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Conserved domains on  [gi|1340728814|ref|WP_103678119|]
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NAD(P)/FAD-dependent oxidoreductase [Superficieibacter electus]

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];
18-416 7.26e-152

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


:

Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 435.72  E-value: 7.26e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814  18 LELATQLGKKLGrgKKAKITLIDRNHSHLWKPLLHEVATGSLDEGVDALSYLAHARNHDFQFQLGSVIDLNRESKTLTLA 97
Cdd:COG1252    14 LEAARRLRKKLG--GDAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRAGVRFIQGEVTGIDPEARTVTLA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814  98 ElrdekgellvpERKLPYDKLIMALGSTSNDFNTPGVKDHCIFLDNPHQARRFHQEMLNLFLKFSANlgasGKVNIAIVG 177
Cdd:COG1252    92 D-----------GRTLSYDYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAFERAERR----RLLTIVVVG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 178 GGATGVELSAELHNAVKQLHSYgyKGLTNEALNVTLVEAGERILPALPPRISGAAHNELTKLGVRVLTKTMVTSADEGGL 257
Cdd:COG1252   157 GGPTGVELAGELAELLRKLLRY--PGIDPDKVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDADGV 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 258 HTKEGEYIQADLMVWAAGIKAPDFMKDLGgLETNRINQLVVEPTLQTTRDADIYAIGDCASCARPEGGFVPPRAQAAHQM 337
Cdd:COG1252   235 TLEDGEEIPADTVIWAAGVKAPPLLADLG-LPTDRRGRVLVDPTLQVPGHPNVFAIGDCAAVPDPDGKPVPKTAQAAVQQ 313

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1340728814 338 ATCALHNILAQRKGKPLKAYQYKDHGSLVSLSNFSTVGSLMGnltrgsMMIEGRIARFVYISLYRMHQIALHGYFKTGL 416
Cdd:COG1252   314 AKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVGG------LKLSGFLAWLLKRAIHLYFLPGFRGRLRVLL 386
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
18-416 7.26e-152

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 435.72  E-value: 7.26e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814  18 LELATQLGKKLGrgKKAKITLIDRNHSHLWKPLLHEVATGSLDEGVDALSYLAHARNHDFQFQLGSVIDLNRESKTLTLA 97
Cdd:COG1252    14 LEAARRLRKKLG--GDAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRAGVRFIQGEVTGIDPEARTVTLA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814  98 ElrdekgellvpERKLPYDKLIMALGSTSNDFNTPGVKDHCIFLDNPHQARRFHQEMLNLFLKFSANlgasGKVNIAIVG 177
Cdd:COG1252    92 D-----------GRTLSYDYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAFERAERR----RLLTIVVVG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 178 GGATGVELSAELHNAVKQLHSYgyKGLTNEALNVTLVEAGERILPALPPRISGAAHNELTKLGVRVLTKTMVTSADEGGL 257
Cdd:COG1252   157 GGPTGVELAGELAELLRKLLRY--PGIDPDKVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDADGV 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 258 HTKEGEYIQADLMVWAAGIKAPDFMKDLGgLETNRINQLVVEPTLQTTRDADIYAIGDCASCARPEGGFVPPRAQAAHQM 337
Cdd:COG1252   235 TLEDGEEIPADTVIWAAGVKAPPLLADLG-LPTDRRGRVLVDPTLQVPGHPNVFAIGDCAAVPDPDGKPVPKTAQAAVQQ 313

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1340728814 338 ATCALHNILAQRKGKPLKAYQYKDHGSLVSLSNFSTVGSLMGnltrgsMMIEGRIARFVYISLYRMHQIALHGYFKTGL 416
Cdd:COG1252   314 AKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVGG------LKLSGFLAWLLKRAIHLYFLPGFRGRLRVLL 386
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 30-338 1.71e-55

