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Conserved domains on  [gi|38569921|gb|AAR24491|]
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thioredoxin reductase [uncultured crenarchaeote DeepAnt-EC39]

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

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List of domain hits

 Name Accession Description Interval E-value
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
4-303 7.68e-99

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


:

Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 293.56  E-value: 7.68e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921   4 FEIVIVGAGPAGLSAGMYVARQNVSCLVISKD-LGGQMNLIPKLENYPGTIMS-SGQILAKTLETQYLSFKGEIVYDTVE 81
Cdd:COG0492   1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGePGGQLATTKEIENYPGFPEGiSGPELAERLREQAERFGAEILLEEVT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921  82 KIDESEDGFKIKTTR-SEYKAKAIVLAPGKVPNMLGVENESEYFNKGIHYCTKCDAPFYQGRITASVGVGSYLVESGLLL 160
Cdd:COG0492  81 SVDKDDGPFRVTTDDgTEYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGKDVVVVGGGDSALEEALYL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921 161 SRMASKMYLILKGSKLAGDKDLVTTLENNKNIEIITQSSVKSISGNSTLQQITLVDS-SGSEKVLDVDALFIELGSKINL 239
Cdd:COG0492 161 TKFASKVTLIHRRDELRASKILVERLRANPKIEVLWNTEVTEIEGDGRVEGVTLKNVkTGEEKELEVDGVFVAIGLKPNT 240

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38569921 240 DYVKHL-VKINTKGEIEIESGGMTSHPAIFAAGDATTIPYKQIIVACGDGSNAGLSAFNYLEKLK 303
Cdd:COG0492 241 ELLKGLgLELDEDGYIVVDEDMETSVPGVFAAGDVRDYKYRQAATAAGEGAIAALSAARYLEPLK 305
 
Name Accession Description Interval E-value
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
4-303 7.68e-99

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 293.56  E-value: 7.68e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921   4 FEIVIVGAGPAGLSAGMYVARQNVSCLVISKD-LGGQMNLIPKLENYPGTIMS-SGQILAKTLETQYLSFKGEIVYDTVE 81
Cdd:COG0492   1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGePGGQLATTKEIENYPGFPEGiSGPELAERLREQAERFGAEILLEEVT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921  82 KIDESEDGFKIKTTR-SEYKAKAIVLAPGKVPNMLGVENESEYFNKGIHYCTKCDAPFYQGRITASVGVGSYLVESGLLL 160
Cdd:COG0492  81 SVDKDDGPFRVTTDDgTEYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGKDVVVVGGGDSALEEALYL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921 161 SRMASKMYLILKGSKLAGDKDLVTTLENNKNIEIITQSSVKSISGNSTLQQITLVDS-SGSEKVLDVDALFIELGSKINL 239
Cdd:COG0492 161 TKFASKVTLIHRRDELRASKILVERLRANPKIEVLWNTEVTEIEGDGRVEGVTLKNVkTGEEKELEVDGVFVAIGLKPNT 240

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38569921 240 DYVKHL-VKINTKGEIEIESGGMTSHPAIFAAGDATTIPYKQIIVACGDGSNAGLSAFNYLEKLK 303
Cdd:COG0492 241 ELLKGLgLELDEDGYIVVDEDMETSVPGVFAAGDVRDYKYRQAATAAGEGAIAALSAARYLEPLK 305
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 4-299 2.97e-60

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 200.77  E-value: 2.97e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921    4 FEIVIVGAGPAGLSAGMYVARQNVSCLVISKDLGGQMNLIPKLENYPGTIMSSGQILAKTLETQYLSFKGEIV-YDTVEK 82
Cdd:PRK15317 212 YDVLVVGGGPAGAAAAIYAARKGIRTGIVAERFGGQVLDTMGIENFISVPETEGPKLAAALEEHVKEYDVDIMnLQRASK 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921   83 IDESEDGFKIKTTRSE-YKAKAIVLAPGKVPNMLGVENESEYFNKGIHYCTKCDAPFYQGRITASVGVGSYLVESGLLLS 161
Cdd:PRK15317 292 LEPAAGLIEVELANGAvLKAKTVILATGARWRNMNVPGEDEYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLA 371

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921  162 RMASKMYLILKGSKLAGDKDLVTTLENNKNIEIITQSSVKSISGNST-LQQITLVD-SSGSEKVLDVDALFIELGSKINL 239
Cdd:PRK15317 372 GIVKHVTVLEFAPELKADQVLQDKLRSLPNVTIITNAQTTEVTGDGDkVTGLTYKDrTTGEEHHLELEGVFVQIGLVPNT 451

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921  240 DYVKHLVKINTKGEIEIESGGMTSHPAIFAAGDATTIPYKQIIVACGDGSNAGLSAFNYL 299
Cdd:PRK15317 452 EWLKGTVELNRRGEIIVDARGATSVPGVFAAGDCTTVPYKQIIIAMGEGAKAALSAFDYL 511
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 4-288 3.30e-30

