|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02546 |
PLN02546 |
glutathione reductase |
44-545 |
0e+00 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 1051.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 44 RRRTFIVRAESQNGADPvPAHYDFDLFTIGAGSGGVRAARFAANYGASVAICELPFSTISSETTGGVGGTCVIRGCVPKK 123
Cdd:PLN02546 58 HRRRSVSRAAAPNGAES-ERHYDFDLFTIGAGSGGVRASRFASNFGASAAVCELPFATISSDTLGGVGGTCVLRGCVPKK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 124 LLVYASKFSHEFEESNGFGWRYDSEPKHDWSSFIANKNAELQRLTGIYKNILNNAGVKLIEGHGKIIDPHTVDVNGKLYS 203
Cdd:PLN02546 137 LLVYASKYSHEFEESRGFGWKYETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDVDGKLYT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 204 AKHILVAVGGRPFIPDIPGKEYAIDSDAALDLPTKPVKIAIVGGGYIALEFAGIFNGLKSEVHVFIRQKKVLRGFDEEIR 283
Cdd:PLN02546 217 ARNILIAVGGRPFIPDIPGIEHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKKVLRGFDEEVR 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 284 DFVEEQMSVRGIEFHTEESPQAITKSADGSFSLKTNKGTVDGFSHIMFATGRRPNTQNLGLESVGVKLAKDGAIEVDEYS 363
Cdd:PLN02546 297 DFVAEQMSLRGIEFHTEESPQAIIKSADGSLSLKTNKGTVEGFSHVMFATGRKPNTKNLGLEEVGVKMDKNGAIEVDEYS 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 364 QTSVSSIWAVGDVTNRINLTPVALMEGGALVKTLFQDNPTKPDYRAVPSAVFSQPPIGQVGLTEEQAVQQYGDIDIFTAN 443
Cdd:PLN02546 377 RTSVPSIWAVGDVTDRINLTPVALMEGGALAKTLFGNEPTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYGDVDVFTAN 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 444 FRPLKATLSGLPDRVFMKLVVCAKTNEVLGLHMCGEDAPEIVQGFAVALKARLTKADFDATVGIHPSAAEEFVTMRTPTR 523
Cdd:PLN02546 457 FRPLKATLSGLPDRVFMKLIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEEFVTMRTPTR 536
|
490 500
....*....|....*....|..
gi 1199701057 524 KIRKSESSEGKSGSQAKAAAGV 545
Cdd:PLN02546 537 KIRKDSPSEGKTKDEVKAAAGV 558
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
65-519 |
0e+00 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 669.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 65 YDFDLFTIGAGSGGVRAARFAANYGASVAICElpfstissetTGGVGGTCVIRGCVPKKLLVYASKFSHEFEE-SNGFGW 143
Cdd:PRK06116 3 KDYDLIVIGGGSGGIASANRAAMYGAKVALIE----------AKRLGGTCVNVGCVPKKLMWYGAQIAEAFHDyAPGYGF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 144 RYDsEPKHDWSSFIANKNAELQRLTGIYKNILNNAGVKLIEGHGKIIDPHTVDVNGKLYSAKHILVAVGGRPFIPDIPGK 223
Cdd:PRK06116 73 DVT-ENKFDWAKLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNGERYTADHILIATGGRPSIPDIPGA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 224 EYAIDSDAALDLPTKPVKIAIVGGGYIALEFAGIFNGLKSEVHVFIRQKKVLRGFDEEIRDFVEEQMSVRGIEFHTEESP 303
Cdd:PRK06116 152 EYGITSDGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 304 QAITKSADGSFSLKTNKGTVDGFSHIMFATGRRPNTQNLGLESVGVKLAKDGAIEVDEYSQTSVSSIWAVGDVTNRINLT 383
Cdd:PRK06116 232 KAVEKNADGSLTLTLEDGETLTVDCLIWAIGREPNTDGLGLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGDVTGRVELT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 384 PVALMEGGALVKTLFQDNP-TKPDYRAVPSAVFSQPPIGQVGLTEEQAVQQYGD--IDIFTANFRPLKATLSGLPDRVFM 460
Cdd:PRK06116 312 PVAIAAGRRLSERLFNNKPdEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEdnVKVYRSSFTPMYTALTGHRQPCLM 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1199701057 461 KLVVCAKTNEVLGLHMCGEDAPEIVQGFAVALKARLTKADFDATVGIHPSAAEEFVTMR 519
Cdd:PRK06116 392 KLVVVGKEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFVTMR 450
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
46-525 |
0e+00 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 635.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 46 RTFIVRAE-SQNGAD-PVPAHYDFDLFTIGAGSGGVRAARFAANYGASVAICELPFSTISSETTGGVGGTCVIRGCVPKK 123
Cdd:PLN02507 3 RKMLIDGEvAKVNADeANATHYDFDLFVIGAGSGGVRAARFSANFGAKVGICELPFHPISSESIGGVGGTCVIRGCVPKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 124 LLVYASKFSHEFEESNGFGWRYDSEPKHDWSSFIANKNAELQRLTGIYKNILNNAGVKLIEGHGKIIDPHTVDV-----N 198
Cdd:PLN02507 83 ILVYGATFGGEFEDAKNYGWEINEKVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVtqldgT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 199 GKLYSAKHILVAVGGRPFIPDIPGKEYAIDSDAALDLPTKPVKIAIVGGGYIALEFAGIFNGLKSEVHVFIRQKKVLRGF 278
Cdd:PLN02507 163 KLRYTAKHILIATGSRAQRPNIPGKELAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 279 DEEIRDFVEEQMSVRGIEFHTEESPQAITKSADGsFSLKTNKGTVDGFSHIMFATGRRPNTQNLGLESVGVKLAKDGAIE 358
Cdd:PLN02507 243 DDEMRAVVARNLEGRGINLHPRTNLTQLTKTEGG-IKVITDHGEEFVADVVLFATGRAPNTKRLNLEAVGVELDKAGAVK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 359 VDEYSQTSVSSIWAVGDVTNRINLTPVALMEGGALVKTLFQDNPTKPDYRAVPSAVFSQPPIGQVGLTEEQAVQQY-GDI 437
Cdd:PLN02507 322 VDEYSRTNIPSIWAIGDVTNRINLTPVALMEGTCFAKTVFGGQPTKPDYENVACAVFCIPPLSVVGLSEEEAVEQAkGDI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 438 DIFTANFRPLKATLSGLPDRVFMKLVVCAKTNEVLGLHMCGEDAPEIVQGFAVALKARLTKADFDATVGIHPSAAEEFVT 517
Cdd:PLN02507 402 LVFTSSFNPMKNTISGRQEKTVMKLIVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEFVT 481
|
....*...
