVALVE---------KGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 120 AQPvQHNWKAMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVNEHTVhgvdKAGKVTQLSAKHIVIATGGRPKYPTQ 199
Cdd:COG1249 73 GAP-SVDWAALMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTV----EVTGGETLTADHIVIATGSRPRVPPI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 200 VKGALEHGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVM-MRSVPLRGFDQQMASLVTEHMESHGTRFL 278
Cdd:COG1249 148 PGLDEVRVLTSDEALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVeRGDRLLPGEDPEISEALEKALEKEGIDIL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 279 KGCVPSLIRKLPtNQLQVTWEDlaSGKEDVGTFDTVLWAIGRVPETRNLNLEKAGVNTNPKNQkIIVDAQEATSVPHIYA 358
Cdd:COG1249 228 TGAKVTSVEKTG-DGVTVTLED--GGGEEAVEADKVLVATGRRPNTDGLGLEAAGVELDERGG-IKVDEYLRTSVPGIYA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 359 IGDVAeGRPELTPTAIKAGKLLAQRLFGKSSTLMNYSNVPTTVFTPLEYGCVGLSEEEAVALHGQehIEVYHAYYKPLEF 438
Cdd:COG1249 304 IGDVT-GGPQLAHVASAEGRVAAENILGKKPRPVDYRAIPSVVFTDPEIASVGLTEEEAREAGID--VKVGKFPFAANGR 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55250718 439 TVADRDAsQCYIKMVCMREpPQLVLGLHFLGPNAGEVTQGFALGIQCGASYAQVMQTVGIHPTCSEEVV 507
Cdd:COG1249 381 ALALGET-EGFVKLIADAE-TGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALK 447
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
42-509 |
3.13e-127 |
|
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: 378.80 E-value: 3.13e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 42 FDLLVIGGGSGGLACAKEAAQLGRKVAVADYVEpsprgtkwgLGGTCVNVGCIPKKLMHQAALLGGMIRDAQHYGWEVAQ 121
Cdd:TIGR01421 3 YDYLVIGGGSGGIASARRAAEHGAKALLVEAKK---------LGGTCVNVGCVPKKVMWYASDLAERMHDAADYGFYQND 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 122 PVQHNWKAMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVNEHTVHgVDKagkvTQLSAKHIVIATGGRPKYPTQVK 201
Cdd:TIGR01421 74 ENTFNWPELKEKRDAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGTVE-VNG----RDYTAPHILIATGGKPSFPENIP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 202 GAlEHGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVMMR-SVPLRGFDQQMASLVTEHMESHGTRFLKG 280
Cdd:TIGR01421 149 GA-ELGTDSDGFFALEELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRhERVLRSFDSMISETITEEYEKEGINVHKL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 281 CVPSLIRKLPTNQLQVTWEDLASgkedVGTFDTVLWAIGRVPETRNLNLEKAGVNTNPKNQkIIVDAQEATSVPHIYAIG 360
Cdd:TIGR01421 228 SKPVKVEKTVEGKLVIHFEDGKS----IDDVDELIWAIGRKPNTKGLGLENVGIKLNEKGQ-IIVDEYQNTNVPGIYALG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 361 DVAeGRPELTPTAIKAGKLLAQRLF-GKSSTLMNYSNVPTTVFTPLEYGCVGLSEEEAVALHGQEHIEVYHAYYKPLEFT 439
Cdd:TIGR01421 303 DVV-GKVELTPVAIAAGRKLSERLFnGKTDDKLDYNNVPTVVFSHPPIGTIGLTEKEAIEKYGKENIKVYNSSFTPMYYA 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 440 VADRdASQCYIKMVCMrEPPQLVLGLHFLGPNAGEVTQGFALGIQCGASYAQVMQTVGIHPTCSEEVVKL 509
Cdd:TIGR01421 382 MTSE-KQKCRMKLVCA-GKEEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEELVTM 449
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
41-507 |
2.62e-115 |
|
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: 348.34 E-value: 2.62e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 41 NFDLLVIGGGSGGLACAKEAAQLGRKVAVADyvepSPRgtkwgLGGTCVNVGCIPKKLMHQAALLGGMIRDAQHYGWEVA 120
Cdd:TIGR01424 2 DYDLFVIGAGSGGVRAARLAAALGAKVAIAE----EFR-----VGGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGWTVG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 121 QpVQHNWKAMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVNEHTVHGVDKAGKVTqlsAKHIVIATGGRPKYPtQV 200
Cdd:TIGR01424 73 K-ARFDWKKLLAAKDQEIARLSGLYRKGLANAGAELLDGRAELVGPNTVEVLASGKTYT---AEKILIAVGGRPPKP-AL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 201 KGAlEHGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVMMR-SVPLRGFDQQMASLVTEHMESHGTRFLK 279
Cdd:TIGR01424 148 PGH-ELGITSNEAFHLPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRgKEILRGFDDDMRRGLAAALEERGIRILP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 280 GCVPSLIRKLPTNQLQVTwedLASGKEDVGtfDTVLWAIGRVPETRNLNLEKAGVNTNPKNqKIIVDAQEATSVPHIYAI 359
Cdd:TIGR01424 227 EDSITSISKDDDGRLKAT---LSKHEEIVA--DVVLFATGRSPNTNGLGLEAAGVRLNDLG-AIAVDEYSRTSTPSIYAV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 360 GDVAEgRPELTPTAIKAGKLLAQRLFGKSSTLMNYSNVPTTVFTPLEYGCVGLSEEEAVALHGQehIEVYHAYYKPLEFT 439
Cdd:TIGR01424 301 GDVTD-RINLTPVAIHEATCFAETEFGNNPTSFDHDLIATAVFSQPPIGTVGLTEEEARRKFGD--IEVYRAEFRPMKAT 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55250718 440 VADRDaSQCYIKMVcMREPPQLVLGLHFLGPNAGEVTQGFALGIQCGASYAQVMQTVGIHPTCSEEVV 507
Cdd:TIGR01424 378 FSGRQ-EKTLMKLV-VDAKDDKVLGAHMVGPDAAEIIQGLAIALKMGATKDDFDSTVAVHPTSAEELV 443
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
41-514 |
4.05e-97 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 303.28 E-value: 4.05e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 41 NFDLLVIGGGSGGLACAKEAAQLGRKVAVADY-VEPSPRGTKWGLGGTCVNVGCIPKKLMHQAALLGGMIRDAQHYGWEV 119
Cdd:PLN02507 25 DFDLFVIGAGSGGVRAARFSANFGAKVGICELpFHPISSESIGGVGGTCVIRGCVPKKILVYGATFGGEFEDAKNYGWEI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 120 AQPVQHNWKAMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVNEHTVHGVDKAGKVTQLSAKHIVIATGGRPKYPTq 199
Cdd:PLN02507 105 NEKVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRYTAKHILIATGSRAQRPN- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 200 VKGAlEHGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVMMR-SVPLRGFDQQMASLVTEHMESHGTRFL 278
Cdd:PLN02507 184 IPGK-ELAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRkELPLRGFDDEMRAVVARNLEGRGINLH 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 279 KGCVPSLIRKLpTNQLQVTWEDlasGKEDVGtfDTVLWAIGRVPETRNLNLEKAGVNTNpKNQKIIVDAQEATSVPHIYA 358
Cdd:PLN02507 263 PRTNLTQLTKT-EGGIKVITDH---GEEFVA--DVVLFATGRAPNTKRLNLEAVGVELD-KAGAVKVDEYSRTNIPSIWA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 359 IGDVAEgRPELTPTAIKAGKLLAQRLFGKSSTLMNYSNVPTTVFTPLEYGCVGLSEEEAVAlHGQEHIEVYHAYYKPLEF 438
Cdd:PLN02507 336 IGDVTN-RINLTPVALMEGTCFAKTVFGGQPTKPDYENVACAVFCIPPLSVVGLSEEEAVE-QAKGDILVFTSSFNPMKN 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55250718 439 TVADRDaSQCYIKMVCMREPPQlVLGLHFLGPNAGEVTQGFALGIQCGASYAQVMQTVGIHPTCSEEVVKLHISKR 514
Cdd:PLN02507 414 TISGRQ-EKTVMKLIVDAETDK-VLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEFVTMRSVTR 487
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
42-510 |
3.12e-95 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 300.38 E-value: 3.12e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 42 FDLLVIGGGSGGLACAKEAAQLGRKVAVADyvepsprgtKWGLGGTCVNVGCIPKKLMHQAALLGGMIRDAQHYGWEVAQ 121
Cdd:PTZ00058 49 YDLIVIGGGSGGMAAARRAARNKAKVALVE---------KDYLGGTCVNVGCVPKKIMFNAASIHDILENSRHYGFDTQF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 122 PVqhNWKAMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVNEHTVHGV--------------DKAGKVTQ------- 180
Cdd:PTZ00058 120 SF--NLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLIKkvsqvdgeadesddDEVTIVSAgvsqldd 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 181 ---LSAKHIVIATGGRPKYPtQVKGaLEHGITSDDIFWLKEsPGKTLVVGASYVALECAGFLTGIGLDTTVMMR-SVPLR 256
Cdd:PTZ00058 198 gqvIEGKNILIAVGNKPIFP-DVKG-KEFTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARgNRLLR 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 257 GFDQQMASLVTEHMESHGTRFLKGCVPSLIRKLPTNQLQVTWEDlaSGKEDvgTFDTVLWAIGRVPETRNLNLEkaGVNT 336