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: 185.98  E-value: 1.71e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814  30 RGKKAKITLI-DRNHSHLWKPLLHEVATGSLDEGVDAL---SYLAHARNHDFQFQLG-------SVIDLNRESKTLTLAE 98
Cdd:pfam07992  20 AQLGGKVTLIeDEGTCPYGGCVLSKALLGAAEAPEIASlwaDLYKRKEEVVKKLNNGievllgtEVVSIDPGAKKVVLEE 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814  99 LRDEKGEllvperKLPYDKLIMALGSTSNDFNTPGVKDHCIFL-DNPHQARRFHQEMLNLflkfsanlgasgkvNIAIVG 177
Cdd:pfam07992 100 LVDGDGE------TITYDRLVIATGARPRLPPIPGVELNVGFLvRTLDSAEALRLKLLPK--------------RVVVVG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 178 GGATGVELSAELHNAVKQlhsygykgltnealnVTLVEAGERILPALPPRISGAAHNELTKLGVRVLTKTMVTSADEGG- 256
Cdd:pfam07992 160 GGYIGVELAAALAKLGKE---------------VTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGd 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 257 ---LHTKEGEYIQADLMVWAAGIKAPDFMKDLGGLETNRINQLVVEPTLQTTRDaDIYAIGDCascarpeGGFVPPRAQA 333
Cdd:pfam07992 225 gveVILKDGTEIDADLVVVAIGRRPNTELLEAAGLELDERGGIVVDEYLRTSVP-GIYAAGDC-------RVGGPELAQN 296


                  ....*
gi 1340728814 334 AHQMA 338
Cdd:pfam07992 297 AVAQG 301
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 32-401 7.41e-45

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 161.09  E-value: 7.41e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814  32 KKAKITLID-RNHsHLWKPLLHEVATGSLdEGVDALSYLAHARNH-DFQFQLGSVIDLNRESKTLTLAELRDEKGELlVP 109
Cdd:PTZ00318   32 KKYNITVISpRNH-MLFTPLLPQTTTGTL-EFRSICEPVRPALAKlPNRYLRAVVYDVDFEEKRVKCGVVSKSNNAN-VN 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 110 ERKLPYDKLIMALGSTSNDFNTPGVKDHCIFLDNPHQARRFHQEMLNLFLKfsANLG------ASGKVNIAIVGGGATGV 183
Cdd:PTZ00318  109 TFSVPYDKLVVAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIVQCIER--ASLPttsveeRKRLLHFVVVGGGPTGV 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 184 ELSAELHNAVKQLHSYGYKGLTNEAlNVTLVEAGERILPALPPRISGAAHNELTKLGVRVLTKTMVTSADEGGLHTKEGE 263
Cdd:PTZ00318  187 EFAAELADFFRDDVRNLNPELVEEC-KVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEVLDKEVVLKDGE 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 264 YIQADLMVWAAGIKAPDFMKDLGGLETNRiNQLVVEPTLQTTRDADIYAIGDCASCarpEGGFVPPRAQAAHQMATCALH 343
Cdd:PTZ00318  266 VIPTGLVVWSTGVGPGPLTKQLKVDKTSR-GRISVDDHLRVKPIPNVFALGDCAAN---EERPLPTLAQVASQQGVYLAK 341

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1340728814 344 NILAQRKGKPL-KAYQYKDHGSLVSLSNFSTVGSLmgnltrGSMMIEGRIARFVYISLY 401
Cdd:PTZ00318  342 EFNNELKGKPMsKPFVYRSLGSLAYLGNYSAIVQL------GAFDLSGFKALLFWRSAY 394
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 97-360 1.32e-17

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: 84.62  E-value: 1.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814  97 AELRDeKGELLV----PERKLPYDKLIMALGSTSNDFNTPGVKDHCIFLDNphqarrfhQEMLNLflkfsanlgasGKV- 171
Cdd:TIGR01350 111 AKFLD-PGTVSVtgenGEETLEAKNIIIATGSRPRSLPGPFDFDGKVVITS--------TGALNL-----------EEVp 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 172 -NIAIVGGGATGVELSAelhnavkQLHSYGYKgltnealnVTLVEAGERILPALPPRISGAAHNELTKLGVRVLTKTMVT 250
Cdd:TIGR01350 171 eSLVIIGGGVIGIEFAS-------IFASLGSK--------VTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVT 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 251 --SADEGGLHTK----EGEYIQADLMVWAAGIKaPDFmKDLG----GLETNRINQLVVEPTLQTTrDADIYAIGDCAsca 320
Cdd:TIGR01350 236 avEKNDDQVTYEnkggETETLTGEKVLVAVGRK-PNT-EGLGleklGVELDERGRIVVDEYMRTN-VPGIYAIGDVI--- 309

