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Conserved domains on  [gi|2030879356|gb|QUM60972|]
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NAD(P)/FAD-dependent oxidoreductase [Enterococcus faecium]

Protein Classification

dihydrolipoyl dehydrogenase family protein( domain architecture ID 11441193)

dihydrolipoyl dehydrogenase family protein belonging to the class-I pyridine nucleotide-disulfide oxidoreductase superfamily may function as a FAD/NAD(P)-dependent oxidoreductase, similar to dihydrolipoyl dehydrogenase which catalyzes the oxidation of dihydrolipoamide to lipoamide and is often a component of multienzyme 2-oxo-acid dehydrogenase complexes

EC:  1.-.-.-
Gene Ontology:  GO:0016491|GO:0000166
SCOP:  4000121

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
1-439 1.05e-133

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: 392.53  E-value: 1.05e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   1 MKTYDAIIIGSGVSGLSAAYGLKEAGKTVLVVEEDLWGGTCPNRGCDPKKVLLSAVEARNRVKQLSGKGFN-EIPTANWE 79
Cdd:COG1249     1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISaGAPSVDWA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  80 ELQKFKRTFTDPVPESRKKQLAEAEIDHLSGTARFLDDSSIEV-NEEVFHADYLVLATGQRPTILPVEG--KEYLKTSAD 156
Cdd:COG1249    81 ALMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVtGGETLTADHIVIATGSRPRVPPIPGldEVRVLTSDE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 157 FLSLPVLPKEIIFIGGGYIAFELATIANAAGSKVTIVHHNQRPLKEFEASLVEEAVHQMEASGIQFAFGVETQKIISEGT 236
Cdd:COG1249   161 ALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 237 RYRLV----GKETELVADMIFCATGRQPNTESLALEQANIVFDKHG-IAVNDYLQTSNPKIFACGDIVSRktPKLTPVAT 311
Cdd:COG1249   241 GVTVTledgGGEEAVEADKVLVATGRRPNTDGLGLEAAGVELDERGgIKVDEYLRTSVPGIYAIGDVTGG--PQLAHVAS 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 312 FEGNYVAKRITDATSEPIKYPIIPTIVYASPKLAEVGVTKSHASSSD---QVVEMDLTSWFTYHRVNEPVAKAELTFDQQ 388
Cdd:COG1249   319 AEGRVAAENILGKKPRPVDYRAIPSVVFTDPEIASVGLTEEEAREAGidvKVGKFPFAANGRALALGETEGFVKLIADAE 398
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2030879356 389 N-YLIGAAVISEQADELIDDLTLVINQKLTKKELDSYIMGYPTLASDLSYLL 439
Cdd:COG1249   399 TgRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAA 450
 
Name Accession Description Interval E-value
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
1-439 1.05e-133

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: 392.53  E-value: 1.05e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   1 MKTYDAIIIGSGVSGLSAAYGLKEAGKTVLVVEEDLWGGTCPNRGCDPKKVLLSAVEARNRVKQLSGKGFN-EIPTANWE 79
Cdd:COG1249     1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISaGAPSVDWA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  80 ELQKFKRTFTDPVPESRKKQLAEAEIDHLSGTARFLDDSSIEV-NEEVFHADYLVLATGQRPTILPVEG--KEYLKTSAD 156
Cdd:COG1249    81 ALMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVtGGETLTADHIVIATGSRPRVPPIPGldEVRVLTSDE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 157 FLSLPVLPKEIIFIGGGYIAFELATIANAAGSKVTIVHHNQRPLKEFEASLVEEAVHQMEASGIQFAFGVETQKIISEGT 236
Cdd:COG1249   161 ALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 237 RYRLV----GKETELVADMIFCATGRQPNTESLALEQANIVFDKHG-IAVNDYLQTSNPKIFACGDIVSRktPKLTPVAT 311
Cdd:COG1249   241 GVTVTledgGGEEAVEADKVLVATGRRPNTDGLGLEAAGVELDERGgIKVDEYLRTSVPGIYAIGDVTGG--PQLAHVAS 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 312 FEGNYVAKRITDATSEPIKYPIIPTIVYASPKLAEVGVTKSHASSSD---QVVEMDLTSWFTYHRVNEPVAKAELTFDQQ 388
Cdd:COG1249   319 AEGRVAAENILGKKPRPVDYRAIPSVVFTDPEIASVGLTEEEAREAGidvKVGKFPFAANGRALALGETEGFVKLIADAE 398
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2030879356 389 N-YLIGAAVISEQADELIDDLTLVINQKLTKKELDSYIMGYPTLASDLSYLL 439
Cdd:COG1249   399 TgRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAA 450
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
1-421 1.19e-87

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 274.36  E-value: 1.19e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   1 MKTYDAIIIGSGVSGLSAAYGLKEAGKTVLVVEEDLWGGTCPNRGCDPKKVLLSAVEARNRVKQLSGKGFN-EIPTANWE 79
Cdd:PRK06292    1 MEKYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGPLGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHaDGPKIDFK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  80 ELQKFKRT----FTDPVPESrkkQLAEAEIDHLSGTARFLDDSSIEVNEEVFHADYLVLATGQR-PTILPVE---GKEYL 151
Cdd:PRK06292   81 KVMARVRRerdrFVGGVVEG---LEKKPKIDKIKGTARFVDPNTVEVNGERIEAKNIVIATGSRvPPIPGVWlilGDRLL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 152 kTSADFLSLPVLPKEIIFIGGGYIAFELATIANAAGSKVTIVHHNQRPLKEFEASLVEEAVHQMEASgIQFAFGVETQKI 231
Cdd:PRK06292  158 -TSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILSKE-FKIKLGAKVTSV 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 232 ISEGTR----YRLVGKETELVADMIFCATGRQPNTESLALEQANIVFDKHG-IAVNDYLQTSNPKIFACGDiVSRKTPkL 306
Cdd:PRK06292  236 EKSGDEkveeLEKGGKTETIEADYVLVATGRRPNTDGLGLENTGIELDERGrPVVDEHTQTSVPGIYAAGD-VNGKPP-L 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 307 TPVATFEGNYVAKRITDATSEPIKYPIIPTIVYASPKLAEVGVTKSHASSSD---QVVEMDLTswftyhrvNEPVAKAEL 383
Cdd:PRK06292  314 LHEAADEGRIAAENAAGDVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGidyVVGEVPFE--------AQGRARVMG 385
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 2030879356 384 T--------FDQQNY-LIGAAVISEQADELIDDLTLVINQKLTKKEL 421
Cdd:PRK06292  386 KndgfvkvyADKKTGrLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDL 432
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
3-432 7.88e-81

dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.


Pssm-ID: 273568 [Multi-domain]  Cd Length: 460  Bit Score: 256.80  E-value: 7.88e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   3 TYDAIIIGSGVSGLSAAYGLKEAGKTVLVVEEDLWGGTCPNRGCDPKKVLLSAVEARNRVKQLSGKGFN-EIPTANWEEL 81
Cdd:TIGR01350   1 AYDVIVIGGGPGGYVAAIRAAQLGLKVALVEKEYLGGTCLNVGCIPTKALLHSAEVYDEIKHAKDLGIEvENVSVDWEKM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  82 QKFKRTFTDPVPESRKKQLAEAEIDHLSGTARFLDDSSIEVN----EEVFHADYLVLATGQRPTILPVE---GKEYLKTS 154
Cdd:TIGR01350  81 QKRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTgengEETLEAKNIIIATGSRPRSLPGPfdfDGKVVITS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 155 ADFLSLPVLPKEIIFIGGGYIAFELATIANAAGSKVTIVHHNQRPLKEFEASLVEEAVHQMEASGIQFAFG--VETQKII 232
Cdd:TIGR01350 161 TGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNtkVTAVEKN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 233 SEGTRYRLVGKETE-LVADMIFCATGRQPNTESLALEQANIVFDKHG-IAVNDYLQTSNPKIFACGDIVSrkTPKLTPVA 310
Cdd:TIGR01350 241 DDQVTYENKGGETEtLTGEKVLVAVGRKPNTEGLGLEKLGVELDERGrIVVDEYMRTNVPGIYAIGDVIG--GPMLAHVA 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 311 TFEGNYVAKRITDATSEPIKYPIIPTIVYASPKLAEVGVTKSHASSSD---QVVEMDLTSWFTYHRVNEPVAKAELTFDQ 387
Cdd:TIGR01350 319 SHEGIVAAENIAGKEPAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGydvKIGKFPFAANGKALALGETDGFVKIIADK 398
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 2030879356 388 Q-NYLIGAAVISEQADELIDDLTLVINQKLTKKELDSYIMGYPTLA 432
Cdd:TIGR01350 399 KtGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLS 444
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
4-314 2.37e-66

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: 214.10  E-value: 2.37e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   4 YDAIIIGSGVSGLSAAYGLKEAGKTVLVVEEdlwGGTCPNRGCDPKKVLLSAVEARNRVKqlsgkgfneiptaNWEELQK 83
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIED---EGTCPYGGCVLSKALLGAAEAPEIAS-------------LWADLYK 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  84 FKRTFTDPVPESRKKQLAEAEIDHLSGTARFLDDSSIEVNEEVFHADYLVLATGQRPTILPVEGKEYLK-------TSAD 156
Cdd:pfam07992  65 RKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELVDGDGETITYDRLVIATGARPRLPPIPGVELNVgflvrtlDSAE 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 157 FLSLPVLPKEIIFIGGGYIAFELATIANAAGSKVTIVHHNQRPLKEFEASLVEEAVHQMEASGIQFAFGVETQKIISEGT 236
Cdd:pfam07992 145 ALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGD 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 237 RYRLVGKE-TELVADMIFCATGRQPNTEslALEQANIVFDKHG-IAVNDYLQTSNPKIFACGDiVSRKTPKLTPVATFEG 314
Cdd:pfam07992 225 GVEVILKDgTEIDADLVVVAIGRRPNTE--LLEAAGLELDERGgIVVDEYLRTSVPGIYAAGD-CRVGGPELAQNAVAQG 301
 
Name Accession Description Interval E-value
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
1-439 1.05e-133

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: 392.53  E-value: 1.05e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   1 MKTYDAIIIGSGVSGLSAAYGLKEAGKTVLVVEEDLWGGTCPNRGCDPKKVLLSAVEARNRVKQLSGKGFN-EIPTANWE 79
Cdd:COG1249     1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISaGAPSVDWA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  80 ELQKFKRTFTDPVPESRKKQLAEAEIDHLSGTARFLDDSSIEV-NEEVFHADYLVLATGQRPTILPVEG--KEYLKTSAD 156
Cdd:COG1249    81 ALMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVtGGETLTADHIVIATGSRPRVPPIPGldEVRVLTSDE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 157 FLSLPVLPKEIIFIGGGYIAFELATIANAAGSKVTIVHHNQRPLKEFEASLVEEAVHQMEASGIQFAFGVETQKIISEGT 236
Cdd:COG1249   161 ALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 237 RYRLV----GKETELVADMIFCATGRQPNTESLALEQANIVFDKHG-IAVNDYLQTSNPKIFACGDIVSRktPKLTPVAT 311
Cdd:COG1249   241 GVTVTledgGGEEAVEADKVLVATGRRPNTDGLGLEAAGVELDERGgIKVDEYLRTSVPGIYAIGDVTGG--PQLAHVAS 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 312 FEGNYVAKRITDATSEPIKYPIIPTIVYASPKLAEVGVTKSHASSSD---QVVEMDLTSWFTYHRVNEPVAKAELTFDQQ 388
Cdd:COG1249   319 AEGRVAAENILGKKPRPVDYRAIPSVVFTDPEIASVGLTEEEAREAGidvKVGKFPFAANGRALALGETEGFVKLIADAE 398
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2030879356 389 N-YLIGAAVISEQADELIDDLTLVINQKLTKKELDSYIMGYPTLASDLSYLL 439
Cdd:COG1249   399 TgRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAA 450
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
1-421 1.19e-87

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 274.36  E-value: 1.19e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   1 MKTYDAIIIGSGVSGLSAAYGLKEAGKTVLVVEEDLWGGTCPNRGCDPKKVLLSAVEARNRVKQLSGKGFN-EIPTANWE 79
Cdd:PRK06292    1 MEKYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGPLGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHaDGPKIDFK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  80 ELQKFKRT----FTDPVPESrkkQLAEAEIDHLSGTARFLDDSSIEVNEEVFHADYLVLATGQR-PTILPVE---GKEYL 151
Cdd:PRK06292   81 KVMARVRRerdrFVGGVVEG---LEKKPKIDKIKGTARFVDPNTVEVNGERIEAKNIVIATGSRvPPIPGVWlilGDRLL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 152 kTSADFLSLPVLPKEIIFIGGGYIAFELATIANAAGSKVTIVHHNQRPLKEFEASLVEEAVHQMEASgIQFAFGVETQKI 231
Cdd:PRK06292  158 -TSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILSKE-FKIKLGAKVTSV 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 232 ISEGTR----YRLVGKETELVADMIFCATGRQPNTESLALEQANIVFDKHG-IAVNDYLQTSNPKIFACGDiVSRKTPkL 306
Cdd:PRK06292  236 EKSGDEkveeLEKGGKTETIEADYVLVATGRRPNTDGLGLENTGIELDERGrPVVDEHTQTSVPGIYAAGD-VNGKPP-L 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 307 TPVATFEGNYVAKRITDATSEPIKYPIIPTIVYASPKLAEVGVTKSHASSSD---QVVEMDLTswftyhrvNEPVAKAEL 383
Cdd:PRK06292  314 LHEAADEGRIAAENAAGDVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGidyVVGEVPFE--------AQGRARVMG 385
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 2030879356 384 T--------FDQQNY-LIGAAVISEQADELIDDLTLVINQKLTKKEL 421
Cdd:PRK06292  386 KndgfvkvyADKKTGrLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDL 432
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
3-432 7.88e-81

dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.


