|
Name |
Accession |
Description |
Interval |
E-value |
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
1-277 |
6.25e-128 |
|
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: 372.26 E-value: 6.25e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 1 MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLpDGQLQVTWEDSTTGKEdtGTFDTVLWAIGRVPDTRSLNL 80
Cdd:TIGR01438 210 VRSILLRGFDQDCANKVGEHMEEHGVKFKRQFVPIKVEQI-EAKVLVEFTDSTNGIE--EEYDTVLLAIGRDACTRKLNL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 81 EKAGVDTSPDTQKILVDSREATSVPHIYAIGDVVEGRPELTPTAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGC 160
Cdd:TIGR01438 287 ENVGVKINKKTGKIPADEEEQTNVPYIYAVGDILEDKPELTPVAIQAGRLLAQRLFKGSTVICDYENVPTTVFTPLEYGA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 161 VGLSEEEAVARHGQEHVEVYHAHYKPLEFTVAGRD-ASQCYVKMVCLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGAS 239
Cdd:TIGR01438 367 CGLSEEKAVEKFGEENVEVFHSYFWPLEWTIPSRDnHNKCYAKLVCNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLT 446
|
250 260 270
....*....|....*....|....*....|....*...
gi 6649223 240 YAQVMRTVGIHPTCSEEVVKLRISKRSGLDPTVTGCUG 277
Cdd:TIGR01438 447 KKDLDNTIGIHPVCAEVFTTLSVTKRSGQDILQQGCCG 484
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
1-277 |
7.48e-94 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 285.56 E-value: 7.48e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 1 MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDgQLQVTWEDSTTGKedtgtFDTVLWAIGRVPDTRSLNL 80
Cdd:PTZ00052 212 VRSIPLRGFDRQCSEKVVEYMKEQGTLFLEGVVPINIEKMDD-KIKVLFSDGTTEL-----FDTVLYATGRKPDIKGLNL 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 81 EKAGVDTSPDTQKILVDsrEATSVPHIYAIGDVVEGRPELTPTAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGC 160
Cdd:PTZ00052 286 NAIGVHVNKSNKIIAPN--DCTNIPNIFAVGDVVEGRPELTPVAIKAGILLARRLFKQSNEFIDYTFIPTTIFTPIEYGA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 161 VGLSEEEAVARHGQEHVEVYHAHYKPLEFTVAGRD--------------ASQCYVKMVCLREPPQLVLGLHFLGPNAGEV 226
Cdd:PTZ00052 364 CGYSSEAAIAKYGEDDIEEYLQEFNTLEIAAVHREkherarkdeydfdvSSNCLAKLVCVKSEDNKVVGFHFVGPNAGEI 443
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 6649223 227 TQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKLRISKRSGLDPTVTGCUG 277
Cdd:PTZ00052 444 TQGFSLALKLGAKKSDFDSMIGIHPTDAEVFMNLSVTRRSGESFAAKGGCG 494
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
5-261 |
2.62e-85 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 262.01 E-value: 2.62e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 5 PLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVTWEDsttGKEDTgtFDTVLWAIGRVPDTRSLNLEKAG 84
Cdd:PRK06116 202 PLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADGSLTLTLED---GETLT--VDCLIWAIGREPNTDGLGLENAG 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 85 VDTSpDTQKILVDSREATSVPHIYAIGDVvEGRPELTPTAIMAGRLLVQRLFGGSSDL-MDYDNVPTTVFTPLEYGCVGL 163
Cdd:PRK06116 277 VKLN-EKGYIIVDEYQNTNVPGIYAVGDV-TGRVELTPVAIAAGRRLSERLFNNKPDEkLDYSNIPTVVFSHPPIGTVGL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 164 SEEEAVARHGQEHVEVYHAHYKPLEFTVAGRDAsQCYVKMVCLREPPQlVLGLHFLGPNAGEVTQGFALGIKCGASYAQV 243
Cdd:PRK06116 355 TEEEAREQYGEDNVKVYRSSFTPMYTALTGHRQ-PCLMKLVVVGKEEK-VVGLHGIGFGADEMIQGFAVAIKMGATKADF 432
|
250
....*....|....*...
