|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
1-442 |
4.50e-129 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 380.54 E-value: 4.50e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 1 MKVVVIGCTHAGTAAVKSILKNNPEADVTVYERNDNVSFLSCGIALYVGGVVKDPAGLFYSNPEELASLGAKVKMEHDVT 80
Cdd:PRK09564 1 MKIIIIGGTAAGMSAAAKAKRLNKELEITVYEKTDIVSFGACGLPYFVGGFFDDPNTMIARTPEEFIKSGIDVKTEHEVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 81 DVDTENKQVTAKDLKTGETETVSYDKLVMTTGSWPIIPPIKGIESENILLCKNYNQANEI--IAKAEEAKKVVIVGGGYI 158
Cdd:PRK09564 81 KVDAKNKTITVKNLKTGSIFNDTYDKLMIATGARPIIPPIKNINLENVYTLKSMEDGLALkeLLKDEEIKNIVIIGAGFI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 159 GIELVEAFVESGKEVTLIDGLDRILNKYLDKPFTDVLEKELVDRGVTLALGENVSEFipDENGKVKQVTTASQTFDADMV 238
Cdd:PRK09564 161 GLEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSL--IGEDKVEGVVTDKGEYEADVV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 239 ILCVGFRPNTKLVEGK-VETLPNGAIKVNEYMQTSNPDIFAAGDSAVVNYNPSGTQNYIPLATNAVRQGLLVGNNLTEQK 317
Cdd:PRK09564 239 IVATGVKPNTEFLEDTgLKTLKNGAIIVDEYGETSIENIYAAGDCATIYNIVSNKNVYVPLATTANKLGRMVGENLAGRH 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 318 MAYRGTQGTSGLYLFGWTIGSTGVTTESAPMNNLDVQATLFEDNYRPEFMPTTEKVMMELVYEKGTNRIVGAQFMSKYDI 397
Cdd:PRK09564 319 VSFKGTLGSACIKVLDLEAARTGLTEEEAKKLGIDYKTVFIKDKNHTNYYPGQEDLYVKLIYEADTKVILGGQIIGKKGA 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 498429787 398 TQSANTMSLAVQNKMTVEDLALSDFFFQPHFDRPWNYLNLLAQAA 442
Cdd:PRK09564 399 VLRIDALAVAIYAKLTTQELGMMDFCYAPPFARTWDALNVAGNVA 443
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
21-340 |
2.44e-122 |
|
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: 358.74 E-value: 2.44e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 21 KNNPEADVTVYERNDNVSFLSCGIALYVGGVVKDPAGLFYSNPEELASLGAKVKMEHDVTDVDTENKQVTakdLKTGETE 100
Cdd:COG0446 1 RLGPDAEITVIEKGPHHSYQPCGLPYYVGGGIKDPEDLLVRTPESFERKGIDVRTGTEVTAIDPEAKTVT---LRDGETL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 101 tvSYDKLVMTTGSWPIIPPIKGIESENILLCKNYNQANEIIA--KAEEAKKVVIVGGGYIGIELVEAFVESGKEVTLIDG 178
Cdd:COG0446 78 --SYDKLVLATGARPRPPPIPGLDLPGVFTLRTLDDADALREalKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVER 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 179 LDRILNKYlDKPFTDVLEKELVDRGVTLALGENVSEFIPDENGKVkqVTTASQTFDADMVILCVGFRPNTKLVEG-KVET 257
Cdd:COG0446 156 APRLLGVL-DPEMAALLEEELREHGVELRLGETVVAIDGDDKVAV--TLTDGEEIPADLVVVAPGVRPNTELAKDaGLAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 258 LPNGAIKVNEYMQTSNPDIFAAGDSAVVNYNPSGTQNYIPLATNAVRQGLLVGNNLTEQKMAYRGtQGTSGLYLFGWTIG 337
Cdd:COG0446 233 GERGWIKVDETLQTSDPDVYAAGDCAEVPHPVTGKTVYIPLASAANKQGRVAAENILGGPAPFPG-LGTFISKVFDLCIA 311
|
...
gi 498429787 338 STG 340
Cdd:COG0446 312 STG 314
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
1-344 |
4.14e-84 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 263.93 E-value: 4.14e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 1 MKVVVIGCTHAGTAAVKSILKNNPEADVTV--------YERndnvsflscgIAL--YVGGVvKDPAGLFYSNPEELASLG 70
Cdd:COG1251 2 MRIVIIGAGMAGVRAAEELRKLDPDGEITVigaephppYNR----------PPLskVLAGE-TDEEDLLLRPADFYEENG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 71 AKVKMEHDVTDVDTENKQVTakdlkTGETETVSYDKLVMTTGSWPIIPPIKGIESENILLCKNYNQANEIIAKAEEAKKV 150
Cdd:COG1251 71 IDLRLGTRVTAIDRAARTVT-----LADGETLPYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRAALAPGKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 151 VIVGGGYIGIELVEAFVESGKEVTLIDGLDRILNKYLDKPFTDVLEKELVDRGVTLALGENVSEFIPDenGKVKQVTTAS 230
Cdd:COG1251 146 VVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGD--DRVTGVRLAD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 231 -QTFDADMVILCVGFRPNTKLVEG-KVETlpNGAIKVNEYMQTSNPDIFAAGDSAVVNYNPSGtQNYIPLATNAVRQGLL 308
Cdd:COG1251 224 gEELPADLVVVAIGVRPNTELARAaGLAV--DRGIVVDDYLRTSDPDIYAAGDCAEHPGPVYG-RRVLELVAPAYEQARV 300
|
330 340 350
....*....|....*....|....*....|....*.
gi 498429787 309 VGNNLTEQKMAYRGTQGTSGLYLFGWTIGSTGVTTE 344
Cdd:COG1251 301 AAANLAGGPAAYEGSVPSTKLKVFGVDVASAGDAEG 336
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
1-306 |
3.61e-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: 237.22 E-value: 3.61e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 1 MKVVVIGCTHAGTAAVKSILKNNpeADVTVYERNDNVSFLSCGIALYVGGVVKDP------AGLFYSNPEELASLGAKVK 74
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLG--GKVTLIEDEGTCPYGGCVLSKALLGAAEAPeiaslwADLYKRKEEVVKKLNNGIE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 75 --MEHDVTDVDTENKQVTAKDLKTGETETVSYDKLVMTTGSWPIIPPIKGIESENILLCKNYNQANEIIAKAEEaKKVVI 152
Cdd:pfam07992 79 vlLGTEVVSIDPGAKKVVLEELVDGDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLLP-KRVVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 153 VGGGYIGIELVEAFVESGKEVTLIDGLDRILNkYLDKPFTDVLEKELVDRGVTLALGENVSEFIPDENGkVKQVTTASQT 232
Cdd:pfam07992 158 VGGGYIGVELAAALAKLGKEVTLIEALDRLLR-AFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDG-VEVILKDGTE 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498429787 233 FDADMVILCVGFRPNTKLVE-GKVETLPNGAIKVNEYMQTSNPDIFAAGDSAVvnynpsgtqNYIPLATNAVRQG 306
Cdd:pfam07992 236 IDADLVVVAIGRRPNTELLEaAGLELDERGGIVVDEYLRTSVPGIYAAGDCRV---------GGPELAQNAVAQG 301
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
1-442 |
2.14e-64 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 213.88 E-value: 2.14e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 1 MKVVVIGCTHAGTAAVKSILKNNPEADVTVYERNDNVSFLSCGIALYVGGVVKDPAGLFYSNPEEL-ASLGAKVKMEHDV 79
Cdd:PRK13512 2 PKIIVVGAVAGGATCASQIRRLDKESDIIIFEKDRDMSFANCALPYYIGEVVEDRKYALAYTPEKFyDRKQITVKTYHEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 80 TDVDTENKQVTAKDLKTGETETVSYDKLVMTTGSWPIIPPikgIESENILLCKNYNQANEI--IAKAEEAKKVVIVGGGY 157
Cdd:PRK13512 82 IAINDERQTVTVLNRKTNEQFEESYDKLILSPGASANSLG---FESDITFTLRNLEDTDAIdqFIKANQVDKALVVGAGY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 158 IGIELVEAFVESGKEVTLIDGLDRIlNKYLDKPFTDVLEKELVDRGVTLALGENVSEFipDENgkvkQVTTAS-QTFDAD 236
Cdd:PRK13512 159 ISLEVLENLYERGLHPTLIHRSDKI-NKLMDADMNQPILDELDKREIPYRLNEEIDAI--NGN----EVTFKSgKVEHYD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 237 MVILCVGFRPNTKLVEG-KVETLPNGAIKVNEYMQTSNPDIFAAGDSAVVNYNPSGTQNYIPLATNAVRQGLLVGNNLT- 314
Cdd:PRK13512 232 MIIEGVGTHPNSKFIESsNIKLDDKGFIPVNDKFETNVPNIYAIGDIITSHYRHVDLPASVPLAWGAHRAASIVAEQIAg 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 315 EQKMAYRGTQGTSGLYLFGWTIGSTGVTTESapMNNLDVQATLFEDNYRPEFMPTTEKVMMELVYEKGTNRIVGAQFMSK 394
Cdd:PRK13512 312 NDTIEFKGFLGNNIVKFFDYTFASVGVKPNE--LKQFDYKMVEVTQGAHANYYPGNSPLHLRVYYDTSNRKILRAAAVGK 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 498429787 395 YDITQSANTMSLAVQNKMTVEDLALSDFFFQPHFDRPWNYLNLLAQAA 442
Cdd:PRK13512 390 EGADKRIDVLSMAMMNQLTVDELTEFEVAYAPPYSHPKDLINMIGYKA 437
