|
Name |
Accession |
Description |
Interval |
E-value |
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
33-427 |
1.17e-86 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 269.70 E-value: 1.17e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 33 GELAIISREQVPPYERPALSKGyihLENKATLPNFYVAAgiggerqfPQWYKEKGIELILGTEIVKADLAAKTLVSGTGQ 112
Cdd:COG1251 27 GEITVIGAEPHPPYNRPPLSKV---LAGETDEEDLLLRP--------ADFYEENGIDLRLGTRVTAIDRAARTVTLADGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 113 VFKYQTLLAATGSSVIRLsdfGVPGADAKNIFYLRELEDADYL-AYAmetKEKGKAVVVGGGYIGLELGAALKANNLDVT 191
Cdd:COG1251 96 TLPYDKLVLATGSRPRVP---PIPGADLPGVFTLRTLDDADALrAAL---APGKRVVVIGGGLIGLEAAAALRKRGLEVT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 192 MVYPEPWCMPRLFTAGIASFYEGYYANKGINIVKGTVASGFTtnSNGEVTEVKLKDGRTLEADIVIVGVGGRPIISLFKD 271
Cdd:COG1251 170 VVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIE--GDDRVTGVRLADGEELPADLVVVAIGVRPNTELARA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 272 ---QVEeekGGLKTDGFFKTSLPDVYAIGDVATFPMKLYNEmRRVEHVDHARKSAEQAVKAIKaaeeGNSIPEYDYLPYF 348
Cdd:COG1251 248 aglAVD---RGIVVDDYLRTSDPDIYAAGDCAEHPGPVYGR-RVLELVAPAYEQARVAAANLA----GGPAAYEGSVPST 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 349 YSRAFDLSWQFYGDNVG--ESVLFGDndpespkPKFGSY---WIKERKVVGAFLeGGSPEENNAIAKLARAQPSVESLEV 423
Cdd:COG1251 320 KLKVFGVDVASAGDAEGdeEVVVRGD-------PARGVYkklVLRDGRLVGAVL-VGDTSDAGALRQLIKNGRPLPPRAL 391
|
....
gi 18414298 424 LSKE 427
Cdd:COG1251 392 LDAA 395
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
33-362 |
1.00e-67 |
|
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: 218.53 E-value: 1.00e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 33 GELAIISREQVPPYERPALSKgyihlenkatlpnfYVAAGIGGERQF----PQWYKEKGIELILGTEIVKADLAAKTLVS 108
Cdd:COG0446 6 AEITVIEKGPHHSYQPCGLPY--------------YVGGGIKDPEDLlvrtPESFERKGIDVRTGTEVTAIDPEAKTVTL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 109 GTGQVFKYQTLLAATGSSVIRLSdfgVPGADAKNIFYLRELEDADYLAYAMETKEKGKAVVVGGGYIGLELGAALKANNL 188
Cdd:COG0446 72 RDGETLSYDKLVLATGARPRPPP---IPGLDLPGVFTLRTLDDADALREALKEFKGKRAVVIGGGPIGLELAEALRKRGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 189 DVTMVYPEPWCMPRlFTAGIASFYEGYYANKGINIVKGTVASGFTTNSNGEVTevkLKDGRTLEADIVIVGVGGRPIISL 268
Cdd:COG0446 149 KVTLVERAPRLLGV-LDPEMAALLEEELREHGVELRLGETVVAIDGDDKVAVT---LTDGEEIPADLVVVAPGVRPNTEL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 269 FKD-QVE-EEKGGLKTDGFFKTSLPDVYAIGDVATFPMKLYNEMRRVEHVDHARKSAEQAVKAIKAAEegnsiPEYDYLP 346
Cdd:COG0446 225 AKDaGLAlGERGWIKVDETLQTSDPDVYAAGDCAEVPHPVTGKTVYIPLASAANKQGRVAAENILGGP-----APFPGLG 299
|
330
....*....|....*.