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: 116.26  E-value: 3.30e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921     4 FEIVIVGAGPAGLSAGMYVARQNVSCLVISKD---LGGQMNLIPKLENYPGT--IMSSGQILAKTLETQYLSFKGEIVY- 77
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEgtcPYGGCVLSKALLGAAEApeIASLWADLYKRKEEVVKKLNNGIEVl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921    78 --DTVEKIDESEDGFKIKTTRS----EYKAKAIVLAPGKVPNMLGVENESEYFNKGIHYCTKCDAPFYQ---GRItASVG 148
Cdd:pfam07992  81 lgTEVVSIDPGAKKVVLEELVDgdgeTITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKllpKRV-VVVG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921   149 vGSYL-VESGLLLSRMASKMYLILKGSKLAGDKD-----LVTTLENNKNIEIITQSSVKSISGNSTLQQITLvdssGSEK 222
Cdd:pfam07992 160 -GGYIgVELAAALAKLGKEVTLIEALDRLLRAFDeeisaALEKALEKNGVEVRLGTSVKEIIGDGDGVEVIL----KDGT 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38569921   223 VLDVDALFIELGSKINLDYVKHL-VKINTKGEIEIESGGMTSHPAIFAAGDATTIPYKQIIVACGDG 288
Cdd:pfam07992 235 EIDADLVVVAIGRRPNTELLEAAgLELDERGGIVVDEYLRTSVPGIYAAGDCRVGGPELAQNAVAQG 301
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
 100-274 3.80e-06

trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase.


Pssm-ID: 200098 [Multi-domain]  Cd Length: 486  Bit Score: 48.05  E-value: 3.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921   100 KAKAIVLAPGKVPNMLGVEneseyfnkGIHYCTKCDAPFY---QGRITASVGVGSYLVE-SGLLLS--------RMASKM 167
Cdd:TIGR01423 151 QAEHILLATGSWPQMLGIP--------GIEHCISSNEAFYldePPRRVLTVGGGFISVEfAGIFNAykprggkvTLCYRN 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921   168 YLILKGSKLAGDKDLVTTLENNkNIEIITQSSVKSISGNSTLQQITLVDSSgseKVLDVDALFIELG-----SKINLDYV 242
Cdd:TIGR01423 223 NMILRGFDSTLRKELTKQLRAN-GINIMTNENPAKVTLNADGSKHVTFESG---KTLDVDVVMMAIGrvprtQTLQLDKV 298

                         170       180       190
                  ....*....|....*....|....*....|..
gi 38569921   243 KhlVKINTKGEIEIESGGMTSHPAIFAAGDAT 274
Cdd:TIGR01423 299 G--VELTKKGAIQVDEFSRTNVPNIYAIGDVT 328
 
Name Accession Description Interval E-value
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
4-303 7.68e-99

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 293.56  E-value: 7.68e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921   4 FEIVIVGAGPAGLSAGMYVARQNVSCLVISKD-LGGQMNLIPKLENYPGTIMS-SGQILAKTLETQYLSFKGEIVYDTVE 81
Cdd:COG0492   1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGePGGQLATTKEIENYPGFPEGiSGPELAERLREQAERFGAEILLEEVT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921  82 KIDESEDGFKIKTTR-SEYKAKAIVLAPGKVPNMLGVENESEYFNKGIHYCTKCDAPFYQGRITASVGVGSYLVESGLLL 160
Cdd:COG0492  81 SVDKDDGPFRVTTDDgTEYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGKDVVVVGGGDSALEEALYL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921 161 SRMASKMYLILKGSKLAGDKDLVTTLENNKNIEIITQSSVKSISGNSTLQQITLVDS-SGSEKVLDVDALFIELGSKINL 239
Cdd:COG0492 161 TKFASKVTLIHRRDELRASKILVERLRANPKIEVLWNTEVTEIEGDGRVEGVTLKNVkTGEEKELEVDGVFVAIGLKPNT 240

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38569921 240 DYVKHL-VKINTKGEIEIESGGMTSHPAIFAAGDATTIPYKQIIVACGDGSNAGLSAFNYLEKLK 303
Cdd:COG0492 241 ELLKGLgLELDEDGYIVVDEDMETSVPGVFAAGDVRDYKYRQAATAAGEGAIAALSAARYLEPLK 305
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 4-299 2.97e-60

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 200.77  E-value: 2.97e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921    4 FEIVIVGAGPAGLSAGMYVARQNVSCLVISKDLGGQMNLIPKLENYPGTIMSSGQILAKTLETQYLSFKGEIV-YDTVEK 82
Cdd:PRK15317 212 YDVLVVGGGPAGAAAAIYAARKGIRTGIVAERFGGQVLDTMGIENFISVPETEGPKLAAALEEHVKEYDVDIMnLQRASK 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921   83 IDESEDGFKIKTTRSE-YKAKAIVLAPGKVPNMLGVENESEYFNKGIHYCTKCDAPFYQGRITASVGVGSYLVESGLLLS 161
Cdd:PRK15317 292 LEPAAGLIEVELANGAvLKAKTVILATGARWRNMNVPGEDEYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLA 371

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921  162 RMASKMYLILKGSKLAGDKDLVTTLENNKNIEIITQSSVKSISGNST-LQQITLVD-SSGSEKVLDVDALFIELGSKINL 239
Cdd:PRK15317 372 GIVKHVTVLEFAPELKADQVLQDKLRSLPNVTIITNAQTTEVTGDGDkVTGLTYKDrTTGEEHHLELEGVFVQIGLVPNT 451

