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Conserved domains on  [gi|125714671|gb|ABN53163|]
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FAD-dependent pyridine nucleotide-disulfide oxidoreductase [Acetivibrio thermocellus ATCC 27405]

Protein Classification

NAD(P)/FAD-dependent oxidoreductase( domain architecture ID 11422994)

NAD(P)/FAD-dependent oxidoreductase catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant

CATH:  3.50.50.60
EC:  1.-.-.-
Gene Ontology:  GO:0050660|GO:0016491
PubMed:  33684359

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
2-291 1.91e-92

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


:

Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 276.23  E-value: 1.91e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671   2 YDVIIIGKGPAGISASLYTVRANLKTLVIGKGD--SALKKAERIENYYGFSEAINGERLLAEGEKQAARLGVEIIESEVI 79
Cdd:COG0492    1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEpgGQLATTKEIENYPGFPEGISGPELAERLREQAERFGAEILLEEVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671  80 SIEK-NEFFEVLTSD-DRYMAKAVLIATGQPQKKLRIENLEAFEGRGVSYCTTCDGFFYNNLKVGVVGAGDYVVHEAMEL 157
Cdd:COG0492   81 SVDKdDGPFRVTTDDgTEYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGKDVVVVGGGDSALEEALYL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671 158 LAFTKDITIYTNGNELQVSEKFVEAAKRFR----ISKKPIYKIDGSEFLQKIFFKDGTSE-----DIDGLFIAYESPSSV 228
Cdd:COG0492  161 TKFASKVTLIHRRDELRASKILVERLRANPkievLWNTEVTEIEGDGRVEGVTLKNVKTGeekelEVDGVFVAIGLKPNT 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 125714671 229 DFARKLGI-IVEGNAIVVDKNQQTNLEGLFAAGDCTGG-FKQIATAVGQGALAGRKMIEYVRSLE 291
Cdd:COG0492  241 ELLKGLGLeLDEDGYIVVDEDMETSVPGVFAAGDVRDYkYRQAATAAGEGAIAALSAARYLEPLK 305
 
Name Accession Description Interval E-value
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
2-291 1.91e-92

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 276.23  E-value: 1.91e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671   2 YDVIIIGKGPAGISASLYTVRANLKTLVIGKGD--SALKKAERIENYYGFSEAINGERLLAEGEKQAARLGVEIIESEVI 79
Cdd:COG0492    1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEpgGQLATTKEIENYPGFPEGISGPELAERLREQAERFGAEILLEEVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671  80 SIEK-NEFFEVLTSD-DRYMAKAVLIATGQPQKKLRIENLEAFEGRGVSYCTTCDGFFYNNLKVGVVGAGDYVVHEAMEL 157
Cdd:COG0492   81 SVDKdDGPFRVTTDDgTEYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGKDVVVVGGGDSALEEALYL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671 158 LAFTKDITIYTNGNELQVSEKFVEAAKRFR----ISKKPIYKIDGSEFLQKIFFKDGTSE-----DIDGLFIAYESPSSV 228
Cdd:COG0492  161 TKFASKVTLIHRRDELRASKILVERLRANPkievLWNTEVTEIEGDGRVEGVTLKNVKTGeekelEVDGVFVAIGLKPNT 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 125714671 229 DFARKLGI-IVEGNAIVVDKNQQTNLEGLFAAGDCTGG-FKQIATAVGQGALAGRKMIEYVRSLE 291
Cdd:COG0492  241 ELLKGLGLeLDEDGYIVVDEDMETSVPGVFAAGDVRDYkYRQAATAAGEGAIAALSAARYLEPLK 305
TRX_reduct TIGR01292
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ...
 3-287 9.07e-73

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: 225.97  E-value: 9.07e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671    3 DVIIIGKGPAGISASLYTVRANLKTLVIGKGD--SALKKAERIENYYGFSEAINGERLLAEGEKQAARLGVEIIESEVIS 80
Cdd:TIGR01292   1 DVIIIGAGPAGLTAAIYAARANLKPLLIEGMEpgGQLTTTTEVENYPGFPEGISGPELMEKMKEQAVKFGAEIIYEEVIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671   81 IEK-NEFFEVLTSDDR-YMAKAVLIATGQPQKKLRIENLEAFEGRGVSYCTTCDGFFYNNLKVGVVGAGDYVVHEAMELL 158
Cdd:TIGR01292  81 VDKsDRPFKVYTGDGKeYTAKAVIIATGASARKLGIPGEDEFWGRGVSYCATCDGPFFKNKEVAVVGGGDSAIEEALYLT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671  159 AFTKDITIYTNGNELQVS----EKFVEAAKRFRISKKPIYKIDGSEFLQKIFFKDG-TSE----DIDGLFIAYESPSSVD 229
Cdd:TIGR01292 161 RIAKKVTLVHRRDKFRAEkillDRLKKNPKIEFLWNSTVEEIVGDNKVEGVKIKNTvTGEeeelEVDGVFIAIGHEPNTE 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 125714671  230 FARKLGIIVEGNAIVVDKNQQTNLEGLFAAGDCTG-GFKQIATAVGQGALAGRKMIEYV 287
Cdd:TIGR01292 241 LLKGLLELDENGYIVTDEGMRTSVPGVFAAGDVRDkGYRQAVTAAGDGCIAALSAERYL 299
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 2-276 3.22e-34