Cdd:PTZ00058 275 KFDETIINELENDMKKNNINIITHANVEEIEKVKEKNLTIYLSD--GRKYE--HFDYVIYCVGRSPNTEDLNLK--ALNI 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 337 NPKNQKIIVDAQEATSVPHIYAIGDVAEGRP---------------------------------ELTPTAIKAGKLLAQR 383
Cdd:PTZ00058 349 KTPKGYIKVDDNQRTSVKHIYAVGDCCMVKKnqeiedlnllklyneepylkkkentsgesyynvQLTPVAINAGRLLADR 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 384 LFGKSSTLMNYSNVPTTVFTPLEYGCVGLSEEEAVALHGQEHIEVYHAYYKPLEFTVADRDASQ---CYIKMVCMrEPPQ 460
Cdd:PTZ00058 429 LFGPFSRTTNYKLIPSVIFSHPPIGTIGLSEQEAIDIYGKENVKIYESRFTNLFFSVYDMDPAQkekTYLKLVCV-GKEE 507
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 55250718 461 LVLGLHFLGPNAGEVTQGFALGIQCGASYAQVMQTVGIHPTCSEEVVKLH 510
Cdd:PTZ00058 508 LIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIHPTAAEEFVTMA 557
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
41-514 |
5.83e-89 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 283.69 E-value: 5.83e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 41 NFDLLVIGGGSGGLACAKEAAQLGRKVAVADY-VEPSPRGTKWGLGGTCVNVGCIPKKLMHQAALLGGMIRDAQHYGWEV 119
Cdd:PLN02546 79 DFDLFTIGAGSGGVRASRFASNFGASAAVCELpFATISSDTLGGVGGTCVLRGCVPKKLLVYASKYSHEFEESRGFGWKY 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 120 AQPVQHNWKAMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVNEHTVhGVDkaGKVtqLSAKHIVIATGGRPKYPtQ 199
Cdd:PLN02546 159 ETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTV-DVD--GKL--YTARNILIAVGGRPFIP-D 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 200 VKGaLEHGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVMMRSVP-LRGFDQQMASLVTEHMESHGTRFL 278
Cdd:PLN02546 233 IPG-IEHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKKvLRGFDEEVRDFVAEQMSLRGIEFH 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 279 KGCVPSLIRKLPTNQLQvtwedLASGKEDVGTFDTVLWAIGRVPETRNLNLEKAGVNTNpKNQKIIVDAQEATSVPHIYA 358
Cdd:PLN02546 312 TEESPQAIIKSADGSLS-----LKTNKGTVEGFSHVMFATGRKPNTKNLGLEEVGVKMD-KNGAIEVDEYSRTSVPSIWA 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 359 IGDVAEgRPELTPTAIKAGKLLAQRLFGKSSTLMNYSNVPTTVFTPLEYGCVGLSEEEAVALHGQehIEVYHAYYKPLEF 438
Cdd:PLN02546 386 VGDVTD-RINLTPVALMEGGALAKTLFGNEPTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYGD--VDVFTANFRPLKA 462
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55250718 439 TVADRDASQCYIKMVCMREppQLVLGLHFLGPNAGEVTQGFALGIQCGASYAQVMQTVGIHPTCSEEVVKLHISKR 514
Cdd:PLN02546 463 TLSGLPDRVFMKLIVCAKT--NKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEEFVTMRTPTR 536
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
42-509 |
3.02e-84 |
|
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: 269.53 E-value: 3.02e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 42 FDLLVIGGGSGGLACAKEAAQL-GRKVAVADYVEPSPRGTKWGLGGTCVNVGCIPKKLMHQAALLGGMIRDAQHYGWEV- 119
Cdd:TIGR01423 4 FDLVVIGAGSGGLEAGWNAATLyKKRVAVVDVQTHHGPPFYAALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGWEFd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 120 AQPVQHNWKAMAEAVQNHVKSLNWGHRVQLQDRK-VKYFNIKASFVNEHTV---HGVDKAGKVTQ-LSAKHIVIATGGRP 194
Cdd:TIGR01423 84 RSSVKANWKALIAAKNKAVLDINKSYEGMFADTEgLTFFLGWGALEDKNVVlvrESADPKSAVKErLQAEHILLATGSWP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 195 KYPtQVKGaLEHGITSDDIFWLKESPGKTLVVGASYVALECAGFLTG---IGLDTTVMMRSVP-LRGFDQQMASLVTEHM 270
Cdd:TIGR01423 164 QML-GIPG-IEHCISSNEAFYLDEPPRRVLTVGGGFISVEFAGIFNAykpRGGKVTLCYRNNMiLRGFDSTLRKELTKQL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 271 ESHGTRFLKGCVPSLIRKLPTNQLQVTWEdlaSGKE-DVgtfDTVLWAIGRVPETRNLNLEKAGVNTNPKNqKIIVDAQE 349
Cdd:TIGR01423 242 RANGINIMTNENPAKVTLNADGSKHVTFE---SGKTlDV---DVVMMAIGRVPRTQTLQLDKVGVELTKKG-AIQVDEFS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 350 ATSVPHIYAIGDVAeGRPELTPTAIKAGKLLAQRLFGKSSTLMNYSNVPTTVFTPLEYGCVGLSEEEAVALHgqEHIEVY 429
Cdd:TIGR01423 315 RTNVPNIYAIGDVT-DRVMLTPVAINEGAAFVDTVFGNKPRKTDHTRVASAVFSIPPIGTCGLVEEDAAKKF--EKVAVY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 430 HAYYKPLEFTVADRDASQCYIKMVCMREPPQlVLGLHFLGPNAGEVTQGFALGIQCGASYAQVMQTVGIHPTCSEEVVKL 509
Cdd:TIGR01423 392 ESSFTPLMHNISGSKYKKFVAKIVTNHADGT-VLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAEELCSM 470
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
41-504 |
5.11e-82 |
|
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: 262.58 E-value: 5.11e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 41 NFDLLVIGGGSGGLACAKEAAQLGRKVAVadyVEpsprgtKWGLGGTCVNVGCIPKK-LMHQAALLGgMIRDAQHYGWEV 119
Cdd:TIGR01350 1 AYDVIVIGGGPGGYVAAIRAAQLGLKVAL---VE------KEYLGGTCLNVGCIPTKaLLHSAEVYD-EIKHAKDLGIEV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 120 AQpVQHNWKAMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVNEHTVhGVDKAGKVTQLSAKHIVIATGGRPKY-PT 198
Cdd:TIGR01350 71 EN-VSVDWEKMQKRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTV-SVTGENGEETLEAKNIIIATGSRPRSlPG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 199 QVKGALEHGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTV--MMRSVpLRGFDQQMASLVTEHMESHGTR 276
Cdd:TIGR01350 149 PFDFDGKVVITSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVieMLDRI-LPGEDAEVSKVLQKALKKKGVK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 277 FLKGCVPSLIRKlptNQLQVTWEDLASGKEDVgTFDTVLWAIGRVPETRNLNLEKAGVNTNPKNqKIIVDAQEATSVPHI 356
Cdd:TIGR01350 228 ILTNTKVTAVEK---NDDQVTYENKGGETETL-TGEKVLVAVGRKPNTEGLGLEKLGVELDERG-RIVVDEYMRTNVPGI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 357 YAIGDVAEGrPELTPTAIKAGKLLAQRLFGKSSTLMNYSNVPTTVFTPLEYGCVGLSEEEAvalhGQEHIEvyhayYKPL 436
Cdd:TIGR01350 303 YAIGDVIGG-PMLAHVASHEGIVAAENIAGKEPAHIDYDAVPSVIYTDPEVASVGLTEEQA----KEAGYD-----VKIG 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55250718 437 EFTVADR------DASQCYIKMVcMREPPQLVLGLHFLGPNAGEVTQGFALGIQCGASYAQVMQTVGIHPTCSE 504
Cdd:TIGR01350 373 KFPFAANgkalalGETDGFVKII-ADKKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSE 445
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
40-504 |
1.21e-79 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 256.61 E-value: 1.21e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 40 QNFDLLVIGGGSGGLACAKEAAQLGRKVAVadyVEpsprgtKWGLGGTCVNVGCIPKKlmhqaALL--GGMIRDAQH--- 114
Cdd:PRK06416 3 FEYDVIVIGAGPGGYVAAIRAAQLGLKVAI---VE------KEKLGGTCLNRGCIPSK-----ALLhaAERADEARHsed 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 115 YGWEvAQPVQHNWKAMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVNEHTVhGVDKAGKVTQLSAKHIVIATGGRP 194
Cdd:PRK06416 69 FGIK-AENVGIDFKKVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTV-RVMTEDGEQTYTAKNIILATGSRP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 195 KYPtqvKGaLEHG----ITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTV---MMRSVPlrGFDQQMASLVT 267
Cdd:PRK06416 147 REL---PG-IEIDgrviWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIveaLPRILP--GEDKEISKLAE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 268 EHMESHGTRFLKGcvpSLIRKLPTNQLQVTWEDLASGKEDVGTFDTVLWAIGRVPETRNLNLEKAGVNTNpkNQKIIVDA 347
Cdd:PRK06416 221 RALKKRGIKIKTG---AKAKKVEQTDDGVTVTLEDGGKEETLEADYVLVAVGRRPNTENLGLEELGVKTD--RGFIEVDE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 348 QEATSVPHIYAIGDVAEGrPELTPTAIKAGKLLAQRLFGKSSTlMNYSNVPTTVFTPLEYGCVGLSEEEAVALHGQehIE 427
Cdd:PRK06416 296 QLRTNVPNIYAIGDIVGG-PMLAHKASAEGIIAAEAIAGNPHP-IDYRGIPAVTYTHPEVASVGLTEAKAKEEGFD--VK 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 428 VYHAYYK------PLeftvadrDASQCYIKMVcMREPPQLVLGLHFLGPNAGEVTQGFALGIQCGASYAQVMQTVGIHPT 501
Cdd:PRK06416 372 VVKFPFAgngkalAL-------GETDGFVKLI-FDKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPT 443
|
...