gi 18414298 347 YFYSRAFDLSWQFYGD 362
Cdd:COG0446 300 TFISKVFDLCIASTGT 315
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
31-323 |
6.71e-53 |
|
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: 179.05 E-value: 6.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 31 KPGELAIISREQVPPYERPALSKGYIHlenkatlpnfyVAAGIGGERQFPQWYKEK---------GIELILGTEIVKADL 101
Cdd:pfam07992 22 LGGKVTLIEDEGTCPYGGCVLSKALLG-----------AAEAPEIASLWADLYKRKeevvkklnnGIEVLLGTEVVSIDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 102 AAKTL-----VSGTGQVFKYQTLLAATGSSVIRLsdfGVPGADAKNIFYLRELEDADYLAYAmetKEKGKAVVVGGGYIG 176
Cdd:pfam07992 91 GAKKVvleelVDGDGETITYDRLVIATGARPRLP---PIPGVELNVGFLVRTLDSAEALRLK---LLPKRVVVVGGGYIG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 177 LELGAALKANNLDVTMVYPEPWcMPRLFTAGIASFYEGYYANKGINIVKGTVASGFttNSNGEVTEVKLKDGRTLEADIV 256
Cdd:pfam07992 165 VELAAALAKLGKEVTLIEALDR-LLRAFDEEISAALEKALEKNGVEVRLGTSVKEI--IGDGDGVEVILKDGTEIDADLV 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18414298 257 IVGVGGRPIISLFKDQ-VE-EEKGGLKTDGFFKTSLPDVYAIGDVAtfpmklyneMRRVEHVDHARKSA 323
Cdd:pfam07992 242 VVAIGRRPNTELLEAAgLElDERGGIVVDEYLRTSVPGIYAAGDCR---------VGGPELAQNAVAQG 301
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
33-379 |
7.63e-33 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 128.12 E-value: 7.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 33 GELAIISREQVPPYERPALSKGYihLENKATLPNFYVAAgiggerqfpQWYKEKGIELILGTEIVKADLAAKTLVSGTGQ 112
Cdd:PRK09754 29 GELHLFSDERHLPYERPPLSKSM--LLEDSPQLQQVLPA---------NWWQENNVHLHSGVTIKTLGRDTRELVLTNGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 113 VFKYQTLLAATGSSVIRLsdfgvPGADA--KNIFYLRELEDADYLAYAMetKEKGKAVVVGGGYIGLELGAALKANNLDV 190
Cdd:PRK09754 98 SWHWDQLFIATGAAARPL-----PLLDAlgERCFTLRHAGDAARLREVL--QPERSVVIVGAGTIGLELAASATQRRCKV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 191 TMVYPEPWCMPRLFTAGIASFYEGYYANKGINIVKGTvasGFTTNSNGEVTEVKLKDGRTLEADIVIVGVGGRpiislFK 270
Cdd:PRK09754 171 TVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNN---AIEHVVDGEKVELTLQSGETLQADVVIYGIGIS-----AN 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 271 DQVEEE-----KGGLKTDGFFKTSLPDVYAIGDVATfpMKLYN-EMRRVEHVDHARKSAEQAVKAIKAAEegnsiPEYDY 344
Cdd:PRK09754 243 DQLAREanldtANGIVIDEACRTCDPAIFAGGDVAI--TRLDNgALHRCESWENANNQAQIAAAAMLGLP-----LPLLP 315
|
330 340 350
....*....|....*....|....*....|....*
gi 18414298 345 LPYFYSRAFDLSWQFYGDNVGESVLFgDNDPESPK 379
Cdd:PRK09754 316 PPWFWSDQYSDNLQFIGDMRGDDWLC-RGNPETQK 349
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
34-372 |
1.71e-31 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 127.64 E-value: 1.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 34 ELAIISREQVPPYERPALSKgyiHLENKATLPNFYVAAGiggerqfpQWYKEKGIELILGTEIVKADLAAKTLVSGTGQV 113
Cdd:TIGR02374 26 EITIFGEEPHPNYNRILLSS---VLQGEADLDDITLNSK--------DWYEKHGITLYTGETVIQIDTDQKQVITDAGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 114 FKYQTLLAATGSSVIRLSdfgVPGADAKNIFYLRELEDADYL-AYAMETKekgKAVVVGGGYIGLELGAALKANNLDVTM 192
Cdd:TIGR02374 95 LSYDKLILATGSYPFILP---IPGADKKGVYVFRTIEDLDAImAMAQRFK---KAAVIGGGLLGLEAAVGLQNLGMDVSV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 193 VYPEPWCMPRLFTAGIASFYEGYYANKGINIV--KGTVASgfttNSNGEVTEVKLKDGRTLEADIVIVGVGGRPIISLFK 270
Cdd:TIGR02374 169 IHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLleKDTVEI----VGATKADRIRFKDGSSLEADLIVMAAGIRPNDELAV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 271 DQVEEEKGGLKTDGFFKTSLPDVYAIGDVATFPMKLYN------EMRRVEhVDH-----------ARKSAEQAVKAI--- 330
Cdd:TIGR02374 245 SAGIKVNRGIIVNDSMQTSDPDIYAVGECAEHNGRVYGlvaplyEQAKVL-ADHicgveceeyegSDLSAKLKLLGVdvw 323
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 18414298 331 -----KAAEEGNSIPEYDYLPYFYSRAFdlswqFYGDNVGESVLFGD 372
Cdd:TIGR02374 324 sagdaQETERTTSIKIYDEQKGIYKKLV-----LSDDKLLGAVLFGD 365
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
80-301 |
5.16e-28 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 115.14 E-value: 5.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 80 PQWYKEKGIELILGTEIVKADLAAKTLV---SGTGQVF--KYQTLLAATGSSVIRLSdfgVPGADAKNIFYLRELEDADY 154