Pssm-ID: 273568 [Multi-domain]  Cd Length: 460  Bit Score: 256.80  E-value: 7.88e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   3 TYDAIIIGSGVSGLSAAYGLKEAGKTVLVVEEDLWGGTCPNRGCDPKKVLLSAVEARNRVKQLSGKGFN-EIPTANWEEL 81
Cdd:TIGR01350   1 AYDVIVIGGGPGGYVAAIRAAQLGLKVALVEKEYLGGTCLNVGCIPTKALLHSAEVYDEIKHAKDLGIEvENVSVDWEKM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  82 QKFKRTFTDPVPESRKKQLAEAEIDHLSGTARFLDDSSIEVN----EEVFHADYLVLATGQRPTILPVE---GKEYLKTS 154
Cdd:TIGR01350  81 QKRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTgengEETLEAKNIIIATGSRPRSLPGPfdfDGKVVITS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 155 ADFLSLPVLPKEIIFIGGGYIAFELATIANAAGSKVTIVHHNQRPLKEFEASLVEEAVHQMEASGIQFAFG--VETQKII 232
Cdd:TIGR01350 161 TGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNtkVTAVEKN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 233 SEGTRYRLVGKETE-LVADMIFCATGRQPNTESLALEQANIVFDKHG-IAVNDYLQTSNPKIFACGDIVSrkTPKLTPVA 310
Cdd:TIGR01350 241 DDQVTYENKGGETEtLTGEKVLVAVGRKPNTEGLGLEKLGVELDERGrIVVDEYMRTNVPGIYAIGDVIG--GPMLAHVA 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 311 TFEGNYVAKRITDATSEPIKYPIIPTIVYASPKLAEVGVTKSHASSSD---QVVEMDLTSWFTYHRVNEPVAKAELTFDQ 387
Cdd:TIGR01350 319 SHEGIVAAENIAGKEPAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGydvKIGKFPFAANGKALALGETDGFVKIIADK 398
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 2030879356 388 Q-NYLIGAAVISEQADELIDDLTLVINQKLTKKELDSYIMGYPTLA 432
Cdd:TIGR01350 399 KtGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLS 444
PRK06370 PRK06370
FAD-containing oxidoreductase;
1-432 4.56e-80

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 255.13  E-value: 4.56e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   1 MKTYDAIIIGSGVSGLSAAYGLKEAGKTVLVVEEDLWGGTCPNRGCDPKKVLLSAVEARNRVKQLSGKGFN--EIPTANW 78
Cdd:PRK06370    3 AQRYDAIVIGAGQAGPPLAARAAGLGMKVALIERGLLGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSvgGPVSVDF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  79 EELQKFKRTFTDPVPESRKKQLAEAE-IDHLSGTARFLDDSSIEVNEEVFHADYLVLATGQRPTILPVEGKE---YLkTS 154
Cdd:PRK06370   83 KAVMARKRRIRARSRHGSEQWLRGLEgVDVFRGHARFESPNTVRVGGETLRAKRIFINTGARAAIPPIPGLDevgYL-TN 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 155 ADFLSLPVLPKEIIFIGGGYIAFELATIANAAGSKVTIVHHNQRPLKEFE---ASLVEEAvhqMEASGIQFAFGVETQKI 231
Cdd:PRK06370  162 ETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPREDedvAAAVREI---LEREGIDVRLNAECIRV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 232 ISEGTRYRLV----GKETELVADMIFCATGRQPNTESLALEQANIVFDKHG-IAVNDYLQTSNPKIFACGDIVSRktPKL 306
Cdd:PRK06370  239 ERDGDGIAVGldcnGGAPEITGSHILVAVGRVPNTDDLGLEAAGVETDARGyIKVDDQLRTTNPGIYAAGDCNGR--GAF 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 307 TPVATFEGNYVAKRITDATSEPIKYPIIPTIVYASPKLAEVGVTKSHASSSDQVVEmdltswfTYHRVNEPVAKAELTFD 386
Cdd:PRK06370  317 THTAYNDARIVAANLLDGGRRKVSDRIVPYATYTDPPLARVGMTEAEARKSGRRVL-------VGTRPMTRVGRAVEKGE 389
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2030879356 387 QQNY-----------LIGAAVISEQADELIDDLTLVINQKLTKKELDSYIMGYPTLA 432
Cdd:PRK06370  390 TQGFmkvvvdadtdrILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVS 446
PRK06116 PRK06116
glutathione reductase; Validated
1-432 4.19e-76

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 244.30  E-value: 4.19e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   1 MKTYDAIIIGSGVSGLSAAYGLKEAGKTVLVVEEDLWGGTCPNRGCDPKKVLLSAVEARNRVKQLS-GKGFN-EIPTANW 78
Cdd:PRK06116    2 TKDYDLIVIGGGSGGIASANRAAMYGAKVALIEAKRLGGTCVNVGCVPKKLMWYGAQIAEAFHDYApGYGFDvTENKFDW 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  79 EELQKFKRTFTDPVPESRKKQLAEAEIDHLSGTARFLDDSSIEVNEEVFHADYLVLATGQRPTILPVEGKEYLKTSADFL 158
Cdd:PRK06116   82 AKLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNGERYTADHILIATGGRPSIPDIPGAEYGITSDGFF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 159 SLPVLPKEIIFIGGGYIAFELATIANAAGSKVTIVHHNQRPLKEFEASLVEEAVHQMEASGIQFAFGVETQKII--SEGT 236
Cdd:PRK06116  162 ALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEknADGS 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 237 -RYRLVGKETeLVADMIFCATGRQPNTESLALEQANIVFDKHG-IAVNDYLQTSNPKIFACGDIVSRktPKLTPVATFEG 314
Cdd:PRK06116  242 lTLTLEDGET-LTVDCLIWAIGREPNTDGLGLENAGVKLNEKGyIIVDEYQNTNVPGIYAVGDVTGR--VELTPVAIAAG 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 315 NYVAKRI-TDATSEPIKYPIIPTIVYASPKLAEVGVTKSHASSS--DQVVEMdLTSWFT--YHRV---NEPVaKAELTFD 386
Cdd:PRK06116  319 RRLSERLfNNKPDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQygEDNVKV-YRSSFTpmYTALtghRQPC-LMKLVVV 396
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 2030879356 387 QQN-YLIGAAVISEQADELIDDLTLVINQKLTKKELDSYIMGYPTLA 432
Cdd:PRK06116  397 GKEeKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAA 443
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
4-314 2.37e-66

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: 214.10  E-value: 2.37e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   4 YDAIIIGSGVSGLSAAYGLKEAGKTVLVVEEdlwGGTCPNRGCDPKKVLLSAVEARNRVKqlsgkgfneiptaNWEELQK 83
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIED---EGTCPYGGCVLSKALLGAAEAPEIAS-------------LWADLYK 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  84 FKRTFTDPVPESRKKQLAEAEIDHLSGTARFLDDSSIEVNEEVFHADYLVLATGQRPTILPVEGKEYLK-------TSAD 156
Cdd:pfam07992  65 RKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELVDGDGETITYDRLVIATGARPRLPPIPGVELNVgflvrtlDSAE 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 157 FLSLPVLPKEIIFIGGGYIAFELATIANAAGSKVTIVHHNQRPLKEFEASLVEEAVHQMEASGIQFAFGVETQKIISEGT 236
Cdd:pfam07992 145 ALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGD 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 237 RYRLVGKE-TELVADMIFCATGRQPNTEslALEQANIVFDKHG-IAVNDYLQTSNPKIFACGDiVSRKTPKLTPVATFEG 314
Cdd:pfam07992 225 GVEVILKDgTEIDADLVVVAIGRRPNTE--LLEAAGLELDERGgIVVDEYLRTSVPGIYAAGD-CRVGGPELAQNAVAQG 301
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
3-432 1.13e-63

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 212.31  E-value: 1.13e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   3 TYDAIIIGSGVSGLSAAYGLKEAGKTVLVVEEDLWGGTCPNRGCDPKKVLLSAVEARNRVKQLSGKGFN-EIPTANWEEL 81
Cdd:PRK06416    4 EYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIKaENVGIDFKKV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  82 QKFKRTFTDPVPESRKKQLAEAEIDHLSGTARFLDDSSIEVN----EEVFHADYLVLATGQRPTILP-VE-GKEYLKTSA 155
Cdd:PRK06416   84 QEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMtedgEQTYTAKNIILATGSRPRELPgIEiDGRVIWTSD 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 156 DFLSLPVLPKEIIFIGGGYIAFELATIANAAGSKVTIVHHNQRPLKEFEASLVEEAVHQMEASGIQFAFGVETQKIISEG 235
Cdd:PRK06416  164 EALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPGEDKEISKLAERALKKRGIKIKTGAKAKKVEQTD 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 236 TRYRLV----GKETELVADMIFCATGRQPNTESLALEQANIVFDKHGIAVNDYLQTSNPKIFACGDIVSrkTPKLTPVAT 311
Cdd:PRK06416  244 DGVTVTledgGKEETLEADYVLVAVGRRPNTENLGLEELGVKTDRGFIEVDEQLRTNVPNIYAIGDIVG--GPMLAHKAS 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 312 FEGNYVAKRITDATSePIKYPIIPTIVYASPKLAEVGVTKSHASSSDqvveMDLTSWFTYHRVN-------EPVAKAELT 384
Cdd:PRK06416  322 AEGIIAAEAIAGNPH-PIDYRGIPAVTYTHPEVASVGLTEAKAKEEG----FDVKVVKFPFAGNgkalalgETDGFVKLI 396
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 2030879356 385 FDQQN-YLIGAAVISEQADELIDDLTLVINQKLTKKELDSYIMGYPTLA 432
Cdd:PRK06416  397 FDKKDgEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLS 445
gluta_reduc_2 TIGR01424
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ...
4-435 9.67e-63

glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, e.g., for maintaining the cellular thiol/disulfide status and for protecting against reactive oxygen species such as hydrogen peroxide. Glutathione-disulfide reductase regenerates reduced glutathione from oxidized glutathione (glutathione disulfide) + NADPH. This model represents one of two closely related subfamilies of glutathione-disulfide reductase. Both are closely related to trypanothione reductase, and separate models are built so each of the three can describe proteins with conserved function. This model describes glutathione-disulfide reductases of plants and some bacteria, including cyanobacteria. [Energy metabolism, Electron transport]


Pssm-ID: 213618 [Multi-domain]  Cd Length: 446  Bit Score: 209.28  E-value: 9.67e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   4 YDAIIIGSGVSGLSAAYGLKEAGKTVLVVEEDLWGGTCPNRGCDPKKVLLSAVEARNRVKQLSGKGF-NEIPTANWEELQ 82
Cdd:TIGR01424   3 YDLFVIGAGSGGVRAARLAAALGAKVAIAEEFRVGGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGWtVGKARFDWKKLL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  83 KFKRTFTDPVPESRKKQLAEAEIDHLSGTARFLDDSSIEVNEE--VFHADYLVLATGQRPTILPVEGKEYLKTSADFLSL 160
Cdd:TIGR01424  83 AAKDQEIARLSGLYRKGLANAGAELLDGRAELVGPNTVEVLASgkTYTAEKILIAVGGRPPKPALPGHELGITSNEAFHL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 161 PVLPKEIIFIGGGYIAFELATIANAAGSKVTIVHHNQRPLKEFEASLVEEAVHQMEASGIQFAFGVETQKI--ISEGTRY 238
Cdd:TIGR01424 163 PTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRGKEILRGFDDDMRRGLAAALEERGIRILPEDSITSIskDDDGRLK 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 239 RLVGKETELVADMIFCATGRQPNTESLALEQANI-VFDKHGIAVNDYLQTSNPKIFACGDIVSRKtpKLTPVATFEGNYV 317
Cdd:TIGR01424 243 ATLSKHEEIVADVVLFATGRSPNTNGLGLEAAGVrLNDLGAIAVDEYSRTSTPSIYAVGDVTDRI--NLTPVAIHEATCF 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 318 AKriTDATSEPIK--YPIIPTIVYASPKLAEVGVTKSHASSSDQVVEmdltswfTYHRVNEPVaKAELTFDQQNYL---- 391
Cdd:TIGR01424 321 AE--TEFGNNPTSfdHDLIATAVFSQPPIGTVGLTEEEARRKFGDIE-------VYRAEFRPM-KATFSGRQEKTLmklv 390
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2030879356 392 --------IGAAVISEQADELIDDLTLVINQKLTKKELDSYIMGYPTLASDL 435
Cdd:TIGR01424 391 vdakddkvLGAHMVGPDAAEIIQGLAIALKMGATKDDFDSTVAVHPTSAEEL 442
PRK07251 PRK07251
FAD-containing oxidoreductase;
1-435 1.03e-56

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 193.43  E-value: 1.03e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   1 MKTYDAIIIGSGVSGLSAAYGLKEAGKTVLVVEED--LWGGTCPNRGCDPKKVLLSAVEarnrvKQLSgkgfneiptanW 78
Cdd:PRK07251    1 MLTYDLIVIGFGKAGKTLAAKLASAGKKVALVEESkaMYGGTCINIGCIPTKTLLVAAE-----KNLS-----------F 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  79 EELQKFKRTFTDPVPESRKKQLAEAEIDHLSGTARFLDDSSIEV----NEEVFHADYLVLATGQRPTILPVEGkeyLKTS 154
Cdd:PRK07251   65 EQVMATKNTVTSRLRGKNYAMLAGSGVDLYDAEAHFVSNKVIEVqagdEKIELTAETIVINTGAVSNVLPIPG---LADS 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 155 ADF------LSLPVLPKEIIFIGGGYIAFELATIANAAGSKVTIVHHNQRPLKEFEASLVEEAVHQMEASGIQFAFGVET 228
Cdd:PRK07251  142 KHVydstgiQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYMEEDGITFLLNAHT 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 229 QKIISEGTRYRLVGKETELVADMIFCATGRQPNTESLALEQANIVFDKHG-IAVNDYLQTSNPKIFACGDIvsRKTPKLT 307
Cdd:PRK07251  222 TEVKNDGDQVLVVTEDETYRFDALLYATGRKPNTEPLGLENTDIELTERGaIKVDDYCQTSVPGVFAVGDV--NGGPQFT 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 308 PVATFEGNYVAKRITDATSEPIK-YPIIPTIVYASPKLAEVGVTKSHASSSD---QVVEMDLTSWFTYHRVNEPVAKAEL 383
Cdd:PRK07251  300 YISLDDFRIVFGYLTGDGSYTLEdRGNVPTTMFITPPLSQVGLTEKEAKEAGlpyAVKELLVAAMPRAHVNNDLRGAFKV 379
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2030879356 384 TFDQQNYLI-GAAVISEQADELIDDLTLVINQKLTKKELDSYIMGYPTLASDL 435
Cdd:PRK07251  380 VVNTETKEIlGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAENL 432
TGR TIGR01438
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ...
4-438 4.48e-56

thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member of the pyridine nucleotide disulfide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly, where SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily, Cys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-term arm of the protein is proposed to allow broad substrate specificity.