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: 126.28  E-value: 3.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671    2 YDVIIIGKGPAGISASLYTVRANLKTLVIGKG------DSALKKAerIENYYGF-SEAINGERLLAEGEKQAARLGVEI- 73
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEgtcpygGCVLSKA--LLGAAEApEIASLWADLYKRKEEVVKKLNNGIe 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671   74 --IESEVISIEKNE--FFEVLTSDD---RYMAKAVLIATGQPQKKLRIENLEAFEGRGVSYCTTCDGFFYNNL--KVGVV 144
Cdd:pfam07992  79 vlLGTEVVSIDPGAkkVVLEELVDGdgeTITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLLpkRVVVV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671  145 GAGDYVVHEAMELLAFTKDITIYTNGNEL------QVSEKFVEAAKRFRISKKP---IYKIDGSEFLQKIFFKDGTSEDI 215
Cdd:pfam07992 159 GGGYIGVELAAALAKLGKEVTLIEALDRLlrafdeEISAALEKALEKNGVEVRLgtsVKEIIGDGDGVEVILKDGTEIDA 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 125714671  216 DGLFIAYESPSSVDFARKLGI-IVEGNAIVVDKNQQTNLEGLFAAGDCT-GGFKQIATAVGQG 276
Cdd:pfam07992 239 DLVVVAIGRRPNTELLEAAGLeLDERGGIVVDEYLRTSVPGIYAAGDCRvGGPELAQNAVAQG 301
PRK10262 PRK10262
thioredoxin reductase; Provisional
 4-293 1.51e-30

thioredoxin reductase; Provisional


Pssm-ID: 182343 [Multi-domain]  Cd Length: 321  Bit Score: 117.08  E-value: 1.51e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671   4 VIIIGKGPAGISASLYTVRANLKTLVIGKGDSA--LKKAERIENYYGFSEAINGERLLAEGEKQAARLGVEIIESEVISI 81
Cdd:PRK10262   9 LLILGSGPAGYTAAVYAARANLQPVLITGMEKGgqLTTTTEVENWPGDPNDLTGPLLMERMHEHATKFETEIIFDHINKV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671  82 E-KNEFFEVLTSDDRYMAKAVLIATGQPQKKLRIENLEAFEGRGVSYCTTCDGFFYNNLKVGVVGAGDYVVHEAMELLAF 160
Cdd:PRK10262  89 DlQNRPFRLTGDSGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNI 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671 161 TKDITIYTNGNELQVSEKF-------VEAAKRFRISKKPIYKIDGSEF-LQKIFFKDGTSED------IDGLFIAY-ESP 225
Cdd:PRK10262 169 ASEVHLIHRRDGFRAEKILikrlmdkVENGNIILHTNRTLEEVTGDQMgVTGVRLRDTQNSDniesldVAGLFVAIgHSP 248

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 125714671 226 SSVDFARKL----GII-----VEGNAivvdknQQTNLEGLFAAGDCTGG-FKQIATAVGQGALAGRKMIEYVRSLETA 293
Cdd:PRK10262 249 NTAIFEGQLelenGYIkvqsgIHGNA------TQTSIPGVFAAGDVMDHiYRQAITSAGTGCMAALDAERYLDGLADA 320
 
Name Accession Description Interval E-value
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
2-291 1.91e-92

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 276.23  E-value: 1.91e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671   2 YDVIIIGKGPAGISASLYTVRANLKTLVIGKGD--SALKKAERIENYYGFSEAINGERLLAEGEKQAARLGVEIIESEVI 79
Cdd:COG0492    1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEpgGQLATTKEIENYPGFPEGISGPELAERLREQAERFGAEILLEEVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671  80 SIEK-NEFFEVLTSD-DRYMAKAVLIATGQPQKKLRIENLEAFEGRGVSYCTTCDGFFYNNLKVGVVGAGDYVVHEAMEL 157
Cdd:COG0492   81 SVDKdDGPFRVTTDDgTEYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGKDVVVVGGGDSALEEALYL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671 158 LAFTKDITIYTNGNELQVSEKFVEAAKRFR----ISKKPIYKIDGSEFLQKIFFKDGTSE-----DIDGLFIAYESPSSV 228
Cdd:COG0492  161 TKFASKVTLIHRRDELRASKILVERLRANPkievLWNTEVTEIEGDGRVEGVTLKNVKTGeekelEVDGVFVAIGLKPNT 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 125714671 229 DFARKLGI-IVEGNAIVVDKNQQTNLEGLFAAGDCTGG-FKQIATAVGQGALAGRKMIEYVRSLE 291
Cdd:COG0492  241 ELLKGLGLeLDEDGYIVVDEDMETSVPGVFAAGDVRDYkYRQAATAAGEGAIAALSAARYLEPLK 305
TRX_reduct TIGR01292
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ...
 3-287 9.07e-73

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: 225.97  E-value: 9.07e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671    3 DVIIIGKGPAGISASLYTVRANLKTLVIGKGD--SALKKAERIENYYGFSEAINGERLLAEGEKQAARLGVEIIESEVIS 80
Cdd:TIGR01292   1 DVIIIGAGPAGLTAAIYAARANLKPLLIEGMEpgGQLTTTTEVENYPGFPEGISGPELMEKMKEQAVKFGAEIIYEEVIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671   81 IEK-NEFFEVLTSDDR-YMAKAVLIATGQPQKKLRIENLEAFEGRGVSYCTTCDGFFYNNLKVGVVGAGDYVVHEAMELL 158
Cdd:TIGR01292  81 VDKsDRPFKVYTGDGKeYTAKAVIIATGASARKLGIPGEDEFWGRGVSYCATCDGPFFKNKEVAVVGGGDSAIEEALYLT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671  159 AFTKDITIYTNGNELQVS----EKFVEAAKRFRISKKPIYKIDGSEFLQKIFFKDG-TSE----DIDGLFIAYESPSSVD 229
Cdd:TIGR01292 161 RIAKKVTLVHRRDKFRAEkillDRLKKNPKIEFLWNSTVEEIVGDNKVEGVKIKNTvTGEeeelEVDGVFIAIGHEPNTE 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 125714671  230 FARKLGIIVEGNAIVVDKNQQTNLEGLFAAGDCTG-GFKQIATAVGQGALAGRKMIEYV 287
Cdd:TIGR01292 241 LLKGLLELDENGYIVTDEGMRTSVPGVFAAGDVRDkGYRQAVTAAGDGCIAALSAERYL 299
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 2-276 3.22e-34