gi 55250718 502 CSE 504
Cdd:PRK06416 444 LSE 446
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
40-508 |
3.14e-76 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 247.78 E-value: 3.14e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 40 QNFDLLVIGGGSGGLACAKEAAQLGRKVAVadyVEPSPrgtkwgLGGTCVNVGCIPKKLMHQAALLGGMIRDAQHYGWEV 119
Cdd:PRK06292 2 EKYDVIVIGAGPAGYVAARRAAKLGKKVAL---IEKGP------LGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 120 AQPVQhNWKAMAEAVQNHVKSLNWGH-RVQLQDRKVKYFNIKASFVNEHTVHgVDKagkvTQLSAKHIVIATGGR-PKYP 197
Cdd:PRK06292 73 DGPKI-DFKKVMARVRRERDRFVGGVvEGLEKKPKIDKIKGTARFVDPNTVE-VNG----ERIEAKNIVIATGSRvPPIP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 198 tQVKGALEHGI-TSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVM-MRSVPLRGFDQQMASLVTEHMESHgT 275
Cdd:PRK06292 147 -GVWLILGDRLlTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFeRGDRILPLEDPEVSKQAQKILSKE-F 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 276 RFLKGcvpSLIRKLPTNQLQVTWEDLASGKEDVGTFDTVLWAIGRVPETRNLNLEKAGVNTNPKNQkIIVDAQEATSVPH 355
Cdd:PRK06292 225 KIKLG---AKVTSVEKSGDEKVEELEKGGKTETIEADYVLVATGRRPNTDGLGLENTGIELDERGR-PVVDEHTQTSVPG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 356 IYAIGDVAeGRPELTPTAIKAGKLLAQRLFGKSSTLMNYSNVPTTVFTPLEYGCVGLSEEEAVALhGQEHIEVY------ 429
Cdd:PRK06292 301 IYAAGDVN-GKPPLLHEAADEGRIAAENAAGDVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAA-GIDYVVGEvpfeaq 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 430 ---HAYYKPLEF--TVADRDAsqcyikmvcmreppQLVLGLHFLGPNAGEVTQGFALGIQCGASYAQVMQTVGIHPTcSE 504
Cdd:PRK06292 379 graRVMGKNDGFvkVYADKKT--------------GRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPT-LS 443
|
....
gi 55250718 505 EVVK 508
Cdd:PRK06292 444 EGLR 447
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
39-509 |
8.13e-72 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 236.25 E-value: 8.13e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 39 QQNFDLLVIGGGSGGLACAKEAAQLGRKVAVadyVEPSPrgtkwgLGGTCVNVGCIPKKLMHQAALLGGMIRDAQHYGWE 118
Cdd:PRK06370 3 AQRYDAIVIGAGQAGPPLAARAAGLGMKVAL---IERGL------LGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 119 VAQPVQHNWKA----MAEAVQN-HVKSLNWghrvqLQDRK-VKYFNIKASFVNEHTVHgVDkaGKVtqLSAKHIVIATGG 192
Cdd:PRK06370 74 VGGPVSVDFKAvmarKRRIRARsRHGSEQW-----LRGLEgVDVFRGHARFESPNTVR-VG--GET--LRAKRIFINTGA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 193 RPKYPtQVKGALEHG-ITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVMMRSvP--LRGFDQQMASLVTEH 269
Cdd:PRK06370 144 RAAIP-PIPGLDEVGyLTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERG-PrlLPREDEDVAAAVREI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 270 MESHGTRFLKGCVPSLIRKLPtNQLQVTWeDLASGKEDVgTFDTVLWAIGRVPETRNLNLEKAGVNTNPKNQkIIVDAQE 349
Cdd:PRK06370 222 LEREGIDVRLNAECIRVERDG-DGIAVGL-DCNGGAPEI-TGSHILVAVGRVPNTDDLGLEAAGVETDARGY-IKVDDQL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 350 ATSVPHIYAIGDVaEGRPELTPTAIKAGKLLAQRLFG----KSSTLmnysNVPTTVFTPLEYGCVGLSEEEAVALhGQEh 425
Cdd:PRK06370 298 RTTNPGIYAAGDC-NGRGAFTHTAYNDARIVAANLLDggrrKVSDR----IVPYATYTDPPLARVGMTEAEARKS-GRR- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 426 IEVYHayykpLEFTVADR----DASQCYIKMVCMREPPQlVLGLHFLGPNAGEVTQGFALGIQCGASYAQVMQTVGIHPT 501
Cdd:PRK06370 371 VLVGT-----RPMTRVGRavekGETQGFMKVVVDADTDR-ILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPT 444
|
....*...
gi 55250718 502 CSEEVVKL 509
Cdd:PRK06370 445 VSELIPTL 452
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
42-377 |
3.61e-65 |
|
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: 213.72 E-value: 3.61e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 42 FDLLVIGGGSGGLACAKEAAQLGRKVAVAdyvepsprgtkwGLGGTCVNVGCIPKKLMHQAAllgGMIRDAQHygwevaq 121
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLI------------EDEGTCPYGGCVLSKALLGAA---EAPEIASL------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 122 pvqhnWKAMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVNEHTVhgvdkAGKVTQLSAKHIVIATGGRPKYPTqVK 201
Cdd:pfam07992 59 -----WADLYKRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELV-----DGDGETITYDRLVIATGARPRLPP-IP 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 202 GALEHG------ITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVM-MRSVPLRGFDQQMASLVTEHMESHG 274
Cdd:pfam07992 128 GVELNVgflvrtLDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIeALDRLLRAFDEEISAALEKALEKNG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 275 TRFLKGCVPSLIRKLPTNQLQVTwedlasGKEDVGTFDTVLWAIGRVPETRNLnlEKAGVNTNPKNQkIIVDAQEATSVP 354
Cdd:pfam07992 208 VEVRLGTSVKEIIGDGDGVEVIL------KDGTEIDADLVVVAIGRRPNTELL--EAAGLELDERGG-IVVDEYLRTSVP 278
|
330 340
....*....|....*....|...
