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Conserved domains on  [gi|446459564|ref|WP_000537418|]
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MULTISPECIES: thioredoxin-disulfide reductase [Enterobacteriaceae]

Protein Classification

thioredoxin-disulfide reductase( domain architecture ID 11484639)

thioredoxin-disulfide reductase is a pyridine nucleotide-disulfide oxidoreductase, whose active site is a redox-active disulfide bond

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10262 PRK10262
thioredoxin reductase; Provisional
 1-320 0e+00

thioredoxin reductase; Provisional


:

Pssm-ID: 182343 [Multi-domain]  Cd Length: 321  Bit Score: 619.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564   1 MGTTKHSKLLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNDLTGPLLMERMHEHATKFETEI 80
Cdd:PRK10262   1 MGTTKHSKLLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNDLTGPLLMERMHEHATKFETEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  81 IFDHINKVDLQNRPFRLNGDNGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVE 160
Cdd:PRK10262  81 IFDHINKVDLQNRPFRLTGDSGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 161 EALYLSNIASEVHLIHRRDGFRAEKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQNSDNIESLDVAGL 240
Cdd:PRK10262 161 EALYLSNIASEVHLIHRRDGFRAEKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQNSDNIESLDVAGL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 241 FVAIGHSPNTAIFEGQLELENGYIKVQSGIHGNATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYLDGLADA 320
Cdd:PRK10262 241 FVAIGHSPNTAIFEGQLELENGYIKVQSGIHGNATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYLDGLADA 320
 
Name Accession Description Interval E-value
PRK10262 PRK10262
thioredoxin reductase; Provisional
 1-320 0e+00

thioredoxin reductase; Provisional


Pssm-ID: 182343 [Multi-domain]  Cd Length: 321  Bit Score: 619.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564   1 MGTTKHSKLLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNDLTGPLLMERMHEHATKFETEI 80
Cdd:PRK10262   1 MGTTKHSKLLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNDLTGPLLMERMHEHATKFETEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  81 IFDHINKVDLQNRPFRLNGDNGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVE 160
Cdd:PRK10262  81 IFDHINKVDLQNRPFRLTGDSGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 161 EALYLSNIASEVHLIHRRDGFRAEKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQNSDNIESLDVAGL 240
Cdd:PRK10262 161 EALYLSNIASEVHLIHRRDGFRAEKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQNSDNIESLDVAGL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 241 FVAIGHSPNTAIFEGQLELENGYIKVQSGIHGNATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYLDGLADA 320
Cdd:PRK10262 241 FVAIGHSPNTAIFEGQLELENGYIKVQSGIHGNATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYLDGLADA 320
TRX_reduct TIGR01292
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ...
 8-314 2.68e-170

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: 474.42  E-value: 2.68e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564    8 KLLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNDLTGPLLMERMHEHATKFETEIIFDHINK 87
Cdd:TIGR01292   1 DVIIIGAGPAGLTAAIYAARANLKPLLIEGMEPGGQLTTTTEVENYPGFPEGISGPELMEKMKEQAVKFGAEIIYEEVIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564   88 VDLQNRPFRLNGDNG-EYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLS 166
Cdd:TIGR01292  81 VDKSDRPFKVYTGDGkEYTAKAVIIATGASARKLGIPGEDEFWGRGVSYCATCDGPFFKNKEVAVVGGGDSAIEEALYLT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  167 NIASEVHLIHRRDGFRAEKILIKRLMdkvENGNIILHTNRTLEEVTGDQmGVTGVRLRDTQNSDnIESLDVAGLFVAIGH 246
Cdd:TIGR01292 161 RIAKKVTLVHRRDKFRAEKILLDRLK---KNPKIEFLWNSTVEEIVGDN-KVEGVKIKNTVTGE-EEELEVDGVFIAIGH 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446459564  247 SPNTAIFEGQLEL-ENGYIKVQSGihgnaTQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYL 314
Cdd:TIGR01292 236 EPNTELLKGLLELdENGYIVTDEG-----MRTSVPGVFAAGDVRDKGYRQAVTAAGDGCIAALSAERYL 299
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
8-317 1.41e-158

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 444.95  E-value: 1.41e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564   8 KLLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNDLTGPLLMERMHEHATKFETEIIFDHINK 87
Cdd:COG0492    2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQLATTKEIENYPGFPEGISGPELAERLREQAERFGAEILLEEVTS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  88 VDLQNRPFRLNGDNG-EYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLS 166
Cdd:COG0492   82 VDKDDGPFRVTTDDGtEYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGKDVVVVGGGDSALEEALYLT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 167 NIASEVHLIHRRDGFRAEKILIKRLMdkvENGNIILHTNRTLEEVTGDQmGVTGVRLRDTQnSDNIESLDVAGLFVAIGH 246
Cdd:COG0492  162 KFASKVTLIHRRDELRASKILVERLR---ANPKIEVLWNTEVTEIEGDG-RVEGVTLKNVK-TGEEKELEVDGVFVAIGL 236

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446459564 247 SPNTAIFEGQ-LEL-ENGYIKVqsgihGNATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYLDGL 317
Cdd:COG0492  237 KPNTELLKGLgLELdEDGYIVV-----DEDMETSVPGVFAAGDVRDYKYRQAATAAGEGAIAALSAARYLEPL 304
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 8-303 1.02e-59

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: 193.30  E-value: 1.02e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564    8 KLLILGSGPAGYTAAVYAARANLQPVLIT--GMEKGGQLTTTTEVENWPGDPNDL-TGPLLMERMHEHATKFETEIIF-- 82
Cdd:pfam07992   2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEdeGTCPYGGCVLSKALLGAAEAPEIAsLWADLYKRKEEVVKKLNNGIEVll 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564   83 -DHINKVDLQNRPFRLN----GDNGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRN--QKVAVIGGG 155
Cdd:pfam07992  82 gTEVVSIDPGAKKVVLEelvdGDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLlpKRVVVVGGG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  156 NTAVEEALYLSNIASEVHLIHRRD--GFRAEKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRlrdtqnsDNIE 233
Cdd:pfam07992 162 YIGVELAAALAKLGKEVTLIEALDrlLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVIL-------KDGT 234

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446459564  234 SLDVAGLFVAIGHSPNTAIFE-GQLEL-ENGYIKVQSGIhgnatQTSIPGVFAAGDVMDHIYRQAITSAGTG 303
Cdd:pfam07992 235 EIDADLVVVAIGRRPNTELLEaAGLELdERGGIVVDEYL-----RTSVPGIYAAGDCRVGGPELAQNAVAQG 301
 
Name Accession Description Interval E-value
PRK10262 PRK10262
thioredoxin reductase; Provisional
 1-320 0e+00

thioredoxin reductase; Provisional


Pssm-ID: 182343 [Multi-domain]  Cd Length: 321  Bit Score: 619.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564   1 MGTTKHSKLLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNDLTGPLLMERMHEHATKFETEI 80
Cdd:PRK10262   1 MGTTKHSKLLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNDLTGPLLMERMHEHATKFETEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  81 IFDHINKVDLQNRPFRLNGDNGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVE 160
Cdd:PRK10262  81 IFDHINKVDLQNRPFRLTGDSGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 161 EALYLSNIASEVHLIHRRDGFRAEKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQNSDNIESLDVAGL 240
Cdd:PRK10262 161 EALYLSNIASEVHLIHRRDGFRAEKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQNSDNIESLDVAGL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 241 FVAIGHSPNTAIFEGQLELENGYIKVQSGIHGNATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYLDGLADA 320
Cdd:PRK10262 241 FVAIGHSPNTAIFEGQLELENGYIKVQSGIHGNATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYLDGLADA 320
TRX_reduct TIGR01292
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ...
 8-314 2.68e-170

