|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
1-316 |
2.07e-161 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 452.98 E-value: 2.07e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 1 MSEAKHSRLIILGSGPAGYSAAVYAARANLKPVVITGIQAGGQLTTTVEVDNWPGDVEGLTGPVLMERMQQHAERFDTEI 80
Cdd:PRK10262 1 MGTTKHSKLLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNDLTGPLLMERMHEHATKFETEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 81 VYDHIHTAKLQQRPFELIGDGGTYTCDALIIATGASAQYLGLPSEETFAGKGVSACATCDGFFYRNQVVAVVGGGNTAVE 160
Cdd:PRK10262 81 IFDHINKVDLQNRPFRLTGDSGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 161 EALYLSNIAKEVHLIHRRDKLRSEKILQDKLFEKAANGNIRLHWNQNLDEVLGDATGVTGARLRDSQTGETRE-LALSGV 239
Cdd:PRK10262 161 EALYLSNIASEVHLIHRRDGFRAEKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQNSDNIEsLDVAGL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495222737 240 FIAIGHKPNTDLFVNQLPMHDGYLRVKSGNEGDATATAIPGVFAAGDVADHVYRQAVTSAGAGCMAALDAEKYLDDI 316
Cdd:PRK10262 241 FVAIGHSPNTAIFEGQLELENGYIKVQSGIHGNATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYLDGL 317
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
9-313 |
1.83e-155 |
|
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a member of the pyridine nucleotide-disulphide oxidoreductases (pfam00070). [Energy metabolism, Electron transport]
Pssm-ID: 273540 [Multi-domain] Cd Length: 299 Bit Score: 436.67 E-value: 1.83e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 9 LIILGSGPAGYSAAVYAARANLKPVVITGIQAGGQLTTTVEVDNWPGDVEGLTGPVLMERMQQHAERFDTEIVYDHIHTA 88
Cdd:TIGR01292 2 VIIIGAGPAGLTAAIYAARANLKPLLIEGMEPGGQLTTTTEVENYPGFPEGISGPELMEKMKEQAVKFGAEIIYEEVIKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 89 KLQQRPFELI-GDGGTYTCDALIIATGASAQYLGLPSEETFAGKGVSACATCDGFFYRNQVVAVVGGGNTAVEEALYLSN 167
Cdd:TIGR01292 82 DKSDRPFKVYtGDGKEYTAKAVIIATGASARKLGIPGEDEFWGRGVSYCATCDGPFFKNKEVAVVGGGDSAIEEALYLTR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 168 IAKEVHLIHRRDKLRSEKILQDKLFEkaaNGNIRLHWNQNLDEVLGDaTGVTGARLRDSQTGETRELALSGVFIAIGHKP 247
Cdd:TIGR01292 162 IAKKVTLVHRRDKFRAEKILLDRLKK---NPKIEFLWNSTVEEIVGD-NKVEGVKIKNTVTGEEEELEVDGVFIAIGHEP 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495222737 248 NTDLFVNQLPM-HDGYLRVKSGnegdaTATAIPGVFAAGDVADHVYRQAVTSAGAGCMAALDAEKYL 313
Cdd:TIGR01292 238 NTELLKGLLELdENGYIVTDEG-----MRTSVPGVFAAGDVRDKGYRQAVTAAGDGCIAALSAERYL 299
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
9-317 |
4.67e-153 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 431.08 E-value: 4.67e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 9 LIILGSGPAGYSAAVYAARANLKPVVITGIQAGGQLTTTVEVDNWPGDVEGLTGPVLMERMQQHAERFDTEIVYDHIHTA 88
Cdd:COG0492 3 VVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQLATTKEIENYPGFPEGISGPELAERLREQAERFGAEILLEEVTSV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 89 KLQQRPFELIGD-GGTYTCDALIIATGASAQYLGLPSEETFAGKGVSACATCDGFFYRNQVVAVVGGGNTAVEEALYLSN 167
Cdd:COG0492 83 DKDDGPFRVTTDdGTEYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGKDVVVVGGGDSALEEALYLTK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 168 IAKEVHLIHRRDKLRSEKILQDKLFekaANGNIRLHWNQNLDEVLGDaTGVTGARLRDSQTGETRELALSGVFIAIGHKP 247
Cdd:COG0492 163 FASKVTLIHRRDELRASKILVERLR---ANPKIEVLWNTEVTEIEGD-GRVEGVTLKNVKTGEEKELEVDGVFVAIGLKP 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495222737 248 NTDLFVNQ-LPM-HDGYLRVksgneGDATATAIPGVFAAGDVADHVYRQAVTSAGAGCMAALDAEKYLDDIP 317
Cdd:COG0492 239 NTELLKGLgLELdEDGYIVV-----DEDMETSVPGVFAAGDVRDYKYRQAATAAGEGAIAALSAARYLEPLK 305
|
|
| AhpF_homolog |
TIGR03143 |
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase ... |
9-315 |
1.65e-65 |
|
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase homologs is found adjacent to alkylhydroperoxide reductase C subunit predominantly in cases where there is only one C subunit in the genome and that genome is lacking the F subunit partner (also a thioredcxin reductase homolog) that is usually found (TIGR03140).
