|
Name |
Accession |
Description |
Interval |
E-value |
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
127-501 |
0e+00 |
|
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member of the pyridine nucleotide disulfide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly, where SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily, Cys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-term arm of the protein is proposed to allow broad substrate specificity.
Pssm-ID: 273624 [Multi-domain] Cd Length: 484 Bit Score: 550.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 127 HDYDLIIIGGGSGGLSCAKEAANLGKKVMVLDFVVPSPQGTTWGLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGWEY 206
Cdd:TIGR01438 1 YDYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPTPLGTRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 207 NQQVKHNWEAMTEAIQSHIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIK----------------------------- 257
Cdd:TIGR01438 81 EETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKatnkkgkekiysaerfliatgerprypgi 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 258 --------------------------------------------------------------------------VQQLEK 263
Cdd:TIGR01438 161 pgakelcitsddlfslpycpgktlvvgasyvalecagflagigldvtvmvrsillrgfdqdcankvgehmeehgVKFKRQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 264 GLPGKL-----KVVAKSTEGPETVEGIYNTVLLAIGRDSCTRKIGLEKIGVKINEKNGKIPVNDVEQTNVPHVYAIGDIL 338
Cdd:TIGR01438 241 FVPIKVeqieaKVLVEFTDSTNGIEEEYDTVLLAIGRDACTRKLNLENVGVKINKKTGKIPADEEEQTNVPYIYAVGDIL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 339 DGKPELTPVAIQAGKLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEMYKKENLEVYHTLFWPLEWTVAGR 418
Cdd:TIGR01438 321 EDKPELTPVAIQAGRLLAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENVEVFHSYFWPLEWTIPSR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 419 DN-NTCYAKIICNKFDNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTLEITKSSGLDITQK 497
Cdd:TIGR01438 401 DNhNKCYAKLVCNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTLSVTKRSGQDILQQ 480
|
....
gi 296010807 498 GCUG 501
Cdd:TIGR01438 481 GCCG 484
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
124-501 |
3.67e-122 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 366.84 E-value: 3.67e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 124 DSAHDYDLIIIGGGSGGLSCAKEAANLGKKVMVLDFVVPSPQGTTWGLGGTCVNVGCIPKKLMHQAALLGHALQ-DAKKY 202
Cdd:PTZ00052 1 HLTFMYDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKPSTQGTKWGLGGTCVNVGCVPKKLMHYAANIGSIFHhDSQMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 203 GWEYNQqvKHNWEAMTEAIQSHIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIKVQQLE-------------------- 262
Cdd:PTZ00052 81 GWKTSS--SFNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTVSYGDNSqeetitakyiliatggrpsi 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 263 --------------------KGLPGKLKVVAKSTEGPETV---------------------------------------- 282
Cdd:PTZ00052 159 pedvpgakeysitsddifslSKDPGKTLIVGASYIGLETAgflnelgfdvtvavrsiplrgfdrqcsekvveymkeqgtl 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 283 --EGI-----------------------YNTVLLAIGRDSCTRKIGLEKIGVKINEKNGKIPVNDVeqTNVPHVYAIGDI 337
Cdd:PTZ00052 239 flEGVvpiniekmddkikvlfsdgttelFDTVLYATGRKPDIKGLNLNAIGVHVNKSNKIIAPNDC--TNIPNIFAVGDV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 338 LDGKPELTPVAIQAGKLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEMYKKENLEVYHTLFWPLEWTVAG 417
Cdd:PTZ00052 317 VEGRPELTPVAIKAGILLARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQEFNTLEIAAVH 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 418 RD--------------NNTCYAKIICNKFDNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTT 483
Cdd:PTZ00052 397 REkherarkdeydfdvSSNCLAKLVCVKSEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHPTDAEVFMN 476
|
490
....*....|....*...
gi 296010807 484 LEITKSSGLDITQKGCUG 501
Cdd:PTZ00052 477 LSVTRRSGESFAAKGGCG 494
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
144-484 |
5.30e-86 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 272.03 E-value: 5.30e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 144 AKEAANLGKKVMVLDfvvpspqgtTWGLGGTCVNVGCIPKKLMHQAALLGHALQD-AKKYGWEYNQQvKHNWEAMTEAIQ 222
Cdd:PRK06116 20 ANRAAMYGAKVALIE---------AKRLGGTCVNVGCVPKKLMWYGAQIAEAFHDyAPGYGFDVTEN-KFDWAKLIANRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 223 SHIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIKVQ-----------------------------------QLEKgLPG 267
Cdd:PRK06116 90 AYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNgerytadhiliatggrpsipdipgaeygitsdgffALEE-LPK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 268 KLKVV-------------------------------------------AKSTEG--------PETVE----GIYN----- 287
Cdd:PRK06116 169 RVAVVgagyiavefagvlnglgsethlfvrgdaplrgfdpdiretlveEMEKKGirlhtnavPKAVEknadGSLTltled 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 288 -------TVLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNVPHVYAIGDIlDGKPELTPVAIQAGKLLARRLF 360
Cdd:PRK06116 249 getltvdCLIWAIGREPNTDGLGLENAGVKLNEK-GYIIVDEYQNTNVPGIYAVGDV-TGRVELTPVAIAAGRRLSERLF 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 361 -GVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEMYKKENLEVYHTLFWPLEWTVAGRDNnTCYAKIICNKfDNERVVG 439
Cdd:PRK06116 327 nNKPDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVKVYRSSFTPMYTALTGHRQ-PCLMKLVVVG-KEEKVVG 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 296010807 440 FHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 484
Cdd:PRK06116 405 LHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFVTM 449
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
143-484 |
1.46e-71 |
|
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: 234.60 E-value: 1.46e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 143 CAKEAANLGKKVMVLDfvvpspQGTtwgLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGWEYnQQVKHNWEAMTEAIQ 222
Cdd:COG1249 18 AAIRAAQLGLKVALVE------KGR---LGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISA-GAPSVDWAALMARKD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 223 SHIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIKV-------------------------------------------- 258
Cdd:COG1249 88 KVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVtggetltadhiviatgsrprvppipgldevrvltsdealeleel 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 259 ---------------------------------------------QQLEKGL-------------------PGKLKVVAK 274
Cdd:COG1249 168 pkslvvigggyiglefaqifarlgsevtlvergdrllpgedpeisEALEKALekegidiltgakvtsvektGDGVTVTLE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 275 STEGPETVEGiyNTVLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNVPHVYAIGDILdGKPELTPVAIQAGKL 354
Cdd:COG1249 248 DGGGEEAVEA--DKVLVATGRRPNTDGLGLEAAGVELDER-GGIKVDEYLRTSVPGIYAIGDVT-GGPQLAHVASAEGRV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 355 LARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEmyKKENLEVYHTLFWPLEWTVAGRDNnTCYAKIICNKfDN 434
Cdd:COG1249 324 AAENILGKKPRPVDYRAIPSVVFTDPEIASVGLTEEEARE--AGIDVKVGKFPFAANGRALALGET-EGFVKLIADA-ET 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 296010807 435 ERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 484
Cdd:COG1249 400 GRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEA 449
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
144-484 |
1.54e-64 |
|
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: 215.86 E-value: 1.54e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 144 AKEAANLGKKVMVLDfvvpspqgtTWGLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGWEYNQQVKHNWEAMTEAIQS 223
Cdd:TIGR01421 18 ARRAAEHGAKALLVE---------AKKLGGTCVNVGCVPKKVMWYASDLAERMHDAADYGFYQNDENTFNWPELKEKRDA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 224 HIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIKVQ------------------------------------QLEKgLPG 267