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: 126.28  E-value: 3.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671    2 YDVIIIGKGPAGISASLYTVRANLKTLVIGKG------DSALKKAerIENYYGF-SEAINGERLLAEGEKQAARLGVEI- 73
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEgtcpygGCVLSKA--LLGAAEApEIASLWADLYKRKEEVVKKLNNGIe 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671   74 --IESEVISIEKNE--FFEVLTSDD---RYMAKAVLIATGQPQKKLRIENLEAFEGRGVSYCTTCDGFFYNNL--KVGVV 144
Cdd:pfam07992  79 vlLGTEVVSIDPGAkkVVLEELVDGdgeTITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLLpkRVVVV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671  145 GAGDYVVHEAMELLAFTKDITIYTNGNEL------QVSEKFVEAAKRFRISKKP---IYKIDGSEFLQKIFFKDGTSEDI 215
Cdd:pfam07992 159 GGGYIGVELAAALAKLGKEVTLIEALDRLlrafdeEISAALEKALEKNGVEVRLgtsVKEIIGDGDGVEVILKDGTEIDA 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 125714671  216 DGLFIAYESPSSVDFARKLGI-IVEGNAIVVDKNQQTNLEGLFAAGDCT-GGFKQIATAVGQG 276
Cdd:pfam07992 239 DLVVVAIGRRPNTELLEAAGLeLDERGGIVVDEYLRTSVPGIYAAGDCRvGGPELAQNAVAQG 301
PRK10262 PRK10262
thioredoxin reductase; Provisional
 4-293 1.51e-30

thioredoxin reductase; Provisional


Pssm-ID: 182343 [Multi-domain]  Cd Length: 321  Bit Score: 117.08  E-value: 1.51e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671   4 VIIIGKGPAGISASLYTVRANLKTLVIGKGDSA--LKKAERIENYYGFSEAINGERLLAEGEKQAARLGVEIIESEVISI 81
Cdd:PRK10262   9 LLILGSGPAGYTAAVYAARANLQPVLITGMEKGgqLTTTTEVENWPGDPNDLTGPLLMERMHEHATKFETEIIFDHINKV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671  82 E-KNEFFEVLTSDDRYMAKAVLIATGQPQKKLRIENLEAFEGRGVSYCTTCDGFFYNNLKVGVVGAGDYVVHEAMELLAF 160
Cdd:PRK10262  89 DlQNRPFRLTGDSGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNI 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671 161 TKDITIYTNGNELQVSEKF-------VEAAKRFRISKKPIYKIDGSEF-LQKIFFKDGTSED------IDGLFIAY-ESP 225
Cdd:PRK10262 169 ASEVHLIHRRDGFRAEKILikrlmdkVENGNIILHTNRTLEEVTGDQMgVTGVRLRDTQNSDniesldVAGLFVAIgHSP 248

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 125714671 226 SSVDFARKL----GII-----VEGNAivvdknQQTNLEGLFAAGDCTGG-FKQIATAVGQGALAGRKMIEYVRSLETA 293
Cdd:PRK10262 249 NTAIFEGQLelenGYIkvqsgIHGNA------TQTSIPGVFAAGDVMDHiYRQAITSAGTGCMAALDAERYLDGLADA 320
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 2-280 8.70e-30

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 117.57  E-value: 8.70e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671   2 YDVIIIGKGPAGISASLYTVRANLKTLVIgkgdsalkkAER----------IENYYGFSEaINGERLLAEGEKQAARLGV 71
Cdd:PRK15317 212 YDVLVVGGGPAGAAAAIYAARKGIRTGIV---------AERfggqvldtmgIENFISVPE-TEGPKLAAALEEHVKEYDV 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671  72 EIIESE-VISIEKN-EFFEV-LTSDDRYMAKAVLIATGQPQKKLRIENLEAFEGRGVSYCTTCDGFFYNNLKVGVVGAGD 148
Cdd:PRK15317 282 DIMNLQrASKLEPAaGLIEVeLANGAVLKAKTVILATGARWRNMNVPGEDEYRNKGVAYCPHCDGPLFKGKRVAVIGGGN 361

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671 149 YVVHEAMELLAFTKDITIYTNGNELQVSEKFVEAAKrfriSKKPIYKI----------DGSEfLQKIFFKDGTSE----- 213
Cdd:PRK15317 362 SGVEAAIDLAGIVKHVTVLEFAPELKADQVLQDKLR----SLPNVTIItnaqttevtgDGDK-VTGLTYKDRTTGeehhl 436

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 125714671 214 DIDGLFIAYE-SPSSvDFarkLGIIVEGNA---IVVDKNQQTNLEGLFAAGDCTGG-FKQIATAVGQGALAG 280
Cdd:PRK15317 437 ELEGVFVQIGlVPNT-EW---LKGTVELNRrgeIIVDARGATSVPGVFAAGDCTTVpYKQIIIAMGEGAKAA 504
Pyr_redox_3 pfam13738
Pyridine nucleotide-disulphide oxidoreductase;
77-260 5.55e-12

Pyridine nucleotide-disulphide oxidoreductase;


Pssm-ID: 404603 [Multi-domain]  Cd Length: 296  Bit Score: 64.94  E-value: 5.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671   77 EVISIEKNE-FFEVLTSDDRYMAKAVLIATGQPQK--KLRIENLeafegrGVSYCTTCDGFFYNNLKVGVVGAGDYVVHE 153
Cdd:pfam13738  97 EVTSVKKEDdGFVVTTSKGTYQARYVIIATGEFDFpnKLGVPEL------PKHYSYVKDFHPYAGQKVVVIGGYNSAVDA 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671  154 AMELLAFTKDITIYTNGNELQVS-------------EKFVEAAKRFRI---SKKPIYKIDGSEFLQKIFFKDGTSEDIDG 217
Cdd:pfam13738 171 ALELVRKGARVTVLYRGSEWEDRdsdpsyslspdtlNRLEELVKNGKIkahFNAEVKEITEVDVSYKVHTEDGRKVTSND 250