Pssm-ID: 132187 [Multi-domain] Cd Length: 555 Bit Score: 215.41 E-value: 1.65e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 9 LIILGSGPAGYSAAVYAARANLKPVVITGIQAGGQLTTTVEVDNWPGdVEGLTGPVLMERMQQHAERFDTEIVYDHIHTA 88
Cdd:TIGR03143 7 LIIIGGGPAGLSAGIYAGRAKLDTLIIEKDDFGGQITITSEVVNYPG-ILNTTGPELMQEMRQQAQDFGVKFLQAEVLDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 89 KLQQRPFELIGDGGTYTCDALIIATGASAQYLGLPSEETFAGKGVSACATCDGFFYRNQVVAVVGGGNTAVEEALYLSNI 168
Cdd:TIGR03143 86 DFDGDIKTIKTARGDYKTLAVLIATGASPRKLGFPGEEEFTGRGVAYCATCDGEFFTGMDVFVIGGGFAAAEEAVFLTRY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 169 AKEVHLIHRRDKLRSEKILQDKLfekAANGNIRLHWNQNLDEVLGDAtGVTGARLRDSQTGETRELALS------GVFIA 242
Cdd:TIGR03143 166 ASKVTVIVREPDFTCAKLIAEKV---KNHPKIEVKFNTELKEATGDD-GLRYAKFVNNVTGEITEYKAPkdagtfGVFVF 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495222737 243 IGHKPNTDLFVNQLPMHD-GYLRVKsgnegDATATAIPGVFAAGDVADHVYRQAVTSAGAGCMAALDAEKYLDD 315
Cdd:TIGR03143 242 VGYAPSSELFKGVVELDKrGYIPTN-----EDMETNVPGVYAAGDLRPKELRQVVTAVADGAIAATSAERYVKE 310
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
10-313 |
6.96e-65 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 212.71 E-value: 6.96e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 10 IILGSGPAGYSAAVYAARANLKpvviTGIQA---GGQLTTTVEVDNWPGdVEGLTGPVLMERMQQHAERFDTEIVyDHIH 86
Cdd:PRK15317 215 LVVGGGPAGAAAAIYAARKGIR----TGIVAerfGGQVLDTMGIENFIS-VPETEGPKLAAALEEHVKEYDVDIM-NLQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 87 TAKLQQRPfELI----GDGGTYTCDALIIATGASAQYLGLPSEETFAGKGVSACATCDGFFYRNQVVAVVGGGNTAVEEA 162
Cdd:PRK15317 289 ASKLEPAA-GLIevelANGAVLKAKTVILATGARWRNMNVPGEDEYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAA 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 163 LYLSNIAKEVHLIHRRDKLRSEKILQDKLfekAANGNIRLHWNQNLDEVLGDATGVTGARLRDSQTGETRELALSGVFIA 242
Cdd:PRK15317 368 IDLAGIVKHVTVLEFAPELKADQVLQDKL---RSLPNVTIITNAQTTEVTGDGDKVTGLTYKDRTTGEEHHLELEGVFVQ 444
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495222737 243 IGHKPNTDLFVNQLPMHD-GYLRVksgnegDAT-ATAIPGVFAAGDVADHVYRQAVTSAGAGCMAALDAEKYL 313
Cdd:PRK15317 445 IGLVPNTEWLKGTVELNRrGEIIV------DARgATSVPGVFAAGDCTTVPYKQIIIAMGEGAKAALSAFDYL 511
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
8-302 |
7.15e-51 |
|
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: 170.19 E-value: 7.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 8 RLIILGSGPAGYSAAVYAARANLKPVVIT--GIQAGGQLTTTVEVDNWPGDVEGL-TGPVLMERMQQHAERFDTEI---- 80
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEdeGTCPYGGCVLSKALLGAAEAPEIAsLWADLYKRKEEVVKKLNNGIevll 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 81 ---VYDHIHTAKLQQRPFELIGDGGTYTCDALIIATGASAQYLGLPSEETFAGKGVSACATCDGFFYRN--QVVAVVGGG 155
Cdd:pfam07992 82 gteVVSIDPGAKKVVLEELVDGDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLlpKRVVVVGGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 156 NTAVEEALYLSNIAKEVHLIHRRDKLRS--EKILQDKLFEKAANGNIRLHWNQNLDEVLGDATGVTGarlrdsQTGETRE 233
Cdd:pfam07992 162 YIGVELAAALAKLGKEVTLIEALDRLLRafDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEV------ILKDGTE 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495222737 234 LALSGVFIAIGHKPNTDLFVNQ-LPM-HDGYLRVKsgnegDATATAIPGVFAAGDVADHVYRQAVTSAGAG 302
Cdd:pfam07992 236 IDADLVVVAIGRRPNTELLEAAgLELdERGGIVVD-----EYLRTSVPGIYAAGDCRVGGPELAQNAVAQG 301
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
9-319 |
1.15e-19 |
|
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: 88.99 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 9 LIILGSGPAGYSAAVYAARANLKPVVI-----------TG-------IQAGGQLTTTVEVDN--WPGDVEGLTGPVLMER 68
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVekgrlggtclnVGcipskalLHAAEVAHEARHAAEfgISAGAPSVDWAALMAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 69 MQQHAERFDTEIVY-------DHIH-TAKLQqRPFEL-IGDGGTYTCDALIIATGASAQYLGLPSeetFAGKGVSacaTC 139
Cdd:COG1249 86 KDKVVDRLRGGVEEllkkngvDVIRgRARFV-DPHTVeVTGGETLTADHIVIATGSRPRVPPIPG---LDEVRVL---TS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 140 DGFFYRNQV---VAVVGGGNTAVEEALYLSNIAKEVHLIHRRDKL--RSEKILQDKLFEKAANGNIRLHWNQNLDEVLGD 214
Cdd:COG1249 159 DEALELEELpksLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLlpGEDPEISEALEKALEKEGIDILTGAKVTSVEKT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 215 ATGVTgARLRDSQTGETRELALsgVFIAIGHKPNTDLF--------VNQlpmhDGYLRVksgnegDAT-ATAIPGVFAAG 285
Cdd:COG1249 239 GDGVT-VTLEDGGGEEAVEADK--VLVATGRRPNTDGLgleaagveLDE----RGGIKV------DEYlRTSVPGIYAIG 305
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 495222737 286 DVAD-----HV-YRQAVTsagAGCMAALDAEKYLDD--IPGV 319
Cdd:COG1249 306 DVTGgpqlaHVaSAEGRV---AAENILGKKPRPVDYraIPSV 344
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
100-291 |
1.43e-17 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 82.90 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 100 DGGTYTCDALIIATGASAQYLGLPseetfagkGVSACATCDGFFYRNQV---VAVVGGGNTAVEEALYLSNIAKEVHLIH 176
Cdd:PRK06116 126 NGERYTADHILIATGGRPSIPDIP--------GAEYGITSDGFFALEELpkrVAVVGAGYIAVEFAGVLNGLGSETHLFV 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 177 RRDK-LRS-EKILQDKLFEKAANGNIRLHWNQNLDEVLGDATGVTGARLRDSQTGETrelalSGVFIAIGHKPNTD---L 251
Cdd:PRK06116 198 RGDApLRGfDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADGSLTLTLEDGETLTV-----DCLIWAIGREPNTDglgL 272
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495222737 252 FVNQLPMHD-GYLRVksgnegDA-TATAIPGVFAAGDVADHV 291
Cdd:PRK06116 273 ENAGVKLNEkGYIIV------DEyQNTNVPGIYAVGDVTGRV 308
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
100-293 |
3.46e-16 |
|