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1340728814 321 rpeGGfvPPRAQAAHQMATCALHNILaqrkGKPLKAYQYK 360
Cdd:TIGR01350 310 ---GG--PMLAHVASHEGIVAAENIA----GKEPAHIDYD 340
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
18-416 7.26e-152

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 435.72  E-value: 7.26e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814  18 LELATQLGKKLGrgKKAKITLIDRNHSHLWKPLLHEVATGSLDEGVDALSYLAHARNHDFQFQLGSVIDLNRESKTLTLA 97
Cdd:COG1252    14 LEAARRLRKKLG--GDAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRAGVRFIQGEVTGIDPEARTVTLA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814  98 ElrdekgellvpERKLPYDKLIMALGSTSNDFNTPGVKDHCIFLDNPHQARRFHQEMLNLFLKFSANlgasGKVNIAIVG 177
Cdd:COG1252    92 D-----------GRTLSYDYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAFERAERR----RLLTIVVVG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 178 GGATGVELSAELHNAVKQLHSYgyKGLTNEALNVTLVEAGERILPALPPRISGAAHNELTKLGVRVLTKTMVTSADEGGL 257
Cdd:COG1252   157 GGPTGVELAGELAELLRKLLRY--PGIDPDKVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDADGV 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 258 HTKEGEYIQADLMVWAAGIKAPDFMKDLGgLETNRINQLVVEPTLQTTRDADIYAIGDCASCARPEGGFVPPRAQAAHQM 337
Cdd:COG1252   235 TLEDGEEIPADTVIWAAGVKAPPLLADLG-LPTDRRGRVLVDPTLQVPGHPNVFAIGDCAAVPDPDGKPVPKTAQAAVQQ 313

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1340728814 338 ATCALHNILAQRKGKPLKAYQYKDHGSLVSLSNFSTVGSLMGnltrgsMMIEGRIARFVYISLYRMHQIALHGYFKTGL 416
Cdd:COG1252   314 AKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVGG------LKLSGFLAWLLKRAIHLYFLPGFRGRLRVLL 386
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 30-338 1.71e-55

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: 185.98  E-value: 1.71e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814  30 RGKKAKITLI-DRNHSHLWKPLLHEVATGSLDEGVDAL---SYLAHARNHDFQFQLG-------SVIDLNRESKTLTLAE 98
Cdd:pfam07992  20 AQLGGKVTLIeDEGTCPYGGCVLSKALLGAAEAPEIASlwaDLYKRKEEVVKKLNNGievllgtEVVSIDPGAKKVVLEE 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814  99 LRDEKGEllvperKLPYDKLIMALGSTSNDFNTPGVKDHCIFL-DNPHQARRFHQEMLNLflkfsanlgasgkvNIAIVG 177
Cdd:pfam07992 100 LVDGDGE------TITYDRLVIATGARPRLPPIPGVELNVGFLvRTLDSAEALRLKLLPK--------------RVVVVG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 178 GGATGVELSAELHNAVKQlhsygykgltnealnVTLVEAGERILPALPPRISGAAHNELTKLGVRVLTKTMVTSADEGG- 256
Cdd:pfam07992 160 GGYIGVELAAALAKLGKE---------------VTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGd 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 257 ---LHTKEGEYIQADLMVWAAGIKAPDFMKDLGGLETNRINQLVVEPTLQTTRDaDIYAIGDCascarpeGGFVPPRAQA 333
Cdd:pfam07992 225 gveVILKDGTEIDADLVVVAIGRRPNTELLEAAGLELDERGGIVVDEYLRTSVP-GIYAAGDC-------RVGGPELAQN 296


                  ....*
gi 1340728814 334 AHQMA 338
Cdd:pfam07992 297 AVAQG 301
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 32-401 7.41e-45