gi 55250718 355 HIYAIGDVAEGRPELTPTAIKAG 377
Cdd:pfam07992 279 GIYAAGDCRVGGPELAQNAVAQG 301
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
42-504 |
2.24e-59 |
|
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: 203.42 E-value: 2.24e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 42 FDLLVIGGGSGGLACAKEAAQLGRKVAVadyVEpspRGTkwgLGGTCVNVGCIPKKLMHQAALLGGMIRDAQhYGWEVAQ 121
Cdd:TIGR02053 1 YDLVIIGSGAAAFAAAIKAAELGASVAM---VE---RGP---LGGTCVNVGCVPSKMLLRAAEVAHYARKPP-FGGLAAT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 122 P-------VQHNWKAMAEAVQNHVKSLnwghrvqLQDRKVKYFNIKASFVNEHTVHgVDKAGKVtqLSAKHIVIATGGRP 194
Cdd:TIGR02053 71 VavdfgelLEGKREVVEELRHEKYEDV-------LSSYGVDYLRGRARFKDPKTVK-VDLGREV--RGAKRFLIATGARP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 195 KYPtQVKGALEHG-ITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVMMRSVP-LRGFDQQMASLVTEHMES 272
Cdd:TIGR02053 141 AIP-PIPGLKEAGyLTSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSDRlLPREEPEISAAVEEALAE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 273 HGTRFLKGcvpSLIRKLPTNQLQVTWEDLASGKEDVGTFDTVLWAIGRVPETRNLNLEKAGVNTNPKNQkIIVDAQEATS 352
Cdd:TIGR02053 220 EGIEVVTS---AQVKAVSVRGGGKIITVEKPGGQGEVEADELLVATGRRPNTDGLGLEKAGVKLDERGG-ILVDETLRTS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 353 VPHIYAIGDVAeGRPELTPTAIKAGKLLAQRLFGKSSTLMNYSNVPTTVFTPLEYGCVGLSEEEavALHGQEHIEVYHAY 432
Cdd:TIGR02053 296 NPGIYAAGDVT-GGLQLEYVAAKEGVVAAENALGGANAKLDLLVIPRVVFTDPAVASVGLTEAE--AQKAGIECDCRTLP 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55250718 433 YKPLEFTVADRDaSQCYIKMVCMREPPQlVLGLHFLGPNAGEVTQGFALGIQCGASYAQVMQTVGIHPTCSE 504
Cdd:TIGR02053 373 LTNVPRARINRD-TRGFIKLVAEPGTGK-VLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAE 442
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
39-474 |
7.69e-59 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 201.92 E-value: 7.69e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 39 QQNFDLLVIGGGSGGLACAKEAAQLGRKVAVadyVEPSPRgtkwgLGGTCVNVGCIPKKLMHQAAL-LGGMIRDAQHYGW 117
Cdd:PRK05249 3 MYDYDLVVIGSGPAGEGAAMQAAKLGKRVAV---IERYRN-----VGGGCTHTGTIPSKALREAVLrLIGFNQNPLYSSY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 118 EVAQPV------QHnwkamAEAVQNHVKSLnwgHRVQLQDRKVKYFNIKASFVNEHTVHGVDKAGKVTQLSAKHIVIATG 191
Cdd:PRK05249 75 RVKLRItfadllAR-----ADHVINKQVEV---RRGQYERNRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 192 GRPKYPTQVKGALEHGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVM-MRSVPLRGFDQQMASLVTEHM 270
Cdd:PRK05249 147 SRPYRPPDVDFDHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLInTRDRLLSFLDDEISDALSYHL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 271 ESHGTRFLKGCVPSLIRKLPtNQLQVTwedLASGKEDVGtfDTVLWAIGRVPETRNLNLEKAGVNTNPKNQkIIVDAQEA 350
Cdd:PRK05249 227 RDSGVTIRHNEEVEKVEGGD-DGVIVH---LKSGKKIKA--DCLLYANGRTGNTDGLNLENAGLEADSRGQ-LKVNENYQ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 351 TSVPHIYAIGDVAeGRPELTPTAIKAGKLLAQRLFGKSSTLMnYSNVPTTVFTPLEYGCVGLSEEEAVALHGqeHIEVYH 430
Cdd:PRK05249 300 TAVPHIYAVGDVI-GFPSLASASMDQGRIAAQHAVGEATAHL-IEDIPTGIYTIPEISSVGKTEQELTAAKV--PYEVGR 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 55250718 431 AYYKPLeftvA------DRDASqcyIKMVCMREPPQLvLGLHFLGPNAGE 474
Cdd:PRK05249 376 ARFKEL----AraqiagDNVGM---LKILFHRETLEI-LGVHCFGERATE 417
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
39-515 |
7.61e-50 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 178.20 E-value: 7.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 39 QQNFDLLVIGGGSGGLACAKEAAQLGRKVAVADyvEPSPRGTKWGLGGTCVNVGCIPKKlmhqaALLGG--MIRDAQH-- 114
Cdd:PRK06327 2 SKQFDVVVIGAGPGGYVAAIRAAQLGLKVACIE--AWKNPKGKPALGGTCLNVGCIPSK-----ALLASseEFENAGHhf 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 115 --YGWEVAQpVQHNWKAMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFV---NEHTVHGVDKAGKVTqLSAKHIVIA 189
Cdd:PRK06327 75 adHGIHVDG-VKIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVgktDAGYEIKVTGEDETV-ITAKHVIIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 190 TGGRPKYPTQVKGALEHGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVmMRSVP--LRGFDQQMASLVT 267
Cdd:PRK06327 153 TGSEPRHLPGVPFDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTI-LEALPafLAAADEQVAKEAA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 268 EHMESHGTRFLKGCVPSLIRKLpTNQLQVTWEDlASGKEDVGTFDTVLWAIGRVPETRNLNLEKAGVNTNPKNQkIIVDA 347
Cdd:PRK06327 232 KAFTKQGLDIHLGVKIGEIKTG-GKGVSVAYTD-ADGEAQTLEVDKLIVSIGRVPNTDGLGLEAVGLKLDERGF-IPVDD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 348 QEATSVPHIYAIGDVAEGrPELTPTAIKAGKLLAQRLFGKSSTlMNYSNVPTTVFTPLEYGCVGLSEEEAVAlhgqEHIE 427
Cdd:PRK06327 309 HCRTNVPNVYAIGDVVRG-PMLAHKAEEEGVAVAERIAGQKGH-IDYNTIPWVIYTSPEIAWVGKTEQQLKA----EGVE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 428 vyhayYKPLEF-------TVADRDASQcYIKMVCMREPPQlVLGLHFLGPNAGEVTQGFALGIQCGASYAQVMQTVGIHP 500
Cdd:PRK06327 383 -----YKAGKFpfmangrALAMGEPDG-FVKIIADAKTDE-ILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHP 455
|
490
....*....|....*...
gi 55250718 501 TCSeEVVK---LHISKRS 515
Cdd:PRK06327 456 TLS-EVWHeaaLAVDKRP 472
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
46-484 |
8.27e-44 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 163.40 E-value: 8.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 46 VIGGGSGGLACAKEAAQLGRKVAVADyvepspRGTkwgLGGTCVNVGCIPKKLMHQAALLGGMIRDAQHYGWEVAQPVQH 125
Cdd:PRK13748 103 VIGSGGAAMAAALKAVEQGARVTLIE------RGT---IGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDGGIAATVPTI 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 126 NWKAMAEAVQNHVKSLnwghrvqlqdRKVKYFNI------------KASFVNEHT--VHGVDkaGKVTQLSAKHIVIATG 191
Cdd:PRK13748 174 DRSRLLAQQQARVDEL----------RHAKYEGIldgnpaitvlhgEARFKDDQTliVRLND--GGERVVAFDRCLIATG 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 192 GRPKYPTqVKGALEHGI-TSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVMMRSVPLRGFDQQMASLVTEHM 270
Cdd:PRK13748 242 ASPAVPP-IPGLKETPYwTSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILARSTLFFREDPAIGEAVTAAF 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 271 ESHGTRFLKGcvpslirklpTNQLQVTWED----LASGKEDVGTfDTVLWAIGRVPETRNLNLEKAGVNTNPKNQkIIVD 346
Cdd:PRK13748 321 RAEGIEVLEH----------TQASQVAHVDgefvLTTGHGELRA-DKLLVATGRAPNTRSLALDAAGVTVNAQGA-IVID 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 347 AQEATSVPHIYAIGDVAEgRPELTPTAIKAGKLLAQRLFGKSSTLmNYSNVPTTVFTPLEYGCVGLSEEEAvalHgQEHI 426
Cdd:PRK13748 389 QGMRTSVPHIYAAGDCTD-QPQFVYVAAAAGTRAAINMTGGDAAL-DLTAMPAVVFTDPQVATVGYSEAEA---H-HDGI 462
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55250718 427 E----------VYHAyykpleftVADRDaSQCYIKMVcMREPPQLVLGLHFLGPNAGEVTQGFALGIQ 484
Cdd:PRK13748 463 EtdsrtltldnVPRA--------LANFD-TRGFIKLV-IEEGSGRLIGVQAVAPEAGELIQTAALAIR 520
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
42-506 |
5.56e-42 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 155.88 E-value: 5.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 42 FDLLVIGGGSGGLACAKEAAqlGRKVAVADyvepspRGTkwgLGGTCVNVGCIPKKLMHQAALLGGMIRDAQHYGwevaq 121
Cdd:PRK07846 2 YDLIIIGTGSGNSILDERFA--DKRIAIVE------KGT---FGGTCLNVGCIPTKMFVYAADVARTIREAARLG----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 122 pvqhnwkamaeaVQNHVKSLNWGhrvQLQDR---------------------KVKYFNIKASFVNEHTVHgvdkAGKVTQ 180
Cdd:PRK07846 66 ------------VDAELDGVRWP---DIVSRvfgridpiaaggeeyrgrdtpNIDVYRGHARFIGPKTLR----TGDGEE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 181 LSAKHIVIATGGRPKYPTQVKGALEHGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVMMRS-VPLRGFD 259
Cdd:PRK07846 127 ITADQVVIAAGSRPVIPPVIADSGVRYHTSDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSgRLLRHLD 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 260 QQMASLVTEHMESHGTRFLkGCVPSLIRKLPtNQLQVTwedLASGkeDVGTFDTVLWAIGRVPETRNLNLEKAGVNTNpK 339
Cdd:PRK07846 207 DDISERFTELASKRWDVRL-GRNVVGVSQDG-SGVTLR---LDDG--STVEADVLLVATGRVPNGDLLDAAAAGVDVD-E 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 340 NQKIIVDAQEATSVPHIYAIGDVAEgrP-ELTPTAIKAGKLLAQRLFGKSSTL-MNYSNVPTTVFTPLEYGCVGLSEEEA 417
Cdd:PRK07846 279 DGRVVVDEYQRTSAEGVFALGDVSS--PyQLKHVANHEARVVQHNLLHPDDLIaSDHRFVPAAVFTHPQIASVGLTENEA 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 418 VALhgQEHIEVYHAYYKPLEFTVADRDASQCyIKMVCMREPPQLvLGLHFLGPNAGEVTQGFalgIQcGASYAQVMQTVG 497
Cdd:PRK07846 357 RAA--GLDITVKVQNYGDVAYGWAMEDTTGF-VKLIADRDTGRL-LGAHIIGPQASTLIQPL---IQ-AMSFGLDAREMA 428
|
490
....*....|....