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: 77.54 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 100 DGGTYTCDALIIATGASAQYL---GLPSEETFAGKGVSACATCDGFFYRNQV--VAVVGGGNTAVEEALYLSNIAKEVHL 174
Cdd:COG0446 73 DGETLSYDKLVLATGARPRPPpipGLDLPGVFTLRTLDDADALREALKEFKGkrAVVIGGGPIGLELAEALRKRGLKVTL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 175 IHRRDKL--RSEKILQDKLFEKAANGNIRLHWNQNLDEVLGDatGVTGARLRDsqtgeTRELALSGVFIAIGHKPNTDLF 252
Cdd:COG0446 153 VERAPRLlgVLDPEMAALLEEELREHGVELRLGETVVAIDGD--DKVAVTLTD-----GEEIPADLVVVAPGVRPNTELA 225
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495222737 253 VN-QLPMHD-GYLRVksgnegDAT-ATAIPGVFAAGDVADHVYR 293
Cdd:COG0446 226 KDaGLALGErGWIKV------DETlQTSDPDVYAAGDCAEVPHP 263
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
9-287 |
1.48e-14 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 73.67 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 9 LIILGSGPAGYSAAVYAARANLKPVVITGiqagGQLTTTV-------------------EVDNWPG---DVEGLT--GPV 64
Cdd:PRK06292 6 VIVIGAGPAGYVAARRAAKLGKKVALIEK----GPLGGTClnvgcipskaliaaaeafhEAKHAEEfgiHADGPKidFKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 65 LMERMQQHAERFDTEIVYDHIHTAKLQ--------QRPFELIGDGGTYTCDALIIATGASAqyLGLPSEETFAGKGVsac 136
Cdd:PRK06292 82 VMARVRRERDRFVGGVVEGLEKKPKIDkikgtarfVDPNTVEVNGERIEAKNIVIATGSRV--PPIPGVWLILGDRL--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 137 ATCDGFFYRNQV---VAVVGGGNTAVEEALYLSNIAKEVHLIHRRDKL--RSEKILQdKLFEKAANGNIRLHWNQNLDEV 211
Cdd:PRK06292 157 LTSDDAFELDKLpksLAVIGGGVIGLELGQALSRLGVKVTVFERGDRIlpLEDPEVS-KQAQKILSKEFKIKLGAKVTSV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 212 LGDATGVTGARlrdSQTGETRELALSGVFIAIGHKPNTD--------LFVNQlpmhDGYLRVksgneGDATATAIPGVFA 283
Cdd:PRK06292 236 EKSGDEKVEEL---EKGGKTETIEADYVLVATGRRPNTDglglentgIELDE----RGRPVV-----DEHTQTSVPGIYA 303
|
....
gi 495222737 284 AGDV 287
Cdd:PRK06292 304 AGDV 307
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
11-288 |
2.82e-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: 72.86 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 11 ILGSGPAGYSAAVYAARANLKPVVI-TGIQAGGQLTTtvevdnwpgdveG-----LTGPVLMERMQQHAE-----RFDTE 79
Cdd:COG0493 126 VVGSGPAGLAAAYQLARAGHEVTVFeALDKPGGLLRY------------GipefrLPKDVLDREIELIEAlgvefRTNVE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 80 IVYDhIHTAKLQQRpfeligdggtYtcDALIIATGAS-AQYLGLPSEETfagKGV-------SACATCDGFFYRNQV--- 148
Cdd:COG0493 194 VGKD-ITLDELLEE----------F--DAVFLATGAGkPRDLGIPGEDL---KGVhsamdflTAVNLGEAPDTILAVgkr 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 149 VAVVGGGNTAVE---EALYLSniAKEVHLIHRRDK----LRSEKIlqdklfEKAANGNIRLHWNQNLDEVLGDATG-VTG 220
Cdd:COG0493 258 VVVIGGGNTAMDcarTALRLG--AESVTIVYRRTReempASKEEV------EEALEEGVEFLFLVAPVEIIGDENGrVTG 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 221 ARLR-------DSQ--------TGETRELALSGVFIAIGHKPNTDLFVNQLPM---HDGYLRVksgnEGDATATAIPGVF 282
Cdd:COG0493 330 LECVrmelgepDESgrrrpvpiEGSEFTLPADLVILAIGQTPDPSGLEEELGLeldKRGTIVV----DEETYQTSLPGVF 405
|
....*.
gi 495222737 283 AAGDVA 288
Cdd:COG0493 406 AGGDAV 411
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
149-219 |
3.45e-14 |
|
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: 66.84 E-value: 3.45e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495222737 149 VAVVGGGNTAVEEALYLSNIAKEVHLIHRRDKLRS------EKILQDKLFEKaangNIRLHWNQNLDEVLGDATGVT 219
Cdd:pfam00070 2 VVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPgfdpeiAKILQEKLEKN----GIEFLLNTTVEAIEGNGDGVV 74
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
3-313 |
7.01e-14 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 71.97 E-value: 7.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 3 EAKHSRLIILGSGPAGYSAAVYAARANLKPVVITGI-QAGGQLTTTVEVDNWPGDVegltgpvLMERMQQHAERFDTEIV 81
Cdd:PRK12831 137 EKKGKKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALhEPGGVLVYGIPEFRLPKET-------VVKKEIENIKKLGVKIE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 82 YDHI--HTAKLQqrpfELIGDGGTytcDALIIATGAsaqylGLPSeetFAG-KGVSAcatcDGFFYRNQV---------- 148
Cdd:PRK12831 210 TNVVvgKTVTID----ELLEEEGF---DAVFIGSGA-----GLPK---FMGiPGENL----NGVFSANEFltrvnlmkay 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 149 -------------VAVVGGGNTAVEEALYLSNIAKEVHLIHRrdklRSEKILQDKLFE--KAANGNIRLHWNQNLDEVLG 213
Cdd:PRK12831 271 kpeydtpikvgkkVAVVGGGNVAMDAARTALRLGAEVHIVYR----RSEEELPARVEEvhHAKEEGVIFDLLTNPVEILG 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 214 DATG-VTGARL-------RDSQ--------TGETRELALSGVFIAIGHKPNTdLFVNQLPMHD----GYLRVksgnEGDA 273
Cdd:PRK12831 347 DENGwVKGMKCikmelgePDASgrrrpveiEGSEFVLEVDTVIMSLGTSPNP-LISSTTKGLKinkrGCIVA----DEET 421
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 495222737 274 TATAIPGVFAAGDvadhvyrqAVTSA-------GAGCMAALDAEKYL 313
Cdd:PRK12831 422 GLTSKEGVFAGGD--------AVTGAatvilamGAGKKAAKAIDEYL 460
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
107-313 |
1.07e-13 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 71.36 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 107 DALIIATGASA-QYLGLPSEETfagKGV-----------SACATCDGFFYRNqvVAVVGGGNTA---VEEALYLSniAKE 171
Cdd:PRK11749 227 DAVFIGTGAGLpRFLGIPGENL---GGVysavdfltrvnQAVADYDLPVGKR--VVVIGGGNTAmdaARTAKRLG--AES 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 172 VHLIHRRDklRSEKILQDKLFEKAANGNIRLHWNQNLDEVLGDATGVTGARL--------------RDSQTGETRELALS 237
Cdd:PRK11749 300 VTIVYRRG--REEMPASEEEVEHAKEEGVEFEWLAAPVEILGDEGRVTGVEFvrmelgepdasgrrRVPIEGSEFTLPAD 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 238 GVFIAIGHKPNTDLFVNQLPM---HDGYLRVksgneGDAT-ATAIPGVFAAGDV---ADHVyrqaVTSAGAGCMAALDAE 310
Cdd:PRK11749 378 LVIKAIGQTPNPLILSTTPGLelnRWGTIIA-----DDETgRTSLPGVFAGGDIvtgAATV----VWAVGDGKDAAEAIH 448
|
...
