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Conserved domains on  [gi|1787610894|ref|WP_157933326|]
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NAD(P)/FAD-dependent oxidoreductase [Vibrio lentus]

Protein Classification

NAD(P)/FAD-dependent oxidoreductase( domain architecture ID 11441299)

NAD(P)/FAD-dependent oxidoreductase catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant; similar to sulfide:quinone oxidoreductase which catalyzes the oxidation of hydrogen sulfide using quinone as the electron acceptor

EC:  1.6.-.-
Gene Ontology:  GO:0003954|GO:0006116
PubMed:  15590775|28181562

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
20-329 8.54e-39

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


:

Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 141.81  E-value: 8.54e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894  20 QELEKK---GVSTLLVDKKDYFevTYATLrN--VAAPTVTKDDARKPYQSFLKGA---FLQSGVSEL--TRNQATLDNGS 89
Cdd:COG1252    18 RRLRKKlggDAEVTLIDPNPYH--LFQPL-LpeVAAGTLSPDDIAIPLRELLRRAgvrFIQGEVTGIdpEARTVTLADGR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894  90 TIDFKMAIIASG--TRYPSMPIA-------KSSSAFnlTDRNNELLQHNQNIQNAE--NILIIGGGVVGVELAGEIAHAF 158
Cdd:COG1252    95 TLSYDYLVIATGsvTNFFGIPGLaehalplKTLEDA--LALRERLLAAFERAERRRllTIVVVGGGPTGVELAGELAELL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 159 PSK-----------KLVLAHRGEALLDGFKSKTRRVAFQQLTALGVDIEFNTGYQNISGSYIDQRSGKTATADIVFEAVG 227
Cdd:COG1252   173 RKLlrypgidpdkvRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDADGVTLEDGEEIPADTVIWAAG 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 228 TLPNSEFLQAQLPhvLNNKGFVKVNSQLEVSGEDNLYALGDVADVGEA------KLGYLAQQQGEYLARLISNKLKSKST 301
Cdd:COG1252   253 VKAPPLLADLGLP--TDRRGRVLVDPTLQVPGHPNVFAIGDCAAVPDPdgkpvpKTAQAAVQQAKVLAKNIAALLRGKPL 330

                         330       340
                  ....*....|....*....|....*....
gi 1787610894 302 KGYKRNPLMALIPTGPKSGVAE-MPFAVT 329
Cdd:COG1252   331 KPFRYRDKGCLASLGRGAAVADvGGLKLS 359
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
20-329 8.54e-39

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 141.81  E-value: 8.54e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894  20 QELEKK---GVSTLLVDKKDYFevTYATLrN--VAAPTVTKDDARKPYQSFLKGA---FLQSGVSEL--TRNQATLDNGS 89
Cdd:COG1252    18 RRLRKKlggDAEVTLIDPNPYH--LFQPL-LpeVAAGTLSPDDIAIPLRELLRRAgvrFIQGEVTGIdpEARTVTLADGR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894  90 TIDFKMAIIASG--TRYPSMPIA-------KSSSAFnlTDRNNELLQHNQNIQNAE--NILIIGGGVVGVELAGEIAHAF 158
Cdd:COG1252    95 TLSYDYLVIATGsvTNFFGIPGLaehalplKTLEDA--LALRERLLAAFERAERRRllTIVVVGGGPTGVELAGELAELL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 159 PSK-----------KLVLAHRGEALLDGFKSKTRRVAFQQLTALGVDIEFNTGYQNISGSYIDQRSGKTATADIVFEAVG 227
Cdd:COG1252   173 RKLlrypgidpdkvRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDADGVTLEDGEEIPADTVIWAAG 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 228 TLPNSEFLQAQLPhvLNNKGFVKVNSQLEVSGEDNLYALGDVADVGEA------KLGYLAQQQGEYLARLISNKLKSKST 301
Cdd:COG1252   253 VKAPPLLADLGLP--TDRRGRVLVDPTLQVPGHPNVFAIGDCAAVPDPdgkpvpKTAQAAVQQAKVLAKNIAALLRGKPL 330

                         330       340
                  ....*....|....*....|....*....
gi 1787610894 302 KGYKRNPLMALIPTGPKSGVAE-MPFAVT 329
Cdd:COG1252   331 KPFRYRDKGCLASLGRGAAVADvGGLKLS 359
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 5-285 3.22e-20