gi 55250718 498 -----IHPTCSEEV 506
Cdd:PRK07846 429 rgqywIHPALPEVV 442
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
40-504 |
8.15e-42 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 155.29 E-value: 8.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 40 QNFDLLVIGGGSGGLACAKEAAQLGRKVAVadyVEPSPRGtkwgLGGTCVNVGCIPKKLMHQAAllggmirdaqHYGWEV 119
Cdd:PRK07251 2 LTYDLIVIGFGKAGKTLAAKLASAGKKVAL---VEESKAM----YGGTCINIGCIPTKTLLVAA----------EKNLSF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 120 AQpvqhnwkAMAEavQNHVKS-LNWGHRVQLQDRKVKYFNIKASFVNEHTVH---GVDKagkvTQLSAKHIVIATGGRP- 194
Cdd:PRK07251 65 EQ-------VMAT--KNTVTSrLRGKNYAMLAGSGVDLYDAEAHFVSNKVIEvqaGDEK----IELTAETIVINTGAVSn 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 195 KYPTQVKGALEHGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVM-MRSVPLRGFDQQMASLVTEHMESH 273
Cdd:PRK07251 132 VLPIPGLADSKHVYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLdAASTILPREEPSVAALAKQYMEED 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 274 GTRFLKGCVPSLIrKLPTNQLQVTWEDlasGKEdvgTFDTVLWAIGRVPETRNLNLEKAGVNTNpKNQKIIVDAQEATSV 353
Cdd:PRK07251 212 GITFLLNAHTTEV-KNDGDQVLVVTED---ETY---RFDALLYATGRKPNTEPLGLENTDIELT-ERGAIKVDDYCQTSV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 354 PHIYAIGDVaEGRPELTPTAIKAGKLLAQRLFGKSS-TLMNYSNVPTTVFTPLEYGCVGLSEEEAVALHGQehievyhay 432
Cdd:PRK07251 284 PGVFAVGDV-NGGPQFTYISLDDFRIVFGYLTGDGSyTLEDRGNVPTTMFITPPLSQVGLTEKEAKEAGLP--------- 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55250718 433 YKPLEFTVAD--RDASQCYIK---MVCMREPPQLVLGLHFLGPNAGEVTQGFALGIQCGASYAQVMQTVGIHPTCSE 504
Cdd:PRK07251 354 YAVKELLVAAmpRAHVNNDLRgafKVVVNTETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAE 430
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
42-506 |
5.19e-38 |
|
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: 144.90 E-value: 5.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 42 FDLLVIGGGSGGLACAKEAAqlGRKVAVADyvepspRGTkwgLGGTCVNVGCIPKKLMHQAALLGGMIRDAQHYGweVAQ 121
Cdd:TIGR03452 3 YDLIIIGTGSGNSIPDPRFA--DKRIAIVE------KGT---FGGTCLNVGCIPTKMFVYAAEVAQSIGESARLG--IDA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 122 PVQH-NWKAMAEAVqnhvkslnWGHRVQL------------QDRKVKYFNIKASFVNEHTVhgvdKAGKVTQLSAKHIVI 188
Cdd:TIGR03452 70 EIDSvRWPDIVSRV--------FGDRIDPiaaggedyrrgdETPNIDVYDGHARFVGPRTL----RTGDGEEITGDQIVI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 189 ATGGRPKYPTQVkgaLEHGI---TSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVMMRS-VPLRGFDQQMAS 264
Cdd:TIGR03452 138 AAGSRPYIPPAI---ADSGVryhTNEDIMRLPELPESLVIVGGGYIAAEFAHVFSALGTRVTIVNRStKLLRHLDEDISD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 265 LVTEHMESHGTRFLKGCVPSLIRKlpTNQLQVTWEDlasgkEDVGTFDTVLWAIGRVPETRNLNLEKAGVNTNpKNQKII 344
Cdd:TIGR03452 215 RFTEIAKKKWDIRLGRNVTAVEQD--GDGVTLTLDD-----GSTVTADVLLVATGRVPNGDLLDAEAAGVEVD-EDGRIK 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 345 VDAQEATSVPHIYAIGDVAEgrP-ELTPTAIKAGKLLAQRLFGKSSTL-MNYSNVPTTVFTPLEYGCVGLSEEEAVAlHG 422
Cdd:TIGR03452 287 VDEYGRTSARGVWALGDVSS--PyQLKHVANAEARVVKHNLLHPNDLRkMPHDFVPSAVFTHPQIATVGLTEQEARE-AG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 423 QEhIEVYHAYYKPLEFTVADRDaSQCYIKMVCMREPPQLvLGLHFLGPNAGEVTQGFALGIQCGASYAQVMQ-TVGIHPT 501
Cdd:TIGR03452 364 HD-ITVKIQNYGDVAYGWAMED-TTGFCKLIADRDTGKL-LGAHIIGPQASSLIQPLITAMAFGLDAREMARkQYWIHPA 440
|
....*
gi 55250718 502 CSEEV 506
Cdd:TIGR03452 441 LPEVV 445
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
397-509 |
3.96e-35 |
|
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: 127.28 E-value: 3.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 397 VPTTVFTPLEYGCVGLSEEEAVALHGQehIEVYHAYYKPLEFTVADRDASqCYIKMVCMREPpQLVLGLHFLGPNAGEVT 476
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGE--VKVGKFPFAANGRALAYGDTD-GFVKLVADRET-GKILGAHIVGPNAGELI 76
|
90 100 110
....*....|....*....|....*....|...
gi 55250718 477 QGFALGIQCGASYAQVMQTVGIHPTCSEEVVKL 509
Cdd:pfam02852 77 QEAALAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
42-504 |
4.29e-33 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 133.50 E-value: 4.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 42 FDLLVIGGGSGGLACAKEAAQLGRKVAVADYVEPSprgtkwgLGGTCVNVGCIPKKLMHQAALLGGMIRDAQH---YG-- 116
Cdd:PTZ00153 117 YDVGIIGCGVGGHAAAINAMERGLKVIIFTGDDDS-------IGGTCVNVGCIPSKALLYATGKYRELKNLAKlytYGiy 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 117 ---------------WEVAQPVQHNWKAMAEAVQNHVKSLNWG-------HRVQLQDRKVKYFNIKASFVNEHTVHGvDK 174
Cdd:PTZ00153 190 tnafkngkndpvernQLVADTVQIDITKLKEYTQSVIDKLRGGienglksKKFCKNSEHVQVIYERGHIVDKNTIKS-EK 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 175 AGKVTQLsaKHIVIATGGRPKYPTQVKGALEHGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDtTVMMRSVP 254
Cdd:PTZ00153 269 SGKEFKV--KNIIIATGSTPNIPDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSE-VVSFEYSP 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 255 --LRGFDQQMASLVTE-HMESHGTRFLKGCVPSLIRKLPTNQ-LQVTWEDLASGKEDVGTF----------DTVLWAIGR 320
Cdd:PTZ00153 346 qlLPLLDADVAKYFERvFLKSKPVRVHLNTLIEYVRAGKGNQpVIIGHSERQTGESDGPKKnmndiketyvDSCLVATGR 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 321 VPETRNLNLEKAGVNTN----PKNQKIIVDAQEATSVPHIYAIGDvAEGRPELTPTAI------------KAGKLLAQRL 384
Cdd:PTZ00153 426 KPNTNNLGLDKLKIQMKrgfvSVDEHLRVLREDQEVYDNIFCIGD-ANGKQMLAHTAShqalkvvdwiegKGKENVNINV 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 385 FGKSSTLMNYSNVPTTVFTPLEYGCVGLSEEEAVALHGQEHIEVYHAYYKP-------LEFTVADRDASQCYIKM----- 452
Cdd:PTZ00153 505 ENWASKPIIYKNIPSVCYTTPELAFIGLTEKEAKELYPPDNVGVEISFYKAnskvlceNNISFPNNSKNNSYNKGkyntv 584
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 453 --------VCMREPPQLVLGLHFLGPNAGEVTQGFALGIQCGASYAQVMQTVGIHPTCSE 504
Cdd:PTZ00153 585 dntegmvkIVYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISE 644
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
40-504 |
3.85e-32 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 128.36 E-value: 3.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 40 QNFDLLVIGGGSGGLACAKEAAQLGRKVAVadyVEPSPRGtkwgLGGTCVNVGCIP-KKLMHQAALLGGMIRDAQHYGWE 118