gi 495222737 311 KYL 313
Cdd:PRK11749 449 EYL 451
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
99-290 |
1.07e-12 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 67.86 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 99 GDGGTYTCDALIIATGASAQYLGLPSEEtfaGKGVsacatcdgFFYRN--------------QVVAVVGGGNTAVEEALY 164
Cdd:COG1251 92 ADGETLPYDKLVLATGSRPRVPPIPGAD---LPGV--------FTLRTlddadalraalapgKRVVVIGGGLIGLEAAAA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 165 LSNIAKEVHLIHRRDKL-------RSEKILQDKLfekAANGnIRLHWNQNLDEVLGDaTGVTGARLRDsqtGETreLALS 237
Cdd:COG1251 161 LRKRGLEVTVVERAPRLlprqldeEAGALLQRLL---EALG-VEVRLGTGVTEIEGD-DRVTGVRLAD---GEE--LPAD 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495222737 238 GVFIAIGHKPNTDLFVN-QLPMHDG-----YLRvksgnegdataTAIPGVFAAGDVADH 290
Cdd:COG1251 231 LVVVAIGVRPNTELARAaGLAVDRGivvddYLR-----------TSDPDIYAAGDCAEH 278
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
16-285 |
1.10e-12 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 67.25 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 16 PAGYSAAVYAARANLKPVVItgIQAGgQLTTTVevDNWP-----------------GDV---------------EGLTGP 63
Cdd:pfam13738 1 PAGIGCAIALKKAGLEDYLI--LEKG-NIGNSF--YRYPthmtffspsftsngfgiPDLnaispgtspaftfnrEHPSGN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 64 VLMERMQQHAERFDTEIVYDH-IHTAKLQQRPFELIGDGGTYTCDALIIATGasaqYLGLPSEETFAGKGVSACATCDGF 142
Cdd:pfam13738 76 EYAEYLRRVADHFELPINLFEeVTSVKKEDDGFVVTTSKGTYQARYVIIATG----EFDFPNKLGVPELPKHYSYVKDFH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 143 FYRNQVVAVVGGGNTAVEEALYLSNIAKEVHLIHRRDKLRSEK----------ILQdKLFEKAANGNIRLHWNQNLDEVL 212
Cdd:pfam13738 152 PYAGQKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDRDsdpsyslspdTLN-RLEELVKNGKIKAHFNAEVKEIT 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495222737 213 GDATGVTgarlrdSQTGETRELALSGVFI-AIGHKPNTDLFVNQL--PMHDGYLRVksgNEGDATaTAIPGVFAAG 285
Cdd:pfam13738 231 EVDVSYK------VHTEDGRKVTSNDDPIlATGYHPDLSFLKKGLfeLDEDGRPVL---TEETES-TNVPGLFLAG 296
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
8-313 |
1.27e-11 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 65.35 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 8 RLIILGSGPAGYSAAVYAARANLKPVVITGIQA-GGQLTTTVEVDNWPGDVEGLTgpvlMERMQQHAERFDTEIVYDHIH 86
Cdd:PRK12775 432 KVAICGSGPAGLAAAADLVKYGVDVTVYEALHVvGGVLQYGIPSFRLPRDIIDRE----VQRLVDIGVKIETNKVIGKTF 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 87 TAKlqqrpfELIGDGGTytcDALIIATGASA-QYLGLPSEetFAGKGVSA--------CATCDGFFYRN------QVVAV 151
Cdd:PRK12775 508 TVP------QLMNDKGF---DAVFLGVGAGApTFLGIPGE--FAGQVYSAnefltrvnLMGGDKFPFLDtpislgKSVVV 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 152 VGGGNTAVEEALYLSNI-AKEVHLIHRRDKLRSEKILQDklFEKAANGNIRLHWNQNLDEVLGDATG-VTGARLRDSQ-- 227
Cdd:PRK12775 577 IGAGNTAMDCLRVAKRLgAPTVRCVYRRSEAEAPARIEE--IRHAKEEGIDFFFLHSPVEIYVDAEGsVRGMKVEEMElg 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 228 ------------TGETRELALSGVFIAIGHKPNT-------DLFVNQLpmhdGYLRVKSGNEGDATATAIPGVFAAGDVA 288
Cdd:PRK12775 655 epdekgrrkpmpTGEFKDLECDTVIYALGTKANPiitqstpGLALNKW----GNIAADDGKLESTQSTNLPGVFAGGDIV 730
|
330 340
....*....|....*....|....*
gi 495222737 289 DHvYRQAVTSAGAGCMAALDAEKYL 313
Cdd:PRK12775 731 TG-GATVILAMGAGRRAARSIATYL 754
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
107-293 |
7.72e-10 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 59.41 E-value: 7.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 107 DALIIATGASAQYLGLPSEETFAGKGVSACATCDGFFYRNQV--VAVVGGGNTAVEEALYLSNIAKEVHLIHRRDKLRS- 183
Cdd:PRK13512 107 DKLILSPGASANSLGFESDITFTLRNLEDTDAIDQFIKANQVdkALVVGAGYISLEVLENLYERGLHPTLIHRSDKINKl 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 184 -EKILQDKLFEKAANGNIRLHWNQNLDEVLGDATGVTgarlrdSQTGETRELALSGVfiaiGHKPNTDLFVNQLPMHD-- 260
Cdd:PRK13512 187 mDADMNQPILDELDKREIPYRLNEEIDAINGNEVTFK------SGKVEHYDMIIEGV----GTHPNSKFIESSNIKLDdk 256
|
170 180 190
....*....|....*....|....*....|...