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921  240 DYVKHLVKINTKGEIEIESGGMTSHPAIFAAGDATTIPYKQIIVACGDGSNAGLSAFNYL 299
Cdd:PRK15317 452 EWLKGTVELNRRGEIIVDARGATSVPGVFAAGDCTTVPYKQIIIAMGEGAKAALSAFDYL 511
PRK10262 PRK10262
thioredoxin reductase; Provisional
 5-302 1.67e-39

thioredoxin reductase; Provisional


Pssm-ID: 182343 [Multi-domain]  Cd Length: 321  Bit Score: 141.35  E-value: 1.67e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921    5 EIVIVGAGPAGLSAGMYVARQNVS-CLVISKDLGGQMNLIPKLENYPGTIMS-SGQILAKTLETQYLSFKGEIVYDTVEK 82
Cdd:PRK10262   8 KLLILGSGPAGYTAAVYAARANLQpVLITGMEKGGQLTTTTEVENWPGDPNDlTGPLLMERMHEHATKFETEIIFDHINK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921   83 IDESEDGFKIKTTRSEYKAKAIVLAPGKVPNMLGVENESEYFNKGIHYCTKCDAPFYQGRITASVGVGSYLVESGLLLSR 162
Cdd:PRK10262  88 VDLQNRPFRLTGDSGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSN 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921  163 MASKMYLILKGSKLAGDKDLVTTLEN---NKNIEIITQSSVKSISGNST-LQQITLVDSSGSEKV--LDVDALFIELGSK 236
Cdd:PRK10262 168 IASEVHLIHRRDGFRAEKILIKRLMDkveNGNIILHTNRTLEEVTGDQMgVTGVRLRDTQNSDNIesLDVAGLFVAIGHS 247

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38569921  237 INLDYVKHLVKINTkGEIEIESG-----GMTSHPAIFAAGDATTIPYKQIIVACGDGSNAGLSAFNYLEKL 302
Cdd:PRK10262 248 PNTAIFEGQLELEN-GYIKVQSGihgnaTQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYLDGL 317
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 4-288 3.30e-30

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: 116.26  E-value: 3.30e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921     4 FEIVIVGAGPAGLSAGMYVARQNVSCLVISKD---LGGQMNLIPKLENYPGT--IMSSGQILAKTLETQYLSFKGEIVY- 77
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEgtcPYGGCVLSKALLGAAEApeIASLWADLYKRKEEVVKKLNNGIEVl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921    78 --DTVEKIDESEDGFKIKTTRS----EYKAKAIVLAPGKVPNMLGVENESEYFNKGIHYCTKCDAPFYQ---GRItASVG 148
Cdd:pfam07992  81 lgTEVVSIDPGAKKVVLEELVDgdgeTITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKllpKRV-VVVG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921   149 vGSYL-VESGLLLSRMASKMYLILKGSKLAGDKD-----LVTTLENNKNIEIITQSSVKSISGNSTLQQITLvdssGSEK 222
Cdd:pfam07992 160 -GGYIgVELAAALAKLGKEVTLIEALDRLLRAFDeeisaALEKALEKNGVEVRLGTSVKEIIGDGDGVEVIL----KDGT 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38569921   223 VLDVDALFIELGSKINLDYVKHL-VKINTKGEIEIESGGMTSHPAIFAAGDATTIPYKQIIVACGDG 288
Cdd:pfam07992 235 EIDADLVVVAIGRRPNTELLEAAgLELDERGGIVVDEYLRTSVPGIYAAGDCRVGGPELAQNAVAQG 301
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 1-277 1.82e-14

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 73.67  E-value: 1.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921    1 MQEFEIVIVGAGPAGLSAGMYVARQNVSCLVISKD-LGG------------------QMNLIPKLE----NYPGTIMSSG 57
Cdd:PRK06292   1 MEKYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGpLGGtclnvgcipskaliaaaeAFHEAKHAEefgiHADGPKIDFK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921   58 QILAKTLETQYLSFKGeiVYDTVEKIDEsEDGFK----------IKTTRSEYKAKAIVLAPG-KVPNMLGVENEseyfnK 126
Cdd:PRK06292  81 KVMARVRRERDRFVGG--VVEGLEKKPK-IDKIKgtarfvdpntVEVNGERIEAKNIVIATGsRVPPIPGVWLI-----L 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921  127 GIHYCTKcDAPFYQGRITASVGV--GSYL-VESGLLLSRMASKMYLILKGSKLAG--DKDLVTTLEN--NKNIEIITQSS 199
Cdd:PRK06292 153 GDRLLTS-DDAFELDKLPKSLAVigGGVIgLELGQALSRLGVKVTVFERGDRILPleDPEVSKQAQKilSKEFKIKLGAK 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921  200 VKSISGNSTlQQITLVDSSGSEKVLDVDALFIELGSKINLDY--VKHL-VKINTKGEIEIESGGMTSHPAIFAAGDATTI 276
Cdd:PRK06292 232 VTSVEKSGD-EKVEELEKGGKTETIEADYVLVATGRRPNTDGlgLENTgIELDERGRPVVDEHTQTSVPGIYAAGDVNGK 310


                 .
gi 38569921  277 P 277
Cdd:PRK06292 311 P 311
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 1-274 7.06e-11

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: 62.80  E-value: 7.06e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921   1 MQEFEIVIVGAGPAGLSAGMYVARQNVSCLVISKD-LGG------------------QMNLIPKLENYpGTIMSSGQI-L 60
Cdd:COG1249   1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGrLGGtclnvgcipskallhaaeVAHEARHAAEF-GISAGAPSVdW 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921  61 AKTLEtqylsFKGEIVYDTVEKIDESEDGFKIK----------------TTRSEYKAKAIVLAPGKVPNMLGVENESEyf 124
Cdd:COG1249  80 AALMA-----RKDKVVDRLRGGVEELLKKNGVDvirgrarfvdphtvevTGGETLTADHIVIATGSRPRVPPIPGLDE-- 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921 125 nkgIHYCTKCDApFYQGRITASVGV--GSYL-VESGLLLSRMASKMYLILKGSKLAG--DKDLVTTLEN---NKNIEIIT 196
Cdd:COG1249 153 ---VRVLTSDEA-LELEELPKSLVVigGGYIgLEFAQIFARLGSEVTLVERGDRLLPgeDPEISEALEKaleKEGIDILT 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921 197 QSSVKSISGNStlQQITL-VDSSGSEKVLDVDALFIELGSK-----INLDYVKhlVKINTKGEIEIESGGMTSHPAIFAA 270
Cdd:COG1249 229 GAKVTSVEKTG--DGVTVtLEDGGGEEAVEADKVLVATGRRpntdgLGLEAAG--VELDERGGIKVDEYLRTSVPGIYAI 304