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: 474.42  E-value: 2.68e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564    8 KLLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNDLTGPLLMERMHEHATKFETEIIFDHINK 87
Cdd:TIGR01292   1 DVIIIGAGPAGLTAAIYAARANLKPLLIEGMEPGGQLTTTTEVENYPGFPEGISGPELMEKMKEQAVKFGAEIIYEEVIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564   88 VDLQNRPFRLNGDNG-EYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLS 166
Cdd:TIGR01292  81 VDKSDRPFKVYTGDGkEYTAKAVIIATGASARKLGIPGEDEFWGRGVSYCATCDGPFFKNKEVAVVGGGDSAIEEALYLT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  167 NIASEVHLIHRRDGFRAEKILIKRLMdkvENGNIILHTNRTLEEVTGDQmGVTGVRLRDTQNSDnIESLDVAGLFVAIGH 246
Cdd:TIGR01292 161 RIAKKVTLVHRRDKFRAEKILLDRLK---KNPKIEFLWNSTVEEIVGDN-KVEGVKIKNTVTGE-EEELEVDGVFIAIGH 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446459564  247 SPNTAIFEGQLEL-ENGYIKVQSGihgnaTQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYL 314
Cdd:TIGR01292 236 EPNTELLKGLLELdENGYIVTDEG-----MRTSVPGVFAAGDVRDKGYRQAVTAAGDGCIAALSAERYL 299
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
8-317 1.41e-158

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 444.95  E-value: 1.41e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564   8 KLLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNDLTGPLLMERMHEHATKFETEIIFDHINK 87
Cdd:COG0492    2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQLATTKEIENYPGFPEGISGPELAERLREQAERFGAEILLEEVTS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  88 VDLQNRPFRLNGDNG-EYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLS 166
Cdd:COG0492   82 VDKDDGPFRVTTDDGtEYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGKDVVVVGGGDSALEEALYLT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 167 NIASEVHLIHRRDGFRAEKILIKRLMdkvENGNIILHTNRTLEEVTGDQmGVTGVRLRDTQnSDNIESLDVAGLFVAIGH 246
Cdd:COG0492  162 KFASKVTLIHRRDELRASKILVERLR---ANPKIEVLWNTEVTEIEGDG-RVEGVTLKNVK-TGEEKELEVDGVFVAIGL 236

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446459564 247 SPNTAIFEGQ-LEL-ENGYIKVqsgihGNATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYLDGL 317
Cdd:COG0492  237 KPNTELLKGLgLELdEDGYIVV-----DEDMETSVPGVFAAGDVRDYKYRQAATAAGEGAIAALSAARYLEPL 304
AhpF_homolog TIGR03143
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase ...
 9-317 4.70e-68

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: 221.96  E-value: 4.70e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564    9 LLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNdLTGPLLMERMHEHATKFETEIIFDHINKV 88
Cdd:TIGR03143   7 LIIIGGGPAGLSAGIYAGRAKLDTLIIEKDDFGGQITITSEVVNYPGILN-TTGPELMQEMRQQAQDFGVKFLQAEVLDV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564   89 DLQNRPFRLNGDNGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNI 168
Cdd:TIGR03143  86 DFDGDIKTIKTARGDYKTLAVLIATGASPRKLGFPGEEEFTGRGVAYCATCDGEFFTGMDVFVIGGGFAAAEEAVFLTRY 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  169 ASEVHLIHRRDGFRAEKILIKRLMDkveNGNIILHTNRTLEEVTGDQM--------GVTGVRLRDTQNSDNieslDVAGL 240
Cdd:TIGR03143 166 ASKVTVIVREPDFTCAKLIAEKVKN---HPKIEVKFNTELKEATGDDGlryakfvnNVTGEITEYKAPKDA----GTFGV 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446459564  241 FVAIGHSPNTAIFEGQLEL-ENGYIkvqsgIHGNATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYLDGL 317
Cdd:TIGR03143 239 FVFVGYAPSSELFKGVVELdKRGYI-----PTNEDMETNVPGVYAAGDLRPKELRQVVTAVADGAIAATSAERYVKEL 311
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 10-314 4.14e-65

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 213.48  E-value: 4.14e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  10 LILGSGPAGYTAAVYAARANLQpvliTGM--EK-GGQLTTTTEVENWPGDPnDLTGPLLMERMHEHATKFETEIIfDHI- 85
Cdd:PRK15317 215 LVVGGGPAGAAAAIYAARKGIR----TGIvaERfGGQVLDTMGIENFISVP-ETEGPKLAAALEEHVKEYDVDIM-NLQr 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  86 -NKVDLQNRPFRLNGDNGE-YTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEAL 163
Cdd:PRK15317 289 aSKLEPAAGLIEVELANGAvLKAKTVILATGARWRNMNVPGEDEYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAI 368

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 164 YLSNIASEVHLIHRRDGFRAEKILIKRLMDKvenGNIILHTNRTLEEVTGDQMGVTGVRLRDtQNSDNIESLDVAGLFVA 243
Cdd:PRK15317 369 DLAGIVKHVTVLEFAPELKADQVLQDKLRSL---PNVTIITNAQTTEVTGDGDKVTGLTYKD-RTTGEEHHLELEGVFVQ 444

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446459564 244 IGHSPNTAIFEGQLELEN-GYIKVQSgiHGnatQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYL 314
Cdd:PRK15317 445 IGLVPNTEWLKGTVELNRrGEIIVDA--RG---ATSVPGVFAAGDCTTVPYKQIIIAMGEGAKAALSAFDYL 511
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 8-303 1.02e-59

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: 193.30  E-value: 1.02e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564    8 KLLILGSGPAGYTAAVYAARANLQPVLIT--GMEKGGQLTTTTEVENWPGDPNDL-TGPLLMERMHEHATKFETEIIF-- 82
Cdd:pfam07992   2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEdeGTCPYGGCVLSKALLGAAEAPEIAsLWADLYKRKEEVVKKLNNGIEVll 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564   83 -DHINKVDLQNRPFRLN----GDNGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRN--QKVAVIGGG 155
Cdd:pfam07992  82 gTEVVSIDPGAKKVVLEelvdGDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLlpKRVVVVGGG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  156 NTAVEEALYLSNIASEVHLIHRRD--GFRAEKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRlrdtqnsDNIE 233
Cdd:pfam07992 162 YIGVELAAALAKLGKEVTLIEALDrlLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVIL-------KDGT 234

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446459564  234 SLDVAGLFVAIGHSPNTAIFE-GQLEL-ENGYIKVQSGIhgnatQTSIPGVFAAGDVMDHIYRQAITSAGTG 303
Cdd:pfam07992 235 EIDADLVVVAIGRRPNTELLEaAGLELdERGGIVVDEYL-----RTSVPGIYAAGDCRVGGPELAQNAVAQG 301
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 4-288 3.40e-23

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: 99.01  E-value: 3.40e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564   4 TKHSKLLILGSGPAGYTAAVYAARANLQPVLItgmEK---GG------------------QLTTTTEVEN--WPGDPNDL 60
Cdd:COG1249    1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALV---EKgrlGGtclnvgcipskallhaaeVAHEARHAAEfgISAGAPSV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  61 TGPLLMERMHEHATKFeTEIIFDHI--NKVDLqnrpfrLNG------------DNGE-YTCDALIIATGASARYLglPSE 125
Cdd:COG1249   78 DWAALMARKDKVVDRL-RGGVEELLkkNGVDV------IRGrarfvdphtvevTGGEtLTADHIVIATGSRPRVP--PIP 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 126 EAFKGRGVsacaTCDGFFYRNQ---KVAVIGGGNTAVEEALYLSNIASEVHLIHRRDGF--RAEKILIKRLMDKVENGNI 200
Cdd:COG1249  149 GLDEVRVL----TSDEALELEElpkSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLlpGEDPEISEALEKALEKEGI 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 201 ILHTNRTLEEVTGDQMGVTgVRLRDtqnSDNIESLDVAGLFVAIGHSPNTAifegQLELEN--------GYIKVqsgihg 272
Cdd:COG1249  225 DILTGAKVTSVEKTGDGVT-VTLED---GGGEEAVEADKVLVATGRRPNTD----GLGLEAagvelderGGIKV------ 290

