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Conserved domains on  [gi|42567414|ref|NP_195271|]
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NADPH-dependent thioredoxin reductase B [Arabidopsis thaliana]

Protein Classification

thioredoxin-disulfide reductase( domain architecture ID 11492183)

thioredoxin-disulfide reductase catalyzes the NADPH-dependent reduction of the redox protein thioredoxin

CATH:  3.50.50.60
EC:  1.8.1.9
Gene Ontology:  GO:0004791|GO:0071949|GO:0019430|GO:0045454|GO:0004791
PubMed:  11012661|10657232
SCOP:  4000117

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TRX_reduct TIGR01292
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ...
 55-364 2.01e-144

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: 411.25  E-value: 2.01e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414    55 IVGSGPAAHTAAIYAARAELKPLLFEGWMandiaPGGQLTTTTDVENFPGFPEGILGVELTDKFRKQSERFGTTIFTETV 134
Cdd:TIGR01292   4 IIGAGPAGLTAAIYAARANLKPLLIEGME-----PGGQLTTTTEVENYPGFPEGISGPELMEKMKEQAVKFGAEIIYEEV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414   135 TKVDFSSKPFKLFT-DSKAILADAVILATGAVAKRLSFVGSGEasggFWNRGISACAVCDGaaPIFRNKPLAVIGGGDSA 213
Cdd:TIGR01292  79 IKVDKSDRPFKVYTgDGKEYTAKAVIIATGASARKLGIPGEDE----FWGRGVSYCATCDG--PFFKNKEVAVVGGGDSA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414   214 MEEANFLTKYGSKVYIIHRRDAFRASKIMQQRALSNPKIDVIWNSSVVEAYGDGerdVLGGLKVKNVVTGDVSDLKVSGL 293
Cdd:TIGR01292 153 IEEALYLTRIAKKVTLVHRRDKFRAEKILLDRLKKNPKIEFLWNSTVEEIVGDN---KVEGVKIKNTVTGEEEELEVDGV 229

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42567414   294 FFAIGHEPATKFLDGGVELDSDGYVVTKPGtTQTSVPGVFAAGDVQDKKYRQAITAAGTGCMAALDAEHYL 364
Cdd:TIGR01292 230 FIAIGHEPNTELLKGLLELDENGYIVTDEG-MRTSVPGVFAAGDVRDKGYRQAVTAAGDGCIAALSAERYL 299
 
Name Accession Description Interval E-value
TRX_reduct TIGR01292
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ...
 55-364 2.01e-144

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: 411.25  E-value: 2.01e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414    55 IVGSGPAAHTAAIYAARAELKPLLFEGWMandiaPGGQLTTTTDVENFPGFPEGILGVELTDKFRKQSERFGTTIFTETV 134
Cdd:TIGR01292   4 IIGAGPAGLTAAIYAARANLKPLLIEGME-----PGGQLTTTTEVENYPGFPEGISGPELMEKMKEQAVKFGAEIIYEEV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414   135 TKVDFSSKPFKLFT-DSKAILADAVILATGAVAKRLSFVGSGEasggFWNRGISACAVCDGaaPIFRNKPLAVIGGGDSA 213
Cdd:TIGR01292  79 IKVDKSDRPFKVYTgDGKEYTAKAVIIATGASARKLGIPGEDE----FWGRGVSYCATCDG--PFFKNKEVAVVGGGDSA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414   214 MEEANFLTKYGSKVYIIHRRDAFRASKIMQQRALSNPKIDVIWNSSVVEAYGDGerdVLGGLKVKNVVTGDVSDLKVSGL 293
Cdd:TIGR01292 153 IEEALYLTRIAKKVTLVHRRDKFRAEKILLDRLKKNPKIEFLWNSTVEEIVGDN---KVEGVKIKNTVTGEEEELEVDGV 229

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42567414   294 FFAIGHEPATKFLDGGVELDSDGYVVTKPGtTQTSVPGVFAAGDVQDKKYRQAITAAGTGCMAALDAEHYL 364
Cdd:TIGR01292 230 FIAIGHEPNTELLKGLLELDENGYIVTDEG-MRTSVPGVFAAGDVRDKGYRQAVTAAGDGCIAALSAERYL 299
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
51-367 2.81e-138

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 395.64  E-value: 2.81e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  51 TRLCIVGSGPAAHTAAIYAARAELKPLLFEGwmandIAPGGQLTTTTDVENFPGFPEGILGVELTDKFRKQSERFGTTIF 130
Cdd:COG0492   1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEG-----GEPGGQLATTKEIENYPGFPEGISGPELAERLREQAERFGAEIL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414 131 TETVTKVDFSSKPFKLFTDS-KAILADAVILATGAVAKRLSFVGSGEasggFWNRGISACAVCDGAApiFRNKPLAVIGG 209
Cdd:COG0492  76 LEEVTSVDKDDGPFRVTTDDgTEYEAKAVIIATGAGPRKLGLPGEEE----FEGRGVSYCATCDGFF--FRGKDVVVVGG 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414 210 GDSAMEEANFLTKYGSKVYIIHRRDAFRASKIMQQRALSNPKIDVIWNSSVVEAYGDgerDVLGGLKVKNVVTGDVSDLK 289
Cdd:COG0492 150 GDSALEEALYLTKFASKVTLIHRRDELRASKILVERLRANPKIEVLWNTEVTEIEGD---GRVEGVTLKNVKTGEEKELE 226

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42567414 290 VSGLFFAIGHEPATKFLDG-GVELDSDGYVVTKPgTTQTSVPGVFAAGDVQDKKYRQAITAAGTGCMAALDAEHYLQEI 367
Cdd:COG0492 227 VDGVFVAIGLKPNTELLKGlGLELDEDGYIVVDE-DMETSVPGVFAAGDVRDYKYRQAATAAGEGAIAALSAARYLEPL 304
PRK10262 PRK10262
thioredoxin reductase; Provisional
 48-370 6.38e-80

thioredoxin reductase; Provisional


Pssm-ID: 182343 [Multi-domain]  Cd Length: 321  Bit Score: 247.67  E-value: 6.38e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414   48 THNTRLCIVGSGPAAHTAAIYAARAELKPLLFEGwmandIAPGGQLTTTTDVENFPGFPEGILGVELTDKFRKQSERFGT 127
Cdd:PRK10262   4 TKHSKLLILGSGPAGYTAAVYAARANLQPVLITG-----MEKGGQLTTTTEVENWPGDPNDLTGPLLMERMHEHATKFET 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  128 TIFTETVTKVDFSSKPFKLFTDSKAILADAVILATGAVAKRLSfVGSGEAsggFWNRGISACAVCDGAapIFRNKPLAVI 207
Cdd:PRK10262  79 EIIFDHINKVDLQNRPFRLTGDSGEYTCDALIIATGASARYLG-LPSEEA---FKGRGVSACATCDGF--FYRNQKVAVI 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  208 GGGDSAMEEANFLTKYGSKVYIIHRRDAFRASKIMQQRAL---SNPKIDVIWNSSVVEAYGDgeRDVLGGLKVKNVVTGD 284
Cdd:PRK10262 153 GGGNTAVEEALYLSNIASEVHLIHRRDGFRAEKILIKRLMdkvENGNIILHTNRTLEEVTGD--QMGVTGVRLRDTQNSD 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  285 -VSDLKVSGLFFAIGHEPATKFLDGGVELDsDGYVVTKPG----TTQTSVPGVFAAGDVQDKKYRQAITAAGTGCMAALD 359
Cdd:PRK10262 231 nIESLDVAGLFVAIGHSPNTAIFEGQLELE-NGYIKVQSGihgnATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALD 309