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
99-418 |
3.01e-50 |
|
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: 176.82 E-value: 3.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 99 TETVSYDKLVMTTGSWPIIPPIKGIESENILlcknynQANEIIAKAEEAKKVVIVGGGYIGIELVEAFVESGKEVTLIDG 178
Cdd:COG1249 126 GETLTADHIVIATGSRPRVPPIPGLDEVRVL------TSDEALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVER 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 179 LDRILNKYlDKPFTDVLEKELVDRGVTLALGENVSEFIPDENGKVkqVTTAS----QTFDADMVILCVGFRPNTK---LV 251
Cdd:COG1249 200 GDRLLPGE-DPEISEALEKALEKEGIDILTGAKVTSVEKTGDGVT--VTLEDgggeEAVEADKVLVATGRRPNTDglgLE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 252 EGKVETLPNGAIKVNEYMQTSNPDIFAAGDsavVNynpsgtqNYIPLATNAVRQGLLVGNNLTEQK---MAYRGTqgTSG 328
Cdd:COG1249 277 AAGVELDERGGIKVDEYLRTSVPGIYAIGD---VT-------GGPQLAHVASAEGRVAAENILGKKprpVDYRAI--PSV 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 329 LYlfgwT---IGSTGVTTESAPMNNLDVQATL--FEDNYRPEFMPTTEkVMMELVYEKGTNRIVGAQFMSkYDITQSANT 403
Cdd:COG1249 345 VF----TdpeIASVGLTEEEAREAGIDVKVGKfpFAANGRALALGETE-GFVKLIADAETGRILGAHIVG-PHAGELIHE 418
|
330
....*....|....*
gi 498429787 404 MSLAVQNKMTVEDLA 418
Cdd:COG1249 419 AALAMEMGLTVEDLA 433
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
1-313 |
5.31e-42 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 152.98 E-value: 5.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 1 MKVVVIGCTHAGTAAVKSILKN-NPEADVTVYERND--NVSFLSCGIAlyVGGVvkDPAGLFYSNPEELASLGAKVKMEH 77
Cdd:COG1252 2 KRIVIVGGGFAGLEAARRLRKKlGGDAEVTLIDPNPyhLFQPLLPEVA--AGTL--SPDDIAIPLRELLRRAGVRFIQGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 78 dVTDVDTENKQVTAKDlktgeTETVSYDKLVMTTGSWPIIPPIKGIEsENILLCKNYNQA----NEIIAKAEEAK----- 148
Cdd:COG1252 78 -VTGIDPEARTVTLAD-----GRTLSYDYLVIATGSVTNFFGIPGLA-EHALPLKTLEDAlalrERLLAAFERAErrrll 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 149 KVVIVGGGYIGIELV--------EAFVESGK-----EVTLIDGLDRILNKyLDKPFTDVLEKELVDRGVTLALGENVSEF 215
Cdd:COG1252 151 TIVVVGGGPTGVELAgelaellrKLLRYPGIdpdkvRITLVEAGPRILPG-LGEKLSEAAEKELEKRGVEVHTGTRVTEV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 216 ipDENGkvkqVTTAS-QTFDADMVILCVGFRPNTKLVEGKVETLPNGAIKVNEYMQT-SNPDIFAAGDSAVVnynPSGTQ 293
Cdd:COG1252 230 --DADG----VTLEDgEEIPADTVIWAAGVKAPPLLADLGLPTDRRGRVLVDPTLQVpGHPNVFAIGDCAAV---PDPDG 300
|
330 340
....*....|....*....|.
gi 498429787 294 NYIP-LATNAVRQGLLVGNNL 313
Cdd:COG1252 301 KPVPkTAQAAVQQAKVLAKNI 321
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
79-286 |
1.50e-37 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 140.82 E-value: 1.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 79 VTDVDTENKQVTAKDlktgetETVSYDKLVMTTGSWPIIPPIKGIESeniLLCKN----YNQANEIIAkaeEAKKVVIVG 154
Cdd:PRK04965 81 VTDIDAEAQVVKSQG------NQWQYDKLVLATGASAFVPPIPGREL---MLTLNsqqeYRAAETQLR---DAQRVLVVG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 155 GGYIGIELVEAFVESGKEVTLIDGLDRILNKYLDKPFTDVLEKELVDRGVTLALGENVSEFIPDENGkVKQVTTASQTFD 234
Cdd:PRK04965 149 GGLIGTELAMDLCRAGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSG-IRATLDSGRSIE 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498429787 235 ADMVILCVGFRPNTKLV-EGKVETlpNGAIKVNEYMQTSNPDIFAAGDSAVVN 286
Cdd:PRK04965 228 VDAVIAAAGLRPNTALArRAGLAV--NRGIVVDSYLQTSAPDIYALGDCAEIN 278
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
98-418 |
2.90e-35 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 136.08 E-value: 2.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 98 ETETVSYDKLVMTTGS-WPIIPPIKGIESENILLcknynqANEIIAKAEEAKKVVIVGGGYIGIELVEAFVESGKEVTLI 176
Cdd:PRK06292 125 NGERIEAKNIVIATGSrVPPIPGVWLILGDRLLT------SDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVF 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 177 DGLDRILN---KYLDKPFTDVLEKELvdrgvTLALGENVSEFIPDENGKVK--QVTTASQTFDADMVILCVGFRPNT--- 248
Cdd:PRK06292 199 ERGDRILPledPEVSKQAQKILSKEF-----KIKLGAKVTSVEKSGDEKVEelEKGGKTETIEADYVLVATGRRPNTdgl 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 249 KLVEGKVETLPNGAIKVNEYMQTSNPDIFAAGDsavVNynpsgtqNYIPLATNAVRQGLLVGNNLTEQKMA---YRGTQG 325
Cdd:PRK06292 274 GLENTGIELDERGRPVVDEHTQTSVPGIYAAGD---VN-------GKPPLLHEAADEGRIAAENAAGDVAGgvrYHPIPS 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 326 TsglyLFgwT---IGSTGVTTESAPMNNLDVQATL--FEDNYRPEFMPTTEKvMMELVYEKGTNRIVGAQFMSKyDITQS 400
Cdd:PRK06292 344 V----VF--TdpqIASVGLTEEELKAAGIDYVVGEvpFEAQGRARVMGKNDG-FVKVYADKKTGRLLGAHIIGP-DAEHL 415
|
330
....*....|....*...
gi 498429787 401 ANTMSLAVQNKMTVEDLA 418
Cdd:PRK06292 416 IHLLAWAMQQGLTVEDLL 433
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
3-286 |
3.30e-34 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 135.73 E-value: 3.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 3 VVVIGCTHAGTAAVKSILK-NNPEADVTVYERNDNVSFLSCGIALYVGGVvKDPAGLFYSNPEELASLGAKVKMEHDVTD 81
Cdd:TIGR02374 1 LVLVGNGMAGHRCIEEVLKlNRHMFEITIFGEEPHPNYNRILLSSVLQGE-ADLDDITLNSKDWYEKHGITLYTGETVIQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 82 VDTENKQVTakdlkTGETETVSYDKLVMTTGSWPIIPPIKGIESENILLCKNYNQANEIIAKAEEAKKVVIVGGGYIGIE 161
Cdd:TIGR02374 80 IDTDQKQVI-----TDAGRTLSYDKLILATGSYPFILPIPGADKKGVYVFRTIEDLDAIMAMAQRFKKAAVIGGGLLGLE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 162 LVEAFVESGKEVTLIDGLDRILNKYLDKPFTDVLEKELVDRGVTLALGENVSEFIPDenGKVKQVTTASQT-FDADMVIL 240
Cdd:TIGR02374 155 AAVGLQNLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVGA--TKADRIRFKDGSsLEADLIVM 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 498429787 241 CVGFRPNTKLveGKVETLP-NGAIKVNEYMQTSNPDIFAAGDSAVVN 286
Cdd:TIGR02374 233 AAGIRPNDEL--AVSAGIKvNRGIIVNDSMQTSDPDIYAVGECAEHN 277
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
95-419 |
9.67e-31 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 123.33 E-value: 9.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 95 KTGETETVSYDKLVMTTGSWPIIPPikGIESENillcknynqanEIIAKAEEA-------KKVVIVGGGYIGIELVEAFV 167
Cdd:PRK06416 126 TEDGEQTYTAKNIILATGSRPRELP--GIEIDG-----------RVIWTSDEAlnldevpKSLVVIGGGYIGVEFASAYA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 168 ESGKEVTLIDGLDRILNKYlDKPFTDVLEKELVDRGVTLALGENVSEFIPDENGkVK---QVTTASQTFDADMVILCVGF 244
Cdd:PRK06416 193 SLGAEVTIVEALPRILPGE-DKEISKLAERALKKRGIKIKTGAKAKKVEQTDDG-VTvtlEDGGKEETLEADYVLVAVGR 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 245 RPNTK---LVEGKVETlPNGAIKVNEYMQTSNPDIFAAGDsaVVnynpSGTQnyipLATNAVRQGLLVGNNLTEQK--MA 319
Cdd:PRK06416 271 RPNTEnlgLEELGVKT-DRGFIEVDEQLRTNVPNIYAIGD--IV----GGPM----LAHKASAEGIIAAEAIAGNPhpID 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 320 YRGTQGTsglylfgwT-----IGSTGVTTESAPMNNLDVQA--TLFEDNYRPEFMPTTEKvMMELVYEKGTNRIVGAQF- 391
Cdd:PRK06416 340 YRGIPAV--------TythpeVASVGLTEAKAKEEGFDVKVvkFPFAGNGKALALGETDG-FVKLIFDKKDGEVLGAHMv 410
|
330 340 350
....*....|....*....|....*....|.