                        330
                 ....*....|....*..
gi 446459564 273 NAT-QTSIPGVFAAGDV 288
Cdd:COG1249  291 DEYlRTSVPGIYAIGDV 307
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 65-294 2.16e-22

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: 95.26  E-value: 2.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  65 LMERMHEHATKFETEIIFDH-INKVDLQNRPFRLNgDNGEYTCDALIIATGASARYL---GLPSEEAFKGRGVSACATCD 140
Cdd:COG0446   38 LLVRTPESFERKGIDVRTGTeVTAIDPEAKTVTLR-DGETLSYDKLVLATGARPRPPpipGLDLPGVFTLRTLDDADALR 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 141 GFFYRN--QKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDGF--RAEKILIKRLMDKVENGNIILHTNRTLEEVTGDqm 216
Cdd:COG0446  117 EALKEFkgKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLlgVLDPEMAALLEEELREHGVELRLGETVVAIDGD-- 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 217 GVTGVRLRDTqnsdniESLDVAGLFVAIGHSPNTAIFEG-QLEL-ENGYIKVqsgihgNAT-QTSIPGVFAAGDVMDHIY 293
Cdd:COG0446  195 DKVAVTLTDG------EEIPADLVVVAPGVRPNTELAKDaGLALgERGWIKV------DETlQTSDPDVYAAGDCAEVPH 262


                 .
gi 446459564 294 R 294
Cdd:COG0446  263 P 263
PRK06116 PRK06116
glutathione reductase; Validated
 101-292 1.05e-20

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 91.76  E-value: 1.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 101 NGE-YTCDALIIATGASARYLGLPseeafkgrGVSACATCDGFFYRN---QKVAVIGGGNTAVEEALYLSNIASEVHLIH 176
Cdd:PRK06116 126 NGErYTADHILIATGGRPSIPDIP--------GAEYGITSDGFFALEelpKRVAVVGAGYIAVEFAGVLNGLGSETHLFV 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 177 RRD----GFraEKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRLrdtqnsDNIESLDVAGLFVAIGHSPNTAi 252
Cdd:PRK06116 198 RGDaplrGF--DPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADGSLTLTL------EDGETLTVDCLIWAIGREPNTD- 268

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 446459564 253 fegQLELEN--------GYIKVQsgihgNATQTSIPGVFAAGDVMDHI 292
Cdd:PRK06116 269 ---GLGLENagvklnekGYIIVD-----EYQNTNVPGIYAVGDVTGRV 308
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 9-288 3.63e-20

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 90.62  E-value: 3.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564   9 LLILGSGPAGYTAAVYAARANLQPVLItgmEKGgQLTTT-------------------TEVENWP-----GDPNDLTGPL 64
Cdd:PRK06292   6 VIVIGAGPAGYVAARRAAKLGKKVALI---EKG-PLGGTclnvgcipskaliaaaeafHEAKHAEefgihADGPKIDFKK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  65 LMERMHEHATKFETEII--FDHINKVDL---------QNRpfrLNGDNGEYTCDALIIATGAsaRYLGLPSEEAFKGRGV 133
Cdd:PRK06292  82 VMARVRRERDRFVGGVVegLEKKPKIDKikgtarfvdPNT---VEVNGERIEAKNIVIATGS--RVPPIPGVWLILGDRL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 134 sacATCDGFFYRN---QKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDGF----------RAEKILIKRlmdkvengnI 200
Cdd:PRK06292 157 ---LTSDDAFELDklpKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRIlpledpevskQAQKILSKE---------F 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 201 ILHTNRTLEEVTGDQmgvtGVRLRDTQNSDNIESLDVAGLFVAIGHSPNTAIF---EGQLEL-ENGYIKVqsgihGNATQ 276
Cdd:PRK06292 225 KIKLGAKVTSVEKSG----DEKVEELEKGGKTETIEADYVLVATGRRPNTDGLgleNTGIELdERGRPVV-----DEHTQ 295

                        330
                 ....*....|..
gi 446459564 277 TSIPGVFAAGDV 288
Cdd:PRK06292 296 TSVPGIYAAGDV 307
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 8-288 1.61e-19

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: 88.27  E-value: 1.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564   8 KLLILGSGPAGYTAAVYAARANLQPVLITGMEK-GGQLT------------TTTEVEnwpgdpndltgplLMERMhehAT 74
Cdd:COG0493  123 KVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKpGGLLRygipefrlpkdvLDREIE-------------LIEAL---GV 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  75 KFETEIIFD-HINKVDLQNrpfrlngdngEYtcDALIIATGAS-ARYLGLPSEEAfKG--------RGVSACATCDGFFY 144
Cdd:COG0493  187 EFRTNVEVGkDITLDELLE----------EF--DAVFLATGAGkPRDLGIPGEDL-KGvhsamdflTAVNLGEAPDTILA 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 145 RNQKVAVIGGGNTAVE---EALYLSniASEVHLIHRRDgfRAE-KILIKRLMDKVENGnIILHTNRTLEEVTGDQMG-VT 219
Cdd:COG0493  254 VGKRVVVIGGGNTAMDcarTALRLG--AESVTIVYRRT--REEmPASKEEVEEALEEG-VEFLFLVAPVEIIGDENGrVT 328

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 220 GVRLRDTQNSDNIES-----LDVAG---------LFVAIGHSPNTAIFEGQLELE---NGYIKVqsgiHGNATQTSIPGV 282
Cdd:COG0493  329 GLECVRMELGEPDESgrrrpVPIEGseftlpadlVILAIGQTPDPSGLEEELGLEldkRGTIVV----DEETYQTSLPGV 404


                 ....*.
gi 446459564 283 FAAGDV 288
Cdd:COG0493  405 FAGGDA 410
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
6-288 6.92e-18

NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 83.27  E-value: 6.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564   6 HSKLLILGSGPAGYTAA-VYAARANLQPVLITGMEKGG-----QLttttevenwpgdPNDLTGPLLMERMHEHATKFETE 79
Cdd:COG1251    1 KMRIVIIGAGMAGVRAAeELRKLDPDGEITVIGAEPHPpynrpPL------------SKVLAGETDEEDLLLRPADFYEE 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  80 -----IIFDHINKVDLQNRPFRLnGDNGEYTCDALIIATGASARYLGLPSEEAfkgRGVsacatcdgFFYRN-------- 146
Cdd:COG1251   69 ngidlRLGTRVTAIDRAARTVTL-ADGETLPYDKLVLATGSRPRVPPIPGADL---PGV--------FTLRTlddadalr 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 147 ------QKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDgfraekilikRLMDKV--------------ENGnIILHTNR 206
Cdd:COG1251  137 aalapgKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAP----------RLLPRQldeeagallqrlleALG-VEVRLGT 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 207 TLEEVTGDQmGVTGVRLRDTqnsdniESLDVAGLFVAIGHSPNTAIFEG-QLELENGyIKVqsgihgNAT-QTSIPGVFA 284
Cdd:COG1251  206 GVTEIEGDD-RVTGVRLADG------EELPADLVVVAIGVRPNTELARAaGLAVDRG-IVV------DDYlRTSDPDIYA 271


                 ....
gi 446459564 285 AGDV 288
Cdd:COG1251  272 AGDC 275
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 107-320 9.53e-18

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 83.30  E-value: 9.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 107 DALIIATGASA-RYLGLPSEEAfkgRGV-SAC--------ATCDGFFYRNQKVAVIGGGNTA---VEEALYLSniASEVH 173
Cdd:PRK11749 227 DAVFIGTGAGLpRFLGIPGENL---GGVySAVdfltrvnqAVADYDLPVGKRVVVIGGGNTAmdaARTAKRLG--AESVT 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 174 LIHRRDgfRAEKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQNSDNIES-------------LDVAGL 240
Cdd:PRK11749 302 IVYRRG--REEMPASEEEVEHAKEEGVEFEWLAAPVEILGDEGRVTGVEFVRMELGEPDASgrrrvpiegseftLPADLV 379