                ....
gi 38569921 271 GDAT 274
Cdd:COG1249 305 GDVT 308
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 8-291 4.21e-10

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: 60.15  E-value: 4.21e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921   8 IVGAGPAGLSAGMYVARQNVSCLVISKD--LGGqMNL--IP--KLENypgtimssgQILAKtlETQYLSFKG-EIVYDTv 80
Cdd:COG0493 126 VVGSGPAGLAAAYQLARAGHEVTVFEALdkPGG-LLRygIPefRLPK---------DVLDR--EIELIEALGvEFRTNV- 192

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921  81 eKIDESedgFKIKTTRSEYKAkaIVLAPG-KVPNMLGVENESEyfnKGIHYCTkcdapfyqgritasvgvgSYLVEsgll 159
Cdd:COG0493 193 -EVGKD---ITLDELLEEFDA--VFLATGaGKPRDLGIPGEDL---KGVHSAM------------------DFLTA---- 241

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921 160 LSRMASKMYLILKG------------------SKLAGDKDlVT-----TLENNK------------NIEIITQSSVKSIS 204
Cdd:COG0493 242 VNLGEAPDTILAVGkrvvvigggntamdcartALRLGAES-VTivyrrTREEMPaskeeveealeeGVEFLFLVAPVEII 320

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921 205 GNS-------TLQQITLV--DSSG---------SEKVLDVDALFIELGSKINLDYVKHL--VKINTKGEIEIESG-GMTS 263
Cdd:COG0493 321 GDEngrvtglECVRMELGepDESGrrrpvpiegSEFTLPADLVILAIGQTPDPSGLEEElgLELDKRGTIVVDEEtYQTS 400

                       330       340
                ....*....|....*....|....*...
gi 38569921 264 HPAIFAAGDATTIPyKQIIVACGDGSNA 291
Cdd:COG0493 401 LPGVFAGGDAVRGP-SLVVWAIAEGRKA 427
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
 4-301 5.21e-08

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 53.84  E-value: 5.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921    4 FEIVIVGAGPAGLSAGMYVArqnvsCLviskdlGGQMNLIPKLEnYPGTIMSSG---------QILA--KTLETQYLSFK 72
Cdd:PRK12770  19 KKVAIIGAGPAGLAAAGYLA-----CL------GYEVHVYDKLP-EPGGLMLFGipefripieRVREgvKELEEAGVVFH 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921   73 GEI-VYDTVEKIDESEDGF-----KIKTTRSEYKAkaIVLAPG-------KVP--NMLGVENESEYFNKgIH-----YCT 132
Cdd:PRK12770  87 TRTkVCCGEPLHEEEGDEFverivSLEELVKKYDA--VLIATGtwksrklGIPgeDLPGVYSALEYLFR-IRaaklgYLP 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921  133 KCDAPFYQGRITASVGVGSYLV---ESGLLLSrmASKMYLILKGSK---LAGDKDL-------VTTLENNKNIEIITQSS 199
Cdd:PRK12770 164 WEKVPPVEGKKVVVVGAGLTAVdaaLEAVLLG--AEKVYLAYRRTIneaPAGKYEIerliargVEFLELVTPVRIIGEGR 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921  200 VKSISgnstLQQITLVDSS-----------GSEKVLDVDALFIELG----SKINLDYVKhlVKINTKGEIEIESGGMTSH 264
Cdd:PRK12770 242 VEGVE----LAKMRLGEPDesgrprpvpipGSEFVLEADTVVFAIGeiptPPFAKECLG--IELNRKGEIVVDEKHMTSR 315

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 38569921  265 PAIFAAGDATTIPYKqIIVACGDGSNAGLSAFNYLEK 301
Cdd:PRK12770 316 EGVFAAGDVVTGPSK-IGKAIKSGLRAAQSIHEWLDL 351
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 31-278 1.85e-07

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: 51.74  E-value: 1.85e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921  31 VISKD--LGGQMNLIPKLenYPGTIMSSGQILAKTLEtQYLSFKGE-IVYDTVEKIDESEdgfKIKTTRS--EYKAKAIV 105
Cdd:COG0446  10 VIEKGphHSYQPCGLPYY--VGGGIKDPEDLLVRTPE-SFERKGIDvRTGTEVTAIDPEA---KTVTLRDgeTLSYDKLV 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921 106 LAPGKVPNMLGVENESEyfnKGIHYCTKCDAPFY--------QGRiTASVGVGSYLvesGLL----LSRMASKMYLILKG 173
Cdd:COG0446  84 LATGARPRPPPIPGLDL---PGVFTLRTLDDADAlrealkefKGK-RAVVIGGGPI---GLElaeaLRKRGLKVTLVERA 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921 174 SKLAG--DKDLVTTLENN---KNIEIITQSSVKSISGNstlQQITLVDSSGSEkvLDVDALFIELGSKINLDYVKHL-VK 247
Cdd:COG0446 157 PRLLGvlDPEMAALLEEElreHGVELRLGETVVAIDGD---DKVAVTLTDGEE--IPADLVVVAPGVRPNTELAKDAgLA 231