gi 6649223 244 MRTVGIHPTCSEEVVKLR 261
Cdd:PRK06116 433 DNTVAIHPTAAEEFVTMR 450
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
5-258 |
3.04e-68 |
|
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: 218.03 E-value: 3.04e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 5 PLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGqLQVTWEDSttGKEDTGTFDTVLWAIGRVPDTRSLNLEKAG 84
Cdd:COG1249 203 LLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDG-VTVTLEDG--GGEEAVEADKVLVATGRRPNTDGLGLEAAG 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 85 VDTSPDTQkILVDSREATSVPHIYAIGDVVeGRPELTPTAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLS 164
Cdd:COG1249 280 VELDERGG-IKVDEYLRTSVPGIYAIGDVT-GGPQLAHVASAEGRVAAENILGKKPRPVDYRAIPSVVFTDPEIASVGLT 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 165 EEEAVARHGQehVEVYHAHYKPLEFTVAGRDAsQCYVKMVCLREpPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVM 244
Cdd:COG1249 358 EEEAREAGID--VKVGKFPFAANGRALALGET-EGFVKLIADAE-TGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLA 433
|
250
....*....|....
gi 6649223 245 RTVGIHPTCSEEVV 258
Cdd:COG1249 434 DTIHAHPTLSEALK 447
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
6-265 |
1.30e-52 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 179.69 E-value: 1.30e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 6 LRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVTwedstTGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGV 85
Cdd:PLN02546 288 LRGFDEEVRDFVAEQMSLRGIEFHTEESPQAIIKSADGSLSLK-----TNKGTVEGFSHVMFATGRKPNTKNLGLEEVGV 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 86 DTSpDTQKILVDSREATSVPHIYAIGDVVEgRPELTPTAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSE 165
Cdd:PLN02546 363 KMD-KNGAIEVDEYSRTSVPSIWAVGDVTD-RINLTPVALMEGGALAKTLFGNEPTKPDYRAVPSAVFSQPPIGQVGLTE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 166 EEAVARHGQehVEVYHAHYKPLEFTVAGRDASQCYVKMVCLREppQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMR 245
Cdd:PLN02546 441 EQAIEEYGD--VDVFTANFRPLKATLSGLPDRVFMKLIVCAKT--NKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDA 516
|
250 260
....*....|....*....|
gi 6649223 246 TVGIHPTCSEEVVKLRISKR 265
Cdd:PLN02546 517 TVGIHPTAAEEFVTMRTPTR 536
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
2-265 |
6.60e-51 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 174.23 E-value: 6.60e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 2 RSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGqLQVTwedSTTGKEDTGtfDTVLWAIGRVPDTRSLNLE 81
Cdd:PLN02507 235 KELPLRGFDDEMRAVVARNLEGRGINLHPRTNLTQLTKTEGG-IKVI---TDHGEEFVA--DVVLFATGRAPNTKRLNLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 82 KAGVDTSpDTQKILVDSREATSVPHIYAIGDVVEgRPELTPTAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCV 161
Cdd:PLN02507 309 AVGVELD-KAGAVKVDEYSRTNIPSIWAIGDVTN-RINLTPVALMEGTCFAKTVFGGQPTKPDYENVACAVFCIPPLSVV 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 162 GLSEEEAVARHGQEhVEVYHAHYKPLEFTVAGRDaSQCYVKMVCLREPPQlVLGLHFLGPNAGEVTQGFALGIKCGASYA 241
Cdd:PLN02507 387 GLSEEEAVEQAKGD-ILVFTSSFNPMKNTISGRQ-EKTVMKLIVDAETDK-VLGASMCGPDAPEIMQGIAVALKCGATKA 463
|
250 260
....*....|....*....|....
gi 6649223 242 QVMRTVGIHPTCSEEVVKLRISKR 265
Cdd:PLN02507 464 QFDSTVGIHPSAAEEFVTMRSVTR 487
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
6-260 |
8.24e-49 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 169.80 E-value: 8.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 6 LRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVTWEDSttGKEDTgtFDTVLWAIGRVPDTRSLNLEKAGV 85
Cdd:PTZ00058 273 LRKFDETIINELENDMKKNNINIITHANVEEIEKVKEKNLTIYLSDG--RKYEH--FDYVIYCVGRSPNTEDLNLKALNI 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 86 DTSPDTqkILVDSREATSVPHIYAIGDVVEGRP---------------------------------ELTPTAIMAGRLLV 132
Cdd:PTZ00058 349 KTPKGY--IKVDDNQRTSVKHIYAVGDCCMVKKnqeiedlnllklyneepylkkkentsgesyynvQLTPVAINAGRLLA 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 133 QRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKPLEFTVAGRDASQ---CYVKMVCLrEP 209
Cdd:PTZ00058 427 DRLFGPFSRTTNYKLIPSVIFSHPPIGTIGLSEQEAIDIYGKENVKIYESRFTNLFFSVYDMDPAQkekTYLKLVCV-GK 505
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 6649223 210 PQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKL 260
Cdd:PTZ00058 506 EELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIHPTAAEEFVTM 556
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
6-261 |
3.36e-45 |
|
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: 158.60 E-value: 3.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 6 LRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVTWEdstTGKedTGTFDTVLWAIGRVPDTRSLNLEKAGV 85
Cdd:TIGR01423 226 LRGFDSTLRKELTKQLRANGINIMTNENPAKVTLNADGSKHVTFE---SGK--TLDVDVVMMAIGRVPRTQTLQLDKVGV 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 86 DTSPDTqKILVDSREATSVPHIYAIGDVVeGRPELTPTAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSE 165
Cdd:TIGR01423 301 ELTKKG-AIQVDEFSRTNVPNIYAIGDVT-DRVMLTPVAINEGAAFVDTVFGNKPRKTDHTRVASAVFSIPPIGTCGLVE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 166 EEAVARHgqEHVEVYHAHYKPLEFTVAGRDASQCYVKMVClREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMR 245
Cdd:TIGR01423 379 EDAAKKF--EKVAVYESSFTPLMHNISGSKYKKFVAKIVT-NHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYN 455
|
250
....*....|....*.