gi 498429787 392 ---MSkyDITQSAntmSLAVQNKMTVEDLAL 419
Cdd:PRK06416 411 garAS--ELIQEA---QLAINWEATPEDLAL 436
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
100-389 |
6.73e-30 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 120.65 E-value: 6.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 100 ETVSYDKLVMTTGSWPIIPPIKGIEsenilLCKNynqANEIIAKAEEAKKVVIVGGGYIGIELVEAFVESGKEVTLIDGL 179
Cdd:PRK06116 128 ERYTADHILIATGGRPSIPDIPGAE-----YGIT---SDGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRG 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 180 DRILNKYlDKPFTDVLEKELVDRGVTLALGENVSEFIPDENGKVKQVTTASQTFDADMVILCVGFRPNTK---LVEGKVE 256
Cdd:PRK06116 200 DAPLRGF-DPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADGSLTLTLEDGETLTVDCLIWAIGREPNTDglgLENAGVK 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 257 TLPNGAIKVNEYMQTSNPDIFAAGDSAvvnynpsgtqNYIPLATNAVRQGLLVG----NNLTEQKMAYRG------TQGt 326
Cdd:PRK06116 279 LNEKGYIIVDEYQNTNVPGIYAVGDVT----------GRVELTPVAIAAGRRLSerlfNNKPDEKLDYSNiptvvfSHP- 347
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498429787 327 sglylfgwTIGSTGVTTESApmnnldvQATLFEDN---YRPEF--MPTT-----EKVMMELVYEKGTNRIVGA 389
Cdd:PRK06116 348 --------PIGTVGLTEEEA-------REQYGEDNvkvYRSSFtpMYTAltghrQPCLMKLVVVGKEEKVVGL 405
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
100-281 |
6.84e-29 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 118.00 E-value: 6.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 100 ETVSYDKLVMTTGSWPIIPPIKGIESenillcKNYNQANEIIAKAEEAKKVVIVGGGYIGIELVEAFVESGKEVTLIDGL 179
Cdd:PRK06370 130 ETLRAKRIFINTGARAAIPPIPGLDE------VGYLTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERG 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 180 DRILNKYlDKPFTDVLEKELVDRGVTLALGENVSEFIPDENGKVKQVTTAS--QTFDADMVILCVGFRPNTK---LVEGK 254
Cdd:PRK06370 204 PRLLPRE-DEDVAAAVREILEREGIDVRLNAECIRVERDGDGIAVGLDCNGgaPEITGSHILVAVGRVPNTDdlgLEAAG 282
|
170 180
....*....|....*....|....*..
gi 498429787 255 VETLPNGAIKVNEYMQTSNPDIFAAGD 281
Cdd:PRK06370 283 VETDARGYIKVDDQLRTTNPGIYAAGD 309
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
70-340 |
8.29e-26 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 110.59 E-value: 8.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 70 GAKVKMEHDVTDVDTENKQVTAKdlkTGETetVSYDKLVMTTGSWPIIPPIKGIESENILLCKNYNQANEIIAKAEEAKK 149
Cdd:PRK14989 73 GIKVLVGERAITINRQEKVIHSS---AGRT--VFYDKLIMATGSYPWIPPIKGSETQDCFVYRTIEDLNAIEACARRSKR 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 150 VVIVGGGYIGIELVEAFVESGKEVTLIDGLDRILNKYLDKPFTDVLEKELVDRGVTLALGENVSEFIPDENGKVKQVTTA 229
Cdd:PRK14989 148 GAVVGGGLLGLEAAGALKNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSKNTLEIVQEGVEARKTMRFA 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 230 SQT-FDADMVILCVGFRPNTKLV-EGKVETLPNGAIKVNEYMQTSNPDIFAAGDSAVVNYNPSG--TQNYiPLATNAVRQ 305
Cdd:PRK14989 228 DGSeLEVDFIVFSTGIRPQDKLAtQCGLAVAPRGGIVINDSCQTSDPDIYAIGECASWNNRVFGlvAPGY-KMAQVAVDH 306
|
250 260 270
....*....|....*....|....*....|....*
gi 498429787 306 glLVGNNLteqkmAYRGTQGTSGLYLFGWTIGSTG 340
Cdd:PRK14989 307 --LLGSEN-----AFEGADLSAKLKLLGVDVGGIG 334
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
97-306 |
2.08e-23 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 102.16 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 97 GETETVSYDKLVMTTGSWPIIPPIKGIESENILlcknynQANEIIAKAEEAKKVVIVGGGYIGIELVEAFVESGKEVTLI 176
Cdd:PRK05249 131 GEVETLTADKIVIATGSRPYRPPDVDFDHPRIY------DSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLI 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 177 DGLDRILNkYLDKPFTDVLEKELVDRGVTLALGENVSEFIPDENGKVkqVTTAS-QTFDADMVILCVGFRPNTK---LVE 252
Cdd:PRK05249 205 NTRDRLLS-FLDDEISDALSYHLRDSGVTIRHNEEVEKVEGGDDGVI--VHLKSgKKIKADCLLYANGRTGNTDglnLEN 281
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498429787 253 GKVETLPNGAIKVNEYMQTSNPDIFAAGDsaVVNYnPSgtqnyipLATNAVRQG 306
Cdd:PRK05249 282 AGLEADSRGQLKVNENYQTAVPHIYAVGD--VIGF-PS-------LASASMDQG 325
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
93-281 |
1.33e-22 |
|
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: 100.05 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 93 DLKTGETETVSYDKLVMTTGSWPIIPPIKGIEsenilLCKNYNQANEIiakAEEAKKVVIVGGGYIGIE---LVEAFVES 169
Cdd:TIGR01423 141 DPKSAVKERLQAEHILLATGSWPQMLGIPGIE-----HCISSNEAFYL---DEPPRRVLTVGGGFISVEfagIFNAYKPR 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 170 GKEVTLIDGLDRILNKYlDKPFTDVLEKELVDRGVTLALGENVSEFIPDENGKVKQVTTASQTFDADMVILCVGFRPNT- 248
Cdd:TIGR01423 213 GGKVTLCYRNNMILRGF-DSTLRKELTKQLRANGINIMTNENPAKVTLNADGSKHVTFESGKTLDVDVVMMAIGRVPRTq 291
|
170 180 190
....*....|....*....|....*....|....*
gi 498429787 249 --KLVEGKVETLPNGAIKVNEYMQTSNPDIFAAGD 281
Cdd:TIGR01423 292 tlQLDKVGVELTKKGAIQVDEFSRTNVPNIYAIGD 326
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
27-306 |
3.72e-22 |
|
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: 98.28 E-value: 3.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 27 DVTVYERNDnvsflscgialYVGGVvkdpagLFYSNPEE-------------LASLGAKVKMEHDVTdvdtenKQVTAKD 93
Cdd:COG0493 146 EVTVFEALD-----------KPGGL------LRYGIPEFrlpkdvldreielIEALGVEFRTNVEVG------KDITLDE 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 94 LKTGetetvsYDKLVMTTGSW-PIIPPIKGIESENILLC----KNYNQANEIIAKAEEAKKVVIVGGGYIGIE-LVEAFV 167
Cdd:COG0493 203 LLEE------FDAVFLATGAGkPRDLGIPGEDLKGVHSAmdflTAVNLGEAPDTILAVGKRVVVIGGGNTAMDcARTALR 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 168 ESGKEVTLIDGLDRILNKYldkpftDVLEKEL-VDRGVTLALGENVSEFIPDENGKVKQVTTA----------------- 229
Cdd:COG0493 277 LGAESVTIVYRRTREEMPA------SKEEVEEaLEEGVEFLFLVAPVEIIGDENGRVTGLECVrmelgepdesgrrrpvp 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 230 ----SQTFDADMVILCVGFRPNTKLVEGK--VETLPNGAIKVNE-YMQTSNPDIFAAGDsaVVNYnPSgtqnyipLATNA 302
Cdd:COG0493 351 iegsEFTLPADLVILAIGQTPDPSGLEEElgLELDKRGTIVVDEeTYQTSLPGVFAGGD--AVRG-PS-------LVVWA 420
|
....