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 241 FVAIGHSPNTAIFEGQLELE---NGYIKVqsgihGNAT-QTSIPGVFAAGDVMdhiyRQA---ITSAGTGCMAALDAERY 313
Cdd:PRK11749 380 IKAIGQTPNPLILSTTPGLElnrWGTIIA-----DDETgRTSLPGVFAGGDIV----TGAatvVWAVGDGKDAAEAIHEY 450


                 ....*..
gi 446459564 314 LDGLADA 320
Cdd:PRK11749 451 LEGAASA 457
Pyr_redox_3 pfam13738
Pyridine nucleotide-disulphide oxidoreductase;
16-286 4.22e-17

Pyridine nucleotide-disulphide oxidoreductase;


Pssm-ID: 404603 [Multi-domain]  Cd Length: 296  Bit Score: 79.96  E-value: 4.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564   16 PAGYTAAVYAARANLQPVLItgMEKG------------GQLTTTTEVENWPGDP------NDLTGPLLMERMH------- 70
Cdd:pfam13738   1 PAGIGCAIALKKAGLEDYLI--LEKGnignsfyrypthMTFFSPSFTSNGFGIPdlnaisPGTSPAFTFNREHpsgneya 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564   71 ----EHATKFETEII-FDHINKVDLQNRPFRLNGDNGEYTCDALIIATG--ASARYLGLPsEEAFKGRGVSACATcdgff 143
Cdd:pfam13738  79 eylrRVADHFELPINlFEEVTSVKKEDDGFVVTTSKGTYQARYVIIATGefDFPNKLGVP-ELPKHYSYVKDFHP----- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  144 YRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDGFRAE----KILIK-----RLMDKVENGNIILHTNRTLEEVTGD 214
Cdd:pfam13738 153 YAGQKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDRdsdpSYSLSpdtlnRLEELVKNGKIKAHFNAEVKEITEV 232

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446459564  215 QMGVtgvrlrdTQNSDNIESLDVAGLFV-AIGHSPNTAIFEGQL--ELENGYIKVQSgihgnATQ-TSIPGVFAAG 286
Cdd:pfam13738 233 DVSY-------KVHTEDGRKVTSNDDPIlATGYHPDLSFLKKGLfeLDEDGRPVLTE-----ETEsTNVPGLFLAG 296
PRK12831 PRK12831
putative oxidoreductase; Provisional
 5-316 2.74e-16

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 78.91  E-value: 2.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564   5 KHSKLLILGSGPAGYTAAVYAARANLQPVLITGM-EKGGQLT-------------TTTEVENwpgdpndltgpllmerMH 70
Cdd:PRK12831 139 KGKKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALhEPGGVLVygipefrlpketvVKKEIEN----------------IK 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  71 EHATKFETEIIFDHINKVD--LQNRPFrlngdngeytcDALIIATGASA-RYLGLPSEEAfkgRGV-SAC---------- 136
Cdd:PRK12831 203 KLGVKIETNVVVGKTVTIDelLEEEGF-----------DAVFIGSGAGLpKFMGIPGENL---NGVfSANefltrvnlmk 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 137 ATCDGF---FYRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRrdgfRAEKILIKRLMD---KVENGnIILH--TNRTl 208
Cdd:PRK12831 269 AYKPEYdtpIKVGKKVAVVGGGNVAMDAARTALRLGAEVHIVYR----RSEEELPARVEEvhhAKEEG-VIFDllTNPV- 342

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 209 eEVTGDQMG-VTGVRL----------------RDTQNSDNIesLDVAGLFVAIGHSPNTAIFEGQLELE---NGYIKVQS 268
Cdd:PRK12831 343 -EILGDENGwVKGMKCikmelgepdasgrrrpVEIEGSEFV--LEVDTVIMSLGTSPNPLISSTTKGLKinkRGCIVADE 419

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446459564 269 gihgNATQTSIPGVFAAGDvmdhiyrqAITSAGT-------GCMAALDAERYLDG 316
Cdd:PRK12831 420 ----ETGLTSKEGVFAGGD--------AVTGAATvilamgaGKKAAKAIDEYLSK 462
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 148-226 6.15e-16

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 71.47  E-value: 6.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  148 KVAVIGGGNTAVEEALYLSNIASEVHLIHRRDGFRA--EKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVtGVRLRD 225
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPgfDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGV-VVVLTD 79


                  .
gi 446459564  226 T 226
Cdd:pfam00070  80 G 80
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
8-288 9.44e-16

NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 77.09  E-value: 9.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564   8 KLLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVenwPG------DPNDLTGPLLmermhEHATKFETEII 81
Cdd:COG1252    3 RIVIVGGGFAGLEAARRLRKKLGGDAEVTLIDPNPYHLFQPLL---PEvaagtlSPDDIAIPLR-----ELLRRAGVRFI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  82 FDHINKVDLQNRpfRLNGDNG-EYTCDALIIATGASARYLGLPSEEAFkgrGVSACATCDGFFYRNQ------------- 147
Cdd:COG1252   75 QGEVTGIDPEAR--TVTLADGrTLSYDYLVIATGSVTNFFGIPGLAEH---ALPLKTLEDALALRERllaaferaerrrl 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 148 -KVAVIGGGNTAVEEALYLSNIASEVHLIHRRDGFRAEKILI---------------KRLMDKVENGNIILHTNRTLEEV 211
Cdd:COG1252  150 lTIVVVGGGPTGVELAGELAELLRKLLRYPGIDPDKVRITLVeagprilpglgeklsEAAEKELEKRGVEVHTGTRVTEV 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 212 TGDqmgvtGVRLRDTqnsdniESLDVAGLFVAIGHSPNTAIFEGQLEL-ENGYIKVqsgihgNATQTSI--PGVFAAGDV 288
Cdd:COG1252  230 DAD-----GVTLEDG------EEIPADTVIWAAGVKAPPLLADLGLPTdRRGRVLV------DPTLQVPghPNVFAIGDC 292
PRK07251 PRK07251
FAD-containing oxidoreductase;
100-288 1.49e-13

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 70.93  E-value: 1.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 100 DNGEYTCDALIIATGASARYLGLP----SEEAFKGRGVSACATcdgffyRNQKVAVIGGGNTAVEEALYLSNIASEVHLI 175
Cdd:PRK07251 113 EKIELTAETIVINTGAVSNVLPIPgladSKHVYDSTGIQSLET------LPERLGIIGGGNIGLEFAGLYNKLGSKVTVL 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 176 HRRDGF--RAEKILIKRLMDKVENGNIILHTNRTLEEVT--GDQMGVTgvrlrdtqNSDNIESLDVagLFVAIGHSPNTA 251
Cdd:PRK07251 187 DAASTIlpREEPSVAALAKQYMEEDGITFLLNAHTTEVKndGDQVLVV--------TEDETYRFDA--LLYATGRKPNTE 256

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446459564 252 ifegQLELENGYIKV--QSGIHGNAT-QTSIPGVFAAGDV 288
Cdd:PRK07251 257 ----PLGLENTDIELteRGAIKVDDYcQTSVPGVFAVGDV 292
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
 107-291 1.01e-12

nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 68.70  E-value: 1.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  107 DALIIATGASARYLGLPSEE---AFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDGFRA 183
Cdd:TIGR02374  98 DKLILATGSYPFILPIPGADkkgVYVFRTIEDLDAIMAMAQRFKKAAVIGGGLLGLEAAVGLQNLGMDVSVIHHAPGLMA 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  184 EKI---LIKRLMDKVENGNIILHTNRTLEEVTGDQMgVTGVRLRDTqnsdniESLDVAGLFVAIGHSPNTaifegQLELE 260
Cdd:TIGR02374 178 KQLdqtAGRLLQRELEQKGLTFLLEKDTVEIVGATK-ADRIRFKDG------SSLEADLIVMAAGIRPND-----ELAVS 245