Cdd:NF040477 2 NHYQAIIIGFGKAGKTLAATLAKAGWRVAI---IEQSAQM----YGGTCINIGCIPtKTLVHDAEQHQDFSTAMQRKSSV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 119 VAQPVQHNWKAMAEAVQnhvkslnwghrvqlqdrkVKYFNIKASFVNEHTVHgVDKAGKVTQLSAKHIVIATGGRPKYPT 198
Cdd:NF040477 75 VGFLRDKNYHNLADLDN------------------VDVINGRAEFIDNHTLR-VFQADGEQELRGEKIFINTGAQSVLPP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 199 QVKGALEHGI-TSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVMMRS-VPLRGFDQQMASLVTEHMESHGTR 276
Cdd:NF040477 136 IPGLTTTPGVyDSTGLLNLTQLPARLGILGGGYIGVEFASMFARFGSKVTIFEAAeLFLPREDRDIAQAIATILQDQGVE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 277 F-LKGCVPSLIRKLPTNQLQVtwedlasgKEDVGTFDTVLWAIGRVPETRNLNLEKAGVNTNPKNqKIIVDAQEATSVPH 355
Cdd:NF040477 216 LiLNAQVQRVSSHEGEVQLET--------AEGVLTVDALLVASGRKPATAGLQLQNAGVAVNERG-AIVVDKYLRTTADN 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 356 IYAIGDVAEGrPELTPTAIKAGKLLAQRLF--GKSSTlMNYSNVPTTVFTPLEYGCVGLSEEEAVALHGQEHIEVYHAYY 433
Cdd:NF040477 287 IWAMGDVTGG-LQFTYISLDDFRIVRDSLLgeGKRST-DDRQNVPYSVFMTPPLSRIGMTEEQARASGADIQVVTLPVAA 364
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55250718 434 KPLEFTVADrdaSQCYIKMVcMREPPQLVLGLHFLGPNAGEVTQGFALGIQCGASYAQVMQTVGIHPTCSE 504
Cdd:NF040477 365 IPRARVMND---TRGVLKAV-VDNKTQRILGVSLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSE 431
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
157-411 |
2.33e-30 |
|
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: 120.69 E-value: 2.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 157 FNIKasFVNEHTVHGVDKAGKV------TQLSAKHIVIATGGRPKYPtQVKGALEHGITS----DDIFWLKE-----SPG 221
Cdd:COG0446 49 KGID--VRTGTEVTAIDPEAKTvtlrdgETLSYDKLVLATGARPRPP-PIPGLDLPGVFTlrtlDDADALREalkefKGK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 222 KTLVVGASYVALECAGFLTGIGLDTTVM-MRSVPLRGFDQQMASLVTEHMESHGTRFLKGCvpSLIRKLPTNQLQVTWED 300
Cdd:COG0446 126 RAVVIGGGPIGLELAEALRKRGLKVTLVeRAPRLLGVLDPEMAALLEEELREHGVELRLGE--TVVAIDGDDKVAVTLTD 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 301 lasgKEDVgTFDTVLWAIGRVPETRnLnLEKAGVNTNPKNQkIIVDAQEATSVPHIYAIGDVAE------GRPELTP--- 371
Cdd:COG0446 204 ----GEEI-PADLVVVAPGVRPNTE-L-AKDAGLALGERGW-IKVDETLQTSDPDVYAAGDCAEvphpvtGKTVYIPlas 275
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 55250718 372 TAIKAGKLLAQRLFGKSSTLMNYSNVPTTVFtPLEYGCVG 411
Cdd:COG0446 276 AANKQGRVAAENILGGPAPFPGLGTFISKVF-DLCIASTG 314
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
42-509 |
1.51e-27 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 115.11 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 42 FDLLVIGGGSGGLACAKEAAQLGRKVAVadyVEPSPRGtkwgLGGTCVNVGCIPKKLmhqaallggMIRDAQHYGwEVAQ 121
Cdd:PRK08010 4 YQAVIIGFGKAGKTLAVTLAKAGWRVAL---IEQSNAM----YGGTCINIGCIPTKT---------LVHDAQQHT-DFVR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 122 PVQHNwkamaEAVQNHVKSLNWGHRVQLQDrkVKYFNIKASFVNEHTVHgVDKAGKVTQLSAKHIVIATGGRPKYP---- 197
Cdd:PRK08010 67 AIQRK-----NEVVNFLRNKNFHNLADMPN--IDVIDGQAEFINNHSLR-VHRPEGNLEIHGEKIFINTGAQTVVPpipg 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 198 -TQVKGALEhgitSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVM-MRSVPLRGFDQQMASLVTEHMESHGT 275
Cdd:PRK08010 139 iTTTPGVYD----STGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILeAASLFLPREDRDIADNIATILRDQGV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 276 RF-LKGCVPSLIRKlpTNQLQVTWEDLASgkedvgTFDTVLWAIGRVPETRNLNLEKAGVNTNPKNqKIIVDAQEATSVP 354
Cdd:PRK08010 215 DIiLNAHVERISHH--ENQVQVHSEHAQL------AVDALLIASGRQPATASLHPENAGIAVNERG-AIVVDKYLHTTAD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 355 HIYAIGDVAEGRpELTPTAIKAGKLLAQRLF--GKSSTlMNYSNVPTTVFTPLEYGCVGLSEEEAVALHGQEHIEVYHAY 432
Cdd:PRK08010 286 NIWAMGDVTGGL-QFTYISLDDYRIVRDELLgeGKRST-DDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVA 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55250718 433 YKPLEFTVADrdaSQCYIKMVcMREPPQLVLGLHFLGPNAGEVTQGFALGIQCGASYAQVMQTVGIHPTCSEEVVKL 509
Cdd:PRK08010 364 AIPRARVMND---TRGVLKAI-VDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLNDL 436
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
167-398 |
8.27e-25 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 106.38 E-value: 8.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 167 HTVHGVDKAGKV------TQLSAKHIVIATGGRPKYPtQVKGALEHGITS----DDIFWLKE--SPGKTLVV-GASYVAL 233
Cdd:COG1251 77 TRVTAIDRAARTvtladgETLPYDKLVLATGSRPRVP-PIPGADLPGVFTlrtlDDADALRAalAPGKRVVViGGGLIGL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 234 ECAGFLTGIGLDTTV-MMRSVPL-RGFDQQMASLVTEHMESHGTRFLKGCVPSLIRKlPTNQLQVTwedLASGKE-DVgt 310
Cdd:COG1251 156 EAAAALRKRGLEVTVvERAPRLLpRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEG-DDRVTGVR---LADGEElPA-- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 311 fDTVLWAIGRVPETRnLnLEKAGVNTNpknQKIIVDAQEATSVPHIYAIGDVAE------GRP--ELTPTAIKAGKLLAQ 382
Cdd:COG1251 230 -DLVVVAIGVRPNTE-L-ARAAGLAVD---RGIVVDDYLRTSDPDIYAAGDCAEhpgpvyGRRvlELVAPAYEQARVAAA 303
|
250 260
....*....|....*....|.
gi 55250718 383 RLFGKS-----STLMNYSNVP 398
Cdd:COG1251 304 NLAGGPaayegSVPSTKLKVF 324
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
42-373 |
9.64e-22 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 95.57 E-value: 9.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 42 FDLLVIGGGSGGLACAKEAAQLGRKVAVADYVEPSPRGTKWglggTCV-NVGCIPKKLMhQAALLGGMIRDAQHYGweva 120
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQLATT----KEIeNYPGFPEGIS-GPELAERLREQAERFG---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 121 qpvqhnwkamAEAVQNHVKSLnwghrvqlqDRKVKYFNIKASfvnehtvhgvdkagKVTQLSAKHIVIATGGRPKYPtQV 200
Cdd:COG0492 72 ----------AEILLEEVTSV---------DKDDGPFRVTTD--------------DGTEYEAKAVIIATGAGPRKL-GL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 201 KGALE---HGI----TSDDIFWlkesPGKT-LVVGASYVALECAGFLTGIGLDTTVMMRSVPLRGfdqqMASLVTEHMES 272
Cdd:COG0492 118 PGEEEfegRGVsycaTCDGFFF----RGKDvVVVGGGDSALEEALYLTKFASKVTLIHRRDELRA----SKILVERLRAN 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 273 HGTRFLKGCVPSLIRKlpTNQLQ-VTWEDLASGKEDVGTFDTVLWAIGRVPETRNLnlEKAGVNTNPKNQkIIVDAQEAT 351
Cdd:COG0492 190 PKIEVLWNTEVTEIEG--DGRVEgVTLKNVKTGEEKELEVDGVFVAIGLKPNTELL--KGLGLELDEDGY-IVVDEDMET 264
|
330 340
....*....|....*....|..