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 125714671  218 LFIA---YEspSSVDFARKLGIIVEGNAIVV--DKNQQTNLEGLFAAG 260
Cdd:pfam13738 251 DPILatgYH--PDLSFLKKGLFELDEDGRPVltEETESTNVPGLFLAG 296
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 1-283 3.20e-10

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: 60.49  E-value: 3.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671   1 MYDVIIIGKGPAGISASLYTVRANLKTLVIGKGD-----------------------SALKKAERienyYGFS---EAIN 54
Cdd:COG1249    3 DYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGRlggtclnvgcipskallhaaevaHEARHAAE----FGISagaPSVD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671  55 GERLLA----------EG-EKQAARLGVEIIESEVISIEKNEFfeVLTSDDRYMAKAVLIATG-QPQkklRIENLEAFEG 122
Cdd:COG1249   79 WAALMArkdkvvdrlrGGvEELLKKNGVDVIRGRARFVDPHTV--EVTGGETLTADHIVIATGsRPR---VPPIPGLDEV 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671 123 RGVSYcttcDGFFynNLK-----VGVVGAGdYVvheAMEL----LAFTKDITIytngnelqvsekfVEAAKRfriskkPI 193
Cdd:COG1249  154 RVLTS----DEAL--ELEelpksLVVIGGG-YI---GLEFaqifARLGSEVTL-------------VERGDR------LL 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671 194 YKIDG--SEFLQKIFFKDG----TSEDI-------DGLFIAYESPSSVDFAR--------------------KLGIIV-E 239
Cdd:COG1249  205 PGEDPeiSEALEKALEKEGidilTGAKVtsvektgDGVTVTLEDGGGEEAVEadkvlvatgrrpntdglgleAAGVELdE 284

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 125714671 240 GNAIVVDKNQQTNLEGLFAAGDCTGGFkQIA-TAVGQGALAGRKM 283
Cdd:COG1249  285 RGGIKVDEYLRTSVPGIYAIGDVTGGP-QLAhVASAEGRVAAENI 328
PRK06116 PRK06116
glutathione reductase; Validated
 40-281 8.16e-10

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 59.01  E-value: 8.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671  40 AERIENY---YGFSEAING---ERLLAEGEKQAARL-----------GVEIIESEVISIEKNEffeVLTSDDRYMAKAVL 102
Cdd:PRK06116  60 AEAFHDYapgYGFDVTENKfdwAKLIANRDAYIDRLhgsyrnglennGVDLIEGFARFVDAHT---VEVNGERYTADHIL 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671 103 IATGQPQKKLRIEnleafegrGVSYCTTCDGFFYnnLK-----VGVVGAGdYV--------------------------- 150
Cdd:PRK06116 137 IATGGRPSIPDIP--------GAEYGITSDGFFA--LEelpkrVAVVGAG-YIavefagvlnglgsethlfvrgdaplrg 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671 151 --------VHEAMEllafTKDITIYTNgnelqvseKFVEAakrfrISKKPiykiDGSeflQKIFFKDGTSEDIDGLFIAY 222
Cdd:PRK06116 206 fdpdiretLVEEME----KKGIRLHTN--------AVPKA-----VEKNA----DGS---LTLTLEDGETLTVDCLIWAI 261

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 125714671 223 ESPSSVDfarKLGI------IVEGNAIVVDKNQQTNLEGLFAAGDCTGGFKQIATAVGQG-ALAGR 281
Cdd:PRK06116 262 GREPNTD---GLGLenagvkLNEKGYIIVDEYQNTNVPGIYAVGDVTGRVELTPVAIAAGrRLSER 324
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 56-281 1.28e-09

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: 58.28  E-value: 1.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671  56 ERLLAEGEKQAARLGVEII-ESEVISI--EKNEffeVLTSDDR---YmaKAVLIATG-QPqkklRIENLEAFEGRGVSYC 128
Cdd:COG0446   36 EDLLVRTPESFERKGIDVRtGTEVTAIdpEAKT---VTLRDGEtlsY--DKLVLATGaRP----RPPPIPGLDLPGVFTL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671 129 TTCDGFFY--------NNLKVGVVGAGdYVVHEAMEllAFTK---DITIYTNGNEL--QVSEKFVEAAK--------RFR 187
Cdd:COG0446  107 RTLDDADAlrealkefKGKRAVVIGGG-PIGLELAE--ALRKrglKVTLVERAPRLlgVLDPEMAALLEeelrehgvELR 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671 188 ISKKPIyKIDGSEFLqKIFFKDGTSEDIDGLFIAYESPSSVDFARKLGI-IVEGNAIVVDKNQQTNLEGLFAAGDCTGGF 266
Cdd:COG0446  184 LGETVV-AIDGDDKV-AVTLTDGEEIPADLVVVAPGVRPNTELAKDAGLaLGERGWIKVDETLQTSDPDVYAAGDCAEVP 261

                        250       260
                 ....*....|....*....|....*
gi 125714671 267 KQI----------ATAVGQGALAGR 281
Cdd:COG0446  262 HPVtgktvyiplaSAANKQGRVAAE 286
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 1-288 1.89e-09