gi 1199701057 518 MRTPTRKI 525
Cdd:PLN02507 482 MRSVTRRV 489
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
65-519 |
0e+00 |
|
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: 583.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 65 YDFDLFTIGAGSGGVRAARFAANYGASVAICELPFstissettggVGGTCVIRGCVPKKLLVYASKFSHEFEESNGFGWR 144
Cdd:TIGR01424 1 FDYDLFVIGAGSGGVRAARLAAALGAKVAIAEEFR----------VGGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGWT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 145 YDsEPKHDWSSFIANKNAELQRLTGIYKNILNNAGVKLIEGHGKIIDPHTVDV--NGKLYSAKHILVAVGGRPFIPDIPG 222
Cdd:TIGR01424 71 VG-KARFDWKKLLAAKDQEIARLSGLYRKGLANAGAELLDGRAELVGPNTVEVlaSGKTYTAEKILIAVGGRPPKPALPG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 223 KEYAIDSDAALDLPTKPVKIAIVGGGYIALEFAGIFNGLKSEVHVFIRQKKVLRGFDEEIRDFVEEQMSVRGIEFHTEES 302
Cdd:TIGR01424 150 HELGITSNEAFHLPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRGKEILRGFDDDMRRGLAAALEERGIRILPEDS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 303 PQAITKSADGSFSLKTNKGTVDGFSHIMFATGRRPNTQNLGLESVGVKLAKDGAIEVDEYSQTSVSSIWAVGDVTNRINL 382
Cdd:TIGR01424 230 ITSISKDDDGRLKATLSKHEEIVADVVLFATGRSPNTNGLGLEAAGVRLNDLGAIAVDEYSRTSTPSIYAVGDVTDRINL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 383 TPVALMEGGALVKTLFQDNPTKPDYRAVPSAVFSQPPIGQVGLTEEQAVQQYGDIDIFTANFRPLKATLSGLPDRVFMKL 462
Cdd:TIGR01424 310 TPVAIHEATCFAETEFGNNPTSFDHDLIATAVFSQPPIGTVGLTEEEARRKFGDIEVYRAEFRPMKATFSGRQEKTLMKL 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1199701057 463 VVCAKTNEVLGLHMCGEDAPEIVQGFAVALKARLTKADFDATVGIHPSAAEEFVTMR 519
Cdd:TIGR01424 390 VVDAKDDKVLGAHMVGPDAAEIIQGLAIALKMGATKDDFDSTVAVHPTSAEELVTMR 446
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
65-519 |
0e+00 |
|
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: 519.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 65 YDFDLFTIGAGSGGVRAARFAANYGASVAICElpfstissetTGGVGGTCVIRGCVPKKLLVYASKFSHEFEESNGFGWR 144
Cdd:COG1249 2 KDYDLVVIGAGPGGYVAAIRAAQLGLKVALVE----------KGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGIS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 145 YDsEPKHDWSSFIANKNAELQRLTGIYKNILNNAGVKLIEGHGKIIDPHTVDVNG-KLYSAKHILVAVGGRPFIPDIPG- 222
Cdd:COG1249 72 AG-APSVDWAALMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVTGgETLTADHIVIATGSRPRVPPIPGl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 223 -KEYAIDSDAALDLPTKPVKIAIVGGGYIALEFAGIFNGLKSEVHVFIRQKKVLRGFDEEIRDFVEEQMSVRGIEFHTEE 301
Cdd:COG1249 151 dEVRVLTSDEALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 302 SPQAITKSADGsFSLKTNKG---TVDGFSHIMFATGRRPNTQNLGLESVGVKLAKDGAIEVDEYSQTSVSSIWAVGDVTN 378
Cdd:COG1249 231 KVTSVEKTGDG-VTVTLEDGggeEAVEADKVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRTSVPGIYAIGDVTG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 379 RINLTPVALMEGGALVKTLFQDNPTKPDYRAVPSAVFSQPPIGQVGLTEEQAVQQYGDIDIFTANFRPLKATLSGLPDRV 458
Cdd:COG1249 310 GPQLAHVASAEGRVAAENILGKKPRPVDYRAIPSVVFTDPEIASVGLTEEEAREAGIDVKVGKFPFAANGRALALGETEG 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199701057 459 FMKLVVCAKTNEVLGLHMCGEDAPEIVQGFAVALKARLTKADFDATVGIHPSAAEEFVTMR 519
Cdd:COG1249 390 FVKLIADAETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAA 450
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
63-519 |
7.20e-147 |
|
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: 430.03 E-value: 7.20e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 63 AHYDFdlFTIGAGSGGVRAARFAANYGASVAICElpfstissetTGGVGGTCVIRGCVPKKLLVYASKFSHEFEESNGFG 142
Cdd:TIGR01421 1 KHYDY--LVIGGGSGGIASARRAAEHGAKALLVE----------AKKLGGTCVNVGCVPKKVMWYASDLAERMHDAADYG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 143 WRYDSEPKHDWSSFIANKNAELQRLTGIYKNILNNAGVKLIEGHGKIIDPHTVDVNGKLYSAKHILVAVGGRPFIPD-IP 221
Cdd:TIGR01421 69 FYQNDENTFNWPELKEKRDAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVNGRDYTAPHILIATGGKPSFPEnIP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 222 GKEYAIDSDAALDLPTKPVKIAIVGGGYIALEFAGIFNGLKSEVHVFIRQKKVLRGFDEEIRDFVEEQMSVRGIEFHTEE 301
Cdd:TIGR01421 149 GAELGTDSDGFFALEELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRHERVLRSFDSMISETITEEYEKEGINVHKLS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 302 SPQAITKSADGSFSLKTNKG-TVDGFSHIMFATGRRPNTQNLGLESVGVKLAKDGAIEVDEYSQTSVSSIWAVGDVTNRI 380
Cdd:TIGR01421 229 KPVKVEKTVEGKLVIHFEDGkSIDDVDELIWAIGRKPNTKGLGLENVGIKLNEKGQIIVDEYQNTNVPGIYALGDVVGKV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 381 NLTPVALMEGGALVKTLFQDNPT-KPDYRAVPSAVFSQPPIGQVGLTEEQAVQQYG--DIDIFTANFRPLKATLSGLPDR 457
Cdd:TIGR01421 309 ELTPVAIAAGRKLSERLFNGKTDdKLDYNNVPTVVFSHPPIGTIGLTEKEAIEKYGkeNIKVYNSSFTPMYYAMTSEKQK 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199701057 458 VFMKLVVCAKTNEVLGLHMCGEDAPEIVQGFAVALKARLTKADFDATVGIHPSAAEEFVTMR 519
Cdd:TIGR01421 389 CRMKLVCAGKEEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEELVTMR 450
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
67-522 |
1.52e-132 |
|
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: 394.72 E-value: 1.52e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 67 FDLFTIGAGSGGVRAARFAAN-YGASVAICEL------PFstissetTGGVGGTCVIRGCVPKKLLVYASKFSHEFEESN 139
Cdd:TIGR01423 4 FDLVVIGAGSGGLEAGWNAATlYKKRVAVVDVqthhgpPF-------YAALGGTCVNVGCVPKKLMVTGAQYMDTLRESA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 140 GFGWRYDSEP-KHDWSSFIANKNAELQRLTGIYKNILNNA-GVKLIEGHGKIIDPHTV------DVNGKL---YSAKHIL 208
Cdd:TIGR01423 77 GFGWEFDRSSvKANWKALIAAKNKAVLDINKSYEGMFADTeGLTFFLGWGALEDKNVVlvresaDPKSAVkerLQAEHIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 209 VAVGGRPFIPDIPGKEYAIDSDAALDLPTKPVKIAIVGGGYIALEFAGIFNGLKS---EVHVFIRQKKVLRGFDEEIRDF 285
Cdd:TIGR01423 157 LATGSWPQMLGIPGIEHCISSNEAFYLDEPPRRVLTVGGGFISVEFAGIFNAYKPrggKVTLCYRNNMILRGFDSTLRKE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 286 VEEQMSVRGIEFHTEESPQAITKSADGSFSLKTNKGTVDGFSHIMFATGRRPNTQNLGLESVGVKLAKDGAIEVDEYSQT 365
Cdd:TIGR01423 237 LTKQLRANGINIMTNENPAKVTLNADGSKHVTFESGKTLDVDVVMMAIGRVPRTQTLQLDKVGVELTKKGAIQVDEFSRT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 366 SVSSIWAVGDVTNRINLTPVALMEGGALVKTLFQDNPTKPDYRAVPSAVFSQPPIGQVGLTEEQAVQQYGDIDIFTANFR 445
Cdd:TIGR01423 317 NVPNIYAIGDVTDRVMLTPVAINEGAAFVDTVFGNKPRKTDHTRVASAVFSIPPIGTCGLVEEDAAKKFEKVAVYESSFT 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199701057 446 PLKATLSGLPDRVFM-KLVVCAKTNEVLGLHMCGEDAPEIVQGFAVALKARLTKADFDATVGIHPSAAEEFVTMRTPT 522
Cdd:TIGR01423 397 PLMHNISGSKYKKFVaKIVTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAEELCSMRTPS 474
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
65-523 |
2.75e-126 |
|
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: 378.43 E-value: 2.75e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 65 YDFDLFTIGAGSGGVRAARFAANYGASVAIceLPFSTISSE-TTGGVGGTCVIRGCVPKKLLVYASKFSHEFEESNGFGW 143
Cdd:TIGR01438 1 YDYDLIVIGGGSGGLAAAKEAAAYGAKVML--LDFVTPTPLgTRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 144 RYDSEPKHDWSSFIANKNAELQRLTGIYKNILNNAGVKLIEGHGKIIDPHTV---DVNGK--LYSAKHILVAVGGRPFIP 218
