|
Name |
Accession |
Description |
Interval |
E-value |
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
42-500 |
0e+00 |
|
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: 772.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 42 SFDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHSEFMHDHVDYGFQSC-EGKFSWHV 120
Cdd:TIGR01421 2 HYDYLVIGGGSGGIASARRAAEHGAKALLVEAKKLGGTCVNVGCVPKKVMWYASDLAERMHDAADYGFYQNdENTFNWPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 121 IKQKRDAYVSRLNTIYQNNLTKSHIEIIHGYATFADgpRPTVEVNGKKFTAPHILIATGGVPTVPheSQIPGASLGITSD 200
Cdd:TIGR01421 82 LKEKRDAYVDRLNGIYQKNLEKNKVDVIFGHARFTK--DGTVEVNGRDYTAPHILIATGGKPSFP--ENIPGAELGTDSD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 201 GFFQLEDLPSRSVIVGAGYIAVEIAGILSALGSKTSLMIRHDKVLRNFDSLISSNCTEELENAGVEVLKFTQVKEVKKTS 280
Cdd:TIGR01421 158 GFFALEELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRHERVLRSFDSMISETITEEYEKEGINVHKLSKPVKVEKTV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 281 SGLELQVVTSVpgrkpttTMIPDVDCLLWAIGRDPNSKGLNLNKVGIQTDEKGHILVDEFQNTNVKGVYAVGDVCGKALL 360
Cdd:TIGR01421 238 EGKLVIHFEDG-------KSIDDVDELIWAIGRKPNTKGLGLENVGIKLNEKGQIIVDEYQNTNVPGIYALGDVVGKVEL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 361 TPVAIAAGRKLAHRLFECKQDSKLDYDNIPTVVFSHPPIGTVGLTEDEAVHKYGKDNVKIYSTAFTPMYHAVTTRKTKCV 440
Cdd:TIGR01421 311 TPVAIAAGRKLSERLFNGKTDDKLDYNNVPTVVFSHPPIGTIGLTEKEAIEKYGKENIKVYNSSFTPMYYAMTSEKQKCR 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 441 MKMVCANKEEKVVGIHMQGIGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTLR 500
Cdd:TIGR01421 391 MKLVCAGKEEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEELVTMR 450
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
43-500 |
0e+00 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 678.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 43 FDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHSEFMHDH-VDYGFQSCEGKFSWHVI 121
Cdd:PRK06116 5 YDLIVIGGGSGGIASANRAAMYGAKVALIEAKRLGGTCVNVGCVPKKLMWYGAQIAEAFHDYaPGYGFDVTENKFDWAKL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 122 KQKRDAYVSRLNTIYQNNLTKSHIEIIHGYATFADGPrpTVEVNGKKFTAPHILIATGGVPTVPhesQIPGASLGITSDG 201
Cdd:PRK06116 85 IANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAH--TVEVNGERYTADHILIATGGRPSIP---DIPGAEYGITSDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 202 FFQLEDLPSRSVIVGAGYIAVEIAGILSALGSKTSLMIRHDKVLRNFDSLISSNCTEELENAGVEVLKFTQVKEVKKTSS 281
Cdd:PRK06116 160 FFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNAD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 282 GlELQVVTSvPGRKPTttmipdVDCLLWAIGRDPNSKGLNLNKVGIQTDEKGHILVDEFQNTNVKGVYAVGDVCGKALLT 361
Cdd:PRK06116 240 G-SLTLTLE-DGETLT------VDCLIWAIGREPNTDGLGLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGDVTGRVELT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 362 PVAIAAGRKLAHRLFECKQDSKLDYDNIPTVVFSHPPIGTVGLTEDEAVHKYGKDNVKIYSTAFTPMYHAVTTRKTKCVM 441
Cdd:PRK06116 312 PVAIAAGRRLSERLFNNKPDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVKVYRSSFTPMYTALTGHRQPCLM 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 160298213 442 KMVCANKEEKVVGIHMQGIGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTLR 500
Cdd:PRK06116 392 KLVVVGKEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFVTMR 450
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
55-500 |
2.04e-160 |
|
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: 462.63 E-value: 2.04e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 55 LASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHSEFMHDHVDYGFQSCEGKFSWHVIKQKRDAYVSRLNT 134
Cdd:COG1249 16 YVAAIRAAQLGLKVALVEKGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISAGAPSVDWAALMARKDKVVDRLRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 135 IYQNNLTKSHIEIIHGYATFADgPRpTVEVNGKK-FTAPHILIATGGVPTVPhesQIPGAS--LGITSDGFFQLEDLPSR 211
Cdd:COG1249 96 GVEELLKKNGVDVIRGRARFVD-PH-TVEVTGGEtLTADHIVIATGSRPRVP---PIPGLDevRVLTSDEALELEELPKS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 212 SVIVGAGYIAVEIAGILSALGSKTSLMIRHDKVLRNFDSLISSNCTEELENAGVEVLKFTQVKEVKKTSSGLelqVVTSV 291
Cdd:COG1249 171 LVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDGV---TVTLE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 292 PGRKPTTTmipDVDCLLWAIGRDPNSKGLNLNKVGIQTDEKGHILVDEFQNTNVKGVYAVGDVCGKALLTPVAIAAGRKL 371
Cdd:COG1249 248 DGGGEEAV---EADKVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRTSVPGIYAIGDVTGGPQLAHVASAEGRVA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 372 AHRLFEcKQDSKLDYDNIPTVVFSHPPIGTVGLTEDEAVHKygKDNVKIYSTAFTPMYHAVTTRKTKCVMKMVCANKEEK 451
Cdd:COG1249 325 AENILG-KKPRPVDYRAIPSVVFTDPEIASVGLTEEEAREA--GIDVKVGKFPFAANGRALALGETEGFVKLIADAETGR 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 160298213 452 VVGIHMQGIGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTLR 500
Cdd:COG1249 402 ILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAA 450
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
43-499 |
1.92e-144 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 425.95 E-value: 1.92e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 43 FDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHSEFMHDHVDYGFQSCEGkFSWHVIK 122
Cdd:PTZ00058 49 YDLIVIGGGSGGMAAARRAARNKAKVALVEKDYLGGTCVNVGCVPKKIMFNAASIHDILENSRHYGFDTQFS-FNLPLLV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 123 QKRDAYVSRLNTIYQNNLTKSHIEIIHGYATFADGPRPTVEV---------------------------NGKKFTAPHIL 175
Cdd:PTZ00058 128 ERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLIKKvsqvdgeadesdddevtivsagvsqldDGQVIEGKNIL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 176 IATGGVPTVPhesQIPGASLGITSDGFFQLEDlPSRSVIVGAGYIAVEIAGILSALGSKTSLMIRHDKVLRNFDSLISSN 255
Cdd:PTZ00058 208 IAVGNKPIFP---DVKGKEFTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLRKFDETIINE 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 256 CTEELENAGVEVLKFTQVKEVKKTSSGLELQVVTSvpGRKPTTtmipdVDCLLWAIGRDPNSKGLNLNKVGIQTdEKGHI 335
Cdd:PTZ00058 284 LENDMKKNNINIITHANVEEIEKVKEKNLTIYLSD--GRKYEH-----FDYVIYCVGRSPNTEDLNLKALNIKT-PKGYI 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 336 LVDEFQNTNVKGVYAVGDVCGKAL----------------------------------LTPVAIAAGRKLAHRLFECKQD 381
Cdd:PTZ00058 356 KVDDNQRTSVKHIYAVGDCCMVKKnqeiedlnllklyneepylkkkentsgesyynvqLTPVAINAGRLLADRLFGPFSR 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 382 sKLDYDNIPTVVFSHPPIGTVGLTEDEAVHKYGKDNVKIYSTAFTPMYHAV----TTRKTKCVMKMVCANKEEKVVGIHM 457
Cdd:PTZ00058 436 -TTNYKLIPSVIFSHPPIGTIGLSEQEAIDIYGKENVKIYESRFTNLFFSVydmdPAQKEKTYLKLVCVGKEELIKGLHI 514
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 160298213 458 QGIGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTL 499