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 57.88  E-value: 1.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671   1 MYDVIIIGKGPAGISASLYTVRANLKTLVIGKGD-----------------SALKKAERIENYYGF-----SEAINGERL 58
Cdd:PRK06292   3 KYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGPlggtclnvgcipskaliAAAEAFHEAKHAEEFgihadGPKIDFKKV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671  59 LAegEKQAARLG-VEIIESEVISIEKNEFF----------EVLTSDDRYMAKAVLIATGqpQKKLRIENLEAFEGRGvsY 127
Cdd:PRK06292  83 MA--RVRRERDRfVGGVVEGLEKKPKIDKIkgtarfvdpnTVEVNGERIEAKNIVIATG--SRVPPIPGVWLILGDR--L 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671 128 CTTCDGFFYNNL--KVGVVGAGdYVvheAMEL-LAFTK---DITIYTNGNEL------QVSEKFVEA-AKRFRIskKPIY 194
Cdd:PRK06292 157 LTSDDAFELDKLpkSLAVIGGG-VI---GLELgQALSRlgvKVTVFERGDRIlpledpEVSKQAQKIlSKEFKI--KLGA 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671 195 KIDGSEFLQKIFF----KDGTSEDI---------------DGLFIAyespssvdfarKLGIIV-EGNAIVVDKNQQTNLE 254
Cdd:PRK06292 231 KVTSVEKSGDEKVeeleKGGKTETIeadyvlvatgrrpntDGLGLE-----------NTGIELdERGRPVVDEHTQTSVP 299

                        330       340       350
                 ....*....|....*....|....*....|....
gi 125714671 255 GLFAAGDCTGGFKQIATAVGQGALAGRKMIEYVR 288
Cdd:PRK06292 300 GIYAAGDVNGKPPLLHEAADEGRIAAENAAGDVA 333
TIGR00275 TIGR00275
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ...
 5-106 8.29e-09

flavoprotein, HI0933 family; The model when searched with a partial length search brings in proteins with a dinucleotide-binding motif (Rossman fold) over the initial 40 residues of the model, including oxidoreductases and dehydrogenases. Partially characterized members include an FAD-binding protein from Bacillus cereus and flavoprotein HI0933 from Haemophilus influenzae. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272992 [Multi-domain]  Cd Length: 400  Bit Score: 56.07  E-value: 8.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671    5 IIIGKGPAGISASLYTVRANLKTLVIGKGDSALKK----------------AERIENYYG--------------FSEAIN 54
Cdd:TIGR00275   1 IIIGGGAAGLMAAITAARAGLSVLLLEKNKKIGKKllisgggrcnltnscpTPEFVAYYPrngkflrsalsrfsNKDLID 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 125714671   55 -----GERLLAE--G----------------EKQAARLGVEII-ESEVISIEKNEF-FEVLTSDDRYMAKAVLIATG 106
Cdd:TIGR00275  81 ffeslGLELKVEedGrvfpcsdsaadvldalLNELKELGVEILtNSKVKSIEKEDGgFGVETSGGEYEADKVIIATG 157
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 231-293 5.29e-08

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 53.64  E-value: 5.29e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 125714671 231 ARKLGIIVEGNAIVVDKNQQTNLEGLFAAGDCTGGFKQIATAVGQGALAGRKMIEYVRSLETA 293
Cdd:PRK11749 395 TPGLELNRWGTIIADDETGRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAEAIHEYLEGAASA 457
PTZ00058 PTZ00058
glutathione reductase; Provisional
 2-268 2.45e-07

glutathione reductase; Provisional


Pssm-ID: 185420 [Multi-domain]  Cd Length: 561  Bit Score: 51.93  E-value: 2.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671   2 YDVIIIGKGPAGISASLYTVRANLKTLVIGKGD-----------------SALKKAERIEN--YYGF--SEAINGERLLA 60
Cdd:PTZ00058  49 YDLIVIGGGSGGMAAARRAARNKAKVALVEKDYlggtcvnvgcvpkkimfNAASIHDILENsrHYGFdtQFSFNLPLLVE 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671  61 EGEKQAARL-----------GVEIIESE--VISIEKNEFFEVLTSDDRYMAKAVLIATGQPQKKLRIENLEAFEG----- 122
Cdd:PTZ00058 129 RRDKYIRRLndiyrqnlkkdNVEYFEGKgsLLSENQVLIKKVSQVDGEADESDDDEVTIVSAGVSQLDDGQVIEGknili 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671 123 -----------RGVSYCTTCDGFFY--NNLKVGVVGAGDYVVHEAMELLAFTKDITIYTNGNEL------QVSEKFVEAA 183
Cdd:PTZ00058 209 avgnkpifpdvKGKEFTISSDDFFKikEAKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLlrkfdeTIINELENDM 288

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671 184 KRFRIS------KKPIYKIDGSEFLqkIFFKDGTSEdIDGLFIAY---ESPSSVDFARK-LGIIVEGNAIVVDKNQQTNL 253
Cdd:PTZ00058 289 KKNNINiithanVEEIEKVKEKNLT--IYLSDGRKY-EHFDYVIYcvgRSPNTEDLNLKaLNIKTPKGYIKVDDNQRTSV 365

                        330
                 ....*....|....*
gi 125714671 254 EGLFAAGDCTGGFKQ 268
Cdd:PTZ00058 366 KHIYAVGDCCMVKKN 380
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
1-287 3.86e-07

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 50.91  E-value: 3.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671   1 MYDVIIIGKGPAGISAsLYTVRANLKT---LVIGkgdsalkkAERIENY------YGFSEAINGERLLAEGEKQAARLGV 71
Cdd:COG1251    1 KMRIVIIGAGMAGVRA-AEELRKLDPDgeiTVIG--------AEPHPPYnrpplsKVLAGETDEEDLLLRPADFYEENGI 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671  72 EII-ESEVISI---EKneffEVLTSDDR---YmaKAVLIATG-QPqKKLRIENLEAfegRGVsycttcdgFFYNNL---- 139
Cdd:COG1251   72 DLRlGTRVTAIdraAR----TVTLADGEtlpY--DKLVLATGsRP-RVPPIPGADL---PGV--------FTLRTLddad 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671 140 ----------KVGVVGAGdYVVHEAME-LLAFTKDITIYTNGNEL---QVSEkfvEAAKRFR----------ISKKPIYK 195
Cdd:COG1251  134 alraalapgkRVVVIGGG-LIGLEAAAaLRKRGLEVTVVERAPRLlprQLDE---EAGALLQrllealgvevRLGTGVTE 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671 196 IDGSEFLQKIFFKDGTSEDID------GLfiayeSPSsVDFARKLGIIVeGNAIVVDKNQQTNLEGLFAAGDCtggfkqi 269
Cdd:COG1251  210 IEGDDRVTGVRLADGEELPADlvvvaiGV-----RPN-TELARAAGLAV-DRGIVVDDYLRTSDPDIYAAGDC------- 275