Cdd:TIGR01421 89 YVDRLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVNgrdytaphiliatggkpsfpenipgaelgtdsdgffALEE-LPK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 268 KLKVV-------------------------------------------------------AKSTEGPETVEGIY------ 286
Cdd:TIGR01421 168 RVVIVgagyiavelagvlhglgsethlvirhervlrsfdsmisetiteeyekeginvhklSKPVKVEKTVEGKLvihfed 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 287 -------NTVLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNVPHVYAIGDILdGKPELTPVAIQAGKLLARRL 359
Cdd:TIGR01421 248 gksiddvDELIWAIGRKPNTKGLGLENVGIKLNEK-GQIIVDEYQNTNVPGIYALGDVV-GKVELTPVAIAAGRKLSERL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 360 F-GVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEMYKKENLEVYHTLFWPLEWTVaGRDNNTCYAKIIC-NKfdNERV 437
Cdd:TIGR01421 326 FnGKTDDKLDYNNVPTVVFSHPPIGTIGLTEKEAIEKYGKENIKVYNSSFTPMYYAM-TSEKQKCRMKLVCaGK--EEKV 402
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 296010807 438 VGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 484
Cdd:TIGR01421 403 VGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEELVTM 449
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
147-484 |
3.39e-60 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 207.42 E-value: 3.39e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 147 AANLGKKVMV--LDFVVPSPQgTTWGLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGWEYNQQVKHNWEAMTEAIQSH 224
Cdd:PLN02546 98 ASNFGASAAVceLPFATISSD-TLGGVGGTCVLRGCVPKKLLVYASKYSHEFEESRGFGWKYETEPKHDWNTLIANKNAE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 225 IGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIKV-------------------------------QQLEKGLPGKLKVVA 273
Cdd:PLN02546 177 LQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDVdgklytarniliavggrpfipdipgiehaidSDAALDLPSKPEKIA 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 274 ----------------------------------------------------------------KSTEG-------PETV 282
Cdd:PLN02546 257 ivgggyialefagifnglksdvhvfirqkkvlrgfdeevrdfvaeqmslrgiefhteespqaiiKSADGslslktnKGTV 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 283 EGiYNTVLLAIGRDSCTRKIGLEKIGVKINeKNGKIPVNDVEQTNVPHVYAIGDILDgKPELTPVAIQAGKLLARRLFGV 362
Cdd:PLN02546 337 EG-FSHVMFATGRKPNTKNLGLEEVGVKMD-KNGAIEVDEYSRTSVPSIWAVGDVTD-RINLTPVALMEGGALAKTLFGN 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 363 SLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEMYKkeNLEVYHTLFWPLEWTVAGRDNNTCYAKIICNKfdNERVVGFHL 442
Cdd:PLN02546 414 EPTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYG--DVDVFTANFRPLKATLSGLPDRVFMKLIVCAK--TNKVLGVHM 489
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 296010807 443 LGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 484
Cdd:PLN02546 490 CGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEEFVTM 531
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
123-484 |
1.26e-58 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 201.58 E-value: 1.26e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 123 DDSAHDYDLIIIGGGSGGLSCAKEAANLGKKVMVLDFVV-PSPQGTTWGLGGTCVNVGCIPKKLMHQAALLGHALQDAKK 201
Cdd:PLN02507 20 NATHYDFDLFVIGAGSGGVRAARFSANFGAKVGICELPFhPISSESIGGVGGTCVIRGCVPKKILVYGATFGGEFEDAKN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 202 YGWEYNQQVKHNWEAMTEAIQSHIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIKVQQLEK------------------ 263
Cdd:PLN02507 100 YGWEINEKVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGtklrytakhiliatgsra 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 264 ---GLPGK-----------------------------------------------------------LKVVAKSTEG--- 278
Cdd:PLN02507 180 qrpNIPGKelaitsdealsleelpkravvlgggyiavefasiwrgmgatvdlffrkelplrgfddemRAVVARNLEGrgi 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 279 ---PET-------VEG------------IYNTVLLAIGRDSCTRKIGLEKIGVKInEKNGKIPVNDVEQTNVPHVYAIGD 336
Cdd:PLN02507 260 nlhPRTnltqltkTEGgikvitdhgeefVADVVLFATGRAPNTKRLNLEAVGVEL-DKAGAVKVDEYSRTNIPSIWAIGD 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 337 ILDgKPELTPVAIQAGKLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEMYKKENLeVYHTLFWPLEWTVA 416
Cdd:PLN02507 339 VTN-RINLTPVALMEGTCFAKTVFGGQPTKPDYENVACAVFCIPPLSVVGLSEEEAVEQAKGDIL-VFTSSFNPMKNTIS 416
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296010807 417 GRDNNTCYAKIICNKFDneRVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 484
Cdd:PLN02507 417 GRQEKTVMKLIVDAETD--KVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEFVTM 482
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
144-484 |
1.00e-56 |
|
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: 195.03 E-value: 1.00e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 144 AKEAANLGKKVMV--LDFVvpspqgttwglGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGWEyNQQVKHNWEAMTEAI 221
Cdd:TIGR01424 18 ARLAAALGAKVAIaeEFRV-----------GGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGWT-VGKARFDWKKLLAAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 222 QSHIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIKVQQLEK------------------GLPGK--------------- 268
Cdd:TIGR01424 86 DQEIARLSGLYRKGLANAGAELLDGRAELVGPNTVEVLASGKtytaekiliavggrppkpALPGHelgitsneafhlptl 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 269 ----------------------------------------------------------------LKVVAKSTEGPETV-- 282
Cdd:TIGR01424 166 pksiliagggyiavefagifrglgvqttliyrgkeilrgfdddmrrglaaaleergirilpedsITSISKDDDGRLKAtl 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 283 ----EGIYNTVLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNVPHVYAIGDILDgKPELTPVAIQAGKLLARR 358
Cdd:TIGR01424 246 skheEIVADVVLFATGRSPNTNGLGLEAAGVRLNDL-GAIAVDEYSRTSTPSIYAVGDVTD-RINLTPVAIHEATCFAET 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 359 LFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEmyKKENLEVYHTLFWPLEWTVAGRDNNtCYAKIICNKfDNERVV 438
Cdd:TIGR01424 324 EFGNNPTSFDHDLIATAVFSQPPIGTVGLTEEEARR--KFGDIEVYRAEFRPMKATFSGRQEK-TLMKLVVDA-KDDKVL 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 296010807 439 GFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 484
Cdd:TIGR01424 400 GAHMVGPDAAEIIQGLAIALKMGATKDDFDSTVAVHPTSAEELVTM 445
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
171-484 |
9.25e-47 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 170.95 E-value: 9.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 171 LGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGweYNQQVKHNWEAMTEAIQSHIGSLNWGYRVTLREKGVTYVNSFGEF 250
Cdd:PTZ00058 82 LGGTCVNVGCVPKKIMFNAASIHDILENSRHYG--FDTQFSFNLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 251 VDLHKI-------------------------KVQQLEKG--LPGKLKVVAKSTEgPET--VEGIYNT------------- 288
Cdd:PTZ00058 160 LSENQVlikkvsqvdgeadesdddevtivsaGVSQLDDGqvIEGKNILIAVGNK-PIFpdVKGKEFTissddffkikeak 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 --------------------------------------------------------------------------------
Cdd:PTZ00058 239 rigiagsgyiavelinvvnrlgaesyifargnrllrkfdetiinelendmkknniniithanveeiekvkeknltiylsd 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 289 ---------VLLAIGRDSCTRKIGLEkiGVKINEKNGKIPVNDVEQTNVPHVYAIGDILDGKP----------------- 342
Cdd:PTZ00058 319 grkyehfdyVIYCVGRSPNTEDLNLK--ALNIKTPKGYIKVDDNQRTSVKHIYAVGDCCMVKKnqeiedlnllklyneep 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 343 ----------------ELTPVAIQAGKLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEMYKKENLEVYHT 406
Cdd:PTZ00058 397 ylkkkentsgesyynvQLTPVAINAGRLLADRLFGPFSRTTNYKLIPSVIFSHPPIGTIGLSEQEAIDIYGKENVKIYES 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 407 LFWPLEWTV---AGRDNNTCYAKIICNKfDNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTT 483
Cdd:PTZ00058 477 RFTNLFFSVydmDPAQKEKTYLKLVCVG-KEELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIHPTAAEEFVT 555
|
.