                        330
                 ....*....|.
gi 42567414  360 AEHYLQEIGSQ 370
Cdd:PRK10262 310 AERYLDGLADA 320
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 51-353 3.09e-44

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: 154.78  E-value: 3.09e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414    51 TRLCIVGSGPAAHTAAIYAARAELKPLLFEgwmANDIAPGGQLTTTTDVENFPGFPEGIL-GVELTDKFRKQSERFGTTI 129
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIE---DEGTCPYGGCVLSKALLGAAEAPEIASlWADLYKRKEEVVKKLNNGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414   130 FT---ETVTKVDFSSKPFKLFTDS----KAILADAVILATGAVAKRLSFvgSGEASGGFwnRGISACAVCDGAAPIFRNK 202
Cdd:pfam07992  78 EVllgTEVVSIDPGAKKVVLEELVdgdgETITYDRLVIATGARPRLPPI--PGVELNVG--FLVRTLDSAEALRLKLLPK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414   203 PLAVIGGGDSAMEEANFLTKYGSKVYIIHRRDAF------RASKIMqQRALSNPKIDVIWNSSVVEAYGDGErdvlgGLK 276
Cdd:pfam07992 154 RVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLlrafdeEISAAL-EKALEKNGVEVRLGTSVKEIIGDGD-----GVE 227

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42567414   277 vknVVTGDVSDLKVSGLFFAIGHEPATKFLD-GGVELDSDGYVVTKPgTTQTSVPGVFAAGDVQDKKYRQAITAAGTG 353
Cdd:pfam07992 228 ---VILKDGTEIDADLVVVAIGRRPNTELLEaAGLELDERGGIVVDE-YLRTSVPGIYAAGDCRVGGPELAQNAVAQG 301
 
Name Accession Description Interval E-value
TRX_reduct TIGR01292
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ...
 55-364 2.01e-144

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: 411.25  E-value: 2.01e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414    55 IVGSGPAAHTAAIYAARAELKPLLFEGWMandiaPGGQLTTTTDVENFPGFPEGILGVELTDKFRKQSERFGTTIFTETV 134
Cdd:TIGR01292   4 IIGAGPAGLTAAIYAARANLKPLLIEGME-----PGGQLTTTTEVENYPGFPEGISGPELMEKMKEQAVKFGAEIIYEEV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414   135 TKVDFSSKPFKLFT-DSKAILADAVILATGAVAKRLSFVGSGEasggFWNRGISACAVCDGaaPIFRNKPLAVIGGGDSA 213
Cdd:TIGR01292  79 IKVDKSDRPFKVYTgDGKEYTAKAVIIATGASARKLGIPGEDE----FWGRGVSYCATCDG--PFFKNKEVAVVGGGDSA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414   214 MEEANFLTKYGSKVYIIHRRDAFRASKIMQQRALSNPKIDVIWNSSVVEAYGDGerdVLGGLKVKNVVTGDVSDLKVSGL 293
Cdd:TIGR01292 153 IEEALYLTRIAKKVTLVHRRDKFRAEKILLDRLKKNPKIEFLWNSTVEEIVGDN---KVEGVKIKNTVTGEEEELEVDGV 229

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42567414   294 FFAIGHEPATKFLDGGVELDSDGYVVTKPGtTQTSVPGVFAAGDVQDKKYRQAITAAGTGCMAALDAEHYL 364
Cdd:TIGR01292 230 FIAIGHEPNTELLKGLLELDENGYIVTDEG-MRTSVPGVFAAGDVRDKGYRQAVTAAGDGCIAALSAERYL 299
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
51-367 2.81e-138

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 395.64  E-value: 2.81e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  51 TRLCIVGSGPAAHTAAIYAARAELKPLLFEGwmandIAPGGQLTTTTDVENFPGFPEGILGVELTDKFRKQSERFGTTIF 130
Cdd:COG0492   1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEG-----GEPGGQLATTKEIENYPGFPEGISGPELAERLREQAERFGAEIL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414 131 TETVTKVDFSSKPFKLFTDS-KAILADAVILATGAVAKRLSFVGSGEasggFWNRGISACAVCDGAApiFRNKPLAVIGG 209
Cdd:COG0492  76 LEEVTSVDKDDGPFRVTTDDgTEYEAKAVIIATGAGPRKLGLPGEEE----FEGRGVSYCATCDGFF--FRGKDVVVVGG 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414 210 GDSAMEEANFLTKYGSKVYIIHRRDAFRASKIMQQRALSNPKIDVIWNSSVVEAYGDgerDVLGGLKVKNVVTGDVSDLK 289
Cdd:COG0492 150 GDSALEEALYLTKFASKVTLIHRRDELRASKILVERLRANPKIEVLWNTEVTEIEGD---GRVEGVTLKNVKTGEEKELE 226

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42567414 290 VSGLFFAIGHEPATKFLDG-GVELDSDGYVVTKPgTTQTSVPGVFAAGDVQDKKYRQAITAAGTGCMAALDAEHYLQEI 367
Cdd:COG0492 227 VDGVFVAIGLKPNTELLKGlGLELDEDGYIVVDE-DMETSVPGVFAAGDVRDYKYRQAATAAGEGAIAALSAARYLEPL 304
PRK10262 PRK10262
thioredoxin reductase; Provisional
 48-370 6.38e-80

thioredoxin reductase; Provisional


Pssm-ID: 182343 [Multi-domain]  Cd Length: 321  Bit Score: 247.67  E-value: 6.38e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414   48 THNTRLCIVGSGPAAHTAAIYAARAELKPLLFEGwmandIAPGGQLTTTTDVENFPGFPEGILGVELTDKFRKQSERFGT 127
Cdd:PRK10262   4 TKHSKLLILGSGPAGYTAAVYAARANLQPVLITG-----MEKGGQLTTTTEVENWPGDPNDLTGPLLMERMHEHATKFET 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  128 TIFTETVTKVDFSSKPFKLFTDSKAILADAVILATGAVAKRLSfVGSGEAsggFWNRGISACAVCDGAapIFRNKPLAVI 207
Cdd:PRK10262  79 EIIFDHINKVDLQNRPFRLTGDSGEYTCDALIIATGASARYLG-LPSEEA---FKGRGVSACATCDGF--FYRNQKVAVI 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  208 GGGDSAMEEANFLTKYGSKVYIIHRRDAFRASKIMQQRAL---SNPKIDVIWNSSVVEAYGDgeRDVLGGLKVKNVVTGD 284
Cdd:PRK10262 153 GGGNTAVEEALYLSNIASEVHLIHRRDGFRAEKILIKRLMdkvENGNIILHTNRTLEEVTGD--QMGVTGVRLRDTQNSD 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  285 -VSDLKVSGLFFAIGHEPATKFLDGGVELDsDGYVVTKPG----TTQTSVPGVFAAGDVQDKKYRQAITAAGTGCMAALD 359
Cdd:PRK10262 231 nIESLDVAGLFVAIGHSPNTAIFEGQLELE-NGYIKVQSGihgnATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALD 309