                        330
                 ....*....|....*...
gi 125714671 270 atAVGQGALAGRKMIEYV 287
Cdd:COG1251  276 --AEHPGPVYGRRVLELV 291
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
 61-289 7.61e-07

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 49.99  E-value: 7.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671  61 EGEKQAARLGVEII-------ESEVISIEKNEFFEVLTSDDRYMAK--AVLIATGQPQ-KKLRI--ENLEA--------F 120
Cdd:PRK12770  73 EGVKELEEAGVVFHtrtkvccGEPLHEEEGDEFVERIVSLEELVKKydAVLIATGTWKsRKLGIpgEDLPGvysaleylF 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671 121 EGRGVSYCTTCDGFFYNNL--KVGVVGAG----DyVVHEAMELLAfTKDITIYTNG-----------NELQ--------- 174
Cdd:PRK12770 153 RIRAAKLGYLPWEKVPPVEgkKVVVVGAGltavD-AALEAVLLGA-EKVYLAYRRTineapagkyeiERLIargveflel 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671 175 ------VSEKFVEAAK--RFRISK-------KPIyKIDGSEFLqkiffkdgtsEDIDGLFIAY-ESPSSVDFARKLGI-I 237
Cdd:PRK12770 231 vtpvriIGEGRVEGVElaKMRLGEpdesgrpRPV-PIPGSEFV----------LEADTVVFAIgEIPTPPFAKECLGIeL 299

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 125714671 238 VEGNAIVVDKNQQTNLEGLFAAGDCTGGFKQIATAVGQGALAGRKMIEYVRS 289
Cdd:PRK12770 300 NRKGEIVVDEKHMTSREGVFAAGDVVTGPSKIGKAIKSGLRAAQSIHEWLDL 351
HI0933_like pfam03486
HI0933-like protein;
2-106 3.41e-06

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 47.96  E-value: 3.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671    2 YDVIIIGKGPAGISASLYTVRANLKTLVIGKGDSALKK------------------AERIENYYGfseaiNGERL----- 58
Cdd:pfam03486   1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLGRKilisgggrcnvtnlseepDNFLSRYPG-----NPKFLksals 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671   59 ---------LAEG---------------------------EKQAARLGVEII-ESEVISIEKNE--FFEVLTSDDRYMAK 99
Cdd:pfam03486  76 rftpwdfiaFFESlgvplkeedhgrlfpdsdkasdivdalLNELKELGVKIRlRTRVLSVEKDDdgRFRVKTGGEELEAD 155


                  ....*..
gi 125714671  100 AVLIATG 106
Cdd:pfam03486 156 SLVLATG 162
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 235-288 1.20e-05

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 46.41  E-value: 1.20e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 125714671 235 GIIVEGNAIVVDKNQQ-TNLEGLFAAGDCTGGFKQIATAVGQGALAGRKMIEYVR 288
Cdd:PRK12771 390 GVEVGRGVVQVDPNFMmTGRPGVFAGGDMVPGPRTVTTAIGHGKKAARNIDAFLG 444
PTZ00052 PTZ00052
thioredoxin reductase; Provisional
 87-283 3.82e-05

thioredoxin reductase; Provisional


Pssm-ID: 185416 [Multi-domain]  Cd Length: 499  Bit Score: 44.81  E-value: 3.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671  87 FEVLTSDDRYMAKAVLIATGqpqkkLRIENLEAFEGrGVSYCTTCDGFFYNNLKVG---VVGAgDYVvheAMELLAFTKD 163
Cdd:PTZ00052 134 YGDNSQEETITAKYILIATG-----GRPSIPEDVPG-AKEYSITSDDIFSLSKDPGktlIVGA-SYI---GLETAGFLNE 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671 164 I---------TIYTNGNELQVSEKFVEAAK----RFRISKKPIyKIDGSEFLQKIFFKDGTSEDIDGLFIAYESPSSVDF 230
Cdd:PTZ00052 204 LgfdvtvavrSIPLRGFDRQCSEKVVEYMKeqgtLFLEGVVPI-NIEKMDDKIKVLFSDGTTELFDTVLYATGRKPDIKG 282

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 125714671 231 AR--KLGIIVEGNAIVVDKNQQTNLEGLFAAGDCTGGFKQIA-TAVGQGALAGRKM 283
Cdd:PTZ00052 283 LNlnAIGVHVNKSNKIIAPNDCTNIPNIFAVGDVVEGRPELTpVAIKAGILLARRL 338
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 224-286 5.54e-05

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: 44.36  E-value: 5.54e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 125714671 224 SPSSVDFARKLGIIVEGN-AIVVDK-NQQTNLEGLFAAGDCTGGFKQIATAVGQGALAGRKMIEY 286
Cdd:COG0493  370 TPDPSGLEEELGLELDKRgTIVVDEeTYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAIDRY 434
glycerol3P_GlpB TIGR03378
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are ...
 2-37 6.29e-05

glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are the B subunit, product of the glpB gene, of a three-subunit, membrane-anchored, FAD-dependent anaerobic glycerol-3-phosphate dehydrogenase. [Energy metabolism, Anaerobic]


