|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02507 |
PLN02507 |
glutathione reductase |
1-499 |
0e+00 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 1047.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 1 MARKMLVDGEIDKVAADEANATHYDFDLFVIGAGSGGVRAARFSANHGAKVGICELPFHPISSEEIGGVGGTCVIRGCVP 80
Cdd:PLN02507 1 MARKMLIDGEVAKVNADEANATHYDFDLFVIGAGSGGVRAARFSANFGAKVGICELPFHPISSESIGGVGGTCVIRGCVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 81 KKILVYGATYGGELEDAKNYGWEINEKVDFTWKKLLQKKTDEILRLNNIYKRLLANAAVKLYEGEGRVVGPNEVEVRQID 160
Cdd:PLN02507 81 KKILVYGATFGGEFEDAKNYGWEINEKVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 161 GTKISYTAKHILIATGSRAQKPNIPGHELAITSDEALSLEEFPKRAIVLGGGYIAVEFASIWRGMGATVDLFFRKELPLR 240
Cdd:PLN02507 161 GTKLRYTAKHILIATGSRAQRPNIPGKELAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 241 GFDDEMRALVARNLEGRGVNLHPQTSLTQLTKTDQGIKVISSHGEEFVADVVLFATGRSPNTKRLNLEAVGVELDQAGAV 320
Cdd:PLN02507 241 GFDDEMRAVVARNLEGRGINLHPRTNLTQLTKTEGGIKVITDHGEEFVADVVLFATGRAPNTKRLNLEAVGVELDKAGAV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 321 KVDEYSRTNIPSIWAVGDATNRINLTPVALMEATCFANTAFGGKPTKAEYSNVACAVFCIPPLAVVGLSEEEAVEQATGD 400
Cdd:PLN02507 321 KVDEYSRTNIPSIWAIGDVTNRINLTPVALMEGTCFAKTVFGGQPTKPDYENVACAVFCIPPLSVVGLSEEEAVEQAKGD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 401 ILVFTSGFNPMKNTISGRQEKTLMKLIVDEKSDKVIGASMCGPDAAEIMQGIAIALKCGATKAQFDSTVGIHPSSAEEFV 480
Cdd:PLN02507 401 ILVFTSSFNPMKNTISGRQEKTVMKLIVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEFV 480
|
490
....*....|....*....
gi 15230074 481 TMRSVTRRIAHKPKPKTNL 499
Cdd:PLN02507 481 TMRSVTRRVTAKGKPKTNL 499
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
24-483 |
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: 771.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 24 YDFDLFVIGAGSGGVRAARFSANHGAKVGICELPFhpisseeiggVGGTCVIRGCVPKKILVYGATYGGELEDAKNYGWE 103
Cdd:TIGR01424 1 FDYDLFVIGAGSGGVRAARLAAALGAKVAIAEEFR----------VGGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGWT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 104 iNEKVDFTWKKLLQKKTDEILRLNNIYKRLLANAAVKLYEGEGRVVGPNEVEVRQIDGTkisYTAKHILIATGSRAQKPN 183
Cdd:TIGR01424 71 -VGKARFDWKKLLAAKDQEIARLSGLYRKGLANAGAELLDGRAELVGPNTVEVLASGKT---YTAEKILIAVGGRPPKPA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 184 IPGHELAITSDEALSLEEFPKRAIVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRALVARNLEGRGVNLHP 263
Cdd:TIGR01424 147 LPGHELGITSNEAFHLPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRGKEILRGFDDDMRRGLAAALEERGIRILP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 264 QTSLTQLTKTDQG-IKVISSHGEEFVADVVLFATGRSPNTKRLNLEAVGVELDQAGAVKVDEYSRTNIPSIWAVGDATNR 342
Cdd:TIGR01424 227 EDSITSISKDDDGrLKATLSKHEEIVADVVLFATGRSPNTNGLGLEAAGVRLNDLGAIAVDEYSRTSTPSIYAVGDVTDR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 343 INLTPVALMEATCFANTAFGGKPTKAEYSNVACAVFCIPPLAVVGLSEEEAVEQAtGDILVFTSGFNPMKNTISGRQEKT 422
Cdd:TIGR01424 307 INLTPVAIHEATCFAETEFGNNPTSFDHDLIATAVFSQPPIGTVGLTEEEARRKF-GDIEVYRAEFRPMKATFSGRQEKT 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15230074 423 LMKLIVDEKSDKVIGASMCGPDAAEIMQGIAIALKCGATKAQFDSTVGIHPSSAEEFVTMR 483
Cdd:TIGR01424 386 LMKLVVDAKDDKVLGAHMVGPDAAEIIQGLAIALKMGATKDDFDSTVAVHPTSAEELVTMR 446
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
24-483 |
0e+00 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 614.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 24 YDFDLFVIGAGSGGVRAARFSANHGAKVGICELPFhpisseeiggVGGTCVIRGCVPKKILVYGATYGGELED-AKNYGW 102
Cdd:PRK06116 3 KDYDLIVIGGGSGGIASANRAAMYGAKVALIEAKR----------LGGTCVNVGCVPKKLMWYGAQIAEAFHDyAPGYGF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 103 EINEKvDFTWKKLLQKKTDEILRLNNIYKRLLANAAVKLYEGEGRVVGPNEVEVrqiDGTKisYTAKHILIATGSRAQKP 182
Cdd:PRK06116 73 DVTEN-KFDWAKLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEV---NGER--YTADHILIATGGRPSIP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 183 NIPGHELAITSDEALSLEEFPKRAIVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRALVARNLEGRGVNLH 262
Cdd:PRK06116 147 DIPGAEYGITSDGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLH 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 263 PQTSLTQLTKTDQG-IKVISSHGEEFVADVVLFATGRSPNTKRLNLEAVGVELDQAGAVKVDEYSRTNIPSIWAVGDATN 341
Cdd:PRK06116 227 TNAVPKAVEKNADGsLTLTLEDGETLTVDCLIWAIGREPNTDGLGLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGDVTG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 342 RINLTPVALMEATCFANTAFGGKP-TKAEYSNVACAVFCIPPLAVVGLSEEEAVEQATGD-ILVFTSGFNPMKNTISGRQ 419
Cdd:PRK06116 307 RVELTPVAIAAGRRLSERLFNNKPdEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDnVKVYRSSFTPMYTALTGHR 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15230074 420 EKTLMKLIVDEKSDKVIGASMCGPDAAEIMQGIAIALKCGATKAQFDSTVGIHPSSAEEFVTMR 483
Cdd:PRK06116 387 QPCLMKLVVVGKEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFVTMR 450
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
14-496 |
0e+00 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 599.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 14 VAADEANAT----HYDFDLFVIGAGSGGVRAARFSANHGAKVGICELPFHPISSEEIGGVGGTCVIRGCVPKKILVYGAT 89
Cdd:PLN02546 64 SRAAAPNGAeserHYDFDLFTIGAGSGGVRASRFASNFGASAAVCELPFATISSDTLGGVGGTCVLRGCVPKKLLVYASK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 90 YGGELEDAKNYGWEINEKVDFTWKKLLQKKTDEILRLNNIYKRLLANAAVKLYEGEGRVVGPNEVEVrqiDGtKIsYTAK 169
Cdd:PLN02546 144 YSHEFEESRGFGWKYETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDV---DG-KL-YTAR 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 170 HILIATGSRAQKPNIPGHELAITSDEALSLEEFPKRAIVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRAL 249
Cdd:PLN02546 219 NILIAVGGRPFIPDIPGIEHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKKVLRGFDEEVRDF 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 250 VARNLEGRGVNLHPQTSLTQLTKTDQGIKVISSHGEEFVA-DVVLFATGRSPNTKRLNLEAVGVELDQAGAVKVDEYSRT 328
Cdd:PLN02546 299 VAEQMSLRGIEFHTEESPQAIIKSADGSLSLKTNKGTVEGfSHVMFATGRKPNTKNLGLEEVGVKMDKNGAIEVDEYSRT 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 329 NIPSIWAVGDATNRINLTPVALMEATCFANTAFGGKPTKAEYSNVACAVFCIPPLAVVGLSEEEAVEQaTGDILVFTSGF 408
Cdd:PLN02546 379 SVPSIWAVGDVTDRINLTPVALMEGGALAKTLFGNEPTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEE-YGDVDVFTANF 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 409 NPMKNTISGRQEKTLMKLIVDEKSDKVIGASMCGPDAAEIMQGIAIALKCGATKAQFDSTVGIHPSSAEEFVTMRSVTRR 488
Cdd:PLN02546 458 RPLKATLSGLPDRVFMKLIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEEFVTMRTPTRK 537
|
....*...