Cdd:PRK09564 63 PEEFIKSGIDVKTEHEVVKVDAKNKTITvknLKTGSIFndTYDKLMIATGARPIIPP---IKNINLENVYTLKSMEDGLA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 155 LAYAMETKEKGKAVVVGGGYIGLELGAALKANNLDVTMVYPEPWCMPRLFTAGIASFYEGYYANKGINIVKGTVASGFTT 234
Cdd:PRK09564 140 LKELLKDEEIKNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSLIG 219
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18414298 235 NSNGEVTEVklkDGRTLEADIVIVGVGGRPIISLFKDQVEE--EKGGLKTDGFFKTSLPDVYAIGDVAT 301
Cdd:PRK09564 220 EDKVEGVVT---DKGEYEADVVIVATGVKPNTEFLEDTGLKtlKNGAIIVDEYGETSIENIYAAGDCAT 285
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
84-344 |
1.52e-27 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 112.92 E-value: 1.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 84 KEKGIELILGtEIVKADLAAKTLVSGTGQVFKYQTLLAATGSsviRLSDFGVPGAdAKNIFYLRELEDADYL-------A 156
Cdd:COG1252 67 RRAGVRFIQG-EVTGIDPEARTVTLADGRTLSYDYLVIATGS---VTNFFGIPGL-AEHALPLKTLEDALALrerllaaF 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 157 YAMETKEKGKAVVVGGGYIGLELGAAL-------------KANNLDVTMVYPEPWCMPRlFTAGIASFYEGYYANKGINI 223
Cdd:COG1252 142 ERAERRRLLTIVVVGGGPTGVELAGELaellrkllrypgiDPDKVRITLVEAGPRILPG-LGEKLSEAAEKELEKRGVEV 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 224 VKGTVASGFTTNsngevtEVKLKDGRTLEADIVIV--GVGGRPIISLFKDQVEEeKGGLKTDGFFKT-SLPDVYAIGDVA 300
Cdd:COG1252 221 HTGTRVTEVDAD------GVTLEDGEEIPADTVIWaaGVKAPPLLADLGLPTDR-RGRVLVDPTLQVpGHPNVFAIGDCA 293
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 18414298 301 TFPMKLYNEMRRVEHvdHARKSAEQAVKAIKAAEEGNSIPEYDY 344
Cdd:COG1252 294 AVPDPDGKPVPKTAQ--AAVQQAKVLAKNIAALLRGKPLKPFRY 335
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
84-304 |
3.93e-23 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 100.99 E-value: 3.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 84 KEKGIELILGTeivkADLAAKTLVS----GTGQVFKYQTLLAATGSSVIRLsdfgvPG--ADAKNIFYLREledadylay 157
Cdd:PRK06416 103 KKNKVDIIRGE----AKLVDPNTVRvmteDGEQTYTAKNIILATGSRPREL-----PGieIDGRVIWTSDE--------- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 158 AMETKE-KGKAVVVGGGYIGLELGAALKANNLDVTMVypEpwCMPRL---FTAGIASFYEGYYANKGINIVKGTVASGFT 233
Cdd:PRK06416 165 ALNLDEvPKSLVVIGGGYIGVEFASAYASLGAEVTIV--E--ALPRIlpgEDKEISKLAERALKKRGIKIKTGAKAKKVE 240
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18414298 234 TNSNG-EVTEVKLKDGRTLEADIVIVGVGGRPIIS---LFKDQVEEEKGGLKTDGFFKTSLPDVYAIGDVATFPM 304
Cdd:PRK06416 241 QTDDGvTVTLEDGGKEETLEADYVLVAVGRRPNTEnlgLEELGVKTDRGFIEVDEQLRTNVPNIYAIGDIVGGPM 315
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
81-304 |
1.33e-22 |
|
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: 99.39 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 81 QWYKEKGIELILGT-EIVkadlAAKTLVSGTGQVFKYQTLLAATGSSVIRLSdfgVPGADAKNIFYLREledadylayAM 159
Cdd:COG1249 99 ELLKKNGVDVIRGRaRFV----DPHTVEVTGGETLTADHIVIATGSRPRVPP---IPGLDEVRVLTSDE---------AL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 160 ETKEKGK-AVVVGGGYIGLELGAALKANNLDVTMVYPepwcMPRL---FTAGIASFYEGYYANKGINIVKGTVASGFTTN 235
Cdd:COG1249 163 ELEELPKsLVVIGGGYIGLEFAQIFARLGSEVTLVER----GDRLlpgEDPEISEALEKALEKEGIDILTGAKVTSVEKT 238
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18414298 236 SNGevTEVKLKDGR---TLEADIVIVGVGGRPIISLFKdqVEE------EKGGLKTDGFFKTSLPDVYAIGDVATFPM 304
Cdd:COG1249 239 GDG--VTVTLEDGGgeeAVEADKVLVATGRRPNTDGLG--LEAagveldERGGIKVDEYLRTSVPGIYAIGDVTGGPQ 312
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
83-347 |
2.69e-20 |
|
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: 92.71 E-value: 2.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 83 YKEKGIELILGTEIVKADLAAKTLVSGTGQVFKYQTLLAATGSSVIRLSdfGVPGADAKNIFYLREledadylayAMETK 162
Cdd:TIGR01350 99 LKKNKVTVIKGEAKFLDPGTVSVTGENGEETLEAKNIIIATGSRPRSLP--GPFDFDGKVVITSTG---------ALNLE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 163 EK-GKAVVVGGGYIGLELGAALKANNLDVTMVYPEPWCMPrLFTAGIASFYEGYYANKGINIVKGTVASGFTTNSNGEVT 241