                       250       260       270
                ....*....|....*....|....*....|.
gi 38569921 248 INTKGEIEIESGGMTSHPAIFAAGDATTIPY 278
Cdd:COG0446 232 LGERGWIKVDETLQTSDPDVYAAGDCAEVPH 262
PRK12831 PRK12831
putative oxidoreductase; Provisional
 215-301 2.34e-07

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 51.94  E-value: 2.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921  215 VDSSGSEKVLDVDALFIELGSKIN---LDYVKHLvKINTKGEIEI-ESGGMTSHPAIFAAGDATTiPYKQIIVACGDGSN 290
Cdd:PRK12831 374 VEIEGSEFVLEVDTVIMSLGTSPNpliSSTTKGL-KINKRGCIVAdEETGLTSKEGVFAGGDAVT-GAATVILAMGAGKK 451

                         90
                 ....*....|.
gi 38569921  291 AGLSAFNYLEK 301
Cdd:PRK12831 452 AAKAIDEYLSK 462
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 6-305 7.71e-07

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 50.18  E-value: 7.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921    6 IVIVGAGPAGLSAGMYVARQNVSCLVI-SKDLGGQMNL--IP--KLENypgtimssgQILAKtlETQYLSFKG-EIVYDT 79
Cdd:PRK11749 143 VAVIGAGPAGLTAAHRLARKGYDVTIFeARDKAGGLLRygIPefRLPK---------DIVDR--EVERLLKLGvEIRTNT 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921   80 V----EKIDESEDGFKikttrseykakAIVLAPGkV--PNMLGVENESeyfNKGIHYCTkcdapfyqgritasvgvgSYL 153
Cdd:PRK11749 212 EvgrdITLDELRAGYD-----------AVFIGTG-AglPRFLGIPGEN---LGGVYSAV------------------DFL 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921  154 VESglllsRMASKMYLILKGSKL----AGDK--DLVTT--------------------------LENNK--NIEIITQSS 199
Cdd:PRK11749 259 TRV-----NQAVADYDLPVGKRVvvigGGNTamDAARTakrlgaesvtivyrrgreempaseeeVEHAKeeGVEFEWLAA 333

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921  200 VKSISGNS------TLQQITLV--DSSG--------SEKVLDVDALFIELGSKINLDYVKHL--VKINTKGEIEI-ESGG 260
Cdd:PRK11749 334 PVEILGDEgrvtgvEFVRMELGepDASGrrrvpiegSEFTLPADLVIKAIGQTPNPLILSTTpgLELNRWGTIIAdDETG 413

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 38569921  261 MTSHPAIFAAGDATTiPYKQIIVACGDGSNAGLSAFNYLEKLKGK 305
Cdd:PRK11749 414 RTSLPGVFAGGDIVT-GAATVVWAVGDGKDAAEAIHEYLEGAASA 457
Pyr_redox_3 pfam13738
Pyridine nucleotide-disulphide oxidoreductase;
70-271 8.30e-07

Pyridine nucleotide-disulphide oxidoreductase;


Pssm-ID: 404603 [Multi-domain]  Cd Length: 296  Bit Score: 49.53  E-value: 8.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921    70 SFKGEIVYDT-VEKIDESEDGFKIKTTRSEYKAKAIVLAPGK--VPNMLGVEneseyfNKGIHYCTKCDAPFYQGRITAS 146
Cdd:pfam13738  87 HFELPINLFEeVTSVKKEDDGFVVTTSKGTYQARYVIIATGEfdFPNKLGVP------ELPKHYSYVKDFHPYAGQKVVV 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921   147 VGVGSYLVESGLLLSRMASKMYLILKGSKL-AGDKDLVTTL-----------ENNKNIEIITQSSVKSISGNStlqQITL 214
Cdd:pfam13738 161 IGGYNSAVDAALELVRKGARVTVLYRGSEWeDRDSDPSYSLspdtlnrleelVKNGKIKAHFNAEVKEITEVD---VSYK 237

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 38569921   215 VDSSGSEKVLDVDALFIELGSKINLDYVK-HLVKINTKGEIEIESGGM-TSHPAIFAAG 271
Cdd:pfam13738 238 VHTEDGRKVTSNDDPILATGYHPDLSFLKkGLFELDEDGRPVLTEETEsTNVPGLFLAG 296
PTZ00058 PTZ00058
glutathione reductase; Provisional
 51-282 1.15e-06

glutathione reductase; Provisional


Pssm-ID: 185420 [Multi-domain]  Cd Length: 561  Bit Score: 50.00  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921   51 GTIMSSGQILAKTLETQYLSFKG---EIVYDTVEKIDESEDGFKIKttrseykAKAIVLAPGKVPNMLGVEneseyfnkG 127
Cdd:PTZ00058 157 GSLLSENQVLIKKVSQVDGEADEsddDEVTIVSAGVSQLDDGQVIE-------GKNILIAVGNKPIFPDVK--------G 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921  128 IHYCTKCDApFYQGRITASVGV---GSYLVESGLLLSRMASKMYLILKGSKL--AGDKDLVTTLENN---KNIEIITQSS 199
Cdd:PTZ00058 222 KEFTISSDD-FFKIKEAKRIGIagsGYIAVELINVVNRLGAESYIFARGNRLlrKFDETIINELENDmkkNNINIITHAN 300

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921  200 VKSISGNSTLQQITLVDSSGSEkvLDVDALFIELGSKINLDYV--KHLVKINTKGEIEIESGGMTSHPAIFAAGDATTIP 277
Cdd:PTZ00058 301 VEEIEKVKEKNLTIYLSDGRKY--EHFDYVIYCVGRSPNTEDLnlKALNIKTPKGYIKVDDNQRTSVKHIYAVGDCCMVK 378


                 ....*
gi 38569921  278 YKQII 282
Cdd:PTZ00058 379 KNQEI 383
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
 100-274 3.80e-06

trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase.