gi 6649223 246 TVGIHPTCSEEVVKLR 261
Cdd:TIGR01423 456 TIGVHPTSAEELCSMR 471
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
6-260 |
1.86e-38 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 140.34 E-value: 1.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 6 LRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGqlqVTWEDSTTGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGV 85
Cdd:PRK06370 207 LPREDEDVAAAVREILEREGIDVRLNAECIRVERDGDG---IAVGLDCNGGAPEITGSHILVAVGRVPNTDDLGLEAAGV 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 86 DTSPDTQkILVDSREATSVPHIYAIGDvVEGRPELTPTAIMAGRLLVQRLFGGS----SDLmdydNVPTTVFTPLEYGCV 161
Cdd:PRK06370 284 ETDARGY-IKVDDQLRTTNPGIYAAGD-CNGRGAFTHTAYNDARIVAANLLDGGrrkvSDR----IVPYATYTDPPLARV 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 162 GLSEEEAVARhGQEhVEVYHahykpLEFTVAGR----DASQCYVKMVcLREPPQLVLGLHFLGPNAGEVTQGFALGIKCG 237
Cdd:PRK06370 358 GMTEAEARKS-GRR-VLVGT-----RPMTRVGRavekGETQGFMKVV-VDADTDRILGATILGVHGDEMIHEILDAMYAG 429
|
250 260
....*....|....*....|...
gi 6649223 238 ASYAQVMRTVGIHPTCSEEVVKL 260
Cdd:PRK06370 430 APYTTLSRAIHIHPTVSELIPTL 452
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
148-260 |
2.51e-38 |
|
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: 130.37 E-value: 2.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 148 VPTTVFTPLEYGCVGLSEEEAVARHGQehVEVYHAHYKPLEFTVAGRDASqCYVKMVCLREPpQLVLGLHFLGPNAGEVT 227
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGE--VKVGKFPFAANGRALAYGDTD-GFVKLVADRET-GKILGAHIVGPNAGELI 76
|
90 100 110
....*....|....*....|....*....|...
gi 6649223 228 QGFALGIKCGASYAQVMRTVGIHPTCSEEVVKL 260
Cdd:pfam02852 77 QEAALAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
8-255 |
2.39e-37 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 137.20 E-value: 2.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 8 GFDQQMSSMVIEHMASHGTRFLRGcapSRVRRLPDGQLQVTWEDSTTGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDT 87
Cdd:PRK06416 210 GEDKEISKLAERALKKRGIKIKTG---AKAKKVEQTDDGVTVTLEDGGKEETLEADYVLVAVGRRPNTENLGLEELGVKT 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 88 spDTQKILVDSREATSVPHIYAIGDVVEGrPELTPTAIMAGRLLVQRLFGGSSDlMDYDNVPTTVFTPLEYGCVGLSEEE 167
Cdd:PRK06416 287 --DRGFIEVDEQLRTNVPNIYAIGDIVGG-PMLAHKASAEGIIAAEAIAGNPHP-IDYRGIPAVTYTHPEVASVGLTEAK 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 168 AVARHGQehVEVYhahykplEFTVAGR------DASQCYVKMVcLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYA 241
Cdd:PRK06416 363 AKEEGFD--VKVV-------KFPFAGNgkalalGETDGFVKLI-FDKKDGEVLGAHMVGARASELIQEAQLAINWEATPE 432
|
250
....*....|....