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: 89.30  E-value: 3.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894   5 DVLIIGGGFAGVAAAQELEKKGVSTLLVDKKD---YFEVTYA-TLRNVAAPTVT----------KDDARKPYQSFLKGAF 70
Cdd:pfam07992   2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGtcpYGGCVLSkALLGAAEAPEIaslwadlykrKEEVVKKLNNGIEVLL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894  71 LQSGVS------ELTRNQATLDNGSTIDFKMAIIASG--TRYPSMPIAKSSSAFNLT--DRNNELLQHNqniqNAENILI 140
Cdd:pfam07992  82 GTEVVSidpgakKVVLEELVDGDGETITYDRLVIATGarPRLPPIPGVELNVGFLVRtlDSAEALRLKL----LPKRVVV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 141 IGGGVVGVELAGeIAHAFPsKKLVLAHRGEALLDGFKSKTRRVAFQQLTALGVDIEFNTGYQNISGSYIDQR----SGKT 216
Cdd:pfam07992 158 VGGGYIGVELAA-ALAKLG-KEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEvilkDGTE 235

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 217 ATADIVFEAVGTLPNSEFL-QAQLPhvLNNKGFVKVNSQLEVSgEDNLYALGDVaDVGEAKLGYLAQQQG 285
Cdd:pfam07992 236 IDADLVVVAIGRRPNTELLeAAGLE--LDERGGIVVDEYLRTS-VPGIYAAGDC-RVGGPELAQNAVAQG 301
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 90-299 7.08e-20

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: 90.39  E-value: 7.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894  90 TIDFKMAIIASGT--RYPSMPIAK-------SSSAFNLTdrnnellqhnqniQNAENILIIGGGVVGVELAgEIAHAFPS 160
Cdd:TIGR01350 129 TLEAKNIIIATGSrpRSLPGPFDFdgkvvitSTGALNLE-------------EVPESLVIIGGGVIGIEFA-SIFASLGS 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 161 KKLVLaHRGEALLDGFKSKTRRVAFQQLTALGVDIEFNTGYQNISGS------YIDQRSGKTATADIVFEAVGTLPNSEF 234
Cdd:TIGR01350 195 KVTVI-EMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEKNddqvtyENKGGETETLTGEKVLVAVGRKPNTEG 273

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1787610894 235 LQ-AQLPHVLNNKGFVKVNSQLEVSgEDNLYALGDVadVGEAKLGYLAQQQGEYLARLISNKLKSK 299
Cdd:TIGR01350 274 LGlEKLGVELDERGRIVVDEYMRTN-VPGIYAIGDV--IGGPMLAHVASHEGIVAAENIAGKEPAH 336
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
 97-270 7.78e-18

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 84.06  E-value: 7.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894  97 IIASGTRYPSMPIaKSSSAFNL-----TDRNNELLQHNQniqnAENILIIGGGVVGVELAGEIAHAFPSKKLVlaHRGEA 171
Cdd:PRK13512  110 ILSPGASANSLGF-ESDITFTLrnledTDAIDQFIKANQ----VDKALVVGAGYISLEVLENLYERGLHPTLI--HRSDK 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 172 LLDGFKSKTRRVAFQQLTALGVDIEFNTGYQNISGSYIDQRSGKTATADIVFEAVGTLPNSEFLQAQlPHVLNNKGFVKV 251
Cdd:PRK13512  183 INKLMDADMNQPILDELDKREIPYRLNEEIDAINGNEVTFKSGKVEHYDMIIEGVGTHPNSKFIESS-NIKLDDKGFIPV 261

                         170
                  ....*....|....*....
gi 1787610894 252 NSQLEVSGEdNLYALGDVA 270
Cdd:PRK13512  262 NDKFETNVP-NIYAIGDII 279
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
20-329 8.54e-39

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 141.81  E-value: 8.54e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894  20 QELEKK---GVSTLLVDKKDYFevTYATLrN--VAAPTVTKDDARKPYQSFLKGA---FLQSGVSEL--TRNQATLDNGS 89
Cdd:COG1252    18 RRLRKKlggDAEVTLIDPNPYH--LFQPL-LpeVAAGTLSPDDIAIPLRELLRRAgvrFIQGEVTGIdpEARTVTLADGR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894  90 TIDFKMAIIASG--TRYPSMPIA-------KSSSAFnlTDRNNELLQHNQNIQNAE--NILIIGGGVVGVELAGEIAHAF 158
Cdd:COG1252    95 TLSYDYLVIATGsvTNFFGIPGLaehalplKTLEDA--LALRERLLAAFERAERRRllTIVVVGGGPTGVELAGELAELL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 159 PSK-----------KLVLAHRGEALLDGFKSKTRRVAFQQLTALGVDIEFNTGYQNISGSYIDQRSGKTATADIVFEAVG 227
Cdd:COG1252   173 RKLlrypgidpdkvRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDADGVTLEDGEEIPADTVIWAAG 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 228 TLPNSEFLQAQLPhvLNNKGFVKVNSQLEVSGEDNLYALGDVADVGEA------KLGYLAQQQGEYLARLISNKLKSKST 301
Cdd:COG1252   253 VKAPPLLADLGLP--TDRRGRVLVDPTLQVPGHPNVFAIGDCAAVPDPdgkpvpKTAQAAVQQAKVLAKNIAALLRGKPL 330