Cdd:PTZ00058 515 VGLNADEILQGFAVALKMNATKADFDETIPIHPTAAEEFVTM 556
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
43-500 |
3.92e-139 |
|
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: 408.43 E-value: 3.92e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 43 FDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHSEFMHDHVDYGFQSCEGKFSWHVIK 122
Cdd:TIGR01424 3 YDLFVIGAGSGGVRAARLAAALGAKVAIAEEFRVGGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGWTVGKARFDWKKLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 123 QKRDAYVSRLNTIYQNNLTKSHIEIIHGYATFADGprPTVEV--NGKKFTAPHILIATGGVPTVPhesQIPGASLGITSD 200
Cdd:TIGR01424 83 AAKDQEIARLSGLYRKGLANAGAELLDGRAELVGP--NTVEVlaSGKTYTAEKILIAVGGRPPKP---ALPGHELGITSN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 201 GFFQLEDLPSRSVIVGAGYIAVEIAGILSALGSKTSLMIRHDKVLRNFDSLISSNCTEELENAGVEVLKFTQVKEVKKTS 280
Cdd:TIGR01424 158 EAFHLPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRGKEILRGFDDDMRRGLAAALEERGIRILPEDSITSISKDD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 281 SGlELQVVTSVPGrkpttTMIPDVdcLLWAIGRDPNSKGLNLNKVGIQTDEKGHILVDEFQNTNVKGVYAVGDVCGKALL 360
Cdd:TIGR01424 238 DG-RLKATLSKHE-----EIVADV--VLFATGRSPNTNGLGLEAAGVRLNDLGAIAVDEYSRTSTPSIYAVGDVTDRINL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 361 TPVAIAAGRKLAHRLFECKQdSKLDYDNIPTVVFSHPPIGTVGLTEDEAVHKYGKdnVKIYSTAFTPMYHAVTTRKTKCV 440
Cdd:TIGR01424 310 TPVAIHEATCFAETEFGNNP-TSFDHDLIATAVFSQPPIGTVGLTEEEARRKFGD--IEVYRAEFRPMKATFSGRQEKTL 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 441 MKMVCANKEEKVVGIHMQGIGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTLR 500
Cdd:TIGR01424 387 MKLVVDAKDDKVLGAHMVGPDAAEIIQGLAIALKMGATKDDFDSTVAVHPTSAEELVTMR 446
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
43-499 |
1.37e-122 |
|
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: 367.25 E-value: 1.37e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 43 FDYLVIGGGSGGLASARRAAELGARAAVVESHK---------LGGTCVNVGCVPKKVMWNTAVHSEFMHDHVDYGFQSCE 113
Cdd:TIGR01438 3 YDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTptplgtrwgIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 114 G-KFSWHVIKQKRDAYVSRLNTIYQNNLTKSHIEIIHGYATFADGPRPTVEVNGKK---FTAPHILIATGGVPTVPhesQ 189
Cdd:TIGR01438 83 TvKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKekiYSAERFLIATGERPRYP---G 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 190 IPGAS-LGITSDGFFQLEDLPSRSVIVGAGYIAVEIAGILSALGSKTSLMIRhDKVLRNFDSLISSNCTEELENAGVEVL 268
Cdd:TIGR01438 160 IPGAKeLCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVR-SILLRGFDQDCANKVGEHMEEHGVKFK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 269 KFTQVKEVKKTSSGLELQVVTSvpgrkpTTTMIPDVDCLLWAIGRDPNSKGLNLNKVGIQTDEK-GHILVDEFQNTNVKG 347
Cdd:TIGR01438 239 RQFVPIKVEQIEAKVLVEFTDS------TNGIEEEYDTVLLAIGRDACTRKLNLENVGVKINKKtGKIPADEEEQTNVPY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 348 VYAVGDVC-GKALLTPVAIAAGRKLAHRLFEcKQDSKLDYDNIPTVVFSHPPIGTVGLTEDEAVHKYGKDNVKIYSTAFT 426
Cdd:TIGR01438 313 IYAVGDILeDKPELTPVAIQAGRLLAQRLFK-GSTVICDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENVEVFHSYFW 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160298213 427 PMYHAVTTRK--TKCVMKMVCANKE-EKVVGIHMQGIGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTL 499
Cdd:TIGR01438 392 PLEWTIPSRDnhNKCYAKLVCNKKEnERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTL 467
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
43-500 |
3.53e-115 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 348.73 E-value: 3.53e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 43 FDYLVIGGGSGGLASARRAAELGARAAVVE----------SHKLGGTCVNVGCVPKKVMWNTAVHSEFMHDHVDYGFQSC 112
Cdd:PLN02507 26 FDLFVIGAGSGGVRAARFSANFGAKVGICElpfhpissesIGGVGGTCVIRGCVPKKILVYGATFGGEFEDAKNYGWEIN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 113 EG-KFSWHVIKQKRDAYVSRLNTIYQNNLTKSHIEIIHGYATFAdGPRpTVEV-----NGKKFTAPHILIATGGVPTVPH 186
Cdd:PLN02507 106 EKvDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIV-GPN-EVEVtqldgTKLRYTAKHILIATGSRAQRPN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 187 esqIPGASLGITSDGFFQLEDLPSRSVIVGAGYIAVEIAGILSALGSKTSLMIRHDKVLRNFDSLISSNCTEELENAGVE 266
Cdd:PLN02507 184 ---IPGKELAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRAVVARNLEGRGIN 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 267 VLKFTQVKEVKKTSSGLElqvVTSVPGRKPTTtmipdvDCLLWAIGRDPNSKGLNLNKVGIQTDEKGHILVDEFQNTNVK 346
Cdd:PLN02507 261 LHPRTNLTQLTKTEGGIK---VITDHGEEFVA------DVVLFATGRAPNTKRLNLEAVGVELDKAGAVKVDEYSRTNIP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 347 GVYAVGDVCGKALLTPVAIAAGRKLAHRLFEcKQDSKLDYDNIPTVVFSHPPIGTVGLTEDEAVhKYGKDNVKIYSTAFT 426
Cdd:PLN02507 332 SIWAIGDVTNRINLTPVALMEGTCFAKTVFG-GQPTKPDYENVACAVFCIPPLSVVGLSEEEAV-EQAKGDILVFTSSFN 409
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160298213 427 PMYHAVTTRKTKCVMKMVCANKEEKVVGIHMQGIGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTLR 500
Cdd:PLN02507 410 PMKNTISGRQEKTVMKLIVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEFVTMR 483
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
2-500 |
2.33e-113 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 346.09 E-value: 2.33e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 2 ALLPRaLGVGAAPSLRRAARALTCAMASPGEPQPPAPDtssFDYLVIGGGSGGLASARRAAELGARAAVVE--------- 72
Cdd:PLN02546 43 KTLTR-LSSPRPLSHHHRRRSVSRAAAPNGAESERHYD---FDLFTIGAGSGGVRASRFASNFGASAAVCElpfatissd 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 73 -SHKLGGTCVNVGCVPKKVMWNTAVHS-EFMHDHvdyGF---QSCEGKFSWHVIKQKRDAYVSRLNTIYQNNLTKSHIEI 147
Cdd:PLN02546 119 tLGGVGGTCVLRGCVPKKLLVYASKYShEFEESR---GFgwkYETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 148 IHGYATFADgPRpTVEVNGKKFTAPHILIATGGVPTVPhesQIPGASLGITSDGFFQLEDLPSRSVIVGAGYIAVEIAGI 227
Cdd:PLN02546 196 IEGRGKIVD-PH-TVDVDGKLYTARNILIAVGGRPFIP---DIPGIEHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGI 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 228 LSALGSKTSLMIRHDKVLRNFDSLISSNCTEELENAGVEVLKFTQVKEVKKTSSGLelqvvTSVPGRKPTTTMIPDVdcl 307
Cdd:PLN02546 271 FNGLKSDVHVFIRQKKVLRGFDEEVRDFVAEQMSLRGIEFHTEESPQAIIKSADGS-----LSLKTNKGTVEGFSHV--- 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 308 LWAIGRDPNSKGLNLNKVGIQTDEKGHILVDEFQNTNVKGVYAVGDVCGKALLTPVAIAAGRKLAHRLFEcKQDSKLDYD 387
Cdd:PLN02546 343 MFATGRKPNTKNLGLEEVGVKMDKNGAIEVDEYSRTSVPSIWAVGDVTDRINLTPVALMEGGALAKTLFG-NEPTKPDYR 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 388 NIPTVVFSHPPIGTVGLTEDEAVHKYGkdNVKIYSTAFTPMYHAVTTRKTKCVMKMVCANKEEKVVGIHMQGIGCDEMLQ 467
Cdd:PLN02546 422 AVPSAVFSQPPIGQVGLTEEQAIEEYG--DVDVFTANFRPLKATLSGLPDRVFMKLIVCAKTNKVLGVHMCGEDAPEIIQ 499
|
490 500 510
....*....|....*....|....*....|...