Cdd:TIGR01438 79 KVEETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIkatNKKGKekIYSAERFLIATGERPRYP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 219 DIPG-KEYAIDSDAALDLPTKPVKIAIVGGGYIALEFAGIFNGLKSEVHVFIRQkKVLRGFDEEIRDFVEEQMSVRGIEF 297
Cdd:TIGR01438 159 GIPGaKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRS-ILLRGFDQDCANKVGEHMEEHGVKF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 298 HTEESPQAITKSADGSFSLKTNK--GTVDGFSHIMFATGRRPNTQNLGLESVGVKL-AKDGAIEVDEYSQTSVSSIWAVG 374
Cdd:TIGR01438 238 KRQFVPIKVEQIEAKVLVEFTDStnGIEEEYDTVLLAIGRDACTRKLNLENVGVKInKKTGKIPADEEEQTNVPYIYAVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 375 DVT-NRINLTPVALMEGGALVKTLFQDNPTKPDYRAVPSAVFSQPPIGQVGLTEEQAVQQYGD--IDIFTANFRPLKATL 451
Cdd:TIGR01438 318 DILeDKPELTPVAIQAGRLLAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAVEKFGEenVEVFHSYFWPLEWTI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199701057 452 SGLPD--RVFMKLVVCAKTNE-VLGLHMCGEDAPEIVQGFAVALKARLTKADFDATVGIHPSAAEEFVTMRTPTR 523
Cdd:TIGR01438 398 PSRDNhnKCYAKLVCNKKENErVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTLSVTKR 472
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
66-513 |
1.14e-113 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 345.24 E-value: 1.14e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 66 DFDLFTIGAGSGGVRAARFAANYGASVAICElpfstissettGGV-GGTCVIRGCVPKKLLVYASKFSHEFEESNGFGWR 144
Cdd:PRK06292 3 KYDVIVIGAGPAGYVAARRAAKLGKKVALIE-----------KGPlGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 145 YDSePKHDWSSFIANKNAELQRLT-GIYKNILNNAGVKLIEGHGKIIDPHTVDVNGKLYSAKHILVAVGGRpfIPDIPGK 223
Cdd:PRK06292 72 ADG-PKIDFKKVMARVRRERDRFVgGVVEGLEKKPKIDKIKGTARFVDPNTVEVNGERIEAKNIVIATGSR--VPPIPGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 224 EYA-----IDSDAALDLPTKPVKIAIVGGGYIALEFAGIFNGLKSEVHVFIRQKKVLRGFDEEIRDFVEEQMSvRGIEFH 298
Cdd:PRK06292 149 WLIlgdrlLTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILS-KEFKIK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 299 TEESPQAITKSADGSFSL--KTNKGTVDGFSHIMFATGRRPNTQNLGLESVGVKLAKDGAIEVDEYSQTSVSSIWAVGDV 376
Cdd:PRK06292 228 LGAKVTSVEKSGDEKVEEleKGGKTETIEADYVLVATGRRPNTDGLGLENTGIELDERGRPVVDEHTQTSVPGIYAAGDV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 377 TNRINLTPVALMEGGALVKTLFQDNPTKPDYRAVPSAVFSQPPIGQVGLTEEQAVQQYGDIDIFTANFRPL-KATLSGLp 455
Cdd:PRK06292 308 NGKPPLLHEAADEGRIAAENAAGDVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEVPFEAQgRARVMGK- 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199701057 456 DRVFMKLVVCAKTNEVLGLHMCGEDAPEIVQGFAVALKARLTKADFDATVGIHPSAAE 513
Cdd:PRK06292 387 NDGFVKVYADKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSE 444
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
66-518 |
5.34e-105 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 326.19 E-value: 5.34e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 66 DFDLFTIGAGSGGVRAARFAANYGASVAICELPFstissettggVGGTCVIRGCVPKKLLVYASKFSHEFEESNGFGwrY 145
Cdd:PTZ00058 48 VYDLIVIGGGSGGMAAARRAARNKAKVALVEKDY----------LGGTCVNVGCVPKKIMFNAASIHDILENSRHYG--F 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 146 DSEPKHDWSSFIANKNAELQRLTGIYKNILNNAGVKLIEGHGKIIDPHTVDV---------------------------- 197
Cdd:PTZ00058 116 DTQFSFNLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLIkkvsqvdgeadesdddevtivsagvsql 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 198 -NGKLYSAKHILVAVGGRPFIPDIPGKEYAIDSDAALDLpTKPVKIAIVGGGYIALEFAGIFNGLKSEVHVFIRQKKVLR 276
Cdd:PTZ00058 196 dDGQVIEGKNILIAVGNKPIFPDVKGKEFTISSDDFFKI-KEAKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLR 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 277 GFDEEIRDFVEEQMSVRGIEFHTEESPQAITK-SADGSFSLKTNKGTVDGFSHIMFATGRRPNTQNLGLESVGVKLAKdG 355
Cdd:PTZ00058 275 KFDETIINELENDMKKNNINIITHANVEEIEKvKEKNLTIYLSDGRKYEHFDYVIYCVGRSPNTEDLNLKALNIKTPK-G 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 356 AIEVDEYSQTSVSSIWAVGDV----------------------------------TNRINLTPVALMEGGALVKTLFQDN 401
Cdd:PTZ00058 354 YIKVDDNQRTSVKHIYAVGDCcmvkknqeiedlnllklyneepylkkkentsgesYYNVQLTPVAINAGRLLADRLFGPF 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 402 PTKPDYRAVPSAVFSQPPIGQVGLTEEQAVQQYG--DIDIFTANFRPLKATLSGL----PDRVFMKLVVCAKTNEVLGLH 475
Cdd:PTZ00058 434 SRTTNYKLIPSVIFSHPPIGTIGLSEQEAIDIYGkeNVKIYESRFTNLFFSVYDMdpaqKEKTYLKLVCVGKEELIKGLH 513
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1199701057 476 MCGEDAPEIVQGFAVALKARLTKADFDATVGIHPSAAEEFVTM 518
Cdd:PTZ00058 514 IVGLNADEILQGFAVALKMNATKADFDETIPIHPTAAEEFVTM 556
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
65-515 |
4.14e-103 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 319.46 E-value: 4.14e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 65 YDFDLFTIGAGSGGVRAARFAANYGASVAIcelpFSTISSETTG---GVGGTCVIRGCVPKKLLVYASKFSHEFE-ESNG 140
Cdd:PTZ00052 4 FMYDLVVIGGGSGGMAAAKEAAAHGKKVAL----FDYVKPSTQGtkwGLGGTCVNVGCVPKKLMHYAANIGSIFHhDSQM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 141 FGWRYDSepKHDWSSFIANKNAELQRLTGIYKNILNNAGVKLIEGHGKIIDPHTV---DVNG-KLYSAKHILVAVGGRPF 216
Cdd:PTZ00052 80 YGWKTSS--SFNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTVsygDNSQeETITAKYILIATGGRPS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 217 IP-DIPG-KEYAIDSDAALDLPTKPVKIAIVGGGYIALEFAGIFNGLKSEVHVFIRQKkVLRGFDEEIRDFVEEQMSVRG 294
Cdd:PTZ00052 158 IPeDVPGaKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRSI-PLRGFDRQCSEKVVEYMKEQG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 295 IEFHTEESPQAITKSADgSFSLKTNKGTVDGFSHIMFATGRRPNTQNLGLESVGVKLAKDGAIEVDEYSqTSVSSIWAVG 374
Cdd:PTZ00052 237 TLFLEGVVPINIEKMDD-KIKVLFSDGTTELFDTVLYATGRKPDIKGLNLNAIGVHVNKSNKIIAPNDC-TNIPNIFAVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 375 DVT-NRINLTPVALMEGGALVKTLFQDNPTKPDYRAVPSAVFSQPPIGQVGLTEEQAVQQYG--DIDIFTANFRPLKATL 451
Cdd:PTZ00052 315 DVVeGRPELTPVAIKAGILLARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGedDIEEYLQEFNTLEIAA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 452 S---------------GLPDRVFMKLVvCAKT--NEVLGLHMCGEDAPEIVQGFAVALKARLTKADFDATVGIHPSAAEE 514
Cdd:PTZ00052 395 VhrekherarkdeydfDVSSNCLAKLV-CVKSedNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHPTDAEV 473
|
.
gi 1199701057 515 F 515
Cdd:PTZ00052 474 F 474
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
67-513 |
7.24e-99 |
|
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: 306.88 E-value: 7.24e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 67 FDLFTIGAGSGGVRAARFAANYGASVAICELPFstissettggVGGTCVIRGCVPKKLLVYASKFSHEFEESNGFGWRYD 146
Cdd:TIGR01350 2 YDVIVIGGGPGGYVAAIRAAQLGLKVALVEKEY----------LGGTCLNVGCIPTKALLHSAEVYDEIKHAKDLGIEVE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 147 SePKHDWSSFIANKNAELQRLTGIYKNILNNAGVKLIEGHGKIIDPHTVDVNGK----LYSAKHILVAVGGRPFIPDIP- 221