gi 15230074 489 IAHKPKPK 496
Cdd:PLN02546 538 IRKDSPSE 545
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
24-483 |
1.76e-175 |
|
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: 501.15 E-value: 1.76e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 24 YDFDLFVIGAGSGGVRAARFSANHGAKVGICELpfhpisseeiGGVGGTCVIRGCVPKKILVYGATYGGELEDAKNYGWE 103
Cdd:COG1249 2 KDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEK----------GRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGIS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 104 InEKVDFTWKKLLQKKTDEILRLNNIYKRLLANAAVKLYEGEGRVVGPNEVEVrqiDGTKIsYTAKHILIATGSRAQKPN 183
Cdd:COG1249 72 A-GAPSVDWAALMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEV---TGGET-LTADHIVIATGSRPRVPP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 184 IPG--HELAITSDEALSLEEFPKRAIVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRALVARNLEGRGVNL 261
Cdd:COG1249 147 IPGldEVRVLTSDEALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 262 HPQTSLTQLTKTDQGIKVISSHG---EEFVADVVLFATGRSPNTKRLNLEAVGVELDQAGAVKVDEYSRTNIPSIWAVGD 338
Cdd:COG1249 227 LTGAKVTSVEKTGDGVTVTLEDGggeEAVEADKVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRTSVPGIYAIGD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 339 ATNRINLTPVALMEATCFANTAFGGKPTKAEYSNVACAVFCIPPLAVVGLSEEEAVEQAtGDILVFTSGFNPMKNTISGR 418
Cdd:COG1249 307 VTGGPQLAHVASAEGRVAAENILGKKPRPVDYRAIPSVVFTDPEIASVGLTEEEAREAG-IDVKVGKFPFAANGRALALG 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15230074 419 QEKTLMKLIVDEKSDKVIGASMCGPDAAEIMQGIAIALKCGATKAQFDSTVGIHPSSAEEFVTMR 483
Cdd:COG1249 386 ETEGFVKLIADAETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAA 450
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
23-483 |
2.05e-137 |
|
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: 403.84 E-value: 2.05e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 23 HYDFdlFVIGAGSGGVRAARFSANHGAKVGICElpfhpisSEEIGGvggTCVIRGCVPKKILVYGATYGGELEDAKNYGW 102
Cdd:TIGR01421 2 HYDY--LVIGGGSGGIASARRAAEHGAKALLVE-------AKKLGG---TCVNVGCVPKKVMWYASDLAERMHDAADYGF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 103 EINEKVDFTWKKLLQKKTDEILRLNNIYKRLLANAAVKLYEGEGRVVGPNEVEVrqiDGTKisYTAKHILIATGSRAQKP 182
Cdd:TIGR01421 70 YQNDENTFNWPELKEKRDAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGTVEV---NGRD--YTAPHILIATGGKPSFP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 183 -NIPGHELAITSDEALSLEEFPKRAIVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRALVARNLEGRGVNL 261
Cdd:TIGR01421 145 eNIPGAELGTDSDGFFALEELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRHERVLRSFDSMISETITEEYEKEGINV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 262 HPQTSLTQLTKTDQGIKVI--SSHGEEFVADVVLFATGRSPNTKRLNLEAVGVELDQAGAVKVDEYSRTNIPSIWAVGDA 339
Cdd:TIGR01421 225 HKLSKPVKVEKTVEGKLVIhfEDGKSIDDVDELIWAIGRKPNTKGLGLENVGIKLNEKGQIIVDEYQNTNVPGIYALGDV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 340 TNRINLTPVALMEATCFANTAFGGKPT-KAEYSNVACAVFCIPPLAVVGLSEEEAVEQATGD-ILVFTSGFNPMKNTISG 417
Cdd:TIGR01421 305 VGKVELTPVAIAAGRKLSERLFNGKTDdKLDYNNVPTVVFSHPPIGTIGLTEKEAIEKYGKEnIKVYNSSFTPMYYAMTS 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15230074 418 RQEKTLMKLIVDEKSDKVIGASMCGPDAAEIMQGIAIALKCGATKAQFDSTVGIHPSSAEEFVTMR 483
Cdd:TIGR01421 385 EKQKCRMKLVCAGKEEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEELVTMR 450
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
26-484 |
5.16e-130 |
|
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: 386.25 E-value: 5.16e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 26 FDLFVIGAGSGGVRAARFSAN-HGAKVGICEL------PFHpisseeiGGVGGTCVIRGCVPKKILVYGATYGGELEDAK 98
Cdd:TIGR01423 4 FDLVVIGAGSGGLEAGWNAATlYKKRVAVVDVqthhgpPFY-------AALGGTCVNVGCVPKKLMVTGAQYMDTLRESA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 99 NYGWEIN-EKVDFTWKKLLQKKTDEILRLNNIYKRLLANA-AVKLYEGEGRVVGPNEVEVRQI----DGTKISYTAKHIL 172
Cdd:TIGR01423 77 GFGWEFDrSSVKANWKALIAAKNKAVLDINKSYEGMFADTeGLTFFLGWGALEDKNVVLVRESadpkSAVKERLQAEHIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 173 IATGSRAQKPNIPGHELAITSDEALSLEEFPKRAIVLGGGYIAVEFASI---WRGMGATVDLFFRKELPLRGFDDEMRAL 249
Cdd:TIGR01423 157 LATGSWPQMLGIPGIEHCISSNEAFYLDEPPRRVLTVGGGFISVEFAGIfnaYKPRGGKVTLCYRNNMILRGFDSTLRKE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 250 VARNLEGRGVNLHPQTSLTQLTKTDQGIK-VISSHGEEFVADVVLFATGRSPNTKRLNLEAVGVELDQAGAVKVDEYSRT 328
Cdd:TIGR01423 237 LTKQLRANGINIMTNENPAKVTLNADGSKhVTFESGKTLDVDVVMMAIGRVPRTQTLQLDKVGVELTKKGAIQVDEFSRT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 329 NIPSIWAVGDATNRINLTPVALMEATCFANTAFGGKPTKAEYSNVACAVFCIPPLAVVGLSEEEAVEQATgDILVFTSGF 408
Cdd:TIGR01423 317 NVPNIYAIGDVTDRVMLTPVAINEGAAFVDTVFGNKPRKTDHTRVASAVFSIPPIGTCGLVEEDAAKKFE-KVAVYESSF 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15230074 409 NPMKNTISGRQEKTLMKLIVDEKSD-KVIGASMCGPDAAEIMQGIAIALKCGATKAQFDSTVGIHPSSAEEFVTMRS 484
Cdd:TIGR01423 396 TPLMHNISGSKYKKFVAKIVTNHADgTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAEELCSMRT 472
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
24-488 |
4.25e-124 |
|
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: 371.11 E-value: 4.25e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 24 YDFDLFVIGAGSGGVRAARFSANHGAKVGICELpFHPISSEEIGGVGGTCVIRGCVPKKILVYGATYGGELEDAKNYGWE 103
Cdd:TIGR01438 1 YDYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDF-VTPTPLGTRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 104 INEKVDFTWKKLLQKKTDEILRLNNIYKRLLANAAVKLYEGEGRVVGPNEVEVRQIDGTKISYTAKHILIATGSRAQKPN 183
Cdd:TIGR01438 80 VEETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERPRYPG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 184 IPG-HELAITSDEALSLEEFPKRAIVLGGGYIAVEFASIWRGMGATVDLFFRkELPLRGFDDEMRALVARNLEGRGVNLH 262
Cdd:TIGR01438 160 IPGaKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVR-SILLRGFDQDCANKVGEHMEEHGVKFK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 263 PQTSLTQLTKTDQGIKVISSHGEEFVA---DVVLFATGRSPNTKRLNLEAVGVELDQ-AGAVKVDEYSRTNIPSIWAVGD 338
Cdd:TIGR01438 239 RQFVPIKVEQIEAKVLVEFTDSTNGIEeeyDTVLLAIGRDACTRKLNLENVGVKINKkTGKIPADEEEQTNVPYIYAVGD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 339 -ATNRINLTPVALMEATCFANTAFGGKPTKAEYSNVACAVFCIPPLAVVGLSEEEAVEQ-ATGDILVFTSGFNPMKNTIS 416
Cdd:TIGR01438 319 iLEDKPELTPVAIQAGRLLAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAVEKfGEENVEVFHSYFWPLEWTIP 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15230074 417 GRQE--KTLMKLIVDEK-SDKVIGASMCGPDAAEIMQGIAIALKCGATKAQFDSTVGIHPSSAEEFVTMrSVTRR 488
Cdd:TIGR01438 399 SRDNhnKCYAKLVCNKKeNERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTL-SVTKR 472
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
25-477 |
1.85e-106 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 324.82 E-value: 1.85e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 25 DFDLFVIGAGSGGVRAARFSANHGAKVGICElpfhpisseeiGGV-GGTCVIRGCVPKKILVYGATYGGELEDAKNYGwe 103
Cdd:PRK06292 3 KYDVIVIGAGPAGYVAARRAAKLGKKVALIE-----------KGPlGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFG-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 104 IN-EKVDFTWKKLLQKKTDEILRLNN-IYKRLLANAAVKLYEGEGRVVGPNEVEVrqiDGTKIsyTAKHILIATGSRaqK 181
Cdd:PRK06292 70 IHaDGPKIDFKKVMARVRRERDRFVGgVVEGLEKKPKIDKIKGTARFVDPNTVEV---NGERI--EAKNIVIATGSR--V 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 182 PNIPGHELA-----ITSDEALSLEEFPKRAIVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRALVARNLEG 256
Cdd:PRK06292 143 PPIPGVWLIlgdrlLTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILSK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 257 RgVNLHPQTSLTQLTKTDQGIKVISSHG---EEFVADVVLFATGRSPNTKRLNLEAVGVELDQAGAVKVDEYSRTNIPSI 333
Cdd:PRK06292 223 E-FKIKLGAKVTSVEKSGDEKVEELEKGgktETIEADYVLVATGRRPNTDGLGLENTGIELDERGRPVVDEHTQTSVPGI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 334 WAVGDATNRINLTPVALMEATCFANTAFGGKPTKAEYSNVACAVFCIPPLAVVGLSEEEAvEQATGDILVftsGFNPMKN 413