                        330
                 ....*....|.
gi 42567414  360 AEHYLQEIGSQ 370
Cdd:PRK10262 310 AERYLDGLADA 320
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 90-364 1.24e-44

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 160.71  E-value: 1.24e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414   90 GGQLTTTTDVENFPGFPEgILGVELTDKFRKQSERFGTTIFT-ETVTKVDFSSKPFKLFTDSKAIL-ADAVILATGAVAK 167
Cdd:PRK15317 245 GGQVLDTMGIENFISVPE-TEGPKLAAALEEHVKEYDVDIMNlQRASKLEPAAGLIEVELANGAVLkAKTVILATGARWR 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  168 RLSFVGSGEasggFWNRGISACAVCDGaaPIFRNKPLAVIGGGDSAMEEANFLTKYGSKVYIIHRRDAFRASKIMQQRAL 247
Cdd:PRK15317 324 NMNVPGEDE----YRNKGVAYCPHCDG--PLFKGKRVAVIGGGNSGVEAAIDLAGIVKHVTVLEFAPELKADQVLQDKLR 397

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  248 SNPKIDVIWNSSVVEAYGDGERdvLGGLKVKNVVTGDVSDLKVSGLFFAIGHEPATKFLDGGVELDSDGYVVT-KPGttQ 326
Cdd:PRK15317 398 SLPNVTIITNAQTTEVTGDGDK--VTGLTYKDRTTGEEHHLELEGVFVQIGLVPNTEWLKGTVELNRRGEIIVdARG--A 473

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 42567414  327 TSVPGVFAAGDVQDKKYRQAITAAGTGCMAALDAEHYL 364
Cdd:PRK15317 474 TSVPGVFAAGDCTTVPYKQIIIAMGEGAKAALSAFDYL 511
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 51-353 3.09e-44

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: 154.78  E-value: 3.09e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414    51 TRLCIVGSGPAAHTAAIYAARAELKPLLFEgwmANDIAPGGQLTTTTDVENFPGFPEGIL-GVELTDKFRKQSERFGTTI 129
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIE---DEGTCPYGGCVLSKALLGAAEAPEIASlWADLYKRKEEVVKKLNNGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414   130 FT---ETVTKVDFSSKPFKLFTDS----KAILADAVILATGAVAKRLSFvgSGEASGGFwnRGISACAVCDGAAPIFRNK 202
Cdd:pfam07992  78 EVllgTEVVSIDPGAKKVVLEELVdgdgETITYDRLVIATGARPRLPPI--PGVELNVG--FLVRTLDSAEALRLKLLPK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414   203 PLAVIGGGDSAMEEANFLTKYGSKVYIIHRRDAF------RASKIMqQRALSNPKIDVIWNSSVVEAYGDGErdvlgGLK 276
Cdd:pfam07992 154 RVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLlrafdeEISAAL-EKALEKNGVEVRLGTSVKEIIGDGD-----GVE 227

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42567414   277 vknVVTGDVSDLKVSGLFFAIGHEPATKFLD-GGVELDSDGYVVTKPgTTQTSVPGVFAAGDVQDKKYRQAITAAGTG 353
Cdd:pfam07992 228 ---VILKDGTEIDADLVVVAIGRRPNTELLEaAGLELDERGGIVVDE-YLRTSVPGIYAAGDCRVGGPELAQNAVAQG 301
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 123-338 1.05e-19

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: 88.71  E-value: 1.05e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414 123 ERFGTTIFTET-VTKVDFSSKpfKLFTDSKAILA-DAVILATGAVAKRLSFVGSgEASGGFWNRGISACAVCDGAAPIFR 200
Cdd:COG0446  47 ERKGIDVRTGTeVTAIDPEAK--TVTLRDGETLSyDKLVLATGARPRPPPIPGL-DLPGVFTLRTLDDADALREALKEFK 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414 201 NKPLAVIGGGDSAMEEANFLTKYGSKVYIIHRRDAF--RASKIMQQRALSNPK---IDVIWNSSVVEAYGDGerdvlggl 275
Cdd:COG0446 124 GKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLlgVLDPEMAALLEEELRehgVELRLGETVVAIDGDD-------- 195

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42567414 276 KVKnVVTGDVSDLKVSGLFFAIGHEPATKFLDG-GVELDSDGYVVTKPgTTQTSVPGVFAAGDV 338
Cdd:COG0446 196 KVA-VTLTDGEEIPADLVVVAPGVRPNTELAKDaGLALGERGWIKVDE-TLQTSDPDVYAAGDC 257
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 148-338 6.96e-18

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: 84.75  E-value: 6.96e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414 148 TDSKAILADAVILATGAVAKRLSFVGSGEA----SGGFWNrgisacavcdgaapiFRNKP--LAVIGGGDSAMEEANFLT 221
Cdd:COG1249 124 TGGETLTADHIVIATGSRPRVPPIPGLDEVrvltSDEALE---------------LEELPksLVVIGGGYIGLEFAQIFA 188

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414 222 KYGSKVYIIHRRDAF------RASKIMqQRALSNPKIDVIWNSSVVEAYGDGerdvlGGLKVKNVVTGDVSDLKVSGLFF 295
Cdd:COG1249 189 RLGSEVTLVERGDRLlpgedpEISEAL-EKALEKEGIDILTGAKVTSVEKTG-----DGVTVTLEDGGGEEAVEADKVLV 262

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 42567414 296 AIGHEPATKFLD---GGVELDSDGYVVTKpGTTQTSVPGVFAAGDV 338
Cdd:COG1249 263 ATGRRPNTDGLGleaAGVELDERGGIKVD-EYLRTSVPGIYAIGDV 307
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 156-338 7.15e-18

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: 84.42  E-value: 7.15e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414 156 DAVILATGA-VAKRLSFvgSGEASGGFW---------NRGisacavCDGAAPIFRNKPLAVIGGGDSAME---EANFLtk 222
Cdd:COG0493 208 DAVFLATGAgKPRDLGI--PGEDLKGVHsamdfltavNLG------EAPDTILAVGKRVVVIGGGNTAMDcarTALRL-- 277

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414 223 yGSK-VYIIHRRDAFR--ASKIMQQRALSNpKIDVIWNSSVVEAYGD---------------GERDVLGGLKVKnVVTGD 284
Cdd:COG0493 278 -GAEsVTIVYRRTREEmpASKEEVEEALEE-GVEFLFLVAPVEIIGDengrvtglecvrmelGEPDESGRRRPV-PIEGS 354

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42567414 285 VSDLKVSGLFFAIGHEPATKFLDG--GVELDSDGYVVTKPGTTQTSVPGVFAAGDV 338
Cdd:COG0493 355 EFTLPADLVILAIGQTPDPSGLEEelGLELDKRGTIVVDEETYQTSLPGVFAGGDA 410
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 156-366 3.02e-15