Cdd:TIGR01350 72 N-VSVDWEKMQKRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGEngeeTLEAKNIIIATGSRPRSLPGPf 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 222 --GKEYAIDSDAALDLPTKPVKIAIVGGGYIALEFAGIFNGLKSEVHVFIRQKKVLRGFDEEIRDFVEEQMSVRGIEFHT 299
Cdd:TIGR01350 151 dfDGKVVITSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 300 EESPQAITKSADGSFSL--KTNKGTVDGfSHIMFATGRRPNTQNLGLESVGVKLAKDGAIEVDEYSQTSVSSIWAVGDVT 377
Cdd:TIGR01350 231 NTKVTAVEKNDDQVTYEnkGGETETLTG-EKVLVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDVI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 378 NRINLTPVALMEGGALVKTLFQDNPTKPDYRAVPSAVFSQPPIGQVGLTEEQAVQQYGDIDIFTANFRPL-KATLSGLPD 456
Cdd:TIGR01350 310 GGPMLAHVASHEGIVAAENIAGKEPAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGYDVKIGKFPFAANgKALALGETD 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1199701057 457 RvFMKLVVCAKTNEVLGLHMCGEDAPEIVQGFAVALKARLTKADFDATVGIHPSAAE 513
Cdd:TIGR01350 390 G-FVKIIADKKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSE 445
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
66-513 |
8.34e-98 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 304.38 E-value: 8.34e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 66 DFDLFTIGAGSGGVRAARFAANYGASVAICElpfstissetTGGVGGTCVIRGCVPKKLLVYASKFSHEFEESNGFGWRY 145
Cdd:PRK06416 4 EYDVIVIGAGPGGYVAAIRAAQLGLKVAIVE----------KEKLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIKA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 146 DSEpKHDWSSFIANKNAELQRLTGIYKNILNNAGVKLIEGHGKIIDPHTVDVN----GKLYSAKHILVAVGGRPF-IPDI 220
Cdd:PRK06416 74 ENV-GIDFKKVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMtedgEQTYTAKNIILATGSRPReLPGI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 221 -PGKEYAIDSDAALDLPTKPVKIAIVGGGYIALEFAGIFNGLKSEVHVFIRQKKVLRGFDEEIRDFVEEQMSVRGIEFHT 299
Cdd:PRK06416 153 eIDGRVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPGEDKEISKLAERALKKRGIKIKT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 300 EESPQAITKSADG---SFSLKTNKGTVDgFSHIMFATGRRPNTQNLGLESVGVKLAKdGAIEVDEYSQTSVSSIWAVGDV 376
Cdd:PRK06416 233 GAKAKKVEQTDDGvtvTLEDGGKEETLE-ADYVLVAVGRRPNTENLGLEELGVKTDR-GFIEVDEQLRTNVPNIYAIGDI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 377 TNRINLTPVALMEGGALVKTLfQDNPTKPDYRAVPSAVFSQPPIGQVGLTEEQAVQQYGDIDifTANFrPLKA---TLSG 453
Cdd:PRK06416 311 VGGPMLAHKASAEGIIAAEAI-AGNPHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFDVK--VVKF-PFAGngkALAL 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 454 LPDRVFMKLVVCAKTNEVLGLHMCGEDAPEIVQGFAVALKARLTKADFDATVGIHPSAAE 513
Cdd:PRK06416 387 GETDGFVKLIFDKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSE 446
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
67-513 |
1.95e-96 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 300.97 E-value: 1.95e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 67 FDLFTIGAGSGGVRAARFAANYGASVAICElpfstissetTGGVGGTCVIRGCVPKKLLVYASKFSHEFEESNGFGWRYD 146
Cdd:PRK06370 6 YDAIVIGAGQAGPPLAARAAGLGMKVALIE----------RGLLGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 147 SEPKHDWSSFIANKNA-ELQRLTGIYKNILNNAGVKLIEGHGKIIDPHTVDVNGKLYSAKHILVAVGGRPFIPDIPGKEY 225
Cdd:PRK06370 76 GPVSVDFKAVMARKRRiRARSRHGSEQWLRGLEGVDVFRGHARFESPNTVRVGGETLRAKRIFINTGARAAIPPIPGLDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 226 A--IDSDAALDLPTKPVKIAIVGGGYIALEFAGIFNGLKSEVHVFIRQKKVLRGFDEEIRDFVEEQMSVRGIEFHTEESP 303
Cdd:PRK06370 156 VgyLTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILEREGIDVRLNAEC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 304 QAITKSADG---SFSLKTNKGTVDGfSHIMFATGRRPNTQNLGLESVGVKLAKDGAIEVDEYSQTSVSSIWAVGDVTNRI 380
Cdd:PRK06370 236 IRVERDGDGiavGLDCNGGAPEITG-SHILVAVGRVPNTDDLGLEAAGVETDARGYIKVDDQLRTTNPGIYAAGDCNGRG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 381 NLTPVALMEGGALVKTLFQDNPTKPDYRAVPSAVFSQPPIGQVGLTEEQAVQQYGDIDIFTanfRPLK----ATLSGlPD 456
Cdd:PRK06370 315 AFTHTAYNDARIVAANLLDGGRRKVSDRIVPYATYTDPPLARVGMTEAEARKSGRRVLVGT---RPMTrvgrAVEKG-ET 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1199701057 457 RVFMKLVVCAKTNEVLGLHMCGEDAPEIVQGFAVALKARLTKADFDATVGIHPSAAE 513
Cdd:PRK06370 391 QGFMKVVVDADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSE 447
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
67-513 |
1.05e-93 |
|
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: 293.94 E-value: 1.05e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 67 FDLFTIGAGSGGVRAARFAANYGASVAICElpfstissetTGGVGGTCVIRGCVPKKLLVYASKFSHEFEESNGFGwrYD 146
Cdd:TIGR02053 1 YDLVIIGSGAAAFAAAIKAAELGASVAMVE----------RGPLGGTCVNVGCVPSKMLLRAAEVAHYARKPPFGG--LA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 147 SEPKHDWSSFIANKN---AELQRLTgiYKNILNNAGVKLIEGHGKIIDPHTVDVNG--KLYSAKHILVAVGGRPFIPDIP 221
Cdd:TIGR02053 69 ATVAVDFGELLEGKRevvEELRHEK--YEDVLSSYGVDYLRGRARFKDPKTVKVDLgrEVRGAKRFLIATGARPAIPPIP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 222 G-KEY-AIDSDAALDLPTKPVKIAIVGGGYIALEFAGIFNGLKSEVHVFIRQKKVLRGFDEEIRDFVEEQMSVRGIEFHT 299
Cdd:TIGR02053 147 GlKEAgYLTSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSDRLLPREEPEISAAVEEALAEEGIEVVT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 300 EESPQAItkSADGSFSLKTNKGTVDGFS----HIMFATGRRPNTQNLGLESVGVKLAKDGAIEVDEYSQTSVSSIWAVGD 375
Cdd:TIGR02053 227 SAQVKAV--SVRGGGKIITVEKPGGQGEveadELLVATGRRPNTDGLGLEKAGVKLDERGGILVDETLRTSNPGIYAAGD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 376 VTNRINLTPVALMEGGALVKTLFQDNPTKPDYRAVPSAVFSQPPIGQVGLTEEQAVQQYGDIDIFTANFRPLKATLSGLP 455
Cdd:TIGR02053 305 VTGGLQLEYVAAKEGVVAAENALGGANAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNVPRARINRD 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199701057 456 DRVFMKLVVCAKTNEVLGLHMCGEDAPEIVQGFAVALKARLTKADFDATVGIHPSAAE 513
Cdd:TIGR02053 385 TRGFIKLVAEPGTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAE 442
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
67-390 |
2.80e-76 |
|
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: 242.99 E-value: 2.80e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 67 FDLFTIGAGSGGVRAARFAANYGASVAICELpfstissettggvGGTCVIRGCVPKKLLVYASKFSHEFeesngfgwryd 146
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIED-------------EGTCPYGGCVLSKALLGAAEAPEIA----------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 147 sepkHDWSSFIANKNAELQRLTGIYKNILNNAGVKLIEGHGKIIDPHTVDVNGKLYSAKHILVAVGGRPFIPDIPGKEY- 225
Cdd:pfam07992 57 ----SLWADLYKRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELVDGDGETITYDRLVIATGARPRLPPIPGVELn 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 226 ------AIDSDAALDLPTKPVKIAIVGGGYIALEFAGIFNGLKSEVHVFIRQKKVLRGFDEEIRDFVEEQMSVRGIEFHT 299
Cdd:pfam07992 133 vgflvrTLDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 300 EESPQAITKSADGsFSLKTNKGTVDGFSHIMFATGRRPNTQnlGLESVGVKLAKDGAIEVDEYSQTSVSSIWAVGDVT-N 378
Cdd:pfam07992 213 GTSVKEIIGDGDG-VEVILKDGTEIDADLVVVAIGRRPNTE--LLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDCRvG 289
|
330
....*....|..