gi 55250718 352 SVPHIYAIGDVAEGRPELTPTA 373
Cdd:COG0492 265 SVPGVFAAGDVRDYKYRQAATA 286
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
46-503 |
2.52e-20 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 93.77 E-value: 2.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 46 VIGGGSGGLACAKEAAQLGRKVAVadyVEPSprgtkwGLGGTCVNVGCIPKKLMHQAALLGGMIRDAQHYGWEVAQPVQH 125
Cdd:PRK07845 6 IIGGGPGGYEAALVAAQLGADVTV---IERD------GLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRFIDDGEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 126 nwKAMAEAVQNHVKSLNWGH----RVQLQDRKVKYFNIKASFVNE----HTVHGVDKAGKVTQLSAKHIVIATGGRPKyp 197
Cdd:PRK07845 77 --RVDLPAVNARVKALAAAQsadiRARLEREGVRVIAGRGRLIDPglgpHRVKVTTADGGEETLDADVVLIATGASPR-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 198 tQVKGALEHG---ITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTT-VMMRSVPLRGFDQQMASLVTEHMESH 273
Cdd:PRK07845 153 -ILPTAEPDGeriLTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTlVSSRDRVLPGEDADAAEVLEEVFARR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 274 GTRFLKGC-VPSLIRKlpTNQLQVTwedLASGKEDVGTFdtVLWAIGRVPETRNLNLEKAGVNTNPKNQkIIVDAQEATS 352
Cdd:PRK07845 232 GMTVLKRSrAESVERT--GDGVVVT---LTDGRTVEGSH--ALMAVGSVPNTAGLGLEEAGVELTPSGH-ITVDRVSRTS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 353 VPHIYAIGDVAEGRPeLTPTAIKAGKLLAQRLFGKSSTLMNYSNVPTTVFTPLEYGCVGLSEEEAVAlhGQEHIEVY--- 429
Cdd:PRK07845 304 VPGIYAAGDCTGVLP-LASVAAMQGRIAMYHALGEAVSPLRLKTVASNVFTRPEIATVGVSQAAIDS--GEVPARTVmlp 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55250718 430 ---HAYYKPLEFtvadRDAsqcYIKMVCmREPPQLVLGLHFLGPNAGEVTQGFALGIQCGASYAQVMQTVGIHPTCS 503
Cdd:PRK07845 381 latNPRAKMSGL----RDG---FVKLFC-RPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYPSLS 449
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
222-288 |
1.58e-15 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 71.47 E-value: 1.58e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55250718 222 KTLVVGASYVALECAGFLTGIGLDTTVM-MRSVPLRGFDQQMASLVTEHMESHGTRFLKGCVPSLIRK 288
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVeRRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEG 68
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
166-420 |
9.98e-15 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 76.23 E-value: 9.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 166 EHTVHGVDKAGKvtQLSAKHI-------------VIATGGRPKYPTQVKGALEH--GITS-DDIFWLKESPGKT-----L 224
Cdd:PRK09564 76 EHEVVKVDAKNK--TITVKNLktgsifndtydklMIATGARPIIPPIKNINLENvyTLKSmEDGLALKELLKDEeikniV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 225 VVGASYVALECAGFLTGIGLDTTVMMRS--VPLRGFDQQMASLVTEHMESHGTRFLKGC-VPSLIRklptnqlqvtwEDL 301
Cdd:PRK09564 154 IIGAGFIGLEAVEAAKHLGKNVRIIQLEdrILPDSFDKEITDVMEEELRENGVELHLNEfVKSLIG-----------EDK 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 302 ASG-KEDVGTFDT--VLWAIGRVPET---RNLNLEKAgvntnpKNQKIIVDAQEATSVPHIYAIGDVA------EGRPEL 369
Cdd:PRK09564 223 VEGvVTDKGEYEAdvVIVATGVKPNTeflEDTGLKTL------KNGAIIVDEYGETSIENIYAAGDCAtiynivSNKNVY 296
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 55250718 370 TP---TAIKAGKLLAQRLFGK----SSTLmnySNVPTTVFTpLEYGCVGLSEEEAVAL 420
Cdd:PRK09564 297 VPlatTANKLGRMVGENLAGRhvsfKGTL---GSACIKVLD-LEAARTGLTEEEAKKL 350
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
222-440 |
4.34e-11 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 64.80 E-value: 4.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 222 KTLVVGASYVALECAGFLTGIGLDTTVMMRSVP-LRGFDQQMASLVTEHMESHGTRF-LKGCVPSLirklptNQLQVTWE 299
Cdd:PRK13512 150 KALVVGAGYISLEVLENLYERGLHPTLIHRSDKiNKLMDADMNQPILDELDKREIPYrLNEEIDAI------NGNEVTFK 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 300 dlaSGKEDvgTFDTVLWAIGRVPETRnlNLEKAGVNTNPKNQkIIVDAQEATSVPHIYAIGDVAEG------RPELTPTA 373
Cdd:PRK13512 224 ---SGKVE--HYDMIIEGVGTHPNSK--FIESSNIKLDDKGF-IPVNDKFETNVPNIYAIGDIITShyrhvdLPASVPLA 295
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55250718 374 I---KAGKLLAQRLFGKSS-TLMNYSNVPTTVFTPLEYGCVGLSEEE------AVALHGQEHIEVYHAYYKPLEFTV 440
Cdd:PRK13512 296 WgahRAASIVAEQIAGNDTiEFKGFLGNNIVKFFDYTFASVGVKPNElkqfdyKMVEVTQGAHANYYPGNSPLHLRV 372
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
168-419 |
2.22e-10 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 62.46 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 168 TVHGVDKAGKVTQLSAK------HIVIATGGRPKYPtQVKGALEHGITSDDI-----FW----------LKESPGKTLVV 226
Cdd:COG1252 77 EVTGIDPEARTVTLADGrtlsydYLVIATGSVTNFF-GIPGLAEHALPLKTLedalaLRerllaaferaERRRLLTIVVV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 227 GASY----VALECAGFLTGIGLDTTVMMRSV----------PLRGFDQQMASLVTEHMESHGTRFL-----KGCVPSLIR 287
Cdd:COG1252 156 GGGPtgveLAGELAELLRKLLRYPGIDPDKVritlveagprILPGLGEKLSEAAEKELEKRGVEVHtgtrvTEVDADGVT 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 288 klptnqlqvtwedLASGKE-DvgtFDTVLWAIG-RVPE-TRNLNLEkagvnTNPKNQkIIVDA-QEATSVPHIYAIGDVA 363
Cdd:COG1252 236 -------------LEDGEEiP---ADTVIWAAGvKAPPlLADLGLP-----TDRRGR-VLVDPtLQVPGHPNVFAIGDCA 293
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55250718 364 -------EGRPELTPTAIKAGKLLAQ----RLFGKsstlmnysnvPTTVFTPLEYGC-VGLSEEEAVA 419
Cdd:COG1252 294 avpdpdgKPVPKTAQAAVQQAKVLAKniaaLLRGK----------PLKPFRYRDKGClASLGRGAAVA 351
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
163-386 |
3.53e-10 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 62.54 E-value: 3.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 163 FVNEhTVHGVDKAGKVTQLSAKHI------VIATGGRPKYPTqVKGALEHGITS-------DDIFWLKESPGKTLVVGAS 229
Cdd:TIGR02374 72 YTGE-TVIQIDTDQKQVITDAGRTlsydklILATGSYPFILP-IPGADKKGVYVfrtiedlDAIMAMAQRFKKAAVIGGG 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 230 YVALECAGFLTGIGLDTTV--MMRSVPLRGFDQQMASLVTEHMESHGTRFLkgcvpslirkLPTNQLQVTWEDLASGKE- 306
Cdd:TIGR02374 150 LLGLEAAVGLQNLGMDVSVihHAPGLMAKQLDQTAGRLLQRELEQKGLTFL----------LEKDTVEIVGATKADRIRf 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 307 ---DVGTFDTVLWAIGRVPetrnlNLEKAGVNTNPKNQKIIVDAQEATSVPHIYAIGDVAEGRPE---LTPTAIKAGKLL 380
Cdd:TIGR02374 220 kdgSSLEADLIVMAAGIRP-----NDELAVSAGIKVNRGIIVNDSMQTSDPDIYAVGECAEHNGRvygLVAPLYEQAKVL 294
|
....*.
gi 55250718 381 AQRLFG 386
Cdd:TIGR02374 295 ADHICG 300
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
304-384 |
3.72e-08 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 55.38 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 304 GKEDVGTFDTVLWAIGRVPeTRNLNLEKAGVNTNPKNqKIIVDAQEATSVPHIYAIGDVAEGrPELTPTAIKAGKLLAQR 383
Cdd:PRK12770 268 GSEFVLEADTVVFAIGEIP-TPPFAKECLGIELNRKG-EIVVDEKHMTSREGVFAAGDVVTG-PSKIGKAIKSGLRAAQS 344
|
.
gi 55250718 384 L 384
Cdd:PRK12770 345 I 345
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
312-378 |
1.97e-06 |
|
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: 50.13 E-value: 1.97e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55250718 312 DTVLWAIGRVPETRNLnLEKAGVNTNPKNqKIIVDAQE-ATSVPHIYAIGDVAEGrPELTPTAIKAGK 378
Cdd:COG0493 361 DLVILAIGQTPDPSGL-EEELGLELDKRG-TIVVDEETyQTSLPGVFAGGDAVRG-PSLVVWAIAEGR 425
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
224-391 |
4.41e-06 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 48.76 E-value: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 224 LVVGASYVALECAGFLTGIGLDTTVMMRSvplrgfDQQMASLVTE--------HMESHGTRF-LKGCVPSLIRklPTNQL 294
Cdd:PRK04965 145 LVVGGGLIGTELAMDLCRAGKAVTLVDNA------ASLLASLMPPevssrlqhRLTEMGVHLlLKSQLQGLEK--TDSGI 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 295 QVTwedLASGKE-DVgtfDTVLWAIGRVPETRnLNLEkAGVNTNpknQKIIVDAQEATSVPHIYAIGDVAE--GR--PEL 369
Cdd:PRK04965 217 RAT---LDSGRSiEV---DAVIAAAGLRPNTA-LARR-AGLAVN---RGIVVDSYLQTSAPDIYALGDCAEinGQvlPFL 285
|
170 180
....*....|....*....|..