gi 296010807 484 L 484
Cdd:PTZ00058 556 M 556
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
143-480 |
2.71e-45 |
|
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: 164.74 E-value: 2.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 143 CAKEAANLGKKVMVldfvVPSPQgttwgLGGTCVNVGCIPKK-LMHQAALLgHALQDAKKYGWEYNQqVKHNWEAMTEAI 221
Cdd:TIGR01350 16 AAIRAAQLGLKVAL----VEKEY-----LGGTCLNVGCIPTKaLLHSAEVY-DEIKHAKDLGIEVEN-VSVDWEKMQKRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 222 QSHIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIKV----------------------------------------QQL 261
Cdd:TIGR01350 85 NKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVtgengeetleakniiiatgsrprslpgpfdfdgkvvitstGAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 262 E-KGLPGKL-----------------------------------------KVVAK------------------------- 274
Cdd:TIGR01350 165 NlEEVPESLviigggvigiefasifaslgskvtviemldrilpgedaevsKVLQKalkkkgvkiltntkvtaveknddqv 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 275 --STEGPETVEGIYNTVLLAIGRDSCTRKIGLEKIGVKINEkNGKIPVNDVEQTNVPHVYAIGDILdGKPELTPVAIQAG 352
Cdd:TIGR01350 245 tyENKGGETETLTGEKVLVAVGRKPNTEGLGLEKLGVELDE-RGRIVVDEYMRTNVPGIYAIGDVI-GGPMLAHVASHEG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 353 KLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAiemyKKENLEVYHTLFwPLewTVAGR----DNNTCYAKII 428
Cdd:TIGR01350 323 IVAAENIAGKEPAHIDYDAVPSVIYTDPEVASVGLTEEQA----KEAGYDVKIGKF-PF--AANGKalalGETDGFVKII 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 296010807 429 CNKfDNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEV 480
Cdd:TIGR01350 396 ADK-KTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEA 446
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
147-479 |
3.57e-43 |
|
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: 159.75 E-value: 3.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 147 AANL-GKKVMVLDfvVPSPQGTTW--GLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGWEYNQQ-VKHNWEAMTEAIQ 222
Cdd:TIGR01423 22 AATLyKKRVAVVD--VQTHHGPPFyaALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGWEFDRSsVKANWKALIAAKN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 223 SHIGSLNWGYRVTLRE-KGVTYVNSFGEFVDLHKIKV------------------------------------------- 258
Cdd:TIGR01423 100 KAVLDINKSYEGMFADtEGLTFFLGWGALEDKNVVLVresadpksavkerlqaehillatgswpqmlgipgiehcissne 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 259 -------------------------------------------------------QQLEKGL------------PGKlkv 271
Cdd:TIGR01423 180 afyldepprrvltvgggfisvefagifnaykprggkvtlcyrnnmilrgfdstlrKELTKQLranginimtnenPAK--- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 272 VAKSTEGPETV------EGIYNTVLLAIGRDSCTRKIGLEKIGVKINeKNGKIPVNDVEQTNVPHVYAIGDILDgKPELT 345
Cdd:TIGR01423 257 VTLNADGSKHVtfesgkTLDVDVVMMAIGRVPRTQTLQLDKVGVELT-KKGAIQVDEFSRTNVPNIYAIGDVTD-RVMLT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 346 PVAIQAGKLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEMYKKenLEVYHTLFWPLEWTVAGRDNNTCYA 425
Cdd:TIGR01423 335 PVAINEGAAFVDTVFGNKPRKTDHTRVASAVFSIPPIGTCGLVEEDAAKKFEK--VAVYESSFTPLMHNISGSKYKKFVA 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 296010807 426 KIICNKFDNErVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGE 479
Cdd:TIGR01423 413 KIVTNHADGT-VLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAE 465
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
372-484 |
1.06e-37 |
|
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases.
Pssm-ID: 427019 [Multi-domain] Cd Length: 109 Bit Score: 133.83 E-value: 1.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 372 IPTTVFTPLEYGCCGLSEEKAIEMYKKenLEVYHTLFWPLEWTVAGRDNNtCYAKIICNKfDNERVVGFHLLGPNAGEIT 451
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGE--VKVGKFPFAANGRALAYGDTD-GFVKLVADR-ETGKILGAHIVGPNAGELI 76
|
90 100 110
....*....|....*....|....*....|...
gi 296010807 452 QGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 484
Cdd:pfam02852 77 QEAALAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| GRX_GRXh_1_2_like |
cd03419 |
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ... |
39-120 |
1.41e-36 |
|
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of proteins similar to human GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, which are members of this subfamily. Also included in this subfamily are the N-terminal GRX domains of proteins similar to human thioredoxin reductase 1 and 3.
Pssm-ID: 239511 [Multi-domain] Cd Length: 82 Bit Score: 129.97 E-value: 1.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 39 RVMIFSKSYCPHSTRVKELFSSLGVVYNILELDQVDDGASVQEVLTEISNQKTVPNIFVNKVHVGGCDRTFQAHQNGLLQ 118
Cdd:cd03419 1 PVVVFSKSYCPYCKRAKSLLKELGVKPAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSGKLV 80
|
..
gi 296010807 119 KL 120
Cdd:cd03419 81 KL 82
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
143-483 |
2.75e-34 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 134.15 E-value: 2.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 143 CAKEAANLGKKVMVLDfvvpspQGTtwgLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGWEYnQQVKHNWEAMTEAIQ 222
Cdd:PRK06292 18 AARRAAKLGKKVALIE------KGP---LGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHA-DGPKIDFKKVMARVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 223 SHIGSLNWGYRVTLREK-GVTYVNSFGEFVDLHKIKV--QQLE---------------KG-------------------- 264
Cdd:PRK06292 88 RERDRFVGGVVEGLEKKpKIDKIKGTARFVDPNTVEVngERIEakniviatgsrvppiPGvwlilgdrlltsddafeldk 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 265 LPGKLKVV----------------------------------------------------------------------AK 274
Cdd:PRK06292 168 LPKSLAVIgggviglelgqalsrlgvkvtvfergdrilpledpevskqaqkilskefkiklgakvtsveksgdekveeLE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 275 STEGPETVEGIYntVLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNVPHVYAIGDIlDGKPELTPVAIQAGKL 354
Cdd:PRK06292 248 KGGKTETIEADY--VLVATGRRPNTDGLGLENTGIELDER-GRPVVDEHTQTSVPGIYAAGDV-NGKPPLLHEAADEGRI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 355 LARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEMYKKenlevYHTLFWPLEWTVAGR-DNNTCYA-KIICNKf 432
Cdd:PRK06292 324 AAENAAGDVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGID-----YVVGEVPFEAQGRARvMGKNDGFvKVYADK- 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 296010807 433 DNERVVGFHLLGPNAGEITQGFAAAMKCGLT-KQLLdDTIGIHPTCGEVFTT 483
Cdd:PRK06292 398 KTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTvEDLL-RMPFYHPTLSEGLRT 448
|
|
| GRX_euk |
TIGR02180 |
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ... |
40-121 |
2.63e-33 |
|
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress, reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This model represents eukaryotic glutaredoxins and includes sequences from fungi, plants and metazoans as well as viruses.