gi 1199701057 379 RINLTPVALMEG 390
Cdd:pfam07992 290 GPELAQNAVAQG 301
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
66-513 |
4.34e-74 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 242.17 E-value: 4.34e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 66 DFDLFTIGAGSGG-VRAARFAanyGASVAICElpfstissetTGGVGGTCVIRGCVPKKLLVYASKFSHEFEESNGFGwr 144
Cdd:PRK07846 1 HYDLIIIGTGSGNsILDERFA---DKRIAIVE----------KGTFGGTCLNVGCIPTKMFVYAADVARTIREAARLG-- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 145 YDSE-PKHDWSSF----------IANKNAElqrltgiYKNiLNNAGVKLIEGHGKIIDPHTVDV-NGKLYSAKHILVAVG 212
Cdd:PRK07846 66 VDAElDGVRWPDIvsrvfgridpIAAGGEE-------YRG-RDTPNIDVYRGHARFIGPKTLRTgDGEEITADQVVIAAG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 213 GRPFIPDIPGKEYAI--DSDAALDLPTKPVKIAIVGGGYIALEFAGIFNGLKSEVHVFIRQKKVLRGFDEEIRDFVEEQM 290
Cdd:PRK07846 138 SRPVIPPVIADSGVRyhTSDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLDDDISERFTELA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 291 SVRgIEFHTEESPQAITKsADGSFSLKTNKGTVDGFSHIMFATGRRPNTQNLGLESVGVKLAKDGAIEVDEYSQTSVSSI 370
Cdd:PRK07846 218 SKR-WDVRLGRNVVGVSQ-DGSGVTLRLDDGSTVEADVLLVATGRVPNGDLLDAAAAGVDVDEDGRVVVDEYQRTSAEGV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 371 WAVGDVTNRINLTPVALMEGGALVKTLFQ-DNPTKPDYRAVPSAVFSQPPIGQVGLTEEQAVQQYGDIDIFTANFRPLKA 449
Cdd:PRK07846 296 FALGDVSSPYQLKHVANHEARVVQHNLLHpDDLIASDHRFVPAAVFTHPQIASVGLTENEARAAGLDITVKVQNYGDVAY 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199701057 450 TLSGLPDRVFMKLVVCAKTNEVLGLHMCGEDAPEIVQGFAVALKARLTKADFdAT--VGIHPSAAE 513
Cdd:PRK07846 376 GWAMEDTTGFVKLIADRDTGRLLGAHIIGPQASTLIQPLIQAMSFGLDAREM-ARgqYWIHPALPE 440
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
67-515 |
3.98e-64 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 215.77 E-value: 3.98e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 67 FDLFTIGAGSGG-VRAARFAAnYGASVAICElpfstissETTGGVGGTCVIRGCVPKKLLVYASKFSHEFEESngfgwry 145
Cdd:PRK07251 4 YDLIVIGFGKAGkTLAAKLAS-AGKKVALVE--------ESKAMYGGTCINIGCIPTKTLLVAAEKNLSFEQV------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 146 dsepkhdwssfIANKNAELQRLTGIYKNILNNAGVKLIEGHGKIIDPHTVDVNG----KLYSAKHILVAVGGRPFIPDIP 221
Cdd:PRK07251 68 -----------MATKNTVTSRLRGKNYAMLAGSGVDLYDAEAHFVSNKVIEVQAgdekIELTAETIVINTGAVSNVLPIP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 222 G---KEYAIDSDAALDLPTKPVKIAIVGGGYIALEFAGIFNGLKSEVHVFIRQKKVLRGFDEEIRDFVEEQMSVRGIEFH 298
Cdd:PRK07251 137 GladSKHVYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYMEEDGITFL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 299 TEESPQAItKSADGSFSLKTNKGTVdGFSHIMFATGRRPNTQNLGLESVGVKLAKDGAIEVDEYSQTSVSSIWAVGDVTN 378
Cdd:PRK07251 217 LNAHTTEV-KNDGDQVLVVTEDETY-RFDALLYATGRKPNTEPLGLENTDIELTERGAIKVDDYCQTSVPGVFAVGDVNG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 379 RINLTPVALMEGGALVKTLFQDNP-TKPDYRAVPSAVFSQPPIGQVGLTEEQAVQQYGDI---DIFTANFrP---LKATL 451
Cdd:PRK07251 295 GPQFTYISLDDFRIVFGYLTGDGSyTLEDRGNVPTTMFITPPLSQVGLTEKEAKEAGLPYavkELLVAAM-PrahVNNDL 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199701057 452 SGLpdrvfMKLVVCAKTNEVLGLHMCGEDAPEIVQGFAVALKARLTKADFDATVGIHPSAAEEF 515
Cdd:PRK07251 374 RGA-----FKVVVNTETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAENL 432
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
66-513 |
6.20e-64 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 216.33 E-value: 6.20e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 66 DFDLFTIGAGSGGVRAARFAANYGASVAICElpfSTISSETTGGVGGTCVIRGCVPKK-LLVYASKF---SHEFEEsngF 141
Cdd:PRK06327 4 QFDVVVIGAGPGGYVAAIRAAQLGLKVACIE---AWKNPKGKPALGGTCLNVGCIPSKaLLASSEEFenaGHHFAD---H 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 142 GWRYDsEPKHDWSSFIANKNAELQRLTGIYKNILNNAGVKLIEGHGKII----DPHTVDVNGK---LYSAKHILVAVGGR 214
Cdd:PRK06327 78 GIHVD-GVKIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVgktdAGYEIKVTGEdetVITAKHVIIATGSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 215 P-FIPDIPGKEYAI-DSDAALDLPTKPVKIAIVGGGYIALEFAGIFNGLKSEVHVFIRQKKVLRGFDEEIRDFVEEQMSV 292
Cdd:PRK06327 157 PrHLPGVPFDNKIIlDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAAADEQVAKEAAKAFTK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 293 RGIEFHTEESPQAITKSADG---SFSLKTNKGTVDGFSHIMFATGRRPNTQNLGLESVGVKLAKDGAIEVDEYSQTSVSS 369
Cdd:PRK06327 237 QGLDIHLGVKIGEIKTGGKGvsvAYTDADGEAQTLEVDKLIVSIGRVPNTDGLGLEAVGLKLDERGFIPVDDHCRTNVPN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 370 IWAVGDVTNRINLTPVAlMEGGALVKTLFQDNPTKPDYRAVPSAVFSQPPIGQVGLTEEQAVQQYGDIDI----FTANFR 445
Cdd:PRK06327 317 VYAIGDVVRGPMLAHKA-EEEGVAVAERIAGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLKAEGVEYKAgkfpFMANGR 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199701057 446 PLKAtlsGLPDRvFMKLVVCAKTNEVLGLHMCGEDAPEIVQGFAVALKARLTKADFDATVGIHPSAAE 513
Cdd:PRK06327 396 ALAM---GEPDG-FVKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSE 459
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
62-485 |
4.10e-58 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 200.38 E-value: 4.10e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 62 PAHYDFDLFTIGAGSGGVRAARFAANYGASVAICElpfstisseTTGGVGGTCVIRGCVPKKLLVYASKFSHEFEEsNGF 141
Cdd:PRK05249 1 MHMYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIE---------RYRNVGGGCTHTGTIPSKALREAVLRLIGFNQ-NPL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 142 gwrYDSEPKHDWSSF---IANKNAELQRLTGIYKNILNNAGVKLIEGHGKIIDPHTVDVNG-----KLYSAKHILVAVGG 213
Cdd:PRK05249 71 ---YSSYRVKLRITFadlLARADHVINKQVEVRRGQYERNRVDLIQGRARFVDPHTVEVECpdgevETLTADKIVIATGS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 214 RPF-IPDIP-GKEYAIDSDAALDLPTKPVKIAIVGGGYIALEFAGIFNGLKSEVHVFIRQKKVLRGFDEEIRDFVEEQMS 291
Cdd:PRK05249 148 RPYrPPDVDfDHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSFLDDEISDALSYHLR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 292 VRGIEFHTEESPQAITKSADGSF-------SLKTNKgtvdgfshIMFATGRRPNTQNLGLESVGVKLAKDGAIEVDEYSQ 364
Cdd:PRK05249 228 DSGVTIRHNEEVEKVEGGDDGVIvhlksgkKIKADC--------LLYANGRTGNTDGLNLENAGLEADSRGQLKVNENYQ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 365 TSVSSIWAVGDVTNRINLTPVAlMEGGALVKTLFQDNPTKPDYRAVPSAVFSQPPIGQVGLTEEQAVQQYGDIDIFTANF 444
Cdd:PRK05249 300 TAVPHIYAVGDVIGFPSLASAS-MDQGRIAAQHAVGEATAHLIEDIPTGIYTIPEISSVGKTEQELTAAKVPYEVGRARF 378
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1199701057 445 RPL-KATLSGlpDRV-FMKLVVCAKTNEVLGLHMCGEDAPEIV 485
Cdd:PRK05249 379 KELaRAQIAG--DNVgMLKILFHRETLEILGVHCFGERATEII 419
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
72-497 |
2.52e-56 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 198.07 E-value: 2.52e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 72 IGAGSGGVRAARFAANYGASVAICElpfstissetTGGVGGTCVIRGCVPKKLLVYASKFSHEFEESNGFGWRYDSEPKH 151
Cdd:PRK13748 104 IGSGGAAMAAALKAVEQGARVTLIE----------RGTIGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDGGIAATVPTI 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 152 DWSSFIANKNAELQRLT-GIYKNIL-NNAGVKLIEGHGKIIDPHTVDV-----NGKLYSAKHILVAVGGRPFIPDIPG-K 223
Cdd:PRK13748 174 DRSRLLAQQQARVDELRhAKYEGILdGNPAITVLHGEARFKDDQTLIVrlndgGERVVAFDRCLIATGASPAVPPIPGlK 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 224 EYAI-DSDAALDLPTKPVKIAIVGGGYIALEFAGIFNGLKSEVHVFIRQKKVLRGfDEEIRDFVEEQMSVRGIEF--HTE 300
Cdd:PRK13748 254 ETPYwTSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILARSTLFFRE-DPAIGEAVTAAFRAEGIEVleHTQ 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 301 ESPQAitkSADGSFSLKTNKGTVDGfSHIMFATGRRPNTQNLGLESVGVKLAKDGAIEVDEYSQTSVSSIWAVGDVTNRI 380