gi 6649223 242 QVMRTVGIHPTCSE 255
Cdd:PRK06416 433 DLALTIHPHPTLSE 446
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
6-255 |
8.96e-37 |
|
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: 135.46 E-value: 8.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 6 LRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDgqlQVTWEDSTtGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGV 85
Cdd:TIGR01350 206 LPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEKNDD---QVTYENKG-GETETLTGEKVLVAVGRKPNTEGLGLEKLGV 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 86 DTSPDtQKILVDSREATSVPHIYAIGDVVEGrPELTPTAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSE 165
Cdd:TIGR01350 282 ELDER-GRIVVDEYMRTNVPGIYAIGDVIGG-PMLAHVASHEGIVAAENIAGKEPAHIDYDAVPSVIYTDPEVASVGLTE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 166 EEAVARHGqehvevyhaHYKPLEFTVA--GR----DASQCYVKMVCLREpPQLVLGLHFLGPNAGEVTQGFALGIKCGAS 239
Cdd:TIGR01350 360 EQAKEAGY---------DVKIGKFPFAanGKalalGETDGFVKIIADKK-TGEILGAHIIGPHATELISEAALAMELEGT 429
|
250
....*....|....*.
gi 6649223 240 YAQVMRTVGIHPTCSE 255
Cdd:TIGR01350 430 VEELARTIHPHPTLSE 445
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
6-277 |
1.26e-32 |
|
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: 124.46 E-value: 1.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 6 LRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVTwedSTTGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGV 85
Cdd:TIGR02053 202 LPREEPEISAAVEEALAEEGIEVVTSAQVKAVSVRGGGKIITV---EKPGGQGEVEADELLVATGRRPNTDGLGLEKAGV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 86 DTSPDTQkILVDSREATSVPHIYAIGDVVeGRPELTPTAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSE 165
Cdd:TIGR02053 279 KLDERGG-ILVDETLRTSNPGIYAAGDVT-GGLQLEYVAAKEGVVAAENALGGANAKLDLLVIPRVVFTDPAVASVGLTE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 166 EEAvarhgQEHVEVYHAHYKPLEFTVAGR--DASQCYVKMVCLREPPQlVLGLHFLGPNAGEVTQGFALGIKCGASYAQV 243
Cdd:TIGR02053 357 AEA-----QKAGIECDCRTLPLTNVPRARinRDTRGFIKLVAEPGTGK-VLGVQVVAPEAAEVINEAALAIRAGMTVDDL 430
|
250 260 270
....*....|....*....|....*....|....*
gi 6649223 244 MRTVGIHPTCSEevvKLRISKRSGL-DPTVTGCUG 277
Cdd:TIGR02053 431 IDTLHPFPTMAE---GLKLAAQTFYrDVSKLSCCA 462
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
6-259 |
5.92e-31 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 119.90 E-value: 5.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 6 LRGFDQQMSSMVIEHMASHgTRFLRGCAPSRVRRLPDGQLQVTWEDsttGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGV 85
Cdd:PRK06292 205 LPLEDPEVSKQAQKILSKE-FKIKLGAKVTSVEKSGDEKVEELEKG---GKTETIEADYVLVATGRRPNTDGLGLENTGI 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 86 DTSpDTQKILVDSREATSVPHIYAIGDVVeGRPELTPTAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSE 165
Cdd:PRK06292 281 ELD-ERGRPVVDEHTQTSVPGIYAAGDVN-GKPPLLHEAADEGRIAAENAAGDVAGGVRYHPIPSVVFTDPQIASVGLTE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 166 EEAVARhGQEHVEvyhAHYkplEFTVAGR----DASQCYVKMVCLREpPQLVLGLHFLGPNAGEVTQGFALGIKCGASYA 241
Cdd:PRK06292 359 EELKAA-GIDYVV---GEV---PFEAQGRarvmGKNDGFVKVYADKK-TGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVE 430
|
250
....*....|....*...
gi 6649223 242 QVMRTVGIHPTcSEEVVK 259
Cdd:PRK06292 431 DLLRMPFYHPT-LSEGLR 447
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
10-266 |
4.71e-26 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 106.16 E-value: 4.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 10 DQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGqLQVTWEDSTtGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSp 89
Cdd:PRK06327 223 DEQVAKEAAKAFTKQGLDIHLGVKIGEIKTGGKG-VSVAYTDAD-GEAQTLEVDKLIVSIGRVPNTDGLGLEAVGLKLD- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 90 DTQKILVDSREATSVPHIYAIGDVVEGrPELTPTAIMAGrLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAV 169
Cdd:PRK06327 300 ERGFIPVDDHCRTNVPNVYAIGDVVRG-PMLAHKAEEEG-VAVAERIAGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLK 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 170 ArhgqEHVEvYHAHYKPleFTVAGR----DASQCYVKMVCLREPPQlVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMR 245
Cdd:PRK06327 378 A----EGVE-YKAGKFP--FMANGRalamGEPDGFVKIIADAKTDE-ILGVHVIGPNASELIAEAVVAMEFKASSEDIAR 449
|
250 260
....*....|....*....|....