Pssm-ID: 274016 [Multi-domain] Cd Length: 83 Bit Score: 121.20 E-value: 2.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 40 VMIFSKSYCPHSTRVKELFSSLGV-VYNILELDQVDDGASVQEVLTEISNQKTVPNIFVNKVHVGGCDRTFQAHQNGLLQ 118
Cdd:TIGR02180 1 VVVFSKSYCPYCKKAKEILAKLNVkPYEVVELDQLSNGSEIQDYLEEITGQRTVPNIFINGKFIGGCSDLLALYKNGKLA 80
|
...
gi 296010807 119 KLL 121
Cdd:TIGR02180 81 ELL 83
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
143-480 |
2.51e-32 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 128.73 E-value: 2.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 143 CAKEAANLGKKVMVL--DFvvpspqgttwgLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGWEYnQQVKHNWEAMTEA 220
Cdd:PRK06416 19 AAIRAAQLGLKVAIVekEK-----------LGGTCLNRGCIPSKALLHAAERADEARHSEDFGIKA-ENVGIDFKKVQEW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 221 IQSHIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIKVQQLEKG------------------LPG--------------- 267
Cdd:PRK06416 87 KNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDGEqtytakniilatgsrpreLPGieidgrviwtsdeal 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 268 KLKVVAKS------------------------------------------------------------------------ 275
Cdd:PRK06416 167 NLDEVPKSlvvigggyigvefasayaslgaevtivealprilpgedkeisklaeralkkrgikiktgakakkveqtddgv 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 276 ------TEGPETVEGIYntVLLAIGRDSCTRKIGLEKIGVKINEknGKIPVNDVEQTNVPHVYAIGDILdGKPELTPVAI 349
Cdd:PRK06416 247 tvtledGGKEETLEADY--VLVAVGRRPNTENLGLEELGVKTDR--GFIEVDEQLRTNVPNIYAIGDIV-GGPMLAHKAS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 350 QAGKLLARRLFGVSLEkCDYINIPTTVFTPLEYGCCGLSEEKAIEmyKKENLEVYHTLFwplewtvAGR------DNNTC 423
Cdd:PRK06416 322 AEGIIAAEAIAGNPHP-IDYRGIPAVTYTHPEVASVGLTEAKAKE--EGFDVKVVKFPF-------AGNgkalalGETDG 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 296010807 424 YAKIICNKFDNErVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEV 480
Cdd:PRK06416 392 FVKLIFDKKDGE-VLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEA 447
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
144-501 |
1.21e-29 |
|
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: 120.99 E-value: 1.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 144 AKEAANLGKKVMVLDfvvpspQGTtwgLGGTCVNVGCIPKKLMHQAA--------------------LLGHALQDAKK-- 201
Cdd:TIGR02053 16 AIKAAELGASVAMVE------RGP---LGGTCVNVGCVPSKMLLRAAevahyarkppfgglaatvavDFGELLEGKREvv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 202 --------------YGWEY---------------------------------NQQVKH-----------NWEAMTE---- 219
Cdd:TIGR02053 87 eelrhekyedvlssYGVDYlrgrarfkdpktvkvdlgrevrgakrfliatgaRPAIPPipglkeagyltSEEALALdrip 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 220 ---------AIQSHIGSL--NWGYRVTL------------REKGVTYVNSF-GEFVDLHK-IKVQQLEKGLPGKLKVVAK 274
Cdd:TIGR02053 167 eslavigggAIGVELAQAfaRLGSEVTIlqrsdrllpreePEISAAVEEALaEEGIEVVTsAQVKAVSVRGGGKIITVEK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 275 StEGPETVEGIYntVLLAIGRDSCTRKIGLEKIGVKINEkNGKIPVNDVEQTNVPHVYAIGDILDGkPELTPVAIQAGKL 354
Cdd:TIGR02053 247 P-GGQGEVEADE--LLVATGRRPNTDGLGLEKAGVKLDE-RGGILVDETLRTSNPGIYAAGDVTGG-LQLEYVAAKEGVV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 355 LARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIemykkENLEVYHTLFWPLEWTVAGRDN--NTCYAKIICNKf 432
Cdd:TIGR02053 322 AAENALGGANAKLDLLVIPRVVFTDPAVASVGLTEAEAQ-----KAGIECDCRTLPLTNVPRARINrdTRGFIKLVAEP- 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296010807 433 DNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTLEITKSSglDITQKGCUG 501
Cdd:TIGR02053 396 GTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGLKLAAQTFYR--DVSKLSCCA 462
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
143-484 |
1.93e-23 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 102.97 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 143 CAKEAANLGKKVMVLdfvvpspqGTTWgLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGWEYNQQVKHNWEAMTEAIQ 222
Cdd:PRK06370 20 LAARAAGLGMKVALI--------ERGL-LGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGGPVSVDFKAVMARKR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 223 SHIGSLNWGYRVTLRE-KGVTYVNSFGEFVDLHKIKVQ-------------------------------------QLEKg 264
Cdd:PRK06370 91 RIRARSRHGSEQWLRGlEGVDVFRGHARFESPNTVRVGgetlrakrifintgaraaippipgldevgyltnetifSLDE- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 265 LPGKLKVVAKSTEGPE------------TV-------------------------EGI---YNT---------------- 288
Cdd:PRK06370 170 LPEHLVIIGGGYIGLEfaqmfrrfgsevTViergprllprededvaaavreilerEGIdvrLNAecirverdgdgiavgl 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 289 -------------VLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNVPHVYAIGDIlDGKPELTPVAIQAGKLL 355
Cdd:PRK06370 250 dcnggapeitgshILVAVGRVPNTDDLGLEAAGVETDAR-GYIKVDDQLRTTNPGIYAAGDC-NGRGAFTHTAYNDARIV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 356 ARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEmyKKENLEVYHTLFwplewTVAGR----DNNTCYAKIICNK 431
Cdd:PRK06370 328 AANLLDGGRRKVSDRIVPYATYTDPPLARVGMTEAEARK--SGRRVLVGTRPM-----TRVGRavekGETQGFMKVVVDA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 296010807 432 fDNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 484
Cdd:PRK06370 401 -DTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIPTL 452
|
|
| GRX_family |
cd02066 |
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ... |
39-113 |
7.10e-23 |
|
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, as well as E. coli GRX1 and GRX3, which are members of this family. E. coli GRX2, however, is a 24-kDa protein that belongs to the GSH S-transferase (GST) family.
Pssm-ID: 239017 [Multi-domain] Cd Length: 72 Bit Score: 91.76 E-value: 7.10e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296010807 39 RVMIFSKSYCPHSTRVKELFSSLGVVYniLELDQVDDGAsVQEVLTEISNQKTVPNIFVNKVHVGGCDRTFQAHQ 113
Cdd:cd02066 1 KVVVFSKSTCPYCKRAKRLLESLGIEF--EEIDILEDGE-LREELKELSGWPTVPQIFINGEFIGGYDDLKALHE 72
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
147-480 |
3.48e-22 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 99.23 E-value: 3.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 147 AANLGKKVMVLDfVVPSPQGTTwGLGGTCVNVGCIPKK-LMHQAALLGHALQDAKKYGWEYNQqVKHNWEAMTEAIQSHI 225
Cdd:PRK06327 23 AAQLGLKVACIE-AWKNPKGKP-ALGGTCLNVGCIPSKaLLASSEEFENAGHHFADHGIHVDG-VKIDVAKMIARKDKVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 226 GSLNWGYRVTLREKGVTYVNSFGEFV----DLHKIKVQQLEK-------------------------------------- 263
Cdd:PRK06327 100 KKMTGGIEGLFKKNKITVLKGRGSFVgktdAGYEIKVTGEDEtvitakhviiatgseprhlpgvpfdnkiildntgalnf 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 264 -GLPGKLKV-------------------------------------VAKSTEGPETVEGI-------------------- 285
Cdd:PRK06327 180 tEVPKKLAVigagviglelgsvwrrlgaevtilealpaflaaadeqVAKEAAKAFTKQGLdihlgvkigeiktggkgvsv 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 286 -------------YNTVLLAIGRDSCTRKIGLEKIGVKINEkNGKIPVNDVEQTNVPHVYAIGDILdGKPELTPVAIQAG 352
Cdd:PRK06327 260 aytdadgeaqtleVDKLIVSIGRVPNTDGLGLEAVGLKLDE-RGFIPVDDHCRTNVPNVYAIGDVV-RGPMLAHKAEEEG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 353 KLLARRLFGVSlEKCDYINIPTTVFTPLEYGCCGLSEEKAiemyKKENLEVYHTLFwPleWTVAGR----DNNTCYAKII 428
Cdd:PRK06327 338 VAVAERIAGQK-GHIDYNTIPWVIYTSPEIAWVGKTEQQL----KAEGVEYKAGKF-P--FMANGRalamGEPDGFVKII 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 296010807 429 CNKfDNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEV 480
Cdd:PRK06327 410 ADA-KTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEV 460
|
|
| GRX_bact |
TIGR02181 |
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ... |
40-121 |
8.33e-18 |
|
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress, reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This family of glutaredoxins includes the E. coli protein GrxC (Grx3) which appears to have a secondary role in reducing ribonucleotide reductase (in the absence of GrxA) possibly indicating a role in the reduction of other protein disulfides. [Energy metabolism, Electron transport]
Pssm-ID: 274017 [Multi-domain] Cd Length: 79 Bit Score: 78.07 E-value: 8.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 40 VMIFSKSYCPHSTRVKELFSSLGVVYNILELDqvDDGASVQEVLtEISNQKTVPNIFVNKVHVGGCDRTFQAHQNGLLQK 119
Cdd:TIGR02181 1 VTIYTKPYCPYCTRAKALLSSKGVTFTEIRVD--GDPALRDEMM-QRSGRRTVPQIFIGDVHVGGCDDLYALDREGKLDP 77
|
..