Cdd:PRK06292 302 YAAGDVNGKPPLLHEAADEGRIAAENAAGDVAGGVRYHPIPSVVFTDPQIASVGLTEEEL-KAAGIDYVV---GEVPFEA 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15230074 414 TISGR---QEKTLMKLIVDEKSDKVIGASMCGPDAAEIMQGIAIALKCGATKAQFDSTVGIHPSSAE 477
Cdd:PRK06292 378 QGRARvmgKNDGFVKVYADKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSE 444
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
25-477 |
5.88e-105 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 321.32 E-value: 5.88e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 25 DFDLFVIGAGSGGVRAARFSANHGAKVGICElpfhpisSEEIGGvggTCVIRGCVPKKILVYGATYGGELEDAKNYGWEI 104
Cdd:PRK06416 4 EYDVIVIGAGPGGYVAAIRAAQLGLKVAIVE-------KEKLGG---TCLNRGCIPSKALLHAAERADEARHSEDFGIKA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 105 nEKVDFTWKKLLQKKTDEILRLNNIYKRLLANAAVKLYEGEGRVVGPNEVEVRQIDGTKIsYTAKHILIATGSRAQK-PN 183
Cdd:PRK06416 74 -ENVGIDFKKVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDGEQT-YTAKNIILATGSRPRElPG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 184 I-PGHELAITSDEALSLEEFPKRAIVLGGGYIAVEFASIWRGMGATVDLFfrkE-LP--LRGFDDEMRALVARNLEGRGV 259
Cdd:PRK06416 152 IeIDGRVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIV---EaLPriLPGEDKEISKLAERALKKRGI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 260 NLHPQTSLTQLTKTDQGIKV---ISSHGEEFVADVVLFATGRSPNTKRLNLEAVGVELDQaGAVKVDEYSRTNIPSIWAV 336
Cdd:PRK06416 229 KIKTGAKAKKVEQTDDGVTVtleDGGKEETLEADYVLVAVGRRPNTENLGLEELGVKTDR-GFIEVDEQLRTNVPNIYAI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 337 GDATNRINLTPVALMEATcFANTAFGGKPTKAEYSNVACAVFCIPPLAVVGLSEEEAVEQAtGDILVFTSGF--NPmKNT 414
Cdd:PRK06416 308 GDIVGGPMLAHKASAEGI-IAAEAIAGNPHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEG-FDVKVVKFPFagNG-KAL 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15230074 415 ISGRQEKtLMKLIVDEKSDKVIGASMCGPDAAEIMQGIAIALKCGATKAQFDSTVGIHPSSAE 477
Cdd:PRK06416 385 ALGETDG-FVKLIFDKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSE 446
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
26-477 |
8.20e-100 |
|
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: 308.03 E-value: 8.20e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 26 FDLFVIGAGSGGVRAARFSANHGAKVGICELPFhpisseeiggVGGTCVIRGCVPKKILVYGATYGGELEDAKNYGWEIn 105
Cdd:TIGR01350 2 YDVIVIGGGPGGYVAAIRAAQLGLKVALVEKEY----------LGGTCLNVGCIPTKALLHSAEVYDEIKHAKDLGIEV- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 106 EKVDFTWKKLLQKKTDEILRLNNIYKRLLANAAVKLYEGEGRVVGPNEVEVRQIDGTKiSYTAKHILIATGSRAQKPNIP 185
Cdd:TIGR01350 71 ENVSVDWEKMQKRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGENGEE-TLEAKNIIIATGSRPRSLPGP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 186 ---GHELAITSDEALSLEEFPKRAIVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRALVARNLEGRGVNLH 262
Cdd:TIGR01350 150 fdfDGKVVITSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKIL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 263 PQTSLTQLTKTDQGIKVISSHGEE--FVADVVLFATGRSPNTKRLNLEAVGVELDQAGAVKVDEYSRTNIPSIWAVGDAT 340
Cdd:TIGR01350 230 TNTKVTAVEKNDDQVTYENKGGETetLTGEKVLVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDVI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 341 NRINLTPVALMEATCFANTAFGGKPTKAEYSNVACAVFCIPPLAVVGLSEEEAVEQAtgdILVFTSGFNPMKNTISGRQE 420
Cdd:TIGR01350 310 GGPMLAHVASHEGIVAAENIAGKEPAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAG---YDVKIGKFPFAANGKALALG 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 15230074 421 KT--LMKLIVDEKSDKVIGASMCGPDAAEIMQGIAIALKCGATKAQFDSTVGIHPSSAE 477
Cdd:TIGR01350 387 ETdgFVKIIADKKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSE 445
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
24-488 |
3.30e-96 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 299.82 E-value: 3.30e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 24 YDFDLFVIGAGSGGVRAARFSANHGAKVGICELpFHPISSEEIGGVGGTCVIRGCVPKKILVYGATYGGELE-DAKNYGW 102
Cdd:PTZ00052 4 FMYDLVVIGGGSGGMAAAKEAAAHGKKVALFDY-VKPSTQGTKWGLGGTCVNVGCVPKKLMHYAANIGSIFHhDSQMYGW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 103 EINEKvdFTWKKLLQKKTDEILRLNNIYKRLLANAAVKLYEGEGRVVGPNEVEVRQIdGTKISYTAKHILIATGSRaqkP 182
Cdd:PTZ00052 83 KTSSS--FNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTVSYGDN-SQEETITAKYILIATGGR---P 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 183 NIP-----GHELAITSDEALSLEEFPKRAIVLGGGYIAVEFASIWRGMGATVDLFFRkELPLRGFDDEMRALVARNLEGR 257
Cdd:PTZ00052 157 SIPedvpgAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVR-SIPLRGFDRQCSEKVVEYMKEQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 258 GVNLHPQTSLTQLTKTDQGIKVISSHGEEFVADVVLFATGRSPNTKRLNLEAVGVELDQAGAvKVDEYSRTNIPSIWAVG 337
Cdd:PTZ00052 236 GTLFLEGVVPINIEKMDDKIKVLFSDGTTELFDTVLYATGRKPDIKGLNLNAIGVHVNKSNK-IIAPNDCTNIPNIFAVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 338 D-ATNRINLTPVALMEATCFANTAFGGKPTKAEYSNVACAVFCIPPLAVVGLSEEEAVEQ-ATGDILVFTSGFNPMKNTI 415
Cdd:PTZ00052 315 DvVEGRPELTPVAIKAGILLARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKyGEDDIEEYLQEFNTLEIAA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 416 SGRQE---------------KTLMKLIVDEKSD-KVIGASMCGPDAAEIMQGIAIALKCGATKAQFDSTVGIHPSSAEEF 479
Cdd:PTZ00052 395 VHREKherarkdeydfdvssNCLAKLVCVKSEDnKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHPTDAEVF 474
|
....*....
gi 15230074 480 VTMrSVTRR 488
Cdd:PTZ00052 475 MNL-SVTRR 482
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
25-482 |
5.66e-96 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 301.15 E-value: 5.66e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 25 DFDLFVIGAGSGGVRAARFSANHGAKVGICELPFhpisseeiggVGGTCVIRGCVPKKILVYGATYGGELEDAKNYGWEI 104
Cdd:PTZ00058 48 VYDLIVIGGGSGGMAAARRAARNKAKVALVEKDY----------LGGTCVNVGCVPKKIMFNAASIHDILENSRHYGFDT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 105 NEKVDFTwkkLLQKKTDE-ILRLNNIYKRLLANAAVKLYEGEGRVVGPNEVEVRQI------------------------ 159
Cdd:PTZ00058 118 QFSFNLP---LLVERRDKyIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLIKKVsqvdgeadesdddevtivsagvsq 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 160 --DGTKIsyTAKHILIATGSRAQKPNIPGHELAITSDEALSLEEfPKRAIVLGGGYIAVEFASIWRGMGATVDLFFRKEL 237
Cdd:PTZ00058 195 ldDGQVI--EGKNILIAVGNKPIFPDVKGKEFTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARGNR 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 238 PLRGFDDEMRALVARNLEGRGVNLHPQTSLTQLTKTDQ-GIKV-ISSHGEEFVADVVLFATGRSPNTKRLNLEAVGVeLD 315
Cdd:PTZ00058 272 LLRKFDETIINELENDMKKNNINIITHANVEEIEKVKEkNLTIyLSDGRKYEHFDYVIYCVGRSPNTEDLNLKALNI-KT 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 316 QAGAVKVDEYSRTNIPSIWAVGDA----------------------------------TNRINLTPVALMEATCFANTAF 361
Cdd:PTZ00058 351 PKGYIKVDDNQRTSVKHIYAVGDCcmvkknqeiedlnllklyneepylkkkentsgesYYNVQLTPVAINAGRLLADRLF 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 362 GGKPTKAEYSNVACAVFCIPPLAVVGLSEEEAVEQATGDIL-VFTSGFNPMKNTI----SGRQEKTLMKLIVDEKSDKVI 436
Cdd:PTZ00058 431 GPFSRTTNYKLIPSVIFSHPPIGTIGLSEQEAIDIYGKENVkIYESRFTNLFFSVydmdPAQKEKTYLKLVCVGKEELIK 510
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 15230074 437 GASMCGPDAAEIMQGIAIALKCGATKAQFDSTVGIHPSSAEEFVTM 482
Cdd:PTZ00058 511 GLHIVGLNADEILQGFAVALKMNATKADFDETIPIHPTAAEEFVTM 556
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
26-477 |
1.46e-88 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 279.01 E-value: 1.46e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 26 FDLFVIGAGSGGVRAARFSANHGAKVGICELpfhpisseeiGGVGGTCVIRGCVPKKILVYGATYGGELEDAKNYGWEIN 105
Cdd:PRK06370 6 YDAIVIGAGQAGPPLAARAAGLGMKVALIER----------GLLGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 106 EKVDFTWKKLLQKKTDEILRLNNIYKRLLANAA-VKLYEGEGRVVGPNEVEVrqiDGTKIsyTAKHILIATGSRAQKPNI 184
Cdd:PRK06370 76 GPVSVDFKAVMARKRRIRARSRHGSEQWLRGLEgVDVFRGHARFESPNTVRV---GGETL--RAKRIFINTGARAAIPPI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 185 PGHELA--ITSDEALSLEEFPKRAIVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRALVARNLEGRGVNLH 262
Cdd:PRK06370 151 PGLDEVgyLTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILEREGIDVR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 263 PQTSLTQLTKTDQGIKVI---SSHGEEFVADVVLFATGRSPNTKRLNLEAVGVELDQAGAVKVDEYSRTNIPSIWAVGDA 339
Cdd:PRK06370 231 LNAECIRVERDGDGIAVGldcNGGAPEITGSHILVAVGRVPNTDDLGLEAAGVETDARGYIKVDDQLRTTNPGIYAAGDC 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 340 TNRINLTPVALMEATCFANTAFGGKPTKAEYSNVACAVFCIPPLAVVGLSEEEAveQATG-DILVFTsgfNPMknTISGR 418
Cdd:PRK06370 311 NGRGAFTHTAYNDARIVAANLLDGGRRKVSDRIVPYATYTDPPLARVGMTEAEA--RKSGrRVLVGT---RPM--TRVGR 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15230074 419 -----QEKTLMKLIVDEKSDKVIGASMCGPDAAEIMQGIAIALKCGATKAQFDSTVGIHPSSAE 477
Cdd:PRK06370 384 avekgETQGFMKVVVDADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSE 447
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
26-477 |
5.84e-85 |
|
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: 269.68 E-value: 5.84e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 26 FDLFVIGAGSGGVRAARFSANHGAKVGICELpfhpisseeiGGVGGTCVIRGCVPKKILVYGATYGGELEDAKNYGWEIN 105
Cdd:TIGR02053 1 YDLVIIGSGAAAFAAAIKAAELGASVAMVER----------GPLGGTCVNVGCVPSKMLLRAAEVAHYARKPPFGGLAAT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 106 EKVDFTwkKLLQKKTD--EILRlNNIYKRLLANAAVKLYEGEGRVVGPNEVEVrqiDGTKISYTAKHILIATGSRAQKPN 183
Cdd:TIGR02053 71 VAVDFG--ELLEGKREvvEELR-HEKYEDVLSSYGVDYLRGRARFKDPKTVKV---DLGREVRGAKRFLIATGARPAIPP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 184 IPGHELA--ITSDEALSLEEFPKRAIVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRALVARNLEGRGVNL 261
Cdd:TIGR02053 145 IPGLKEAgyLTSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSDRLLPREEPEISAAVEEALAEEGIEV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 262 HPQTSLTQLTKtDQGIKVISSHGE----EFVADVVLFATGRSPNTKRLNLEAVGVELDQAGAVKVDEYSRTNIPSIWAVG 337
Cdd:TIGR02053 225 VTSAQVKAVSV-RGGGKIITVEKPggqgEVEADELLVATGRRPNTDGLGLEKAGVKLDERGGILVDETLRTSNPGIYAAG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 338 DATNRINLTPVALMEATCFANTAFGGKPTKAEYSNVACAVFCIPPLAVVGLSEEEAVEQAtgdiLVFTSGFNPMKNTISG 417
Cdd:TIGR02053 304 DVTGGLQLEYVAAKEGVVAAENALGGANAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAG----IECDCRTLPLTNVPRA 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15230074 418 ---RQEKTLMKLIVDEKSDKVIGASMCGPDAAEIMQGIAIALKCGATKAQFDSTVGIHPSSAE 477
Cdd:TIGR02053 380 rinRDTRGFIKLVAEPGTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAE 442
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
26-353 |
2.23e-75 |
|
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: 239.53 E-value: 2.23e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 26 FDLFVIGAGSGGVRAARFSANHGAKVGICELpfhpisseeiggvGGTCVIRGCVPKKILVYgatYGGELEDAKNygwein 105
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIED-------------EGTCPYGGCVLSKALLG---AAEAPEIASL------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 106 ekvdftWKKLLQKKTDEILRLNNIYKRLLANAAVKLYEGEGRVVGPNEVevrqiDGTKISYTAKHILIATGSRAQKPNIP 185
Cdd:pfam07992 59 ------WADLYKRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELV-----DGDGETITYDRLVIATGARPRLPPIP 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 186 GHEL-------AITSDEALSLEEFPKRAIVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRALVARNLEGRG 258
Cdd:pfam07992 128 GVELnvgflvrTLDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 259 VNLHPQTSLTQLTKTDQGIKVISSHGEEFVADVVLFATGRSPNTKrlNLEAVGVELDQAGAVKVDEYSRTNIPSIWAVGD 338
Cdd:pfam07992 208 VEVRLGTSVKEIIGDGDGVEVILKDGTEIDADLVVVAIGRRPNTE--LLEAAGLELDERGGIVVDEYLRTSVPGIYAAGD 285
|
330
....*....|....*.
gi 15230074 339 AT-NRINLTPVALMEA 353
Cdd:pfam07992 286 CRvGGPELAQNAVAQG 301
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
25-477 |
3.53e-75 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 243.71 E-value: 3.53e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 25 DFDLFVIGAGSGG-VRAARFsanHGAKVGICELpfhpisseeiGGVGGTCVIRGCVPKKILVYGATYGGELEDAKNYGwe 103
Cdd:PRK07846 1 HYDLIIIGTGSGNsILDERF---ADKRIAIVEK----------GTFGGTCLNVGCIPTKMFVYAADVARTIREAARLG-- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 104 inekVDFT-----WKKLLQK---KTDEILRLNNIYkRLLANAAVKLYEGEGRVVGPNEVEVRqiDGTKIsyTAKHILIAT 175
Cdd:PRK07846 66 ----VDAEldgvrWPDIVSRvfgRIDPIAAGGEEY-RGRDTPNIDVYRGHARFIGPKTLRTG--DGEEI--TADQVVIAA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 176 GSRAQKPNIPGHELAI--TSDEALSLEEFPKRAIVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRALVARn 253
Cdd:PRK07846 137 GSRPVIPPVIADSGVRyhTSDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLDDDISERFTE- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 254 LEGRGVNLHPQTSLTQLTKTDQGIKVISSHGEEFVADVVLFATGRSPNTKRLNLEAVGVELDQAGAVKVDEYSRTNIPSI 333
Cdd:PRK07846 216 LASKRWDVRLGRNVVGVSQDGSGVTLRLDDGSTVEADVLLVATGRVPNGDLLDAAAAGVDVDEDGRVVVDEYQRTSAEGV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 334 WAVGDATNRINLTPVALMEATCFA-NTAFGGKPTKAEYSNVACAVFCIPPLAVVGLSEEEAVE---------QATGDI-- 401
Cdd:PRK07846 296 FALGDVSSPYQLKHVANHEARVVQhNLLHPDDLIASDHRFVPAAVFTHPQIASVGLTENEARAaglditvkvQNYGDVay 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 402 ---LVFTSGFnpmkntisgrqektlMKLIVDEKSDKVIGASMCGPDAAEIMQGIAIALKCGATKAQF-DSTVGIHPSSAE 477
Cdd:PRK07846 376 gwaMEDTTGF---------------VKLIADRDTGRLLGAHIIGPQASTLIQPLIQAMSFGLDAREMaRGQYWIHPALPE 440
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
22-461 |
4.70e-67 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 222.72 E-value: 4.70e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 22 THYDFDLFVIGAGSGGVRAARFSANHGAKVGICElpfhpisseEIGGVGGTCVIRGCVPKKILVYGATYGGELEDAKNYG 101
Cdd:PRK05249 2 HMYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIE---------RYRNVGGGCTHTGTIPSKALREAVLRLIGFNQNPLYS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 102 wEINEKVDFTWKKLLQKKTDEILRLNNIYKRLLANAAVKLYEGEGRVVGPNEVEVRQIDGTKISYTAKHILIATGSR-AQ 180
Cdd:PRK05249 73 -SYRVKLRITFADLLARADHVINKQVEVRRGQYERNRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATGSRpYR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 181 KPNIP-GHELAITSDEALSLEEFPKRAIVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRALVARNLEGRGV 259
Cdd:PRK05249 152 PPDVDfDHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSFLDDEISDALSYHLRDSGV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 260 NLHPQTSLTQLTKTDQGIKVISSHGEEFVADVVLFATGRSPNTKRLNLEAVGVELDQAGAVKVDEYSRTNIPSIWAVGDA 339
Cdd:PRK05249 232 TIRHNEEVEKVEGGDDGVIVHLKSGKKIKADCLLYANGRTGNTDGLNLENAGLEADSRGQLKVNENYQTAVPHIYAVGDV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 340 TNRINLTPVAlMEATCFANTAFGGKPTKAEYSNVACAVFCIPPLAVVGLSEEEAVEQAtGDILVFTSGFnpmKNT----I 415
Cdd:PRK05249 312 IGFPSLASAS-MDQGRIAAQHAVGEATAHLIEDIPTGIYTIPEISSVGKTEQELTAAK-VPYEVGRARF---KELaraqI 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 15230074 416 SGrQEKTLMKLIVDEKSDKVIGASMCGPDAAEIMQ-GIAIaLKCGAT 461
Cdd:PRK05249 387 AG-DNVGMLKILFHRETLEILGVHCFGERATEIIHiGQAI-MEQKGT 431
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
26-479 |
3.84e-61 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 206.52 E-value: 3.84e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 26 FDLFVIGAGSGGVRAARFSANHGAKVGICElpfhpissEEIGGVGGTCVIRGCVPKKILVYGATYGGELEDAknygweIN 105
Cdd:PRK07251 4 YDLIVIGFGKAGKTLAAKLASAGKKVALVE--------ESKAMYGGTCINIGCIPTKTLLVAAEKNLSFEQV------MA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 106 EKVDFTwkkllqkktdeiLRLNNIYKRLLANAAVKLYEGEGRVVGPNEVEVRQIDgTKISYTAKHILIATGSRAQKPNIP 185
Cdd:PRK07251 70 TKNTVT------------SRLRGKNYAMLAGSGVDLYDAEAHFVSNKVIEVQAGD-EKIELTAETIVINTGAVSNVLPIP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 186 GheLAIT-----SDEALSLEEFPKRAIVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRALVARNLEGRGVN 260
Cdd:PRK07251 137 G--LADSkhvydSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYMEEDGIT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 261 LHPQTSLTQLtKTDQGIKVISSHGEEFVADVVLFATGRSPNTKRLNLEAVGVELDQAGAVKVDEYSRTNIPSIWAVGDAT 340