Cdd:TIGR01350 168 EVpESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILP-GEDAEVSKVLQKALKKKGVKILTNTKVTAVEKNDDQVTY 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 242 EVKLKDGRTLEADIVIVGVGGRP---IISLFKDQVE-EEKGGLKTDGFFKTSLPDVYAIGDVATFPMklynemrrVEHVd 317
Cdd:TIGR01350 247 ENKGGETETLTGEKVLVAVGRKPnteGLGLEKLGVElDERGRIVVDEYMRTNVPGIYAIGDVIGGPM--------LAHV- 317
|
250 260 270
....*....|....*....|....*....|
gi 18414298 318 hARKSAEQAVKAIkAAEEGNSIpEYDYLPY 347
Cdd:TIGR01350 318 -ASHEGIVAAENI-AGKEPAHI-DYDAVPS 344
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
81-301 |
4.41e-17 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 82.91 E-value: 4.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 81 QWYKEKGIELILGTEIVKADLAAKTLV---SGTGQVFK--YQTLLAATGSSVIRLsdfgvpGADAKNIFYLRELEDADYL 155
Cdd:PRK13512 66 KFYDRKQITVKTYHEVIAINDERQTVTvlnRKTNEQFEesYDKLILSPGASANSL------GFESDITFTLRNLEDTDAI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 156 AYAMETKEKGKAVVVGGGYIGLELGAALKANNLDVTMVYPEPWC---MPRLFTAGIASFYEG----YYANKGINIVKGtv 228
Cdd:PRK13512 140 DQFIKANQVDKALVVGAGYISLEVLENLYERGLHPTLIHRSDKInklMDADMNQPILDELDKreipYRLNEEIDAING-- 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18414298 229 asgfttnsngevTEVKLKDGRTLEADIVIVGVGGRPIISLFKDQ--VEEEKGGLKTDGFFKTSLPDVYAIGDVAT 301
Cdd:PRK13512 218 ------------NEVTFKSGKVEHYDMIIEGVGTHPNSKFIESSniKLDDKGFIPVNDKFETNVPNIYAIGDIIT 280
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
87-306 |
2.18e-16 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 79.39 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 87 GIELILgTEIVKADLA--AKTLVSGTGQVFKYQTLLAATGSSVIRLsdfGVPGADA---KNIFYLrelEDADYLAYamet 161
Cdd:COG0492 71 GAEILL-EEVTSVDKDdgPFRVTTDDGTEYEAKAVIIATGAGPRKL---GLPGEEEfegRGVSYC---ATCDGFFF---- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 162 keKGKAV-VVGGGYIGLELgaalkANNL-----DVTMVYP--EPWCMP----RLFtagiasfyegyyANKGINIVKGTVA 229
Cdd:COG0492 140 --RGKDVvVVGGGDSALEE-----ALYLtkfasKVTLIHRrdELRASKilveRLR------------ANPKIEVLWNTEV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 230 SGFttNSNGEVTEVKLKDGRT-----LEADIVIVGVGGRPIISLFKDQVEE--EKGGLKTDGFFKTSLPDVYAIGDVATF 302
Cdd:COG0492 201 TEI--EGDGRVEGVTLKNVKTgeekeLEVDGVFVAIGLKPNTELLKGLGLEldEDGYIVVDEDMETSVPGVFAAGDVRDY 278
|
....
gi 18414298 303 PMKL 306
Cdd:COG0492 279 KYRQ 282
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
84-304 |
3.62e-15 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 77.14 E-value: 3.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 84 KEKGIELILGT-EIVkadlAAKTLVSGtGQVFKYQTLLAATGSSVIRlsdfgVPGADaknifylrELEDADYLAY--AME 160
Cdd:PRK06292 103 KKPKIDKIKGTaRFV----DPNTVEVN-GERIEAKNIVIATGSRVPP-----IPGVW--------LILGDRLLTSddAFE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 161 TKEKGKAV-VVGGGYIGLELGAALKANNLDVTMVYPEPWCMPrLFTAGIASFYEGYYAnKGINIVKGTVASGFTTNSNGE 239
Cdd:PRK06292 165 LDKLPKSLaVIGGGVIGLELGQALSRLGVKVTVFERGDRILP-LEDPEVSKQAQKILS-KEFKIKLGAKVTSVEKSGDEK 242
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 240 VTEVKLKDG-RTLEADIVIVGVGGRP---IISLFKDQVE-EEKGGLKTDGFFKTSLPDVYAIGDVATFPM 304
Cdd:PRK06292 243 VEELEKGGKtETIEADYVLVATGRRPntdGLGLENTGIElDERGRPVVDEHTQTSVPGIYAAGDVNGKPP 312
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
80-318 |
9.24e-15 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 76.70 E-value: 9.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 80 PQWYKEKGIELILGTEIVKADLAAKTLVSGTGQVFKYQTLLAATGSSVIrlsdfgVP---GADAKNIFYLRELEDADyla 156
Cdd:PRK14989 66 EGFYEKHGIKVLVGERAITINRQEKVIHSSAGRTVFYDKLIMATGSYPW------IPpikGSETQDCFVYRTIEDLN--- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 157 yAME--TKEKGKAVVVGGGYIGLELGAALKANNLDVTMVYPEPWCMPRLFTAGIASFYEGYYANKGINIVKGTVASGFTT 234
Cdd:PRK14989 137 -AIEacARRSKRGAVVGGGLLGLEAAGALKNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSKNTLEIVQ 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 235 NSNGEVTEVKLKDGRTLEADIVIVGVGGRPIISLFKdQVE---EEKGGLKTDGFFKTSLPDVYAIGDVATFPMKLYN--- 308
Cdd:PRK14989 216 EGVEARKTMRFADGSELEVDFIVFSTGIRPQDKLAT-QCGlavAPRGGIVINDSCQTSDPDIYAIGECASWNNRVFGlva 294
|
250
....*....|...