gi 296010807 120 LL 121
Cdd:TIGR02181 78 LL 79
|
|
| Glutaredoxin |
pfam00462 |
Glutaredoxin; |
40-102 |
3.74e-16 |
|
Glutaredoxin;
Pssm-ID: 425695 [Multi-domain] Cd Length: 60 Bit Score: 72.54 E-value: 3.74e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296010807 40 VMIFSKSYCPHSTRVKELFSSLGVVYNILELDQVDDgasVQEVLTEISNQKTVPNIFVNKVHV 102
Cdd:pfam00462 1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDVDEDPE---IREELKELSGWPTVPQVFIDGEHI 60
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
288-479 |
7.71e-16 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 79.82 E-value: 7.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 288 TVLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNVPHVYAIGDILdGKPELTPVAIQAGKLLARRLFGVSLEKc 367
Cdd:PRK05249 263 CLLYANGRTGNTDGLNLENAGLEADSR-GQLKVNENYQTAVPHIYAVGDVI-GFPSLASASMDQGRIAAQHAVGEATAH- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 368 dYIN-IPTTVFTPLEYGCCGLSEEKAIEM---YkkenlEVYHTLFwplewtvagRDN--------NTCYAKIICNKfDNE 435
Cdd:PRK05249 340 -LIEdIPTGIYTIPEISSVGKTEQELTAAkvpY-----EVGRARF---------KELaraqiagdNVGMLKILFHR-ETL 403
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 296010807 436 RVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGE 479
Cdd:PRK05249 404 EILGVHCFGERATEIIHIGQAIMEQKGTIEYFVNTTFNYPTMAE 447
|
|
| GRX_GRXb_1_3_like |
cd03418 |
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ... |
40-106 |
7.99e-14 |
|
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of bacterial GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including E. coli GRX1 and GRX3, which are members of this subfamily.
Pssm-ID: 239510 [Multi-domain] Cd Length: 75 Bit Score: 66.46 E-value: 7.99e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296010807 40 VMIFSKSYCPHSTRVKELFSSLGVVYnilELDQVDDGASVQEVLTEISNQ-KTVPNIFVNKVHVGGCD 106
Cdd:cd03418 2 VEIYTKPNCPYCVRAKALLDKKGVDY---EEIDVDGDPALREEMINRSGGrRTVPQIFIGDVHIGGCD 66
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
272-480 |
1.34e-13 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 72.68 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 272 VAKSTEGPETVEGiyNTVLLAIGRDSCTRKIGLEKIGVKINEkNGKIPVNDVEQTNVPHVYAIGDILDgKPELTPVAIQA 351
Cdd:PRK07846 239 VTLRLDDGSTVEA--DVLLVATGRVPNGDLLDAAAAGVDVDE-DGRVVVDEYQRTSAEGVFALGDVSS-PYQLKHVANHE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 352 GKLLARRLF-GVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEmyKKENLEVYHTLF------WPLEWTvagrdnnTCY 424
Cdd:PRK07846 315 ARVVQHNLLhPDDLIASDHRFVPAAVFTHPQIASVGLTENEARA--AGLDITVKVQNYgdvaygWAMEDT-------TGF 385
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 296010807 425 AKIICNKfDNERVVGFHLLGPNAGEITQGFAAAMKCGLT-KQLLDDTIGIHPTCGEV 480
Cdd:PRK07846 386 VKLIADR-DTGRLLGAHIIGPQASTLIQPLIQAMSFGLDaREMARGQYWIHPALPEV 441
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
143-352 |
1.49e-13 |
|
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: 71.20 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 143 CAKEAANLGKKVMVLdfvvpspqgttwGLGGTCVNVGCIPKKLMHQAALLGHALqdakkygweynqqvkHNWEAMTEAIQ 222
Cdd:pfam07992 15 AALTLAQLGGKVTLI------------EDEGTCPYGGCVLSKALLGAAEAPEIA---------------SLWADLYKRKE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 223 SHIGSLNWGYRVTLREKGVTYVNSFGEFVDLH-------KIKVQQL---------------------------------- 261
Cdd:pfam07992 68 EVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEElvdgdgeTITYDRLviatgarprlppipgvelnvgflvrtldsaealr 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 262 EKGLPGKLKVV----------------------------AKSTEGPE--------------------TVEGI-------- 285
Cdd:pfam07992 148 LKLLPKRVVVVgggyigvelaaalaklgkevtliealdrLLRAFDEEisaalekalekngvevrlgtSVKEIigdgdgve 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296010807 286 ----------YNTVLLAIGRDSCTRkiGLEKIGVKINEkNGKIPVNDVEQTNVPHVYAIGDILDGKPELTPVAIQAG 352
Cdd:pfam07992 228 vilkdgteidADLVVVAIGRRPNTE--LLEAAGLELDE-RGGIVVDEYLRTSVPGIYAAGDCRVGGPELAQNAVAQG 301
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
290-500 |
2.32e-13 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 72.49 E-value: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 290 LLAIGRDSCTRKIGLEKIGVKINeKNGKIPVNDVEQTNVPHVYAIGDILDgKPELTPVAIQAGKLLARRLFGVSlEKCDY 369
Cdd:PRK13748 358 LVATGRAPNTRSLALDAAGVTVN-AQGAIVIDQGMRTSVPHIYAAGDCTD-QPQFVYVAAAAGTRAAINMTGGD-AALDL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 370 INIPTTVFTPLEYGCCGLSEEKAiemyKKENLEVyhtlfwplEWTVAGRDNntcYAKIICNkFDNE------------RV 437
Cdd:PRK13748 435 TAMPAVVFTDPQVATVGYSEAEA----HHDGIET--------DSRTLTLDN---VPRALAN-FDTRgfiklvieegsgRL 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 438 VGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPT-------CGEVFTTleitkssglDITQKGCU 500
Cdd:PRK13748 499 IGVQAVAPEAGELIQTAALAIRNRMTVQELADQLFPYLTmveglklAAQTFNK---------DVKQLSCC 559
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
285-479 |
4.02e-13 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 71.32 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 285 IYNTVLLAIGRDSCTRKIGLEKIGVKINEkNGKIPVNDVEQTNVPHVYAIGDIlDGKPELTPVAIQAGKLLARRLFGVS- 363
Cdd:PRK07251 241 RFDALLYATGRKPNTEPLGLENTDIELTE-RGAIKVDDYCQTSVPGVFAVGDV-NGGPQFTYISLDDFRIVFGYLTGDGs 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 364 --LEkcDYINIPTTVFTPLEYGCCGLSEEKAIEM---YKKENLevyhtlfwPLEWTVAGRDNNTCYA--KIICNKfDNER 436
Cdd:PRK07251 319 ytLE--DRGNVPTTMFITPPLSQVGLTEKEAKEAglpYAVKEL--------LVAAMPRAHVNNDLRGafKVVVNT-ETKE 387
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 296010807 437 VVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGE 479
Cdd:PRK07251 388 ILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAE 430
|
|
| GlrX-like_plant |
TIGR02189 |
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ... |
33-121 |
2.53e-12 |
|
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to plants. Multiple isoforms are found in A. thaliana and O.sativa.