gi 498429787 303 VRQG 306
Cdd:COG0493 421 IAEG 424
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
64-312 |
5.23e-22 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 95.96 E-value: 5.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 64 EELASLGAKVKMEHdVTDVDTENKQVTakdLKTGETETVSYDKLVMTTGSWPIIPPIKGIE-----------SENILLCK 132
Cdd:COG0492 65 EQAERFGAEILLEE-VTSVDKDDGPFR---VTTDDGTEYEAKAVIIATGAGPRKLGLPGEEefegrgvsycaTCDGFFFR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 133 NynqaneiiakaeeaKKVVIVGGGYIGIELVEAFVESGKEVTLI---DGLDrilnkyldkpftdvLEKELVDR-----GV 204
Cdd:COG0492 141 G--------------KDVVVVGGGDSALEEALYLTKFASKVTLIhrrDELR--------------ASKILVERlranpKI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 205 TLALGENVSEFIPDenGKVKQVTTAS------QTFDADMVILCVGFRPNTKLVEGK-VETLPNGAIKVNEYMQTSNPDIF 277
Cdd:COG0492 193 EVLWNTEVTEIEGD--GRVEGVTLKNvktgeeKELEVDGVFVAIGLKPNTELLKGLgLELDEDGYIVVDEDMETSVPGVF 270
|
250 260 270
....*....|....*....|....*....|....*
gi 498429787 278 AAGDSAVVNYNpsgtqnyipLATNAVRQGLLVGNN 312
Cdd:COG0492 271 AAGDVRDYKYR---------QAATAAGEGAIAALS 296
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
94-418 |
1.42e-20 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 94.45 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 94 LKTGETETVSYDKLVMTTGSWPIIPPIKGIESenillcKNYNQANEIIAKAEEAKKVVIVGGGYIGIELVEAFVESGKEV 173
Cdd:PRK13748 223 LNDGGERVVAFDRCLIATGASPAVPPIPGLKE------TPYWTSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKV 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 174 TLidgLDRILNKYLDKPftdvlekelvdrgvtlALGENVSEFIPDENGKVKQVTTASQ---------------TFDADMV 238
Cdd:PRK13748 297 TI---LARSTLFFREDP----------------AIGEAVTAAFRAEGIEVLEHTQASQvahvdgefvlttghgELRADKL 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 239 ILCVGFRPNTK---LVEGKVETLPNGAIKVNEYMQTSNPDIFAAGDSA-----VVNYNPSGTQNYIPL----------AT 300
Cdd:PRK13748 358 LVATGRAPNTRslaLDAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTdqpqfVYVAAAAGTRAAINMtggdaaldltAM 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 301 NAV----RQGLLVGnnLTEQKMAYRGTQGTSGLylfgwtigstgVTTESAP--MNNLDVQAtlfednyrpefmpttekvM 374
Cdd:PRK13748 438 PAVvftdPQVATVG--YSEAEAHHDGIETDSRT-----------LTLDNVPraLANFDTRG------------------F 486
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 498429787 375 MELVYEKGTNRIVGAQFMSKY--DITQSAntmSLAVQNKMTVEDLA 418
Cdd:PRK13748 487 IKLVIEEGSGRLIGVQAVAPEagELIQTA---ALAIRNRMTVQELA 529
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
92-281 |
1.90e-20 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 93.09 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 92 KDLKTGETETVSYDKLVMTTGSWPIIPPIkgiesenILLCK-NYNQANEIIAKAEEAKKVVIVGGGYIGIELVEAFVESG 170
Cdd:PRK07846 117 KTLRTGDGEEITADQVVIAAGSRPVIPPV-------IADSGvRYHTSDTIMRLPELPESLVIVGGGFIAAEFAHVFSALG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 171 KEVTLIDGLDRILNKYLD---KPFTdvlekELVDRGVTLALGENVSEFIPDENGkVKQVTTASQTFDADMVILCVGFRPN 247
Cdd:PRK07846 190 VRVTVVNRSGRLLRHLDDdisERFT-----ELASKRWDVRLGRNVVGVSQDGSG-VTLRLDDGSTVEADVLLVATGRVPN 263
|
170 180 190
....*....|....*....|....*....|....*..
gi 498429787 248 TKLVE---GKVETLPNGAIKVNEYMQTSNPDIFAAGD 281
Cdd:PRK07846 264 GDLLDaaaAGVDVDEDGRVVVDEYQRTSAEGVFALGD 300
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
88-311 |
2.46e-19 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 89.81 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 88 QVTAKDlktgETETVSYDKLVMTTGSWPIIPPIKGI-ESENIllcknYNqANEIIAKAEEAKKVVIVGGGYIGIELVEAF 166
Cdd:PRK07251 107 EVQAGD----EKIELTAETIVINTGAVSNVLPIPGLaDSKHV-----YD-STGIQSLETLPERLGIIGGGNIGLEFAGLY 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 167 VESGKEVTLIDGLDRILNKYldKPFTDVLEKE-LVDRGVTLALGENVSEfIPDENGKVkQVTTASQTFDADMVILCVGFR 245
Cdd:PRK07251 177 NKLGSKVTVLDAASTILPRE--EPSVAALAKQyMEEDGITFLLNAHTTE-VKNDGDQV-LVVTEDETYRFDALLYATGRK 252
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498429787 246 PNTK---LVEGKVETLPNGAIKVNEYMQTSNPDIFAAGDsavVNYNPSGTqnYIPLATNAVRQGLLVGN 311
Cdd:PRK07251 253 PNTEplgLENTDIELTERGAIKVDDYCQTSVPGVFAVGD---VNGGPQFT--YISLDDFRIVFGYLTGD 316
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
100-284 |
2.40e-18 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 86.52 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 100 ETVSYDKLVMTTGSWPIIPPIKGIESENILLCKNYNQANEIIAKAEEAKKVVIVGGGYIGIELVEAFVESGKEVTLIDGL 179
Cdd:PRK09754 97 ESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELAASATQRRCKVTVIELA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 180 DRILNKYLDKPFTDVLEKELVDRGVTLALGENVSEFIPDEngKVKQVTTASQTFDADMVILCVGFRPNTKL-VEGKVETl 258
Cdd:PRK09754 177 ATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGE--KVELTLQSGETLQADVVIYGIGISANDQLaREANLDT- 253
|
170 180
....*....|....*....|....*.
gi 498429787 259 pNGAIKVNEYMQTSNPDIFAAGDSAV 284
Cdd:PRK09754 254 -ANGIVIDEACRTCDPAIFAGGDVAI 278
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
149-227 |
2.64e-18 |
|
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: 79.17 E-value: 2.64e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498429787 149 KVVIVGGGYIGIELVEAFVESGKEVTLIDGLDRILnKYLDKPFTDVLEKELVDRGVTLALGENVSEFIPDENGKVKQVT 227
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLL-PGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLT 78
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
56-288 |
1.18e-17 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 85.44 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 56 AGLFYSNPEELASLGAKVKMEHDVTDvDTENKQVTAKDLKTGETETVSYDKLVMTTGSWPIIPPIKGIEsenillcknYN 135
Cdd:PTZ00058 156 KGSLLSENQVLIKKVSQVDGEADESD-DDEVTIVSAGVSQLDDGQVIEGKNILIAVGNKPIFPDVKGKE---------FT 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 136 QANEIIAKAEEAKKVVIVGGGYIGIELVEAFVESGKEVTLIDGLDRILNKYlDKPFTDVLEKELVDRGVTLalgenVSEF 215
Cdd:PTZ00058 226 ISSDDFFKIKEAKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLRKF-DETIINELENDMKKNNINI-----ITHA 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 216 IPDENGKVKQ------VTTASQTFDADMVILCVGFRPNTKLV--EGKVETLPNGAIKVNEYMQTSNPDIFAAGDSAVVNY 287
Cdd:PTZ00058 300 NVEEIEKVKEknltiyLSDGRKYEHFDYVIYCVGRSPNTEDLnlKALNIKTPKGYIKVDDNQRTSVKHIYAVGDCCMVKK 379
|
.