gi 55250718 370 TPTAIKAgKLLAQRLFGKSSTL 391
Cdd:PRK04965 286 QPIQLSA-MALAKNLLGQNTPL 306
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
43-89 |
6.51e-06 |
|
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: 48.44 E-value: 6.51e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 55250718 43 DLLVIGGGSGGLACAKEAAQLGRKVAVADYVEPSPRGTKWGLGGTCV 89
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGATAWSSGGIDA 47
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
312-382 |
6.53e-05 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 45.56 E-value: 6.53e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55250718 312 DTVLWAIGRVPETRNLNLEKaGVNTNPKNQKIIVDAQEATSVPHIYAIGDVAEGrPELTPTAIKAGKLLAQ 382
Cdd:PRK11749 377 DLVIKAIGQTPNPLILSTTP-GLELNRWGTIIADDETGRTSLPGVFAGGDIVTG-AATVVWAVGDGKDAAE 445
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
43-92 |
7.85e-05 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 45.29 E-value: 7.85e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 55250718 43 DLLVIGGGSGGLACAKEAAQLGRKVAVadyVEPSPRgtkwgLGGTCVNVG 92
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLL---VERRGF-----LGGMLTSGL 42
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
43-87 |
9.60e-05 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 45.10 E-value: 9.60e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 55250718 43 DLLVIGGGSGGLACAKEAAQLGRKVAVadyVEPSPRgtkwgLGGT 87
Cdd:PRK06134 14 DVLVIGSGAAGLSAAVTAAWHGLKVIV---VEKDPV-----FGGT 50
|
|
| Lys_Orn_oxgnase |
pfam13434 |
L-lysine 6-monooxygenase/L-ornithine 5-monooxygenase; This is a family of Rossmann fold ... |
134-203 |
1.58e-04 |
|
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: 43.73 E-value: 1.58e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55250718 134 VQNHVKS-LNWGHRVqlqdRKVKYF--NIKASFvnehTVHGVDKAGKVTQLSAKHIVIATGGRPKYPTQVKGA 203
Cdd:pfam13434 104 AASHLPNrLRFGQEV----ESVEPDaeRGEPLL----RVRVRDADGEETTFLARNLVLGTGGEPYIPECARGG 168
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
41-69 |
1.92e-04 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 43.69 E-value: 1.92e-04
10 20
....*....|....*....|....*....
gi 55250718 41 NFDLLVIGGGSGGLACAKEAAQLGRKVAV 69
Cdd:PRK05329 2 KFDVLVIGGGLAGLTAALAAAEAGKRVAL 30
|
|
| GlpB |
COG3075 |
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism]; |
41-69 |
4.22e-04 |
|
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 442309 Cd Length: 415 Bit Score: 42.86 E-value: 4.22e-04
10 20
....*....|....*....|....*....
gi 55250718 41 NFDLLVIGGGSGGLACAKEAAQLGRKVAV 69
Cdd:COG3075 2 KFDVVVIGGGLAGLTAAIRAAEAGLRVAI 30
|
|
| PRK09126 |
PRK09126 |
FAD-dependent hydroxylase; |
40-78 |
6.89e-04 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236385 [Multi-domain] Cd Length: 392 Bit Score: 42.24 E-value: 6.89e-04
10 20 30
....*....|....*....|....*....|....*....
gi 55250718 40 QNFDLLVIGGGSGGLACAKEAAQLGRKVAVadyVEPSPR 78
Cdd:PRK09126 2 MHSDIVVVGAGPAGLSFARSLAGSGLKVTL---IERQPL 37
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
312-382 |
7.06e-04 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 42.07 E-value: 7.06e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55250718 312 DTVLWAIGRVPETRNLnLEKAGVNTNPKNQKIIVDAQEATSVPHIYAIGDVAEGrPELTPTAIKAGKLLAQ 382
Cdd:PRK12810 390 DLVLLAMGFTGPEAGL-LAQFGVELDERGRVAAPDNAYQTSNPKVFAAGDMRRG-QSLVVWAIAEGRQAAR 458
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
42-80 |
8.48e-04 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 41.74 E-value: 8.48e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 55250718 42 FDLLVIGGGSGGLACAKEAAQLGRKVAVadyVE--PSPRGT 80
Cdd:COG1053 4 YDVVVVGSGGAGLRAALEAAEAGLKVLV---LEkvPPRGGH 41
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
42-85 |
1.80e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 40.97 E-value: 1.80e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 55250718 42 FDLLVIGGGSGGLACAKEAAQLGRKVAVADYVEPSPRGTKWGLG 85
Cdd:PRK12839 9 YDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKASTCGGATAWSGG 52
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
41-194 |
2.00e-03 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 41.00 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 41 NFDLLVIGGGSGGLACAKEAAQLGRKVAVadyVEPSPRgtkwgLGGTCVNVGCIPKKLMHQAALLGGMIRDAQ------- 113
Cdd:COG1148 140 NKRALVIGGGIAGMTAALELAEQGYEVYL---VEKEPE-----LGGRAAQLHKTFPGLDCPQCILEPLIAEVEanpnitv 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 114 HYGWEVaqpvqhnwkamaEAVQNHVkslnwGH-RVQLQDRKVKYFNIKasfvnehtvHGVdkagkvtqlsakhIVIATGG 192
Cdd:COG1148 212 YTGAEV------------EEVSGYV-----GNfTVTIKKGPREEIEIE---------VGA-------------IVLATGF 252
|
..
gi 55250718 193 RP 194
Cdd:COG1148 253 KP 254
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
297-362 |
2.57e-03 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 40.53 E-value: 2.57e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55250718 297 TWEDLASGKEDVGTFDTVLWAIGRVPETRNLnleKAGVNTNPKNQkIIVDAQEATSVPHIYAIGDV 362
Cdd:PRK15317 424 TYKDRTTGEEHHLELEGVFVQIGLVPNTEWL---KGTVELNRRGE-IIVDARGATSVPGVFAAGDC 485
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
43-192 |
4.08e-03 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 39.30 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 43 DLLVIGGGSGGLACAKEAAQLGRKVAVADyvepspRGTKWGLGGTCVNVGCI-------PKKLMHQAALLGGMIRD---- 111
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLE------RGDDPGSGASGRNAGLIhpglrylEPSELARLALEALDLWEelee 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55250718 112 --AQHYGWEVAQPVQHNWKAMAEAVQNHVKSLN-WGHRVQLQDRK-----------------------------VKYFNI 159
Cdd:pfam01266 75 elGIDCGFRRCGVLVLARDEEEEALEKLLAALRrLGVPAELLDAEelrelepllpglrgglfypdgghvdparlLRALAR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 55250718 160 KAS-----FVNEHTVHGVDKAGKVTQL----SAKHIVIATGG 192
Cdd:pfam01266 155 AAEalgvrIIEGTEVTGIEEEGGVWGVvttgEADAVVNAAGA 196
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
40-71 |
4.23e-03 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 39.50 E-value: 4.23e-03
10 20 30
....*....|....*....|....*....|..
gi 55250718 40 QNFDLLVIGGGSGGLACAKEAAQLGRKVAVAD 71
Cdd:COG0665 1 ATADVVVIGGGIAGLSTAYHLARRGLDVTVLE 32
|
|
| PLN02463 |
PLN02463 |
lycopene beta cyclase |
42-77 |
6.38e-03 |
|
lycopene beta cyclase
Pssm-ID: 178082 [Multi-domain] Cd Length: 447 Bit Score: 38.93 E-value: 6.38e-03
10 20 30
....*....|....*....|....*....|....*.
gi 55250718 42 FDLLVIGGGSGGLACAKEAAQLGRKVAVADyvePSP 77
Cdd:PLN02463 29 VDLVVVGGGPAGLAVAQQVSEAGLSVCCID---PSP 61
|
|
| PRK08849 |
PRK08849 |
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional |
42-77 |
6.82e-03 |
|
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
Pssm-ID: 181564 [Multi-domain] Cd Length: 384 Bit Score: 38.98 E-value: 6.82e-03
10 20 30
....*....|....*....|....*....|....*.
gi 55250718 42 FDLLVIGGGSGGLACAKEAAQLGRKVAVADYVEPSP 77
Cdd:PRK08849 4 YDIAVVGGGMVGAATALGFAKQGRSVAVIEGGEPKA 39
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
42-87 |
7.16e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 38.95 E-value: 7.16e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 55250718 42 FDLLVIGGGSGGLACAKEAAQLGRKVAVADYVEPSPRGTKWGLGGT 87
Cdd:PRK12843 17 FDVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGTTATSAGTT 62
|
|
| |