gi 160298213 468 GFAVAVKMGATKADFDNTVAIHPTSSEELVTLR 500
Cdd:PLN02546 500 GFAVAVKAGLTKADFDATVGIHPTAAEEFVTMR 532
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
43-499 |
5.97e-98 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 304.44 E-value: 5.97e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 43 FDYLVIGGGSGGLASARRAAELGARAAVVESHK---------LGGTCVNVGCVPKKVMWNTA-VHSEFMHDHVDYGFqSC 112
Cdd:PTZ00052 6 YDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKpstqgtkwgLGGTCVNVGCVPKKLMHYAAnIGSIFHHDSQMYGW-KT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 113 EGKFSWHVIKQKRDAYVSRLNTIYQNNLTKSHIEIIHGYATFADGPRPTVEVNGKK--FTAPHILIATGGVPTVPHEsqI 190
Cdd:PTZ00052 85 SSSFNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTVSYGDNSQEetITAKYILIATGGRPSIPED--V 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 191 PGA-SLGITSDGFFQLEDLPSRSVIVGAGYIAVEIAGILSALGSKTSLMIRhDKVLRNFDSLISSNCTEELENAGVEVLK 269
Cdd:PTZ00052 163 PGAkEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVR-SIPLRGFDRQCSEKVVEYMKEQGTLFLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 270 FTQVKEVKKTSSglELQVVTSvpgrKPTTTMIpdvDCLLWAIGRDPNSKGLNLNKVGIQTDEKGHILVDEfQNTNVKGVY 349
Cdd:PTZ00052 242 GVVPINIEKMDD--KIKVLFS----DGTTELF---DTVLYATGRKPDIKGLNLNAIGVHVNKSNKIIAPN-DCTNIPNIF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 350 AVGDVC-GKALLTPVAIAAGRKLAHRLFEcKQDSKLDYDNIPTVVFSHPPIGTVGLTEDEAVHKYGKDNVKIYSTAFTPM 428
Cdd:PTZ00052 312 AVGDVVeGRPELTPVAIKAGILLARRLFK-QSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQEFNTL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 429 -------YHAVTTRK--------TKCVMKMVC-ANKEEKVVGIHMQGIGCDEMLQGFAVAVKMGATKADFDNTVAIHPTS 492
Cdd:PTZ00052 391 eiaavhrEKHERARKdeydfdvsSNCLAKLVCvKSEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHPTD 470
|
....*..
gi 160298213 493 SEELVTL 499
Cdd:PTZ00052 471 AEVFMNL 477
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
40-500 |
4.35e-96 |
|
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: 299.20 E-value: 4.35e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 40 TSSFDYLVIGGGSGGLASARRAAEL-GARAAVVESHK---------LGGTCVNVGCVPKKVMWNTAVHSEFMHDHVDYG- 108
Cdd:TIGR01423 1 SKAFDLVVIGAGSGGLEAGWNAATLyKKRVAVVDVQThhgppfyaaLGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGw 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 109 -FQSCEGKFSWHVIKQKRDAYVSRLNTIYQNNLTKSH-IEIIHGYATFADGP----RPTVEVNGK---KFTAPHILIATG 179
Cdd:TIGR01423 81 eFDRSSVKANWKALIAAKNKAVLDINKSYEGMFADTEgLTFFLGWGALEDKNvvlvRESADPKSAvkeRLQAEHILLATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 180 GVPTVPhesQIPGASLGITSDGFFQLEDLPSRSVIVGAGYIAVEIAGILSA---LGSKTSLMIRHDKVLRNFDSLISSNC 256
Cdd:TIGR01423 161 SWPQML---GIPGIEHCISSNEAFYLDEPPRRVLTVGGGFISVEFAGIFNAykpRGGKVTLCYRNNMILRGFDSTLRKEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 257 TEELENAGVEVLKFTQVKEVKKTSSGLelQVVTSVPGRKPtttmipDVDCLLWAIGRDPNSKGLNLNKVGIQTDEKGHIL 336
Cdd:TIGR01423 238 TKQLRANGINIMTNENPAKVTLNADGS--KHVTFESGKTL------DVDVVMMAIGRVPRTQTLQLDKVGVELTKKGAIQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 337 VDEFQNTNVKGVYAVGDVCGKALLTPVAIAAGRKLAHRLFECKQdSKLDYDNIPTVVFSHPPIGTVGLTEDEAVHKYgkD 416
Cdd:TIGR01423 310 VDEFSRTNVPNIYAIGDVTDRVMLTPVAINEGAAFVDTVFGNKP-RKTDHTRVASAVFSIPPIGTCGLVEEDAAKKF--E 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 417 NVKIYSTAFTPMYHAVTTRK-TKCVMKMVCANKEEKVVGIHMQGIGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEE 495
Cdd:TIGR01423 387 KVAVYESSFTPLMHNISGSKyKKFVAKIVTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAEE 466
|
....*
gi 160298213 496 LVTLR 500
Cdd:TIGR01423 467 LCSMR 471
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
42-496 |
1.62e-93 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 291.66 E-value: 1.62e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 42 SFDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHSEFMHDHVDYGFQSCEGKFSWHVI 121
Cdd:PRK06416 4 EYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIKAENVGIDFKKV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 122 KQKRDAYVSRLNTIYQNNLTKSHIEIIHGYATFAdGPRpTVEVNGKK----FTAPHILIATGGVPTVphesqIPGASLG- 196
Cdd:PRK06416 84 QEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLV-DPN-TVRVMTEDgeqtYTAKNIILATGSRPRE-----LPGIEIDg 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 197 ---ITSDGFFQLEDLPSRSVIVGAGYIAVEIAGILSALGSKTSLMIRHDKVLRNFDSLISSNCTEELENAGVEVLKFTQV 273
Cdd:PRK06416 157 rviWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPGEDKEISKLAERALKKRGIKIKTGAKA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 274 KEVKKTSSGLElqvVTSVPGRKPTTTmipDVDCLLWAIGRDPNSKGLNLNKVGIQTDeKGHILVDEFQNTNVKGVYAVGD 353
Cdd:PRK06416 237 KKVEQTDDGVT---VTLEDGGKEETL---EADYVLVAVGRRPNTENLGLEELGVKTD-RGFIEVDEQLRTNVPNIYAIGD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 354 VCGKALLTPVAIAAGRKLAHRLfeCKQDSKLDYDNIPTVVFSHPPIGTVGLTEDEAvhKYGKDNVKIYSTAFTPMYHAVT 433
Cdd:PRK06416 310 IVGGPMLAHKASAEGIIAAEAI--AGNPHPIDYRGIPAVTYTHPEVASVGLTEAKA--KEEGFDVKVVKFPFAGNGKALA 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160298213 434 TRKTKCVMKMVCANKEEKVVGIHMQGIGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEEL 496
Cdd:PRK06416 386 LGETDGFVKLIFDKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEAL 448
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
42-499 |
7.80e-92 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 287.48 E-value: 7.80e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 42 SFDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHSEFMHDHVDYGFQSCEG-KFSWHV 120
Cdd:PRK06370 5 RYDAIVIGAGQAGPPLAARAAGLGMKVALIERGLLGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGGPvSVDFKA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 121 IKQKRDAYVSRLNTIYQNNLTK-SHIEIIHGYATFAdGPRpTVEVNGKKFTAPHILIATGGVPTVPHesqIPG-ASLG-I 197
Cdd:PRK06370 85 VMARKRRIRARSRHGSEQWLRGlEGVDVFRGHARFE-SPN-TVRVGGETLRAKRIFINTGARAAIPP---IPGlDEVGyL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 198 TSDGFFQLEDLPSRSVIVGAGYIAVEIAGILSALGSKTSLMIRHDKVLRNFDSLISSNCTEELENAGVEVLKFTQVKEVK 277
Cdd:PRK06370 160 TNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILEREGIDVRLNAECIRVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 278 KTSSGLELQVVtsVPGRKPTTTmipdVDCLLWAIGRDPNSKGLNLNKVGIQTDEKGHILVDEFQNTNVKGVYAVGDVCGK 357
Cdd:PRK06370 240 RDGDGIAVGLD--CNGGAPEIT----GSHILVAVGRVPNTDDLGLEAAGVETDARGYIKVDDQLRTTNPGIYAAGDCNGR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 358 ALLTPVAIAAGRKLAHRLFEcKQDSKLDYDNIPTVVFSHPPIGTVGLTEDEAVhKYGKDnVKIYSTAFTPMYHAVTTRKT 437
Cdd:PRK06370 314 GAFTHTAYNDARIVAANLLD-GGRRKVSDRIVPYATYTDPPLARVGMTEAEAR-KSGRR-VLVGTRPMTRVGRAVEKGET 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160298213 438 KCVMKMVCANKEEKVVGIHMQGIGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTL 499
Cdd:PRK06370 391 QGFMKVVVDADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIPTL 452
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
43-496 |
2.18e-89 |
|
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: 281.23 E-value: 2.18e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 43 FDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWnTAVHSEFMHDHVDYGFQSCEGKFSW-HVI 121