Pssm-ID: 273624 [Multi-domain]  Cd Length: 484  Bit Score: 192.76  E-value: 4.48e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   4 YDAIIIGSGVSGLSAAYGLKEAGKTVLVVEE-------DLWG--GTCPNRGCDPKKVLLSAVEARNRVKQLSGKGFNEIP 74
Cdd:TIGR01438   3 YDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFvtptplgTRWGigGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVEE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  75 TA--NWEELQKFKRTFTDPVPESRKKQLAEAEIDHLSGTARFLDDSSIEV-----NEEVFHADYLVLATGQRPTILPVEG 147
Cdd:TIGR01438  83 TVkhDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKAtnkkgKEKIYSAERFLIATGERPRYPGIPG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 148 -KEYLKTSADFLSLPVLPKEIIFIGGGYIAFELATIANAAGSKVTIVHHNQrPLKEFEASLVEEAVHQMEASGIQFAFGV 226
Cdd:TIGR01438 163 aKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSI-LLRGFDQDCANKVGEHMEEHGVKFKRQF 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 227 ETQKIISEGTR--YRLVGKETELVA--DMIFCATGRQPNTESLALEQANIVFDKHG--IAVNDYLQTSNPKIFACGDIVS 300
Cdd:TIGR01438 242 VPIKVEQIEAKvlVEFTDSTNGIEEeyDTVLLAIGRDACTRKLNLENVGVKINKKTgkIPADEEEQTNVPYIYAVGDILE 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 301 RKtPKLTPVATFEGNYVAKRITDATSEPIKYPIIPTIVYASPKLAEVGVTKS-----HASSSDQVVEMDLT--SWFTYHR 373
Cdd:TIGR01438 322 DK-PELTPVAIQAGRLLAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEkavekFGEENVEVFHSYFWplEWTIPSR 400
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2030879356 374 VNEP--VAKAELTFDQQNYLIGAAVISEQADELIDDLTLVINQKLTKKELDSYIMGYPTLASDLSYL 438
Cdd:TIGR01438 401 DNHNkcYAKLVCNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTL 467
PLN02546 PLN02546
glutathione reductase
4-435 8.22e-55

glutathione reductase


Pssm-ID: 215301 [Multi-domain]  Cd Length: 558  Bit Score: 191.24  E-value: 8.22e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   4 YDAIIIGSGVSGLSAAYGLKEAGKTVLVVE--------EDLWG--GTCPNRGCDPKKVLLSAVEARNRVKQLSGKG--FN 71
Cdd:PLN02546   80 FDLFTIGAGSGGVRASRFASNFGASAAVCElpfatissDTLGGvgGTCVLRGCVPKKLLVYASKYSHEFEESRGFGwkYE 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  72 EIPTANWEELQKFKRTFTDPVPESRKKQLAEAEIDHLSGTARFLDDSSIEVNEEVFHADYLVLATGQRPTILPVEGKEYL 151
Cdd:PLN02546  160 TEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDVDGKLYTARNILIAVGGRPFIPDIPGIEHA 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 152 KTSADFLSLPVLPKEIIFIGGGYIAFELATIANAAGSKVTIVHHNQRPLKEFEASLVEEAVHQMEASGIQFAFGVETQKI 231
Cdd:PLN02546  240 IDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKKVLRGFDEEVRDFVAEQMSLRGIEFHTEESPQAI 319
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 232 I--SEGTRYRLVGKETELVADMIFCATGRQPNTESLALEQANIVFDKHG-IAVNDYLQTSNPKIFACGDIVSRKTpkLTP 308
Cdd:PLN02546  320 IksADGSLSLKTNKGTVEGFSHVMFATGRKPNTKNLGLEEVGVKMDKNGaIEVDEYSRTSVPSIWAVGDVTDRIN--LTP 397
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 309 VATFEGNYVAKriTDATSEPIK--YPIIPTIVYASPKLAEVGVTKSHASSSDQVVEMdLTSWF-----TYHRVNEPVAKA 381
Cdd:PLN02546  398 VALMEGGALAK--TLFGNEPTKpdYRAVPSAVFSQPPIGQVGLTEEQAIEEYGDVDV-FTANFrplkaTLSGLPDRVFMK 474
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2030879356 382 ELTFDQQNYLIGAAVISEQADELIDDLTLVINQKLTKKELDSYIMGYPTLASDL 435
Cdd:PLN02546  475 LIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEEF 528
PLN02507 PLN02507
glutathione reductase
4-435 7.21e-53

glutathione reductase


Pssm-ID: 215281 [Multi-domain]  Cd Length: 499  Bit Score: 184.63  E-value: 7.21e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   4 YDAIIIGSGVSGLSAAYGLKEAGKTVLVVEEDLW----------GGTCPNRGCDPKKVLLSAVEARNRVKQLSGKGF--N 71
Cdd:PLN02507   26 FDLFVIGAGSGGVRAARFSANFGAKVGICELPFHpissesiggvGGTCVIRGCVPKKILVYGATFGGEFEDAKNYGWeiN 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  72 EIPTANWEELQKFKRTFTDPVPESRKKQLAEAEIDHLSGTARFLDDSSIEVNE-----EVFHADYLVLATGQRPTILPVE 146
Cdd:PLN02507  106 EKVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQldgtkLRYTAKHILIATGSRAQRPNIP 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 147 GKEYLKTSADFLSLPVLPKEIIFIGGGYIAFELATIANAAGSKVTIVHHNQRPLKEFEASLVEEAVHQMEASGIQFAFGV 226
Cdd:PLN02507  186 GKELAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRAVVARNLEGRGINLHPRT 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 227 ETQKI--ISEGTRYRLVGKEtELVADMIFCATGRQPNTESLALEQANIVFDKHG-IAVNDYLQTSNPKIFACGDIVSRKT 303
Cdd:PLN02507  266 NLTQLtkTEGGIKVITDHGE-EFVADVVLFATGRAPNTKRLNLEAVGVELDKAGaVKVDEYSRTNIPSIWAIGDVTNRIN 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 304 pkLTPVATFEGNYVAKriTDATSEPIK--YPIIPTIVYASPKLAEVGVTKSHA---SSSDQVVemdLTSWFTYHRvNEPV 378
Cdd:PLN02507  345 --LTPVALMEGTCFAK--TVFGGQPTKpdYENVACAVFCIPPLSVVGLSEEEAveqAKGDILV---FTSSFNPMK-NTIS 416
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2030879356 379 AKAELTF------DQQNYLIGAAVISEQADELIDDLTLVINQKLTKKELDSYIMGYPTLASDL 435
Cdd:PLN02507  417 GRQEKTVmklivdAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEF 479
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
1-350 3.34e-52

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


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 181.89  E-value: 3.34e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   1 MKTYDAIIIGSGVSGLSAAYGLKEAGKTVLVVE-EDLWGGTCPNRGCDPKKVLlsaveaRNRVKQLSG-------KGFNE 72
Cdd:PRK05249    3 MYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIErYRNVGGGCTHTGTIPSKAL------REAVLRLIGfnqnplySSYRV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  73 IPTANWEELQKFKRTFTDPVPESRKKQLAEAEIDHLSGTARFLDDSSIEV-----NEEVFHADYLVLATGQRP---TILP 144
Cdd:PRK05249   77 KLRITFADLLARADHVINKQVEVRRGQYERNRVDLIQGRARFVDPHTVEVecpdgEVETLTADKIVIATGSRPyrpPDVD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 145 VEGKEYLKtSADFLSLPVLPKEIIFIGGGYIAFELATIANAAGSKVTIVHHNQRPLKEFEASLVEEAVHQMEASGIQFAF 224
Cdd:PRK05249  157 FDHPRIYD-SDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSFLDDEISDALSYHLRDSGVTIRH 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 225 GvETQKIISEGTRYRLV----GKetELVADMIFCATGRQPNTESLALEQANIVFDKHG-IAVNDYLQTSNPKIFACGDIV 299
Cdd:PRK05249  236 N-EEVEKVEGGDDGVIVhlksGK--KIKADCLLYANGRTGNTDGLNLENAGLEADSRGqLKVNENYQTAVPHIYAVGDVI 312
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2030879356 300 SrkTPKLTPVATFEGNYVAKRITDATS-EPIKYpiIPTIVYASPKLAEVGVT 350
Cdd:PRK05249  313 G--FPSLASASMDQGRIAAQHAVGEATaHLIED--IPTGIYTIPEISSVGKT 360
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
2-435 2.24e-46

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: 166.69  E-value: 2.24e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   2 KTYDAIIIGSGVSGLSAAYGLKEA-GKTVLVVEED---------LWGGTCPNRGCDPKKVLLSAVEARNRVKQLSGKGFN 71
Cdd:TIGR01423   2 KAFDLVVIGAGSGGLEAGWNAATLyKKRVAVVDVQthhgppfyaALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGWE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  72 ---EIPTANWEELQKFKRTFTDPVPESRKKQLAEAE-IDHLSGTARFLDDSSIEVNE---------EVFHADYLVLATGQ 138
Cdd:TIGR01423  82 fdrSSVKANWKALIAAKNKAVLDINKSYEGMFADTEgLTFFLGWGALEDKNVVLVREsadpksavkERLQAEHILLATGS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 139 RPTILPVEGKEYLKTSADFLSLPVLPKEIIFIGGGYIAFELATIANA---AGSKVTIVHHNQRPLKEFEASLVEEAVHQM 215
Cdd:TIGR01423 162 WPQMLGIPGIEHCISSNEAFYLDEPPRRVLTVGGGFISVEFAGIFNAykpRGGKVTLCYRNNMILRGFDSTLRKELTKQL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 216 EASGIQFAFGVETQKII--SEGTRYRLVGKETELVADMIFCATGRQPNTESLALEQANI-VFDKHGIAVNDYLQTSNPKI 292
Cdd:TIGR01423 242 RANGINIMTNENPAKVTlnADGSKHVTFESGKTLDVDVVMMAIGRVPRTQTLQLDKVGVeLTKKGAIQVDEFSRTNVPNI 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 293 FACGDIVSRKTpkLTPVATFEGNYVAKRITDATSEPIKYPIIPTIVYASPKLAEVGVTKSHASSSDQVVEMDLTSwFT-- 370
Cdd:TIGR01423 322 YAIGDVTDRVM--LTPVAINEGAAFVDTVFGNKPRKTDHTRVASAVFSIPPIGTCGLVEEDAAKKFEKVAVYESS-FTpl 398
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2030879356 371 YHRVNEPVAK---AELTFDQQN-YLIGAAVISEQADELIDDLTLVInqKLTKKELDSY--IMGYPTLASDL 435
Cdd:TIGR01423 399 MHNISGSKYKkfvAKIVTNHADgTVLGVHLLGDSSPEIIQAVGICL--KLNAKISDFYntIGVHPTSAEEL 467
PTZ00058 PTZ00058
glutathione reductase; Provisional
4-435 4.20e-46