gi 495222737 261 GYLRVKsgnegDATATAIPGVFAAGDVADHVYR 293
Cdd:PRK13512 257 GFIPVN-----DKFETNVPNIYAIGDIITSHYR 284
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
107-306 |
2.26e-09 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 58.35 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 107 DALIIATGA-SAQYLGLPSEEtfAGKGVSACAtcdgfFYRN----------QVVAVVGGGNTAVE---EALYLSniAKEV 172
Cdd:PRK12771 224 DAVFVAIGAqLGKRLPIPGED--AAGVLDAVD-----FLRAvgegeppflgKRVVVIGGGNTAMDaarTARRLG--AEEV 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 173 HLIHRRDklRSEKILQDKLFEKAANGNIRLHWNQNLDEVLGDATGVTGARL-------RDSQ------TGETRELALSGV 239
Cdd:PRK12771 295 TIVYRRT--REDMPAHDEEIEEALREGVEINWLRTPVEIEGDENGATGLRVitvekmeLDEDgrpspvTGEEETLEADLV 372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495222737 240 FIAIGHKPNTDLF--VNQLPMHDGYLRVKSGNegdaTATAIPGVFAAGDVADHVyRQAVTSAGAGCMAA 306
Cdd:PRK12771 373 VLAIGQDIDSAGLesVPGVEVGRGVVQVDPNF----MMTGRPGVFAGGDMVPGP-RTVTTAIGHGKKAA 436
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
8-288 |
7.25e-09 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 56.29 E-value: 7.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 8 RLIILGSGPAGYSAAVYAARANLKPVVITGIQ--------------AGGQLTttvevdnwPGDVeglTGPVlmermQQHA 73
Cdd:COG1252 3 RIVIVGGGFAGLEAARRLRKKLGGDAEVTLIDpnpyhlfqpllpevAAGTLS--------PDDI---AIPL-----RELL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 74 ERFDTEIVYDHIHTAKLQQRpfELI-GDGGTYTCDALIIATGASAQYLGLPSEETFAgkgVSACATCDGFFYRNQV---- 148
Cdd:COG1252 67 RRAGVRFIQGEVTGIDPEAR--TVTlADGRTLSYDYLVIATGSVTNFFGIPGLAEHA---LPLKTLEDALALRERLlaaf 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 149 ----------VAVVGGGNTAVEEALYLSNIAKEVHLIH--RRDKLR------SEKILQD---KLFEKAAN----GNIRLH 203
Cdd:COG1252 142 eraerrrlltIVVVGGGPTGVELAGELAELLRKLLRYPgiDPDKVRitlveaGPRILPGlgeKLSEAAEKelekRGVEVH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 204 WNQNLDEVlgDATGVTgarlrdsqTGETRELALSGVFIAIGHKPNTdlFVNQLPM---HDGYLRVksgnegDAT--ATAI 278
Cdd:COG1252 222 TGTRVTEV--DADGVT--------LEDGEEIPADTVIWAAGVKAPP--LLADLGLptdRRGRVLV------DPTlqVPGH 283
|
330
....*....|
gi 495222737 279 PGVFAAGDVA 288
Cdd:COG1252 284 PNVFAIGDCA 293
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
2-178 |
7.31e-09 |
|
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: 56.41 E-value: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 2 SEAKHSRLIILGSGPAGYSAAVYAARANLKPVVI---TGIqaGG--QLTT----TVEVDNW---------PGDVEGL-TG 62
Cdd:COG2072 2 AATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLekaDDV--GGtwRDNRypglRLDTPSHlyslpffpnWSDDPDFpTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 63 PVLMERMQQHAERFDteiVYDHIH--------TAKLQQRPFEL-IGDGGTYTCDALIIATGA--SAQYLGLPSEETFAGK 131
Cdd:COG2072 80 DEILAYLEAYADKFG---LRRPIRfgtevtsaRWDEADGRWTVtTDDGETLTARFVVVATGPlsRPKIPDIPGLEDFAGE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495222737 132 GV-SAcatcdgfFYRNQV------VAVVGGGNTAVEEALYLSNIAKEVHLIHRR 178
Cdd:COG2072 157 QLhSA-------DWRNPVdlagkrVLVVGTGASAVQIAPELARVAAHVTVFQRT 203
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
107-288 |
1.16e-08 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 55.82 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 107 DALIIATGASAQylgLPSEETFAGKGVSACATC-DGFFYR-------NQVVAVVGGGNTAVEEALYLSNIAKEVHLIHRR 178
Cdd:PRK09564 105 DKLMIATGARPI---IPPIKNINLENVYTLKSMeDGLALKellkdeeIKNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 179 DKLRSEKIlqDKLFEKAANGNIR-----LHWNQNLDEVLGDaTGVTGARLrdsqtgETRELALSGVFIAIGHKPNTDLFV 253
Cdd:PRK09564 182 DRILPDSF--DKEITDVMEEELRengveLHLNEFVKSLIGE-DKVEGVVT------DKGEYEADVVIVATGVKPNTEFLE 252
|
170 180 190
....*....|....*....|....*....|....*..