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 76.76  E-value: 3.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  156 DAVILATGAVAKRlsFVG-SGEASGG--FWNRGISACAVCDGAAPIFRNKPLAVIGGGDSAMEEANFLTKYGSK-VYIIH 231
Cdd:PRK11749 227 DAVFIGTGAGLPR--FLGiPGENLGGvySAVDFLTRVNQAVADYDLPVGKRVVVIGGGNTAMDAARTAKRLGAEsVTIVY 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  232 RRD--AFRASKIMQQRALSNpKIDVIWNSSVVEAYGD--------------GERDVLGGLKVknVVTGDVSDLKVSGLFF 295
Cdd:PRK11749 305 RRGreEMPASEEEVEHAKEE-GVEFEWLAAPVEILGDegrvtgvefvrmelGEPDASGRRRV--PIEGSEFTLPADLVIK 381

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42567414  296 AIGHEPATKFLDG--GVELDSDGYVVTKPGTTQTSVPGVFAAGDVqdkkYRQA---ITAAGTGCMAALDAEHYLQE 366
Cdd:PRK11749 382 AIGQTPNPLILSTtpGLELNRWGTIIADDETGRTSLPGVFAGGDI----VTGAatvVWAVGDGKDAAEAIHEYLEG 453
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 204-338 8.83e-14

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 72.13  E-value: 8.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  204 LAVIGGGDSAMEEANFLTKYGSKVYIIHRRDAF----------RASKIMQQRalsnpkIDVIWNSSVVEAYGDGERDVlg 273
Cdd:PRK06292 172 LAVIGGGVIGLELGQALSRLGVKVTVFERGDRIlpledpevskQAQKILSKE------FKIKLGAKVTSVEKSGDEKV-- 243

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42567414  274 glkVKNVVTGDVSDLKVSGLFFAIGHEPATKFLD---GGVELDSDGYVVTKPgTTQTSVPGVFAAGDV 338
Cdd:PRK06292 244 ---EELEKGGKTETIEADYVLVATGRRPNTDGLGlenTGIELDERGRPVVDE-HTQTSVPGIYAAGDV 307
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 204-272 9.12e-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: 66.07  E-value: 9.12e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42567414   204 LAVIGGGDSAMEEANFLTKYGSKVYIIHRRDAFR------ASKIMQQRALSNpKIDVIWNSSVVEAYGDGERDVL 272
Cdd:pfam00070   2 VVVVGGGYIGLELAGALARLGSKVTVVERRDRLLpgfdpeIAKILQEKLEKN-GIEFLLNTTVEAIEGNGDGVVV 75
Pyr_redox_3 pfam13738
Pyridine nucleotide-disulphide oxidoreductase;
111-336 9.74e-14

Pyridine nucleotide-disulphide oxidoreductase;


Pssm-ID: 404603 [Multi-domain]  Cd Length: 296  Bit Score: 71.10  E-value: 9.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414   111 GVELTDKFRKQSERFGTTIFT-ETVTKVDFSSKPFKLFTDSKAILADAVILATG--AVAKRLSFVGSGEASGGFWNrgis 187
Cdd:pfam13738  74 GNEYAEYLRRVADHFELPINLfEEVTSVKKEDDGFVVTTSKGTYQARYVIIATGefDFPNKLGVPELPKHYSYVKD---- 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414   188 acavcdgaAPIFRNKPLAVIGGGDSAMEEANFLTKYGSKVYIIHRRDAFRASK---------IMQQR---ALSNPKIDVI 255
Cdd:pfam13738 150 --------FHPYAGQKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDRDsdpsyslspDTLNRleeLVKNGKIKAH 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414   256 WNSSVVE----------AYGDGERdvlggLKVKNVVtgdvsdlkvsglFFAIGHEPATKFLD-GGVELDSDGYVVTKPGT 324
Cdd:pfam13738 222 FNAEVKEitevdvsykvHTEDGRK-----VTSNDDP------------ILATGYHPDLSFLKkGLFELDEDGRPVLTEET 284

                         250
                  ....*....|..
gi 42567414   325 TQTSVPGVFAAG 336
Cdd:pfam13738 285 ESTNVPGLFLAG 296
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
132-338 1.33e-13

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 71.33  E-value: 1.33e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414 132 ETVTKVDFSSKpfKLFTDSKAILA-DAVILATGAVAKRLSFVGSgEASGGFWNRGISACAVCDGAAPifRNKPLAVIGGG 210
Cdd:COG1251  77 TRVTAIDRAAR--TVTLADGETLPyDKLVLATGSRPRVPPIPGA-DLPGVFTLRTLDDADALRAALA--PGKRVVVIGGG 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414 211 DSAMEEANFLTKYGSKVYIIHRRDAF-------RASKIMQqRALSNPKIDVIWNSSVVEaygdgerdVLGGLKVKNVVTG 283
Cdd:COG1251 152 LIGLEAAAALRKRGLEVTVVERAPRLlprqldeEAGALLQ-RLLEALGVEVRLGTGVTE--------IEGDDRVTGVRLA 222

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42567414 284 DVSDLKVSGLFFAIGHEPATKFLDG-GVELDsDGYVVTkpGTTQTSVPGVFAAGDV 338
Cdd:COG1251 223 DGEELPADLVVVAIGVRPNTELARAaGLAVD-RGIVVD--DYLRTSDPDIYAAGDC 275
PRK06370 PRK06370
FAD-containing oxidoreductase;
204-338 2.59e-13

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 71.00  E-value: 2.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  204 LAVIGGGDSAMEEANFLTKYGSKVYIIHR------RDAFRASKIMQQrALSNPKIDVIWNSSVVEAYGDGerdvlGGLKV 277
Cdd:PRK06370 174 LVIIGGGYIGLEFAQMFRRFGSEVTVIERgprllpREDEDVAAAVRE-ILEREGIDVRLNAECIRVERDG-----DGIAV 247

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42567414  278 KNVVTGDVSDLKVSGLFFAIGHEPATKFLD---GGVELDSDGYVVTKpGTTQTSVPGVFAAGDV 338
Cdd:PRK06370 248 GLDCNGGAPEITGSHILVAVGRVPNTDDLGleaAGVETDARGYIKVD-DQLRTTNPGIYAAGDC 310
PRK07251 PRK07251
FAD-containing oxidoreductase;
149-338 3.68e-12

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 67.08  E-value: 3.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  149 DSKAILADAVILATGAVAKRLSFVGSGEASGGFWNRGISACAVcdgaapifRNKPLAVIGGGDSAMEEANFLTKYGSKVY 228
Cdd:PRK07251 113 EKIELTAETIVINTGAVSNVLPIPGLADSKHVYDSTGIQSLET--------LPERLGIIGGGNIGLEFAGLYNKLGSKVT 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  229 IIHRRDAF--RASKIMQQRA---LSNPKIDVIWNSSVVEAYGDGErdvlgglkvKNVVTGDVSDLKVSGLFFAIGHEPAT 303
Cdd:PRK07251 185 VLDAASTIlpREEPSVAALAkqyMEEDGITFLLNAHTTEVKNDGD---------QVLVVTEDETYRFDALLYATGRKPNT 255