gi 6649223 246 TVGIHPTCSeEVVK---LRISKRS 266
Cdd:PRK06327 450 ICHAHPTLS-EVWHeaaLAVDKRP 472
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
10-225 |
4.72e-25 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 103.31 E-value: 4.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 10 DQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLqVTWEDsttGKEDTGtfDTVLWAIGRVPDTRSLNLEKAGVDTSP 89
Cdd:PRK05249 215 DDEISDALSYHLRDSGVTIRHNEEVEKVEGGDDGVI-VHLKS---GKKIKA--DCLLYANGRTGNTDGLNLENAGLEADS 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 90 DTQkILVDSREATSVPHIYAIGDVVeGRPELTPTAIMAGRLLVQRLFGGSSDLMdYDNVPTTVFTPLEYGCVGLSEEEAV 169
Cdd:PRK05249 289 RGQ-LKVNENYQTAVPHIYAVGDVI-GFPSLASASMDQGRIAAQHAVGEATAHL-IEDIPTGIYTIPEISSVGKTEQELT 365
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6649223 170 ARHGqeHVEVYHAHYKPLeftvA-GRDASQCY--VKMVCLREPPQLvLGLHFLGPNAGE 225
Cdd:PRK05249 366 AAKV--PYEVGRARFKEL----ArAQIAGDNVgmLKILFHRETLEI-LGVHCFGERATE 417
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
1-128 |
6.02e-23 |
|
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: 95.46 E-value: 6.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 1 MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVTwedsttGKEDTGTFDTVLWAIGRVPDTRslNL 80
Cdd:pfam07992 183 ALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVIL------KDGTEIDADLVVVAIGRRPNTE--LL 254
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 6649223 81 EKAGVDTSPDTQkILVDSREATSVPHIYAIGDVVEGRPELTPTAIMAG 128
Cdd:pfam07992 255 EAAGLELDERGG-IVVDEYLRTSVPGIYAAGDCRVGGPELAQNAVAQG 301
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
46-235 |
1.92e-18 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 84.82 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 46 QVTWEDS----TTGKedtGTF--DTVLWAIGRVPDTRSLNLEKAGVDTSPDTQkILVDSREATSVPHIYAIGDVVEgRPE 119
Cdd:PRK13748 335 QVAHVDGefvlTTGH---GELraDKLLVATGRAPNTRSLALDAAGVTVNAQGA-IVIDQGMRTSVPHIYAAGDCTD-QPQ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 120 LTPTAIMAGRLLVQRLFGGSSDLmDYDNVPTTVFTPLEYGCVGLSEEEavARHGQEHVEVYHAHYKPLEFTVAGRDaSQC 199
Cdd:PRK13748 410 FVYVAAAAGTRAAINMTGGDAAL-DLTAMPAVVFTDPQVATVGYSEAE--AHHDGIETDSRTLTLDNVPRALANFD-TRG 485
|
170 180 190
....*....|....*....|....*....|....*.
gi 6649223 200 YVKMVcLREPPQLVLGLHFLGPNAGEVTQGFALGIK 235
Cdd:PRK13748 486 FIKLV-IEEGSGRLIGVQAVAPEAGELIQTAALAIR 520
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
13-255 |
1.12e-17 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 82.10 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 13 MSSMVIEHMASHGTRFLRGCAPSRVRRlPDGQLQVTWEDSTTgkedtgTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQ 92
Cdd:PRK07251 200 VAALAKQYMEEDGITFLLNAHTTEVKN-DGDQVLVVTEDETY------RFDALLYATGRKPNTEPLGLENTDIELT-ERG 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 93 KILVDSREATSVPHIYAIGDvVEGRPELTPTAIMAGRLLVQRLFGGSS-DLMDYDNVPTTVFTPLEYGCVGLSEEEAVAR 171
Cdd:PRK07251 272 AIKVDDYCQTSVPGVFAVGD-VNGGPQFTYISLDDFRIVFGYLTGDGSyTLEDRGNVPTTMFITPPLSQVGLTEKEAKEA 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 172 HGQehvevyhahYKPLEFTVAG--RDASQCYVK---MVCLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRT 246
Cdd:PRK07251 351 GLP---------YAVKELLVAAmpRAHVNNDLRgafKVVVNTETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQ 421
|
....*....