Pssm-ID: 274023 [Multi-domain] Cd Length: 99 Bit Score: 62.86 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 33 DLIEGNRVMIFSKSYCPHSTRVKELFSSLGVVYNILELDQVDDGASVQEVLTEISNQKTVPNIFVNKVHVGGCDRTFQAH 112
Cdd:TIGR02189 3 RMVSEKAVVIFSRSSCCMCHVVKRLLLTLGVNPAVHEIDKEPAGKDIENALSRLGCSPAVPAVFVGGKLVGGLENVMALH 82
|
....*....
gi 296010807 113 QNGLLQKLL 121
Cdd:TIGR02189 83 ISGSLVPML 91
|
|
| GrxC |
COG0695 |
Glutaredoxin [Posttranslational modification, protein turnover, chaperones]; |
39-106 |
4.83e-12 |
|
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440459 [Multi-domain] Cd Length: 74 Bit Score: 61.37 E-value: 4.83e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296010807 39 RVMIFSKSYCPHSTRVKELFSSLGVVYNilELDqVDDGASVQEVLTEISNQKTVPNIFVNKVHVGGCD 106
Cdd:COG0695 1 KVTLYTTPGCPYCARAKRLLDEKGIPYE--EID-VDEDPEAREELRERSGRRTVPVIFIGGEHLGGFD 65
|
|
| PRK10638 |
PRK10638 |
glutaredoxin 3; Provisional |
40-122 |
1.26e-11 |
|
glutaredoxin 3; Provisional
Pssm-ID: 182607 [Multi-domain] Cd Length: 83 Bit Score: 60.60 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 40 VMIFSKSYCPHSTRVKELFSSLGVVYNILEldqVDDGASVQEVLTEISNQKTVPNIFVNKVHVGGCDRTFQAHQNGLLQK 119
Cdd:PRK10638 4 VEIYTKATCPFCHRAKALLNSKGVSFQEIP---IDGDAAKREEMIKRSGRTTVPQIFIDAQHIGGCDDLYALDARGGLDP 80
|
...
gi 296010807 120 LLQ 122
Cdd:PRK10638 81 LLK 83
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
172-484 |
2.28e-11 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 65.57 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 172 GGTCVNVGCIP-KKLMHqaallghalqDAKKYGweynqqvkhnweAMTEAIQ--SHIGSLnwgyrvtLREKG-------- 240
Cdd:NF040477 40 GGTCINIGCIPtKTLVH----------DAEQHQ------------DFSTAMQrkSSVVGF-------LRDKNyhnladld 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 241 -VTYVNSFGEFVDLHKIKVQQLE-----------------------------------------KGLPGKLKV------- 271
Cdd:NF040477 91 nVDVINGRAEFIDNHTLRVFQADgeqelrgekifintgaqsvlppipgltttpgvydstgllnlTQLPARLGIlgggyig 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 272 ----------------------------------VAK-------------------STEGP---ETVEGIY--NTVLLAI 293
Cdd:NF040477 171 vefasmfarfgskvtifeaaelflpredrdiaqaIATilqdqgvelilnaqvqrvsSHEGEvqlETAEGVLtvDALLVAS 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 294 GRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNVPHVYAIGDIlDGKPELTPVAIQAGKLLARRLFGVSLEKC-DYINI 372
Cdd:NF040477 251 GRKPATAGLQLQNAGVAVNER-GAIVVDKYLRTTADNIWAMGDV-TGGLQFTYISLDDFRIVRDSLLGEGKRSTdDRQNV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 373 PTTVFTPLEYGCCGLSEEKAIEmyKKENLEVYhTLfwPLEWTVAGR---DNNTCYAKIICNKfdNERVVGFHLLGPNAGE 449
Cdd:NF040477 329 PYSVFMTPPLSRIGMTEEQARA--SGADIQVV-TL--PVAAIPRARvmnDTRGVLKAVVDNK--TQRILGVSLLCVDSHE 401
|
410 420 430
....*....|....*....|....*....|....*
gi 296010807 450 ITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 484
Cdd:NF040477 402 MINIVKTVMDAGLPYTVLRDQIFTHPTMSESLNDL 436
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
236-484 |
2.79e-10 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 62.34 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 236 LREKGVTYV-NSFGEFVDLHKIKVQqlekglpgklkvvAKSTEGPETVEGIyntvLLAIGRDSCTRKIGLEKIGVKINEK 314
Cdd:PRK08010 209 LRDQGVDIIlNAHVERISHHENQVQ-------------VHSEHAQLAVDAL----LIASGRQPATASLHPENAGIAVNER 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 315 nGKIPVNDVEQTNVPHVYAIGDILDGKpELTPVAIQAGKLLARRLFGVSLEKC-DYINIPTTVFTPLEYGCCGLSEEKAi 393
Cdd:PRK08010 272 -GAIVVDKYLHTTADNIWAMGDVTGGL-QFTYISLDDYRIVRDELLGEGKRSTdDRKNVPYSVFMTPPLSRVGMTEEQA- 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 394 emykKENLEVYHTLFWPLEWTVAGR---DNNTCYAKIICNKfdNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDT 470
Cdd:PRK08010 349 ----RESGADIQVVTLPVAAIPRARvmnDTRGVLKAIVDNK--TQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQ 422
|
250
....*....|....
gi 296010807 471 IGIHPTCGEVFTTL 484
Cdd:PRK08010 423 IFTHPSMSESLNDL 436
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
165-480 |
7.31e-10 |
|
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and related species, can form a disulfide-linked dimer called mycothione. This enzyme can reduce mycothione to regenerate two mycothiol molecules. The enzyme shows some sequence similarity to glutathione-disulfide reductase, trypanothione-disulfide reductase, and dihydrolipoamide dehydrogenase. The characterized protein from M. tuberculosis, a homodimer, has FAD as a cofactor, one per monomer, and uses NADPH as a substrate.
Pssm-ID: 132493 [Multi-domain] Cd Length: 452 Bit Score: 60.93 E-value: 7.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 165 QGTtwgLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGweYNQQVKH-NWEAMTEAIQSH----IGSLNWGYRVTLREK 239
Cdd:TIGR03452 31 KGT---FGGTCLNVGCIPTKMFVYAAEVAQSIGESARLG--IDAEIDSvRWPDIVSRVFGDridpIAAGGEDYRRGDETP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 240 GVTYVNSFGEFVDLHKIKVQQLEK-------------------------------------------------------- 263
Cdd:TIGR03452 106 NIDVYDGHARFVGPRTLRTGDGEEitgdqiviaagsrpyippaiadsgvryhtnedimrlpelpeslvivgggyiaaefa 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 264 ----GLPGKLKVVAKS-------------------------------TEGPETVEGIY-----------NTVLLAIGRDS 297
Cdd:TIGR03452 186 hvfsALGTRVTIVNRStkllrhldedisdrfteiakkkwdirlgrnvTAVEQDGDGVTltlddgstvtaDVLLVATGRVP 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 298 CTRKIGLEKIGVKINEkNGKIPVNDVEQTNVPHVYAIGDIldGKP-ELTPVAIQAGKLLARRLFG-VSLEKCDYINIPTT 375
Cdd:TIGR03452 266 NGDLLDAEAAGVEVDE-DGRIKVDEYGRTSARGVWALGDV--SSPyQLKHVANAEARVVKHNLLHpNDLRKMPHDFVPSA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 376 VFTPLEYGCCGLSEEKAIEMYKKENLEV--YHTLF--WPLEWTvagrdnnTCYAKIICNKfDNERVVGFHLLGPNAGEIT 451
Cdd:TIGR03452 343 VFTHPQIATVGLTEQEAREAGHDITVKIqnYGDVAygWAMEDT-------TGFCKLIADR-DTGKLLGAHIIGPQASSLI 414
|
410 420 430
....*....|....*....|....*....|
gi 296010807 452 QGFAAAMKCGLT-KQLLDDTIGIHPTCGEV 480
Cdd:TIGR03452 415 QPLITAMAFGLDaREMARKQYWIHPALPEV 444
|
|
| GRX_PICOT_like |
cd03028 |
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ... |
33-118 |
4.25e-09 |
|
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of PICOT and GRX-PICOT-like proteins. The non-PICOT members of this family contain only the GRX-like domain, whereas PICOT contains an N-terminal TRX-like domain followed by one to three GRX-like domains. It is interesting to note that PICOT from plants contain three repeats of the GRX-like domain, metazoan proteins (except for insect) have two repeats, while fungal sequences contain only one copy of the domain. PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli. Both GRX and TRX domains of PICOT are required for its activity. Characterized non-PICOT members of this family include CXIP1, a CAX-interacting protein in Arabidopsis thaliana, and PfGLP-1, a GRX-like protein from Plasmodium falciparum.