gi 498429787 288 N 288
Cdd:PTZ00058 380 N 380
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
78-416 |
3.20e-17 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 84.16 E-value: 3.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 78 DVTDVDTENKQVTAKDLktgetetvsydklVMTTGSWPIIPPIKGIESenillCKNYNQANEIIAKAEeakKVVIVGGGY 157
Cdd:PLN02546 204 DPHTVDVDGKLYTARNI-------------LIAVGGRPFIPDIPGIEH-----AIDSDAALDLPSKPE---KIAIVGGGY 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 158 IGIELVEAFVESGKEVTLIDGLDRILNKYlDKPFTDVLEKELVDRGVTLALGENVSEFIPDENGKVkQVTTASQTFDA-D 236
Cdd:PLN02546 263 IALEFAGIFNGLKSDVHVFIRQKKVLRGF-DEEVRDFVAEQMSLRGIEFHTEESPQAIIKSADGSL-SLKTNKGTVEGfS 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 237 MVILCVGFRPNTK---LVEGKVETLPNGAIKVNEYMQTSNPDIFAAGD-SAVVNYNPsgtqnyIPLATNAVRQGLLVGNN 312
Cdd:PLN02546 341 HVMFATGRKPNTKnlgLEEVGVKMDKNGAIEVDEYSRTSVPSIWAVGDvTDRINLTP------VALMEGGALAKTLFGNE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 313 LTeqKMAYRGTQGTsglyLFGW-TIGSTGVTTESAPMNNLDVQAtlFEDNYRP---EFMPTTEKVMMELVYEKGTNRIVG 388
Cdd:PLN02546 415 PT--KPDYRAVPSA----VFSQpPIGQVGLTEEQAIEEYGDVDV--FTANFRPlkaTLSGLPDRVFMKLIVCAKTNKVLG 486
|
330 340
....*....|....*....|....*...
gi 498429787 389 AQfMSKYDITQSANTMSLAVQNKMTVED 416
Cdd:PLN02546 487 VH-MCGEDAPEIIQGFAVAVKAGLTKAD 513
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
70-281 |
5.21e-17 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 82.94 E-value: 5.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 70 GAKVKM-EHDVTDVDTENKQVTAKDlktGETETVSYDKLVMTTGSWPIIPPIKGIESENillcknynQANEIIAKAEEAK 148
Cdd:PLN02507 136 NAGVKLyEGEGKIVGPNEVEVTQLD---GTKLRYTAKHILIATGSRAQRPNIPGKELAI--------TSDEALSLEELPK 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 149 KVVIVGGGYIGIELVEAFVESGKEVTLIDGLDRILNKYlDKPFTDVLEKELVDRGVTLALGENVSEFIPDENGkVKQVTT 228
Cdd:PLN02507 205 RAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGF-DDEMRAVVARNLEGRGINLHPRTNLTQLTKTEGG-IKVITD 282
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498429787 229 ASQTFDADMVILCVGFRPNTK---LVEGKVETLPNGAIKVNEYMQTSNPDIFAAGD 281
Cdd:PLN02507 283 HGEEFVADVVLFATGRAPNTKrlnLEAVGVELDKAGAVKVDEYSRTNIPSIWAIGD 338
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
93-418 |
1.24e-16 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 81.90 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 93 DLKTGETETVSYDKLVMTTGSWPIIPPIKGIESENILlcknynqANEIIAKAEEA-KKVVIVGGGYIGIELVEAFVESGK 171
Cdd:PRK06327 135 KVTGEDETVITAKHVIIATGSEPRHLPGVPFDNKIIL-------DNTGALNFTEVpKKLAVIGAGVIGLELGSVWRRLGA 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 172 EVTLIDGLDRILNKyLDKPFTDVLEKELVDRGVTLALGENVSEFIPDENGKVKQVTTAS---QTFDADMVILCVGFRPNT 248
Cdd:PRK06327 208 EVTILEALPAFLAA-ADEQVAKEAAKAFTKQGLDIHLGVKIGEIKTGGKGVSVAYTDADgeaQTLEVDKLIVSIGRVPNT 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 249 K---LVEGKVETLPNGAIKVNEYMQTSNPDIFAAGDsaVVnynpSGTQnyipLATNAVRQGLLVGNNLTEQKMAYRGTQG 325
Cdd:PRK06327 287 DglgLEAVGLKLDERGFIPVDDHCRTNVPNVYAIGD--VV----RGPM----LAHKAEEEGVAVAERIAGQKGHIDYNTI 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 326 TSGLYLFGwTIGSTGVTTESAPMNNLDVQATL--FEDNYRPEFMPTTEKvMMELVYEKGTNRIVGAQfMSKYDITQSANT 403
Cdd:PRK06327 357 PWVIYTSP-EIAWVGKTEQQLKAEGVEYKAGKfpFMANGRALAMGEPDG-FVKIIADAKTDEILGVH-VIGPNASELIAE 433
|
330
....*....|....*
gi 498429787 404 MSLAVQNKMTVEDLA 418
Cdd:PRK06327 434 AVVAMEFKASSEDIA 448
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
2-325 |
4.67e-16 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 79.81 E-value: 4.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 2 KVVVIGCTHAGTAAVKSIlknNPE-ADVTVYERNDNVSFLSCGIALYVGGVVkdpaglFYSNPE----ELASLGAKVkME 76
Cdd:PTZ00318 12 NVVVLGTGWAGAYFVRNL---DPKkYNITVISPRNHMLFTPLLPQTTTGTLE------FRSICEpvrpALAKLPNRY-LR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 77 HDVTDVDTENKQVTAKDLKTGETE-----TVSYDKLVMTTGSWPIIPPIKGIEsENILLCKNYNQANEI-------IAKA 144
Cdd:PTZ00318 82 AVVYDVDFEEKRVKCGVVSKSNNAnvntfSVPYDKLVVAHGARPNTFNIPGVE-ERAFFLKEVNHARGIrkrivqcIERA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 145 -------EEAKK---VVIVGGGYIGIE----LVEAFVESGK----------EVTLIDGLDRILNKYlDKPFTDVLEKELV 200
Cdd:PTZ00318 161 slpttsvEERKRllhFVVVGGGPTGVEfaaeLADFFRDDVRnlnpelveecKVTVLEAGSEVLGSF-DQALRKYGQRRLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 201 DRGVTLALGENVSEFIPDEngkvkQVTTASQTFDADMVILCVGFRPNTKLVEGKVETLPNGAIKVNEYMQTSN-PDIFAA 279
Cdd:PTZ00318 240 RLGVDIRTKTAVKEVLDKE-----VVLKDGEVIPTGLVVWSTGVGPGPLTKQLKVDKTSRGRISVDDHLRVKPiPNVFAL 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498429787 280 GDSAVVNYNPsgtqnYIPLATNAVRQGLLVG---NNLTEQK-------------MAYRGTQG 325
Cdd:PTZ00318 315 GDCAANEERP-----LPTLAQVASQQGVYLAkefNNELKGKpmskpfvyrslgsLAYLGNYS 371
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
105-392 |
7.75e-16 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 79.29 E-value: 7.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 105 DKLVMTTGSWPIIPPIKGIESENILLcknynQANEIIAKAEEAKKVVIVGGGYIGIELVEAFVESGKEVTLIDGLDRILN 184
Cdd:PRK08010 121 EKIFINTGAQTVVPPIPGITTTPGVY-----DSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLP 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 185 KYlDKPFTDVLEKELVDRGVTLALGENVsEFIPDENGKVkQVTTASQTFDADMVILCVGFRPNT---KLVEGKVETLPNG 261
Cdd:PRK08010 196 RE-DRDIADNIATILRDQGVDIILNAHV-ERISHHENQV-QVHSEHAQLAVDALLIASGRQPATaslHPENAGIAVNERG 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 262 AIKVNEYMQTSNPDIFAAGDSAvvnynpSGTQ-NYIPLAT-NAVRQGLlvgnnLTEQKMAYRGTQGTSGLYLFGWTIGST 339
Cdd:PRK08010 273 AIVVDKYLHTTADNIWAMGDVT------GGLQfTYISLDDyRIVRDEL-----LGEGKRSTDDRKNVPYSVFMTPPLSRV 341
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 498429787 340 GVTTESAPMNNLDVQATLFEDNY--RPEFMPTTEKVMMELVyEKGTNRIVGAQFM 392
Cdd:PRK08010 342 GMTEEQARESGADIQVVTLPVAAipRARVMNDTRGVLKAIV-DNKTQRILGASLL 395
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
332-429 |
5.14e-14 |
|
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: 67.96 E-value: 5.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 332 FGWTIGSTGVTTESAPMNNLDVQ--ATLFEDNYRPEFMPTTEkVMMELVYEKGTNRIVGAQFMSkYDITQSANTMSLAVQ 409
Cdd:pfam02852 7 TDPEIASVGLTEEEAKEKGGEVKvgKFPFAANGRALAYGDTD-GFVKLVADRETGKILGAHIVG-PNAGELIQEAALAIK 84
|
90 100
....*....|....*....|
gi 498429787 410 NKMTVEDLALsDFFFQPHFD 429
Cdd:pfam02852 85 MGATVEDLAN-TIHIHPTLS 103
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
88-306 |
2.10e-13 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 71.81 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 88 QVTAKDlktGETETVSYDKLVMTTGSWPIIPPIKGIESENILlckNYNQANEIiakAEEAKKVVIVGGGYIGIELVEAFV 167
Cdd:PRK07845 127 KVTTAD---GGEETLDADVVLIATGASPRILPTAEPDGERIL---TWRQLYDL---DELPEHLIVVGSGVTGAEFASAYT 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 168 ESGKEVTLIDGLDRILnkyldkPFTD-----VLEKELVDRGVTLALGENVSEFIPDENGKVkqVTTAS-QTFDADMVILC 241
Cdd:PRK07845 198 ELGVKVTLVSSRDRVL------PGEDadaaeVLEEVFARRGMTVLKRSRAESVERTGDGVV--VTLTDgRTVEGSHALMA 269
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498429787 242 VGFRPNTK---LVEGKVETLPNGAIKVNEYMQTSNPDIFAAGDSAVVnynpsgtqnyIPLATNAVRQG 306
Cdd:PRK07845 270 VGSVPNTAglgLEEAGVELTPSGHITVDRVSRTSVPGIYAAGDCTGV----------LPLASVAAMQG 327
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
2-281 |
3.65e-13 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 70.96 E-value: 3.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 2 KVVVIGCTHAGTAAVKSILKNNpeADVTVYERNDNVsflscgialyvGGVvkdpagLFYSNPEelaslgakVKMEHDVtd 81
Cdd:PRK12810 145 KVAVVGSGPAGLAAADQLARAG--HKVTVFERADRI-----------GGL------LRYGIPD--------FKLEKEV-- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 82 VDTENKQVTA------------KDLkTGETETVSYDKLVMTTGSW-PIIPPIKGIESENILL-----------CKNYNQA 137
Cdd:PRK12810 196 IDRRIELMEAegiefrtnvevgKDI-TAEELLAEYDAVFLGTGAYkPRDLGIPGRDLDGVHFamdfliqntrrVLGDETE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 138 NEIIAKAeeaKKVVIVGGGYIGIE-LVEAFVESGKEVTLID-----GLDRilNKYLDKP-FTDVLE-----KElvdrGVT 205
Cdd:PRK12810 275 PFISAKG---KHVVVIGGGDTGMDcVGTAIRQGAKSVTQRDimpmpPSRR--NKNNPWPyWPMKLEvsnahEE----GVE 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 206 LALGENVSEFIpDENGKVKQVTTAS---------------QTFDADMVILCVGFRP--NTKLVEGKVETLPNGAIKVNEY 268
Cdd:PRK12810 346 REFNVQTKEFE-GENGKVTGVKVVRtelgegdfepvegseFVLPADLVLLAMGFTGpeAGLLAQFGVELDERGRVAAPDN 424
|
330
....*....|....