                         330       340
                  ....*....|....*....|....*....
gi 1787610894 302 KGYKRNPLMALIPTGPKSGVAE-MPFAVT 329
Cdd:COG1252   331 KPFRYRDKGCLASLGRGAAVADvGGLKLS 359
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 81-295 2.86e-23

Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 100.16  E-value: 2.86e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894  81 NQATLDNGSTIDFKMAIIASGTRyPSMP-IAK--------SSSAFNLTDRnnellqhnqniqnAENILIIGGGVVGVELA 151
Cdd:COG1249   119 HTVEVTGGETLTADHIVIATGSR-PRVPpIPGldevrvltSDEALELEEL-------------PKSLVVIGGGYIGLEFA 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 152 GeIAHAFPSkKLVLAHRGEALLDGFKSKTRRVAFQQLTALGVDIEFNTGYQNISGS-------YIDQRSGKTATADIVFE 224
Cdd:COG1249   185 Q-IFARLGS-EVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTgdgvtvtLEDGGGEEAVEADKVLV 262

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1787610894 225 AVGTLPNSEFLqaQLPHV---LNNKGFVKVNSQLEVSgEDNLYALGDVadVGEAKLGYLAQQQGEYLARLISNK 295
Cdd:COG1249   263 ATGRRPNTDGL--GLEAAgveLDERGGIKVDEYLRTS-VPGIYAIGDV--TGGPQLAHVASAEGRVAAENILGK 331
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 5-285 3.22e-20

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: 89.30  E-value: 3.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894   5 DVLIIGGGFAGVAAAQELEKKGVSTLLVDKKD---YFEVTYA-TLRNVAAPTVT----------KDDARKPYQSFLKGAF 70
Cdd:pfam07992   2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGtcpYGGCVLSkALLGAAEAPEIaslwadlykrKEEVVKKLNNGIEVLL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894  71 LQSGVS------ELTRNQATLDNGSTIDFKMAIIASG--TRYPSMPIAKSSSAFNLT--DRNNELLQHNqniqNAENILI 140
Cdd:pfam07992  82 GTEVVSidpgakKVVLEELVDGDGETITYDRLVIATGarPRLPPIPGVELNVGFLVRtlDSAEALRLKL----LPKRVVV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 141 IGGGVVGVELAGeIAHAFPsKKLVLAHRGEALLDGFKSKTRRVAFQQLTALGVDIEFNTGYQNISGSYIDQR----SGKT 216
Cdd:pfam07992 158 VGGGYIGVELAA-ALAKLG-KEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEvilkDGTE 235

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 217 ATADIVFEAVGTLPNSEFL-QAQLPhvLNNKGFVKVNSQLEVSgEDNLYALGDVaDVGEAKLGYLAQQQG 285
Cdd:pfam07992 236 IDADLVVVAIGRRPNTELLeAAGLE--LDERGGIVVDEYLRTS-VPGIYAAGDC-RVGGPELAQNAVAQG 301
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 90-299 7.08e-20

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: 90.39  E-value: 7.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894  90 TIDFKMAIIASGT--RYPSMPIAK-------SSSAFNLTdrnnellqhnqniQNAENILIIGGGVVGVELAgEIAHAFPS 160
Cdd:TIGR01350 129 TLEAKNIIIATGSrpRSLPGPFDFdgkvvitSTGALNLE-------------EVPESLVIIGGGVIGIEFA-SIFASLGS 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 161 KKLVLaHRGEALLDGFKSKTRRVAFQQLTALGVDIEFNTGYQNISGS------YIDQRSGKTATADIVFEAVGTLPNSEF 234
Cdd:TIGR01350 195 KVTVI-EMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEKNddqvtyENKGGETETLTGEKVLVAVGRKPNTEG 273

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1787610894 235 LQ-AQLPHVLNNKGFVKVNSQLEVSgEDNLYALGDVadVGEAKLGYLAQQQGEYLARLISNKLKSK 299
Cdd:TIGR01350 274 LGlEKLGVELDERGRIVVDEYMRTN-VPGIYAIGDV--IGGPMLAHVASHEGIVAAENIAGKEPAH 336
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
 90-271 4.39e-18

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: 85.02  E-value: 4.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894  90 TIDFKMAIIASGTrYPSMP-------IAKSSSAFNLTdrnnellqhnqniQNAENILIIGGGVVGVELAGeIAHAF--PS 160
Cdd:TIGR01423 149 RLQAEHILLATGS-WPQMLgipgiehCISSNEAFYLD-------------EPPRRVLTVGGGFISVEFAG-IFNAYkpRG 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 161 KKLVLAHRGEALLDGFKSKTRRVAFQQLTALGVDIEFNTGYQNIS----GS-YIDQRSGKTATADIVFEAVGTLPNSEFL 235
Cdd:TIGR01423 214 GKVTLCYRNNMILRGFDSTLRKELTKQLRANGINIMTNENPAKVTlnadGSkHVTFESGKTLDVDVVMMAIGRVPRTQTL 293