Pssm-ID: 213807  Cd Length: 419  Bit Score: 44.24  E-value: 6.29e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 125714671    2 YDVIIIGKGPAGISASLYTVRANLKTLVIGKGDSAL 37
Cdd:TIGR03378   1 FDVIIIGGGLAGLSCALRLAEAGKKCAIIAAGQSAL 36
PRK05329 PRK05329
glycerol-3-phosphate dehydrogenase subunit GlpB;
1-37 7.48e-05

glycerol-3-phosphate dehydrogenase subunit GlpB;


Pssm-ID: 235412  Cd Length: 422  Bit Score: 43.69  E-value: 7.48e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 125714671   1 MYDVIIIGKGPAGISASLYTVRANLKTLVIGKGDSAL 37
Cdd:PRK05329   2 KFDVLVIGGGLAGLTAALAAAEAGKRVALVAKGQGAL 38
COG2509 COG2509
FAD-dependent dehydrogenase [General function prediction only];
1-33 8.10e-05

FAD-dependent dehydrogenase [General function prediction only];


Pssm-ID: 441999 [Multi-domain]  Cd Length: 466  Bit Score: 43.95  E-value: 8.10e-05
                         10        20        30
                 ....*....|....*....|....*....|...
gi 125714671   1 MYDVIIIGKGPAGISASLYTVRANLKTLVIGKG 33
Cdd:COG2509   30 KYDVVIVGAGPAGLFAALELAEAGLKPLVLERG 62
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
 20-277 1.32e-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: 43.04  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671   20 TVRANLKTLVIGKGDSALKkaerIENYYgfseaingERLLAEGEKQAARLGVEIIESEVISIEKNEFFEVLTSDDRYMAK 99
Cdd:TIGR01423  86 SVKANWKALIAAKNKAVLD----INKSY--------EGMFADTEGLTFFLGWGALEDKNVVLVRESADPKSAVKERLQAE 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671  100 AVLIATGQPQKKLRIEnleafegrGVSYCTTCDGFFYNN---LKVGVVGAGDYVVHEAMELLAFTK---DITIYTNGNEL 173
Cdd:TIGR01423 154 HILLATGSWPQMLGIP--------GIEHCISSNEAFYLDeppRRVLTVGGGFISVEFAGIFNAYKPrggKVTLCYRNNMI 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671  174 ----------QVSEKFVEAAKRFRISKKPIyKI----DGSeflQKIFFKDGTSEDIDGLFIAY-ESPSSVDFA-RKLGII 237
Cdd:TIGR01423 226 lrgfdstlrkELTKQLRANGINIMTNENPA-KVtlnaDGS---KHVTFESGKTLDVDVVMMAIgRVPRTQTLQlDKVGVE 301

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 125714671  238 VEGN-AIVVDKNQQTNLEGLFAAGDCTGGFKQIATAVGQGA 277
Cdd:TIGR01423 302 LTKKgAIQVDEFSRTNVPNIYAIGDVTDRVMLTPVAINEGA 342
sdhA PRK08641
succinate dehydrogenase flavoprotein subunit; Reviewed
 245-297 1.69e-04

succinate dehydrogenase flavoprotein subunit; Reviewed


Pssm-ID: 236319 [Multi-domain]  Cd Length: 589  Bit Score: 43.04  E-value: 1.69e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 125714671 245 VDKNQQTNLEGLFAAGDCT----G----GFKQIATAVGQGALAGRKMIEYVRSLETANSPV 297
Cdd:PRK08641 360 VDYDQMTNIPGLFAAGECDysyhGanrlGANSLLSAIYGGMVAGPNAVEYIKGLGKSADDV 420
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 1-286 1.94e-04

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 42.44  E-value: 1.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671   1 MYDVIIIGKGPAGISASLYTVRANLKTLVIGKGD--------------SALKKAERIENY-----YGFS--------EAI 53
Cdd:PRK06416   4 EYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKlggtclnrgcipskALLHAAERADEArhsedFGIKaenvgidfKKV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671  54 NG------ERLLAEGEKQAARLGVEIIESEViSIEKNEFFEVLT--SDDRYMAKAVLIATG-QPQkklRIENLEaFEGRG 124
Cdd:PRK06416  84 QEwkngvvNRLTGGVEGLLKKNKVDIIRGEA-KLVDPNTVRVMTedGEQTYTAKNIILATGsRPR---ELPGIE-IDGRV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671 125 VsycTTCDG----------------------F--FYNNL--KVGVVgagdyvvhEAMELL--AFTKDITiytngnelqvs 176
Cdd:PRK06416 159 I---WTSDEalnldevpkslvvigggyigveFasAYASLgaEVTIV--------EALPRIlpGEDKEIS----------- 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671 177 eKFVEaaKRFRisKKpiykidGSEFLQKIFFKdGTSEDIDGLFIAYES---PSSVDFAR-----------------KLGI 236
Cdd:PRK06416 217 -KLAE--RALK--KR------GIKIKTGAKAK-KVEQTDDGVTVTLEDggkEETLEADYvlvavgrrpntenlgleELGV 284

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 125714671 237 IVEGNAIVVDKNQQTNLEGLFAAGDCTGGFkQIA-TAVGQG-----ALAGRKM-IEY 286
Cdd:PRK06416 285 KTDRGFIEVDEQLRTNVPNIYAIGDIVGGP-MLAhKASAEGiiaaeAIAGNPHpIDY 340
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
57-106 4.15e-04

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 41.43  E-value: 4.15e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 125714671  57 RLLAEGEKQAAR-LGVEIIE-SEVISIEK--NEFFEVLTSDDRYMAKAVLIATG 106
Cdd:COG0665  151 AKLVRALARAARaAGVRIREgTPVTGLERegGRVTGVRTERGTVRADAVVLAAG 204
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
 190-297 5.08e-04