gi 18414298 309 ---EMRRVEhVDH 318
Cdd:PRK14989 295 pgyKMAQVA-VDH 306
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
84-301 |
1.09e-14 |
|
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: 75.56 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 84 KEKGIELILGTEIVKaDLAAKTLVSgtgqvfKYQTLLAATGSSVIRlsDFGVPGADAKNIF----YLRELEDADYLAYAM 159
Cdd:COG0493 182 EALGVEFRTNVEVGK-DITLDELLE------EFDAVFLATGAGKPR--DLGIPGEDLKGVHsamdFLTAVNLGEAPDTIL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 160 EtkeKGK-AVVVGGGYIG-------LELGAAlkannlDVTMVYPEPW-CMPrlftagiASFYEGYYA-NKGINIVKGTVA 229
Cdd:COG0493 253 A---VGKrVVVIGGGNTAmdcartaLRLGAE------SVTIVYRRTReEMP-------ASKEEVEEAlEEGVEFLFLVAP 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 230 SGFTTNSNGEVTEVKL---------KDGR-----------TLEADIVIVGVGGRPIISLFKDQVE---EEKGGLKTD-GF 285
Cdd:COG0493 317 VEIIGDENGRVTGLECvrmelgepdESGRrrpvpiegsefTLPADLVILAIGQTPDPSGLEEELGlelDKRGTIVVDeET 396
|
250
....*....|....*.
gi 18414298 286 FKTSLPDVYAIGDVAT 301
Cdd:COG0493 397 YQTSLPGVFAGGDAVR 412
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
87-299 |
4.18e-14 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 73.65 E-value: 4.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 87 GIELILGteivKADLAAKTLVSGTGQVFKYQTLLAATGSSVIRLSdfgVPGA----DAKNIFYLRELEDadylayametk 162
Cdd:PRK06116 107 GVDLIEG----FARFVDAHTVEVNGERYTADHILIATGGRPSIPD---IPGAeygiTSDGFFALEELPK----------- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 163 ekgKAVVVGGGYIGLELGAALKANNLDVTMVY--PEPWcmpRLFTAGIASFYEGYYANKGINIVKGTVASGFTTNSNGEV 240
Cdd:PRK06116 169 ---RVAVVGAGYIAVEFAGVLNGLGSETHLFVrgDAPL---RGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADGSL 242
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18414298 241 TeVKLKDGRTLEADIVIVGVGGRPI---ISLFKDQVE-EEKGGLKTDGFFKTSLPDVYAIGDV 299
Cdd:PRK06116 243 T-LTLEDGETLTVDCLIWAIGREPNtdgLGLENAGVKlNEKGYIIVDEYQNTNVPGIYAVGDV 304
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
88-300 |
4.79e-13 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 69.95 E-value: 4.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 88 IELILGTEIVKADLAAKTLVSGtGQVFKYQTLLAATGSSVIRLSdfgVPGADAknIFYLRELEDadYLAYAMETKEKGKA 167
Cdd:PRK04965 73 LRLFPHTWVTDIDAEAQVVKSQ-GNQWQYDKLVLATGASAFVPP---IPGREL--MLTLNSQQE--YRAAETQLRDAQRV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 168 VVVGGGYIGLELGAALKANNLDVTMVYPEPWCMPRLFTAGIASFYEGYYANKGINIVKGTVASGFTTNSNGEVteVKLKD 247
Cdd:PRK04965 145 LVVGGGLIGTELAMDLCRAGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIR--ATLDS 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 18414298 248 GRTLEADIVIVGVGGRPIISLFKDQVEEEKGGLKTDGFFKTSLPDVYAIGDVA 300
Cdd:PRK04965 223 GRSIEVDAVIAAAGLRPNTALARRAGLAVNRGIVVDSYLQTSAPDIYALGDCA 275
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
166-248 |
5.93e-13 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 63.76 E-value: 5.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 166 KAVVVGGGYIGLELGAALKANNLDVTMVYPEPWCMPrLFTAGIASFYEGYYANKGINIVKGTVASGFTTNSNGEVteVKL 245
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLP-GFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVV--VVL 77
|
...
gi 18414298 246 KDG 248
Cdd:pfam00070 78 TDG 80
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
107-304 |
2.03e-11 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 65.72 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 107 VSGTG-QVFKYQTLLAATGSSVIRLSdfGVPgADAKNIfylreLEDADYLAYameTKEKGKAVVVGGGYIGLELGAALKA 185
Cdd:PRK06327 136 VTGEDeTVITAKHVIIATGSEPRHLP--GVP-FDNKII-----LDNTGALNF---TEVPKKLAVIGAGVIGLELGSVWRR 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 186 NNLDVTMVYpepwCMPRLFTA---GIASFYEGYYANKGINIVKGTVASGFTTNSNGEVTEVKLKDG--RTLEADIVIVGV 260
Cdd:PRK06327 205 LGAEVTILE----ALPAFLAAadeQVAKEAAKAFTKQGLDIHLGVKIGEIKTGGKGVSVAYTDADGeaQTLEVDKLIVSI 280
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 18414298 261 GGRP-IISLFKDQV---EEEKGGLKTDGFFKTSLPDVYAIGDVATFPM 304
Cdd:PRK06327 281 GRVPnTDGLGLEAVglkLDERGFIPVDDHCRTNVPNVYAIGDVVRGPM 328
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
119-299 |
5.80e-11 |
|
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: 64.22 E-value: 5.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 119 LLAATGSSVIRLsdfGVPGAD----AKNIFYLREledadylayametkEKGKAVVVGGGYIGLELGA---ALKANNLDVT 191
Cdd:TIGR01423 155 ILLATGSWPQML---GIPGIEhcisSNEAFYLDE--------------PPRRVLTVGGGFISVEFAGifnAYKPRGGKVT 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 192 MVYPEPWCMpRLFTAGIASFYEGYYANKGINIVKGTVASGFTTNSNGEvTEVKLKDGRTLEADIVIVGVGGRP---IISL 268
Cdd:TIGR01423 218 LCYRNNMIL-RGFDSTLRKELTKQLRANGINIMTNENPAKVTLNADGS-KHVTFESGKTLDVDVVMMAIGRVPrtqTLQL 295
|
170 180 190
....*....|....*....|....*....|..