Pssm-ID: 239326 Cd Length: 90 Bit Score: 53.65 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 33 DLIEGNRVMIFSKSY-----CPHSTRVKELFSSLGVVY---NILEldqvDDgaSVQEVLTEISNQKTVPNIFVNKVHVGG 104
Cdd:cd03028 3 KLIKENPVVLFMKGTpeeprCGFSRKVVQILNQLGVDFgtfDILE----DE--EVRQGLKEYSNWPTFPQLYVNGELVGG 76
|
90
....*....|....
gi 296010807 105 CDRTFQAHQNGLLQ 118
Cdd:cd03028 77 CDIVKEMHESGELQ 90
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
271-336 |
4.56e-08 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 55.25 E-value: 4.56e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296010807 271 VVAKSTEGpETVEGIYntVLLAIGRDSCTRKIGLEKIGVKINEkNGKIPVNDVEQTNVPHVYAIGD 336
Cdd:PRK07845 251 VVVTLTDG-RTVEGSH--ALMAVGSVPNTAGLGLEEAGVELTP-SGHITVDRVSRTSVPGIYAAGD 312
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
236-385 |
6.40e-08 |
|
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: 54.43 E-value: 6.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 236 LREKGVTYVnsFGEfvdlhkiKVQQLEkglpGKLKVVAKSTEGpETVEgiYNTVLLAIGrdsctrkIG-----LEKIGVK 310
Cdd:COG0446 175 LREHGVELR--LGE-------TVVAID----GDDKVAVTLTDG-EEIP--ADLVVVAPG-------VRpntelAKDAGLA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 311 INEKNGkIPVNDVEQTNVPHVYAIGD------ILDGKPELTP---VAIQAGKLLARRLFGVSLEkcdYINIPTTVFTPle 381
Cdd:COG0446 232 LGERGW-IKVDETLQTSDPDVYAAGDcaevphPVTGKTVYIPlasAANKQGRVAAENILGGPAP---FPGLGTFISKV-- 305
|
....
gi 296010807 382 YGCC 385
Cdd:COG0446 306 FDLC 309
|
|
| GRX_hybridPRX5 |
cd03029 |
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ... |
40-106 |
9.33e-08 |
|
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing peroxiredoxin (PRX) and GRX domains, which is found in some pathogenic bacteria and cyanobacteria. PRXs are thiol-specific antioxidant (TSA) proteins that confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins. PRX-GRX hybrid proteins from Haemophilus influenza and Neisseria meningitis exhibit GSH-dependent peroxidase activity. The flow of reducing equivalents in the catalytic cycle of the hybrid protein goes from NADPH -> GSH reductase -> GSH -> GRX domain of hybrid -> PRX domain of hybrid -> peroxide substrate.
Pssm-ID: 239327 [Multi-domain] Cd Length: 72 Bit Score: 49.05 E-value: 9.33e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296010807 40 VMIFSKSYCPHSTRVKELFSSLGVVYNILELDQVDDGASVQEVlteiSNQKTVPNIFVNKVHVGGCD 106
Cdd:cd03029 3 VSLFTKPGCPFCARAKAALQENGISYEEIPLGKDITGRSLRAV----TGAMTVPQVFIDGELIGGSD 65
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
241-352 |
3.69e-07 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 51.66 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 241 VTYVNSFGEFvDLHKIKVQQLEKgLPgKLKVVAKST----EGPETVEGI--------------YNTVLLAIGRDSCTRki 302
Cdd:COG0492 167 VTLIHRRDEL-RASKILVERLRA-NP-KIEVLWNTEvteiEGDGRVEGVtlknvktgeekeleVDGVFVAIGLKPNTE-- 241
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 296010807 303 GLEKIGVKINEkNGKIPVNDVEQTNVPHVYAIGDILDGKPELTPVAIQAG 352
Cdd:COG0492 242 LLKGLGLELDE-DGYIVVDEDMETSVPGVFAAGDVRDYKYRQAATAAGEG 290
|
|
| GRX_DEP |
cd03027 |
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ... |
39-104 |
4.38e-07 |
|
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of uncharacterized proteins containing a GRX domain and additional domains DEP and DUF547, both of which have unknown functions. GRX is a glutathione (GSH) dependent reductase containing a redox active CXXC motif in a TRX fold. It has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. By altering the redox state of target proteins, GRX is involved in many cellular functions.
Pssm-ID: 239325 [Multi-domain] Cd Length: 73 Bit Score: 47.41 E-value: 4.38e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296010807 39 RVMIFSKSYCPHSTRVKELFSSLGVVYniLELDqVDDGASVQEVLTEISNQKTVPNIFVNKVHVGG 104
Cdd:cd03027 2 RVTIYSRLGCEDCTAVRLFLREKGLPY--VEIN-IDIFPERKAELEERTGSSVVPQIFFNEKLVGG 64
|
|
| grxA |
PRK11200 |
glutaredoxin 1; Provisional |
40-112 |
4.48e-06 |
|
glutaredoxin 1; Provisional
Pssm-ID: 183036 [Multi-domain] Cd Length: 85 Bit Score: 44.64 E-value: 4.48e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296010807 40 VMIFSKSYCPHSTRVKELFSSLGVV---YNILELDQVDDGASVQEVLTEISNQ-KTVPNIFVNKVHVGGCDRtFQAH 112
Cdd:PRK11200 3 VVIFGRPGCPYCVRAKELAEKLSEErddFDYRYVDIHAEGISKADLEKTVGKPvETVPQIFVDQKHIGGCTD-FEAY 78
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
262-467 |
4.60e-06 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 48.88 E-value: 4.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 262 EKGLPGKLKVVAKSTEGPETVEGI------YNT--VLLAIGRDSCTRKI---GLEKIgvkineKNGKIPVNDVEQTNVPH 330
Cdd:PRK09564 203 ENGVELHLNEFVKSLIGEDKVEGVvtdkgeYEAdvVIVATGVKPNTEFLedtGLKTL------KNGAIIVDEYGETSIEN 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 331 VYAIGD------ILDGKPELTPVAIQAGKLlaRRLFGVSLEKCDYINIPT------TVFTpLEYGCCGLSEEKAiemyKK 398
Cdd:PRK09564 277 IYAAGDcatiynIVSNKNVYVPLATTANKL--GRMVGENLAGRHVSFKGTlgsaciKVLD-LEAARTGLTEEEA----KK 349
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296010807 399 ENLEVY--------HTLFWPlewtvagrDNNTCYAKIICNKfDNERVVGFHLLGPNAGEI-TQGFAAAMKCGLTKQLL 467
Cdd:PRK09564 350 LGIDYKtvfikdknHTNYYP--------GQEDLYVKLIYEA-DTKVILGGQIIGKKGAVLrIDALAVAIYAKLTTQEL 418
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
289-361 |
3.05e-05 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 46.29 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 289 VLLAIG---RDSCTRKIGLEkigvkINekNGkIPVNDVEQTNVPHVYAIGDI------LDGKP--ELTPVAIQAGKLLAR 357
Cdd:COG1251 232 VVVAIGvrpNTELARAAGLA-----VD--RG-IVVDDYLRTSDPDIYAAGDCaehpgpVYGRRvlELVAPAYEQARVAAA 303
|
....
gi 296010807 358 RLFG 361
Cdd:COG1251 304 NLAG 307
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
256-357 |
3.56e-05 |
|
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: 46.28 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 256 IKVQQLEKGLP---GKLKVVAKstEGPE-TVEGiyNTVLLAIGRDSCTRKIgLEKIGVKINeKNGKIPVNDVE-QTNVPH 330
Cdd:COG0493 330 LECVRMELGEPdesGRRRPVPI--EGSEfTLPA--DLVILAIGQTPDPSGL-EEELGLELD-KRGTIVVDEETyQTSLPG 403
|
90 100
....*....|....*....|....*..