gi 498429787 269 -MQTSNPDIFAAGD 281
Cdd:PRK12810 425 aYQTSNPKVFAAGD 438
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
1-281 |
7.34e-13 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 70.21 E-value: 7.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 1 MKVVVIGCTHAG-TAAVKSILKNNpeaDVTVYERNDNVsflscgialyvGGVvkdpagLFYSNPE----------E---L 66
Cdd:PRK11749 141 KKVAVIGAGPAGlTAAHRLARKGY---DVTIFEARDKA-----------GGL------LRYGIPEfrlpkdivdrEverL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 67 ASLGAKVKMEHDVtdvdteNKQVTAKDLKTGetetvsYDKLVMTTGSW-PIIPPIKGIESENILlcknynQANEIIAKAE 145
Cdd:PRK11749 201 LKLGVEIRTNTEV------GRDITLDELRAG------YDAVFIGTGAGlPRFLGIPGENLGGVY------SAVDFLTRVN 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 146 EA---------KKVVIVGGGYIGIELV-------------------EAFVESGKEVTL--IDGLDRILNKyldKPfTDVL 195
Cdd:PRK11749 263 QAvadydlpvgKRVVVIGGGNTAMDAArtakrlgaesvtivyrrgrEEMPASEEEVEHakEEGVEFEWLA---AP-VEIL 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 196 EKELVDRGVTLA---LGEnvsefiPDENGKVKQVTTASQ-TFDADMVILCVGFRPNTKLVEG--KVETLPNGAIKVNE-Y 268
Cdd:PRK11749 339 GDEGRVTGVEFVrmeLGE------PDASGRRRVPIEGSEfTLPADLVIKAIGQTPNPLILSTtpGLELNRWGTIIADDeT 412
|
330
....*....|...
gi 498429787 269 MQTSNPDIFAAGD 281
Cdd:PRK11749 413 GRTSLPGVFAGGD 425
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
103-315 |
1.74e-12 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 68.48 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 103 SYDKLVMTTGSW-PIIPPIKGIESENILLCKNY----------NQANEIIAKAEEaKKVVIVGGGYIGIELV-EAFVESG 170
Cdd:PRK12770 118 KYDAVLIATGTWkSRKLGIPGEDLPGVYSALEYlfriraaklgYLPWEKVPPVEG-KKVVVVGAGLTAVDAAlEAVLLGA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 171 KEVTLIdgLDRILNKYLDKPFTdvLEKeLVDRGVTL--------ALGEN---VSEFI------PDENGKVKQVTTASQTF 233
Cdd:PRK12770 197 EKVYLA--YRRTINEAPAGKYE--IER-LIARGVEFlelvtpvrIIGEGrveGVELAkmrlgePDESGRPRPVPIPGSEF 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 234 --DADMVILCVGFRPNT--KLVEGKVETLPNGAIKVNEYMQTSNPDIFAAGDsaVVNyNPSgtqnyipLATNAVRQGLLV 309
Cdd:PRK12770 272 vlEADTVVFAIGEIPTPpfAKECLGIELNRKGEIVVDEKHMTSREGVFAAGD--VVT-GPS-------KIGKAIKSGLRA 341
|
....*.
gi 498429787 310 GNNLTE 315
Cdd:PRK12770 342 AQSIHE 347
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
1-281 |
7.40e-10 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 61.30 E-value: 7.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 1 MKVVVIGCTHAGTAAVKSILKNNpeADVTVYErndnvsflscgiALY-VGGVVKD-------PAGLFYSNPEELASLGak 72
Cdd:PRK12778 432 KKVAVIGSGPAGLSFAGDLAKRG--YDVTVFE------------ALHeIGGVLKYgipefrlPKKIVDVEIENLKKLG-- 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 73 VKMEHDVtdvdtenkqVTAKDLKTGETETVSYDKLVMTTGS-WPIIPPIKGIESENILLCKNY-NQANEIIAKAEE---- 146
Cdd:PRK12778 496 VKFETDV---------IVGKTITIEELEEEGFKGIFIASGAgLPNFMNIPGENSNGVMSSNEYlTRVNLMDAASPDsdtp 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 147 ---AKKVVIVGGGYIGIELVEAFVESGKE-VTLI-----DGLDRILNKYldkpftdvleKELVDRGVTLALGENVSEFIP 217
Cdd:PRK12778 567 ikfGKKVAVVGGGNTAMDSARTAKRLGAErVTIVyrrseEEMPARLEEV----------KHAKEEGIEFLTLHNPIEYLA 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 218 DENGKVKQV---------------------TTASQTFDADMVILCVGFRPNtKLVEGKVETLP---NGAIKVNEYMQTSN 273
Cdd:PRK12778 637 DEKGWVKQVvlqkmelgepdasgrrrpvaiPGSTFTVDVDLVIVSVGVSPN-PLVPSSIPGLElnrKGTIVVDEEMQSSI 715
|
....*...