gi 18414298 269 FKDQVE-EEKGGLKTDGFFKTSLPDVYAIGDV 299
Cdd:TIGR01423 296 DKVGVElTKKGAIQVDEFSRTNVPNIYAIGDV 327
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
87-299 |
6.63e-11 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 64.07 E-value: 6.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 87 GIELILGT-EIVKADLAAKTLVSGTGQVFKYQTLLAATGSSVIRLSdfgVPGadaknifylRELEDADYLAYAMETKEKg 165
Cdd:PLN02507 138 GVKLYEGEgKIVGPNEVEVTQLDGTKLRYTAKHILIATGSRAQRPN---IPG---------KELAITSDEALSLEELPK- 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 166 KAVVVGGGYIGLELGAALKANNLDVTMVYPEPwcMP-RLFT----AGIASFYEGyyanKGINIVKGTVASGFTTNSNGev 240
Cdd:PLN02507 205 RAVVLGGGYIAVEFASIWRGMGATVDLFFRKE--LPlRGFDdemrAVVARNLEG----RGINLHPRTNLTQLTKTEGG-- 276
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18414298 241 TEVKLKDGRTLEADIVIVGVGGRPI---ISLFKDQVEEEK-GGLKTDGFFKTSLPDVYAIGDV 299
Cdd:PLN02507 277 IKVITDHGEEFVADVVLFATGRAPNtkrLNLEAVGVELDKaGAVKVDEYSRTNIPSIWAIGDV 339
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
102-315 |
2.26e-10 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 62.28 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 102 AAKTLVSGTGQVFKYQTLLAATGS-----SVIRLSdfGVPGADAKNIFYLRELedadylayametkeKGKAVVVGGGYIG 176
Cdd:PRK07846 115 GPKTLRTGDGEEITADQVVIAAGSrpvipPVIADS--GVRYHTSDTIMRLPEL--------------PESLVIVGGGFIA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 177 LELGAALKANNLDVTMVYPEPwCMPRLFTAGIA-SFYEgyYANKGINIVKGTVASGFTTNSNGevTEVKLKDGRTLEADI 255
Cdd:PRK07846 179 AEFAHVFSALGVRVTVVNRSG-RLLRHLDDDISeRFTE--LASKRWDVRLGRNVVGVSQDGSG--VTLRLDDGSTVEADV 253
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18414298 256 VIVGVGGRP---IISLFKDQVE-EEKGGLKTDGFFKTSLPDVYAIGDVAT-FPMK-LYN-EMRRVEH 315
Cdd:PRK07846 254 LLVATGRVPngdLLDAAAAGVDvDEDGRVVVDEYQRTSAEGVFALGDVSSpYQLKhVANhEARVVQH 320
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
81-301 |
3.71e-10 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 61.73 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 81 QWYKEKGIELILGTEIVKaDLAAKTLVSGtgqvfkYQTLLAATGSSVIRlsDFGVPGADAKNIF----YLRELEDADYLa 156
Cdd:PRK11749 198 ERLLKLGVEIRTNTEVGR-DITLDELRAG------YDAVFIGTGAGLPR--FLGIPGENLGGVYsavdFLTRVNQAVAD- 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 157 yamETKEKGKAVVV-GGGYIG-------LELGAAlkannlDVTMVY---PEPwcMPrlftagiASFYEGYYA-NKGINIV 224
Cdd:PRK11749 268 ---YDLPVGKRVVViGGGNTAmdaartaKRLGAE------SVTIVYrrgREE--MP-------ASEEEVEHAkEEGVEFE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 225 KGTVASGFTTNSNGeVTEVKL---------KDGR----------TLEADIVIVGVGGRPIISLFKDQVEEE---KGGLKT 282
Cdd:PRK11749 330 WLAAPVEILGDEGR-VTGVEFvrmelgepdASGRrrvpiegsefTLPADLVIKAIGQTPNPLILSTTPGLElnrWGTIIA 408
|
250 260
....*....|....*....|
gi 18414298 283 D-GFFKTSLPDVYAIGDVAT 301
Cdd:PRK11749 409 DdETGRTSLPGVFAGGDIVT 428
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
81-299 |
9.20e-10 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 60.22 E-value: 9.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 81 QWYKE-KGIELILGTeivkADLAAKTLVSGTGQVFKYQTLLAATGSsviRLSDFGVPGadaknifylreLEDADYLAYA- 158
Cdd:PRK06370 102 QWLRGlEGVDVFRGH----ARFESPNTVRVGGETLRAKRIFINTGA---RAAIPPIPG-----------LDEVGYLTNEt 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 159 -METKEK-GKAVVVGGGYIGLELGAALKANNLDVTMVYPEPWCMPRlFTAGIASFYEGYYANKGINIVKGTVASGFTTNS 236
Cdd:PRK06370 164 iFSLDELpEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPR-EDEDVAAAVREILEREGIDVRLNAECIRVERDG 242
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18414298 237 NGEVTEVKLKDGR-TLEADIVIVGVGGRPIIS---LFKDQVE-EEKGGLKTDGFFKTSLPDVYAIGDV 299