Cdd:PRK13748 333 ASQVA---HVDGEFVLTTGHGELRA-DKLLVATGRAPNTRSLALDAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQP 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 381 NLTPVAL---------MEGGAlvktlfqdnpTKPDYRAVPSAVFSQPPIGQVGLTEEQAVQQYGDIDIFTANFRPLKATL 451
Cdd:PRK13748 409 QFVYVAAaagtraainMTGGD----------AALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRTLTLDNVPRAL 478
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1199701057 452 SGLPDRVFMKLVVCAKTNEVLGLHMCGEDAPEIVQGFAVALKARLT 497
Cdd:PRK13748 479 ANFDTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAALAIRNRMT 524
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
72-513 |
1.23e-48 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 174.43 E-value: 1.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 72 IGAGSGGVRAARFAANYGASVAICElpfstissETTGGVGGTCVIRGCVPKKLLVYASKFSHEFEESngfgwrydSEPKH 151
Cdd:PRK08010 9 IGFGKAGKTLAVTLAKAGWRVALIE--------QSNAMYGGTCINIGCIPTKTLVHDAQQHTDFVRA--------IQRKN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 152 DWSSFIANKNaelqrltgiYKNILNNAGVKLIEGHGKIIDPHTVDV-----NGKLYSAKhILVAVGGRPFIPDIPG---K 223
Cdd:PRK08010 73 EVVNFLRNKN---------FHNLADMPNIDVIDGQAEFINNHSLRVhrpegNLEIHGEK-IFINTGAQTVVPPIPGittT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 224 EYAIDSDAALDLPTKPVKIAIVGGGYIALEFAGIFNGLKSEVHVFIRQKKVLRGFDEEIRDFVEEQMSVRGIEFHTEESP 303
Cdd:PRK08010 143 PGVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 304 QAITkSADGSFSLKTNKGT--VDGfshIMFATGRRPNTQNLGLESVGVKLAKDGAIEVDEYSQTSVSSIWAVGDVTNRIN 381
Cdd:PRK08010 223 ERIS-HHENQVQVHSEHAQlaVDA---LLIASGRQPATASLHPENAGIAVNERGAIVVDKYLHTTADNIWAMGDVTGGLQ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 382 LTPVALMEGGALVKTLFQDNPTKPDYRA-VPSAVFSQPPIGQVGLTEEQAVQQYGDIDIFTANFRPLKATLSGLPDRVFM 460
Cdd:PRK08010 299 FTYISLDDYRIVRDELLGEGKRSTDDRKnVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDTRGVL 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1199701057 461 KLVVCAKTNEVLGLHMCGEDAPEIVQGFAVALKARLTKADFDATVGIHPSAAE 513
Cdd:PRK08010 379 KAIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSE 431
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
72-510 |
5.29e-46 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 167.73 E-value: 5.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 72 IGAGSGGVRAARFAANYGASVAICElpfstissetTGGVGGTCVIRGCVPKKLLVYASKFSHEFEESNGFGWRYDSEPKH 151
Cdd:PRK07845 7 IGGGPGGYEAALVAAQLGADVTVIE----------RDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRFIDDGEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 152 DWSsfIANKNAELQRLT-----GIyKNILNNAGVKLIEGHGKIID----PHTVDVNG-----KLYSAKHILVAVGGRPFI 217
Cdd:PRK07845 77 RVD--LPAVNARVKALAaaqsaDI-RARLEREGVRVIAGRGRLIDpglgPHRVKVTTadggeETLDADVVLIATGASPRI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 218 pdIPGKEyaIDSDAAL------DLPTKPVKIAIVGGGYIALEFAGIFNGLKSEVHVFIRQKKVLRGFDEEIRDFVEEQMS 291
Cdd:PRK07845 154 --LPTAE--PDGERILtwrqlyDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPGEDADAAEVLEEVFA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 292 VRGIEFHTEESPQAITKSADGSFSLKTNKGTVDGfSHIMFATGRRPNTQNLGLESVGVKLAKDGAIEVDEYSQTSVSSIW 371
Cdd:PRK07845 230 RRGMTVLKRSRAESVERTGDGVVVTLTDGRTVEG-SHALMAVGSVPNTAGLGLEEAGVELTPSGHITVDRVSRTSVPGIY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 372 AVGDVTNRINLTPVALMEG--------GALVKTLfqdnptkpDYRAVPSAVFSQPPIGQVGLTEEqavqqygDIDIFTAN 443
Cdd:PRK07845 309 AAGDCTGVLPLASVAAMQGriamyhalGEAVSPL--------RLKTVASNVFTRPEIATVGVSQA-------AIDSGEVP 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199701057 444 FR----PL----KATLSGLPDRvFMKLVVCAKTNEVLGLHMCGEDAPEIVQGFAVALKARLTKADFDATVGIHPS 510
Cdd:PRK07845 374 ARtvmlPLatnpRAKMSGLRDG-FVKLFCRPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYPS 447
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
67-513 |
7.40e-44 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 165.09 E-value: 7.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 67 FDLFTIGAGSGGVRAARFAANYGASVAIcelpfstisseTTGG---VGGTCVIRGCVPKKLLVYASKFSHEFE------- 136
Cdd:PTZ00153 117 YDVGIIGCGVGGHAAAINAMERGLKVII-----------FTGDddsIGGTCVNVGCIPSKALLYATGKYRELKnlaklyt 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 137 ---ESNGF--GWRYDSEPKHDWSSFIANKNAELQRLT---------GI------YKNILNNAGVKLIEGHGKIIDPHTV- 195
Cdd:PTZ00153 186 ygiYTNAFknGKNDPVERNQLVADTVQIDITKLKEYTqsvidklrgGIenglksKKFCKNSEHVQVIYERGHIVDKNTIk 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 196 -DVNGKLYSAKHILVAVGGRPFIPD-IPGKEYAI-DSDAALDLPTKPVKIAIVGGGYIALEFAGIFNGLKSEVHVFIRQK 272
Cdd:PTZ00153 266 sEKSGKEFKVKNIIIATGSTPNIPDnIEVDQKSVfTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSP 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 273 KVLRGFDEEIRDFVEEQ-MSVRGIEFHTE-----------ESPQAI------TKSADGSFSLKTN--KGTVDGfshIMFA 332
Cdd:PTZ00153 346 QLLPLLDADVAKYFERVfLKSKPVRVHLNtlieyvragkgNQPVIIghserqTGESDGPKKNMNDikETYVDS---CLVA 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 333 TGRRPNTQNLGLESVGVKLaKDGAIEVDEY------SQTSVSSIWAVGDVTNRINLTPVALME-----------GGALVK 395
Cdd:PTZ00153 423 TGRKPNTNNLGLDKLKIQM-KRGFVSVDEHlrvlreDQEVYDNIFCIGDANGKQMLAHTASHQalkvvdwiegkGKENVN 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 396 TLFQDNPTKP-DYRAVPSAVFSQPPIGQVGLTEEQAVQQYG------DIDIFTANFRPLKATLSGLPDRV---------- 458
Cdd:PTZ00153 502 INVENWASKPiIYKNIPSVCYTTPELAFIGLTEKEAKELYPpdnvgvEISFYKANSKVLCENNISFPNNSknnsynkgky 581
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199701057 459 --------FMKLVVCAKTNEVLGLHMCGEDAPEIVQGFAVALKARLTKADFDATVGIHPSAAE 513
Cdd:PTZ00153 582 ntvdntegMVKIVYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISE 644
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
410-518 |
1.27e-41 |
|
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: 145.00 E-value: 1.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 410 VPSAVFSQPPIGQVGLTEEQAVQQYGDIDIFTANFRPLKATLSGLPDRVFMKLVVCAKTNEVLGLHMCGEDAPEIVQGFA 489
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGEVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQEAA 80
|
90 100
....*....|....*....|....*....
gi 1199701057 490 VALKARLTKADFDATVGIHPSAAEEFVTM 518
Cdd:pfam02852 81 LAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
190-415 |
1.65e-32 |
|
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: 126.85 E-value: 1.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 190 IDP--HTVDV-NGKLYSAKHILVAVGGRPFIPDIPGK-----------EYAIDSDAALDLPtKPVKIAIVGGGYIALEFA 255
Cdd:COG0446 62 IDPeaKTVTLrDGETLSYDKLVLATGARPRPPPIPGLdlpgvftlrtlDDADALREALKEF-KGKRAVVIGGGPIGLELA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 256 GIFNGLKSEVHVFIRQKKVLRGFDEEIRDFVEEQMSVRGIEFHTEESPQAITKSADGSFSLkTNKGTVDgFSHIMFATGR 335
Cdd:COG0446 141 EALRKRGLKVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAIDGDDKVAVTL-TDGEEIP-ADLVVVAPGV 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 336 RPNTQnLGLESvGVKLAKDGAIEVDEYSQTSVSSIWAVGDVTN----------RINLTPVALMEGGALVKTLFQDNPTKP 405
Cdd:COG0446 219 RPNTE-LAKDA-GLALGERGWIKVDETLQTSDPDVYAAGDCAEvphpvtgktvYIPLASAANKQGRVAAENILGGPAPFP 296
|
250
....*....|
gi 1199701057 406 DYRAVPSAVF 415
Cdd:COG0446 297 GLGTFISKVF 306
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
207-375 |
1.31e-27 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 115.52 E-value: 1.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 207 ILVAVGGRPFIPDIPG-----------KEYAIDSDAALDLPTKPvKIAIVGGGYIALEFAGIFNGLKSEVHVFIRQKKVL 275
Cdd:PRK09564 107 LMIATGARPIIPPIKNinlenvytlksMEDGLALKELLKDEEIK-NIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRIL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 276 -RGFDEEIRDFVEEQMSVRGIEFHTEESPQAITkSADGSFSLKTNKGTVDGfSHIMFATGRRPNTQnlGLESVGVKLAKD 354
Cdd:PRK09564 186 pDSFDKEITDVMEEELRENGVELHLNEFVKSLI-GEDKVEGVVTDKGEYEA-DVVIVATGVKPNTE--FLEDTGLKTLKN 261
|
170 180
....*....|....*....|.