Cdd:PRK07251 215 FLLNAHTTEV-KNDGDQVLVVTEDETYRFDALLYATGRKPNTEPLGLENTDIELTERGAIKVDDYCQTSVPGVFAVGDVN 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 341 NRINLTPVALMEATCFANTAFG-GKPTKAEYSNVACAVFCIPPLAVVGLSEEEAVEQ----ATGDILVFTSGFNPMKNTI 415
Cdd:PRK07251 294 GGPQFTYISLDDFRIVFGYLTGdGSYTLEDRGNVPTTMFITPPLSQVGLTEKEAKEAglpyAVKELLVAAMPRAHVNNDL 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15230074 416 SGrqektLMKLIVDEKSDKVIGASMCGPDAAEIMQGIAIALKCGATKAQFDSTVGIHPSSAEEF 479
Cdd:PRK07251 374 RG-----AFKVVVNTETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAENL 432
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
25-477 |
4.55e-60 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 204.77 E-value: 4.55e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 25 DFDLFVIGAGSGGVRAARFSANHGAKVGICELPFHPISSEEIGGvggTCVIRGCVPKKILVYGAtygGELEDAKN----Y 100
Cdd:PRK06327 4 QFDVVVIGAGPGGYVAAIRAAQLGLKVACIEAWKNPKGKPALGG---TCLNVGCIPSKALLASS---EEFENAGHhfadH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 101 GWEINE-KVDFtwKKLLQKKTDEILRLNNIYKRLLANAAVKLYEGEGRVVG----PNEVEVRQIDGTKIsyTAKHILIAT 175
Cdd:PRK06327 78 GIHVDGvKIDV--AKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVGktdaGYEIKVTGEDETVI--TAKHVIIAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 176 GSRAQK-PNIP-GHELAITSDEALSLEEFPKRAIVLGGGYIAVEFASIWRGMGATVDLFfrKELP--LRGFDDEMRALVA 251
Cdd:PRK06327 154 GSEPRHlPGVPfDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTIL--EALPafLAAADEQVAKEAA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 252 RNLEGRGVNLHPQTSLTQLTKTDQGIKV--ISSHGEE--FVADVVLFATGRSPNTKRLNLEAVGVELDQAGAVKVDEYSR 327
Cdd:PRK06327 232 KAFTKQGLDIHLGVKIGEIKTGGKGVSVayTDADGEAqtLEVDKLIVSIGRVPNTDGLGLEAVGLKLDERGFIPVDDHCR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 328 TNIPSIWAVGDATNRINLTPVALMEATCFANTAFGGKPtKAEYSNVACAVFCIPPLAVVGLSEEEAVEQAtgdiLVFTSG 407
Cdd:PRK06327 312 TNVPNVYAIGDVVRGPMLAHKAEEEGVAVAERIAGQKG-HIDYNTIPWVIYTSPEIAWVGKTEQQLKAEG----VEYKAG 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15230074 408 FNPMKntISGR-----QEKTLMKLIVDEKSDKVIGASMCGPDAAEIMQGIAIALKCGATKAQFDSTVGIHPSSAE 477
Cdd:PRK06327 387 KFPFM--ANGRalamgEPDGFVKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSE 459
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
30-457 |
3.44e-56 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 196.53 E-value: 3.44e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 30 VIGAGSGGVRAARFSANHGAKVGICELpfhpisseeiGGVGGTCVIRGCVPKKILVYGATYGGELEDAKNYGWEINEKVD 109
Cdd:PRK13748 103 VIGSGGAAMAAALKAVEQGARVTLIER----------GTIGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDGGIAATVPT 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 110 FTWKKLL---QKKTDEiLRLNNiYKRLLA-NAAVKLYEGEGRVVGPNEVEVRQIDGTKISYTAKHILIATGSRAQKPNIP 185
Cdd:PRK13748 173 IDRSRLLaqqQARVDE-LRHAK-YEGILDgNPAITVLHGEARFKDDQTLIVRLNDGGERVVAFDRCLIATGASPAVPPIP 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 186 GheLA----ITSDEALSLEEFPKRAIVLGGGYIAVEFASIWRGMGATV------DLFFRkELPLRGfddemRALVARnLE 255
Cdd:PRK13748 251 G--LKetpyWTSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVtilarsTLFFR-EDPAIG-----EAVTAA-FR 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 256 GRGVNLHPQTSLTQLTKTDQGIKVISSHGEeFVADVVLFATGRSPNTKRLNLEAVGVELDQAGAVKVDEYSRTNIPSIWA 335
Cdd:PRK13748 322 AEGIEVLEHTQASQVAHVDGEFVLTTGHGE-LRADKLLVATGRAPNTRSLALDAAGVTVNAQGAIVIDQGMRTSVPHIYA 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 336 VGDATNRINLTPVALMEATCFANTAFGGKpTKAEYSNVACAVFCIPPLAVVGLSEEEAVEQAT-GDILVFTsgfnpMKNT 414
Cdd:PRK13748 401 AGDCTDQPQFVYVAAAAGTRAAINMTGGD-AALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIeTDSRTLT-----LDNV 474
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 15230074 415 ---ISGRQEKTLMKLIVDEKSDKVIGASMCGPDAAEIMQGIAIALK 457
Cdd:PRK13748 475 praLANFDTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAALAIR 520
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
26-487 |
3.18e-50 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 177.51 E-value: 3.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 26 FDLFVIGAGSGGVRAARFSANHGAKVGICElpfhpissEEIGGVGGTCVIRGCVPKKILVYGATYGGELEDAKNygwEIN 105
Cdd:PRK08010 4 YQAVIIGFGKAGKTLAVTLAKAGWRVALIE--------QSNAMYGGTCINIGCIPTKTLVHDAQQHTDFVRAIQ---RKN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 106 EKVDFtwkkLLQKKTDEILRLNNIykrllanaavKLYEGEGRVVGPNEVEVRQIDGTKISYTAKhILIATGSRAQKPNIP 185
Cdd:PRK08010 73 EVVNF----LRNKNFHNLADMPNI----------DVIDGQAEFINNHSLRVHRPEGNLEIHGEK-IFINTGAQTVVPPIP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 186 GhelaIT-------SDEALSLEEFPKRAIVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRALVARNLEGRG 258
Cdd:PRK08010 138 G----ITttpgvydSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 259 VNLHPQTSLTQLTKTDQGIKVISSHGEEFVaDVVLFATGRSPNTKRLNLEAVGVELDQAGAVKVDEYSRTNIPSIWAVGD 338
Cdd:PRK08010 214 VDIILNAHVERISHHENQVQVHSEHAQLAV-DALLIASGRQPATASLHPENAGIAVNERGAIVVDKYLHTTADNIWAMGD 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 339 ATNRINLTPVALMEATCFANTAFG-GKPTKAEYSNVACAVFCIPPLAVVGLSEEEAVEQAtGDILVFTSGFNPMKNTISG 417
Cdd:PRK08010 293 VTGGLQFTYISLDDYRIVRDELLGeGKRSTDDRKNVPYSVFMTPPLSRVGMTEEQARESG-ADIQVVTLPVAAIPRARVM 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 418 RQEKTLMKLIVDEKSDKVIGASMCGPDAAEIMQGIAIALKCGATKAQFDSTVGIHPSSAEEFVTMRSVTR 487
Cdd:PRK08010 372 NDTRGVLKAIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLNDLFSLVK 441
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
30-474 |
3.36e-48 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 172.74 E-value: 3.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 30 VIGAGSGGVRAARFSANHGAKVGICElpfhpissEEigGVGGTCVIRGCVPKKILVYGATYGGELEDAKNYGWE------ 103
Cdd:PRK07845 6 IIGGGPGGYEAALVAAQLGADVTVIE--------RD--GLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRfiddge 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 104 -------INEKVdftwKKLLQKKTDEIlrlnniyKRLLANAAVKLYEGEGRV----VGPNEVEVRQIDGTKISYTAKHIL 172
Cdd:PRK07845 76 arvdlpaVNARV----KALAAAQSADI-------RARLEREGVRVIAGRGRLidpgLGPHRVKVTTADGGEETLDADVVL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 173 IATGSRaqkPNI-----PGHELAITSDEALSLEEFPKRAIVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMR 247
Cdd:PRK07845 145 IATGAS---PRIlptaePDGERILTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPGEDADAA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 248 ALVARNLEGRGVNLHPQTSLTQLTKTDQGIKVISSHGEEFVADVVLFATGRSPNTKRLNLEAVGVELDQAGAVKVDEYSR 327
Cdd:PRK07845 222 EVLEEVFARRGMTVLKRSRAESVERTGDGVVVTLTDGRTVEGSHALMAVGSVPNTAGLGLEEAGVELTPSGHITVDRVSR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 328 TNIPSIWAVGDATNRINLTPVALMEATCFANTAFGGKPTKAEYSNVACAVFCIPPLAVVGLSEEEAVE-QATGDILVFTS 406
Cdd:PRK07845 302 TSVPGIYAAGDCTGVLPLASVAAMQGRIAMYHALGEAVSPLRLKTVASNVFTRPEIATVGVSQAAIDSgEVPARTVMLPL 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15230074 407 GFNP---MKNTISGrqektLMKLIVDEKSDKVIGASMCGPDAAEIMQGIAIALKCGATKAQFDSTVGIHPS 474
Cdd:PRK07845 382 ATNPrakMSGLRDG-----FVKLFCRPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYPS 447
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
152-378 |
5.16e-42 |
|
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: 152.27 E-value: 5.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 152 NEVEVRqiDGTKISYTakHILIATGSRAQKPNIPGHELA-ITS----DEALSLEEF-----PKRAIVLGGGYIAVEFASI 221
Cdd:COG0446 67 KTVTLR--DGETLSYD--KLVLATGARPRPPPIPGLDLPgVFTlrtlDDADALREAlkefkGKRAVVIGGGPIGLELAEA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 222 WRGMGATVDLFFRKELPLRGFDDEMRALVARNLEGRGVNLHPQTSLTQLtKTDQGIKVISSHGEEFVADVVLFATGRSPN 301
Cdd:COG0446 143 LRKRGLKVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAI-DGDDKVAVTLTDGEEIPADLVVVAPGVRPN 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 302 TKrLnLEAVGVELDQAGAVKVDEYSRTNIPSIWAVGDATN----------RINLTPVALMEATCFANTAFGGKPTKAEYS 371
Cdd:COG0446 222 TE-L-AKDAGLALGERGWIKVDETLQTSDPDVYAAGDCAEvphpvtgktvYIPLASAANKQGRVAAENILGGPAPFPGLG 299
|
....*..