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 42567414  304 KFL---DGGVELDSDGYVVTKPgTTQTSVPGVFAAGDV 338
Cdd:PRK07251 256 EPLgleNTDIELTERGAIKVDD-YCQTSVPGVFAVGDV 292
PRK12831 PRK12831
putative oxidoreductase; Provisional
 197-365 6.95e-12

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 66.58  E-value: 6.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  197 PIFRNKPLAVIGGGDSAMEEANFLTKYGSKVYIIHRrdafRASKIMQQRA---------------LSNPkidviwnssvV 261
Cdd:PRK12831 277 PIKVGKKVAVVGGGNVAMDAARTALRLGAEVHIVYR----RSEEELPARVeevhhakeegvifdlLTNP----------V 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  262 EAYGD---------------GERDVLGglKVKNV-VTGDVSDLKVSGLFFAIGHEP------ATKfldgGVELDSDGYVV 319
Cdd:PRK12831 343 EILGDengwvkgmkcikmelGEPDASG--RRRPVeIEGSEFVLEVDTVIMSLGTSPnplissTTK----GLKINKRGCIV 416

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 42567414  320 TKPGTTQTSVPGVFAAGDvqdkkyrqAITAAGT-------GCMAALDAEHYLQ 365
Cdd:PRK12831 417 ADEETGLTSKEGVFAGGD--------AVTGAATvilamgaGKKAAKAIDEYLS 461
PRK06116 PRK06116
glutathione reductase; Validated
 202-341 2.87e-10

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 61.33  E-value: 2.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  202 KPLAVIGGGDSAMEEANFLTKYGSKVYIIHRRDAFRAS----------KIMQQRAlsnpkIDVIWNSSV--VEAYGDger 269
Cdd:PRK06116 168 KRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGfdpdiretlvEEMEKKG-----IRLHTNAVPkaVEKNAD--- 239

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42567414  270 dvlGGLKVKnvvTGDVSDLKVSGLFFAIGHEPATKFLD---GGVELDSDGYVVTKpGTTQTSVPGVFAAGDVQDK 341
Cdd:PRK06116 240 ---GSLTLT---LEDGETLTVDCLIWAIGREPNTDGLGlenAGVKLNEKGYIIVD-EYQNTNVPGIYAVGDVTGR 307
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
 123-338 3.28e-10

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 60.77  E-value: 3.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  123 ERFGTTIFTETvtKVDFSSKPFKLFTDSKA--------ILA--DAVILATGAVAKRLSFVgSGEASGG--------FWNR 184
Cdd:PRK12770  79 EEAGVVFHTRT--KVCCGEPLHEEEGDEFVerivsleeLVKkyDAVLIATGTWKSRKLGI-PGEDLPGvysaleylFRIR 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  185 GISACAVCDGAAPIFRNKPLAVIGGGDSAM---EEANFLtkYGSKVYIIHRRDAFRA-SKIMQQRALSNPKIDVIWNSSV 260
Cdd:PRK12770 156 AAKLGYLPWEKVPPVEGKKVVVVGAGLTAVdaaLEAVLL--GAEKVYLAYRRTINEApAGKYEIERLIARGVEFLELVTP 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  261 VEAYGDGERDVLGGLKVK------------NVVTGDVSDLKVSGLFFAIGHEPATKFLDG--GVELDSDGYVVTKPgTTQ 326
Cdd:PRK12770 234 VRIIGEGRVEGVELAKMRlgepdesgrprpVPIPGSEFVLEADTVVFAIGEIPTPPFAKEclGIELNRKGEIVVDE-KHM 312

                        250
                 ....*....|..
gi 42567414  327 TSVPGVFAAGDV 338
Cdd:PRK12770 313 TSREGVFAAGDV 324
PRK07846 PRK07846
mycothione reductase; Reviewed
 204-338 3.70e-10

mycothione reductase; Reviewed


Pssm-ID: 181142 [Multi-domain]  Cd Length: 451  Bit Score: 61.12  E-value: 3.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  204 LAVIGGGDSAMEEANFLTKYGSKVYIIHRRDAF----------RASKIMQQRalsnpkIDVIWNSSVVEAYGDGERDVLg 273
Cdd:PRK07846 169 LVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLlrhldddiseRFTELASKR------WDVRLGRNVVGVSQDGSGVTL- 241

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42567414  274 GLKVKNVVTGDVsdlkvsgLFFAIGHEPATKFLD---GGVELDSDGYVVTKPgTTQTSVPGVFAAGDV 338
Cdd:PRK07846 242 RLDDGSTVEADV-------LLVATGRVPNGDLLDaaaAGVDVDEDGRVVVDE-YQRTSAEGVFALGDV 301
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 55-337 6.42e-10

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 60.56  E-value: 6.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414   55 IVGSGPAAHTAAIYAARAELKPLLFEgwmANDiAPGGQLTTttdvenfpGFPEGILGVELTDKFRKQSERFGTTIFTETV 134
Cdd:PRK12810 148 VVGSGPAGLAAADQLARAGHKVTVFE---RAD-RIGGLLRY--------GIPDFKLEKEVIDRRIELMEAEGIEFRTNVE 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  135 TKVDFSSKpfklftdskAILA--DAVILATGA-VAKRLSFVGSgEASGGFW--------NRgisACAVCDGAAPI-FRNK 202
Cdd:PRK12810 216 VGKDITAE---------ELLAeyDAVFLGTGAyKPRDLGIPGR-DLDGVHFamdfliqnTR---RVLGDETEPFIsAKGK 282

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  203 PLAVIGGGDSAME---EANfltKYGSKvyIIHRRDafraskIM----QQRALSNPKIDVIWNSSVVEAY--GD------- 266
Cdd:PRK12810 283 HVVVIGGGDTGMDcvgTAI---RQGAK--SVTQRD------IMpmppSRRNKNNPWPYWPMKLEVSNAHeeGVerefnvq 351

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  267 -----GERDVLGGLKVKNVVTGDVSDLKVSG---------LFFAIG--HEPATKFLDGGVELDSDGYVVTKPGTTQTSVP 330
Cdd:PRK12810 352 tkefeGENGKVTGVKVVRTELGEGDFEPVEGsefvlpadlVLLAMGftGPEAGLLAQFGVELDERGRVAAPDNAYQTSNP 431


                 ....*..
gi 42567414  331 GVFAAGD 337
Cdd:PRK12810 432 KVFAAGD 438
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
 123-338 1.02e-09

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


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 60.23  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414   123 ERFGTTIFT-ETVTKVDFSSKpfKLFTDSKAILA-DAVILATGAVAKRLSFVGSgEASGGFWNRGISACAVCDGAAPifR 200
Cdd:TIGR02374  65 EKHGITLYTgETVIQIDTDQK--QVITDAGRTLSyDKLILATGSYPFILPIPGA-DKKGVYVFRTIEDLDAIMAMAQ--R 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414   201 NKPLAVIGGGDSAMEEANFLTKYGSKVYIIHRRDAFRASKIMQ------QRALSNPKIDVIWNSSVVEAYGDGERDvlgG 274
Cdd:TIGR02374 140 FKKAAVIGGGLLGLEAAVGLQNLGMDVSVIHHAPGLMAKQLDQtagrllQRELEQKGLTFLLEKDTVEIVGATKAD---R 216