gi 1199701057 355 GAIEVDEYSQTSVSSIWAVGD 375
Cdd:PRK09564 262 GAIIVDEYGETSIENIYAAGD 282
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
190-397 |
4.28e-24 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 104.45 E-value: 4.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 190 IDP--HTV-DVNGKLYSAKHILVAVGGRPFIPDIPGKE----YAI----DSDAALDLPTKPVKIAIVGGGYIALEFAGIF 258
Cdd:COG1251 82 IDRaaRTVtLADGETLPYDKLVLATGSRPRVPPIPGADlpgvFTLrtldDADALRAALAPGKRVVVIGGGLIGLEAAAAL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 259 NGLKSEVHVFIRQKKVL-RGFDEEIRDFVEEQMSVRGIEFHTEESPQAITKSADGSfSLKTNKGTVDGFSHIMFATGRRP 337
Cdd:COG1251 162 RKRGLEVTVVERAPRLLpRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVT-GVRLADGEELPADLVVVAIGVRP 240
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199701057 338 NTQnLgLESVGvkLAKDGAIEVDEYSQTSVSSIWAVGDVT---------NRINLTPVALMEGGALVKTL 397
Cdd:COG1251 241 NTE-L-ARAAG--LAVDRGIVVDDYLRTSDPDIYAAGDCAehpgpvygrRVLELVAPAYEQARVAAANL 305
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
241-313 |
1.21e-22 |
|
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: 91.88 E-value: 1.21e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199701057 241 KIAIVGGGYIALEFAGIFNGLKSEVHVFIRQKKVLRGFDEEIRDFVEEQMSVRGIEFHTEESPQAITKSADGS 313
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGV 73
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
171-376 |
1.65e-17 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 84.41 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 171 YKNILNNAGVKLIEGHGKIIDP--HTVDV-NGKLYSAKHILVAVGGRPFIPDIPG-KEYAI---DSDAALDL-------- 235
Cdd:COG1252 62 LRELLRRAGVRFIQGEVTGIDPeaRTVTLaDGRTLSYDYLVIATGSVTNFFGIPGlAEHALplkTLEDALALrerllaaf 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 236 ----PTKPVKIAIVGGGYIALEFAGI----------FNGL---KSEVHVFIRQKKVLRGFDEEIRDFVEEQMSVRGIEFH 298
Cdd:COG1252 142 eraeRRRLLTIVVVGGGPTGVELAGElaellrkllrYPGIdpdKVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVH 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 299 TEESPQAITKSAdgsfsLKTNKGTVDGFSHIMFATGRRPN--TQNLGLEsvgvkLAKDGAIEVDEYSQT-SVSSIWAVGD 375
Cdd:COG1252 222 TGTRVTEVDADG-----VTLEDGEEIPADTVIWAAGVKAPplLADLGLP-----TDRRGRVLVDPTLQVpGHPNVFAIGD 291
|
.
gi 1199701057 376 V 376
Cdd:COG1252 292 C 292
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
191-377 |
5.43e-15 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 75.93 E-value: 5.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 191 DPHTVDV-NGKLYSAKHILVAVGGRPFIPDIPGKE--------YAIDSDAALdLPTKPVkiAIVGGGYIALEFAGIFNGL 261
Cdd:COG0492 87 GPFRVTTdDGTEYEAKAVIIATGAGPRKLGLPGEEefegrgvsYCATCDGFF-FRGKDV--VVVGGGDSALEEALYLTKF 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 262 KSEVHVFIRQKKvLRGfdeeIRDFVEEQMSVRGIEFHTEESPQAITKsaDG---SFSLKTNKG------TVDGfshIMFA 332
Cdd:COG0492 164 ASKVTLIHRRDE-LRA----SKILVERLRANPKIEVLWNTEVTEIEG--DGrveGVTLKNVKTgeekelEVDG---VFVA 233
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1199701057 333 TGRRPNTQnlGLESVGVKLAKDGAIEVDEYSQTSVSSIWAVGDVT 377
Cdd:COG0492 234 IGLKPNTE--LLKGLGLELDEDGYIVVDEDMETSVPGVFAAGDVR 276
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
199-413 |
3.74e-14 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 75.63 E-value: 3.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 199 GKLYSAKHILVAVGGRPFIPDIPGKE----YAI----DSDAALDLPTKPVKIAIVGGGYIALEFAGIFNGLKSEVHV--- 267
Cdd:TIGR02374 92 GRTLSYDKLILATGSYPFILPIPGADkkgvYVFrtieDLDAIMAMAQRFKKAAVIGGGLLGLEAAVGLQNLGMDVSVihh 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 268 --FIRQKKVLRGFDEEIRDFVEEQmsvrGIEFHTEESPQAITKsADGSFSLKTNKGTVDGFSHIMFATGRRPNTQnLGLE 345
Cdd:TIGR02374 172 apGLMAKQLDQTAGRLLQRELEQK----GLTFLLEKDTVEIVG-ATKADRIRFKDGSSLEADLIVMAAGIRPNDE-LAVS 245
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199701057 346 SvGVKLAkdGAIEVDEYSQTSVSSIWAVGDVT--NRINLTPVA-LMEGGALVKTLFQDNPTKPDYRAVPSA 413
Cdd:TIGR02374 246 A-GIKVN--RGIIVNDSMQTSDPDIYAVGECAehNGRVYGLVApLYEQAKVLADHICGVECEEYEGSDLSA 313
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
190-397 |
7.09e-13 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 70.33 E-value: 7.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 190 IDP--HTVDVNGKLYSAKHILVAVGGRPFIPDIPG----------KEYAiDSDAALDLPTkpvKIAIVGGGYIALEFAGI 257
Cdd:PRK04965 84 IDAeaQVVKSQGNQWQYDKLVLATGASAFVPPIPGrelmltlnsqQEYR-AAETQLRDAQ---RVLVVGGGLIGTELAMD 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 258 FNGLKSEVHVFIRQKKVLRGF-DEEIRDFVEEQMSVRGIEFHTEESPQAITKSADGsFSLKTNKG---TVDGfshIMFAT 333
Cdd:PRK04965 160 LCRAGKAVTLVDNAASLLASLmPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSG-IRATLDSGrsiEVDA---VIAAA 235
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 334 GRRPNTQnLGLESvGVKLAKdgAIEVDEYSQTSVSSIWAVGDVTnRIN------LTPvALMEGGALVKTL 397
Cdd:PRK04965 236 GLRPNTA-LARRA-GLAVNR--GIVVDSYLQTSAPDIYALGDCA-EINgqvlpfLQP-IQLSAMALAKNL 299
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
241-376 |
4.47e-11 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 64.80 E-value: 4.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 241 KIAIVGGGYIALEFAGIFNGLKSEVHVFIRQKKVLRGFDEEIRDFVEEQMSVRGIEFHTEESPQAItksaDGSfSLKTNK 320
Cdd:PRK13512 150 KALVVGAGYISLEVLENLYERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDAI----NGN-EVTFKS 224
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1199701057 321 GTVDGFSHIMFATGRRPNTQNLglESVGVKLAKDGAIEVDEYSQTSVSSIWAVGDV 376
Cdd:PRK13512 225 GKVEHYDMIIEGVGTHPNSKFI--ESSNIKLDDKGFIPVNDKFETNVPNIYAIGDI 278
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
154-375 |
1.27e-09 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 60.90 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 154 SSFIANKNAELQRL--TGIYK----NILNNAGVKLIEGHGKIIDPHTvdvnGKLYSAKHILVAVGGRPFIPDIPGKEY-- 225
Cdd:PRK14989 50 SSYFSHHTAEELSLvrEGFYEkhgiKVLVGERAITINRQEKVIHSSA----GRTVFYDKLIMATGSYPWIPPIKGSETqd 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 226 -----AIDSDAALDLPTKPVKI-AIVGGGYIALEFAGIFNGLKSEVHVfIRQKKVLRG--FDEEIRDFVEEQMSVRGIEF 297
Cdd:PRK14989 126 cfvyrTIEDLNAIEACARRSKRgAVVGGGLLGLEAAGALKNLGVETHV-IEFAPMLMAeqLDQMGGEQLRRKIESMGVRV 204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199701057 298 HTEESPQAITKSA-DGSFSLKTNKGTVDGFSHIMFATGRRPntQNLGLESVGVKLAKDGAIEVDEYSQTSVSSIWAVGD 375
Cdd:PRK14989 205 HTSKNTLEIVQEGvEARKTMRFADGSELEVDFIVFSTGIRP--QDKLATQCGLAVAPRGGIVINDSCQTSDPDIYAIGE 281
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
205-378 |
5.36e-07 |
|
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: 52.06 E-value: 5.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 205 KHILVAVG-GRPFIPDIPGKE-----YAID-------SDAALDLPTKPVKIAIVGGGYIALEFAGIFNGLKSE-VHVF-I 269
Cdd:COG0493 208 DAVFLATGaGKPRDLGIPGEDlkgvhSAMDfltavnlGEAPDTILAVGKRVVVIGGGNTAMDCARTALRLGAEsVTIVyR 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 270 RQKKVLRGFDEEIRDFVEEqmsvrGIEFHTEESPQAITKSADGSF-SLKTNK--------------GTVDGFSHIM---- 330