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1787610894 236 QAQLPHV-LNNKGFVKVNsQLEVSGEDNLYALGDVAD 271
Cdd:TIGR01423 294 QLDKVGVeLTKKGAIQVD-EFSRTNVPNIYAIGDVTD 329
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
 97-270 7.78e-18

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 84.06  E-value: 7.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894  97 IIASGTRYPSMPIaKSSSAFNL-----TDRNNELLQHNQniqnAENILIIGGGVVGVELAGEIAHAFPSKKLVlaHRGEA 171
Cdd:PRK13512  110 ILSPGASANSLGF-ESDITFTLrnledTDAIDQFIKANQ----VDKALVVGAGYISLEVLENLYERGLHPTLI--HRSDK 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 172 LLDGFKSKTRRVAFQQLTALGVDIEFNTGYQNISGSYIDQRSGKTATADIVFEAVGTLPNSEFLQAQlPHVLNNKGFVKV 251
Cdd:PRK13512  183 INKLMDADMNQPILDELDKREIPYRLNEEIDAINGNEVTFKSGKVEHYDMIIEGVGTHPNSKFIESS-NIKLDDKGFIPV 261

                         170
                  ....*....|....*....
gi 1787610894 252 NSQLEVSGEdNLYALGDVA 270
Cdd:PRK13512  262 NDKFETNVP-NIYAIGDII 279
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 80-292 3.72e-17

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: 81.01  E-value: 3.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894  80 RNQATLDNGSTIDFKMAIIASGTRYPSMPI--AKSSSAFNLT-----DRNNELLQHnqniQNAENILIIGGGVVGVELAG 152
Cdd:COG0446    66 AKTVTLRDGETLSYDKLVLATGARPRPPPIpgLDLPGVFTLRtlddaDALREALKE----FKGKRAVVIGGGPIGLELAE 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 153 EIAHAfpSKKLVLAHRGEALLDGFKSKTRRVAFQQLTALGVDIEFNTGYQNISGS---YIDQRSGKTATADIVFEAVGTL 229
Cdd:COG0446   142 ALRKR--GLKVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAIDGDdkvAVTLTDGEEIPADLVVVAPGVR 219

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1787610894 230 PNSEFLQ-AQLPhvLNNKGFVKVNSQLEVSgEDNLYALGDVADVGEA--------KLGYLAQQQGEYLARLI 292
Cdd:COG0446   220 PNTELAKdAGLA--LGERGWIKVDETLQTS-DPDVYAAGDCAEVPHPvtgktvyiPLASAANKQGRVAAENI 288
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 140-326 5.87e-16

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 78.27  E-value: 5.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 140 IIGGGVVGVELAGEIAHAF------------PSKKLVLAHRGEALLDGFKSKTRRVAFQQLTALGVDIEFNTGYQNISGS 207
Cdd:PTZ00318  178 VVGGGPTGVEFAAELADFFrddvrnlnpelvEECKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEVLDK 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 208 YIDQRSGKTATADIVFEAVGTLPNSefLQAQLPHVLNNKGFVKVNSQLEVSGEDNLYALGDVADVGEAKLGYLAQ---QQ 284
Cdd:PTZ00318  258 EVVLKDGEVIPTGLVVWSTGVGPGP--LTKQLKVDKTSRGRISVDDHLRVKPIPNVFALGDCAANEERPLPTLAQvasQQ 335

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1787610894 285 GEYLARLISNKLKSK-STKGYKRNPLMALIPTGPKSGVAEMPF 326
Cdd:PTZ00318  336 GVYLAKEFNNELKGKpMSKPFVYRSLGSLAYLGNYSAIVQLGA 378
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
124-280 9.35e-16

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 77.65  E-value: 9.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 124 ELLQHNQNIQNAENILIIGGGVVGVELAGEIAHAfpSKKLVLAHRGEALLDG----FKSkTRrvAFQQLTALGVDIEFNT 199
Cdd:PRK04965  130 EYRAAETQLRDAQRVLVVGGGLIGTELAMDLCRA--GKAVTLVDNAASLLASlmppEVS-SR--LQHRLTEMGVHLLLKS 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 200 GYQNI----SGSYIDQRSGKTATADIVFEAVGTLPNSEFLQAQLPHVlnNKGfVKVNSQLEVSgEDNLYALGDVADVGEA 275
Cdd:PRK04965  205 QLQGLektdSGIRATLDSGRSIEVDAVIAAAGLRPNTALARRAGLAV--NRG-IVVDSYLQTS-APDIYALGDCAEINGQ 280