Cdd:TIGR02053 1 YDLVIIGSGAAAFAAAIKAAELGASVAMVERGPLGGTCVNVGCVPSKMLL-RAAEVAHYARKPPFGGLAATVAVDFgELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 122 KQKRDAYVSRLNTIYQNNLTKSHIEIIHGYATFADGprPTVEVNGKK--FTAPHILIATGGVPTVPHesqIPG-ASLG-I 197
Cdd:TIGR02053 80 EGKREVVEELRHEKYEDVLSSYGVDYLRGRARFKDP--KTVKVDLGRevRGAKRFLIATGARPAIPP---IPGlKEAGyL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 198 TSDGFFQLEDLPSRSVIVGAGYIAVEIAGILSALGSKTSLMIRHDKVLRNFDSLISSNCTEELENAGVEVLKFTQVKEVK 277
Cdd:TIGR02053 155 TSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSDRLLPREEPEISAAVEEALAEEGIEVVTSAQVKAVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 278 KTSSGleLQVVTSVPGRKptttMIPDVDCLLWAIGRDPNSKGLNLNKVGIQTDEKGHILVDEFQNTNVKGVYAVGDVCGK 357
Cdd:TIGR02053 235 VRGGG--KIITVEKPGGQ----GEVEADELLVATGRRPNTDGLGLEKAGVKLDERGGILVDETLRTSNPGIYAAGDVTGG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 358 ALLTPVAIAAGRKLAHRLFEcKQDSKLDYDNIPTVVFSHPPIGTVGLTEDEAVHKYGkdNVKIYSTAFTPMYHAVTTRKT 437
Cdd:TIGR02053 309 LQLEYVAAKEGVVAAENALG-GANAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAGI--ECDCRTLPLTNVPRARINRDT 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 160298213 438 KCVMKMVCANKEEKVVGIHMQGIGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEEL 496
Cdd:TIGR02053 386 RGFIKLVAEPGTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGL 444
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
42-494 |
2.99e-88 |
|
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: 277.99 E-value: 2.99e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 42 SFDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAvhsEFMHDHV---DYGFQSCEGKFSW 118
Cdd:TIGR01350 1 AYDVIVIGGGPGGYVAAIRAAQLGLKVALVEKEYLGGTCLNVGCIPTKALLHSA---EVYDEIKhakDLGIEVENVSVDW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 119 HVIKQKRDAYVSRLNTIYQNNLTKSHIEIIHGYATFADgPRpTVEVNGKK----FTAPHILIATGGVPTVPHESQIPGAS 194
Cdd:TIGR01350 78 EKMQKRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLD-PG-TVSVTGENgeetLEAKNIIIATGSRPRSLPGPFDFDGK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 195 LGITSDGFFQLEDLPSRSVIVGAGYIAVEIAGILSALGSKTSLMIRHDKVLRNFDSLISSNCTEELENAGVEVLKFTQVK 274
Cdd:TIGR01350 156 VVITSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 275 EVKKTSSglelQVVTSVPGRKPTTTmipDVDCLLWAIGRDPNSKGLNLNKVGIQTDEKGHILVDEFQNTNVKGVYAVGDV 354
Cdd:TIGR01350 236 AVEKNDD----QVTYENKGGETETL---TGEKVLVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 355 CGKALLTPVAIAAGRKLAHRLFEcKQDSKLDYDNIPTVVFSHPPIGTVGLTEDEAVHKYGkdNVKIYSTAFTPMYHAVTT 434
Cdd:TIGR01350 309 IGGPMLAHVASHEGIVAAENIAG-KEPAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGY--DVKIGKFPFAANGKALAL 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 435 RKTKCVMKMVCANKEEKVVGIHMQGIGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSE 494
Cdd:TIGR01350 386 GETDGFVKIIADKKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSE 445
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
42-494 |
8.98e-86 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 271.67 E-value: 8.98e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 42 SFDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKV------MWNTAVHSEFMhdHVDYGFQSCEGK 115
Cdd:PRK06292 3 KYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGPLGGTCLNVGCIPSKAliaaaeAFHEAKHAEEF--GIHADGPKIDFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 116 FSWHVIKQKRDAYVSrlnTIYQNNLTKSHIEIIHGYATFADgPRpTVEVNGKKFTAPHILIATGG-VPTVPHESQIPGAS 194
Cdd:PRK06292 81 KVMARVRRERDRFVG---GVVEGLEKKPKIDKIKGTARFVD-PN-TVEVNGERIEAKNIVIATGSrVPPIPGVWLILGDR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 195 LgITSDGFFQLEDLPSRSVIVGAGYIAVEIAGILSALGSKTSLMIRHDKVLRNFDSLISSNCTEELEnagvEVLKF---T 271
Cdd:PRK06292 156 L-LTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILS----KEFKIklgA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 272 QVKEVKKtsSGLELQVVTSVPGRKPTTTmipdVDCLLWAIGRDPNSKGLNLNKVGIQTDEKGHILVDEFQNTNVKGVYAV 351
Cdd:PRK06292 231 KVTSVEK--SGDEKVEELEKGGKTETIE----ADYVLVATGRRPNTDGLGLENTGIELDERGRPVVDEHTQTSVPGIYAA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 352 GDVCGKALLTPVAIAAGRKLAHRLFEcKQDSKLDYDNIPTVVFSHPPIGTVGLTEDEAVHKYGKDNVKIYSTAFTPMYHA 431
Cdd:PRK06292 305 GDVNGKPPLLHEAADEGRIAAENAAG-DVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEVPFEAQGRARV 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160298213 432 VttRKTKCVMKMVCANKEEKVVGIHMQGIGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSE 494
Cdd:PRK06292 384 M--GKNDGFVKVYADKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSE 444
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
67-410 |
4.39e-62 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 209.43 E-value: 4.39e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 67 RAAVVESHKLGGTCVNVGCVPKKVMWNTA-VHSEFMHDhVDYGFQSCEGKFSWHVIkqkRDAYVSRLNTI------YQNN 139
Cdd:PRK07846 24 RIAIVEKGTFGGTCLNVGCIPTKMFVYAAdVARTIREA-ARLGVDAELDGVRWPDI---VSRVFGRIDPIaaggeeYRGR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 140 LTkSHIEIIHGYATFADGPRPTVEVnGKKFTAPHILIATGGVPTVPhesQIPGASlGI---TSDGFFQLEDLPSRSVIVG 216
Cdd:PRK07846 100 DT-PNIDVYRGHARFIGPKTLRTGD-GEEITADQVVIAAGSRPVIP---PVIADS-GVryhTSDTIMRLPELPESLVIVG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 217 AGYIAVEIAGILSALGSKTSLMIRHDKVLRNFDSLISSNCTEeLENAGVEVLKFTQVKEVKKTSSG--LELQVVTSVPGr 294
Cdd:PRK07846 174 GGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLDDDISERFTE-LASKRWDVRLGRNVVGVSQDGSGvtLRLDDGSTVEA- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 295 kptttmipdvDCLLWAIGRDPNSKGLNLNKVGIQTDEKGHILVDEFQNTNVKGVYAVGDVCGKALLTPVAIAAGRKLAHR 374
Cdd:PRK07846 252 ----------DVLLVATGRVPNGDLLDAAAAGVDVDEDGRVVVDEYQRTSAEGVFALGDVSSPYQLKHVANHEARVVQHN 321
|
330 340 350
....*....|....*....|....*....|....*.
gi 160298213 375 LFECKQDSKLDYDNIPTVVFSHPPIGTVGLTEDEAV 410
Cdd:PRK07846 322 LLHPDDLIASDHRFVPAAVFTHPQIASVGLTENEAR 357
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
43-368 |
9.53e-61 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 201.39 E-value: 9.53e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 43 FDYLVIGGGSGGLASARRAAELGARAAVVEshkLGGTCVNVGCVPKKVMWNTAvhsefmHDHvdygfqscEGKFSWHVIK 122
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIE---DEGTCPYGGCVLSKALLGAA------EAP--------EIASLWADLY 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 123 QKRDAYVSRLNTIYQNNLTKSHIEIIHGYATFADgpRPTVEVNGKKFTAPHILIATGGVPTVPHesqIPGASLG------ 196
Cdd:pfam07992 64 KRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVL--EELVDGDGETITYDRLVIATGARPRLPP---IPGVELNvgflvr 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 197 -ITSDGFFQLEDLPSRSVIVGAGYIAVEIAGILSALGSKTSLMIRHDKVLRNFDSLISSNCTEELENAGVEVLKFTQVKE 275
Cdd:pfam07992 139 tLDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 276 VKKTSSGLElqVVTSVPGRKptttmipDVDCLLWAIGRDPNSKGlnLNKVGIQTDEKGHILVDEFQNTNVKGVYAVGDV- 354
Cdd:pfam07992 219 IIGDGDGVE--VILKDGTEI-------DADLVVVAIGRRPNTEL--LEAAGLELDERGGIVVDEYLRTSVPGIYAAGDCr 287
|
330
....*....|....