gi 15230074 372 NVACAVF 378
Cdd:COG0446 300 TFISKVF 306
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
373-482 |
6.09e-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: 131.91 E-value: 6.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 373 VACAVFCIPPLAVVGLSEEEAVEQaTGDILVFTSGFNPMKNTISGRQEKTLMKLIVDEKSDKVIGASMCGPDAAEIMQGI 452
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEK-GGEVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQEA 79
|
90 100 110
....*....|....*....|....*....|
gi 15230074 453 AIALKCGATKAQFDSTVGIHPSSAEEFVTM 482
Cdd:pfam02852 80 ALAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
26-477 |
3.10e-34 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 136.58 E-value: 3.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 26 FDLFVIGAGSGGVRAARFSANHGAKVGIcelpfhpISSEEiGGVGGTCVIRGCVPKKILVYGA-------------TYG- 91
Cdd:PTZ00153 117 YDVGIIGCGVGGHAAAINAMERGLKVII-------FTGDD-DSIGGTCVNVGCIPSKALLYATgkyrelknlaklyTYGi 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 92 --GELEDAKNYGWEINEKVDFTWK----KLLQKKTDEILRLNNIYKRLLANAAVKLYEGEGRVVG-PNEVEVRQIDGTKI 164
Cdd:PTZ00153 189 ytNAFKNGKNDPVERNQLVADTVQiditKLKEYTQSVIDKLRGGIENGLKSKKFCKNSEHVQVIYeRGHIVDKNTIKSEK 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 165 S---YTAKHILIATGSraqKPNIPGH-----ELAITSDEALSLEEFPKRAIVLGGGYIAVEFASIWRGMGATVDLFFRKE 236
Cdd:PTZ00153 269 SgkeFKVKNIIIATGS---TPNIPDNievdqKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSP 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 237 LPLRGFDDEMRALVARN-LEGRGVNLHPQTSLTQL-----------------TKTDQGIKVISSHGEEFVADVVLFATGR 298
Cdd:PTZ00153 346 QLLPLLDADVAKYFERVfLKSKPVRVHLNTLIEYVragkgnqpviighserqTGESDGPKKNMNDIKETYVDSCLVATGR 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 299 SPNTKRLNLEAVGVELDQaGAVKVDEYSRTN------IPSIWAVGDATNRINLTPVALMEA------------TCFANTA 360
Cdd:PTZ00153 426 KPNTNNLGLDKLKIQMKR-GFVSVDEHLRVLredqevYDNIFCIGDANGKQMLAHTASHQAlkvvdwiegkgkENVNINV 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 361 FGGKPTKAEYSNVACAVFCIPPLAVVGLSEEEAVE-QATGDILVFTSGF----------------NPMKNTISGRQEKT- 422
Cdd:PTZ00153 505 ENWASKPIIYKNIPSVCYTTPELAFIGLTEKEAKElYPPDNVGVEISFYkanskvlcennisfpnNSKNNSYNKGKYNTv 584
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 423 -----LMKLIVDEKSDKVIGASMCGPDAAEIMQGIAIALKCGATKAQFDSTVGIHPSSAE 477
Cdd:PTZ00153 585 dntegMVKIVYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISE 644
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
160-338 |
2.42e-33 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 130.65 E-value: 2.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 160 DGTKISYtaKHILIATGSRAQKPNIPGHELA-----ITSDEALSLEEF---PKRAIVLGGGYIAVEFASIWRGMGATVDL 231
Cdd:COG1251 93 DGETLPY--DKLVLATGSRPRVPPIPGADLPgvftlRTLDDADALRAAlapGKRVVVIGGGLIGLEAAAALRKRGLEVTV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 232 FFRKELPL-RGFDDEMRALVARNLEGRGVNLHPQTSLTQLTKTDQGIKVISSHGEEFVADVVLFATGRSPNTkRLnLEAV 310
Cdd:COG1251 171 VERAPRLLpRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRLADGEELPADLVVVAIGVRPNT-EL-ARAA 248
|
170 180
....*....|....*....|....*...
gi 15230074 311 GVELDqaGAVKVDEYSRTNIPSIWAVGD 338
Cdd:COG1251 249 GLAVD--RGIVVDDYLRTSDPDIYAAGD 274
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
152-464 |
1.19e-27 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 115.14 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 152 NEVEVRQID-GTKISYTAKHILIATGSRAQKPNIPGHEL-----------AITSDEALSLEEFpKRAIVLGGGYIAVEFA 219
Cdd:PRK09564 87 KTITVKNLKtGSIFNDTYDKLMIATGARPIIPPIKNINLenvytlksmedGLALKELLKDEEI-KNIVIIGAGFIGLEAV 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 220 SIWRGMGATVDLFFRKELPL-RGFDDEMRALVARNLEGRGVNLHPQTSLTQLTKTDQGIKVISSHGEeFVADVVLFATGR 298
Cdd:PRK09564 166 EAAKHLGKNVRIIQLEDRILpDSFDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEGVVTDKGE-YEADVVIVATGV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 299 SPNTKRLnlEAVGVELDQAGAVKVDEYSRTNIPSIWAVGD-AT--NRINLTPVALMEATCF--------ANTAFGGKPTK 367
Cdd:PRK09564 245 KPNTEFL--EDTGLKTLKNGAIIVDEYGETSIENIYAAGDcATiyNIVSNKNVYVPLATTAnklgrmvgENLAGRHVSFK 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 368 AEYSNVACAVFCIpPLAVVGLSEEEAVEQATGDILVFTSGFNpMKNTISGrQEKTLMKLIVDEKSDKVIGASMCGP-DAA 446
Cdd:PRK09564 323 GTLGSACIKVLDL-EAARTGLTEEEAKKLGIDYKTVFIKDKN-HTNYYPG-QEDLYVKLIYEADTKVILGGQIIGKkGAV 399
|
330
....*....|....*...
gi 15230074 447 EIMQGIAIALKCGATKAQ 464
Cdd:PRK09564 400 LRIDALAVAIYAKLTTQE 417
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
80-388 |
9.34e-21 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 94.04 E-value: 9.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 80 PKKILVYGATYGG-----ELEDAKNYGWE---INEKVDFTWKKLL------QKKTDEIlRLNniYKRLLANAAVKLYEGE 145
Cdd:COG1252 1 MKRIVIVGGGFAGleaarRLRKKLGGDAEvtlIDPNPYHLFQPLLpevaagTLSPDDI-AIP--LRELLRRAGVRFIQGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 146 grVVG--PNEvevRQI---DGTKISYTakHILIATGSRAQKPNIPG-HELAI---TSDEALS----LEEFPKRA------ 206
Cdd:COG1252 78 --VTGidPEA---RTVtlaDGRTLSYD--YLVIATGSVTNFFGIPGlAEHALplkTLEDALAlrerLLAAFERAerrrll 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 207 --IVLGGGYIAVEFA----------SIWRGMG---ATVDLFFRKELPLRGFDDEMRALVARNLEGRGVNLHPQTSLTQLT 271
Cdd:COG1252 151 tiVVVGGGPTGVELAgelaellrklLRYPGIDpdkVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 272 KTdqgiKVISSHGEEFVADVVLFATGRSPNTKrlnLEAVGVELDQAGAVKVDEYSRT-NIPSIWAVGDATNRINLT---- 346
Cdd:COG1252 231 AD----GVTLEDGEEIPADTVIWAAGVKAPPL---LADLGLPTDRRGRVLVDPTLQVpGHPNVFAIGDCAAVPDPDgkpv 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 15230074 347 ----PVALMEATCFANT---AFGGKPTKA-EYSNVAC--------AVFCIPPLAVVGL 388
Cdd:COG1252 304 pktaQAAVQQAKVLAKNiaaLLRGKPLKPfRYRDKGClaslgrgaAVADVGGLKLSGF 361
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
166-340 |
2.17e-20 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 91.72 E-value: 2.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 166 YTAKHILIATGSRAQKPNIPGHEL--------AITSDealsLEEFP-KRAIVLGGGYIAVEFASIWRGMGATVDLFFRKe 236
Cdd:COG0492 99 YEAKAVIIATGAGPRKLGLPGEEEfegrgvsyCATCD----GFFFRgKDVVVVGGGDSALEEALYLTKFASKVTLIHRR- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 237 lplrgfdDEMRA---LVARNLEGRGVNLHPQTSLTQLTKTD--QGIKVISSH-GEEFV--ADVVLFATGRSPNTKrlNLE 308
Cdd:COG0492 174 -------DELRAskiLVERLRANPKIEVLWNTEVTEIEGDGrvEGVTLKNVKtGEEKEleVDGVFVAIGLKPNTE--LLK 244
|
170 180 190
....*....|....*....|....*....|..
gi 15230074 309 AVGVELDQAGAVKVDEYSRTNIPSIWAVGDAT 340
Cdd:COG0492 245 GLGLELDEDGYIVVDEDMETSVPGVFAAGDVR 276
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
121-363 |
8.35e-20 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 91.13 E-value: 8.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 121 DEILRLNNIykRLLANAAVKLYEGEGRVVgpnevevrQIDGTKISYtAKHILiATGSRAQKPNIPGHELAITSDealSLE 200
Cdd:PRK04965 65 GEFAEQFNL--RLFPHTWVTDIDAEAQVV--------KSQGNQWQY-DKLVL-ATGASAFVPPIPGRELMLTLN---SQQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 201 EF---------PKRAIVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFddeMRALVARNLEGR----GVNLHPQTSL 267
Cdd:PRK04965 130 EYraaetqlrdAQRVLVVGGGLIGTELAMDLCRAGKAVTLVDNAASLLASL---MPPEVSSRLQHRltemGVHLLLKSQL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 268 TQLTKTDQGIKVISSHGEEFVADVVLFATGRSPNTKrLNLEAvGVELDQagAVKVDEYSRTNIPSIWAVGDATnRIN--- 344
Cdd:PRK04965 207 QGLEKTDSGIRATLDSGRSIEVDAVIAAAGLRPNTA-LARRA-GLAVNR--GIVVDSYLQTSAPDIYALGDCA-EINgqv 281
|
250 260
....*....|....*....|..