glutathione reductase; Provisional


Pssm-ID: 185420 [Multi-domain]  Cd Length: 561  Bit Score: 167.48  E-value: 4.20e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   4 YDAIIIGSGVSGLSAAYGLKEAGKTVLVVEEDLWGGTCPNRGCDPKKVLLSAVEARNRVKQLSGKGFNEIPTANWEELQK 83
Cdd:PTZ00058   49 YDLIVIGGGSGGMAAARRAARNKAKVALVEKDYLGGTCVNVGCVPKKIMFNAASIHDILENSRHYGFDTQFSFNLPLLVE 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  84 FKRTFTDPVPESRKKQLAEAEIDHLSGTARFLDDSSIEV-----------------------------NEEVFHADYLVL 134
Cdd:PTZ00058  129 RRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLIkkvsqvdgeadesdddevtivsagvsqldDGQVIEGKNILI 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 135 ATGQRPTILPVEGKEYLKTSADFLSLPVlPKEIIFIGGGYIAFELATIANAAGSKVTIVHHNQRPLKEFEASLVEEAVHQ 214
Cdd:PTZ00058  209 AVGNKPIFPDVKGKEFTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLRKFDETIINELEND 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 215 MEASGIQF---AFGVETQKIISEGTRYRLVGKETELVADMIFCATGRQPNTESLALEQANIVFDKHGIAVNDYLQTSNPK 291
Cdd:PTZ00058  288 MKKNNINIithANVEEIEKVKEKNLTIYLSDGRKYEHFDYVIYCVGRSPNTEDLNLKALNIKTPKGYIKVDDNQRTSVKH 367
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 292 IFACGDIVSRKTP--------------------------------KLTPVATFEGNYVAKRITDATSEPIKYPIIPTIVY 339
Cdd:PTZ00058  368 IYAVGDCCMVKKNqeiedlnllklyneepylkkkentsgesyynvQLTPVAINAGRLLADRLFGPFSRTTNYKLIPSVIF 447
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 340 ASPKLAEVGVTKSHA-----SSSDQVVEMDLTSWFTYHRVNEPVAKAE-----LTFDQQNYLIGAAVISEQADELIDDLT 409
Cdd:PTZ00058  448 SHPPIGTIGLSEQEAidiygKENVKIYESRFTNLFFSVYDMDPAQKEKtylklVCVGKEELIKGLHIVGLNADEILQGFA 527
                         490       500
                  ....*....|....*....|....*.
gi 2030879356 410 LVINQKLTKKELDSYIMGYPTLASDL 435
Cdd:PTZ00058  528 VALKMNATKADFDETIPIHPTAAEEF 553
PTZ00052 PTZ00052
thioredoxin reductase; Provisional
4-438 4.51e-46

thioredoxin reductase; Provisional


Pssm-ID: 185416 [Multi-domain]  Cd Length: 499  Bit Score: 166.15  E-value: 4.51e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   4 YDAIIIGSGVSGLSAAyglKEA---GKTVLVVE-------EDLWG--GTCPNRGCDPKKVLLSAVEARNRVKQLSGK-GF 70
Cdd:PTZ00052    6 YDLVVIGGGSGGMAAA---KEAaahGKKVALFDyvkpstqGTKWGlgGTCVNVGCVPKKLMHYAANIGSIFHHDSQMyGW 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  71 NEIPTANWEELQKFKRTFTDPVPESRKKQLAEAEIDHLSGTARFLDDSSIEV----NEEVFHADYLVLATGQRPTIL-PV 145
Cdd:PTZ00052   83 KTSSSFNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTVSYgdnsQEETITAKYILIATGGRPSIPeDV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 146 EG-KEYLKTSADFLSLPVLPKEIIFIGGGYIAFELATIANAAGSKVTiVHHNQRPLKEFEASLVEEAVHQMEASGIQFAF 224
Cdd:PTZ00052  163 PGaKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVT-VAVRSIPLRGFDRQCSEKVVEYMKEQGTLFLE 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 225 GVETQKI--ISEGTRYRLVGKETELVaDMIFCATGRQPNTESLALEQANIVFDKHG--IAVNDylQTSNPKIFACGDIVS 300
Cdd:PTZ00052  242 GVVPINIekMDDKIKVLFSDGTTELF-DTVLYATGRKPDIKGLNLNAIGVHVNKSNkiIAPND--CTNIPNIFAVGDVVE 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 301 RKtPKLTPVATFEGNYVAKRITDATSEPIKYPIIPTIVYASPKLAEVGVT--KSHASSSDQVVEMDLTSWFTY-----HR 373
Cdd:PTZ00052  319 GR-PELTPVAIKAGILLARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSseAAIAKYGEDDIEEYLQEFNTLeiaavHR 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 374 VN-EPVAKAELTFD--------------QQNYLIGAAVISEQADELIDDLTLVINQKLTKKELDSYIMGYPTLASDLSYL 438
Cdd:PTZ00052  398 EKhERARKDEYDFDvssnclaklvcvksEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHPTDAEVFMNL 477
PRK13748 PRK13748
putative mercuric reductase; Provisional
8-435 1.55e-45

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 166.09  E-value: 1.55e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   8 IIGSGVSGLSAAYGLKEAGKTVLVVEEDLWGGTCPNRGCDPKKVLLSAVE-ARNRVKQLSGKGF-NEIPTANWEELQKFK 85
Cdd:PRK13748  103 VIGSGGAAMAAALKAVEQGARVTLIERGTIGGTCVNVGCVPSKIMIRAAHiAHLRRESPFDGGIaATVPTIDRSRLLAQQ 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  86 RTFTDPVPESRKKQLAEAE--IDHLSGTARFLDDSSIEV-----NEEVFHADYLVLATGQRPTILPVEGkeyLK-----T 153
Cdd:PRK13748  183 QARVDELRHAKYEGILDGNpaITVLHGEARFKDDQTLIVrlndgGERVVAFDRCLIATGASPAVPPIPG---LKetpywT 259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 154 SADFLSLPVLPKEIIFIGGGYIAFELATIANAAGSKVTIVHHNQRPLKEFEAslVEEAVHQ-MEASGIQFAFGVETQKII 232
Cdd:PRK13748  260 STEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILARSTLFFREDPA--IGEAVTAaFRAEGIEVLEHTQASQVA 337
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 233 SEGTRYRLVGKETELVADMIFCATGRQPNTESLALEQANIVFDKHG-IAVNDYLQTSNPKIFACGDIVSRktPKLTPVAT 311
Cdd:PRK13748  338 HVDGEFVLTTGHGELRADKLLVATGRAPNTRSLALDAAGVTVNAQGaIVIDQGMRTSVPHIYAAGDCTDQ--PQFVYVAA 415
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 312 FEGNYVAKRIT--DATsepIKYPIIPTIVYASPKLAEVGVtkSHASSSDQVVEMD---LTSwftyhrvnEPVAKAELTFD 386
Cdd:PRK13748  416 AAGTRAAINMTggDAA---LDLTAMPAVVFTDPQVATVGY--SEAEAHHDGIETDsrtLTL--------DNVPRALANFD 482
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 387 QQNY-----------LIGAAVISEQADELIDDLTLVINQKLTKKELDSYIMGYPTLASDL 435
Cdd:PRK13748  483 TRGFiklvieegsgrLIGVQAVAPEAGELIQTAALAIRNRMTVQELADQLFPYLTMVEGL 542
PRK07846 PRK07846
mycothione reductase; Reviewed
3-421 4.04e-45

mycothione reductase; Reviewed


Pssm-ID: 181142 [Multi-domain]  Cd Length: 451  Bit Score: 162.82  E-value: 4.04e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   3 TYDAIIIGSGvSG---LSAAYglkeAGKTVLVVEEDLWGGTCPNRGCDPKKVLLSAVEARNRVKQLSGKGFN-EIPTANW 78
Cdd:PRK07846    1 HYDLIIIGTG-SGnsiLDERF----ADKRIAIVEKGTFGGTCLNVGCIPTKMFVYAADVARTIREAARLGVDaELDGVRW 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  79 EELQKfkRTF--TDPVPES--RKKQLAEAEIDHLSGTARFLDDSSIEVNE-EVFHADYLVLATGQRPTILPVEGKEYLK- 152
Cdd:PRK07846   76 PDIVS--RVFgrIDPIAAGgeEYRGRDTPNIDVYRGHARFIGPKTLRTGDgEEITADQVVIAAGSRPVIPPVIADSGVRy 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 153 -TSADFLSLPVLPKEIIFIGGGYIAFELATIANAAGSKVTIVHHNQRPLKEFEA----SLVEEAVHQMEASGIQFAFGVE 227
Cdd:PRK07846  154 hTSDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLDDdiseRFTELASKRWDVRLGRNVVGVS 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 228 TQkiiSEGTRYRLVGKETeLVADMIFCATGRQPNTESLALEQANIVFDKHG-IAVNDYLQTSNPKIFACGDIVSrktP-K 305
Cdd:PRK07846  234 QD---GSGVTLRLDDGST-VEADVLLVATGRVPNGDLLDAAAAGVDVDEDGrVVVDEYQRTSAEGVFALGDVSS---PyQ 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 306 LTPVATFEGNYVAKRI---TDATSEPIKYPiiPTIVYASPKLAEVGVTKSHASSS--DQVVE------------MDLTSW 368
Cdd:PRK07846  307 LKHVANHEARVVQHNLlhpDDLIASDHRFV--PAAVFTHPQIASVGLTENEARAAglDITVKvqnygdvaygwaMEDTTG 384
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2030879356 369 FtyhrvnepvakAELTFDQQN-YLIGAAVISEQADELIDDLTLVINQKLTKKEL 421
Cdd:PRK07846  385 F-----------VKLIADRDTgRLLGAHIIGPQASTLIQPLIQAMSFGLDAREM 427
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
1-432 6.94e-38

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 143.53  E-value: 6.94e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   1 MKTYDAIIIGSGVSGLSAAYGLKEAGKTVLVVEEDLW-------GGTCPNRGCDPKKVLLSAVEARNRVKQLSGK-GFN- 71
Cdd:PRK06327    2 SKQFDVVVIGAGPGGYVAAIRAAQLGLKVACIEAWKNpkgkpalGGTCLNVGCIPSKALLASSEEFENAGHHFADhGIHv 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  72 EIPTANWEELQKFKRTFTDPVPESRKKQLAEAEIDHLSGTARFL--DDSSIEV-----NEEVFHADYLVLATGQRPTILP 144
Cdd:PRK06327   82 DGVKIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVgkTDAGYEIkvtgeDETVITAKHVIIATGSEPRHLP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 145 ---VEGKEYLkTSADFLSLPVLPKEIIFIGGGYIAFELATIANAAGSKVTIVHHNQRPLKEFEASLVEEAVHQMEASGIQ 221
Cdd:PRK06327  162 gvpFDNKIIL-DNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAAADEQVAKEAAKAFTKQGLD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 222 FAFGVETQKIISEGTRYRL-----VGKETELVADMIFCATGRQPNTESLALEQANIVFDKHG-IAVNDYLQTSNPKIFAC 295
Cdd:PRK06327  241 IHLGVKIGEIKTGGKGVSVaytdaDGEAQTLEVDKLIVSIGRVPNTDGLGLEAVGLKLDERGfIPVDDHCRTNVPNVYAI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 296 GDIVSRktPKLTPVATFEGNYVAKRItDATSEPIKYPIIPTIVYASPKLAEVGVTKSHASSsdQVVEMDLTSwFTYHRVN 375
Cdd:PRK06327  321 GDVVRG--PMLAHKAEEEGVAVAERI-AGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLKA--EGVEYKAGK-FPFMANG 394
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2030879356 376 EPVAKAELT-F---------DQqnyLIGAAVISEQADELIDDLTLVINQKLTKKELDSYIMGYPTLA 432
Cdd:PRK06327  395 RALAMGEPDgFvkiiadaktDE---ILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLS 458
PRK08010 PRK08010
pyridine nucleotide-disulfide oxidoreductase; Provisional
1-439 2.50e-37

pyridine nucleotide-disulfide oxidoreductase; Provisional


Pssm-ID: 181196 [Multi-domain]  Cd Length: 441  Bit Score: 141.30  E-value: 2.50e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   1 MKTYDAIIIGSGVSGLSAAYGLKEAGKTVLVVEED--LWGGTCPNRGCDPKKVLLSAVEARN---RVKQLSGKGFNEIPT 75
Cdd:PRK08010    1 MNKYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSnaMYGGTCINIGCIPTKTLVHDAQQHTdfvRAIQRKNEVVNFLRN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  76 ANWEELQKFKrtftdpvpesrkkqlaeaEIDHLSGTARFLDDSSIEV----NEEVFHADYLVLATGQRPTILPVEG---K 148
Cdd:PRK08010   81 KNFHNLADMP------------------NIDVIDGQAEFINNHSLRVhrpeGNLEIHGEKIFINTGAQTVVPPIPGittT 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 149 EYLKTSADFLSLPVLPKEIIFIGGGYIAFELATIANAAGSKVTIVHHNQRPLKEFEASLVEEAVHQMEASGIQFAFGVET 228
Cdd:PRK08010  143 PGVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHV 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 229 QKIISEGTRYRLVGKETELVADMIFCATGRQPNTESLALEQANI-VFDKHGIAVNDYLQTSNPKIFACGDIVSrkTPKLT 307
Cdd:PRK08010  223 ERISHHENQVQVHSEHAQLAVDALLIASGRQPATASLHPENAGIaVNERGAIVVDKYLHTTADNIWAMGDVTG--GLQFT 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 308 PVATFEGNYV-------AKRITDATSEpikypiIPTIVYASPKLAEVGVTKSHASSSD---QVVEMDLTSWFTYHRVNEP 377
Cdd:PRK08010  301 YISLDDYRIVrdellgeGKRSTDDRKN------VPYSVFMTPPLSRVGMTEEQARESGadiQVVTLPVAAIPRARVMNDT 374
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2030879356 378 --VAKAELTFDQQNyLIGAAVISEQADELIDDLTLVINQKLTKKELDSYIMGYPTLASDLSYLL 439
Cdd:PRK08010  375 rgVLKAIVDNKTQR-ILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLNDLF 437
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
7-327 5.76e-36