gi 160298213 355 CGKALLTPVAIAAG 368
Cdd:pfam07992 288 VGGPELAQNAVAQG 301
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
43-494 |
1.42e-56 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 195.53 E-value: 1.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 43 FDYLVIGGGSGGLASARRAAELGARAAVVESHK-------LGGTCVNVGCVPKKVMWNTAVHSEFM-HDHVDYGFQSCEG 114
Cdd:PRK06327 5 FDVVVIGAGPGGYVAAIRAAQLGLKVACIEAWKnpkgkpaLGGTCLNVGCIPSKALLASSEEFENAgHHFADHGIHVDGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 115 KFSWHVIKQKRDAYVSRLNTIYQNNLTKSHIEIIHGYATF---ADGPRpTVEVNGKK---FTAPHILIATGGVPtvpheS 188
Cdd:PRK06327 85 KIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFvgkTDAGY-EIKVTGEDetvITAKHVIIATGSEP-----R 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 189 QIPGASLG----ITSDGFFQLEDLPSRSVIVGAGYIAVEIAGILSALGSKTSLMIRHDKVLRNFDSLISSNCTEELENAG 264
Cdd:PRK06327 159 HLPGVPFDnkiiLDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAAADEQVAKEAAKAFTKQG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 265 VEVLKFTQVKEVKKTSSGLELQVvTSVPGRKPTTtmipDVDCLLWAIGRDPNSKGLNLNKVGIQTDEKGHILVDEFQNTN 344
Cdd:PRK06327 239 LDIHLGVKIGEIKTGGKGVSVAY-TDADGEAQTL----EVDKLIVSIGRVPNTDGLGLEAVGLKLDERGFIPVDDHCRTN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 345 VKGVYAVGDVCGKALLTPVAIAAGRKLAHRLfeCKQDSKLDYDNIPTVVFSHPPIGTVGLTEDEAVhkygKDNVKIYSTA 424
Cdd:PRK06327 314 VPNVYAIGDVVRGPMLAHKAEEEGVAVAERI--AGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLK----AEGVEYKAGK 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160298213 425 FTPMYH--AVTTRKTKCVMKMVCANKEEKVVGIHMQGIGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSE 494
Cdd:PRK06327 388 FPFMANgrALAMGEPDGFVKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSE 459
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
6-412 |
7.16e-56 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 195.76 E-value: 7.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 6 RALGVGA----APSLRRAARALTCAMASPGEPQPPAPDTSSFDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCV 81
Cdd:PRK13748 58 AGLGYRAtladAPPTDNRGGLLDKMRGWLGGADKHSGNERPLHVAVIGSGGAAMAAALKAVEQGARVTLIERGTIGGTCV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 82 NVGCVPKKVMWNTAVHSEFMHDH-VDYGFQSCEGKFSWHVIKQKRDAYVSRL-NTIYQNNL-TKSHIEIIHGYATFADGP 158
Cdd:PRK13748 138 NVGCVPSKIMIRAAHIAHLRRESpFDGGIAATVPTIDRSRLLAQQQARVDELrHAKYEGILdGNPAITVLHGEARFKDDQ 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 159 RPTVEVNG---KKFTAPHILIATGGVPTVPhesQIPG--ASLGITSDGFFQLEDLPSRSVIVGAGYIAVEIAGILSALGS 233
Cdd:PRK13748 218 TLIVRLNDggeRVVAFDRCLIATGASPAVP---PIPGlkETPYWTSTEALVSDTIPERLAVIGSSVVALELAQAFARLGS 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 234 KTSLMIRHDKVLRNfDSLISSNCTEELENAGVEVLKFTQVKEVkkTSSGLELQVVTSVPGRKptttmipdVDCLLWAIGR 313
Cdd:PRK13748 295 KVTILARSTLFFRE-DPAIGEAVTAAFRAEGIEVLEHTQASQV--AHVDGEFVLTTGHGELR--------ADKLLVATGR 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 314 DPNSKGLNLNKVGIQTDEKGHILVDEFQNTNVKGVYAVGDVCGKALLTPVAIAAGRKLAHRLfeCKQDSKLDYDNIPTVV 393
Cdd:PRK13748 364 APNTRSLALDAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQPQFVYVAAAAGTRAAINM--TGGDAALDLTAMPAVV 441
|
410
....*....|....*....
gi 160298213 394 FSHPPIGTVGLTEDEAVHK 412
Cdd:PRK13748 442 FTDPQVATVGYSEAEAHHD 460
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
43-496 |
4.44e-52 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 182.64 E-value: 4.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 43 FDYLVIGGGSGGLASARRAAELGARAAVVESHKL--GGTCVNVGCVPKKVMWNTAVHsefmhdhvDYGFQscegkfswHV 120
Cdd:PRK07251 4 YDLIVIGFGKAGKTLAAKLASAGKKVALVEESKAmyGGTCINIGCIPTKTLLVAAEK--------NLSFE--------QV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 121 IKQKrDAYVSRLNTIYQNNLTKSHIEIIHGYATFADGPrpTVEVNG----KKFTAPHILIATGGVPTVPhesQIPG--AS 194
Cdd:PRK07251 68 MATK-NTVTSRLRGKNYAMLAGSGVDLYDAEAHFVSNK--VIEVQAgdekIELTAETIVINTGAVSNVL---PIPGlaDS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 195 LGI-TSDGFFQLEDLPSRSVIVGAGYIAVEIAGILSALGSKTSLMIRHDKVLRNFDSLISSNCTEELENAGVEVLKFTQV 273
Cdd:PRK07251 142 KHVyDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYMEEDGITFLLNAHT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 274 KEVKKTSSglelQVVTSVPGRKPTttmipdVDCLLWAIGRDPNSKGLNLNKVGIQTDEKGHILVDEFQNTNVKGVYAVGD 353
Cdd:PRK07251 222 TEVKNDGD----QVLVVTEDETYR------FDALLYATGRKPNTEPLGLENTDIELTERGAIKVDDYCQTSVPGVFAVGD 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 354 VCGKALLTPVAIAAGRKLAHRLFECKQDSKLDYDNIPTVVFSHPPIGTVGLTEDEAVHKYGKDNVKIYSTAFTPMYHavT 433
Cdd:PRK07251 292 VNGGPQFTYISLDDFRIVFGYLTGDGSYTLEDRGNVPTTMFITPPLSQVGLTEKEAKEAGLPYAVKELLVAAMPRAH--V 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160298213 434 TRKTKCVMKMVCANKEEKVVGIHMQGIGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEEL 496
Cdd:PRK07251 370 NNDLRGAFKVVVNTETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAENL 432
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
61-409 |
5.54e-49 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 174.57 E-value: 5.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 61 AAELGARAAVVESHK-LGGTCVNVGCVPKKVMWNTAVHSEFMHD---HVDYGFQsceGKFSW--------HVIKQKRDay 128
Cdd:PRK05249 24 AAKLGKRVAVIERYRnVGGGCTHTGTIPSKALREAVLRLIGFNQnplYSSYRVK---LRITFadllaradHVINKQVE-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 129 vsrlntIYQNNLTKSHIEIIHGYATFADgPRpTVEV---NGKK--FTAPHILIATGGVPTVPHESQIPGASLgITSDGFF 203
Cdd:PRK05249 99 ------VRRGQYERNRVDLIQGRARFVD-PH-TVEVecpDGEVetLTADKIVIATGSRPYRPPDVDFDHPRI-YDSDSIL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 204 QLEDLPSRSVIVGAGYIAVEIAGILSALGSKTSLMIRHDKVLRNFDSLISSNCTEELENAGVEVLKFTQVKEVKKTSSGL 283
Cdd:PRK05249 170 SLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSFLDDEISDALSYHLRDSGVTIRHNEEVEKVEGGDDGV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 284 elqVVTSVPGRKPTTtmipdvDCLLWAIGRDPNSKGLNLNKVGIQTDEKGHILVDE-FQnTNVKGVYAVGDVCGKALLTP 362
Cdd:PRK05249 250 ---IVHLKSGKKIKA------DCLLYANGRTGNTDGLNLENAGLEADSRGQLKVNEnYQ-TAVPHIYAVGDVIGFPSLAS 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 160298213 363 VAIAAGRKLAHRLFEckQDSKLDYDNIPTVVFSHPPIGTVGLTEDEA 409
Cdd:PRK05249 320 ASMDQGRIAAQHAVG--EATAHLIEDIPTGIYTIPEISSVGKTEQEL 364
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
62-496 |
2.58e-46 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 167.11 E-value: 2.58e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 62 AELGARAAVVESHK--LGGTCVNVGCVPKKvmwnTAVHSEFMHdhvdygfqsceGKFSwhVIKQKRDAYVSRL-NTIYQN 138
Cdd:PRK08010 23 AKAGWRVALIEQSNamYGGTCINIGCIPTK----TLVHDAQQH-----------TDFV--RAIQRKNEVVNFLrNKNFHN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 139 NLTKSHIEIIHGYATFADG-------PRPTVEVNGKKftaphILIATGG---VPTVPHESQIPGAslgITSDGFFQLEDL 208
Cdd:PRK08010 86 LADMPNIDVIDGQAEFINNhslrvhrPEGNLEIHGEK-----IFINTGAqtvVPPIPGITTTPGV---YDSTGLLNLKEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 209 PSRSVIVGAGYIAVEIAGILSALGSKTSLMIRHDKVLRNFDSLISSNCTEELENAGVEVLKFTQVKEVkktsSGLELQVV 288
Cdd:PRK08010 158 PGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVERI----SHHENQVQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 289 TSVPGRKPTttmipdVDCLLWAIGRDPNSKGLNLNKVGIQTDEKGHILVDEFQNTNVKGVYAVGDVCGKALLTPVAIAAG 368
Cdd:PRK08010 234 VHSEHAQLA------VDALLIASGRQPATASLHPENAGIAVNERGAIVVDKYLHTTADNIWAMGDVTGGLQFTYISLDDY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 369 RKLAHRLFECKQDSKLDYDNIPTVVFSHPPIGTVGLTEDEAvHKYGKDnVKIYSTAFTPMYHAVTTRKTKCVMKMVCANK 448
Cdd:PRK08010 308 RIVRDELLGEGKRSTDDRKNVPYSVFMTPPLSRVGMTEEQA-RESGAD-IQVVTLPVAAIPRARVMNDTRGVLKAIVDNK 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 160298213 449 EEKVVGIHMQGIGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEEL 496
Cdd:PRK08010 386 TQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESL 433
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
389-499 |
1.17e-43 |
|
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: 149.63 E-value: 1.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 389 IPTVVFSHPPIGTVGLTEDEAVHKYGKdnVKIYSTAFTPMYHAVTTRKTKCVMKMVCANKEEKVVGIHMQGIGCDEMLQG 468
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGE--VKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQE 78
|
90 100 110
....*....|....*....|....*....|.