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42567414   275 LKVKnvvtgDVSDLKVSGLFFAIGHEPATKfLDGGVELDSDGYVVTKpGTTQTSVPGVFAAGDV 338
Cdd:TIGR02374 217 IRFK-----DGSSLEADLIVMAAGIRPNDE-LAVSAGIKVNRGIIVN-DSMQTSDPDIYAVGEC 273
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 156-364 6.90e-09

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 57.19  E-value: 6.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  156 DAVILATGA-VAKRLsFVGSGEAsggfwNRGISACAVCDGAA---PIFRNKPLAVIGGGDSAMEEANFLTKYG-SKVYII 230
Cdd:PRK12771 224 DAVFVAIGAqLGKRL-PIPGEDA-----AGVLDAVDFLRAVGegePPFLGKRVVVIGGGNTAMDAARTARRLGaEEVTIV 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  231 HRRD-------AFRASKIMQQralsnpKIDVIWNSSVVEAyGDGERDVLGGLKVKNVVTGDVSDLK---VSGLFF----- 295
Cdd:PRK12771 298 YRRTredmpahDEEIEEALRE------GVEINWLRTPVEI-EGDENGATGLRVITVEKMELDEDGRpspVTGEEEtlead 370

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42567414  296 ----AIGHEPATKFLDG--GVELDsDGYVVTKPGTTQTSVPGVFAAGDVQdKKYRQAITAAGTGCMAALDAEHYL 364
Cdd:PRK12771 371 lvvlAIGQDIDSAGLESvpGVEVG-RGVVQVDPNFMMTGRPGVFAGGDMV-PGPRTVTTAIGHGKKAARNIDAFL 443
PRK13748 PRK13748
putative mercuric reductase; Provisional
 204-359 9.50e-09

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 57.08  E-value: 9.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  204 LAVIGGGDSAMEEANFLTKYGSKVYIIHRR---------------DAFRASKImqqRALSNPKIdviwnSSVveAYGDGE 268
Cdd:PRK13748 273 LAVIGSSVVALELAQAFARLGSKVTILARStlffredpaigeavtAAFRAEGI---EVLEHTQA-----SQV--AHVDGE 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  269 RdvlgglkvknVVTGDVSDLKVSGLFFAIGHEPATKFLD---GGVELDSDGYVVTKPGtTQTSVPGVFAAGDVQDK-KYR 344
Cdd:PRK13748 343 F----------VLTTGHGELRADKLLVATGRAPNTRSLAldaAGVTVNAQGAIVIDQG-MRTSVPHIYAAGDCTDQpQFV 411

                        170       180
                 ....*....|....*....|..
gi 42567414  345 QAITAAG-------TGCMAALD 359
Cdd:PRK13748 412 YVAAAAGtraainmTGGDAALD 433
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 202-338 3.34e-08

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 55.15  E-value: 3.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  202 KPLAVIGGGDSAMEEANFLTKYGSKVYIIHRRD----AFRA--SKIMqQRALSNPKIDVIWNSSVVEA-YGDgerdvlGG 274
Cdd:PRK06416 173 KSLVVIGGGYIGVEFASAYASLGAEVTIVEALPrilpGEDKeiSKLA-ERALKKRGIKIKTGAKAKKVeQTD------DG 245

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42567414  275 LKVKNVVTGDVSDLKVSGLFFAIGHEPATKFL---DGGVELDSdGYVVTKpGTTQTSVPGVFAAGDV 338
Cdd:PRK06416 246 VTVTLEDGGKEETLEADYVLVAVGRRPNTENLgleELGVKTDR-GFIEVD-EQLRTNVPNIYAIGDI 310
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
 148-338 1.67e-07

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 53.01  E-value: 1.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  148 TDSKAILADAVILATGAVAKRLSFVGsgeasggFWNRGI--SACAVCDGAAPifrnKPLAVIGGGDSAMEEANFLTKYGS 225
Cdd:PRK06327 139 EDETVITAKHVIIATGSEPRHLPGVP-------FDNKIIldNTGALNFTEVP----KKLAVIGAGVIGLELGSVWRRLGA 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  226 KVYIIHRRDAFRASKIMQ-----QRALSNPKIDVIWNSSV--VEAYGDGERDVLGGLKvknvvtGDVSDLKVSGLFFAIG 298
Cdd:PRK06327 208 EVTILEALPAFLAAADEQvakeaAKAFTKQGLDIHLGVKIgeIKTGGKGVSVAYTDAD------GEAQTLEVDKLIVSIG 281

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 42567414  299 HEPATKFLDG---GVELDSDGYVVTKpGTTQTSVPGVFAAGDV 338
Cdd:PRK06327 282 RVPNTDGLGLeavGLKLDERGFIPVD-DHCRTNVPNVYAIGDV 323
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 193-366 2.78e-07

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


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 52.44  E-value: 2.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  193 DGAAPIFRNKPLAVIGGGDSAMEEANFLTKYGS-KVYIIHRRdafrASKIMQQRA--LSNPK---IDVIWNSSVVEAYGD 266
Cdd:PRK12778 562 DSDTPIKFGKKVAVVGGGNTAMDSARTAKRLGAeRVTIVYRR----SEEEMPARLeeVKHAKeegIEFLTLHNPIEYLAD 637

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  267 ---------------GERDVlGGLKVKNVVTGDVSDLKVSGLFFAIGHEP------ATKfldgGVELDSDGYVVTKPgTT 325
Cdd:PRK12778 638 ekgwvkqvvlqkmelGEPDA-SGRRRPVAIPGSTFTVDVDLVIVSVGVSPnplvpsSIP----GLELNRKGTIVVDE-EM 711

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 42567414  326 QTSVPGVFAAGDVqdkkYRQA---ITAAGTGCMAALDAEHYLQE 366
Cdd:PRK12778 712 QSSIPGIYAGGDI----VRGGatvILAMGDGKRAAAAIDEYLSS 751
PRK12775 PRK12775
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ...
 52-365 3.82e-07

putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional


Pssm-ID: 183738 [Multi-domain]  Cd Length: 1006  Bit Score: 52.25  E-value: 3.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414    52 RLCIVGSGPAAHTAAIYAARAELKPLLFEGWMAndiaPGGQLTTttdvenfpGFPEGILGVELTDKFRKQSERFGTTIFT 131
Cdd:PRK12775  432 KVAICGSGPAGLAAAADLVKYGVDVTVYEALHV----VGGVLQY--------GIPSFRLPRDIIDREVQRLVDIGVKIET 499

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414   132 ETVTKVDFSSKpfKLFTDSKAilaDAVILATGAVAKrlSFVG-SGEASGGFW--NRGISACAVCDGA------APIFRNK 202
Cdd:PRK12775  500 NKVIGKTFTVP--QLMNDKGF---DAVFLGVGAGAP--TFLGiPGEFAGQVYsaNEFLTRVNLMGGDkfpfldTPISLGK 572

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414   203 PLAVIGGGDSAMEEANFLTKYGS-KVYIIHRRDAFRA-SKIMQQRALSNPKIDVIWNSSVVEAYGDGERDVlGGLKV--- 277
Cdd:PRK12775  573 SVVVIGAGNTAMDCLRVAKRLGApTVRCVYRRSEAEApARIEEIRHAKEEGIDFFFLHSPVEIYVDAEGSV-RGMKVeem 651