gi 498429787 274 PDIFAAGD 281
Cdd:PRK12778 716 PGIYAGGD 723
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
1-282 |
1.97e-09 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 59.26 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 1 MKVVVIGCTHAGTAAVKSILKNNpeADVTVYErndnvsflscgiALY-VGGVvkdpagLFYSNPE--------------E 65
Cdd:PRK12831 141 KKVAVIGSGPAGLTCAGDLAKMG--YDVTIFE------------ALHePGGV------LVYGIPEfrlpketvvkkeieN 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 66 LASLGAKVKMEHDVtdvdteNKQVTAKDLktgeTETVSYDKLVMTTGSWpiIPPIKGIESENilLCKNYNqANEIIA--- 142
Cdd:PRK12831 201 IKKLGVKIETNVVV------GKTVTIDEL----LEEEGFDAVFIGSGAG--LPKFMGIPGEN--LNGVFS-ANEFLTrvn 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 143 --KAEE---------AKKVVIVGGGYIGIELVEAFVESGKEVTLIdgldrilnkYLDKpftdvlEKELVDR--------- 202
Cdd:PRK12831 266 lmKAYKpeydtpikvGKKVAVVGGGNVAMDAARTALRLGAEVHIV---------YRRS------EEELPARveevhhake 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 203 -GVTLALGENVSEFIPDENGKVKQVT--------------------TASQ-TFDADMVILCVGFRPNTKLVEGK--VETL 258
Cdd:PRK12831 331 eGVIFDLLTNPVEILGDENGWVKGMKcikmelgepdasgrrrpveiEGSEfVLEVDTVIMSLGTSPNPLISSTTkgLKIN 410
|
330 340
....*....|....*....|....*
gi 498429787 259 PNGAIKVNE-YMQTSNPDIFAAGDS 282
Cdd:PRK12831 411 KRGCIVADEeTGLTSKEGVFAGGDA 435
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
73-280 |
1.32e-08 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 56.08 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 73 VKMEHDVTDVDTENKQVTakdLKTgETETVSYDKLVMTTG--SWPIIPPIKGiesenilLCKNYNQANEiiAKAEEAKKV 150
Cdd:pfam13738 92 INLFEEVTSVKKEDDGFV---VTT-SKGTYQARYVIIATGefDFPNKLGVPE-------LPKHYSYVKD--FHPYAGQKV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 151 VIVGGGYIG----IELVEAfvesGKEVTLIDGLDRILN-----KYLDKPftDVLE--KELVDRG-VTLALGENVSEfIPD 218
Cdd:pfam13738 159 VVIGGYNSAvdaaLELVRK----GARVTVLYRGSEWEDrdsdpSYSLSP--DTLNrlEELVKNGkIKAHFNAEVKE-ITE 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498429787 219 ENGKVKQVTTASQTFDADM-VILCVGFRPNTKLVE-GKVETLPNGAIKVN-EYMQTSNPDIFAAG 280
Cdd:pfam13738 232 VDVSYKVHTEDGRKVTSNDdPILATGYHPDLSFLKkGLFELDEDGRPVLTeETESTNVPGLFLAG 296
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
86-417 |
3.44e-08 |
|
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: 55.63 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 86 NKQVTAKDLKTGETETVSYDKLVMTTGSWPIIPPIKGIESENIllcknynQANEIIAKAEEAKKVVIVGGGYIGIELVEA 165
Cdd:TIGR01438 126 DKHRIKATNKKGKEKIYSAERFLIATGERPRYPGIPGAKELCI-------TSDDLFSLPYCPGKTLVVGASYVALECAGF 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 166 FVESGKEVTLIdgLDRILNKYLDKPFTDVLEKELVDRGVTLALGENVSEFIPDENGKVKQVTTASQTFDA--DMVILCVG 243
Cdd:TIGR01438 199 LAGIGLDVTVM--VRSILLRGFDQDCANKVGEHMEEHGVKFKRQFVPIKVEQIEAKVLVEFTDSTNGIEEeyDTVLLAIG 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 244 FRPNTKLVegKVETL------PNGAIKVNEYMQTSNPDIFAAGDSAvvnynpsgtQNYIPLATNAVRQGLLVGNNL---T 314
Cdd:TIGR01438 277 RDACTRKL--NLENVgvkinkKTGKIPADEEEQTNVPYIYAVGDIL---------EDKPELTPVAIQAGRLLAQRLfkgS 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 315 EQKMAYRGTQGTSGLYLfgwTIGSTGVTTESApmnnldvqATLF-EDN---YRPEFMP---------TTEKVMMELV-YE 380
Cdd:TIGR01438 346 TVICDYENVPTTVFTPL---EYGACGLSEEKA--------VEKFgEENvevFHSYFWPlewtipsrdNHNKCYAKLVcNK 414
|
330 340 350
....*....|....*....|....*....|....*....
gi 498429787 381 KGTNRIVGAQFM--SKYDITQSantMSLAVQNKMTVEDL 417
Cdd:TIGR01438 415 KENERVVGFHVVgpNAGEVTQG---FAAALRCGLTKKDL 450
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
64-281 |
1.17e-06 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 50.06 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 64 EELASLGAKVKMEHdVTDVDTENKQVTAkdlkTGETETVSYDKLVMTTGS------WPIIPPIKGIESENILLCKNYNQA 137
Cdd:PRK10262 71 EHATKFETEIIFDH-INKVDLQNRPFRL----TGDSGEYTCDALIIATGAsarylgLPSEEAFKGRGVSACATCDGFFYR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 138 NEiiakaeeakKVVIVGGGYIGIELVEAFVESGKEVTLIDGLDRILNKyldkpftDVLEKELVDR----GVTLALGENVS 213
Cdd:PRK10262 146 NQ---------KVAVIGGGNTAVEEALYLSNIASEVHLIHRRDGFRAE-------KILIKRLMDKvengNIILHTNRTLE 209
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498429787 214 EFIPDENG------KVKQVTTASQTFDADMVILCVGFRPNTKLVEGKVEtLPNGAIKVNEYM-----QTSNPDIFAAGD 281
Cdd:PRK10262 210 EVTGDQMGvtgvrlRDTQNSDNIESLDVAGLFVAIGHSPNTAIFEGQLE-LENGYIKVQSGIhgnatQTSIPGVFAAGD 287
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
3-248 |
1.23e-06 |
|
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: 50.63 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 3 VVVIGCTHAGTAAVKSILKNNPeaDVTVYERNDNVsflscgialyvGGVVKD----------PAGL----FYSNP----- 63
Cdd:COG2072 9 VVVIGAGQAGLAAAYHLRRAGI--DFVVLEKADDV-----------GGTWRDnrypglrldtPSHLyslpFFPNWsddpd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 64 ----EELAS----------LGAKVKMEHDVTDV--DTENKQVTakdLKTGETETVSYDKLVMTTGSW--PIIPPIKGIES 125
Cdd:COG2072 76 fptgDEILAyleayadkfgLRRPIRFGTEVTSArwDEADGRWT---VTTDDGETLTARFVVVATGPLsrPKIPDIPGLED 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 126 ENILLC--KNYNQANEIiakaeEAKKVVIVGGGYIGIELVEAFVESGKEVTLI----------DGLDRILNKYLDKPFTD 193
Cdd:COG2072 153 FAGEQLhsADWRNPVDL-----AGKRVLVVGTGASAVQIAPELARVAAHVTVFqrtppwvlprPNYDPERGRPANYLGLE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 194 vLEKELVDRGVTLALGENVSEFIPD---------------------------ENGKVK------------QVTTAS-QTF 233
Cdd:COG2072 228 -APPALNRRDARAWLRRLLRAQVKDpelglltpdyppgckrpllstdyyealRRGNVElvtggieritedGVVFADgTEH 306
|
330
....*....|....*
gi 498429787 234 DADMVILCVGFRPNT 248
Cdd:COG2072 307 EVDVIVWATGFRADL 321
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
2-281 |
3.04e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 49.38 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 2 KVVVIGCTHAGTAAVKSILKNNPEadVTVYE-RNDNVSFLSCGIALYvggvvKDPAGLFYSNPEELASLGAKVKMEHDVt 80
Cdd:PRK13984 285 KVAIVGSGPAGLSAAYFLATMGYE--VTVYEsLSKPGGVMRYGIPSY-----RLPDEALDKDIAFIEALGVKIHLNTRV- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 81 dvdteNKQVTAKDLKTGetetvsYDKLVMTTG-SWPIIPPIKGIESENI-----LL--CKNYNQANEiiAKAEEAKKVVI 152
Cdd:PRK13984 357 -----GKDIPLEELREK------HDAVFLSTGfTLGRSTRIPGTDHPDViqalpLLreIRDYLRGEG--PKPKIPRSLVV 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 153 VGGGYIGIELVEA-----FVESGKEVTLIDGLDRilnKYLDKPfTDVLE-KELVDRGVTLALGENVSEFIPdENGKVKQV 226
Cdd:PRK13984 424 IGGGNVAMDIARSmarlqKMEYGEVNVKVTSLER---TFEEMP-ADMEEiEEGLEEGVVIYPGWGPMEVVI-ENDKVKGV 498
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498429787 227 TTA------------SQTFD--------ADMVILCVGFRPNTKL----VEGKVEtLPNGAIKVNEYMQTSNPDIFAAGD 281
Cdd:PRK13984 499 KFKkcvevfdeegrfNPKFDesdqiiveADMVVEAIGQAPDYSYlpeeLKSKLE-FVRGRILTNEYGQTSIPWLFAGGD 576
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
148-287 |
7.30e-06 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 48.23 E-value: 7.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 148 KKVVIVGGGYIGIE-------LVeafvesgKEVTLI---DGL--DRILNKYLDKP-----FTDVLEKELvdrgvtLALGE 210
Cdd:PRK15317 352 KRVAVIGGGNSGVEaaidlagIV-------KHVTVLefaPELkaDQVLQDKLRSLpnvtiITNAQTTEV------TGDGD 418
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498429787 211 NVS--EFIPDENGKVKQVttasqtfDADMVILCVGFRPNTKLVEGKVETLPNGAIKVNEYMQTSNPDIFAAGDSAVVNY 287
Cdd:PRK15317 419 KVTglTYKDRTTGEEHHL-------ELEGVFVQIGLVPNTEWLKGTVELNRRGEIIVDARGATSVPGVFAAGDCTTVPY 490
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
2-306 |
8.97e-06 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 48.19 E-value: 8.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 2 KVVVIGCTHAGTAAVKSILKNNpeADVTVYERNDNVS-FLSCGIALYvggvvKDPAGLFYSNPEELASLGAKVKMEhdvt 80
Cdd:PRK12814 195 KVAIIGAGPAGLTAAYYLLRKG--HDVTIFDANEQAGgMMRYGIPRF-----RLPESVIDADIAPLRAMGAEFRFN---- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 81 dvDTENKQVTAKDLKTgetetvSYDKLVMTTG-SWPIIPPIKGIESENIL----LCKNYNQANeiiaKAEEAKKVVIVGG 155
Cdd:PRK12814 264 --TVFGRDITLEELQK------EFDAVLLAVGaQKASKMGIPGEELPGVIsgidFLRNVALGT----ALHPGKKVVVIGG 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 156 GYIGIELVEAFVESGKE-VTLIDGLDRilnkyLDKPFTDVLEKELVDRGVTLAL---------GENVSEFI--------P 217
Cdd:PRK12814 332 GNTAIDAARTALRLGAEsVTILYRRTR-----EEMPANRAEIEEALAEGVSLRElaapvsierSEGGLELTaikmqqgeP 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 218 DENGKVKQVTTASQTFD--ADMVILCVGFRPNTKLVEGK-VETLPNGAIKVN-EYMQTSNPDIFAAGDSAvvnynpSGTQ 293
Cdd:PRK12814 407 DESGRRRPVPVEGSEFTlqADTVISAIGQQVDPPIAEAAgIGTSRNGTVKVDpETLQTSVAGVFAGGDCV------TGAD 480
|
330
....*....|...