gi 296010807 331 VYAIGDILDGkPELTPVAIQAGKLLAR 357
Cdd:COG0493 404 VFAGGDAVRG-PSLVVWAIAEGRKAAR 429
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
304-361 |
9.10e-05 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 44.77 E-value: 9.10e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296010807 304 LEKIGVKINEKnGKIPVNDVEQTNVPHVYAIGDILDG------KPELTPVAI---QAGKLLARRLFG 361
Cdd:PRK13512 246 IESSNIKLDDK-GFIPVNDKFETNVPNIYAIGDIITShyrhvdLPASVPLAWgahRAASIVAEQIAG 311
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
144-483 |
2.19e-04 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 43.75 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 144 AKEAANLGKKVMVLdfvvpspQGTTWGLGGTCVNVGCIPKKLMHQAA----------------LLGHALQDAKKYGWEYN 207
Cdd:PTZ00153 132 AINAMERGLKVIIF-------TGDDDSIGGTCVNVGCIPSKALLYATgkyrelknlaklytygIYTNAFKNGKNDPVERN 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 208 Q----QVKHNWEAMTEAIQSHIGSLNWGYRVTLREKGV------------------------------------------ 241
Cdd:PTZ00153 205 QlvadTVQIDITKLKEYTQSVIDKLRGGIENGLKSKKFcknsehvqviyerghivdkntikseksgkefkvkniiiatgs 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 242 ----------------------------TYVNSFG------EFVDLHKI---KVQQLEKG---LPGKLKVVAK------- 274
Cdd:PTZ00153 285 tpnipdnievdqksvftsdtavkleglqNYMGIVGmgiiglEFMDIYTAlgsEVVSFEYSpqlLPLLDADVAKyfervfl 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 275 -------------------------------STEGPETVEGIYNT---------VLLAIGRDSCTRKIGLEKIGVKINEk 314
Cdd:PTZ00153 365 kskpvrvhlntlieyvragkgnqpviighseRQTGESDGPKKNMNdiketyvdsCLVATGRKPNTNNLGLDKLKIQMKR- 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 315 nGKIPVND---VEQTN---VPHVYAIGDIlDGKPELTPVA-IQA-----------GKLLARRLFGVSLEKCDYINIPTTV 376
Cdd:PTZ00153 444 -GFVSVDEhlrVLREDqevYDNIFCIGDA-NGKQMLAHTAsHQAlkvvdwiegkgKENVNINVENWASKPIIYKNIPSVC 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 377 FTPLEYGCCGLSEEKAIEMYKKENL--EVYH-----TLFWPLEWTVAGRDNNTCYAKIICNKFDN-------------ER 436
Cdd:PTZ00153 522 YTTPELAFIGLTEKEAKELYPPDNVgvEISFykansKVLCENNISFPNNSKNNSYNKGKYNTVDNtegmvkivylkdtKE 601
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 296010807 437 VVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTT 483
Cdd:PTZ00153 602 ILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDA 648
|
|
| NrdH |
cd02976 |
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ... |
39-104 |
3.63e-04 |
|
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active CXXC motif within a TRX fold, characterized by a glutaredoxin (GRX)-like sequence and TRX-like activity profile. In vitro, it displays protein disulfide reductase activity that is dependent on TRX reductase, not glutathione (GSH). It is part of the NrdHIEF operon, where NrdEF codes for class Ib ribonucleotide reductase (RNR-Ib), an efficient enzyme at low oxygen levels. Under these conditions when GSH is mostly conjugated to spermidine, NrdH can still function and act as a hydrogen donor for RNR-Ib. It has been suggested that the NrdHEF system may be the oldest RNR reducing system, capable of functioning in a microaerophilic environment, where GSH was not yet available. NrdH from Corynebacterium ammoniagenes can form domain-swapped dimers, although it is unknown if this happens in vivo. Domain-swapped dimerization, which results in the blocking of the TRX reductase binding site, could be a mechanism for regulating the oxidation state of the protein.
Pssm-ID: 239274 [Multi-domain] Cd Length: 73 Bit Score: 39.13 E-value: 3.63e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296010807 39 RVMIFSKSYCPHSTRVKELFSSLGVVYNilELDqVDDGASVQEVLTEISNQKTVPNIFVNKVHVGG 104
Cdd:cd02976 1 EVTVYTKPDCPYCKATKRFLDERGIPFE--EVD-VDEDPEALEELKKLNGYRSVPVVVIGDEHLSG 63
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
304-393 |
1.37e-03 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 40.89 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 304 LEKIGVKINEKnGKIPVNDVEQT-NVPHVYAIGD---ILDGKPELTP----VAIQAGKLLARRLFGVSLEKcdyiniPTT 375
Cdd:COG1252 259 LADLGLPTDRR-GRVLVDPTLQVpGHPNVFAIGDcaaVPDPDGKPVPktaqAAVQQAKVLAKNIAALLRGK------PLK 331
|
90
....*....|....*....
gi 296010807 376 VFTPLEYGC-CGLSEEKAI 393
Cdd:COG1252 332 PFRYRDKGClASLGRGAAV 350
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
256-356 |
1.42e-03 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 40.93 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 256 IKVQQLEKGLPGKlkvvakSTEGPETVEGIY-----NTVLLAIGRDSCTRKIGLEKiGVKINEKNGKIPVNDVEQTNVPH 330
Cdd:PRK11749 347 VEFVRMELGEPDA------SGRRRVPIEGSEftlpaDLVIKAIGQTPNPLILSTTP-GLELNRWGTIIADDETGRTSLPG 419
|
90 100
....*....|....*....|....*.
gi 296010807 331 VYAIGDILDGkPELTPVAIQAGKLLA 356
Cdd:PRK11749 420 VFAGGDIVTG-AATVVWAVGDGKDAA 444
|
|
| GRXA |
TIGR02183 |
Glutaredoxin, GrxA family; Glutaredoxins are thioltransferases (disulfide reductases) which ... |
40-105 |
2.23e-03 |
|
Glutaredoxin, GrxA family; Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress, reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This model includes the E. coli glyutaredoxin GrxA which appears to have primary responsibility for the reduction of ribonucleotide reductase.
Pssm-ID: 131238 [Multi-domain] Cd Length: 86 Bit Score: 37.11 E-value: 2.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 40 VMIFSKSYCPHSTRVKELFSSLGVVYNILELDQVD---DGASVQEVLTEISNQ-KTVPNIFVNKVHVGGC 105
Cdd:TIGR02183 2 VVIFGRPGCPYCVRAKQLAEKLAIERADFEFRYIDihaEGISKADLEKTVGKPvETVPQIFVDEKHVGGC 71
|
|
| PTZ00062 |
PTZ00062 |
glutaredoxin; Provisional |
34-124 |
5.07e-03 |
|
glutaredoxin; Provisional
Pssm-ID: 240250 [Multi-domain] Cd Length: 204 Bit Score: 38.24 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010807 34 LIEGNRVMIFSKS-----YCPHSTRVKELFSSLGV---VYNILElDQvddgaSVQEVLTEISNQKTVPNIFVNKVHVGGC 105
Cdd:PTZ00062 109 LIRNHKILLFMKGsktfpFCRFSNAVVNMLNSSGVkyeTYNIFE-DP-----DLREELKVYSNWPTYPQLYVNGELIGGH 182
|
90
....*....|....*....
gi 296010807 106 DRTFQAHQNGLLQKLLQDD 124
Cdd:PTZ00062 183 DIIKELYESNSLRKVIPDD 201
|
|
| PHA03050 |
PHA03050 |
glutaredoxin; Provisional |
35-104 |
5.85e-03 |
|
glutaredoxin; Provisional
Pssm-ID: 165343 [Multi-domain] Cd Length: 108 Bit Score: 36.53 E-value: 5.85e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296010807 35 IEGNRVMIFSKSYCPHSTRVKELFSSLGV---VYNILELDQVDDGASVQEVLTEISNQKTVPNIFVNKVHVGG 104
Cdd:PHA03050 10 LANNKVTIFVKFTCPFCRNALDILNKFSFkrgAYEIVDIKEFKPENELRDYFEQITGGRTVPRIFFGKTSIGG 82
|
|
| |