                  ....*
gi 1787610894 276 KLGYL 280
Cdd:PRK04965  281 VLPFL 285
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
79-297 3.51e-14

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 72.87  E-value: 3.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894  79 TRNQATLDNGSTIDFKMAIIASGTRY--PSMPIAKSSSAFNLTDRNnELLQHNQNIQNAENILIIGGGVVGVELAGEIAH 156
Cdd:COG1251    85 AARTVTLADGETLPYDKLVLATGSRPrvPPIPGADLPGVFTLRTLD-DADALRAALAPGKRVVVIGGGLIGLEAAAALRK 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 157 AfpSKKLVLAHRGEALLdgfksktRRV-------AFQQ-LTALGVDIEFNTGYQNISGsyiDQR-------SGKTATADI 221
Cdd:COG1251   164 R--GLEVTVVERAPRLL-------PRQldeeagaLLQRlLEALGVEVRLGTGVTEIEG---DDRvtgvrlaDGEELPADL 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 222 VFEAVGTLPNSEFLQ-AQLpHVlnNKGfVKVNSQLEVSgEDNLYALGDVADVGEAKLGYL-------AQQQGEYLARLI- 292
Cdd:COG1251   232 VVVAIGVRPNTELARaAGL-AV--DRG-IVVDDYLRTS-DPDIYAAGDCAEHPGPVYGRRvlelvapAYEQARVAAANLa 306

                         250
                  ....*....|....*.
gi 1787610894 293 -----------SNKLK 297
Cdd:COG1251   307 ggpaayegsvpSTKLK 322
PRK06116 PRK06116
glutathione reductase; Validated
 87-271 6.79e-14

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 72.11  E-value: 6.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894  87 NGSTIDFKMAIIASGTR--YPSMPIAK----SSSAFNLTdrnnELLQHnqniqnaenILIIGGGVVGVELAGeIAHAFPS 160
Cdd:PRK06116  126 NGERYTADHILIATGGRpsIPDIPGAEygitSDGFFALE----ELPKR---------VAVVGAGYIAVEFAG-VLNGLGS 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 161 kKLVLAHRGEALLDGFKSKTRRVAFQQLTALGVDIEFNTGYQNIS----GSY-IDQRSGKTATADIVFEAVGTLPNSEFL 235
Cdd:PRK06116  192 -ETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEknadGSLtLTLEDGETLTVDCLIWAIGREPNTDGL 270

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1787610894 236 QAQLPHV-LNNKGFVKVNSQLEVSgEDNLYALGDVAD 271
Cdd:PRK06116  271 GLENAGVkLNEKGYIIVDEYQNTN-VPGIYAVGDVTG 306
PRK06370 PRK06370
FAD-containing oxidoreductase;
87-269 3.44e-12

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 67.15  E-value: 3.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894  87 NGSTIDFKMAIIASGTR--YPSMP-IAK-----SSSAFNLTdrnnELLQHnqniqnaenILIIGGGVVGVELAgEIAHAF 158
Cdd:PRK06370  128 GGETLRAKRIFINTGARaaIPPIPgLDEvgyltNETIFSLD----ELPEH---------LVIIGGGYIGLEFA-QMFRRF 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 159 PSkKLVLAHRGEALLDGFKSKTRRVAFQQLTALGVDIEFNTGYQNISGS------YIDQRSGK-TATADIVFEAVGTLPN 231
Cdd:PRK06370  194 GS-EVTVIERGPRLLPREDEDVAAAVREILEREGIDVRLNAECIRVERDgdgiavGLDCNGGApEITGSHILVAVGRVPN 272

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1787610894 232 SEFLQAQLPHV-LNNKGFVKVNSQLEVSgEDNLYALGDV 269
Cdd:PRK06370  273 TDDLGLEAAGVeTDARGYIKVDDQLRTT-NPGIYAAGDC 310
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 87-269 5.28e-11

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 63.66  E-value: 5.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894  87 NGSTIDFKMAIIASGTRYPSMP---------IAKSSSAFNLTDRnnellqhnqniqnAENILIIGGGVVGVELaGEIAHA 157
Cdd:PRK06292  125 NGERIEAKNIVIATGSRVPPIPgvwlilgdrLLTSDDAFELDKL-------------PKSLAVIGGGVIGLEL-GQALSR 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 158 FPSKKLVLAhRGEALLDGFKSKTRRVAfqqLTALGVDIEFNTGYQNIS---------GSYIDQRSGKTATADIVFEAVGT 228
Cdd:PRK06292  191 LGVKVTVFE-RGDRILPLEDPEVSKQA---QKILSKEFKIKLGAKVTSveksgdekvEELEKGGKTETIEADYVLVATGR 266