gi 498429787 294 nyipLATNAVRQG 306
Cdd:PRK12814 481 ----IAINAVEQG 489
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
57-416 |
3.12e-05 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 46.36 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 57 GLFYSNPEELASLgAKVKMEHDVTDVDTenkqvtakdlktGETETVSYDKLVMTTGSWPIIPpikgiesENILLCKNYN- 135
Cdd:PTZ00052 111 GLRSSKVEYINGL-AKLKDEHTVSYGDN------------SQEETITAKYILIATGGRPSIP-------EDVPGAKEYSi 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 136 QANEIIAKAEEAKKVVIVGGGYIGIELVEAFVESGKEVTLidGLDRILNKYLDKPFTDVLEKELVDRGVTLALGEnVSEF 215
Cdd:PTZ00052 171 TSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTV--AVRSIPLRGFDRQCSEKVVEYMKEQGTLFLEGV-VPIN 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 216 IPDENGKVKQVTTASQTFDADMVILCVGFRPNTK---LVEGKVETLPNG-AIKVNEymQTSNPDIFAAGDSAVvnynpsg 291
Cdd:PTZ00052 248 IEKMDDKIKVLFSDGTTELFDTVLYATGRKPDIKglnLNAIGVHVNKSNkIIAPND--CTNIPNIFAVGDVVE------- 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 292 tqNYIPLATNAVRQGLLVGNNL---TEQKMAYR---GTQGTSGLYlfgwtiGSTGVTTESA--------------PMNNL 351
Cdd:PTZ00052 319 --GRPELTPVAIKAGILLARRLfkqSNEFIDYTfipTTIFTPIEY------GACGYSSEAAiakygeddieeylqEFNTL 390
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498429787 352 DVQAT-------LFEDNYRPEFMPTTekvMMELVYEKGT-NRIVGAQFM--SKYDITQSantMSLAVQNKMTVED 416
Cdd:PTZ00052 391 EIAAVhrekherARKDEYDFDVSSNC---LAKLVCVKSEdNKVVGFHFVgpNAGEITQG---FSLALKLGAKKSD 459
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
68-281 |
3.23e-05 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 46.41 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 68 SLGAKVKMEHDVTDvdtenkQVTAKDLKTGetetvsYDKLVMTTG---SWPIipPIKGIESENIL----LCKNYNQANEI 140
Cdd:PRK12771 199 DLGVEVRLGVRVGE------DITLEQLEGE------FDAVFVAIGaqlGKRL--PIPGEDAAGVLdavdFLRAVGEGEPP 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 141 IAkaeeAKKVVIVGGGYIGIELVEAFVESG-KEVTLIDGLDR-----------------ILNKYLDKPftdvLEKELVDR 202
Cdd:PRK12771 265 FL----GKRVVVIGGGNTAMDAARTARRLGaEEVTIVYRRTRedmpahdeeieealregVEINWLRTP----VEIEGDEN 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 203 GVTLALGENVSEFIPDENGKVKQVTTASQTFDADMVILCVGFRPNTKLVEGKVE-TLPNGAIKVNE-YMQTSNPDIFAAG 280
Cdd:PRK12771 337 GATGLRVITVEKMELDEDGRPSPVTGEEETLEADLVVLAIGQDIDSAGLESVPGvEVGRGVVQVDPnFMMTGRPGVFAGG 416
|
.
gi 498429787 281 D 281
Cdd:PRK12771 417 D 417
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
66-282 |
9.05e-05 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 44.90 E-value: 9.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 66 LASLGAKVKMEHDVtdVDTENKQV----TAKDLKTGETETVSydKLVMTTGSWPIIPpiKGIESENillcKNYNQANEII 141
Cdd:PTZ00153 237 LKSKKFCKNSEHVQ--VIYERGHIvdknTIKSEKSGKEFKVK--NIIIATGSTPNIP--DNIEVDQ----KSVFTSDTAV 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 142 AKAEEAKKVVIVGGGYIGIELVEAFVESGKEVTLIDGLDRIL---NKYLDKPFTDVLEKELVDRGVTLALGENV------ 212
Cdd:PTZ00153 307 KLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSPQLLpllDADVAKYFERVFLKSKPVRVHLNTLIEYVragkgn 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 213 -------SEFIPDENGKVKQVTTASQTFDADMVILCVGFRPNTK---LVEGKVeTLPNGAIKVNEYMQTSNPD------I 276
Cdd:PTZ00153 387 qpviighSERQTGESDGPKKNMNDIKETYVDSCLVATGRKPNTNnlgLDKLKI-QMKRGFVSVDEHLRVLREDqevydnI 465
|
....*.
gi 498429787 277 FAAGDS 282
Cdd:PTZ00153 466 FCIGDA 471
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
148-267 |
2.12e-04 |
|
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.
Pssm-ID: 274399 [Multi-domain] Cd Length: 409 Bit Score: 43.37 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 148 KKVVIVGGGYIGIELVEAFVESGKEVTLID-GLDRI--LNKYLDkPFTDVLEKELVDRGVtlalgenvsefipdENGKVK 224
Cdd:TIGR03026 1 MKIAVIGLGYVGLPLAALLADLGHDVTGVDiDQEKVdkLNKGKS-PIYEPGLDELLAKAL--------------KAGRLR 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 498429787 225 QVTTASQTF-DADMVILCVGF------RPNTKLVEGKVET----LPNGAIKVNE 267
Cdd:TIGR03026 66 ATTDYEEAIrDADVIIICVPTplkedgSPDLSYVESAAETiakhLRKGATVVLE 119
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
148-252 |
2.32e-04 |
|
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440534 [Multi-domain] Cd Length: 445 Bit Score: 43.15 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498429787 148 KKVVIVGGGYIGIELVEAFVESGKEVTLIDgldrilnkylDKPFTDVLEKELVDRGVTLALGENVSEFIpdengkvkqvt 227
Cdd:COG0771 5 KKVLVLGLGKSGLAAARLLAKLGAEVTVSD----------DRPAPELAAAELEAPGVEVVLGEHPEELL----------- 63
|
90 100
....*....|....*....|....*
gi 498429787 228 tasqtFDADMVILCVGFRPNTKLVE 252
Cdd:COG0771 64 -----DGADLVVKSPGIPPDHPLLK 83
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
139-177 |
6.46e-04 |
|
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];
Pssm-ID: 440335 [Multi-domain] Cd Length: 296 Bit Score: 41.59 E-value: 6.46e-04
10 20 30
....*....|....*....|....*....|....*....
gi 498429787 139 EIIAKAEEAKKVVIVGGGYIGIELVEAFVESGKEVTLID 177
Cdd:COG0569 87 MERGIKKLKMHVIIIGAGRVGRSLARELEEEGHDVVVID 125
|
|
| NAD_binding_7 |
pfam13241 |
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria. |
148-200 |
1.95e-03 |
|
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.
Pssm-ID: 433055 [Multi-domain] Cd Length: 104 Bit Score: 37.46 E-value: 1.95e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498429787 148 KKVVIVGGGYIGIELVEAFVESGKEVTLI--------DGLDRILNKYLDKpftDVLEKELV 200
Cdd:pfam13241 8 KRVLVVGGGEVAARKARKLLEAGAKVTVVspeitpflEGLLDLIRREFEG---DLDGADLV 65
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
191-243 |
5.28e-03 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 38.73 E-value: 5.28e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 498429787 191 FTDVLEKELVDRGVTLALGENVSEFIPdENGKVKQVTTASQTFDADMVILCVG 243
Cdd:COG0665 153 LVRALARAARAAGVRIREGTPVTGLER-EGGRVTGVRTERGTVRADAVVLAAG 204
|
|
| |