Pssm-ID: 200098 [Multi-domain]  Cd Length: 486  Bit Score: 48.05  E-value: 3.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921   100 KAKAIVLAPGKVPNMLGVEneseyfnkGIHYCTKCDAPFY---QGRITASVGVGSYLVE-SGLLLS--------RMASKM 167
Cdd:TIGR01423 151 QAEHILLATGSWPQMLGIP--------GIEHCISSNEAFYldePPRRVLTVGGGFISVEfAGIFNAykprggkvTLCYRN 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921   168 YLILKGSKLAGDKDLVTTLENNkNIEIITQSSVKSISGNSTLQQITLVDSSgseKVLDVDALFIELG-----SKINLDYV 242
Cdd:TIGR01423 223 NMILRGFDSTLRKELTKQLRAN-GINIMTNENPAKVTLNADGSKHVTFESG---KTLDVDVVMMAIGrvprtQTLQLDKV 298

                         170       180       190
                  ....*....|....*....|....*....|..
gi 38569921   243 KhlVKINTKGEIEIESGGMTSHPAIFAAGDAT 274
Cdd:TIGR01423 299 G--VELTKKGAIQVDEFSRTNVPNIYAIGDVT 328
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 6-301 4.02e-06

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


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 48.20  E-value: 4.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921    6 IVIVGAGPAGLSAGMYVARQNVSCLVISK--DLGGQMNL-IPKLEnYPGTIMSsgqilaktLETQYLSFKG-EIVYDTVE 81
Cdd:PRK12778 434 VAVIGSGPAGLSFAGDLAKRGYDVTVFEAlhEIGGVLKYgIPEFR-LPKKIVD--------VEIENLKKLGvKFETDVIV 504

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921   82 ----KIDE-SEDGFKikttrseykakAIVLAPGK-VPNMLGVENE--------SEYF---NKGIHYCTKCDAPFYQGRIT 144
Cdd:PRK12778 505 gktiTIEElEEEGFK-----------GIFIASGAgLPNFMNIPGEnsngvmssNEYLtrvNLMDAASPDSDTPIKFGKKV 573

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921  145 ASVGVGSYLVESGLLLSRM-ASKMYLILKGSklagDKDLVTTLENNKN-----IEIITQSSVKSISGNST-------LQQ 211
Cdd:PRK12778 574 AVVGGGNTAMDSARTAKRLgAERVTIVYRRS----EEEMPARLEEVKHakeegIEFLTLHNPIEYLADEKgwvkqvvLQK 649

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921  212 ITL--VDSSG---------SEKVLDVDALFIELGSKIN---LDYVKHLvKINTKGEIEIESGGMTSHPAIFAAGDATTiP 277
Cdd:PRK12778 650 MELgePDASGrrrpvaipgSTFTVDVDLVIVSVGVSPNplvPSSIPGL-ELNRKGTIVVDEEMQSSIPGIYAGGDIVR-G 727

                        330       340
                 ....*....|....*....|....
gi 38569921  278 YKQIIVACGDGSNAGLSAFNYLEK 301
Cdd:PRK12778 728 GATVILAMGDGKRAAAAIDEYLSS 751
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 1-35 2.02e-05

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 45.70  E-value: 2.02e-05
                        10        20        30
                ....*....|....*....|....*....|....*
gi 38569921   1 MQEFEIVIVGAGPAGLSAGMYVARQNVSCLVISKD 35
Cdd:COG0654   1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVERA 35
PRK13748 PRK13748
putative mercuric reductase; Provisional
 192-293 3.68e-05

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 45.14  E-value: 3.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921  192 IEIITQSSVKSISGNSTlqQITLVDSSGSekvLDVDALFIELG-----SKINLDYVKhlVKINTKGEIEIESGGMTSHPA 266
Cdd:PRK13748 325 IEVLEHTQASQVAHVDG--EFVLTTGHGE---LRADKLLVATGrapntRSLALDAAG--VTVNAQGAIVIDQGMRTSVPH 397

                         90       100
                 ....*....|....*....|....*...
gi 38569921  267 IFAAGDATTIPykQII-VACGDGSNAGL 293
Cdd:PRK13748 398 IYAAGDCTDQP--QFVyVAAAAGTRAAI 423
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 1-61 3.72e-05

Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440673 [Multi-domain]  Cd Length: 443  Bit Score: 45.21  E-value: 3.72e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38569921   1 MQEFEIVIVGAGPAGLSAGMYVARQNVSCLVISKD--LGGqmnlipklenypGTIMSSGQILA 61
Cdd:COG1053   1 DHEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVppRGG------------HTAAAQGGINA 51
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
8-40 4.03e-05

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 40.98  E-value: 4.03e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 38569921     8 IVGAGPAGLSAGMYVARQNVSCLVISK--DLGGQM 40
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKrdRLGGNA 35
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 1-119 6.60e-05

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: 44.08  E-value: 6.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921   1 MQEFEIVIVGAGPAGLSAGMYVARQNVSCLVI--SKDLGG--QMNlipkleNYPG----------------------TIM 54
Cdd:COG2072   4 TEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLekADDVGGtwRDN------RYPGlrldtpshlyslpffpnwsddpDFP 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921  55 SSGQILAktletqYLS-------FKGEIVYDT-VEKI--DESEDGFKIKTTR-SEYKAKAIVLAPG-----KVPNMLGVE 118
Cdd:COG2072  78 TGDEILA------YLEayadkfgLRRPIRFGTeVTSArwDEADGRWTVTTDDgETLTARFVVVATGplsrpKIPDIPGLE 151