gi 160298213 469 FAVAVKMGATKADFDNTVAIHPTSSEELVTL 499
Cdd:pfam02852 79 AALAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
31-496 |
1.31e-38 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 149.29 E-value: 1.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 31 GEPQPPAPDTSSFDYLVIGGGSGGLASARRAAELGARAAVVESHK--LGGTCVNVGCVPKK-VMWNTAVHSEF--MHDHV 105
Cdd:PTZ00153 105 ATSQSMNFSDEEYDVGIIGCGVGGHAAAINAMERGLKVIIFTGDDdsIGGTCVNVGCIPSKaLLYATGKYRELknLAKLY 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 106 DYGFQSCE--------------------------GKFSWHVIKQKRDAYVSRLNTiYQNNLTKSHIEIIHGYATFADGPR 159
Cdd:PTZ00153 185 TYGIYTNAfkngkndpvernqlvadtvqiditklKEYTQSVIDKLRGGIENGLKS-KKFCKNSEHVQVIYERGHIVDKNT 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 160 PTVEVNGKKFTAPHILIATGGVPTVPHESQIPGASLgITSDGFFQLEDLPSRSVIVGAGYIAVEIAGILSALGSKTSLMI 239
Cdd:PTZ00153 264 IKSEKSGKEFKVKNIIIATGSTPNIPDNIEVDQKSV-FTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFE 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 240 RHDKVLRNFDSLISsNCTEE--LENAGVEVLKFTQVKEVKKTSSGLELQVVTS--------VPGRKPTTTMIPDVDCLLW 309
Cdd:PTZ00153 343 YSPQLLPLLDADVA-KYFERvfLKSKPVRVHLNTLIEYVRAGKGNQPVIIGHSerqtgesdGPKKNMNDIKETYVDSCLV 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 310 AIGRDPNSKGLNLNKVGIQTDeKGHILVDEF------QNTNVKGVYAVGDVCGKALLTPVA----------IAAGRKLAH 373
Cdd:PTZ00153 422 ATGRKPNTNNLGLDKLKIQMK-RGFVSVDEHlrvlreDQEVYDNIFCIGDANGKQMLAHTAshqalkvvdwIEGKGKENV 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 374 RLFECKQDSK-LDYDNIPTVVFSHPPIGTVGLTEDEAVHKYGKDNVKIYSTAFTPMYHAV-------------------- 432
Cdd:PTZ00153 501 NINVENWASKpIIYKNIPSVCYTTPELAFIGLTEKEAKELYPPDNVGVEISFYKANSKVLcennisfpnnsknnsynkgk 580
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160298213 433 --TTRKTKCVMKMVCANKEEKVVGIHMQGIGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEEL 496
Cdd:PTZ00153 581 ynTVDNTEGMVKIVYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVL 646
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
61-408 |
1.03e-35 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 138.45 E-value: 1.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 61 AAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHSEFMHDHVDYGFQSCEGKfSWHVIKQKRDAYVSRLNT-----I 135
Cdd:PRK07845 20 AAQLGADVTVIERDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRFIDDG-EARVDLPAVNARVKALAAaqsadI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 136 yQNNLTKSHIEIIHGYATFAD---GPRpTVEVNG-----KKFTAPHILIATGGVPTVphesqIPGASlgitSDG------ 201
Cdd:PRK07845 99 -RARLEREGVRVIAGRGRLIDpglGPH-RVKVTTadggeETLDADVVLIATGASPRI-----LPTAE----PDGeriltw 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 202 --FFQLEDLPSRSVIVGAGYIAVEIAGILSALGSKTSLMIRHDKVLRNFDSLISSNCTEELENAGVEVLKFTQVKEVKKT 279
Cdd:PRK07845 168 rqLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPGEDADAAEVLEEVFARRGMTVLKRSRAESVERT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 280 SSGLelqVVTSVPGRKPTTTmipdvDCLLwAIGRDPNSKGLNLNKVGIQTDEKGHILVDEFQNTNVKGVYAVGDVCGKAL 359
Cdd:PRK07845 248 GDGV---VVTLTDGRTVEGS-----HALM-AVGSVPNTAGLGLEEAGVELTPSGHITVDRVSRTSVPGIYAAGDCTGVLP 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 160298213 360 LTPVAIAAGR-KLAHRLFECKQDSKLdyDNIPTVVFSHPPIGTVGLTEDE 408
Cdd:PRK07845 319 LASVAAMQGRiAMYHALGEAVSPLRL--KTVASNVFTRPEIATVGVSQAA 366
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
161-375 |
8.05e-24 |
|
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: 101.81 E-value: 8.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 161 TVEV-NGKKFTAPHILIATGGVPTVPhesQIPGASL-GITSDGFFQ--------LEDLPSRS-VIVGAGYIAVEIAGILS 229
Cdd:COG0446 68 TVTLrDGETLSYDKLVLATGARPRPP---PIPGLDLpGVFTLRTLDdadalreaLKEFKGKRaVVIGGGPIGLELAEALR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 230 ALGSKTSLMIRHDKVLRNFDSLISSNCTEELENAGVEVLKFTQVKEVKKTSSglelQVVTSVPGRKptttmIPdVDCLLW 309
Cdd:COG0446 145 KRGLKVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAIDGDDK----VAVTLTDGEE-----IP-ADLVVV 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160298213 310 AIGRDPNSKgLnLNKVGIQTDEKGHILVDEFQNTNVKGVYAVGDVC-------GKALLTPVAIAA---GRKLAHRL 375
Cdd:COG0446 215 APGVRPNTE-L-AKDAGLALGERGWIKVDETLQTSDPDVYAAGDCAevphpvtGKTVYIPLASAAnkqGRVAAENI 288
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
145-368 |
4.10e-23 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 99.42 E-value: 4.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 145 IEIIHGYAT---FADGPRpTVEV-NGKKFTAPHILIATGGVPT---VPHESQIPGASL--GITSDGFFqledLPSRSV-I 214
Cdd:COG0492 72 AEILLEEVTsvdKDDGPF-RVTTdDGTEYEAKAVIIATGAGPRklgLPGEEEFEGRGVsyCATCDGFF----FRGKDVvV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 215 VGAGYIAVEIAGILSALGSKTSLMIRHDKvLRNFDSLIssnctEEL-ENAGVEVLKFTQVKEVKKTSSGLELQVVTSVPG 293
Cdd:COG0492 147 VGGGDSALEEALYLTKFASKVTLIHRRDE-LRASKILV-----ERLrANPKIEVLWNTEVTEIEGDGRVEGVTLKNVKTG 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160298213 294 rkpTTTMIPdVDCLLWAIGRDPNSkGLnLNKVGIQTDEKGHILVDEFQNTNVKGVYAVGDVCGKALLTpVAIAAG 368
Cdd:COG0492 221 ---EEKELE-VDGVFVAIGLKPNT-EL-LKGLGLELDEDGYIVVDEDMETSVPGVFAAGDVRDYKYRQ-AATAAG 288
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
211-287 |
5.45e-20 |
|
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: 84.18 E-value: 5.45e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160298213 211 RSVIVGAGYIAVEIAGILSALGSKTSLMIRHDKVLRNFDSLISSNCTEELENAGVEVLKFTQVKEVKKTSSGLELQV 287
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVL 77
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
165-375 |
1.10e-17 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 84.81 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 165 NGKKFTAPHILIATGGVPTVPhesQIPGASLgitsDGFF---QLEDL---------PSRSVIVGAGYIAVEIAGILSALG 232
Cdd:COG1251 93 DGETLPYDKLVLATGSRPRVP---PIPGADL----PGVFtlrTLDDAdalraalapGKRVVVIGGGLIGLEAAAALRKRG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 233 SKTSLMIRHDKVL-RNFDSLISSNCTEELENAGVEVLKFTQVKEVKKTSSGLElqVVTSvPGRKptttmIPdVDCLLWAI 311
Cdd:COG1251 166 LEVTVVERAPRLLpRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTG--VRLA-DGEE-----LP-ADLVVVAI 236
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160298213 312 GRDPNSkGLnLNKVGIQTDeKGhILVDEFQNTNVKGVYAVGDVC-------GKAL--LTPVAIAAGRKLAHRL 375
Cdd:COG1251 237 GVRPNT-EL-ARAAGLAVD-RG-IVVDDYLRTSDPDIYAAGDCAehpgpvyGRRVleLVAPAYEQARVAAANL 305
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
140-375 |
1.04e-13 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 72.47 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 140 LTKSHIEIIHGYATFADGPRPTVEV-NGKKFTAPHILIATGGVPTVPHesqIPGA---SLGI-TSDGFF----QLEDLPS 210
Cdd:COG1252 66 LRRAGVRFIQGEVTGIDPEARTVTLaDGRTLSYDYLVIATGSVTNFFG---IPGLaehALPLkTLEDALalreRLLAAFE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 211 RS--------VIVGAGYIAVEIAGILSAL-----------GSKTSLMI--RHDKVLRNFDSLISSNCTEELENAGVEVLK 269
Cdd:COG1252 143 RAerrrlltiVVVGGGPTGVELAGELAELlrkllrypgidPDKVRITLveAGPRILPGLGEKLSEAAEKELEKRGVEVHT 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 270 FTQVKEVKK----TSSGLELqvvtsvpgrkptttmipDVDCLLWAIGRDPNSKglnLNKVGIQTDEKGHILVDEF-QNTN 344
Cdd:COG1252 223 GTRVTEVDAdgvtLEDGEEI-----------------PADTVIWAAGVKAPPL---LADLGLPTDRRGRVLVDPTlQVPG 282
|
250 260 270
....*....|....*....|....*....|....*....