gi 495222737 254 NQ-LP-MHDGYLRVKsgNEGdatATAIPGVFAAGDVA 288
Cdd:PRK09564 253 DTgLKtLKNGAIIVD--EYG---ETSIENIYAAGDCA 284
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
1-317 |
3.70e-08 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 54.73 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 1 MSEAKHSRLIILGSGPAGYSAAVYAARANLKPVVI-TGIQAGGQLTTTVEVDNWP-----GDVEGLtgpvlmERMQqhAE 74
Cdd:PRK12814 188 RAPKSGKKVAIIGAGPAGLTAAYYLLRKGHDVTIFdANEQAGGMMRYGIPRFRLPesvidADIAPL------RAMG--AE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 75 -RFDTEIVYDhIHTAKLQQRpfeligdggtytCDALIIATGAS-AQYLGLPSEE--------TFAGKGVSACATCDGffy 144
Cdd:PRK12814 260 fRFNTVFGRD-ITLEELQKE------------FDAVLLAVGAQkASKMGIPGEElpgvisgiDFLRNVALGTALHPG--- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 145 rnQVVAVVGGGNTAVE---EALYLSniAKEVHLIHRRDklRSEKILQDKLFEKAANGNIRLH-WNQNLD-EVLGDATGVT 219
Cdd:PRK12814 324 --KKVVVIGGGNTAIDaarTALRLG--AESVTILYRRT--REEMPANRAEIEEALAEGVSLReLAAPVSiERSEGGLELT 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 220 GARLRD---SQTGETRELALSG---------VFIAIGHKPNTdlfvnQLPMHDGYLRVKSG---NEGDATATAIPGVFAA 284
Cdd:PRK12814 398 AIKMQQgepDESGRRRPVPVEGseftlqadtVISAIGQQVDP-----PIAEAAGIGTSRNGtvkVDPETLQTSVAGVFAG 472
|
330 340 350
....*....|....*....|....*....|....*.
gi 495222737 285 GDV---ADhvyrQAVTSAGAGCMAALDAEKYLDDIP 317
Cdd:PRK12814 473 GDCvtgAD----IAINAVEQGKRAAHAIDLFLNGKP 504
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
4-287 |
4.04e-07 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 50.97 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 4 AKHSRLIILGSGPAGYSAAVYAARANLKPVVI-----------TG-------IQA-------------GGQLTTTVEVDn 52
Cdd:PRK06370 3 AQRYDAIVIGAGQAGPPLAARAAGLGMKVALIergllggtcvnTGcvptktlIASaraahlarraaeyGVSVGGPVSVD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 53 wpgdvegltGPVLMERMQQ--HAERFDTEIVYDHIHTAKLQQ------RPFELIGDGGTYTCDALIIATGASAQYLGLPs 124
Cdd:PRK06370 82 ---------FKAVMARKRRirARSRHGSEQWLRGLEGVDVFRgharfeSPNTVRVGGETLRAKRIFINTGARAAIPPIP- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 125 eetfagkGVSACA--TCDGFFYRNQV---VAVVGGGNTAVEEALYLSNIAKEVHLIHRRDKLRSE------KILQDKLfe 193
Cdd:PRK06370 152 -------GLDEVGylTNETIFSLDELpehLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPRededvaAAVREIL-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 194 kAANGnIRLHWNQNLDEVLGDATGVtgaRLRDSQTGETRELALSGVFIAIGHKPNTDlfvnqlpmhD------------- 260
Cdd:PRK06370 223 -EREG-IDVRLNAECIRVERDGDGI---AVGLDCNGGAPEITGSHILVAVGRVPNTD---------Dlgleaagvetdar 288
|
330 340
....*....|....*....|....*..
gi 495222737 261 GYLRVKsgnegDATATAIPGVFAAGDV 287
Cdd:PRK06370 289 GYIKVD-----DQLRTTNPGIYAAGDC 310
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
107-287 |
5.60e-07 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 50.37 E-value: 5.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 107 DALIIATGA-SAQYLGLPSEEtfaGKGVsaCATCDGFF--------YRNQV---------VAVVGGGNTAV---EEALYL 165
Cdd:PRK12770 120 DAVLIATGTwKSRKLGIPGED---LPGV--YSALEYLFriraaklgYLPWEkvppvegkkVVVVGAGLTAVdaaLEAVLL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 166 SniAKEVHLIHRRDklRSEKILQDKLFEKAANGNIRLHWNQNLDEVLGDaTGVTGARLRDSQ---------------TGE 230
Cdd:PRK12770 195 G--AEKVYLAYRRT--INEAPAGKYEIERLIARGVEFLELVTPVRIIGE-GRVEGVELAKMRlgepdesgrprpvpiPGS 269
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495222737 231 TRELALSGVFIAIGHKPNTdlfvnqlPMHDGYLRVKSGNEGDATA-----TAIPGVFAAGDV 287
Cdd:PRK12770 270 EFVLEADTVVFAIGEIPTP-------PFAKECLGIELNRKGEIVVdekhmTSREGVFAAGDV 324
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
11-313 |
6.16e-07 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 50.90 E-value: 6.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 11 ILGSGPAGYSAAVYAARANLKPVVITGI-QAGGQLT------------TTVEVDNwpgdvegltgpvlMERMQQHAErFD 77
Cdd:PRK12778 436 VIGSGPAGLSFAGDLAKRGYDVTVFEALhEIGGVLKygipefrlpkkiVDVEIEN-------------LKKLGVKFE-TD 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 78 TeIVYDHIHTAKLQQRPFeligdggtytcDALIIATGAsaqylGLPSEETFAGKGVSACATCDGFFYRNQV--------- 148
Cdd:PRK12778 502 V-IVGKTITIEELEEEGF-----------KGIFIASGA-----GLPNFMNIPGENSNGVMSSNEYLTRVNLmdaaspdsd 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 149 --------VAVVGGGNTA---VEEALYLSniAKEVHLIHRrdklRSEKILQDKL--FEKAANGNIRLHWNQNLDEVLGDA 215
Cdd:PRK12778 565 tpikfgkkVAVVGGGNTAmdsARTAKRLG--AERVTIVYR----RSEEEMPARLeeVKHAKEEGIEFLTLHNPIEYLADE 638
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 216 TG-VTGARLRDSQTGET------RELALSG---------VFIAIGHKPNTdLFVNQLPMHD----GYLRVKsgnegDATA 275
Cdd:PRK12778 639 KGwVKQVVLQKMELGEPdasgrrRPVAIPGstftvdvdlVIVSVGVSPNP-LVPSSIPGLElnrkGTIVVD-----EEMQ 712
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 495222737 276 TAIPGVFAAGDVAdhvyRQAVT---SAGAGCMAALDAEKYL 313
Cdd:PRK12778 713 SSIPGIYAGGDIV----RGGATvilAMGDGKRAAAAIDEYL 749
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
100-305 |
1.14e-06 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 49.87 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 100 DGGTYTCDALIIATGasaqylGLPSEETFAGK--GVSACATCDgFFYRNQVVAVVGGGNTAVEEALYLSNIAKEVHLIHR 177