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414   278 -----------KNVVTGDVSDLKVSGLFFAIGHEPATKFLDG--GVELDSDGYVVTKPG----TTQTSVPGVFAAGDVQD 340
Cdd:PRK12775  652 elgepdekgrrKPMPTGEFKDLECDTVIYALGTKANPIITQStpGLALNKWGNIAADDGklesTQSTNLPGVFAGGDIVT 731

                         330       340
                  ....*....|....*....|....*
gi 42567414   341 KKyRQAITAAGTGCMAALDAEHYLQ 365
Cdd:PRK12775  732 GG-ATVILAMGAGRRAARSIATYLR 755
PRK12779 PRK12779
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ...
 197-357 4.10e-07

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


Pssm-ID: 183740 [Multi-domain]  Cd Length: 944  Bit Score: 52.14  E-value: 4.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  197 PIFRNKPLAVIGGGDSAMEEANFLTKYGSKVYIIHRRdafrASKIMQQR------ALSNpKIDVIWNSSVVEAYGDGERD 270
Cdd:PRK12779 443 PEVKGKEVFVIGGGNTAMDAARTAKRLGGNVTIVYRR----TKSEMPARveelhhALEE-GINLAVLRAPREFIGDDHTH 517

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  271 VLGGLKV--------------KNVVTGDVSDLKVSGLFFAIGHE--PATKFLDGGVELDSDGYVVTKPGTTQTSVPGVFA 334
Cdd:PRK12779 518 FVTHALLdvnelgepdksgrrSPKPTGEIERVPVDLVIMALGNTanPIMKDAEPGLKTNKWGTIEVEKGSQRTSIKGVYS 597

                        170       180
                 ....*....|....*....|...
gi 42567414  335 AGDVQdKKYRQAITAAGTGCMAA 357
Cdd:PRK12779 598 GGDAA-RGGSTAIRAAGDGQAAA 619
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
 206-362 1.03e-06

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 50.17  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  206 VIGGGDSAMEEANFLTKYGSKVYIIHRRDAFraSKIMQQRaLSNPKIDVIWNSSVVEAYGDGERDVLGglkvkNVVT--- 282
Cdd:PRK13512 153 VVGAGYISLEVLENLYERGLHPTLIHRSDKI--NKLMDAD-MNQPILDELDKREIPYRLNEEIDAING-----NEVTfks 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  283 GDVSDLKVsgLFFAIGHEPATKFLDG-GVELDSDGYVVTKPgTTQTSVPGVFAAGDVQDKKYR------QAITAAGTGCM 355
Cdd:PRK13512 225 GKVEHYDM--IIEGVGTHPNSKFIESsNIKLDDKGFIPVND-KFETNVPNIYAIGDIITSHYRhvdlpaSVPLAWGAHRA 301


                 ....*..
gi 42567414  356 AALDAEH 362
Cdd:PRK13512 302 ASIVAEQ 308
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
118-338 1.18e-06

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 50.13  E-value: 1.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414 118 FRKQSERFGTTIFTETVTKVDFSSKpfKLFTDSKAILA-DAVILATGA---------VAKRLSFVGSGEASGGFWNRGIS 187
Cdd:COG1252  62 LRELLRRAGVRFIQGEVTGIDPEAR--TVTLADGRTLSyDYLVIATGSvtnffgipgLAEHALPLKTLEDALALRERLLA 139

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414 188 ACAVCDGAAPIfrnkPLAVIGGGDS----AMEEANFLTKYGS---------KVYIIHRRDAF------RASKIMQqRALS 248
Cdd:COG1252 140 AFERAERRRLL----TIVVVGGGPTgvelAGELAELLRKLLRypgidpdkvRITLVEAGPRIlpglgeKLSEAAE-KELE 214

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414 249 NPKIDVIWNSSVVEAYGDGerdvlgglkvknVVTGDVSDLKVSGLFFAIGHEPATKFLDGGVELDSDGYVVTKPgTTQT- 327
Cdd:COG1252 215 KRGVEVHTGTRVTEVDADG------------VTLEDGEEIPADTVIWAAGVKAPPLLADLGLPTDRRGRVLVDP-TLQVp 281

                       250
                ....*....|.
gi 42567414 328 SVPGVFAAGDV 338
Cdd:COG1252 282 GHPNVFAIGDC 292
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
204-338 1.55e-05

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


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 46.69  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  204 LAVIGGGDSAMEEANFLTKYGSKVYIIHRRD---AFRASKIMQqrALSNpkidVIWNSSVVeaygdgerdVLGGLKVKNV 280
Cdd:PRK05249 178 LIIYGAGVIGCEYASIFAALGVKVTLINTRDrllSFLDDEISD--ALSY----HLRDSGVT---------IRHNEEVEKV 242

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42567414  281 VTGD---VSDLKvSG-------LFFAIGHEPATKFLD---GGVELDSDGYV-VTKpgTTQTSVPGVFAAGDV 338
Cdd:PRK05249 243 EGGDdgvIVHLK-SGkkikadcLLYANGRTGNTDGLNlenAGLEADSRGQLkVNE--NYQTAVPHIYAVGDV 311
PLN02507 PLN02507
glutathione reductase
 202-341 1.75e-05

glutathione reductase


Pssm-ID: 215281 [Multi-domain]  Cd Length: 499  Bit Score: 46.73  E-value: 1.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  202 KPLAVIGGGDSAMEEANFLTKYGSKVYIIHRR--------DAFRAskiMQQRALSNPKIDVIWNSSVVEAygdgeRDVLG 273
Cdd:PLN02507 204 KRAVVLGGGYIAVEFASIWRGMGATVDLFFRKelplrgfdDEMRA---VVARNLEGRGINLHPRTNLTQL-----TKTEG 275

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42567414  274 GLKVknvVTGDVSDLKVSGLFFAIGHEPATKFL---DGGVELDSDGYVVTKPgTTQTSVPGVFAAGDVQDK 341
Cdd:PLN02507 276 GIKV---ITDHGEEFVADVVLFATGRAPNTKRLnleAVGVELDKAGAVKVDE-YSRTNIPSIWAIGDVTNR 342
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 200-337 1.92e-05

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 46.19  E-value: 1.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  200 RNKPLAVIGGGDSAMEEANFLTKYGSKVYIIHRRD-----AF--RASKIMQQrALSNPKIDVIWNSSVVEAYGDGerdvl 272
Cdd:PRK09564 148 EIKNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDrilpdSFdkEITDVMEE-ELRENGVELHLNEFVKSLIGED----- 221

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42567414  273 gglKVKNVVTgDVSDLKVSGLFFAIGHEPATKFL-DGGVELDSDG-YVVTKPGttQTSVPGVFAAGD 337
Cdd:PRK09564 222 ---KVEGVVT-DKGEYEADVVIVATGVKPNTEFLeDTGLKTLKNGaIIVDEYG--ETSIENIYAAGD 282
PLN02546 PLN02546
glutathione reductase
 200-341 3.31e-05

glutathione reductase


Pssm-ID: 215301 [Multi-domain]  Cd Length: 558  Bit Score: 45.64  E-value: 3.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  200 RNKPLAVIGGGDSAMEEANFLTKYGSKVYI-IHRRDAFRASK------IMQQRALSNPKIDVIWNSSVVEAYGDGerdvL 272
Cdd:PLN02546 251 KPEKIAIVGGGYIALEFAGIFNGLKSDVHVfIRQKKVLRGFDeevrdfVAEQMSLRGIEFHTEESPQAIIKSADG----S 326