Cdd:COG0493 288 RTREEMPASKEEVEEALEE-----GVEFLFLVAPVEIIGDENGRVtGLECVRmelgepdesgrrrpVPIEGSEFTLpadl 362
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1199701057 331 --FATGRRPNTQNLgLESVGVKLAKDGAIEVDEYS-QTSVSSIWAVGDVTN 378
Cdd:COG0493 363 viLAIGQTPDPSGL-EEELGLELDKRGTIVVDEETyQTSLPGVFAGGDAVR 412
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
206-386 |
1.29e-06 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 50.92 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 206 HILVAVGGRPFIPDIPG-KEYA----------------IDSDAALDLPTKPVKIA-------IVGGGYIALEFAgifngl 261
Cdd:PTZ00318 116 KLVVAHGARPNTFNIPGvEERAfflkevnhargirkriVQCIERASLPTTSVEERkrllhfvVVGGGPTGVEFA------ 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 262 kSEVHVFIRQ---------------------KKVLRGFDEEIRDFVEEQMSVRGIEFHTEESPQAITKSadgsfSLKTNK 320
Cdd:PTZ00318 190 -AELADFFRDdvrnlnpelveeckvtvleagSEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEVLDK-----EVVLKD 263
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199701057 321 GTVDGFSHIMFATG--RRPNTQNLglesvGVKLAKDGAIEVDEYSQTS-VSSIWAVGDVT--NRINLTPVA 386
Cdd:PTZ00318 264 GEVIPTGLVVWSTGvgPGPLTKQL-----KVDKTSRGRISVDDHLRVKpIPNVFALGDCAanEERPLPTLA 329
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
207-378 |
4.62e-06 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 48.83 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 207 ILVAVGG-RPFIPDIPGKE-----------YAIDSDAALDLPTKPV------KIAIVGGGYIALEFA--GIFNGLKSEVH 266
Cdd:PRK12770 122 VLIATGTwKSRKLGIPGEDlpgvysaleylFRIRAAKLGYLPWEKVppvegkKVVVVGAGLTAVDAAleAVLLGAEKVYL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 267 VFIRQKKVLRGFDEEIRDFVEeqmsvRGIEFHTEESPQAITksADGSFS----LKTNKGTVDG----------------- 325
Cdd:PRK12770 202 AYRRTINEAPAGKYEIERLIA-----RGVEFLELVTPVRII--GEGRVEgvelAKMRLGEPDEsgrprpvpipgsefvle 274
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1199701057 326 FSHIMFATGRRPnTQNLGLESVGVKLAKDGAIEVDEYSQTSVSSIWAVGDVTN 378
Cdd:PRK12770 275 ADTVVFAIGEIP-TPPFAKECLGIELNRKGEIVVDEKHMTSREGVFAAGDVVT 326
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
56-113 |
4.47e-05 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 46.27 E-value: 4.47e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199701057 56 NGADPVPAHYDFDLFTIGAGSGGVRAARFAANYGASVAICelpfstissETTGGVGGT 113
Cdd:PRK12843 6 SELSPERWDAEFDVIVIGAGAAGMSAALFAAIAGLKVLLV---------ERTEYVGGT 54
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
198-376 |
1.40e-04 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 44.53 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 198 NGKLYSAKHILVAVGGR----PFIPDIPGKEYAI---DSDAALDLPTKPVK-IAIVGGGYIALEFAGIFNGLKSEVHVFI 269
Cdd:PRK09754 95 NGESWHWDQLFIATGAAarplPLLDALGERCFTLrhaGDAARLREVLQPERsVVIVGAGTIGLELAASATQRRCKVTVIE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 270 RQKKVL-RGFDEEIRDFVEEQMSVRGIEFHTEespQAITKSADGS-FSLKTNKG-TVDGfSHIMFATGRRPNTQnLGLES 346
Cdd:PRK09754 175 LAATVMgRNAPPPVQRYLLQRHQQAGVRILLN---NAIEHVVDGEkVELTLQSGeTLQA-DVVIYGIGISANDQ-LAREA 249
|
170 180 190
....*....|....*....|....*....|
gi 1199701057 347 vgvKLAKDGAIEVDEYSQTSVSSIWAVGDV 376
Cdd:PRK09754 250 ---NLDTANGIVIDEACRTCDPAIFAGGDV 276
|
|
| Lys_Orn_oxgnase |
pfam13434 |
L-lysine 6-monooxygenase/L-ornithine 5-monooxygenase; This is a family of Rossmann fold ... |
193-268 |
2.74e-04 |
|
L-lysine 6-monooxygenase/L-ornithine 5-monooxygenase; This is a family of Rossmann fold oxidoreductases that catalyze NADPH-dependent hydroxylation and are involved in siderophore biosynthesis. This family includes L-ornithine 5-monooxygenase, which catalyzes the hydroxylation of L-ornithine at the N5 position, and L-lysine 6-monooxygenase, which catalyzes the hydroxylation of lysine at the N6 position (EC:1.14.13.59).
Pssm-ID: 433204 [Multi-domain] Cd Length: 338 Bit Score: 43.34 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 193 HTVDVNGKL--YSAKHILVAVGGRPFIPD-IPGKEYAIDSDAAL---DLPTKPVKIAIVGGGYIALEfagIFNGLKSEVH 266
Cdd:pfam13434 135 RVRDADGEEttFLARNLVLGTGGEPYIPEcARGGERVFHSSEYLeriDRLAAKKRIAVVGSGQSAAE---IFRDLLRRGP 211
|
..
gi 1199701057 267 VF 268
Cdd:pfam13434 212 AY 213
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
173-361 |
3.55e-04 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 42.60 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 173 NILNNAGVKLIEGHGKIidpHTVDVNGKLYSAKHILVAVG--GRPFIPDIP--GKEYAIDSDAAldlPTKPVKIAIVGGG 248
Cdd:pfam13738 91 PINLFEEVTSVKKEDDG---FVVTTSKGTYQARYVIIATGefDFPNKLGVPelPKHYSYVKDFH---PYAGQKVVVIGGY 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 249 YIALEFAGIFNGLKSEVHVFIRqKKVLRGFDEE--------IRDFVEEQMSVRGIEFHTEESPQAITKsADGSFSLKTNK 320
Cdd:pfam13738 165 NSAVDAALELVRKGARVTVLYR-GSEWEDRDSDpsyslspdTLNRLEELVKNGKIKAHFNAEVKEITE-VDVSYKVHTED 242
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1199701057 321 GTVDGFSHI-MFATGRRPNTQNlgLESVGVKLAKDGAIEVDE 361
Cdd:pfam13738 243 GRKVTSNDDpILATGYHPDLSF--LKKGLFELDEDGRPVLTE 282
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
236-378 |
1.00e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 42.06 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 236 PTKPVKIAIVGGGYIALEFAGIFNGL------KSEVHVFIRQkkvlRGFD------EEIRDFVEEqmsvrGIEFHTEESP 303
Cdd:PRK13984 415 PKIPRSLVVIGGGNVAMDIARSMARLqkmeygEVNVKVTSLE----RTFEempadmEEIEEGLEE-----GVVIYPGWGP 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 304 QAITKSAD-----------------GSFSLK---TNKGTVDGfSHIMFATGRRPNTQNLGlESVGVKLA-KDGAIEVDEY 362
Cdd:PRK13984 486 MEVVIENDkvkgvkfkkcvevfdeeGRFNPKfdeSDQIIVEA-DMVVEAIGQAPDYSYLP-EELKSKLEfVRGRILTNEY 563
|
170
....*....|....*.
gi 1199701057 363 SQTSVSSIWAVGDVTN 378
Cdd:PRK13984 564 GQTSIPWLFAGGDIVH 579
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
198-270 |
1.47e-03 |
|
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];
Pssm-ID: 441675 [Multi-domain] Cd Length: 414 Bit Score: 41.00 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199701057 198 NGKLYSAKHILVAVGG--RPFIPDIPGKE-YAIDS------DAALDLPTKPVkiAIVGGGY----IALEFAGIfnglKSE 264
Cdd:COG2072 123 DGETLTARFVVVATGPlsRPKIPDIPGLEdFAGEQlhsadwRNPVDLAGKRV--LVVGTGAsavqIAPELARV----AAH 196
|
....*.
gi 1199701057 265 VHVFIR 270
Cdd:COG2072 197 VTVFQR 202
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
337-378 |
5.44e-03 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 39.37 E-value: 5.44e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1199701057 337 PNTQNLGlESVgvKLAKDGAIEVDEYSQTSVSSIWAVGDVTN 378
Cdd:PRK15317 449 PNTEWLK-GTV--ELNRRGEIIVDARGATSVPGVFAAGDCTT 487
|
|
| PRK13369 |
PRK13369 |
glycerol-3-phosphate dehydrogenase; Provisional |
66-96 |
9.22e-03 |
|
glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 237365 [Multi-domain] Cd Length: 502 Bit Score: 38.79 E-value: 9.22e-03
10 20 30
....*....|....*....|....*....|.
gi 1199701057 66 DFDLFTIGAGSGGVRAARFAANYGASVAICE 96
Cdd:PRK13369 6 TYDLFVIGGGINGAGIARDAAGRGLKVLLCE 36
|
|
| |