gi 6649223 247 VGIHPTCSE 255
Cdd:PRK07251 422 IFTHPTMAE 430
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
5-162 |
4.28e-17 |
|
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: 79.47 E-value: 4.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 5 PLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRrlPDGQLQVTWEDsttgkEDTGTFDTVLWAIGRVPDTrSLnLEKAG 84
Cdd:COG0446 159 LLGVLDPEMAALLEEELREHGVELRLGETVVAID--GDDKVAVTLTD-----GEEIPADLVVVAPGVRPNT-EL-AKDAG 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 85 VDTSPdTQKILVDSREATSVPHIYAIGDVVE------GRPELTP---TAIMAGRLLVQRLFGGSsdlMDYDNVPTTVFT- 154
Cdd:COG0446 230 LALGE-RGWIKVDETLQTSDPDVYAAGDCAEvphpvtGKTVYIPlasAANKQGRVAAENILGGP---APFPGLGTFISKv 305
|
....*....
gi 6649223 155 -PLEYGCVG 162
Cdd:COG0446 306 fDLCIASTG 314
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
6-257 |
5.26e-17 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 80.38 E-value: 5.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 6 LRGFDQQMSSMVIEHMashGTRF-LR-GCAPSRVRRLPDGqLQVTWEDSTTGkedtgTFDTVLWAIGRVPDTRSLNLEKA 83
Cdd:PRK07846 202 LRHLDDDISERFTELA---SKRWdVRlGRNVVGVSQDGSG-VTLRLDDGSTV-----EADVLLVATGRVPNGDLLDAAAA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 84 GVDTSPDtQKILVDSREATSVPHIYAIGDVveGRP-ELTPTAIMAGRLLVQRLFGGSSDL-MDYDNVPTTVFTPLEYGCV 161
Cdd:PRK07846 273 GVDVDED-GRVVVDEYQRTSAEGVFALGDV--SSPyQLKHVANHEARVVQHNLLHPDDLIaSDHRFVPAAVFTHPQIASV 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 162 GLSEEEAVARhGQEHVeVYHAHYKPLEFTVAGRDASQCyVKMVCLREPPQLvLGLHFLGPNAGEVTQGF----ALGIKcg 237
Cdd:PRK07846 350 GLTENEARAA-GLDIT-VKVQNYGDVAYGWAMEDTTGF-VKLIADRDTGRL-LGAHIIGPQASTLIQPLiqamSFGLD-- 423
|
250 260
....*....|....*....|..
gi 6649223 238 asyAQVM--RTVGIHPTCSEEV 257
Cdd:PRK07846 424 ---AREMarGQYWIHPALPEVV 442
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
7-172 |
2.20e-12 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 66.32 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 7 RGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRlPDGQLQVTWEDsttgkedtGTF---DTVLWAIGRVPDTrSLnLEKA 83
Cdd:COG1251 180 RQLDEEAGALLQRLLEALGVEVRLGTGVTEIEG-DDRVTGVRLAD--------GEElpaDLVVVAIGVRPNT-EL-ARAA 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 84 GVDTSpdtQKILVDSREATSVPHIYAIGDVVE------GRP--ELTPTAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTP 155
Cdd:COG1251 249 GLAVD---RGIVVDDYLRTSDPDIYAAGDCAEhpgpvyGRRvlELVAPAYEQARVAAANLAGGPAAYEGSVPSTKLKVFG 325
|
170
....*....|....*....
gi 6649223 156 LEYGCVGLSE--EEAVARH 172
Cdd:COG1251 326 VDVASAGDAEgdEEVVVRG 344
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
16-167 |
5.96e-12 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 65.27 E-value: 5.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 16 MVIEH-MASHGTRFLRGCAPSRVRRLPDGQLqVTWEDsttGKEDTGTFdtVLWAIGRVPDTRSLNLEKAGVDTSPdTQKI 94
Cdd:PRK07845 222 EVLEEvFARRGMTVLKRSRAESVERTGDGVV-VTLTD---GRTVEGSH--ALMAVGSVPNTAGLGLEEAGVELTP-SGHI 294
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6649223 95 LVD--SReaTSVPHIYAIGDVVEGRPeLTPTAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEE 167
Cdd:PRK07845 295 TVDrvSR--TSVPGIYAAGDCTGVLP-LASVAAMQGRIAMYHALGEAVSPLRLKTVASNVFTRPEIATVGVSQAA 366
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
39-255 |
1.27e-10 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 61.47 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 39 RLPDGQLQVT--WEDSTTGKEDTGTF----------DTVLWAIGRVPDTRSLNLEKAGVDTS----PDTQKILVDSREAT 102
Cdd:PTZ00153 381 RAGKGNQPVIigHSERQTGESDGPKKnmndiketyvDSCLVATGRKPNTNNLGLDKLKIQMKrgfvSVDEHLRVLREDQE 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 103 SVPHIYAIGDVvEGRPELTPTA----------IMA--GRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVA 170
Cdd:PTZ00153 461 VYDNIFCIGDA-NGKQMLAHTAshqalkvvdwIEGkgKENVNINVENWASKPIIYKNIPSVCYTTPELAFIGLTEKEAKE 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 171 RHGQEHVEVYHAHYKP-------LEFTVAGRDASQCY--------------VKMVCLREPPQlVLGLHFLGPNAGEVTQG 229
Cdd:PTZ00153 540 LYPPDNVGVEISFYKAnskvlceNNISFPNNSKNNSYnkgkyntvdntegmVKIVYLKDTKE-ILGMFIVGSYASILIHE 618
|
250 260
....*....|....*....|....*.