Cdd:PRK06370 243 DGIAVGLDCNGGApEITGSHILVAVGRVPNTDdlgLEAAGVEtDARGYIKVDDQLRTTNPGIYAAGDC 310
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
113-301 |
1.01e-07 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 54.00 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 113 VFKYQTLLAATGSsviRLSDFGVPGADaKNIFYLRE--------------LEDADYLAYAMETKEK-GKAVVVGGGYIGL 177
Cdd:PTZ00318 111 SVPYDKLVVAHGA---RPNTFNIPGVE-ERAFFLKEvnhargirkrivqcIERASLPTTSVEERKRlLHFVVVGGGPTGV 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 178 ELGAALkaNNL---DVTMVYPE--PWCMPRLFTAG--IASFYEGYYANKGINIVKgtvASGFTTNSNGEVTEVK-----L 245
Cdd:PTZ00318 187 EFAAEL--ADFfrdDVRNLNPElvEECKVTVLEAGseVLGSFDQALRKYGQRRLR---RLGVDIRTKTAVKEVLdkevvL 261
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 18414298 246 KDGRTLEADIVI--VGVGGRPIISLFKDQvEEEKGGLKTDGFFKTS-LPDVYAIGDVAT 301
Cdd:PTZ00318 262 KDGEVIPTGLVVwsTGVGPGPLTKQLKVD-KTSRGRISVDDHLRVKpIPNVFALGDCAA 319
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
84-324 |
1.85e-07 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 53.24 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 84 KEKGIELILGTEIVKaDLAAKTLVSgtgqvfKYQTLLAATGSSVIRlsDFGVPGADAKNIFylreleDA-DYLA----YA 158
Cdd:PRK12810 204 EAEGIEFRTNVEVGK-DITAEELLA------EYDAVFLGTGAYKPR--DLGIPGRDLDGVH------FAmDFLIqntrRV 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 159 METKE------KGKAVVV-GGGYIGLE-LGAALKANNLDVTM--VYPEP----------WCMPRLFTAGiasfyegyYAN 218
Cdd:PRK12810 269 LGDETepfisaKGKHVVViGGGDTGMDcVGTAIRQGAKSVTQrdIMPMPpsrrnknnpwPYWPMKLEVS--------NAH 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 219 K-GINIVKGTVASGFTTnSNGEVTEVK-----LKDG---------RTLEADIVIVGVGGR-PIISLFKD-QVE-EEKGGL 280
Cdd:PRK12810 341 EeGVEREFNVQTKEFEG-ENGKVTGVKvvrteLGEGdfepvegseFVLPADLVLLAMGFTgPEAGLLAQfGVElDERGRV 419
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 18414298 281 K-TDGFFKTSLPDVYAIGDvatfpmklyneMRR-----VEHVDHARKSAE 324
Cdd:PRK12810 420 AaPDNAYQTSNPKVFAAGD-----------MRRgqslvVWAIAEGRQAAR 458
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
87-299 |
2.51e-07 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 52.55 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 87 GIELILGT-EIVKADLAAK----TLVSGTGQVFKYQTLLAATGSSVIRLsdfgvPGA--DAKNIFYLRELEDADylayam 159
Cdd:PRK07845 106 GVRVIAGRgRLIDPGLGPHrvkvTTADGGEETLDADVVLIATGASPRIL-----PTAepDGERILTWRQLYDLD------ 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 160 ETKEKgkAVVVGGGYIGLELGAALKANNLDVTMVYPEPWCMPRLfTAGIASFYEGYYANKGINIVKGTVASGFTTNSNGe 239
Cdd:PRK07845 175 ELPEH--LIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPGE-DADAAEVLEEVFARRGMTVLKRSRAESVERTGDG- 250
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18414298 240 vTEVKLKDGRTLEADIVIVGVGGRPI---ISLFKDQVEEEKGG-LKTDGFFKTSLPDVYAIGDV 299
Cdd:PRK07845 251 -VVVTLTDGRTVEGSHALMAVGSVPNtagLGLEEAGVELTPSGhITVDRVSRTSVPGIYAAGDC 313
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
95-300 |
3.36e-07 |
|
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: 52.16 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 95 EIVKADLAAKTLVSGTGQVFKYQTLLAATGssvIRLSDFGVPGADAKNIfylrELEDADYLAYAmetkeKGKAVVVGGGY 174
Cdd:TIGR01438 123 EFVDKHRIKATNKKGKEKIYSAERFLIATG---ERPRYPGIPGAKELCI----TSDDLFSLPYC-----PGKTLVVGASY 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 175 IGLELGAALKANNLDVT-MVYPEPWcmpRLFTAGIASFYEGYYANKGINIVKGTVASGFT-TNSNGEVTEVKLKDGRTLE 252
Cdd:TIGR01438 191 VALECAGFLAGIGLDVTvMVRSILL---RGFDQDCANKVGEHMEEHGVKFKRQFVPIKVEqIEAKVLVEFTDSTNGIEEE 267
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 18414298 253 ADIVIVGVGGRPII-SLFKD----QVEEEKGGLKTDGFFKTSLPDVYAIGDVA 300