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42567414  273 GGLKV-KNVVTGdvsdlkVSGLFFAIGHEPATKFL---DGGVELDSDGYVVTKPgTTQTSVPGVFAAGDVQDK 341
Cdd:PLN02546 327 LSLKTnKGTVEG------FSHVMFATGRKPNTKNLgleEVGVKMDKNGAIEVDE-YSRTSVPSIWAVGDVTDR 392
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
 156-365 6.79e-05

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 44.72  E-value: 6.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  156 DAVILATGA-VAKRLSFvgSGEASGGFWNrGISACA-VCDGAAPIFRNKPLaVIGGGDSAMEEANFLTKYG-SKVYIIHR 232
Cdd:PRK12814 280 DAVLLAVGAqKASKMGI--PGEELPGVIS-GIDFLRnVALGTALHPGKKVV-VIGGGNTAIDAARTALRLGaESVTILYR 355

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  233 R--DAFRASKIMQQRALSNP-KIDVIWNSSVVEAYGD-----------GERDVLGglKVKNV-VTGDVSDLKVSGLFFAI 297
Cdd:PRK12814 356 RtrEEMPANRAEIEEALAEGvSLRELAAPVSIERSEGgleltaikmqqGEPDESG--RRRPVpVEGSEFTLQADTVISAI 433

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42567414  298 GHE--PATKFLDGgVELDSDGYVVTKPGTTQTSVPGVFAAGDV---QDkkyrQAITAAGTGCMAALDAEHYLQ 365
Cdd:PRK12814 434 GQQvdPPIAEAAG-IGTSRNGTVKVDPETLQTSVAGVFAGGDCvtgAD----IAINAVEQGKRAAHAIDLFLN 501
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
 155-341 1.72e-04

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: 43.42  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414   155 ADAVILATGAVAKRLSFvgsgeasggfwnRGISACAVCDGA-----APifrnKPLAVIGGGDSAMEEANFLTKY---GSK 226
Cdd:TIGR01423 152 AEHILLATGSWPQMLGI------------PGIEHCISSNEAfyldePP----RRVLTVGGGFISVEFAGIFNAYkprGGK 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414   227 VYIIHRRDA-FRA--SKIMQQ--RALSNPKIDVIW--NSSVVEAYGDGERDVLgglkvknVVTGDVSDLKVsgLFFAIGH 299
Cdd:TIGR01423 216 VTLCYRNNMiLRGfdSTLRKEltKQLRANGINIMTneNPAKVTLNADGSKHVT-------FESGKTLDVDV--VMMAIGR 286

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 42567414   300 EPATKFLdggvELDSDGYVVTKPGTTQ------TSVPGVFAAGDVQDK 341
Cdd:TIGR01423 287 VPRTQTL----QLDKVGVELTKKGAIQvdefsrTNVPNIYAIGDVTDR 330
PRK07845 PRK07845
flavoprotein disulfide reductase; Reviewed
 204-338 5.57e-04

flavoprotein disulfide reductase; Reviewed


Pssm-ID: 236112 [Multi-domain]  Cd Length: 466  Bit Score: 41.77  E-value: 5.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  204 LAVIGGGDSAMEEANFLTKYGSKVYIIHRR-------DAFRASKImqQRALSNPKIDVIWNSSV--VEAYGDGerdVLGG 274
Cdd:PRK07845 180 LIVVGSGVTGAEFASAYTELGVKVTLVSSRdrvlpgeDADAAEVL--EEVFARRGMTVLKRSRAesVERTGDG---VVVT 254

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42567414  275 LKVKNVVTGdvsdlkvSGLFFAIGHEPATKFL---DGGVELDSDGYVVTKpGTTQTSVPGVFAAGDV 338
Cdd:PRK07845 255 LTDGRTVEG-------SHALMAVGSVPNTAGLgleEAGVELTPSGHITVD-RVSRTSVPGIYAAGDC 313
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
 156-338 8.97e-04

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 41.06  E-value: 8.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  156 DAVILATGAVAKRLSFVGS-GEasggfwnrGISACAVCDGAA----PIFRNKPLAVIGGGDSAMEEANFLTKYGSKVYII 230
Cdd:PRK09754 102 DQLFIATGAAARPLPLLDAlGE--------RCFTLRHAGDAArlreVLQPERSVVIVGAGTIGLELAASATQRRCKVTVI 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  231 HRRDAF--RASKIMQQRALSN----PKIDVIWNSSVVEAYgDGERDVLGgLKVKNVVTGDVsdlkvsgLFFAIGHEPATK 304
Cdd:PRK09754 174 ELAATVmgRNAPPPVQRYLLQrhqqAGVRILLNNAIEHVV-DGEKVELT-LQSGETLQADV-------VIYGIGISANDQ 244

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 42567414  305 F-LDGGveLDSDGYVVTKPgTTQTSVPGVFAAGDV 338
Cdd:PRK09754 245 LaREAN--LDTANGIVIDE-ACRTCDPAIFAGGDV 276
PRK08010 PRK08010
pyridine nucleotide-disulfide oxidoreductase; Provisional
 204-338 1.29e-03

pyridine nucleotide-disulfide oxidoreductase; Provisional


Pssm-ID: 181196 [Multi-domain]  Cd Length: 441  Bit Score: 40.77  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414  204 LAVIGGGDSAMEEANFLTKYGSKVYIIHRRDAF--RASKIMQQ---RALSNPKIDVIWNSSvVEAYGDGERDVLgglkvk 278
Cdd:PRK08010 161 LGILGGGYIGVEFASMFANFGSKVTILEAASLFlpREDRDIADniaTILRDQGVDIILNAH-VERISHHENQVQ------ 233

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42567414  279 nvVTGDVSDLKVSGLFFAIGHEPATKFL---DGGVELDSDGYVVTKPgTTQTSVPGVFAAGDV 338
Cdd:PRK08010 234 --VHSEHAQLAVDALLIASGRQPATASLhpeNAGIAVNERGAIVVDK-YLHTTADNIWAMGDV 293
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 124-233 4.89e-03

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: 38.69  E-value: 4.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567414 124 RFGTTiftetVTKVDFSSKP--FKLFTDS-KAILADAVILATGA--VAKRLSFVGSGEASG-----GFWNRGISacavcd 193
Cdd:COG2072 100 RFGTE-----VTSARWDEADgrWTVTTDDgETLTARFVVVATGPlsRPKIPDIPGLEDFAGeqlhsADWRNPVD------ 168

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 42567414 194 gaapiFRNKPLAVIGGGDSAMEEANFLTKYGSKVYIIHRR 233
Cdd:COG2072 169 -----LAGKRVLVVGTGASAVQIAPELARVAAHVTVFQRT 203
 
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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