                         170       180       190
                  ....*....|....*....|....*....|..
gi 446459564  261 NGyIKVQSGIHGN-ATQTSIPGVFAAGDVMDH 291
Cdd:TIGR02374 246 AG-IKVNRGIIVNdSMQTSDPDIYAVGECAEH 276
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
 103-294 1.49e-12

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 67.89  E-value: 1.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 103 EYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQ--KVAVIGGGNTAVEEALYLSNIASEVHLIHRRDG 180
Cdd:PRK13512 103 EESYDKLILSPGASANSLGFESDITFTLRNLEDTDAIDQFIKANQvdKALVVGAGYISLEVLENLYERGLHPTLIHRSDK 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 181 FRA--EKILIKRLMDKVENGNIILHTNRTLEEVTGDQMgvtgvrlrdTQNSDNIESLDVagLFVAIGHSPNTAIFEG-QL 257
Cdd:PRK13512 183 INKlmDADMNQPILDELDKREIPYRLNEEIDAINGNEV---------TFKSGKVEHYDM--IIEGVGTHPNSKFIESsNI 251

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446459564 258 ELEN-GYIKVQSGIhgnatQTSIPGVFAAGDVMDHIYR 294
Cdd:PRK13512 252 KLDDkGFIPVNDKF-----ETNVPNIYAIGDIITSHYR 284
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 8-287 2.39e-12

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 66.99  E-value: 2.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564   8 KLLILGSGPAGYTAAVYAARanLQPVL-ITGMEKggqltttTEVENWPG------------DPNdltgpLLMERMHEHAT 74
Cdd:PRK09564   2 KIIIIGGTAAGMSAAAKAKR--LNKELeITVYEK-------TDIVSFGAcglpyfvggffdDPN-----TMIARTPEEFI 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  75 KFETEIIFDH-INKVDLQNRPFRL----NGDNGEYTCDALIIATGASARylgLPSEEAFKGRGVSACATC-DGFFYR--- 145
Cdd:PRK09564  68 KSGIDVKTEHeVVKVDAKNKTITVknlkTGSIFNDTYDKLMIATGARPI---IPPIKNINLENVYTLKSMeDGLALKell 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 146 ----NQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRD-----GFRAE--KILIKRLMDKvengNIILHTNRTLEEVTGD 214
Cdd:PRK09564 145 kdeeIKNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDrilpdSFDKEitDVMEEELREN----GVELHLNEFVKSLIGE 220

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446459564 215 QmGVTGVRlrdtQNSDNIESlDVagLFVAIGHSPNTAIFEGQ-LE-LENGYIKV-QSGihgnatQTSIPGVFAAGD 287
Cdd:PRK09564 221 D-KVEGVV----TDKGEYEA-DV--VIVATGVKPNTEFLEDTgLKtLKNGAIIVdEYG------ETSIENIYAAGD 282
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
 8-316 8.76e-12

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 65.01  E-value: 8.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564   8 KLLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTttteVENWPGD----PNDLTGpllMERMHEHATKFETEiifd 83
Cdd:PRK12770  20 KVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLM----LFGIPEFripiERVREG---VKELEEAGVVFHTR---- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  84 hiNKVDLQNRPFRLNGDN------------GEYtcDALIIATGA-SARYLGLPSEEAfkgRGVsacatCDG--FFYR--- 145
Cdd:PRK12770  89 --TKVCCGEPLHEEEGDEfverivsleelvKKY--DAVLIATGTwKSRKLGIPGEDL---PGV-----YSAleYLFRira 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 146 ---------------NQKVAVIGGGNTAV---EEALYLSniASEVHLIHRRDgfRAEKILIKRLMDKVENGNIILHTNRT 207
Cdd:PRK12770 157 aklgylpwekvppveGKKVVVVGAGLTAVdaaLEAVLLG--AEKVYLAYRRT--INEAPAGKYEIERLIARGVEFLELVT 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 208 LEEVTGDQmGVTGVRLRDTQNSDNIES--------------LDVAGLFVAIGHSPNTAIFEGQLELEN---GYIKVQsgi 270
Cdd:PRK12770 233 PVRIIGEG-RVEGVELAKMRLGEPDESgrprpvpipgsefvLEADTVVFAIGEIPTPPFAKECLGIELnrkGEIVVD--- 308

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 446459564 271 hgNATQTSIPGVFAAGDVMdHIYRQAITSAGTGCMAALDAERYLDG 316
Cdd:PRK12770 309 --EKHMTSREGVFAAGDVV-TGPSKIGKAIKSGLRAAQSIHEWLDL 351
PRK12775 PRK12775
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ...
 8-289 4.73e-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: 63.81  E-value: 4.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564    8 KLLILGSGPAGYTAAVYAARANLQPVLITGMEK-GGQLTTTTEVENWPGDPNDLTgpllMERMHEHATKFETEIIFDHIN 86
Cdd:PRK12775  432 KVAICGSGPAGLAAAADLVKYGVDVTVYEALHVvGGVLQYGIPSFRLPRDIIDRE----VQRLVDIGVKIETNKVIGKTF 507

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564   87 KVDlqnrpfRLNGDNGeytCDALIIATGASA-RYLGLPSEeaFKGRGVSA--------CATCDGFFYRN------QKVAV 151
Cdd:PRK12775  508 TVP------QLMNDKG---FDAVFLGVGAGApTFLGIPGE--FAGQVYSAnefltrvnLMGGDKFPFLDtpislgKSVVV 576

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  152 IGGGNTAVEEALYLSNI-ASEVHLIHRRDGFRAEKiLIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRL------- 223
Cdd:PRK12775  577 IGAGNTAMDCLRVAKRLgAPTVRCVYRRSEAEAPA-RIEEIRHAKEEGIDFFFLHSPVEIYVDAEGSVRGMKVeemelge 655

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446459564  224 ------RDTQNSDNIESLDVAGLFVAIGHSPNTAIFEGQ--LELEN-GYIKVQSGIHGNATQTSIPGVFAAGDVM 289
Cdd:PRK12775  656 pdekgrRKPMPTGEFKDLECDTVIYALGTKANPIITQSTpgLALNKwGNIAADDGKLESTQSTNLPGVFAGGDIV 730
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 3-178 2.07e-10

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: 61.03  E-value: 2.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564   3 TTKHSKLLILGSGPAGYTAAVYAARANLQPVLItgmEKGGQL----------TTTTEVENW----PGDPNDLTGPLLMER 68
Cdd:COG2072    3 ATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVL---EKADDVggtwrdnrypGLRLDTPSHlyslPFFPNWSDDPDFPTG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  69 ------MHEHATKFEteiIFDHI---NKV-----DLQNRPFRLNGDNGE-YTCDALIIATGA--SARYLGLPSEEAFKGR 131
Cdd:COG2072   80 deilayLEAYADKFG---LRRPIrfgTEVtsarwDEADGRWTVTTDDGEtLTARFVVVATGPlsRPKIPDIPGLEDFAGE 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 446459564 132 GVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRR 178
Cdd:COG2072  157 QLHSADWRNPVDLAGKRVLVVGTGASAVQIAPELARVAAHVTVFQRT 203
PLN02507 PLN02507
glutathione reductase
 86-292 6.71e-10

glutathione reductase


Pssm-ID: 215281 [Multi-domain]  Cd Length: 499  Bit Score: 59.83  E-value: 6.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  86 NKVDLQnrpfRLNGDNGEYTCDALIIATGASARYLGLPSEEAfkgrgvsACATCDGFFYRN--QKVAVIGGGNTAVEEAL 163
Cdd:PLN02507 152 NEVEVT----QLDGTKLRYTAKHILIATGSRAQRPNIPGKEL-------AITSDEALSLEElpKRAVVLGGGYIAVEFAS 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 164 YLSNIASEVHLIHRRD----GFRAE-KILIKRlmdKVENGNIILH--TNRTLEEVTGDQMGVTgvrlrdtqnSDNIESLD 236
Cdd:PLN02507 221 IWRGMGATVDLFFRKElplrGFDDEmRAVVAR---NLEGRGINLHprTNLTQLTKTEGGIKVI---------TDHGEEFV 288