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 161.09  E-value: 7.41e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814  32 KKAKITLID-RNHsHLWKPLLHEVATGSLdEGVDALSYLAHARNH-DFQFQLGSVIDLNRESKTLTLAELRDEKGELlVP 109
Cdd:PTZ00318   32 KKYNITVISpRNH-MLFTPLLPQTTTGTL-EFRSICEPVRPALAKlPNRYLRAVVYDVDFEEKRVKCGVVSKSNNAN-VN 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 110 ERKLPYDKLIMALGSTSNDFNTPGVKDHCIFLDNPHQARRFHQEMLNLFLKfsANLG------ASGKVNIAIVGGGATGV 183
Cdd:PTZ00318  109 TFSVPYDKLVVAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIVQCIER--ASLPttsveeRKRLLHFVVVGGGPTGV 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 184 ELSAELHNAVKQLHSYGYKGLTNEAlNVTLVEAGERILPALPPRISGAAHNELTKLGVRVLTKTMVTSADEGGLHTKEGE 263
Cdd:PTZ00318  187 EFAAELADFFRDDVRNLNPELVEEC-KVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEVLDKEVVLKDGE 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 264 YIQADLMVWAAGIKAPDFMKDLGGLETNRiNQLVVEPTLQTTRDADIYAIGDCASCarpEGGFVPPRAQAAHQMATCALH 343
Cdd:PTZ00318  266 VIPTGLVVWSTGVGPGPLTKQLKVDKTSR-GRISVDDHLRVKPIPNVFALGDCAAN---EERPLPTLAQVASQQGVYLAK 341

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1340728814 344 NILAQRKGKPL-KAYQYKDHGSLVSLSNFSTVGSLmgnltrGSMMIEGRIARFVYISLY 401
Cdd:PTZ00318  342 EFNNELKGKPMsKPFVYRSLGSLAYLGNYSAIVQL------GAFDLSGFKALLFWRSAY 394
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 30-355 3.06e-37

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: 138.02  E-value: 3.06e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814  30 RGKKAKITLIDRNHSH------LWKPLLHevatgsldeGVDALSYLAHARNHDF-----QFQLGS-VIDLNRESKTLTLA 97
Cdd:COG0446     2 LGPDAEITVIEKGPHHsyqpcgLPYYVGG---------GIKDPEDLLVRTPESFerkgiDVRTGTeVTAIDPEAKTVTLR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814  98 ElrdekgellvpERKLPYDKLIMALGSTSNDFNTPGVKDHCIF-LDNPHQARRFHQEMLNlflkfsanlgASGKvNIAIV 176
Cdd:COG0446    73 D-----------GETLSYDKLVLATGARPRPPPIPGLDLPGVFtLRTLDDADALREALKE----------FKGK-RAVVI 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 177 GGGATGVELsAElhnavkQLHSYGykgltneaLNVTLVEAGERILPALPPRISGAAHNELTKLGVRVLTKTMVTSADEGG 256
Cdd:COG0446   131 GGGPIGLEL-AE------ALRKRG--------LKVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAIDGDD 195

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 257 ---LHTKEGEYIQADLMVWAAGIkAPDFmkDLG---GLETNRINQLVVEPTLQtTRDADIYAIGDCASCARPEGG--FVP 328
Cdd:COG0446   196 kvaVTLTDGEEIPADLVVVAPGV-RPNT--ELAkdaGLALGERGWIKVDETLQ-TSDPDVYAAGDCAEVPHPVTGktVYI 271

                         330       340
                  ....*....|....*....|....*..
gi 1340728814 329 PRAQAAHQMATCALHNILaqrkGKPLK 355
Cdd:COG0446   272 PLASAANKQGRVAAENIL----GGPAP 294
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
30-350 2.12e-33

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 129.49  E-value: 2.12e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814  30 RGKKAKITLIDR-NHSHLWKPLLHEVATGSLDEGVDALSYLAHARNHDFQFQLGS-VIDLNRESKTLTLAElrdekGEll 107
Cdd:COG1251    23 LDPDGEITVIGAePHPPYNRPPLSKVLAGETDEEDLLLRPADFYEENGIDLRLGTrVTAIDRAARTVTLAD-----GE-- 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 108 vperKLPYDKLIMALGSTSNDFNTPGV-KDHCIFLDNPHQARRFHqemlnlflkfsANLGASGKVniAIVGGGATGVELS 186
Cdd:COG1251    96 ----TLPYDKLVLATGSRPRVPPIPGAdLPGVFTLRTLDDADALR-----------AALAPGKRV--VVIGGGLIGLEAA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 187 AELHNAvkqlhsyGYKgltnealnVTLVEAGERILP-ALPPRISGAAHNELTKLGVRVLTKTMVTS--ADEG--GLHTKE 261
Cdd:COG1251   159 AALRKR-------GLE--------VTVVERAPRLLPrQLDEEAGALLQRLLEALGVEVRLGTGVTEieGDDRvtGVRLAD 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 262 GEYIQADLMVWAAGIKaP--DFMKDlGGLETNR-InqlVVEPTLQTTrDADIYAIGDCASCA-RPEGGFVPPRAQAAHQM 337
Cdd:COG1251   224 GEELPADLVVVAIGVR-PntELARA-AGLAVDRgI---VVDDYLRTS-DPDIYAAGDCAEHPgPVYGRRVLELVAPAYEQ 297