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 136.81  E-value: 5.76e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   7 IIIGSGVSGLSAAYGLKEAGKT--VLVVEEDlwggtcPNRGCDpkKVLLSavearnrvKQLSGKgfneiptANWEELQKF 84
Cdd:COG1251     5 VIIGAGMAGVRAAEELRKLDPDgeITVIGAE------PHPPYN--RPPLS--------KVLAGE-------TDEEDLLLR 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  85 KRTFtdpvpesrkkqLAEAEIDHLSGT--------ARFLDDSsievNEEVFHADYLVLATGQRPTILPVEGKE-----YL 151
Cdd:COG1251    62 PADF-----------YEENGIDLRLGTrvtaidraARTVTLA----DGETLPYDKLVLATGSRPRVPPIPGADlpgvfTL 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 152 KTSADFLSL-PVLP--KEIIFIGGGYIAFELATIANAAGSKVTIVHHNQRPLkefEASLVEEA---VHQ-MEASGIQFAF 224
Cdd:COG1251   127 RTLDDADALrAALApgKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLL---PRQLDEEAgalLQRlLEALGVEVRL 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 225 GVETQKIISEGTRYRLVGKE-TELVADMIFCATGRQPNTEsLAlEQANIVFDKhGIAVNDYLQTSNPKIFACGDIVS--- 300
Cdd:COG1251   204 GTGVTEIEGDDRVTGVRLADgEELPADLVVVAIGVRPNTE-LA-RAAGLAVDR-GIVVDDYLRTSDPDIYAAGDCAEhpg 280
                         330       340       350
                  ....*....|....*....|....*....|.
gi 2030879356 301 ----RKTPKLTPVATFEGNYVAKRITDATSE 327
Cdd:COG1251   281 pvygRRVLELVAPAYEQARVAAANLAGGPAA 311
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
98-338 8.35e-33

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: 126.08  E-value: 8.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  98 KQLAEAEIDHLSGTA--RF-LDDSSIEV-NEEVFHADYLVLATGQRPTILPVEG------------------KEYLKTSA 155
Cdd:COG0446    44 ESFERKGIDVRTGTEvtAIdPEAKTVTLrDGETLSYDKLVLATGARPRPPPIPGldlpgvftlrtlddadalREALKEFK 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 156 dflslpvlPKEIIFIGGGYIAFELATIANAAGSKVTIVHHNQRPLKEFEASLVEEAVHQMEASGIQFAFGVETQKIISEG 235
Cdd:COG0446   124 --------GKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAIDGDD 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 236 TRYRLVGKETELVADMIFCATGRQPNTEsLAlEQANIVFDKHG-IAVNDYLQTSNPKIFACGD---IVSRKTPKLTPV-- 309
Cdd:COG0446   196 KVAVTLTDGEEIPADLVVVAPGVRPNTE-LA-KDAGLALGERGwIKVDETLQTSDPDVYAAGDcaeVPHPVTGKTVYIpl 273
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2030879356 310 ---ATFEGNYVAKRITDatsEPIKYPIIPTIV 338
Cdd:COG0446   274 asaANKQGRVAAENILG---GPAPFPGLGTFI 302
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
4-302 6.12e-30

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 117.91  E-value: 6.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   4 YDAIIIGSGVSGLSAAYGLKEAGKTVLVVEEDLWGGTCpnrgcdpkkVLLSAVEarNrvkqlsGKGFNEIPTAnWEELQK 83
Cdd:COG0492     1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQL---------ATTKEIE--N------YPGFPEGISG-PELAER 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  84 FKrtftdpvpesrkKQLAEAEIDHLSGTAR--FLDDSSIEV---NEEVFHADYLVLATGQRPTILPVEG-KEYLKTS--- 154
Cdd:COG0492    63 LR------------EQAERFGAEILLEEVTsvDKDDGPFRVttdDGTEYEAKAVIIATGAGPRKLGLPGeEEFEGRGvsy 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 155 ---ADflsLPVLP-KEIIFIGGGYIAFELATIANAAGSKVTIVHHNqrplKEFEAS--LVEEAvhqMEASGIQFAFGVET 228
Cdd:COG0492   131 catCD---GFFFRgKDVVVVGGGDSALEEALYLTKFASKVTLIHRR----DELRASkiLVERL---RANPKIEVLWNTEV 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 229 QKIISEG--TRYRLV----GKETELVADMIFCATGRQPNTEslALEQANIVFDKHG-IAVNDYLQTSNPKIFACGDIVSR 301
Cdd:COG0492   201 TEIEGDGrvEGVTLKnvktGEEKELEVDGVFVAIGLKPNTE--LLKGLGLELDEDGyIVVDEDMETSVPGVFAAGDVRDY 278

                  .
gi 2030879356 302 K 302
Cdd:COG0492   279 K 279
PTZ00153 PTZ00153
lipoamide dehydrogenase; Provisional
2-432 2.66e-29

lipoamide dehydrogenase; Provisional


Pssm-ID: 173442 [Multi-domain]  Cd Length: 659  Bit Score: 120.79  E-value: 2.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   2 KTYDAIIIGSGVSGLSAAYGLKEAGKTVLVV--EEDLWGGTCPNRGCDPKKVLLSAVearNRVKQLSGK----------- 68
Cdd:PTZ00153  115 EEYDVGIIGCGVGGHAAAINAMERGLKVIIFtgDDDSIGGTCVNVGCIPSKALLYAT---GKYRELKNLaklytygiytn 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  69 GFNEIPTANWEELQKFKRTF-TDPvpeSRKKQLAEAEIDHL-SGTARFLDDSSIEVNEEVFHADY--------------- 131
Cdd:PTZ00153  192 AFKNGKNDPVERNQLVADTVqIDI---TKLKEYTQSVIDKLrGGIENGLKSKKFCKNSEHVQVIYerghivdkntiksek 268
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 132 ---------LVLATGQRPTI---LPVEGKEYLkTSADFLSLPVLPKEIIFIGGGYIAFELATIANAAGSKVTIVHHNQRP 199
Cdd:PTZ00153  269 sgkefkvknIIIATGSTPNIpdnIEVDQKSVF-TSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSPQL 347
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 200 L--------KEFEASLVEEA---------VHQMEASG------IQFAfgvETQKIISEGTRYRLvGKETELVADMIFCAT 256
Cdd:PTZ00153  348 LplldadvaKYFERVFLKSKpvrvhlntlIEYVRAGKgnqpviIGHS---ERQTGESDGPKKNM-NDIKETYVDSCLVAT 423
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 257 GRQPNTESLALEQANIVFDKHGIAVNDYLQTSNPK------IFACGDIVSRKT-------PKLTPVATFEGN---YVAKR 320
Cdd:PTZ00153  424 GRKPNTNNLGLDKLKIQMKRGFVSVDEHLRVLREDqevydnIFCIGDANGKQMlahtashQALKVVDWIEGKgkeNVNIN 503
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 321 ITDATSEPIKYPIIPTIVYASPKLA----------------EVGVTKSHASSSDQVVEMDLTSWFTYHRVNEPVAKAELT 384
Cdd:PTZ00153  504 VENWASKPIIYKNIPSVCYTTPELAfigltekeakelyppdNVGVEISFYKANSKVLCENNISFPNNSKNNSYNKGKYNT 583
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 385 FDQQN------YL------IGAAVISEQADELIDDLTLVINQKLTKKELDSYIMGYPTLA 432
Cdd:PTZ00153  584 VDNTEgmvkivYLkdtkeiLGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTIS 643
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
119-332 4.38e-26

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 108.85  E-value: 4.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 119 SIEVNEEVFHADYLVLATGQRPTILPVEG----------KEYLKTSADFLSlpvlPKEIIFIGGGYIAFELATIANAAGS 188
Cdd:PRK04965   90 VVKSQGNQWQYDKLVLATGASAFVPPIPGrelmltlnsqQEYRAAETQLRD----AQRVLVVGGGLIGTELAMDLCRAGK 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 189 KVTIVHHNQRPLkefeASLVEEAV-----HQMEASGIQFAFGVETQKIISEGTRYRL-VGKETELVADMIFCATGRQPNT 262
Cdd:PRK04965  166 AVTLVDNAASLL----ASLMPPEVssrlqHRLTEMGVHLLLKSQLQGLEKTDSGIRAtLDSGRSIEVDAVIAAAGLRPNT 241
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2030879356 263 eSLAlEQANIVFDKhGIAVNDYLQTSNPKIFACGD---IVSRKTPKLTPvATFEGNYVAKRITdATSEPIKYP 332
Cdd:PRK04965  242 -ALA-RRAGLAVNR-GIVVDSYLQTSAPDIYALGDcaeINGQVLPFLQP-IQLSAMALAKNLL-GQNTPLKLP 309
PRK07845 PRK07845
flavoprotein disulfide reductase; Reviewed
7-431 2.08e-19

flavoprotein disulfide reductase; Reviewed


Pssm-ID: 236112 [Multi-domain]  Cd Length: 466  Bit Score: 90.30  E-value: 2.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   7 IIIGSGVSGLSAAYGLKEAGKTVLVVEEDLWGGTCPNRGCDPKKVLLSAVEARNRVKQLSGKGFN---------EIPTAN 77
Cdd:PRK07845    5 VIIGGGPGGYEAALVAAQLGADVTVIERDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRfiddgearvDLPAVN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  78 weelqkfKRTFTDPVPESR--KKQLAEAEIDHLSGTARF----LDDSSIEVN-----EEVFHADYLVLATGQRPTILP-- 144
Cdd:PRK07845   85 -------ARVKALAAAQSAdiRARLEREGVRVIAGRGRLidpgLGPHRVKVTtadggEETLDADVVLIATGASPRILPta 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 145 -VEGKEYLkTSADFLSLPVLPKEIIFIGGGYIAFELATIANAAGSKVTIVHHNQR--PLKEFEASLVEEAVhqMEASGIQ 221
Cdd:PRK07845  158 ePDGERIL-TWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRvlPGEDADAAEVLEEV--FARRGMT 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 222 FAFG--VETQKIISEGTRYRLV-GKETE----LVadmifcATGRQPNTESLALEQANIVFDKHG-IAVNDYLQTSNPKIF 293
Cdd:PRK07845  235 VLKRsrAESVERTGDGVVVTLTdGRTVEgshaLM------AVGSVPNTAGLGLEEAGVELTPSGhITVDRVSRTSVPGIY 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 294 ACGDiVSRKTPkLTPVATFEGnyvakRIT------DATSePIKYPIIPTIVYASPKLAEVGVTKS---HASSSDQVVEMD 364
Cdd:PRK07845  309 AAGD-CTGVLP-LASVAAMQG-----RIAmyhalgEAVS-PLRLKTVASNVFTRPEIATVGVSQAaidSGEVPARTVMLP 380
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2030879356 365 LTSwftyhrvnEPVAKAELT-------FDQQN--YLIGAAVISEQADELIDDLTLVINQKLTKKELDSYIMGYPTL 431
Cdd:PRK07845  381 LAT--------NPRAKMSGLrdgfvklFCRPGtgVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYPSL 448
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
123-311 2.77e-18

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 86.63  E-value: 2.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 123 NEEVF--HADYLVLATGQRPTILPV-----EGKEYLKTSADFLSLPVLPKE-----IIFIGGGYIAFELATIANAAGSKV 190
Cdd:PRK09564   96 TGSIFndTYDKLMIATGARPIIPPIkninlENVYTLKSMEDGLALKELLKDeeiknIVIIGAGFIGLEAVEAAKHLGKNV 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 191 TIVHHNQRPLKE-FEASLVEEAVHQMEASGIQFAFGVETQKIISEGTRYRLVGKETELVADMIFCATGRQPNTEslALEQ 269
Cdd:PRK09564  176 RIIQLEDRILPDsFDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEGVVTDKGEYEADVVIVATGVKPNTE--FLED 253
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2030879356 270 ANIVFDKHG-IAVNDYLQTSNPKIFACGD------IVSRKtPKLTPVAT 311
Cdd:PRK09564  254 TGLKTLKNGaIIVDEYGETSIENIYAAGDcatiynIVSNK-NVYVPLAT 301
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
165-428 9.25e-18

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 84.83  E-value: 9.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 165 KEIIFIGGGYIAFELATIANAAGSKVTIVHHNQRPLKEFEASLVEEAVHQMEASGIQFAFGVETQKIISEGTRYRLVGKE 244
Cdd:PRK13512  149 DKALVVGAGYISLEVLENLYERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDAINGNEVTFKSGKVE 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 245 TelvADMIFCATGRQPNTEslALEQANIVFDKHG-IAVNDYLQTSNPKIFACGDIVS---RKTPKLTPVATFEGNY---- 316
Cdd:PRK13512  229 H---YDMIIEGVGTHPNSK--FIESSNIKLDDKGfIPVNDKFETNVPNIYAIGDIITshyRHVDLPASVPLAWGAHraas 303
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 317 -VAKRITDATSEPIKYPIIPTIV-YASPKLAEVGVTKSHASSSD-QVVEMDLTSWFTYHRVNEPVaKAELTFDQQNYLI- 392
Cdd:PRK13512  304 iVAEQIAGNDTIEFKGFLGNNIVkFFDYTFASVGVKPNELKQFDyKMVEVTQGAHANYYPGNSPL-HLRVYYDTSNRKIl 382
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2030879356 393 -GAAVISEQADELIDDLTLVINQKLTKKELDSYIMGY 428
Cdd:PRK13512  383 rAAAVGKEGADKRIDVLSMAMMNQLTVDELTEFEVAY 419
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
97-321 1.32e-17