gi 160298213 345 VKGVYAVGDVC-----GKALLTPVAIAA---GRKLAHRL 375
Cdd:COG1252 283 HPNVFAIGDCAavpdpDGKPVPKTAQAAvqqAKVLAKNI 321
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
165-375 |
1.15e-13 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 72.77 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 165 NGKKFTAPH--ILIATGGVPTVPhesQIPGaslgITSDGFFQLEDLP--------------SRSVIVGAGYIAVEIAGIL 228
Cdd:PRK09564 96 TGSIFNDTYdkLMIATGARPIIP---PIKN----INLENVYTLKSMEdglalkellkdeeiKNIVIIGAGFIGLEAVEAA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 229 SALGSKTSLMIRHDKVL-RNFDSLISSNCTEELENAGVEVlkftqvkevkKTSsglelQVVTSVPGRKPTTTMIPD---- 303
Cdd:PRK09564 169 KHLGKNVRIIQLEDRILpDSFDKEITDVMEEELRENGVEL----------HLN-----EFVKSLIGEDKVEGVVTDkgey 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 304 -VDCLLWAIGRDPNSKGLNlnKVGIQTDEKGHILVDEFQNTNVKGVYAVGD-------VCGKALLTPVAIAA---GRKLA 372
Cdd:PRK09564 234 eADVVIVATGVKPNTEFLE--DTGLKTLKNGAIIVDEYGETSIENIYAAGDcatiyniVSNKNVYVPLATTAnklGRMVG 311
|
...
gi 160298213 373 HRL 375
Cdd:PRK09564 312 ENL 314
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
191-374 |
6.20e-12 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 67.50 E-value: 6.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 191 PGAS---LGITSDGFFQLEDLP--------------SRSVIVGAGYIAVEIAGILSALGSKTSLMIRHDKVLRNFDSLIS 253
Cdd:PRK13512 113 PGASansLGFESDITFTLRNLEdtdaidqfikanqvDKALVVGAGYISLEVLENLYERGLHPTLIHRSDKINKLMDADMN 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 254 SNCTEELENAGVEvLKFTQvkEVKKTSSglelQVVTSVPGRkptttmIPDVDCLLWAIGRDPNSKglNLNKVGIQTDEKG 333
Cdd:PRK13512 193 QPILDELDKREIP-YRLNE--EIDAING----NEVTFKSGK------VEHYDMIIEGVGTHPNSK--FIESSNIKLDDKG 257
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 160298213 334 HILVDEFQNTNVKGVYAVGDVCGKA-----LLTPVAIAAGrklAHR 374
Cdd:PRK13512 258 FIPVNDKFETNVPNIYAIGDIITSHyrhvdLPASVPLAWG---AHR 300
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
258-373 |
3.89e-11 |
|
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: 64.77 E-value: 3.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 258 EELENA---GVEVLKFTQVKEVKKTS----SGLELQVVTSVPG-----RKP-----TTTMIPdVDCLLWAIGRDPNSKGL 320
Cdd:COG0493 298 EEVEEAleeGVEFLFLVAPVEIIGDEngrvTGLECVRMELGEPdesgrRRPvpiegSEFTLP-ADLVILAIGQTPDPSGL 376
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 160298213 321 nLNKVGIQTDEKGHILVDEF-QNTNVKGVYAVGDVCGKALLTPVAIAAGRKLAH 373
Cdd:COG0493 377 -EEELGLELDKRGTIVVDEEtYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAAR 429
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
119-367 |
5.29e-11 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 64.17 E-value: 5.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 119 HVIKQKRDAyvsrlntiyqNNLTKS---------HIEII-HGYATFADGPRPTVEVNGKKFTAPHILIATGGVPTVPhes 188
Cdd:PRK04965 48 HVFSQGQRA----------DDLTRQsagefaeqfNLRLFpHTWVTDIDAEAQVVKSQGNQWQYDKLVLATGASAFVP--- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 189 QIPGASLGIT--SDGFFQLEDLP---SRSV-IVGAGYIAVEIAGILSALGSKTSLMIRHDKVLRNF-DSLISSNCTEELE 261
Cdd:PRK04965 115 PIPGRELMLTlnSQQEYRAAETQlrdAQRVlVVGGGLIGTELAMDLCRAGKAVTLVDNAASLLASLmPPEVSSRLQHRLT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 262 NAGVEVLKFTQVKEVKKTSSGLelqVVTSVPGRKPTttmipdVDCLLWAIGRDPNSK-----GLNLNKvGIQtdekghil 336
Cdd:PRK04965 195 EMGVHLLLKSQLQGLEKTDSGI---RATLDSGRSIE------VDAVIAAAGLRPNTAlarraGLAVNR-GIV-------- 256
|
250 260 270
....*....|....*....|....*....|....*..