gi 6649223 230 FALGIKCGASYAQVMRTVGIHPTCSE 255
Cdd:PTZ00153 619 GVLAINLKLSVKDLAHMVHSHPTISE 644
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
42-130 |
3.02e-10 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 59.75 E-value: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 42 DGQLQ-VTWEDSTTGKEDTGTFDTVLWAIGRVPDTrSLnLEKAGVDTSPDtQKILVDSREATSVPHIYAIGDVVEGRPEL 120
Cdd:COG0492 206 DGRVEgVTLKNVKTGEEKELEVDGVFVAIGLKPNT-EL-LKGLGLELDED-GYIVVDEDMETSVPGVFAAGDVRDYKYRQ 282
|
90
....*....|
gi 6649223 121 TPTAIMAGRL 130
Cdd:COG0492 283 AATAAGEGAI 292
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
7-204 |
4.19e-10 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 59.67 E-value: 4.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 7 RGFDQQMSSMVIEHMASHGTRFLRGCAPSRVrrlpDGQLQVTWEDSTTGKEDTgtfDTVLWAIGRVPDTRSLnlEKAGVD 86
Cdd:PRK09564 187 DSFDKEITDVMEEELRENGVELHLNEFVKSL----IGEDKVEGVVTDKGEYEA---DVVIVATGVKPNTEFL--EDTGLK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 87 TSpDTQKILVDSREATSVPHIYAIGD------VVEGRPELTPTAIMA---GRLLVQRLFG---------GSSDLMDYDnv 148
Cdd:PRK09564 258 TL-KNGAIIVDEYGETSIENIYAAGDcatiynIVSNKNVYVPLATTAnklGRMVGENLAGrhvsfkgtlGSACIKVLD-- 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6649223 149 pttvftpLEYGCVGLSEEEAVArHGQEHVEVY-----HAHYKPleftvagrDASQCYVKMV 204
Cdd:PRK09564 335 -------LEAARTGLTEEEAKK-LGIDYKTVFikdknHTNYYP--------GQEDLYVKLI 379
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
42-260 |
5.68e-09 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 56.18 E-value: 5.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 42 DGQLQVTWEDSTTgkedtgTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVVEGRpELT 121
Cdd:PRK08010 229 ENQVQVHSEHAQL------AVDALLIASGRQPATASLHPENAGIAVN-ERGAIVVDKYLHTTADNIWAMGDVTGGL-QFT 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 122 PTAIMAGRLLVQRLFG-GSSDLMDYDNVPTTVFTPLEYGCVGLSEEEavARHGQEHVEVYHAHYKPLEFTVAGRDASQCY 200
Cdd:PRK08010 301 YISLDDYRIVRDELLGeGKRSTDDRKNVPYSVFMTPPLSRVGMTEEQ--ARESGADIQVVTLPVAAIPRARVMNDTRGVL 378
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 201 VKMVCLREppQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKL 260
Cdd:PRK08010 379 KAIVDNKT--QRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLNDL 436
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
13-135 |
4.79e-08 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 53.07 E-value: 4.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 13 MSSMVIEHMASHGTRFLRGCAP------SRVRRLPDGQLQVTWEDST--------TGKEDTGTFDTVLWAIGRVPdTRSL 78
Cdd:PRK12770 212 AGKYEIERLIARGVEFLELVTPvriigeGRVEGVELAKMRLGEPDESgrprpvpiPGSEFVLEADTVVFAIGEIP-TPPF 290
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 6649223 79 NLEKAGVDTSPDTqKILVDSREATSVPHIYAIGDVVEGrPELTPTAIMAGRLLVQRL 135
Cdd:PRK12770 291 AKECLGIELNRKG-EIVVDEKHMTSREGVFAAGDVVTG-PSKIGKAIKSGLRAAQSI 345
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
5-170 |
1.79e-06 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 48.59 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 5 PLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRrlPDGqlqVTWEDSTTGKedtgtFDTVLWAIG-RVPDTrslnLEKA 83
Cdd:COG1252 197 ILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVD--ADG---VTLEDGEEIP-----ADTVIWAAGvKAPPL----LADL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 84 GVDTSPDTQkILVDSR-EATSVPHIYAIGDVV-----EGRPeLTPTAIMA-------GRLLVQRLFGGssdlmdydnvPT 150
Cdd:COG1252 263 GLPTDRRGR-VLVDPTlQVPGHPNVFAIGDCAavpdpDGKP-VPKTAQAAvqqakvlAKNIAALLRGK----------PL 330
|
170 180
....*....|....*....|.