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1787610894 229 LPNSEFLQAQLPHV-LNNKGFVKVNSQLEvSGEDNLYALGDV 269
Cdd:PRK06292  267 RPNTDGLGLENTGIeLDERGRPVVDEHTQ-TSVPGIYAAGDV 307
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 84-293 2.86e-10

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 61.32  E-value: 2.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894  84 TLDNGSTIDFKMAIIASGTRYPSMP--------IAKSSSAFNLTdrnnELLQHnqniqnaenILIIGGGVVGVELAGeIA 155
Cdd:PRK06416  126 TEDGEQTYTAKNIILATGSRPRELPgieidgrvIWTSDEALNLD----EVPKS---------LVVIGGGYIGVEFAS-AY 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 156 HAFPSKKLVLahrgEAL---LDGFKSKTRRVAFQQLTALGVDIEFNT-------GYQNISGSYIDQRSGKTATADIVFEA 225
Cdd:PRK06416  192 ASLGAEVTIV----EALpriLPGEDKEISKLAERALKKRGIKIKTGAkakkveqTDDGVTVTLEDGGKEETLEADYVLVA 267

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1787610894 226 VGTLPNSEFLQaqlphvLNN------KGFVKVNSQLEvSGEDNLYALGDVadVGEAKLGYLAQQQGEYLARLIS 293
Cdd:PRK06416  268 VGRRPNTENLG------LEElgvktdRGFIEVDEQLR-TNVPNIYAIGDI--VGGPMLAHKASAEGIIAAEAIA 332
PRK07846 PRK07846
mycothione reductase; Reviewed
 88-271 8.03e-10

mycothione reductase; Reviewed


Pssm-ID: 181142 [Multi-domain]  Cd Length: 451  Bit Score: 59.97  E-value: 8.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894  88 GSTIDFKMAIIASGTRyPSMP--IAKSSSAFNLTD---RNNELLQHnqniqnaenILIIGGGVVGVELageiAHAFPS-- 160
Cdd:PRK07846  124 GEEITADQVVIAAGSR-PVIPpvIADSGVRYHTSDtimRLPELPES---------LVIVGGGFIAAEF----AHVFSAlg 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 161 KKLVLAHRGEALLDGFKSKTRRvAFQQLTALGVDIEFNTGYQNI----SGSYIDQRSGKTATADIVFEAVGTLPNSEFLQ 236
Cdd:PRK07846  190 VRVTVVNRSGRLLRHLDDDISE-RFTELASKRWDVRLGRNVVGVsqdgSGVTLRLDDGSTVEADVLLVATGRVPNGDLLD 268

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1787610894 237 AQLPHV-LNNKGFVKVNsQLEVSGEDNLYALGDVAD 271
Cdd:PRK07846  269 AAAAGVdVDEDGRVVVD-EYQRTSAEGVFALGDVSS 303
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
 64-292 2.48e-08

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 55.32  E-value: 2.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894  64 SFLKG-AFLQSGVSELTRNQATLDNGSTIDFKMAIIASGTRYPSMP--------IAKSSSAFNLTDRNNELLqhnqniqn 134
Cdd:PRK06327  116 TVLKGrGSFVGKTDAGYEIKVTGEDETVITAKHVIIATGSEPRHLPgvpfdnkiILDNTGALNFTEVPKKLA-------- 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 135 aenilIIGGGVVGVELaGEIAHAFPSKKLVLahrgEAlLDGF-------KSKTrrvAFQQLTALGVDIEFN-------TG 200
Cdd:PRK06327  188 -----VIGAGVIGLEL-GSVWRRLGAEVTIL----EA-LPAFlaaadeqVAKE---AAKAFTKQGLDIHLGvkigeikTG 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 201 YQNISGSYID-QRSGKTATADIVFEAVGTLPNSEFLQAQLPHV-LNNKGFVKVNSQLEvSGEDNLYALGDVadVGEAKLG 278
Cdd:PRK06327  254 GKGVSVAYTDaDGEAQTLEVDKLIVSIGRVPNTDGLGLEAVGLkLDERGFIPVDDHCR-TNVPNVYAIGDV--VRGPMLA 330

                         250
                  ....*....|....
gi 1787610894 279 YLAQQQGEYLARLI 292
Cdd:PRK06327  331 HKAEEEGVAVAERI 344
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 85-272 3.97e-08

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 54.66  E-value: 3.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894  85 LDNGSTID--FKMAIIASGTR--YPSMPIAKSSSAFNLTDRNN-----ELLQhNQNIQNaenILIIGGGVVGVELAgEIA 155
Cdd:PRK09564   94 LKTGSIFNdtYDKLMIATGARpiIPPIKNINLENVYTLKSMEDglalkELLK-DEEIKN---IVIIGAGFIGLEAV-EAA 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 156 HAFPSKKLVLAHRGEALLDGFKSKTRRVAFQQLTALGVDIEFNTGYQNISGsyiDQRSGKTAT------ADIVFEAVGTL 229
Cdd:PRK09564  169 KHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSLIG---EDKVEGVVTdkgeyeADVVIVATGVK 245