                .
gi 38569921 119 N 119
Cdd:COG2072 152 D 152
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 179-274 1.31e-04

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 43.21  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921  179 DKDLVTTLENN---KNIEIITQSSVKSISGNStlQQITL-VDSSGSEKVLDVDALFIELG-----SKINLDYVKhlVKIn 249
Cdd:PRK06416 212 DKEISKLAERAlkkRGIKIKTGAKAKKVEQTD--DGVTVtLEDGGKEETLEADYVLVAVGrrpntENLGLEELG--VKT- 286

                         90       100
                 ....*....|....*....|....*
gi 38569921  250 TKGEIEIESGGMTSHPAIFAAGDAT 274
Cdd:PRK06416 287 DRGFIEVDEQLRTNVPNIYAIGDIV 311
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 3-34 1.65e-04

FAD binding domain; This domain is involved in FAD binding in a number of enzymes.


Pssm-ID: 396193 [Multi-domain]  Cd Length: 348  Bit Score: 42.70  E-value: 1.65e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 38569921     3 EFEIVIVGAGPAGLSAGMYVARQNVSCLVISK 34
Cdd:pfam01494   1 ETDVLIVGGGPAGLMLALLLARAGVRVVLVER 32
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 1-32 2.74e-04

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 42.53  E-value: 2.74e-04
                        10        20        30
                ....*....|....*....|....*....|..
gi 38569921   1 MQEFEIVIVGAGPAGLSAGMYVARQNVSCLVI 32
Cdd:COG1233   1 MMMYDVVVIGAGIGGLAAAALLARAGYRVTVL 32
PRK07843 PRK07843
3-oxosteroid 1-dehydrogenase;
2-34 7.01e-04

3-oxosteroid 1-dehydrogenase;


Pssm-ID: 236111 [Multi-domain]  Cd Length: 557  Bit Score: 41.17  E-value: 7.01e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 38569921    2 QEFEIVIVGAGPAGLSAGMYVARQNVSCLVISK 34
Cdd:PRK07843   6 QEYDVVVVGSGAAGMVAALTAAHRGLSTVVVEK 38
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 6-38 1.08e-03

Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440845 [Multi-domain]  Cd Length: 443  Bit Score: 40.59  E-value: 1.08e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 38569921   6 IVIVGAGPAGLSAGMYVARQNVSCLVISKD--LGG 38
Cdd:COG1232   4 VAVIGGGIAGLTAAYRLAKAGHEVTVLEASdrVGG 38
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 6-34 1.14e-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: 40.35  E-value: 1.14e-03
                          10        20
                  ....*....|....*....|....*....
gi 38569921     6 IVIVGAGPAGLSAGMYVARQNVSCLVISK 34
Cdd:pfam00890   2 VLVIGGGLAGLAAALAAAEAGLKVAVVEK 30
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
3-32 1.31e-03

bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 40.28  E-value: 1.31e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 38569921    3 EFEIVIVGAGPAGLSAGMYVARQNVSCLVI 32
Cdd:PRK06183  10 DTDVVIVGAGPVGLTLANLLGQYGVRVLVL 39
PRK06370 PRK06370
FAD-containing oxidoreductase;
1-272 1.35e-03

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 40.19  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921    1 MQEFEIVIVGAGPAGLS-------AGMYVArqnvscLVISKDLGGQ-MNL--IP-KlenypgTIMSSGQILAKTLETQYL 69
Cdd:PRK06370   3 AQRYDAIVIGAGQAGPPlaaraagLGMKVA------LIERGLLGGTcVNTgcVPtK------TLIASARAAHLARRAAEY 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921   70 SFK--GEIVYDT---VEKIDE--------SEDGFK-------------------IKTTRSEYKAKAIVLAPG---KVPNM 114
Cdd:PRK06370  71 GVSvgGPVSVDFkavMARKRRirarsrhgSEQWLRglegvdvfrgharfespntVRVGGETLRAKRIFINTGaraAIPPI 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921  115 LGVENESEYFNKGIHYCTKCDApfyqgRItASVGvGSYL-VESGLLLSRMASKMYLILKGSKLAG--DKDLVTTLEN--- 188
Cdd:PRK06370 151 PGLDEVGYLTNETIFSLDELPE-----HL-VIIG-GGYIgLEFAQMFRRFGSEVTVIERGPRLLPreDEDVAAAVREile 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921  189 NKNIEIITQSSVKSISGNSTLQQITLVDSSGSEKVlDVDALFIELG-----SKINLDYVKhlVKINTKGEIEIESGGMTS 263
Cdd:PRK06370 224 REGIDVRLNAECIRVERDGDGIAVGLDCNGGAPEI-TGSHILVAVGrvpntDDLGLEAAG--VETDARGYIKVDDQLRTT 300


                 ....*....
gi 38569921  264 HPAIFAAGD 272
Cdd:PRK06370 301 NPGIYAAGD 309
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 179-276 1.36e-03

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 40.02  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921  179 DKDLVTTLENN---KNIEIITQSSVKSISGNstlQQITLVDSSGSEkvLDVDALFIELGSKINLDYVKH-LVKINTKGEI 254
Cdd:PRK09564 190 DKEITDVMEEElreNGVELHLNEFVKSLIGE---DKVEGVVTDKGE--YEADVVIVATGVKPNTEFLEDtGLKTLKNGAI 264

                         90       100
                 ....*....|....*....|..
gi 38569921  255 EIESGGMTSHPAIFAAGDATTI 276
Cdd:PRK09564 265 IVDEYGETSIENIYAAGDCATI 286
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 6-40 2.04e-03

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


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 39.51  E-value: 2.04e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 38569921     6 IVIVGAGPAGLSAGMYVARQNVSCLVISKD--LGGQM 40
Cdd:pfam12831   2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRgfLGGML 38
Thi4 pfam01946
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
 3-40 2.76e-03

Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.