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 237 VAGLFVAIGHSPNTA---IFEGQLELEN-GYIKVQsgihgNATQTSIPGVFAAGDVMDHI 292
Cdd:PLN02507 289 ADVVLFATGRAPNTKrlnLEAVGVELDKaGAVKVD-----EYSRTNIPSIWAIGDVTNRI 343
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 9-288 9.13e-10

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 59.39  E-value: 9.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564   9 LLILGSGPAGYTAAVYAARANLQPVLITGMEKGGqltttTEVeNWPGDPndlTGPLLM--ERMHE--HATKFETEIIFDH 84
Cdd:PRK06416   7 VIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLGG-----TCL-NRGCIP---SKALLHaaERADEarHSEDFGIKAENVG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  85 I--------------------------NKVDLQNRPFRLNGDN----------GEYTCDALIIATGASARylGLPSEEaF 128
Cdd:PRK06416  78 IdfkkvqewkngvvnrltggvegllkkNKVDIIRGEAKLVDPNtvrvmtedgeQTYTAKNIILATGSRPR--ELPGIE-I 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 129 KGRGVsacatcdgFFYRN--------QKVAVIGGGNTAVEEALYLSNIASEVHLIHRRD----GFRAE--KILIKRLmdk 194
Cdd:PRK06416 155 DGRVI--------WTSDEalnldevpKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPrilpGEDKEisKLAERAL--- 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 195 vENGNIILHTNRTLEEVTGDQMGVTgVRLRDTQNsdnIESLDVAGLFVAIGHSPNTAI--FEGQ-LELENGYIKVQSGIH 271
Cdd:PRK06416 224 -KKRGIKIKTGAKAKKVEQTDDGVT-VTLEDGGK---EETLEADYVLVAVGRRPNTENlgLEELgVKTDRGFIEVDEQLR 298

                        330
                 ....*....|....*..
gi 446459564 272 gnatqTSIPGVFAAGDV 288
Cdd:PRK06416 299 -----TNVPNIYAIGDI 310
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 100-316 1.52e-09

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 58.73  E-value: 1.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 100 DNGEYtcDALIIATGA-SARYLGLPSEEAfkGRGVSACAtcdgfFYRN----------QKVAVIGGGNTAVE---EALYL 165
Cdd:PRK12771 219 LEGEF--DAVFVAIGAqLGKRLPIPGEDA--AGVLDAVD-----FLRAvgegeppflgKRVVVIGGGNTAMDaarTARRL 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 166 SniASEVHLIHRRD-----GFRAEkilikrLMDKVENGnIILHTNRTLEEVTGDQMGVTGVRL------------RDTQN 228
Cdd:PRK12771 290 G--AEEVTIVYRRTredmpAHDEE------IEEALREG-VEINWLRTPVEIEGDENGATGLRVitvekmeldedgRPSPV 360

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 229 SDNIESLDVAGLFVAIGHSPNTAIFEG--QLELENGYIKVQSgihgNATQTSIPGVFAAGDVMDHIyRQAITSAGTGCMA 306
Cdd:PRK12771 361 TGEEETLEADLVVLAIGQDIDSAGLESvpGVEVGRGVVQVDP----NFMMTGRPGVFAGGDMVPGP-RTVTTAIGHGKKA 435

                        250
                 ....*....|
gi 446459564 307 ALDAERYLDG 316
Cdd:PRK12771 436 ARNIDAFLGG 445
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 8-314 3.08e-09

bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 58.21  E-value: 3.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564   8 KLLILGSGPAGYTAAvyaaranlqpvliTGMEKGGQLTTTTEVENWPGD-----------PNDLTGPLLmERMHEHATKF 76
Cdd:PRK12778 433 KVAVIGSGPAGLSFA-------------GDLAKRGYDVTVFEALHEIGGvlkygipefrlPKKIVDVEI-ENLKKLGVKF 498

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  77 ETEIIFDHINKVDlqnrpfrlngDNGEYTCDALIIATGAsarylGLPSEEAFKGRGVSACATCDGFFYR----------- 145
Cdd:PRK12778 499 ETDVIVGKTITIE----------ELEEEGFKGIFIASGA-----GLPNFMNIPGENSNGVMSSNEYLTRvnlmdaaspds 563

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 146 ------NQKVAVIGGGNTAVEEALYLSNIASE-VHLIHRrdgfRAEKILIKRLMD----KVENGNIILHTNRTleEVTGD 214
Cdd:PRK12778 564 dtpikfGKKVAVVGGGNTAMDSARTAKRLGAErVTIVYR----RSEEEMPARLEEvkhaKEEGIEFLTLHNPI--EYLAD 637

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 215 QMG-VTGVRL--------------RDTQNSDNIESLDVAGLFVAIGHSPNTAIFEGQLELE---NGYIKVQsgihgNATQ 276
Cdd:PRK12778 638 EKGwVKQVVLqkmelgepdasgrrRPVAIPGSTFTVDVDLVIVSVGVSPNPLVPSSIPGLElnrKGTIVVD-----EEMQ 712

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 446459564 277 TSIPGVFAAGDvmdhIYRQA---ITSAGTGCMAALDAERYL 314
Cdd:PRK12778 713 SSIPGIYAGGD----IVRGGatvILAMGDGKRAAAAIDEYL 749
PRK06370 PRK06370
FAD-containing oxidoreductase;
150-288 1.28e-08

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 55.98  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 150 AVIGGGNTAVEEALYLSNIASEVHLIHRRDGfraekiLIKR--------LMDKVENGNIILHTNRTLEEVTGDQmgvTGV 221
Cdd:PRK06370 175 VIIGGGYIGLEFAQMFRRFGSEVTVIERGPR------LLPRededvaaaVREILEREGIDVRLNAECIRVERDG---DGI 245

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446459564 222 RLRDTQNSDNIEsLDVAGLFVAIGHSPNTaifEGqLELE--------NGYIKVQSGIhgnatQTSIPGVFAAGDV 288
Cdd:PRK06370 246 AVGLDCNGGAPE-ITGSHILVAVGRVPNT---DD-LGLEaagvetdaRGYIKVDDQL-----RTTNPGIYAAGDC 310
PRK12779 PRK12779
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ...
 145-307 2.19e-08

putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional


Pssm-ID: 183740 [Multi-domain]  Cd Length: 944  Bit Score: 55.61  E-value: 2.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 145 RNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDgfRAE-KILIKRLMDKVENGnIILHTNRTLEEVTGDQMG--VTGV 221
Cdd:PRK12779 446 KGKEVFVIGGGNTAMDAARTAKRLGGNVTIVYRRT--KSEmPARVEELHHALEEG-INLAVLRAPREFIGDDHThfVTHA 522

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 222 RL-------------RDTQNSDNIESLDVAGLFVAIGHSPNTAIFEGQLELEN---GYIKVQSGihgnATQTSIPGVFAA 285
Cdd:PRK12779 523 LLdvnelgepdksgrRSPKPTGEIERVPVDLVIMALGNTANPIMKDAEPGLKTnkwGTIEVEKG----SQRTSIKGVYSG 598

                        170       180
                 ....*....|....*....|....*
gi 446459564 286 GDVMdhiyR---QAITSAGTGCMAA 307
Cdd:PRK12779 599 GDAA----RggsTAIRAAGDGQAAA 619
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
 8-316 4.93e-08