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 84.03  E-value: 1.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  97 KKQLAEAEIDHLSGTARFLDDSSIEV---NEEVFHADYLVLATGQRPTILPVEG-KEY---LKTSADFLSL--------- 160
Cdd:COG1252    63 RELLRRAGVRFIQGEVTGIDPEARTVtlaDGRTLSYDYLVIATGSVTNFFGIPGlAEHalpLKTLEDALALrerllaafe 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 161 ---PVLPKEIIFIGGGY----IAFELATIANAAGS---------KVTIVHHNQRPLKEFEASLVEEAVHQMEASGIQfaf 224
Cdd:COG1252   143 raeRRRLLTIVVVGGGPtgveLAGELAELLRKLLRypgidpdkvRITLVEAGPRILPGLGEKLSEAAEKELEKRGVE--- 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 225 gVETQKIISEGTRYRLV-GKETELVADMIFCATGRQPNTeslALEQANIVFDKHG-IAVNDYLQT-SNPKIFACGDIVS- 300
Cdd:COG1252   220 -VHTGTRVTEVDADGVTlEDGEEIPADTVIWAAGVKAPP---LLADLGLPTDRRGrVLVDPTLQVpGHPNVFAIGDCAAv 295
                         250       260
                  ....*....|....*....|....*.
gi 2030879356 301 -----RKTPKLTPVATFEGNYVAKRI 321
Cdd:COG1252   296 pdpdgKPVPKTAQAAVQQAKVLAKNI 321
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
8-300 2.10e-17

NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440259 [Multi-domain]  Cd Length: 434  Bit Score: 84.03  E-value: 2.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   8 IIGSGVSGLSAAYGLKEAGKTVLVVE-EDLWGGTC----PN-RgcDPKKVLlsaveaRNRVKQLSGKGFneiptanweel 81
Cdd:COG0493   126 VVGSGPAGLAAAYQLARAGHEVTVFEaLDKPGGLLrygiPEfR--LPKDVL------DREIELIEALGV----------- 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  82 qKFK------RTFTdpvpesrkkqlaeaeIDHLsgTARFlddssievneevfhaDYLVLATG-QRPTILPVEGK------ 148
Cdd:COG0493   187 -EFRtnvevgKDIT---------------LDEL--LEEF---------------DAVFLATGaGKPRDLGIPGEdlkgvh 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 149 ---EYLKTSA---DFLSLPVLPKEIIFIGGGYIAFELATIANAAGSK-VTIVHHnqRPLKEFEASL--VEEAvhqmEASG 219
Cdd:COG0493   234 samDFLTAVNlgeAPDTILAVGKRVVVIGGGNTAMDCARTALRLGAEsVTIVYR--RTREEMPASKeeVEEA----LEEG 307
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 220 IQFAFGVETQKIISEGT--------------------RYRLV---GKETELVADMIFCATGRQPNTESLaLEQANIVFDK 276
Cdd:COG0493   308 VEFLFLVAPVEIIGDENgrvtglecvrmelgepdesgRRRPVpieGSEFTLPADLVILAIGQTPDPSGL-EEELGLELDK 386
                         330       340
                  ....*....|....*....|....*.
gi 2030879356 277 HG-IAVN-DYLQTSNPKIFACGDIVS 300
Cdd:COG0493   387 RGtIVVDeETYQTSLPGVFAGGDAVR 412
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
130-328 1.03e-15

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


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 79.49  E-value: 1.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 130 DYLVLATGQRPTILPVEGKEY-----LKTSAD---FLSLPVLPKEIIFIGGGYIAFELATIANAAGSKVTIVHHN----Q 197
Cdd:TIGR02374  98 DKLILATGSYPFILPIPGADKkgvyvFRTIEDldaIMAMAQRFKKAAVIGGGLLGLEAAVGLQNLGMDVSVIHHApglmA 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 198 RPLKEFEASLVEEAVHQMeasGIQFAFGVETQKIISEGTRYRLVGKE-TELVADMIFCATGRQPNTEsLALeQANIVFDK 276
Cdd:TIGR02374 178 KQLDQTAGRLLQRELEQK---GLTFLLEKDTVEIVGATKADRIRFKDgSSLEADLIVMAAGIRPNDE-LAV-SAGIKVNR 252
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2030879356 277 hGIAVNDYLQTSNPKIFACGDIVSRKTPKLTPVATF--EGNYVAKRITDATSEP 328
Cdd:TIGR02374 253 -GIIVNDSMQTSDPDIYAVGECAEHNGRVYGLVAPLyeQAKVLADHICGVECEE 305
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
8-299 1.50e-12

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 69.05  E-value: 1.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   8 IIGSGVSGLSAAYGLKEAGKTVLVVEedlwggtcpnrgcdpkkvllsaveARNRVkqlsGkGFNE--IPtanweelqKFK 85
Cdd:PRK11749  145 VIGAGPAGLTAAHRLARKGYDVTIFE------------------------ARDKA----G-GLLRygIP--------EFR 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  86 rtftdpVPesrkKQLAEAEIDHL--SGTarflddsSIEVNEEV------------FHAdyLVLATG-QRPTILPVEGK-- 148
Cdd:PRK11749  188 ------LP----KDIVDREVERLlkLGV-------EIRTNTEVgrditldelragYDA--VFIGTGaGLPRFLGIPGEnl 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 149 -------EYLKTS--ADFLSLPVLPKEIIFIGGGYIAFELATIANAAGSK-VTIVHHnqRPLKEFEASLVEeaVHQMEAS 218
Cdd:PRK11749  249 ggvysavDFLTRVnqAVADYDLPVGKRVVVIGGGNTAMDAARTAKRLGAEsVTIVYR--RGREEMPASEEE--VEHAKEE 324
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 219 GIQFAFGVETQKIISEGT--------RYRLV-------------GKETELVADMIFCATGRQPNTESLALEQAnIVFDKH 277
Cdd:PRK11749  325 GVEFEWLAAPVEILGDEGrvtgvefvRMELGepdasgrrrvpieGSEFTLPADLVIKAIGQTPNPLILSTTPG-LELNRW 403
                         330       340
                  ....*....|....*....|....
gi 2030879356 278 G--IAVNDYLQTSNPKIFACGDIV 299
Cdd:PRK11749  404 GtiIADDETGRTSLPGVFAGGDIV 427
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
8-322 2.22e-12

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 68.09  E-value: 2.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   8 IIGSGVSGLSAAYGLKEAGKTVLVVEEDLWGGTCPNRGCDPKKVLLSAVeaRNRVKQLSGKGFNEIPtanweelqkfkRT 87
Cdd:PRK12770   23 IIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLMLFGIPEFRIPIERV--REGVKELEEAGVVFHT-----------RT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  88 FtdpVPESRKkqLAEAEIDHLSGtarflDDSSIEvnEEVFHADYLVLATGQ-RPTILPVEGKEyLKTSADFLSL------ 160
Cdd:PRK12770   90 K---VCCGEP--LHEEEGDEFVE-----RIVSLE--ELVKKYDAVLIATGTwKSRKLGIPGED-LPGVYSALEYlfrira 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 161 ------------PVLPKEIIFIGGGYIAFELATIANAAGS-KVTIVHhnQRPLKEFEASLVEeaVHQMEASGIQFAFGVE 227
Cdd:PRK12770  157 aklgylpwekvpPVEGKKVVVVGAGLTAVDAALEAVLLGAeKVYLAY--RRTINEAPAGKYE--IERLIARGVEFLELVT 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 228 TQKIISEGT-------RYRLV--------------GKETELVADMIFCATGRQPnTESLALEQANIVFDKHG-IAVNDYL 285
Cdd:PRK12770  233 PVRIIGEGRvegvelaKMRLGepdesgrprpvpipGSEFVLEADTVVFAIGEIP-TPPFAKECLGIELNRKGeIVVDEKH 311
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 2030879356 286 QTSNPKIFACGDIVSrkTPKLTPVATFEGNYVAKRIT 322
Cdd:PRK12770  312 MTSREGVFAAGDVVT--GPSKIGKAIKSGLRAAQSIH 346
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
167-235 8.82e-12

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


Pssm-ID: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 60.68  E-value: 8.82e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2030879356 167 IIFIGGGYIAFELATIANAAGSKVTIVHHNQRPLKEFEASLVEEAVHQMEASGIQFAFGVETQKIISEG 235
Cdd:pfam00070   2 VVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNG 70
PRK14989 PRK14989
nitrite reductase subunit NirD; Provisional
125-300 6.76e-11

nitrite reductase subunit NirD; Provisional


Pssm-ID: 184951 [Multi-domain]  Cd Length: 847  Bit Score: 64.37  E-value: 6.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 125 EVFHaDYLVLATGQRPTILPVEGKE-----YLKTSADFLSLPV---LPKEIIFIGGGYIAFELATIANAAGSKVTIVhhn 196
Cdd:PRK14989   99 TVFY-DKLIMATGSYPWIPPIKGSEtqdcfVYRTIEDLNAIEAcarRSKRGAVVGGGLLGLEAAGALKNLGVETHVI--- 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 197 qrplkEFEASLVEEAVHQM---------EASGIQFAFGVETQKIISEGTRYRLV---GKETELVADMIFCATGRQPNtES 264
Cdd:PRK14989  175 -----EFAPMLMAEQLDQMggeqlrrkiESMGVRVHTSKNTLEIVQEGVEARKTmrfADGSELEVDFIVFSTGIRPQ-DK 248
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2030879356 265 LALEQANIVFDKHGIAVNDYLQTSNPKIFACGDIVS 300
Cdd:PRK14989  249 LATQCGLAVAPRGGIVINDSCQTSDPDIYAIGECAS 284
gltD PRK12810
glutamate synthase subunit beta; Reviewed
8-299 1.29e-10

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 62.87  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   8 IIGSGVSGLSAAYGLKEAGKTVLVVEedlwggtcpnrgcdpkkvllsaveARNRVkqlsGkGFNE--IPTanweelqkFK 85
Cdd:PRK12810  148 VVGSGPAGLAAADQLARAGHKVTVFE------------------------RADRI----G-GLLRygIPD--------FK 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  86 rtFTDPVPESRKKQLAEAEIDHLSGTARFLDDSSIEVNEEvFhaDYLVLATG-QRPTILPVEGKE---------YLKTS- 154
Cdd:PRK12810  191 --LEKEVIDRRIELMEAEGIEFRTNVEVGKDITAEELLAE-Y--DAVFLGTGaYKPRDLGIPGRDldgvhfamdFLIQNt 265
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 155 ----ADFLSLPVLP--KEIIFIGGGYIAFELATIANAAGSK-VT---IvhHNQRPLKEFEASLVEEAVHQMEAS-----G 219
Cdd:PRK12810  266 rrvlGDETEPFISAkgKHVVVIGGGDTGMDCVGTAIRQGAKsVTqrdI--MPMPPSRRNKNNPWPYWPMKLEVSnaheeG 343
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 220 IQFAFGVETQKIISE----------------GTRYRLVGKETELVADMIFCATGRQPNTESLaLEQANIVFDKHG--IAV 281
Cdd:PRK12810  344 VEREFNVQTKEFEGEngkvtgvkvvrtelgeGDFEPVEGSEFVLPADLVLLAMGFTGPEAGL-LAQFGVELDERGrvAAP 422
                         330
                  ....*....|....*...
gi 2030879356 282 NDYLQTSNPKIFACGDIV 299
Cdd:PRK12810  423 DNAYQTSNPKVFAAGDMR 440
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
8-335 1.10e-09

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 60.27  E-value: 1.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   8 IIGSGVSGLSAAYGLKEAGKTVLVVEE-DLWGGT----CPN-RGcdPKKVLlsavearnrvkqlsgkgfneiptanweel 81
Cdd:PRK12771  142 VIGGGPAGLSAAYHLRRMGHAVTIFEAgPKLGGMmrygIPAyRL--PREVL----------------------------- 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  82 qkfkrtftdpvpesrkkqlaEAEIDHLSGT-------ARFLDDSSIEVNEEVFHADYLvlATG-QRPTILPVEGKEYLK- 152
Cdd:PRK12771  191 --------------------DAEIQRILDLgvevrlgVRVGEDITLEQLEGEFDAVFV--AIGaQLGKRLPIPGEDAAGv 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 153 TSA-DFLS------LPVLPKEIIFIGGGYIAFELATIANAAG-SKVTIVHHNQR---PLKEFEaslVEEAvhqmEASGIQ 221
Cdd:PRK12771  249 LDAvDFLRavgegePPFLGKRVVVIGGGNTAMDAARTARRLGaEEVTIVYRRTRedmPAHDEE---IEEA----LREGVE 321
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 222 FAFG--------------------VETQKIISEGTRYRLVGKETELVADMIFCATGRqpNTESLALEQANIVFDKHG-IA 280
Cdd:PRK12771  322 INWLrtpveiegdengatglrvitVEKMELDEDGRPSPVTGEEETLEADLVVLAIGQ--DIDSAGLESVPGVEVGRGvVQ 399
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2030879356 281 VNDYLQ-TSNPKIFACGDIVsrKTPKLTPVATFEGNYVAKRItDA------TSEPIKYPIIP 335
Cdd:PRK12771  400 VDPNFMmTGRPGVFAGGDMV--PGPRTVTTAIGHGKKAARNI-DAflggepYEHRPKREIVK 458
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
123-304 1.57e-09

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 59.55  E-value: 1.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 123 NEEVFHADYLVLATGQRPTILPV-----EGKEYLKTSADFLSL-PVLPKE--IIFIGGGYIAFELATIANAAGSKVTIVH 194
Cdd:PRK09754   95 NGESWHWDQLFIATGAAARPLPLldalgERCFTLRHAGDAARLrEVLQPErsVVIVGAGTIGLELAASATQRRCKVTVIE 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 195 HNQRPLKEFEASLVEE-AVHQMEASGIQFAFgveTQKIIS--EGTRYRLVGKETE-LVADMIFCATGRQPNtESLALEqA 270
Cdd:PRK09754  175 LAATVMGRNAPPPVQRyLLQRHQQAGVRILL---NNAIEHvvDGEKVELTLQSGEtLQADVVIYGIGISAN-DQLARE-A 249
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2030879356 271 NIVFDkHGIAVNDYLQTSNPKIFACGDIVSRKTP 304
Cdd:PRK09754  250 NLDTA-NGIVIDEACRTCDPAIFAGGDVAITRLD 282
PRK13984 PRK13984
putative oxidoreductase; Provisional
161-299 5.93e-08