gi 160298213 337 VDEFQNTNVKGVYAVGDvC----GKAL--LTPVAIAA 367
Cdd:PRK04965 257 VDSYLQTSAPDIYALGD-CaeinGQVLpfLQPIQLSA 292
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
167-359 |
5.37e-10 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 60.77 E-value: 5.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 167 KKFTAphILIATGGvpTVPHESQIPGASL-GITS--DGFF-----QLEDLPS---------RSVIVGAGYIAVEIAGILS 229
Cdd:PRK12770 117 KKYDA--VLIATGT--WKSRKLGIPGEDLpGVYSalEYLFriraaKLGYLPWekvppvegkKVVVVGAGLTAVDAALEAV 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 230 ALGSKTSLMIrHDKVLRnfDSLISSNCTEELENAGVEVLKFTQVKEV--KKTSSGLELQVVTSVPGRK---PTTTMIP-- 302
Cdd:PRK12770 193 LLGAEKVYLA-YRRTIN--EAPAGKYEIERLIARGVEFLELVTPVRIigEGRVEGVELAKMRLGEPDEsgrPRPVPIPgs 269
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160298213 303 ----DVDCLLWAIGRDPNSKGlNLNKVGIQTDEKGHILVDEFQNTNVKGVYAVGDVC------GKAL 359
Cdd:PRK12770 270 efvlEADTVVFAIGEIPTPPF-AKECLGIELNRKGEIVVDEKHMTSREGVFAAGDVVtgpskiGKAI 335
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
174-373 |
3.77e-09 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 58.65 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 174 ILIATG--GVPTVPhesqIPGASLG--------ITS----DGFFQLEdLPSRSVIVGAGYIAVEIAGILSALGSK-TSLM 238
Cdd:PRK11749 229 VFIGTGagLPRFLG----IPGENLGgvysavdfLTRvnqaVADYDLP-VGKRVVVIGGGNTAMDAARTAKRLGAEsVTIV 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 239 IRhdkvlRNFDSLISSNctEELENA---GVEVLKFTQVKEV---KKTSSGLELQVVTSVPGRKPTTTMIP--------DV 304
Cdd:PRK11749 304 YR-----RGREEMPASE--EEVEHAkeeGVEFEWLAAPVEIlgdEGRVTGVEFVRMELGEPDASGRRRVPiegseftlPA 376
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 305 DCLLWAIGRDPNSKGLNLNKvGIQTDEKGHILVDEFQ-NTNVKGVYAVGDVCGKALLTPVAIAAGRKLAH 373
Cdd:PRK11749 377 DLVIKAIGQTPNPLILSTTP-GLELNRWGTIIADDETgRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAE 445
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
161-352 |
4.46e-08 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 54.54 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 161 TVEVNGKKFTAPHILIATG--------GVP-TVPHESQIPGAslgitSDGFFQledlpsRSVIVGAGYIAVEIAGILSAL 231
Cdd:pfam13738 109 VVTTSKGTYQARYVIIATGefdfpnklGVPeLPKHYSYVKDF-----HPYAGQ------KVVVIGGYNSAVDAALELVRK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 232 GSKTSLMIRHDkVLRNFDSLIS---SNCTEE-----LENAGVEVLKFTQVKEVKKTSSGLelqVVTSVPGRKPTTTMIPd 303
Cdd:pfam13738 178 GARVTVLYRGS-EWEDRDSDPSyslSPDTLNrleelVKNGKIKAHFNAEVKEITEVDVSY---KVHTEDGRKVTSNDDP- 252
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 160298213 304 vdclLWAIGRDPNSKglNLNKVGIQTDEKGHILVDEF-QNTNVKGVYAVG 352
Cdd:pfam13738 253 ----ILATGYHPDLS--FLKKGLFELDEDGRPVLTEEtESTNVPGLFLAG 296
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
163-372 |
5.84e-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: 5.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 163 EVNGKKFTAphILIATG-GVPTVPHesqIPGASL-GITS-----------DGFFQLEDLP----SRSVIVGAGYIAVEIA 225
Cdd:PRK12778 512 ELEEEGFKG--IFIASGaGLPNFMN---IPGENSnGVMSsneyltrvnlmDAASPDSDTPikfgKKVAVVGGGNTAMDSA 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 226 GILSALGSKTSLMIRHdkvlRNFDSLISSncTEELENA---GVEVLKFTQVKEVKKTSSGLELQVVTSV--------PGR 294
Cdd:PRK12778 587 RTAKRLGAERVTIVYR----RSEEEMPAR--LEEVKHAkeeGIEFLTLHNPIEYLADEKGWVKQVVLQKmelgepdaSGR 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 295 K-----PTTTMIPDVDCLLWAIGRDPN------SKGLNLNKvgiqtdeKGHILVDEFQNTNVKGVYAVGDVCGKALLTPV 363
Cdd:PRK12778 661 RrpvaiPGSTFTVDVDLVIVSVGVSPNplvpssIPGLELNR-------KGTIVVDEEMQSSIPGIYAGGDIVRGGATVIL 733
|
....*....
gi 160298213 364 AIAAGRKLA 372
Cdd:PRK12778 734 AMGDGKRAA 742
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
161-372 |
2.05e-06 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 50.71 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 161 TVEVNGKKFTAPHILIATG----------GVPT---VPHE--SQIPGASLGITSDGF-----FQLEDLP---SRSVIV-G 216
Cdd:PRK12775 499 TNKVIGKTFTVPQLMNDKGfdavflgvgaGAPTflgIPGEfaGQVYSANEFLTRVNLmggdkFPFLDTPislGKSVVViG 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 217 AGYIAVEIAGILSALGSKTslmIRHdkVLRNFDSLISSNcTEELENA---GVEVLKFTQVKEVKKTSSG---------LE 284
Cdd:PRK12775 579 AGNTAMDCLRVAKRLGAPT---VRC--VYRRSEAEAPAR-IEEIRHAkeeGIDFFFLHSPVEIYVDAEGsvrgmkveeME 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 285 LQVVTSVPGRKPTTT-MIPDVDC--LLWAIGRDPN------SKGLNLNKVG-IQTDEKGhilVDEFQNTNVKGVYAVGDV 354
Cdd:PRK12775 653 LGEPDEKGRRKPMPTgEFKDLECdtVIYALGTKANpiitqsTPGLALNKWGnIAADDGK---LESTQSTNLPGVFAGGDI 729
|
250
....*....|....*...
gi 160298213 355 CGKALLTPVAIAAGRKLA 372
Cdd:PRK12775 730 VTGGATVILAMGAGRRAA 747
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
211-372 |
9.48e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 48.09 E-value: 9.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 211 RSVIVGAGYIAVEIAGILSALGSKTSLMIRhdkvlRNFDSLISSncTEELENA---GVEVLKFTQVKEVKKTSSG----- 282
Cdd:PRK12831 283 KVAVVGGGNVAMDAARTALRLGAEVHIVYR-----RSEEELPAR--VEEVHHAkeeGVIFDLLTNPVEILGDENGwvkgm 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 283 ----LELQVVTSVPGRKPT----TTMIPDVDCLLWAIGRDPNSKGLNLNKvGIQTDEKGHILVDEFQN-TNVKGVYAVGD 353
Cdd:PRK12831 356 kcikMELGEPDASGRRRPVeiegSEFVLEVDTVIMSLGTSPNPLISSTTK-GLKINKRGCIVADEETGlTSKEGVFAGGD 434
|
170 180
....*....|....*....|
gi 160298213 354 -VCGKALLTpVAIAAGRKLA 372
Cdd:PRK12831 435 aVTGAATVI-LAMGAGKKAA 453
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
211-355 |
2.18e-05 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 46.84 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 211 RSVIVGAGYIAVEIAGILSALGSKTSLMIRHDKVL-RNFDSLISSNCTEELENAGVEVLKFTQVKEVKKTSSgLELQVVT 289
Cdd:PRK09754 146 SVVIVGAGTIGLELAASATQRRCKVTVIELAATVMgRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEK-VELTLQS 224
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160298213 290 SvpgrkptTTMIPDVdcLLWAIG---RDPNSKGLNLnkvgiqtDEKGHILVDEFQNTNVKGVYAVGDVC 355
Cdd:PRK09754 225 G-------ETLQADV--VIYGIGisaNDQLAREANL-------DTANGIVIDEACRTCDPAIFAGGDVA 277
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
213-383 |
5.37e-05 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 45.53 E-value: 5.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 213 VIVGAGYIAVEIAGILSALGSKTSLMIRHD--------------KVLRNFDSLISSNCTEELENAGVEVLKFTQVKEVKK 278
Cdd:PTZ00318 177 VVVGGGPTGVEFAAELADFFRDDVRNLNPElveeckvtvleagsEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEVLD 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 279 TssglelQVVTSVPGRKPTTTMIpdvdcllWA--IGRDPNSKGLNLNKvgiqtDEKGHILVDE-FQNTNVKGVYAVGDVC 355
Cdd:PTZ00318 257 K------EVVLKDGEVIPTGLVV-------WStgVGPGPLTKQLKVDK-----TSRGRISVDDhLRVKPIPNVFALGDCA 318
|
170 180 190
....*....|....*....|....*....|....*.
gi 160298213 356 G---KALLTPVAIAA--GRKLAHR---LFECKQDSK 383
Cdd:PTZ00318 319 AneeRPLPTLAQVASqqGVYLAKEfnnELKGKPMSK 354
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
254-373 |
2.29e-04 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 43.61 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 254 SNCTEElenaGVEVLKFTQVKEVKKTS---SGLEL-QVVTSVPGRKP---TTTMIPdVDCLLWAIGRDPNSKGLnLNKVG 326
Cdd:PRK12810 337 SNAHEE----GVEREFNVQTKEFEGENgkvTGVKVvRTELGEGDFEPvegSEFVLP-ADLVLLAMGFTGPEAGL-LAQFG 410
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 160298213 327 IQTDEKGHILVDE--FQnTNVKGVYAVGDVCGKALLTPVAIAAGRKLAH 373
Cdd:PRK12810 411 VELDERGRVAAPDnaYQ-TSNPKVFAAGDMRRGQSLVVWAIAEGRQAAR 458
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
168-354 |
6.54e-03 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 38.89 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 168 KFTAPHILIATGGVPT---VPHESQIPG--ASLGITSDGFFQLEdlpSRSVIVGAGYIAVEIAGILSALGSKTSLMIRHD 242
Cdd:PRK10262 103 EYTCDALIIATGASARylgLPSEEAFKGrgVSACATCDGFFYRN---QKVAVIGGGNTAVEEALYLSNIASEVHLIHRRD 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298213 243 KVlrNFDSLISSNCTEELENAGVEVLKFTQVKEVKKTSSGLE-LQVVTSvpgRKPTTTMIPDVDCLLWAIGRDPNSKGLN 321
Cdd:PRK10262 180 GF--RAEKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTgVRLRDT---QNSDNIESLDVAGLFVAIGHSPNTAIFE 254
|
170 180 190
....*....|....*....|....*....|....*...
gi 160298213 322 lnkvGIQTDEKGHILVDE-----FQNTNVKGVYAVGDV 354
Cdd:PRK10262 255 ----GQLELENGYIKVQSgihgnATQTSIPGVFAAGDV 288
|
|
| |