gi 15230074 345 ---LTPvALMEATCFANTAFGG 363
Cdd:PRK04965 282 lpfLQP-IQLSAMALAKNLLGQ 302
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
205-280 |
1.33e-16 |
|
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: 74.55 E-value: 1.33e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15230074 205 RAIVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRALVARNLEGRGVNLHPQTSLTQLTKTDQGIKVI 280
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVV 76
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
139-476 |
2.39e-15 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 79.10 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 139 VKLYEGEgRVVGPNEVEVRQIDGTKISYTAKHILIATGSRAQKPNIPGHEL-AITS-------DEALSLEEFPKRAIVLG 210
Cdd:TIGR02374 69 ITLYTGE-TVIQIDTDQKQVITDAGRTLSYDKLILATGSYPFILPIPGADKkGVYVfrtiedlDAIMAMAQRFKKAAVIG 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 211 GGYIAVEFASIWRGMGATVDLF-FRKELPLRGFDDEMRALVARNLEGRGVNLHPQTSLTQLTKTDQGIKVISSHGEEFVA 289
Cdd:TIGR02374 148 GGLLGLEAAVGLQNLGMDVSVIhHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVGATKADRIRFKDGSSLEA 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 290 DVVLFATGRSPNTKRlnleAVGVELDQAGAVKVDEYSRTNIPSIWAVGDatnrinltpVALMEATCFANTAFGGKPTKAE 369
Cdd:TIGR02374 228 DLIVMAAGIRPNDEL----AVSAGIKVNRGIIVNDSMQTSDPDIYAVGE---------CAEHNGRVYGLVAPLYEQAKVL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 370 YSNVaCAVFCIPplavvglsEEEAVEQATGDIL---VFTSG-FNPMKNT----ISGRQEKTLMKLIVDEksDKVIGASMC 441
Cdd:TIGR02374 295 ADHI-CGVECEE--------YEGSDLSAKLKLLgvdVWSAGdAQETERTtsikIYDEQKGIYKKLVLSD--DKLLGAVLF 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15230074 442 GP------------DAAEIMQGIAIALKCGATKAQFDSTVGIHPSSA 476
Cdd:TIGR02374 364 GDtsdygrlldmvlKQADISEDPAIIKPQISGPEAGGPGVEAMPDSE 410
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
204-339 |
2.47e-13 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 71.74 E-value: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 204 KRAIVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRALVARNLEGRGVNLHPQTSLTQLTktDQGIKVISSH 283
Cdd:PRK13512 149 DKALVVGAGYISLEVLENLYERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDAIN--GNEVTFKSGK 226
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 15230074 284 GEEFvaDVVLFATGRSPNTKRLnlEAVGVELDQAGAVKVDEYSRTNIPSIWAVGDA 339
Cdd:PRK13512 227 VEHY--DMIIEGVGTHPNSKFI--ESSNIKLDDKGFIPVNDKFETNVPNIYAIGDI 278
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
171-341 |
8.12e-13 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 69.63 E-value: 8.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 171 ILIATGS-RAQKPNIPGHEL-----------AITSDE--ALSLEEFP----KRAIVLGGGYIAVEFASIWRGMGA-TVDL 231
Cdd:PRK12770 122 VLIATGTwKSRKLGIPGEDLpgvysaleylfRIRAAKlgYLPWEKVPpvegKKVVVVGAGLTAVDAALEAVLLGAeKVYL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 232 FFR---KELPLRGFddEMRALVARNLE---------------GRGVNLhPQTSLTQLTKTDQGIKVISShGEEFV--ADV 291
Cdd:PRK12770 202 AYRrtiNEAPAGKY--EIERLIARGVEflelvtpvriigegrVEGVEL-AKMRLGEPDESGRPRPVPIP-GSEFVleADT 277
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15230074 292 VLFATGRSPnTKRLNLEAVGVELDQAGAVKVDEYSRTNIPSIWAVGDATN 341
Cdd:PRK12770 278 VVFAIGEIP-TPPFAKECLGIELNRKGEIVVDEKHMTSREGVFAAGDVVT 326
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
158-337 |
2.81e-12 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 67.25 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 158 QIDGTKISYTAKHILIATGsRAQKPNIPG-HELAITSDEALSLEEFP-KRAIVLGGGYIAVEFA-SIWRgMGATVDLFFR 234
Cdd:pfam13738 109 VVTTSKGTYQARYVIIATG-EFDFPNKLGvPELPKHYSYVKDFHPYAgQKVVVIGGYNSAVDAAlELVR-KGARVTVLYR 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 235 KELPLRGFDDEMRALVARNLE-------GRGVNLHPQTSLTQLTKTDQGIKVISSHGEEF-VADVVLFATGRSPNTKRln 306
Cdd:pfam13738 187 GSEWEDRDSDPSYSLSPDTLNrleelvkNGKIKAHFNAEVKEITEVDVSYKVHTEDGRKVtSNDDPILATGYHPDLSF-- 264
|
170 180 190
....*....|....*....|....*....|..
gi 15230074 307 LEAVGVELDQAGAVKVD-EYSRTNIPSIWAVG 337
Cdd:pfam13738 265 LKKGLFELDEDGRPVLTeETESTNVPGLFLAG 296
|
|
| IucD |
COG3486 |
Lysine/ornithine N-monooxygenase [Secondary metabolites biosynthesis, transport and catabolism] ... |
153-343 |
8.04e-11 |
|
Lysine/ornithine N-monooxygenase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442709 [Multi-domain] Cd Length: 440 Bit Score: 64.03 E-value: 8.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 153 EVEVRQIDGTKISYTAKHILIATGSRaqkPNIP------GHELAITSDEALS-LEEF--PKRAIVLGGGYIAVE-----F 218
Cdd:COG3486 134 RVTVRDGTGERETYRARNLVLGTGTR---PYLPecfrglPGERVFHSSEYLHrKEDLqaAKRVTVVGSGQSAAEifldlL 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 219 ASIWRGmGATVDLFFRKE---------LPLRGFD---------------DEM--------------------RALVARNL 254
Cdd:COG3486 211 RRQDGP-GAELTWVTRSPgffpldyskFTNEIFSpeyvdyfyalpeevrDRLlaeqkllykgispdlineiyDLLYERSV 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 255 EG--RGVNLHPQTSLTQLTKTDQGIKVISSHGE-----EFVADVVLFATGRSPNTKRLnLEAVG--VELDQAGAVKVDE- 324
Cdd:COG3486 290 GGdpPRVRLLPNSEVTAVERAGGGYRLTLRHLEtgerfELETDAVVLATGYRPRLPAF-LEPLAdrIRRDEDGRLRVDRd 368
|
250
....*....|....*....
gi 15230074 325 YsrtnipSIWAVGDATNRI 343
Cdd:COG3486 369 Y------RVDWDGPRTGRI 381
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
169-341 |
2.42e-10 |
|
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: 62.46 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 169 KHILIATGsrAQKP---NIPGHEL-----AI-------TSDEALSLEEFPKRAIVLGGGYIAVEFASIWRGMGAT-VDLF 232
Cdd:COG0493 208 DAVFLATG--AGKPrdlGIPGEDLkgvhsAMdfltavnLGEAPDTILAVGKRVVVIGGGNTAMDCARTALRLGAEsVTIV 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 233 FRkelplRGFDdEMRALVARNLEGR--GVNLHPQTSLTQLTKTDQG----IKVI----------------SSHGEEFV-- 288
Cdd:COG0493 286 YR-----RTRE-EMPASKEEVEEALeeGVEFLFLVAPVEIIGDENGrvtgLECVrmelgepdesgrrrpvPIEGSEFTlp 359
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15230074 289 ADVVLFATGRSPNTKRLnLEAVGVELDQAGAVKVDEYS-RTNIPSIWAVGDATN 341
Cdd:COG0493 360 ADLVILAIGQTPDPSGL-EEELGLELDKRGTIVVDEETyQTSLPGVFAGGDAVR 412
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
149-338 |
9.30e-09 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 57.24 E-value: 9.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 149 VGPNEVEVRQIDGTKISYtaKHILIATGSRAQKpnIP-----GHELAI--TSDEALSLEEF---PKRAIVLGGGYIAVEF 218
Cdd:PRK09754 84 LGRDTRELVLTNGESWHW--DQLFIATGAAARP--LPlldalGERCFTlrHAGDAARLREVlqpERSVVIVGAGTIGLEL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 219 A--SIWRGMGATV-----DLFFRKELPLRgfddeMRALVARNLEgRGVNLHPQTSLTQLTKTDQGIKVISShGEEFVADV 291
Cdd:PRK09754 160 AasATQRRCKVTVielaaTVMGRNAPPPV-----QRYLLQRHQQ-AGVRILLNNAIEHVVDGEKVELTLQS-GETLQADV 232
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15230074 292 VLFATGRSPNTKRlnleAVGVELDQAGAVKVDEYSRTNIPSIWAVGD 338
Cdd:PRK09754 233 VIYGIGISANDQL----AREANLDTANGIVIDEACRTCDPAIFAGGD 275
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
159-338 |
4.67e-07 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 52.42 E-value: 4.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 159 IDGTKISYTAkhILIATG-SRAQKPNIPGHELA-----------ITSDEALSLEefpKRAIVLGGGYIAVEFASIWRGMG 226
Cdd:PRK12814 272 LEELQKEFDA--VLLAVGaQKASKMGIPGEELPgvisgidflrnVALGTALHPG---KKVVVIGGGNTAIDAARTALRLG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 227 A-TVDLFFRKELplrgfdDEMRALVARNLE--GRGVNLHPQTSLTQLTKTDQGIKVISS------------------HGE 285
Cdd:PRK12814 347 AeSVTILYRRTR------EEMPANRAEIEEalAEGVSLRELAAPVSIERSEGGLELTAIkmqqgepdesgrrrpvpvEGS 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15230074 286 EFV--ADVVLFATGRSPNtkRLNLEAVGVELDQAGAVKVD-EYSRTNIPSIWAVGD 338
Cdd:PRK12814 421 EFTlqADTVISAIGQQVD--PPIAEAAGIGTSRNGTVKVDpETLQTSVAGVFAGGD 474
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
170-349 |
6.17e-07 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 51.69 E-value: 6.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 170 HILIATGSRAQKPNIPGHE----------------------LAITSDEALSLEEfPKR---AIVLGGGYIAVEFAsiwrg 224
Cdd:PTZ00318 116 KLVVAHGARPNTFNIPGVEerafflkevnhargirkrivqcIERASLPTTSVEE-RKRllhFVVVGGGPTGVEFA----- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 225 mgATVDLFFRKELP---------------------LRGFDDEMRALVARNLEGRGVNLHPQTSLTQLTKTDqgikVISSH 283
Cdd:PTZ00318 190 --AELADFFRDDVRnlnpelveeckvtvleagsevLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEVLDKE----VVLKD 263
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15230074 284 GEEFVADVVLFATG--RSPNTKRLNleavgVELDQAGAVKVDEYSRT-NIPSIWAVGD--ATNRINLTPVA 349
Cdd:PTZ00318 264 GEVIPTGLVVWSTGvgPGPLTKQLK-----VDKTSRGRISVDDHLRVkPIPNVFALGDcaANEERPLPTLA 329
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
284-339 |
3.44e-06 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 49.39 E-value: 3.44e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 15230074 284 GEEFV--ADVVLFATGRSPNTKRLnLEAVGVELDQAGAVKVDEYS-RTNIPSIWAVGDA 339
Cdd:PRK12810 382 GSEFVlpADLVLLAMGFTGPEAGL-LAQFGVELDERGRVAAPDNAyQTSNPKVFAAGDM 439
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
199-309 |
1.41e-05 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 46.88 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 199 LEEFPKRAIVLGggyiAVEFASIWRGMGATVDLFFRKE----LPLRGFDDEMRALVARnlegRGVNLHPQTSLTQLTKTD 274
Cdd:COG0644 45 LEPLGLDEPLER----PVRGARFYSPGGKSVELPPGRGggyvVDRARFDRWLAEQAEE----AGAEVRTGTRVTDVLRDD 116
|
90 100 110
....*....|....*....|....*....|....*.