Cdd:PLN02546 211 DGKLYTARNILIAVG------GRPFIPDIPGIehAIDSDAALD-LPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIR 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 178 RDK-LRS-EKILQDKLFEKAANGNIRLHWNQNLDEVLGDATGVtgarLRDSQTGETRElALSGVFIAIGHKPNTdlfvNQ 255
Cdd:PLN02546 284 QKKvLRGfDEEVRDFVAEQMSLRGIEFHTEESPQAIIKSADGS----LSLKTNKGTVE-GFSHVMFATGRKPNT----KN 354
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495222737 256 LPMHDgyLRVKSGNEG-----DATATAIPGVFAAGDVADHVYRQAVTSAGAGCMA 305
Cdd:PLN02546 355 LGLEE--VGVKMDKNGaievdEYSRTSVPSIWAVGDVTDRINLTPVALMEGGALA 407
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
77-291 |
6.09e-06 |
|
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: 47.66 E-value: 6.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 77 DTEIVYDHIHTAKLQQRPFELIGDGG--------TYTCDALIIATGASAQYLGLPseetfagkGVSACATCDGFFYRNQV 148
Cdd:TIGR01423 115 DTEGLTFFLGWGALEDKNVVLVRESAdpksavkeRLQAEHILLATGSWPQMLGIP--------GIEHCISSNEAFYLDEP 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 149 ---VAVVGGGNTAVEEAlYLSNIAK----EVHLIHRRDK-LRS-EKILQDKLFEK-AANG-NIRLHWNQNLDEVLGDatg 217
Cdd:TIGR01423 187 prrVLTVGGGFISVEFA-GIFNAYKprggKVTLCYRNNMiLRGfDSTLRKELTKQlRANGiNIMTNENPAKVTLNAD--- 262
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495222737 218 vtGARLRDSQTGETRELALsgVFIAIGHKPNTDLFvnQLPMHDGYLRVKSGNEGDA-TATAIPGVFAAGDVADHV 291
Cdd:TIGR01423 263 --GSKHVTFESGKTLDVDV--VMMAIGRVPRTQTL--QLDKVGVELTKKGAIQVDEfSRTNVPNIYAIGDVTDRV 331
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
9-306 |
2.12e-05 |
|
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: 46.00 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 9 LIILGSGPAGYSAAVYAARANLKPVVITGIQAGGQLT------TTVEVDNWPGDV---EGLTGPVL---------MERMQ 70
Cdd:TIGR01438 5 LIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPTPLGTrwgiggTCVNVGCIPKKLmhqAALLGQALkdsrnygwkVEETV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 71 QHAERFDTEIVYDHI------HTAKLQQRPFELI------------------GDGGTYTCDALIIATGASAQYLGLPSEE 126
Cdd:TIGR01438 85 KHDWKRLVEAVQNHIgslnwgYRVALREKKVKYEnayaefvdkhrikatnkkGKEKIYSAERFLIATGERPRYPGIPGAK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 127 TFagkgvsaCATCDGFFYRNQV---VAVVGGGNTAVEEALYLSNIAKEVHLIHRRDKLRSekilqdklFEKAANGNIRLH 203
Cdd:TIGR01438 165 EL-------CITSDDLFSLPYCpgkTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRG--------FDQDCANKVGEH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 204 WNQN----LDEVLGDATGVTGARLRDSQTG--ETRELALSGVFIAIGHKPNTDlfvnQLPMHDGYLRV-KSGNEGDAT-- 274
Cdd:TIGR01438 230 MEEHgvkfKRQFVPIKVEQIEAKVLVEFTDstNGIEEEYDTVLLAIGRDACTR----KLNLENVGVKInKKTGKIPADee 305
|
330 340 350
....*....|....*....|....*....|...
gi 495222737 275 -ATAIPGVFAAGDVADHVYRQAVTSAGAGCMAA 306
Cdd:TIGR01438 306 eQTNVPYIYAVGDILEDKPELTPVAIQAGRLLA 338
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
86-305 |
2.12e-05 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 45.96 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 86 HTAKLQQrpfeLIGDGGTYTCDALIIATGASAQYLGLPSEE--TFAGKGVSacatCDGFFYRnqvVAVVGGGNTAVEEAL 163
Cdd:PLN02507 152 NEVEVTQ----LDGTKLRYTAKHILIATGSRAQRPNIPGKElaITSDEALS----LEELPKR---AVVLGGGYIAVEFAS 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 164 YLSNIAKEVHLIHRRD-KLRSekiLQDKLFEKAA----NGNIRLHWNQNLDEVLGDATGVTgarlrdSQTGETRELALSG 238
Cdd:PLN02507 221 IWRGMGATVDLFFRKElPLRG---FDDEMRAVVArnleGRGINLHPRTNLTQLTKTEGGIK------VITDHGEEFVADV 291
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495222737 239 VFIAIGHKPNTdlfvNQLPMHDgyLRVKSGNEG-----DATATAIPGVFAAGDVADHVYRQAVTSAGAGCMA 305
Cdd:PLN02507 292 VLFATGRAPNT----KRLNLEA--VGVELDKAGavkvdEYSRTNIPSIWAIGDVTNRINLTPVALMEGTCFA 357
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
145-317 |
2.70e-05 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 45.98 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 145 RNQVVAVVGGGNTAVEEALYLSNIAKEVHLIHRRDKlrSEKILQDKLFEKAANGNIRLHWNQNLDEVLGDATG--VTGA- 221
Cdd:PRK12779 446 KGKEVFVIGGGNTAMDAARTAKRLGGNVTIVYRRTK--SEMPARVEELHHALEEGINLAVLRAPREFIGDDHThfVTHAl 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 222 -------------RLRDSQTGETRELALSGVFIAIGHKPN-------TDLFVNQLpmhdGYLRVKSGNEgdatATAIPGV 281
Cdd:PRK12779 524 ldvnelgepdksgRRSPKPTGEIERVPVDLVIMALGNTANpimkdaePGLKTNKW----GTIEVEKGSQ----RTSIKGV 595
|
170 180 190
....*....|....*....|....*....|....*.
gi 495222737 282 FAAGDVAdHVYRQAVTSAGAGCMAaldAEKYLDDIP 317
Cdd:PRK12779 596 YSGGDAA-RGGSTAIRAAGDGQAA---AKEIVGEIP 627
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
105-287 |
1.20e-04 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 43.58 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 105 TCDALIIATGASAQYLGLP----SEETFAGKGVSACATcdgffyRNQVVAVVGGGNTAVEEALYLSNIAKEVHLIHRRDK 180
Cdd:PRK07251 118 TAETIVINTGAVSNVLPIPgladSKHVYDSTGIQSLET------LPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAAST 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 181 L--RSEKILQDKLFEKAANGNIRLHWNQNLDEVLGDATGVTgarlrdsQTGETRELALSGVFIAIGHKP--------NTD 250
Cdd:PRK07251 192 IlpREEPSVAALAKQYMEEDGITFLLNAHTTEVKNDGDQVL-------VVTEDETYRFDALLYATGRKPnteplgleNTD 264
|
170 180 190
....*....|....*....|....*....|....*..