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 54.77  E-value: 5.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 161 PVLPKEIIFIGGGYIAFE----LATIANAAGSKVTI-VHHNQRPLKEFEASLvEEAVHQMEaSGIQFAFGVETQKIISE- 234
Cdd:PRK13984  415 PKIPRSLVVIGGGNVAMDiarsMARLQKMEYGEVNVkVTSLERTFEEMPADM-EEIEEGLE-EGVVIYPGWGPMEVVIEn 492
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 235 ----GTRYRLV-------GK------ETELV---ADMIFCATGRQPNTESLALE-QANIVFDKHGIAVNDYLQTSNPKIF 293
Cdd:PRK13984  493 dkvkGVKFKKCvevfdeeGRfnpkfdESDQIiveADMVVEAIGQAPDYSYLPEElKSKLEFVRGRILTNEYGQTSIPWLF 572

                  ....*.
gi 2030879356 294 ACGDIV 299
Cdd:PRK13984  573 AGGDIV 578
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
8-300 7.85e-08

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 54.73  E-value: 7.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   8 IIGSGVSGLSAAYGLKEAGKTVLVVEEDLWGGTCPNRGcdpkkvllsavearnrvkqlsgkgfneIPtanweelqKFKrt 87
Cdd:PRK12814  198 IIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMRYG---------------------------IP--------RFR-- 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  88 ftdpVPESrkkqLAEAEIDHLSG-------TARFLDDSSIEVNEEVFHADYLVLATGQRPTI------LP--VEGKEYLK 152
Cdd:PRK12814  241 ----LPES----VIDADIAPLRAmgaefrfNTVFGRDITLEELQKEFDAVLLAVGAQKASKMgipgeeLPgvISGIDFLR 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 153 TSADFlSLPVLPKEIIFIGGGYIAFELATIANAAG-SKVTIVHhnQRPLKEFEA--SLVEEAVHQmeasGIQFAF----- 224
Cdd:PRK12814  313 NVALG-TALHPGKKVVVIGGGNTAIDAARTALRLGaESVTILY--RRTREEMPAnrAEIEEALAE----GVSLRElaapv 385
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 225 -------GVETQKII------SEGTRYRLV---GKETELVADMIFCATGRQPNTEslALEQANIVFDKHGIAVND--YLQ 286
Cdd:PRK12814  386 siersegGLELTAIKmqqgepDESGRRRPVpveGSEFTLQADTVISAIGQQVDPP--IAEAAGIGTSRNGTVKVDpeTLQ 463
                         330
                  ....*....|....
gi 2030879356 287 TSNPKIFACGDIVS 300
Cdd:PRK12814  464 TSVAGVFAGGDCVT 477
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
1-40 1.22e-07

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: 53.68  E-value: 1.22e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2030879356   1 MKTYDAIIIGSGVSGLSAAYGLKEAGKTVLVVE-EDLWGGT 40
Cdd:COG1053     1 DHEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEkVPPRGGH 41
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
2-35 1.23e-07

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 53.37  E-value: 1.23e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2030879356   2 KTYDAIIIGSGVSGLSAAYGLKEAGKTVLVVEED 35
Cdd:COG0665     1 ATADVVVIGGGIAGLSTAYHLARRGLDVTVLERG 34
Pyr_redox_dim pfam02852
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ...
334-432 4.30e-07

Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases.


Pssm-ID: 427019 [Multi-domain]  Cd Length: 109  Bit Score: 48.32  E-value: 4.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 334 IPTIVYASPKLAEVGVTKSHASSSDQVVEmdltswfTYHRVNEPVAKA----------ELTFDQQN-YLIGAAVISEQAD 402
Cdd:pfam02852   1 IPSVVFTDPEIASVGLTEEEAKEKGGEVK-------VGKFPFAANGRAlaygdtdgfvKLVADRETgKILGAHIVGPNAG 73
                          90       100       110
                  ....*....|....*....|....*....|
gi 2030879356 403 ELIDDLTLVINQKLTKKELDSYIMGYPTLA 432
Cdd:pfam02852  74 ELIQEAALAIKMGATVEDLANTIHIHPTLS 103
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
1-39 5.12e-07

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 51.77  E-value: 5.12e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2030879356   1 MKTYDAIIIGSGVSGLSAAYGLKEAGKTVLVVE-EDLWGG 39
Cdd:COG1233     1 MMMYDVVVIGAGIGGLAAAALLARAGYRVTVLEkNDTPGG 40
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
1-149 7.33e-07

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: 51.02  E-value: 7.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   1 MKTYDAIIIGSGVSGLSAAYGLKEAGKTVLVVE--EDLwGGT-CPNR----GCD-PKKVLlsavearnrvkQLSG----K 68
Cdd:COG2072     4 TEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEkaDDV-GGTwRDNRypglRLDtPSHLY-----------SLPFfpnwS 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  69 GFNEIPTanWEE----LQKFKRTF--TDPVPESRKkqLAEAEIDhlSGTARFLddssIEV-NEEVFHADYLVLATG--QR 139
Cdd:COG2072    72 DDPDFPT--GDEilayLEAYADKFglRRPIRFGTE--VTSARWD--EADGRWT----VTTdDGETLTARFVVVATGplSR 141
                         170
                  ....*....|
gi 2030879356 140 PTILPVEGKE 149
Cdd:COG2072   142 PKIPDIPGLE 151
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
1-33 7.45e-07

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 51.08  E-value: 7.45e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2030879356   1 MKTYDAIIIGSGVSGLSAAYGLKEAGKTVLVVE 33
Cdd:COG1231     5 ARGKDVVIVGAGLAGLAAARELRKAGLDVTVLE 37
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
5-39 1.35e-06

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 50.09  E-value: 1.35e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2030879356   5 DAIIIGSGVSGLSAAYGLKEAGKTVLVVEEDLWGG 39
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPG 35
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
130-371 2.23e-06

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 49.77  E-value: 2.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 130 DYLVLATGQRPTILPVEGkeyLKTSADFL--------------------SLPVLPKE-------IIFIGGGYIAFELAT- 181
Cdd:PTZ00318  115 DKLVVAHGARPNTFNIPG---VEERAFFLkevnhargirkrivqcieraSLPTTSVEerkrllhFVVVGGGPTGVEFAAe 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 182 --------IANAAGS-----KVTIVHHNQRPLKEFEASLVEEAVHQMEASGIQfafgVETQKIISEGTRYRLVGKETELV 248
Cdd:PTZ00318  192 ladffrddVRNLNPElveecKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVD----IRTKTAVKEVLDKEVVLKDGEVI 267
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 249 -ADMIFCATG--RQPNTESLALEQanivfDKHG-IAVNDYLQTSN-PKIFACGDIVS---RKTPKLTPVATFEGNYVAKR 320
Cdd:PTZ00318  268 pTGLVVWSTGvgPGPLTKQLKVDK-----TSRGrISVDDHLRVKPiPNVFALGDCAAneeRPLPTLAQVASQQGVYLAKE 342
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2030879356 321 ITDATSEPikyPIIPTIVYAS-PKLAEVGvTKSHASSSDQVVEMDLTSWFTY 371
Cdd:PTZ00318  343 FNNELKGK---PMSKPFVYRSlGSLAYLG-NYSAIVQLGAFDLSGFKALLFW 390
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
5-33 3.11e-06

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: 49.21  E-value: 3.11e-06
                          10        20
                  ....*....|....*....|....*....
gi 2030879356   5 DAIIIGSGVSGLSAAYGLKEAGKTVLVVE 33
Cdd:pfam00890   1 DVLVIGGGLAGLAAALAAAEAGLKVAVVE 29
Pyr_redox_3 pfam13738
Pyridine nucleotide-disulphide oxidoreductase;
120-296 3.88e-06

Pyridine nucleotide-disulphide oxidoreductase;


Pssm-ID: 404603 [Multi-domain]  Cd Length: 296  Bit Score: 48.37  E-value: 3.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 120 IEVNEEVFHADYLVLATG--QRPTILPVegKEYLKTSADFLSLPVLP-KEIIFIGGGYIAFELATIANAAGSKVTIVHHN 196
Cdd:pfam13738 110 VTTSKGTYQARYVIIATGefDFPNKLGV--PELPKHYSYVKDFHPYAgQKVVVIGGYNSAVDAALELVRKGARVTVLYRG 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 197 QrPLKEFEASL-----------VEEAVHQMEasgIQFAFGVETQKIISEGTRYRL---VGKETELVADMIFcATGRQPNT 262
Cdd:pfam13738 188 S-EWEDRDSDPsyslspdtlnrLEELVKNGK---IKAHFNAEVKEITEVDVSYKVhteDGRKVTSNDDPIL-ATGYHPDL 262
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2030879356 263 ESlaLEQANIVFDKHGI-AVNDYLQTSN-PKIFACG 296
Cdd:pfam13738 263 SF--LKKGLFELDEDGRpVLTEETESTNvPGLFLAG 296
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
4-41 4.42e-06

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: 48.68  E-value: 4.42e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2030879356   4 YDAIIIGSGVSGLSAAYGLKEAGKTVLVVE-EDLWGGTC 41
Cdd:COG1232     2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEaSDRVGGLI 40
COG3573 COG3573
Predicted oxidoreductase [General function prediction only];
1-35 4.88e-06

Predicted oxidoreductase [General function prediction only];


Pssm-ID: 442794 [Multi-domain]  Cd Length: 551  Bit Score: 48.64  E-value: 4.88e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2030879356   1 MKTY--DAIIIGSGVSGLSAAYGLKEAGKTVLVVEED 35
Cdd:COG3573     1 MAAMdaDVIVVGAGLAGLVAAAELADAGRRVLLLDQE 37
PRK12831 PRK12831
putative oxidoreductase; Provisional
165-299 7.20e-06

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 48.09  E-value: 7.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 165 KEIIFIGGGYIAFELATIANAAGSKVTIVHhnQRPLKEFEASlVEEaVHQMEASGIQFAF----------------GVET 228
Cdd:PRK12831  282 KKVAVVGGGNVAMDAARTALRLGAEVHIVY--RRSEEELPAR-VEE-VHHAKEEGVIFDLltnpveilgdengwvkGMKC 357
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 229 QKI----ISEGTRYRLV---GKETELVADMIFCATGRQPN------TESLALeqanivfDKHG--IAVNDYLQTSNPKIF 293
Cdd:PRK12831  358 IKMelgePDASGRRRPVeieGSEFVLEVDTVIMSLGTSPNplisstTKGLKI-------NKRGciVADEETGLTSKEGVF 430

                  ....*.
gi 2030879356 294 ACGDIV 299
Cdd:PRK12831  431 AGGDAV 436
NadB COG0029
Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the ...
1-39 8.57e-06

Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 439800 [Multi-domain]  Cd Length: 521  Bit Score: 47.79  E-value: 8.57e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2030879356   1 MKTYDAIIIGSGVSGLSAAYGLKEAGKTVLVVEEDLWGG 39
Cdd:COG0029     2 RLKTDVLVIGSGIAGLSAALKLAERGRVTLLTKGELGES 40
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
161-299 9.29e-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: 9.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 161 PVLP-KEIIFIGGGYIAFELATIANAAGS-KVTIVHhnQRPLKEFEASLveEAVHQMEASGIQFAFGVETQKIISEGT-- 236
Cdd:PRK12778  566 PIKFgKKVAVVGGGNTAMDSARTAKRLGAeRVTIVY--RRSEEEMPARL--EEVKHAKEEGIEFLTLHNPIEYLADEKgw 641
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 237 ------------------RYRLV---GKETELVADMIFCATGRQPN------TESLALEQanivfdKHGIAVNDYLQTSN 289
Cdd:PRK12778  642 vkqvvlqkmelgepdasgRRRPVaipGSTFTVDVDLVIVSVGVSPNplvpssIPGLELNR------KGTIVVDEEMQSSI 715
                         170
                  ....*....|
gi 2030879356 290 PKIFACGDIV 299
Cdd:PRK12778  716 PGIYAGGDIV 725
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
8-41 9.66e-06

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 43.29  E-value: 9.66e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2030879356   8 IIGSGVSGLSAAYGLKEAGKTVLVVE--EDLwGGTC 41
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEkrDRL-GGNA 35
PTZ00367 PTZ00367
squalene epoxidase; Provisional
2-44 1.67e-05

squalene epoxidase; Provisional


Pssm-ID: 240384 [Multi-domain]  Cd Length: 567  Bit Score: 47.15  E-value: 1.67e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2030879356   2 KTYDAIIIGSGVSGLSAAYGLKEAGKTVLVVEEDLWggTCPNR 44
Cdd:PTZ00367   32 YDYDVIIVGGSIAGPVLAKALSKQGRKVLMLERDLF--SKPDR 72
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
1-33 1.72e-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: 46.47  E-value: 1.72e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2030879356   1 MKTYDAIIIGSGVSGLSAAYGLKEAGKTVLVVE 33
Cdd:COG0654     1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVE 33
PRK12834 PRK12834
putative FAD-binding dehydrogenase; Reviewed
1-34 2.06e-05