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 54.35  E-value: 4.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564   8 KLLILGSGPAGYTAAVYAAR---------ANLQPvliTGMEKGG--QLTTTTEVENwpgdpNDLTGPLLMERMHEHATKF 76
Cdd:PRK12814 195 KVAIIGAGPAGLTAAYYLLRkghdvtifdANEQA---GGMMRYGipRFRLPESVID-----ADIAPLRAMGAEFRFNTVF 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  77 ETEIIFDHINKvdlqnrpfrlngdngEYtcDALIIATGAS-ARYLGLPSEE--------AFKGRGVSACATCDGffyrnQ 147
Cdd:PRK12814 267 GRDITLEELQK---------------EF--DAVLLAVGAQkASKMGIPGEElpgvisgiDFLRNVALGTALHPG-----K 324

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 148 KVAVIGGGNTAVE---EALYLSniASEVHLIHRR------------DGFRAEKILIKRL-----MDKVENGNIIlhTNRT 207
Cdd:PRK12814 325 KVVVIGGGNTAIDaarTALRLG--AESVTILYRRtreempanraeiEEALAEGVSLRELaapvsIERSEGGLEL--TAIK 400

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 208 LEEVTGDQMGvtgvRLRDTQNSDNIESLDVAGLFVAIGHSPNTAIFE--GQLELENGYIKVqsgiHGNATQTSIPGVFAA 285
Cdd:PRK12814 401 MQQGEPDESG----RRRPVPVEGSEFTLQADTVISAIGQQVDPPIAEaaGIGTSRNGTVKV----DPETLQTSVAGVFAG 472

                        330       340       350
                 ....*....|....*....|....*....|....
gi 446459564 286 GDVM---DhiyrQAITSAGTGCMAALDAERYLDG 316
Cdd:PRK12814 473 GDCVtgaD----IAINAVEQGKRAAHAIDLFLNG 502
TGR TIGR01438
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ...
 98-290 1.99e-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: 1.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564   98 NGDNGEYTCDALIIATGASARYLGLPSEEAFkgrgvsaCATCDGFF---YRNQKVAVIGGGNTAVEEALYLSNIASEVHL 174
Cdd:TIGR01438 136 KGKEKIYSAERFLIATGERPRYPGIPGAKEL-------CITSDDLFslpYCPGKTLVVGASYVALECAGFLAGIGLDVTV 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  175 IHRRDGFRA-EKILIKRLMDKVENGNIILHTNRTLEEVTgdQMGVTgvRLRDTQNSDNIESLDVAGLFVAIGHSPNTAif 253
Cdd:TIGR01438 209 MVRSILLRGfDQDCANKVGEHMEEHGVKFKRQFVPIKVE--QIEAK--VLVEFTDSTNGIEEEYDTVLLAIGRDACTR-- 282

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 446459564  254 egQLELENGYIKV--QSG--IHGNATQTSIPGVFAAGDVMD 290
Cdd:TIGR01438 283 --KLNLENVGVKInkKTGkiPADEEEQTNVPYIYAVGDILE 321
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
9-288 2.03e-07

Si-specific NAD(P)(+) transhydrogenase;


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 52.08  E-value: 2.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564   9 LLILGSGPAGYTAAVYAARANLQPVLItgmEKGGQL--------T--------TTTEVENW--------PGDPNDLTGPL 64
Cdd:PRK05249   8 LVVIGSGPAGEGAAMQAAKLGKRVAVI---ERYRNVgggcthtgTipskalreAVLRLIGFnqnplyssYRVKLRITFAD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  65 LMERMHeHATKFETEII---FDHiNKVDL---------QNRpFRLNGDNGE---YTCDALIIATGAS-ARylglPSEEAF 128
Cdd:PRK05249  85 LLARAD-HVINKQVEVRrgqYER-NRVDLiqgrarfvdPHT-VEVECPDGEvetLTADKIVIATGSRpYR----PPDVDF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 129 KGRGV--SacatcDGFF---YRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRD---GFrAEKILIKRLMDKVENGNI 200
Cdd:PRK05249 158 DHPRIydS-----DSILsldHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDrllSF-LDDEISDALSYHLRDSGV 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 201 ILHTNRTLEEVTGDQMGVTgVRLRDTQNsdnIESlDVagLFVAIGHSPNTAifegQLELEN--------GYIKVqsgihg 272
Cdd:PRK05249 232 TIRHNEEVEKVEGGDDGVI-VHLKSGKK---IKA-DC--LLYANGRTGNTD----GLNLENagleadsrGQLKV------ 294

                        330
                 ....*....|....*..
gi 446459564 273 NAT-QTSIPGVFAAGDV 288
Cdd:PRK05249 295 NENyQTAVPHIYAVGDV 311
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
 107-292 2.56e-07

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: 51.90  E-value: 2.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  107 DALIIATGASARYLGLPseeafkgrGVSACATCDGFFYRNQ---KVAVIGGGNTAVEEALYLSN---IASEVHLIHRRD- 179
Cdd:TIGR01423 153 EHILLATGSWPQMLGIP--------GIEHCISSNEAFYLDEpprRVLTVGGGFISVEFAGIFNAykpRGGKVTLCYRNNm 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  180 ---GFRAEkiLIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQnsdnieSLDVAGLFVAIGHSPNTaifeGQ 256
Cdd:TIGR01423 225 ilrGFDST--LRKELTKQLRANGINIMTNENPAKVTLNADGSKHVTFESGK------TLDVDVVMMAIGRVPRT----QT 292

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 446459564  257 LELENGYIKV--QSGIHGNA-TQTSIPGVFAAGDVMDHI 292
Cdd:TIGR01423 293 LQLDKVGVELtkKGAIQVDEfSRTNVPNIYAIGDVTDRV 331
PRK13748 PRK13748
putative mercuric reductase; Provisional
 96-309 3.00e-07

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 51.69  E-value: 3.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  96 RLN-GDNGEYTCDALIIATGASARYLGLP---------SEEAFKGRGVSacatcdgffyrnQKVAVIGGGNTAVEEALYL 165
Cdd:PRK13748 222 RLNdGGERVVAFDRCLIATGASPAVPPIPglketpywtSTEALVSDTIP------------ERLAVIGSSVVALELAQAF 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 166 SNIASEVHLIHRR---------------DGFRAEKIlikRLMDKVE-------NGNIILHTNRTleEVTGDQmgvtgvrl 223
Cdd:PRK13748 290 ARLGSKVTILARStlffredpaigeavtAAFRAEGI---EVLEHTQasqvahvDGEFVLTTGHG--ELRADK-------- 356

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 224 rdtqnsdniesldvagLFVAIGHSPNTAifegQLELENGYIKVQSG---IHGNATQTSIPGVFAAGDVMDH---IYRQAI 297
Cdd:PRK13748 357 ----------------LLVATGRAPNTR----SLALDAAGVTVNAQgaiVIDQGMRTSVPHIYAAGDCTDQpqfVYVAAA 416

                        250
                 ....*....|....*..
gi 446459564 298 --TSAG---TGCMAALD 309
Cdd:PRK13748 417 agTRAAinmTGGDAALD 433
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 11-287 5.97e-07

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 50.55  E-value: 5.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  11 ILGSGPAGYTAAVYAARANLQPVLItgmEK----GGQLTTttevenwpGDPNDLTGPLLMER----MHEHATKFET--EI 80
Cdd:PRK12810 148 VVGSGPAGLAAADQLARAGHKVTVF---ERadriGGLLRY--------GIPDFKLEKEVIDRrielMEAEGIEFRTnvEV 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  81 IFDhINKVDLQNrpfrlngdngEYtcDALIIATGAS-ARYLGLPSEEAfkgRGV--------SACATCDGFFY------R 145
Cdd:PRK12810 217 GKD-ITAEELLA----------EY--DAVFLGTGAYkPRDLGIPGRDL---DGVhfamdfliQNTRRVLGDETepfisaK 280