gi 6649223 151 TVFTPLEYGC-VGLSEEEAVA 170
Cdd:COG1252 331 KPFRYRDKGClASLGRGAAVA 351
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
56-129 |
2.23e-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: 48.21 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 56 KEDTGTF-----DTVLWAIGRVPDTRSLnLEKAGVDTSPDTqKILVDSRE-ATSVPHIYAIGDVVEGrPELTPTAIMAGR 129
Cdd:COG0493 349 VPIEGSEftlpaDLVILAIGQTPDPSGL-EEELGLELDKRG-TIVVDEETyQTSLPGVFAGGDAVRG-PSLVVWAIAEGR 425
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
20-142 |
2.12e-05 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 45.29 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 20 HMASHGTRFLRGCAPSRVRRLPDGqLQVTWEDSttgkeDTGTFDTVLWAIGRVPDTrSLNLEkAGVDTSpdtQKILVDSR 99
Cdd:PRK04965 192 RLTEMGVHLLLKSQLQGLEKTDSG-IRATLDSG-----RSIEVDAVIAAAGLRPNT-ALARR-AGLAVN---RGIVVDSY 260
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 6649223 100 EATSVPHIYAIGDVVE--GR--PELTPtAIMAGRLLVQRLFGGSSDL 142
Cdd:PRK04965 261 LQTSAPDIYALGDCAEinGQvlPFLQP-IQLSAMALAKNLLGQNTPL 306
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
42-113 |
1.11e-04 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 43.22 E-value: 1.11e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6649223 42 DGQlQVT---WEDSTTGKEDTGTFDTVLWAIGRVPDTRSLnleKAGVDTSPDTQkILVDSREATSVPHIYAIGDV 113
Cdd:PRK15317 416 DGD-KVTgltYKDRTTGEEHHLELEGVFVQIGLVPNTEWL---KGTVELNRRGE-IIVDARGATSVPGVFAAGDC 485
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
63-129 |
1.45e-03 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 39.76 E-value: 1.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6649223 63 DTVLWAIGRVPDTRSLnLEKAGVDTSPDTQKILVDSREATSVPHIYAIGDVVEGrPELTPTAIMAGR 129
Cdd:PRK12810 390 DLVLLAMGFTGPEAGL-LAQFGVELDERGRVAAPDNAYQTSNPKVFAAGDMRRG-QSLVVWAIAEGR 454
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
18-129 |
3.24e-03 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 38.62 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 18 IEHMASHGTRFLRGCAPSRVRRLPDGQLQVTWE--------DSTTGKE----DTGTF--DTVLWAIGRVPDTRSLNLEKa 83
Cdd:PRK11749 318 VEHAKEEGVEFEWLAAPVEILGDEGRVTGVEFVrmelgepdASGRRRVpiegSEFTLpaDLVIKAIGQTPNPLILSTTP- 396
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 6649223 84 GVDTSPDTQKILVDSREATSVPHIYAIGDVVEGrPELTPTAIMAGR 129
Cdd:PRK11749 397 GLELNRWGTIIADDETGRTSLPGVFAGGDIVTG-AATVVWAVGDGK 441
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
1-48 |
3.61e-03 |
|
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: 35.64 E-value: 3.61e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 6649223 1 MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVT 48
Cdd:pfam00070 30 RRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVL 77
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
58-186 |
4.51e-03 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 38.23 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6649223 58 DTGTFDTVLWAIGRVPDTRSLnlEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVVEG------RPELTPTAIMAGR-- 129
Cdd:PRK13512 226 KVEHYDMIIEGVGTHPNSKFI--ESSNIKLD-DKGFIPVNDKFETNVPNIYAIGDIITShyrhvdLPASVPLAWGAHRaa 302
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6649223 130 -LLVQRLFGGSS-DLMDYDNVPTTVFTPLEYGCVGLSEEEaVARHGQEHVEV---YHAHYKP 186
Cdd:PRK13512 303 sIVAEQIAGNDTiEFKGFLGNNIVKFFDYTFASVGVKPNE-LKQFDYKMVEVtqgAHANYYP 363
|
|
| |