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 183782 [Multi-domain]  Cd Length: 549  Bit Score: 46.82  E-value: 2.06e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2030879356   1 MKTYDAIIIGSGVSGLSAAYGLKEAGKTVLVVEE 34
Cdd:PRK12834    2 AMDADVIVVGAGLAGLVAAAELADAGKRVLLLDQ 35
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
1-33 6.90e-05

L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 44.75  E-value: 6.90e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2030879356   1 MKTYDAIIIGSGVSGLSAAYGLKEA-GKTVLVVE 33
Cdd:COG0579     2 MEMYDVVIIGAGIVGLALARELSRYeDLKVLVLE 35
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
242-323 2.03e-04

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 43.58  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356 242 GKETELVADMIFCATGRQPNTESLaLEQANIVFDKHG---IAVNDYL--QTSNPKIFACGDIVsrKTPKLTPVATFEGNY 316
Cdd:PRK12769  566 GSEFVMPADAVIMAFGFNPHGMPW-LESHGVTVDKWGriiADVESQYryQTSNPKIFAGGDAV--RGADLVVTAMAEGRH 642

                  ....*..
gi 2030879356 317 VAKRITD 323
Cdd:PRK12769  643 AAQGIID 649
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
4-34 3.87e-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: 42.31  E-value: 3.87e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2030879356   4 YDAIIIGSGVSGLSAAYGLKEAGKTVLVVEE 34
Cdd:TIGR02032   1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEK 31
PLN02576 PLN02576
protoporphyrinogen oxidase
2-39 4.01e-04

protoporphyrinogen oxidase


Pssm-ID: 215314 [Multi-domain]  Cd Length: 496  Bit Score: 42.69  E-value: 4.01e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2030879356   2 KTYDAIIIGSGVSGLSAAYGLKEA-GKTVLVVE-EDLWGG 39
Cdd:PLN02576   11 SSKDVAVVGAGVSGLAAAYALASKhGVNVLVTEaRDRVGG 50
PRK05329 PRK05329
glycerol-3-phosphate dehydrogenase subunit GlpB;
1-32 5.24e-04

glycerol-3-phosphate dehydrogenase subunit GlpB;


Pssm-ID: 235412  Cd Length: 422  Bit Score: 42.14  E-value: 5.24e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2030879356   1 MKtYDAIIIGSGVSGLSAAYGLKEAGKTVLVV 32
Cdd:PRK05329    1 MK-FDVLVIGGGLAGLTAALAAAEAGKRVALV 31
PRK07364 PRK07364
FAD-dependent hydroxylase;
3-86 5.80e-04

FAD-dependent hydroxylase;


Pssm-ID: 236001 [Multi-domain]  Cd Length: 415  Bit Score: 41.93  E-value: 5.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   3 TYDAIIIGSGVSGLSAAYGLKEAGKTVLVVEEDlwggtcpnrgcdpkkvLLSAVEARNR---VKQLSGKGFNEIPTanWE 79
Cdd:PRK07364   18 TYDVAIVGGGIVGLTLAAALKDSGLRIALIEAQ----------------PAEAAAAKGQayaLSLLSARIFEGIGV--WE 79
                          90
                  ....*....|.
gi 2030879356  80 EL----QKFKR 86
Cdd:PRK07364   80 KIlpqiGKFRQ 90
PRK12839 PRK12839
FAD-dependent oxidoreductase;
3-39 7.08e-04

FAD-dependent oxidoreductase;


Pssm-ID: 237223 [Multi-domain]  Cd Length: 572  Bit Score: 41.74  E-value: 7.08e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2030879356   3 TYDAIIIGSGVSGLSAAYGLKEAGKTVLVVEE-DLWGG 39
Cdd:PRK12839    8 TYDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKaSTCGG 45
PRK12775 PRK12775
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ...
157-362 8.73e-04

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


Pssm-ID: 183738 [Multi-domain]  Cd Length: 1006  Bit Score: 41.85  E-value: 8.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  157 FLSLPV-LPKEIIFIGGGYIAFELATIANAAGS-KVTIVHHNQrplkEFEA-SLVEEAVHQMEaSGIQFAF--------- 224
Cdd:PRK12775   563 FLDTPIsLGKSVVVIGAGNTAMDCLRVAKRLGApTVRCVYRRS----EAEApARIEEIRHAKE-EGIDFFFlhspveiyv 637
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  225 -------GVETQKII-----SEGTRYRL-VGKETELVADMIFCATGRQPN------TESLALEQ-ANIVFDKHGIavnDY 284
Cdd:PRK12775   638 daegsvrGMKVEEMElgepdEKGRRKPMpTGEFKDLECDTVIYALGTKANpiitqsTPGLALNKwGNIAADDGKL---ES 714
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  285 LQTSN-PKIFACGDIVSRKTPKLtpVATFEGNYVAKRITDATSEPIKYPIIPTIV--YASPKLAEVGVTKSHASSSDQVV 361
Cdd:PRK12775   715 TQSTNlPGVFAGGDIVTGGATVI--LAMGAGRRAARSIATYLRLGKKWPITAEEAaaFQPGKLLPAIELHTHAGAVAAGA 792

                   .
gi 2030879356  362 E 362
Cdd:PRK12775   793 E 793
PRK06134 PRK06134
putative FAD-binding dehydrogenase; Reviewed
3-194 1.03e-03

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 180419 [Multi-domain]  Cd Length: 581  Bit Score: 41.24  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   3 TYDAIIIGSGVSGLSAAYGLKEAGKTVLVVEED-LWGGTCPNRG------CDPKKVLLSAVE----ARNRVKQLSGKGFN 71
Cdd:PRK06134   12 ECDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDpVFGGTTAWSGgwmwipRNPLARRAGIVEdieqPRTYLRHELGARYD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356  72 EiptanweelqkfkrTFTDPVPESRKKQLAEAEIDhlsgTA-RFLDDSSIevneEVFHADYLVLATGQRPTI-LPVEGKE 149
Cdd:PRK06134   92 A--------------ARIDAFLEAGPHMVAFFERH----TAlRFADGNAI----PDYHGDTPGAATGGRSLIaAPFDGRE 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2030879356 150 ylkTSADFLSLPVLPKEIIFIGGGYIA-FELATIANAAGSKVTIVH 194
Cdd:PRK06134  150 ---LGALLERLRKPLRETSFMGMPIMAgADLAAFLNPTRSFRAFLH 192
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
5-90 1.19e-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: 41.06  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030879356   5 DAIIIGSGVSGLSAAYGLKEAGKTVLVVEEDLW-GGT---------CPNRGCDPKKVLLSAVEARNRVKQLSGKGFNEIP 74
Cdd:pfam12831   1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRGFlGGMltsglvgpdMGFYLNKEQVVGGIAREFRQRLRARGGLPGPYGL 80
                          90
                  ....*....|....*...
gi 2030879356  75 TANWE--ELQKFKRTFTD 90
Cdd:pfam12831  81 RGGWVpfDPEVAKAVLDE 98
PRK08274 PRK08274
FAD-dependent tricarballylate dehydrogenase TcuA;
1-39 1.56e-03

FAD-dependent tricarballylate dehydrogenase TcuA;


Pssm-ID: 236214 [Multi-domain]  Cd Length: 466  Bit Score: 40.63  E-value: 1.56e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2030879356   1 MKTYDAIIIGSGVSGLSAAYGLKEAGKTVLVVE---EDLWGG 39
Cdd:PRK08274    2 ASMVDVLVIGGGNAALCAALAAREAGASVLLLEaapREWRGG 43
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
1-33 1.56e-03

Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];


Pssm-ID: 442577 [Multi-domain]  Cd Length: 445  Bit Score: 40.61  E-value: 1.56e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2030879356   1 MKTYDAIIIGSGVSGLSAAYGLKEAGKTVLVVE 33
Cdd:COG3349     1 MMPPRVVVVGGGLAGLAAAVELAEAGFRVTLLE 33
PRK07208 PRK07208
hypothetical protein; Provisional
5-35 1.83e-03

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 40.64  E-value: 1.83e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2030879356   5 DAIIIGSGVSGLSAAYGLKEAGKTVLVVEED 35
Cdd:PRK07208    6 SVVIIGAGPAGLTAAYELLKRGYPVTVLEAD 36
PRK12844 PRK12844
3-ketosteroid-delta-1-dehydrogenase; Reviewed
3-40 2.13e-03

3-ketosteroid-delta-1-dehydrogenase; Reviewed


Pssm-ID: 183787 [Multi-domain]  Cd Length: 557  Bit Score: 40.51  E-value: 2.13e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2030879356   3 TYDAIIIGSGVSGLSAAYGLKEAGKTVLVVEE-DLWGGT 40
Cdd:PRK12844    6 TYDVVVVGSGGGGMCAALAAADSGLEPLIVEKqDKVGGS 44
solA PRK11259
N-methyl-L-tryptophan oxidase;
1-33 2.44e-03

N-methyl-L-tryptophan oxidase;


Pssm-ID: 236887 [Multi-domain]  Cd Length: 376  Bit Score: 39.82  E-value: 2.44e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2030879356   1 MKTYDAIIIGSGVSGLSAAYGLKEAGKTVLVVE 33
Cdd:PRK11259    1 TMRYDVIVIGLGSMGSAAGYYLARRGLRVLGLD 33
PRK07233 PRK07233
hypothetical protein; Provisional
8-35 2.64e-03

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 39.87  E-value: 2.64e-03
                          10        20
                  ....*....|....*....|....*...
gi 2030879356   8 IIGSGVSGLSAAYGLKEAGKTVLVVEED 35
Cdd:PRK07233    4 IVGGGIAGLAAAYRLAKRGHEVTVFEAD 31
PRK07804 PRK07804
L-aspartate oxidase; Provisional
5-32 2.87e-03

L-aspartate oxidase; Provisional


Pssm-ID: 236102 [Multi-domain]  Cd Length: 541  Bit Score: 39.95  E-value: 2.87e-03
                          10        20
                  ....*....|....*....|....*...
gi 2030879356   5 DAIIIGSGVSGLSAAYGLKEAGKTVLVV 32
Cdd:PRK07804   18 DVVVVGSGVAGLTAALAARRAGRRVLVV 45
PRK12842 PRK12842
putative succinate dehydrogenase; Reviewed
3-40 2.94e-03

putative succinate dehydrogenase; Reviewed


Pssm-ID: 237224 [Multi-domain]  Cd Length: 574  Bit Score: 40.06  E-value: 2.94e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2030879356   3 TYDAIIIGSGVSGLSAAYGLKEAGKTVLVVE-EDLWGGT 40
Cdd:PRK12842    9 TCDVLVIGSGAGGLSAAITARKLGLDVVVLEkEPVFGGT 47
glycerol3P_GlpB TIGR03378
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are ...
4-32 3.05e-03

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: 39.62  E-value: 3.05e-03
                          10        20
                  ....*....|....*....|....*....
gi 2030879356   4 YDAIIIGSGVSGLSAAYGLKEAGKTVLVV 32
Cdd:TIGR03378   1 FDVIIIGGGLAGLSCALRLAEAGKKCAII 29
soxA_mon TIGR01377
sarcosine oxidase, monomeric form; Sarcosine oxidase catalyzes the oxidative demethylation of ...
4-34 4.87e-03

sarcosine oxidase, monomeric form; Sarcosine oxidase catalyzes the oxidative demethylation of sarcosine to glycine. The reaction converts tetrahydrofolate to 5,10-methylene-tetrahydrofolate. The enzyme is known in monomeric and heterotetrameric (alpha,beta,gamma,delta) forms [Energy metabolism, Amino acids and amines]


Pssm-ID: 130444 [Multi-domain]  Cd Length: 380  Bit Score: 39.04  E-value: 4.87e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2030879356   4 YDAIIIGSGVSGLSAAYGLKEAGKTVLVVEE 34
Cdd:TIGR01377   1 FDVIVVGAGIMGCFAAYHLAKHGKKTLLLEQ 31
PRK10015 PRK10015
oxidoreductase; Provisional
4-33 5.33e-03

oxidoreductase; Provisional


Pssm-ID: 182194 [Multi-domain]  Cd Length: 429  Bit Score: 38.80  E-value: 5.33e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2030879356   4 YDAIIIGSGVSGLSAAYGLKEAGKTVLVVE 33
Cdd:PRK10015    6 FDAIVVGAGVAGSVAALVMARAGLDVLVIE 35
PRK06847 PRK06847
hypothetical protein; Provisional
5-35 6.23e-03

hypothetical protein; Provisional


Pssm-ID: 235874 [Multi-domain]  Cd Length: 375  Bit Score: 38.70  E-value: 6.23e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2030879356   5 DAIIIGSGVSGLSAAYGLKEAGKTVLVVEED 35
Cdd:PRK06847    6 KVLIVGGGIGGLSAAIALRRAGIAVDLVEID 36
PRK09126 PRK09126
FAD-dependent hydroxylase;
1-33 7.06e-03

FAD-dependent hydroxylase;


Pssm-ID: 236385 [Multi-domain]  Cd Length: 392  Bit Score: 38.38  E-value: 7.06e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2030879356   1 MKTYDAIIIGSGVSGLSAAYGLKEAGKTVLVVE 33
Cdd:PRK09126    1 MMHSDIVVVGAGPAGLSFARSLAGSGLKVTLIE 33
PLN02985 PLN02985
squalene monooxygenase
5-36 9.99e-03

squalene monooxygenase


Pssm-ID: 178566 [Multi-domain]  Cd Length: 514  Bit Score: 38.34  E-value: 9.99e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2030879356   5 DAIIIGSGVSGLSAAYGLKEAGKTVLVVEEDL 36
Cdd:PLN02985   45 DVIIVGAGVGGSALAYALAKDGRRVHVIERDL 76
 
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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