gi 15230074 275 QGIKVISSHGEEFVADVVLFATG-RSPNTKRLNLEA 309
Cdd:COG0644 117 GRVVVRTGDGEEIRADYVVDADGaRSLLARKLGLKR 152
|
|
| Lys_Orn_oxgnase |
pfam13434 |
L-lysine 6-monooxygenase/L-ornithine 5-monooxygenase; This is a family of Rossmann fold ... |
153-297 |
2.15e-05 |
|
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: 46.42 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 153 EVEVRQIDGTKISYTAKHILIATGSraqKPNIP----GHELAITSDEALSLEEF---PKRAIVLGGGYIAVE-FASIWRG 224
Cdd:pfam13434 133 RVRVRDADGEETTFLARNLVLGTGG---EPYIPecarGGERVFHSSEYLERIDRlaaKKRIAVVGSGQSAAEiFRDLLRR 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 225 MGAT----------------------------VDLFFRKELPLR-------------GFDDEM-----RALVARNLEG-R 257
Cdd:pfam13434 210 GPAYeltwvtrspnffplddspfvneifspeyVDYFYSLPEDTRrallreqkgtnydGIDPSLieeiyRLLYEQRVDGdP 289
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15230074 258 GVNLHPQTSLTQLTKT-DQGIKVISSH---GEEFV--ADVVLFATG 297
Cdd:pfam13434 290 RHRLLPNREVQSAERVgDGGVELTLRDgeqGREETleTDVVVLATG 335
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
138-338 |
3.77e-05 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 46.26 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 138 AVKLYEGEgRVVGPNEVE--VRQIDGTKISYtaKHILIATGSRAQKPNIPGHE-----LAITSDEALSLEEFPKRA---I 207
Cdd:PRK14989 73 GIKVLVGE-RAITINRQEkvIHSSAGRTVFY--DKLIMATGSYPWIPPIKGSEtqdcfVYRTIEDLNAIEACARRSkrgA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 208 VLGGGYIAVEFASIWRGMGATVDLF-FRKELPLRGFDDEMRALVARNLEGRGVNLHpqTSLTQLTKTDQGI---KVIS-S 282
Cdd:PRK14989 150 VVGGGLLGLEAAGALKNLGVETHVIeFAPMLMAEQLDQMGGEQLRRKIESMGVRVH--TSKNTLEIVQEGVearKTMRfA 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15230074 283 HGEEFVADVVLFATGRSPNTKRLNleAVGVELDQAGAVKVDEYSRTNIPSIWAVGD 338
Cdd:PRK14989 228 DGSELEVDFIVFSTGIRPQDKLAT--QCGLAVAPRGGIVINDSCQTSDPDIYAIGE 281
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
26-341 |
4.62e-05 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 45.92 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 26 FDLFVIGAGSGGVRAARFSANHGAKVGICelpfhpisSEEIGG-VGGTCVIRG--CVPKkilVYGATYGGELED-AKNYG 101
Cdd:PRK15317 212 YDVLVVGGGPAGAAAAIYAARKGIRTGIV--------AERFGGqVLDTMGIENfiSVPE---TEGPKLAAALEEhVKEYD 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 102 WEINEkvdftwkklLQKktdeilrlnniykrllanaAVKLYEGEGRVvgpnEVEVRqidgTKISYTAKHILIATGSRAQK 181
Cdd:PRK15317 281 VDIMN---------LQR-------------------ASKLEPAAGLI----EVELA----NGAVLKAKTVILATGARWRN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 182 PNIPGHELAITSDEALSleefP---------KRAIVLGGGYIAVEFASIWRGMGATVDLFfrkElplrgFDDEMRA---L 249
Cdd:PRK15317 325 MNVPGEDEYRNKGVAYC----PhcdgplfkgKRVAVIGGGNSGVEAAIDLAGIVKHVTVL---E-----FAPELKAdqvL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 250 V--ARNLEGRGVNLHPQTS--------LTQLTKTDQgikvisSHGEEFVADV--VLFATGRSPNTKRLNleavG-VELDQ 316
Cdd:PRK15317 393 QdkLRSLPNVTIITNAQTTevtgdgdkVTGLTYKDR------TTGEEHHLELegVFVQIGLVPNTEWLK----GtVELNR 462
|
330 340
....*....|....*....|....*
gi 15230074 317 AGAVKVDEYSRTNIPSIWAVGDATN 341
Cdd:PRK15317 463 RGEIIVDARGATSVPGVFAAGDCTT 487
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
171-341 |
7.98e-05 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 45.17 E-value: 7.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 171 ILIATG-SRAQKPNIPGHEL-----AI----TSDEALSLEEFP--KRAIVLGGGYIAVEFASIWRGMGAT-VDLFFRK-- 235
Cdd:PRK11749 229 VFIGTGaGLPRFLGIPGENLggvysAVdfltRVNQAVADYDLPvgKRVVVIGGGNTAMDAARTAKRLGAEsVTIVYRRgr 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 236 -ELPLRGFDDEmralvarNLEGRGVNLHPQTSLTQLTKTDQGIK------------------VISSHGEEFV--ADVVLF 294
Cdd:PRK11749 309 eEMPASEEEVE-------HAKEEGVEFEWLAAPVEILGDEGRVTgvefvrmelgepdasgrrRVPIEGSEFTlpADLVIK 381
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15230074 295 ATGRSPNTKRLNLEAvGVELDQAGAVKVDEYS-RTNIPSIWAVGDATN 341
Cdd:PRK11749 382 AIGQTPNPLILSTTP-GLELNRWGTIIADDETgRTSLPGVFAGGDIVT 428
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
26-77 |
8.46e-05 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 45.11 E-value: 8.46e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 15230074 26 FDLFVIGAGSGGVRAARFSANHGAKVGICElpfhpiSSEEIGGV----GGTCVIRG 77
Cdd:PRK12843 17 FDVIVIGAGAAGMSAALFAAIAGLKVLLVE------RTEYVGGTtatsAGTTWIPG 66
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
158-357 |
1.28e-03 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 40.82 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 158 QIDGTKISYTAKHILIATGSRAQKPNIPGHEL-------AITSDEALSLEEfpKRAIVLGGGYIAVEFASIWRGMGATVD 230
Cdd:PRK10262 96 RLTGDSGEYTCDALIIATGASARYLGLPSEEAfkgrgvsACATCDGFFYRN--QKVAVIGGGNTAVEEALYLSNIASEVH 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230074 231 LFFRKElplrGFDDEmRALVAR---NLEGRGVNLHPQTSLTQLTKTDQGIKVISSHGEEFVADV-------VLFATGRSP 300
Cdd:PRK10262 174 LIHRRD----GFRAE-KILIKRlmdKVENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQNSDNIesldvagLFVAIGHSP 248
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15230074 301 NTKRLNLEavgVELDQaGAVKVDE-----YSRTNIPSIWAVGDATNRINLTPVALMEATCFA 357
Cdd:PRK10262 249 NTAIFEGQ---LELEN-GYIKVQSgihgnATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMA 306
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
246-297 |
2.33e-03 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 40.27 E-value: 2.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 15230074 246 MRALvARNLEGRGVNLHPQTSLTQLTKTDQGIKVISSHGEEFVADVVLFATG 297
Cdd:COG0665 154 VRAL-ARAARAAGVRIREGTPVTGLEREGGRVTGVRTERGTVRADAVVLAAG 204
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
19-55 |
2.56e-03 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 40.47 E-value: 2.56e-03
10 20 30
....*....|....*....|....*....|....*..
gi 15230074 19 ANATHYDFDLFVIGAGSGGVRAARFSANHGAKVGICE 55
Cdd:PRK06134 6 AYPPDLECDVLVIGSGAAGLSAAVTAAWHGLKVIVVE 42
|
|
| |