Pssm-ID: 460393  Cd Length: 232  Bit Score: 38.61  E-value: 2.76e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 38569921     3 EFEIVIVGAGPAGLSAGMYVARQ-NVSCLVISKDL--------GGQM 40
Cdd:pfam01946  17 ESDVVIVGAGSSGLTAAYYLAKNrGLKVAIIERSVspgggawlGGQL 63
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
6-109 3.11e-03

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 39.07  E-value: 3.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921   6 IVIVGAGPAGLSAGMYVARQNVSCLVISKD--LGGQMNLIPKLenYPGT--IMSSGQILAKTLE-----TQYLsfkgeiv 76
Cdd:COG1148 143 ALVIGGGIAGMTAALELAEQGYEVYLVEKEpeLGGRAAQLHKT--FPGLdcPQCILEPLIAEVEanpniTVYT------- 213

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 38569921  77 YDTVEKIDESEDGFKIK-----TTRSEYKAKAIVLAPG 109
Cdd:COG1148 214 GAEVEEVSGYVGNFTVTikkgpREEIEIEVGAIVLATG 251
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 192-291 3.16e-03

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 39.09  E-value: 3.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569921  192 IEIITQSSVKSISGNS---------TLQQITLVDS------SGSEKVLDVDALFIELGSKINLDYVKHLVKINTK-GEIE 255
Cdd:PRK12771 320 VEINWLRTPVEIEGDEngatglrviTVEKMELDEDgrpspvTGEEETLEADLVVLAIGQDIDSAGLESVPGVEVGrGVVQ 399

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 38569921  256 I-ESGGMTSHPAIFAAGDATTIPyKQIIVACGDGSNA 291
Cdd:PRK12771 400 VdPNFMMTGRPGVFAGGDMVPGP-RTVTTAIGHGKKA 435
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 4-34 3.53e-03

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: 38.45  E-value: 3.53e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 38569921     4 FEIVIVGAGPAGLSAGMYVARQNVSCLVISK 34
Cdd:TIGR02032   1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEK 31
PRK07208 PRK07208
hypothetical protein; Provisional
 1-54 4.03e-03

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 38.72  E-value: 4.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 38569921    1 MQEFEIVIVGAGPAGLSAGMYVARQNVSCLVISKD--LGGqmnlIPKLENYPGTIM 54
Cdd:PRK07208   2 TNKKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADpvVGG----ISRTVTYKGNRF 53
PRK08132 PRK08132
FAD-dependent oxidoreductase; Provisional
 6-35 4.24e-03

FAD-dependent oxidoreductase; Provisional


Pssm-ID: 236158 [Multi-domain]  Cd Length: 547  Bit Score: 38.70  E-value: 4.24e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 38569921    6 IVIVGAGPAGLSAGMYVARQNVSCLVISKD 35
Cdd:PRK08132  26 VVVVGAGPVGLALAIDLAQQGVPVVLLDDD 55
PRK05329 PRK05329
glycerol-3-phosphate dehydrogenase subunit GlpB;
3-34 5.17e-03

glycerol-3-phosphate dehydrogenase subunit GlpB;


Pssm-ID: 235412  Cd Length: 422  Bit Score: 38.29  E-value: 5.17e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 38569921    3 EFEIVIVGAGPAGLSAGMYVARQNVSCLVISK 34
Cdd:PRK05329   2 KFDVLVIGGGLAGLTAALAAAEAGKRVALVAK 33
COG2509 COG2509
FAD-dependent dehydrogenase [General function prediction only];
1-32 5.81e-03

FAD-dependent dehydrogenase [General function prediction only];


Pssm-ID: 441999 [Multi-domain]  Cd Length: 466  Bit Score: 38.17  E-value: 5.81e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 38569921   1 MQEFEIVIVGAGPAGLSAGMYVARQNVSCLVI 32
Cdd:COG2509  28 SLKYDVVIVGAGPAGLFAALELAEAGLKPLVL 59
PRK07233 PRK07233
hypothetical protein; Provisional
 6-38 5.83e-03

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 38.33  E-value: 5.83e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 38569921    6 IVIVGAGPAGLSAGMYVARQNVSCLVISKD--LGG 38
Cdd:PRK07233   2 IAIVGGGIAGLAAAYRLAKRGHEVTVFEADdqLGG 36
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
1-40 6.91e-03

Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];


Pssm-ID: 442607 [Multi-domain]  Cd Length: 331  Bit Score: 37.94  E-value: 6.91e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 38569921   1 MQEFEIVIVGAGPAGLSAGMYVARQNVSCLVISKD--LGGQM 40
Cdd:COG3380   1 MSMPDIAIIGAGIAGLAAARALQDAGHEVTVFEKSrgVGGRM 42
PRK09126 PRK09126
FAD-dependent hydroxylase;
1-32 7.70e-03

FAD-dependent hydroxylase;


Pssm-ID: 236385 [Multi-domain]  Cd Length: 392  Bit Score: 37.61  E-value: 7.70e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 38569921    1 MQEFEIVIVGAGPAGLSAGMYVARQNVSCLVI 32
Cdd:PRK09126   1 MMHSDIVVVGAGPAGLSFARSLAGSGLKVTLI 32
 
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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