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1787610894 230 PNSEFLQAQLPHVLNNkGFVKVNSQLEVSgEDNLYALGDVADV 272
Cdd:PRK09564  246 PNTEFLEDTGLKTLKN-GAIIVDEYGETS-IENIYAAGDCATI 286
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 137-207 5.12e-07

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: 46.81  E-value: 5.12e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1787610894 137 NILIIGGGVVGVELAGEIAHAfpSKKLVLAHRGEALLDGFKSKTRRVAFQQLTALGVDIEFNTGYQNISGS 207
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARL--GSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGN 69
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
138-316 1.71e-06

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


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 49.38  E-value: 1.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 138 ILIIGGGVVGVELAgEIAHAFpSKKLVLAHRGEALLDgFKSKTRRVAFQ-QLTALGVDIEFNTGYQNI----SGSYIDQR 212
Cdd:PRK05249  178 LIIYGAGVIGCEYA-SIFAAL-GVKVTLINTRDRLLS-FLDDEISDALSyHLRDSGVTIRHNEEVEKVeggdDGVIVHLK 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 213 SGKTATADIVFEAVGTLPNSEFLQaqLPHV---LNNKGFVKVNSQLEVSgEDNLYALGDVadVGEAKLGYLAQQQGEYLA 289
Cdd:PRK05249  255 SGKKIKADCLLYANGRTGNTDGLN--LENAgleADSRGQLKVNENYQTA-VPHIYAVGDV--IGFPSLASASMDQGRIAA 329

                         170       180
                  ....*....|....*....|....*..
gi 1787610894 290 RLISnklkskstkGYKRNPLMALIPTG 316
Cdd:PRK05249  330 QHAV---------GEATAHLIEDIPTG 347
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
136-271 4.62e-06

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 47.81  E-value: 4.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 136 ENILIIGGGVVGVELAGEIAHAfpSKKLVLAHRGeallDGFKSKtrRVAFQQLTAL-GVDIEFNT------GYQNISGSY 208
Cdd:COG0492   142 KDVVVVGGGDSALEEALYLTKF--ASKVTLIHRR----DELRAS--KILVERLRANpKIEVLWNTevteieGDGRVEGVT 213

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1787610894 209 I-DQRSGKTAT--ADIVFEAVGTLPNSEFLqAQLPHVLNNKGFVKVNSQLEVSgEDNLYALGDVAD 271
Cdd:COG0492   214 LkNVKTGEEKEleVDGVFVAIGLKPNTELL-KGLGLELDEDGYIVVDEDMETS-VPGVFAAGDVRD 277
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
 138-299 1.79e-05

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 46.14  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 138 ILIIGGGVVGVELAGEiAHAFPSKKLVLAHRgealldgfksKTRRVA------FQQLTALGVD-IEFNTGYQNISGSYID 210
Cdd:PRK12770  175 VVVVGAGLTAVDAALE-AVLLGAEKVYLAYR----------RTINEApagkyeIERLIARGVEfLELVTPVRIIGEGRVE 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 211 ------------QRSGKTAT-----------ADIVFEAVGTLPNSEFLQAQLPHVLNNKGFVKVNSqLEVSGEDNLYALG 267
Cdd:PRK12770  244 gvelakmrlgepDESGRPRPvpipgsefvleADTVVFAIGEIPTPPFAKECLGIELNRKGEIVVDE-KHMTSREGVFAAG 322

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1787610894 268 DVAdVGEAKLGyLAQQQGEYLARLISNKLKSK 299
Cdd:PRK12770  323 DVV-TGPSKIG-KAIKSGLRAAQSIHEWLDLK 352
PLN02507 PLN02507
glutathione reductase
 139-271 1.91e-05

glutathione reductase


Pssm-ID: 215281 [Multi-domain]  Cd Length: 499  Bit Score: 46.35  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 139 LIIGGGVVGVELAGeIAHAFPSkKLVLAHRGEALLDGFKSKTRRVAFQQLTALGVDIEFNTGYQNIS----GSYIDQRSG 214
Cdd:PLN02507  207 VVLGGGYIAVEFAS-IWRGMGA-TVDLFFRKELPLRGFDDEMRAVVARNLEGRGINLHPRTNLTQLTktegGIKVITDHG 284