gi 495222737 251 LFVNQlpmhDGYLRVKsgnegDATATAIPGVFAAGDV 287
Cdd:PRK07251 265 IELTE----RGAIKVD-----DYCQTSVPGVFAVGDV 292
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
98-291 |
3.15e-04 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 42.25 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 98 IGDGGTYTCDALIIATGASAQYLGLPSEEtfagkGVSacatcdgfFYRNQVV----------AVVGGGNTAVEEALYLSN 167
Cdd:PRK07846 121 TGDGEEITADQVVIAAGSRPVIPPVIADS-----GVR--------YHTSDTImrlpelpeslVIVGGGFIAAEFAHVFSA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 168 IAKEVHLIHRRDK-LRSEKILQDKLFEKAANGNIRLHWNQNLDEVLGDATGVTgARLRDSQTGETRELalsgvFIAIGHK 246
Cdd:PRK07846 188 LGVRVTVVNRSGRlLRHLDDDISERFTELASKRWDVRLGRNVVGVSQDGSGVT-LRLDDGSTVEADVL-----LVATGRV 261
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495222737 247 PNTDLF---VNQLPMHDGYlRVKSGNEGdatATAIPGVFAAGDVAD-----HV 291
Cdd:PRK07846 262 PNGDLLdaaAAGVDVDEDG-RVVVDEYQ---RTSAEGVFALGDVSSpyqlkHV 310
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
100-288 |
3.55e-04 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 41.83 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 100 DGGTYTCDALIIATGASA---------QYLGLPSEETFagkgvsacATCDGFFYRNQVVAVVGGGNTAVEEALYLSNIAK 170
Cdd:PRK04965 94 QGNQWQYDKLVLATGASAfvppipgreLMLTLNSQQEY--------RAAETQLRDAQRVLVVGGGLIGTELAMDLCRAGK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 171 EVHLIHRRDKL-----------RSEKILQDKlfekaangNIRLHWNQNLDEVLGDATGVTgARLRDSQTGETRElalsgV 239
Cdd:PRK04965 166 AVTLVDNAASLlaslmppevssRLQHRLTEM--------GVHLLLKSQLQGLEKTDSGIR-ATLDSGRSIEVDA-----V 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495222737 240 FIAIGHKPNTdlfvnQLPMHDGyLRVKSGNEGDAT-ATAIPGVFAAGDVA 288
Cdd:PRK04965 232 IAAAGLRPNT-----ALARRAG-LAVNRGIVVDSYlQTSAPDIYALGDCA 275
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
9-287 |
1.77e-03 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 39.75 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 9 LIILGSGPAGYSAAVYAARANLKPVVI-TGIQAGGQLT------------TTVEVDNW--------PGDVEGLTGPVLME 67
Cdd:PRK05249 8 LVVIGSGPAGEGAAMQAAKLGKRVAVIeRYRNVGGGCThtgtipskalreAVLRLIGFnqnplyssYRVKLRITFADLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 68 RMQQ--------HAERFDTEIVyDHIH-TAK-LQQRPFELIGDGG---TYTCDALIIATGaSAQYlgLPSEETFAGKGV- 133
Cdd:PRK05249 88 RADHvinkqvevRRGQYERNRV-DLIQgRARfVDPHTVEVECPDGeveTLTADKIVIATG-SRPY--RPPDVDFDHPRIy 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 134 -SacatcDGFF---YRNQVVAVVGGGNTAVEEALYLSNIAKEVHLIHRRDKLRS----EKI--LQDKLfekaANGNIRLH 203
Cdd:PRK05249 164 dS-----DSILsldHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSflddEISdaLSYHL----RDSGVTIR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 204 WNQNLDEVLGDATGVT-----GARLR-------DSQTGETRELALSgvfiAIGHKPNtdlfvnqlpmHDGYLRVksgneg 271
Cdd:PRK05249 235 HNEEVEKVEGGDDGVIvhlksGKKIKadcllyaNGRTGNTDGLNLE----NAGLEAD----------SRGQLKV------ 294
|
330
....*....|....*..
gi 495222737 272 DAT-ATAIPGVFAAGDV 287
Cdd:PRK05249 295 NENyQTAVPHIYAVGDV 311
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
9-288 |
7.54e-03 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 37.82 E-value: 7.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 9 LIILGSGPAGYSAAVYAARANLKPVVITG------------------IQAGGQL------------TTTVEVD-----NW 53
Cdd:PRK06416 7 VIVIGAGPGGYVAAIRAAQLGLKVAIVEKeklggtclnrgcipskalLHAAERAdearhsedfgikAENVGIDfkkvqEW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 54 P-GDVEGLTGPV--LMERMQqhaerfdTEIVYDHihtAKL---QQRPFELIGDGGTYTCDALIIATGASAQylGLPSEEt 127
Cdd:PRK06416 87 KnGVVNRLTGGVegLLKKNK-------VDIIRGE---AKLvdpNTVRVMTEDGEQTYTAKNIILATGSRPR--ELPGIE- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 128 FAGKGVsacatcdgFFYRNQV--------VAVVGGGNTAVEEALYLSNIAKEVHLIHRRDKL------RSEKILQdKLFE 193
Cdd:PRK06416 154 IDGRVI--------WTSDEALnldevpksLVVIGGGYIGVEFASAYASLGAEVTIVEALPRIlpgedkEISKLAE-RALK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495222737 194 KaanGNIRLHWNQNLDEVLGDATGVTgarLRDSQTGETRELALSGVFIAIGHKPNTD-LFVNQL--PMHDGYLRVKsgne 270
Cdd:PRK06416 225 K---RGIKIKTGAKAKKVEQTDDGVT---VTLEDGGKEETLEADYVLVAVGRRPNTEnLGLEELgvKTDRGFIEVD---- 294
|
330
....*....|....*...
gi 495222737 271 gDATATAIPGVFAAGDVA 288
Cdd:PRK06416 295 -EQLRTNVPNIYAIGDIV 311
|
|
| |