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 41.64  E-value: 5.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671 190 KKPIyKIDGSEF-LQKIFFKDGTSEDIDglfiayespSSVDFARKLGIIVEGNAIVVDKNQQTNLEGLFAAGDCTGGFKQ 268
Cdd:PRK12814 412 RRPV-PVEGSEFtLQADTVISAIGQQVD---------PPIAEAAGIGTSRNGTVKVDPETLQTSVAGVFAGGDCVTGADI 481

                         90       100
                 ....*....|....*....|....*....
gi 125714671 269 IATAVGQGALAGRKMIEYVRSLETANSPV 297
Cdd:PRK12814 482 AINAVEQGKRAAHAIDLFLNGKPVTAPVQ 510
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 2-34 7.89e-04

geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273936 [Multi-domain]  Cd Length: 295  Bit Score: 40.38  E-value: 7.89e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 125714671    2 YDVIIIGKGPAGISASLYTVRANLKTLVIGKGD 34
Cdd:TIGR02032   1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEKKS 33
GlpB COG3075
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
2-37 8.43e-04

Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];


Pssm-ID: 442309  Cd Length: 415  Bit Score: 40.55  E-value: 8.43e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 125714671   2 YDVIIIGKGPAGISASLYTVRANLKTLVIGKGDSAL 37
Cdd:COG3075    3 FDVVVIGGGLAGLTAAIRAAEAGLRVAIVSAGQSAL 38
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 224-286 9.57e-04

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 40.53  E-value: 9.57e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 125714671 224 SPSSVDFARKLGIIVE--GNAIVVDKNQQTNLEGLFAAGDCTGGFKQIATAVGQGALAGRKMIEY 286
Cdd:PRK12810 399 TGPEAGLLAQFGVELDerGRVAAPDNAYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAIDAY 463
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
10-106 1.79e-03

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 39.18  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671  10 GPAGISASLYTVRANLKTLVIGK---------GDSALKKAERIENYYGFSEA----INGERLLAEGEK------------ 64
Cdd:COG0644    2 GPAGSAAARRLARAGLSVLLLEKgsfpgdkicGGGLLPRALEELEPLGLDEPlerpVRGARFYSPGGKsvelppgrgggy 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 125714671  65 -------------QAARLGVEIIE-SEVISIEKNE-FFEVLTSDDR-YMAKAVLIATG 106
Cdd:COG0644   82 vvdrarfdrwlaeQAEEAGAEVRTgTRVTDVLRDDgRVVVRTGDGEeIRADYVVDADG 139
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 241-289 7.33e-03

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


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 37.80  E-value: 7.33e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 125714671 241 NAIVVDKNQQTNLEGLFAAGDCTGGFKQIATAVGQGALAGRKMIEYVRS 289
Cdd:PRK12778 703 GTIVVDEEMQSSIPGIYAGGDIVRGGATVILAMGDGKRAAAAIDEYLSS 751
PRK06854 PRK06854
adenylyl-sulfate reductase subunit alpha;
247-288 7.58e-03

adenylyl-sulfate reductase subunit alpha;


Pssm-ID: 235879 [Multi-domain]  Cd Length: 608  Bit Score: 37.59  E-value: 7.58e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 125714671 247 KNQQTNLEGLFAAGDCTGG--FKQIATAVGQGALAGRKMIEYVR 288
Cdd:PRK06854 389 YNRMTTVEGLFAAGDVVGGspHKFSSGSFAEGRIAAKAAVRYIL 432
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 1-30 7.97e-03

Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 37.52  E-value: 7.97e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 125714671   1 MYDVIIIGKGPAGISASLYTVRANLKTLVI 30
Cdd:COG1233    3 MYDVVVIGAGIGGLAAAALLARAGYRVTVL 32
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 3-35 8.38e-03

FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.


Pssm-ID: 395718 [Multi-domain]  Cd Length: 398  Bit Score: 37.27  E-value: 8.38e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 125714671    3 DVIIIGKGPAGISASLYTVRANLKTLVIGKGDS 35
Cdd:pfam00890   1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQP 33
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 3-34 8.96e-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: 37.20  E-value: 8.96e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 125714671    3 DVIIIGKGPAGISASLYTVRANLKTLVIGKGD 34
Cdd:pfam12831   1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRG 32
PRK07251 PRK07251
FAD-containing oxidoreductase;
2-265 9.27e-03

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 37.42  E-value: 9.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671   2 YDVIIIGKGPAGisaslytvranlKTLViGKGDSALKKAERIEN---YYG-----------------------FSEAING 55
Cdd:PRK07251   4 YDLIVIGFGKAG------------KTLA-AKLASAGKKVALVEEskaMYGgtcinigciptktllvaaeknlsFEQVMAT 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671  56 E-----RLLAEGEKQAARLGVEIIESEViSIEKNEFFEVLTSDDRYM--AKAVLIATGQPQKKLRIENLEafEGRGVSYC 128
Cdd:PRK07251  71 KntvtsRLRGKNYAMLAGSGVDLYDAEA-HFVSNKVIEVQAGDEKIEltAETIVINTGAVSNVLPIPGLA--DSKHVYDS 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125714671 129 TTCDGFFYNNLKVGVVGAGDYVVHEAMELLAFTKDITIYTNGNEL--QVSEKFVEAAKRFriskkpiYKIDGSEFLQKIF 206
Cdd:PRK07251 148 TGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTIlpREEPSVAALAKQY-------MEEDGITFLLNAH 220

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 125714671 207 FKDGTSEDIDGLFIAYESPSSVD-----FARK-----LGI------IVEGNAIVVDKNQQTNLEGLFAAGDCTGG 265
Cdd:PRK07251 221 TTEVKNDGDQVLVVTEDETYRFDallyaTGRKpntepLGLentdieLTERGAIKVDDYCQTSVPGVFAVGDVNGG 295
 
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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