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 215 KTATADIVFEAVGTLPNSEFLQAQLPHV-LNNKGFVKVN--SQLEVSgedNLYALGDVAD 271
Cdd:PLN02507  285 EEFVADVVLFATGRAPNTKRLNLEAVGVeLDKAGAVKVDeySRTNIP---SIWAIGDVTN 341
PTZ00058 PTZ00058
glutathione reductase; Provisional
 85-268 7.09e-05

glutathione reductase; Provisional


Pssm-ID: 185420 [Multi-domain]  Cd Length: 561  Bit Score: 44.61  E-value: 7.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894  85 LDNGSTIDFKMAIIASGTRypsmPIAKSSSAFNLTDRNNELLQhnqnIQNAENILIIGGGVVGVELAGeIAHAFPSKKLV 164
Cdd:PTZ00058  195 LDDGQVIEGKNILIAVGNK----PIFPDVKGKEFTISSDDFFK----IKEAKRIGIAGSGYIAVELIN-VVNRLGAESYI 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 165 LAhRGEALLDGFKSKTRRVAFQQLTALGVDIEFNTGYQNISG-------SYIDQrSGKTATADIVFEAVGTLPNSEFLQA 237
Cdd:PTZ00058  266 FA-RGNRLLRKFDETIINELENDMKKNNINIITHANVEEIEKvkeknltIYLSD-GRKYEHFDYVIYCVGRSPNTEDLNL 343

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1787610894 238 QLPHVLNNKGFVKVNSQLEVSGEdNLYALGD 268
Cdd:PTZ00058  344 KALNIKTPKGYIKVDDNQRTSVK-HIYAVGD 373
PRK08010 PRK08010
pyridine nucleotide-disulfide oxidoreductase; Provisional
 140-269 4.75e-04

pyridine nucleotide-disulfide oxidoreductase; Provisional


Pssm-ID: 181196 [Multi-domain]  Cd Length: 441  Bit Score: 41.92  E-value: 4.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 140 IIGGGVVGVELAGEIAHaFPSKKLVLahrgEALLDGFKSKTRRVAFQQLTAL---GVDIEFNTGYQNISGS----YIDQR 212
Cdd:PRK08010  163 ILGGGYIGVEFASMFAN-FGSKVTIL----EAASLFLPREDRDIADNIATILrdqGVDIILNAHVERISHHenqvQVHSE 237

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1787610894 213 SGKTATaDIVFEAVGTLPNSEFLQAQLPHV-LNNKGFVKVNSQLEVSGeDNLYALGDV 269
Cdd:PRK08010  238 HAQLAV-DALLIASGRQPATASLHPENAGIaVNERGAIVVDKYLHTTA-DNIWAMGDV 293
PRK07251 PRK07251
FAD-containing oxidoreductase;
140-269 6.22e-04

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 41.27  E-value: 6.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787610894 140 IIGGGVVGVELAGeiAHAFPSKKLVLAHRGEALLDGFKSKTRRVAFQQLTALGVDIEFN---TGYQNISGSYIDQRSGKT 216
Cdd:PRK07251  162 IIGGGNIGLEFAG--LYNKLGSKVTVLDAASTILPREEPSVAALAKQYMEEDGITFLLNahtTEVKNDGDQVLVVTEDET 239

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1787610894 217 ATADIVFEAVGTLPNSEFLQAQLPHV-LNNKGFVKVNSQLEVSGEdNLYALGDV 269
Cdd:PRK07251  240 YRFDALLYATGRKPNTEPLGLENTDIeLTERGAIKVDDYCQTSVP-GVFAVGDV 292
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 219-270 1.18e-03

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: 40.50  E-value: 1.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1787610894 219 ADIVFEAVGTLPNSEFLQAQLPHVLNNKGFVKVNSQLEVSGEDNLYALGDVA 270
Cdd:COG0493   360 ADLVILAIGQTPDPSGLEEELGLELDKRGTIVVDEETYQTSLPGVFAGGDAV 411
LacAB_rpiB pfam02502
Ribose/Galactose Isomerase; This family of proteins contains the sugar isomerase enzymes ...
 127-158 2.51e-03

Ribose/Galactose Isomerase; This family of proteins contains the sugar isomerase enzymes ribose 5-phosphate isomerase B (rpiB), galactose isomerase subunit A (LacA) and galactose isomerase subunit B (LacB).


Pssm-ID: 460573  Cd Length: 134  Bit Score: 37.75  E-value: 2.51e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1787610894 127 QHNqniqNAeNILIIGGGVVGVELAGEIAHAF 158
Cdd:pfam02502  95 EHN----DA-NVLCLGARVIGPELAKEIVDAF 121
PRK05571 PRK05571
ribose-5-phosphate isomerase B; Provisional
 127-158 9.76e-03

ribose-5-phosphate isomerase B; Provisional


Pssm-ID: 235509  Cd Length: 148  Bit Score: 36.29  E-value: 9.76e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1787610894 127 QHNqniqNAeNILIIGGGVVGVELAGEIAHAF 158
Cdd:PRK05571   98 EHN----NA-NVLALGARVIGPELAKDIVDAF 124
 
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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