Cdd:TIGR01438 268 YDTVLLAIGRDACTrKLNLEnvgvKINKKTGKIPADEEEQTNVPYIYAVGDIL 320
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
86-299 |
5.75e-07 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 51.67 E-value: 5.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 86 KGIELILGTEivKADLAAKTLVSGTGQVfkyqtllaatgsSVIrlsdFGVPG-ADAKNIFYLRELEdadylayAMETKEK 164
Cdd:PRK07251 104 KVIEVQAGDE--KIELTAETIVINTGAV------------SNV----LPIPGlADSKHVYDSTGIQ-------SLETLPE 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 165 gKAVVVGGGYIGLELgAALKAN-NLDVTMVYPEPWCMPRlFTAGIASFYEGYYANKGINIVKGtVASGFTTNSNGEVteV 243
Cdd:PRK07251 159 -RLGIIGGGNIGLEF-AGLYNKlGSKVTVLDAASTILPR-EEPSVAALAKQYMEEDGITFLLN-AHTTEVKNDGDQV--L 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 244 KLKDGRTLEADIVIVGVGGRPIISLFK----DQVEEEKGGLKTDGFFKTSLPDVYAIGDV 299
Cdd:PRK07251 233 VVTEDETYRFDALLYATGRKPNTEPLGlentDIELTERGAIKVDDYCQTSVPGVFAVGDV 292
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
162-298 |
1.22e-05 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 47.69 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 162 KEKGKAVVVGGGYIGLELGAALKANNLDVTMVYPEPWCMpRLFTAGIASFYEGYYANKGINIVKGTVASGFTTNSNGEVT 241
Cdd:PTZ00058 235 KEAKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLL-RKFDETIINELENDMKKNNINIITHANVEEIEKVKEKNLT 313
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 242 EVKLKDGRTLEADIVIVGVGGRP---IISLFKDQVEEEKGGLKTDGFFKTSLPDVYAIGD 298
Cdd:PTZ00058 314 IYLSDGRKYEHFDYVIYCVGRSPnteDLNLKALNIKTPKGYIKVDDNQRTSVKHIYAVGD 373
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
168-303 |
4.18e-05 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 45.53 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 168 VVVGGGYIGLELGAALKANNLDVTMVYPEPWCMPRLFTAGIASFYegyYA--NKGINIVKGTVASGFTTNSNGevTEVKL 245
Cdd:PRK05249 179 IIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSFLDDEISDALS---YHlrDSGVTIRHNEEVEKVEGGDDG--VIVHL 253
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18414298 246 KDGRTLEADIVIVGVG--------GRPIISLFKDqveeEKGGLKTDGFFKTSLPDVYAIGDVATFP 303
Cdd:PRK05249 254 KSGKKIKADCLLYANGrtgntdglNLENAGLEAD----SRGQLKVNENYQTAVPHIYAVGDVIGFP 315
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
162-346 |
6.74e-04 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 41.73 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 162 KEKGKAVVVGGGYIGLELGAALKANNLDVTMVYPEpwCMPRLFTAGIASFYEGYYANKGINIVKGTVASGFTTNSngEVT 241
Cdd:PTZ00052 180 KDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRS--IPLRGFDRQCSEKVVEYMKEQGTLFLEGVVPINIEKMD--DKI 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 242 EVKLKDGRTLEADIVIVGVGGRPIISLFKDQ---VEEEKGGLKTDGFFKTSLPDVYAIGDVATfpmklynemrrvehvdh 318
Cdd:PTZ00052 256 KVLFSDGTTELFDTVLYATGRKPDIKGLNLNaigVHVNKSNKIIAPNDCTNIPNIFAVGDVVE----------------- 318
|
170 180 190
....*....|....*....|....*....|....*.
gi 18414298 319 arKSAEQAVKAIKAAE--------EGNSIPEYDYLP 346
Cdd:PTZ00052 319 --GRPELTPVAIKAGIllarrlfkQSNEFIDYTFIP 352
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
165-299 |
2.16e-03 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 40.38 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414298 165 GKAVVVGGGYIGLELGAALKANNLDVTMVYPEPWCMPRLfTAGIASFYEGYYANKGINIVKGTVASGFTTNSNGevTEVK 244
Cdd:PRK08010 159 GHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPRE-DRDIADNIATILRDQGVDIILNAHVERISHHENQ--VQVH 235
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 18414298 245 LKDGRTLeADIVIVGVGGRPIISLFKDQ----VEEEKGGLKTDGFFKTSLPDVYAIGDV 299
Cdd:PRK08010 236 SEHAQLA-VDALLIASGRQPATASLHPEnagiAVNERGAIVVDKYLHTTADNIWAMGDV 293
|
|
|