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 146 NQKVAVIGGGNTA---VEEALYLSniASEVHlihRRD-----GFRAEKILI---KRLMDKVENG---NIILHTNRTLEEV 211
Cdd:PRK12810 281 GKHVVVIGGGDTGmdcVGTAIRQG--AKSVT---QRDimpmpPSRRNKNNPwpyWPMKLEVSNAheeGVEREFNVQTKEF 355

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 212 TGDQMGVTGVRLRDTQ----------NSDNIESLDVAglFVAIG--HSPNTAIFEGQLEL-ENGYIKVQSGIHgnatQTS 278
Cdd:PRK12810 356 EGENGKVTGVKVVRTElgegdfepveGSEFVLPADLV--LLAMGftGPEAGLLAQFGVELdERGRVAAPDNAY----QTS 429


                 ....*....
gi 446459564 279 IPGVFAAGD 287
Cdd:PRK12810 430 NPKVFAAGD 438
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
 100-288 6.26e-07

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 50.69  E-value: 6.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 100 DNGEYTCDALIIATGASARYL-GLPseeaFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRR 178
Cdd:PRK06327 140 DETVITAKHVIIATGSEPRHLpGVP----FDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEAL 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 179 DGF--RAEKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTgvrLRDTQNSDNIESLDVAGLFVAIGHSPNTAIFEGQ 256
Cdd:PRK06327 216 PAFlaAADEQVAKEAAKAFTKQGLDIHLGVKIGEIKTGGKGVS---VAYTDADGEAQTLEVDKLIVSIGRVPNTDGLGLE 292

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446459564 257 ---LEL-ENGYIKVQSGIHgnatqTSIPGVFAAGDV 288
Cdd:PRK06327 293 avgLKLdERGFIPVDDHCR-----TNVPNVYAIGDV 323
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
100-287 9.33e-07

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 49.92  E-value: 9.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 100 DNGEYTCDALIIATGASA---------RYLGLPSEEAFkgrgvsacATCDGFFYRNQKVAVIGGGNTAVEEALYLSNIAS 170
Cdd:PRK04965  94 QGNQWQYDKLVLATGASAfvppipgreLMLTLNSQQEY--------RAAETQLRDAQRVLVVGGGLIGTELAMDLCRAGK 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 171 EVHLIHRRDGFRAEKI-------LIKRLMDKvengNIILHTNRTLEEVTgdqmgVTGVRLRDTQNSDniESLDVAGLFVA 243
Cdd:PRK04965 166 AVTLVDNAASLLASLMppevssrLQHRLTEM----GVHLLLKSQLQGLE-----KTDSGIRATLDSG--RSIEVDAVIAA 234

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446459564 244 IGHSPNTaifegQLELENGyIKVQSGIHGNAT-QTSIPGVFAAGD 287
Cdd:PRK04965 235 AGLRPNT-----ALARRAG-LAVNRGIVVDSYlQTSAPDIYALGD 273
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
146-248 1.15e-06

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 49.86  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 146 NQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRD--GFRAEKI------------LIKRLMDKVE-NGNIILHTNRTLEE 210
Cdd:COG1148  140 NKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPelGGRAAQLhktfpgldcpqcILEPLIAEVEaNPNITVYTGAEVEE 219

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446459564 211 VTGDQmgvtG---VRLRdtQNSDNIESLDVAGLFVAIGHSP 248
Cdd:COG1148  220 VSGYV----GnftVTIK--KGPREEIEIEVGAIVLATGFKP 254
PLN02546 PLN02546
glutathione reductase
 145-292 1.27e-05

glutathione reductase


Pssm-ID: 215301 [Multi-domain]  Cd Length: 558  Bit Score: 46.79  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 145 RNQKVAVIGGGNTAVEEALYLSNIASEVHLIHR------------RDgFRAEKILIKrlmdkvengNIILHTNRTLEEVT 212
Cdd:PLN02546 251 KPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRqkkvlrgfdeevRD-FVAEQMSLR---------GIEFHTEESPQAII 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 213 GDQMGVTGVRlrdtQNSDNIESLdvAGLFVAIGHSPNTAifegQLELE--------NGYIKVQSgihgnATQTSIPGVFA 284
Cdd:PLN02546 321 KSADGSLSLK----TNKGTVEGF--SHVMFATGRKPNTK----NLGLEevgvkmdkNGAIEVDE-----YSRTSVPSIWA 385


                 ....*...
gi 446459564 285 AGDVMDHI 292
Cdd:PLN02546 386 VGDVTDRI 393
PTZ00058 PTZ00058
glutathione reductase; Provisional
 131-297 3.29e-05

glutathione reductase; Provisional


Pssm-ID: 185420 [Multi-domain]  Cd Length: 561  Bit Score: 45.38  E-value: 3.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 131 RGVSACATCDGFFY--RNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDGF--RAEKILIKRLMDKVENGNIILHTNR 206
Cdd:PTZ00058 220 KGKEFTISSDDFFKikEAKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLlrKFDETIINELENDMKKNNINIITHA 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 207 TLEEVTGDQMGVTGVRLRDTQNSDNIESldvagLFVAIGHSPNTAIF--EGQLEL-ENGYIKVQsgihgNATQTSIPGVF 283
Cdd:PTZ00058 300 NVEEIEKVKEKNLTIYLSDGRKYEHFDY-----VIYCVGRSPNTEDLnlKALNIKtPKGYIKVD-----DNQRTSVKHIY 369

                        170
                 ....*....|....
gi 446459564 284 AAGDVMDHIYRQAI 297
Cdd:PTZ00058 370 AVGDCCMVKKNQEI 383
PRK07846 PRK07846
mycothione reductase; Reviewed
 99-288 6.09e-04

mycothione reductase; Reviewed


Pssm-ID: 181142 [Multi-domain]  Cd Length: 451  Bit Score: 41.09  E-value: 6.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  99 GDNGEYTCDALIIATGASARYLGLPSEEafkgrGVSacatcdgfFYRN----------QKVAVIGGGNTAVEEALYLSNI 168
Cdd:PRK07846 122 GDGEEITADQVVIAAGSRPVIPPVIADS-----GVR--------YHTSdtimrlpelpESLVIVGGGFIAAEFAHVFSAL 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 169 ASEVHLIHRRDG-FRAEKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTgVRLrdtqnsDNIESLDVAGLFVAIGHS 247
Cdd:PRK07846 189 GVRVTVVNRSGRlLRHLDDDISERFTELASKRWDVRLGRNVVGVSQDGSGVT-LRL------DDGSTVEADVLLVATGRV 261

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446459564 248 PNTAIFE---GQLEL-ENGYIKVQSgiHGnatQTSIPGVFAAGDV 288
Cdd:PRK07846 262 PNGDLLDaaaAGVDVdEDGRVVVDE--YQ---RTSAEGVFALGDV 301
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
 98-288 1.98e-03

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 39.52  E-value: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564  98 NGDNGEYtcDALIIATGASARYLGLPS---EEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNIASEVHL 174
Cdd:PRK09754  95 NGESWHW--DQLFIATGAAARPLPLLDalgERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELAASATQRRCKVTV 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446459564 175 IHRRD---GFRAEKILIKRLMDKVENGNIILHTNRTLEEVtgdqmgVTGVRLRDTQNSDNIESLDVagLFVAIGHSpnta 251
Cdd:PRK09754 173 IELAAtvmGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHV------VDGEKVELTLQSGETLQADV--VIYGIGIS---- 240

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446459564 252 iFEGQLELENGYIKVQSGIHGNATQTSIPGVFAAGDV 288
Cdd:PRK09754 241 -ANDQLAREANLDTANGIVIDEACRTCDPAIFAGGDV 276
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 9-45 2.95e-03

FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 39.13  E-value: 2.95e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 446459564    9 LLILGSGPAGYTAAVYAARANLQPVLItgmEK----GGQLT 45
Cdd:pfam12831   2 VVVVGGGPAGVAAAIAAARAGAKVLLV---ERrgflGGMLT 39
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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