                         330
                  ....*....|...
gi 1340728814 338 ATCALHNILAQRK 350
Cdd:COG1251   298 ARVAAANLAGGPA 310
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 173-350 1.36e-20

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: 93.61  E-value: 1.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 173 IAIVGGGATGVEL-SAelhnavkqLHSYGYKgltnealnVTLVEAGERILPALPPRISGAAHNELTKLGVRVLTKTMVTS 251
Cdd:COG1249   171 LVVIGGGYIGLEFaQI--------FARLGSE--------VTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTS 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 252 ADEGG----LHTKEG---EYIQADLMVWAAGIKApdFMKDLG----GLETNRINQLVVEPTLQTTrDADIYAIGDCAsca 320
Cdd:COG1249   235 VEKTGdgvtVTLEDGggeEAVEADKVLVATGRRP--NTDGLGleaaGVELDERGGIKVDEYLRTS-VPGIYAIGDVT--- 308

                         170       180       190
                  ....*....|....*....|....*....|
gi 1340728814 321 rpeGGfvPPRAQAAHQMATCALHNILAQRK 350
Cdd:COG1249   309 ---GG--PQLAHVASAEGRVAAENILGKKP 333
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
114-317 3.71e-19

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 88.44  E-value: 3.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 114 PYDKLIMALGSTSndFNTPGVKDHCIFLDNPHQARRFHQEMLnlflkfsanlgASGKvNIAIVGGGATGVELSAELHNAV 193
Cdd:PRK04965   99 QYDKLVLATGASA--FVPPIPGRELMLTLNSQQEYRAAETQL-----------RDAQ-RVLVVGGGLIGTELAMDLCRAG 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 194 KQlhsygykgltnealnVTLVEAGERILPAL-PPRISGAAHNELTKLGVRVLTKTMVTSAD--EGGLH--TKEGEYIQAD 268
Cdd:PRK04965  165 KA---------------VTLVDNAASLLASLmPPEVSSRLQHRLTEMGVHLLLKSQLQGLEktDSGIRatLDSGRSIEVD 229

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1340728814 269 LMVWAAGIKAPDFMKDLGGLETNRinQLVVEPTLQTTrDADIYAIGDCA 317
Cdd:PRK04965  230 AVIAAAGLRPNTALARRAGLAVNR--GIVVDSYLQTS-APDIYALGDCA 275
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 97-360 1.32e-17

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: 84.62  E-value: 1.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814  97 AELRDeKGELLV----PERKLPYDKLIMALGSTSNDFNTPGVKDHCIFLDNphqarrfhQEMLNLflkfsanlgasGKV- 171
Cdd:TIGR01350 111 AKFLD-PGTVSVtgenGEETLEAKNIIIATGSRPRSLPGPFDFDGKVVITS--------TGALNL-----------EEVp 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 172 -NIAIVGGGATGVELSAelhnavkQLHSYGYKgltnealnVTLVEAGERILPALPPRISGAAHNELTKLGVRVLTKTMVT 250
Cdd:TIGR01350 171 eSLVIIGGGVIGIEFAS-------IFASLGSK--------VTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVT 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 251 --SADEGGLHTK----EGEYIQADLMVWAAGIKaPDFmKDLG----GLETNRINQLVVEPTLQTTrDADIYAIGDCAsca 320
Cdd:TIGR01350 236 avEKNDDQVTYEnkggETETLTGEKVLVAVGRK-PNT-EGLGleklGVELDERGRIVVDEYMRTN-VPGIYAIGDVI--- 309

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1340728814 321 rpeGGfvPPRAQAAHQMATCALHNILaqrkGKPLKAYQYK 360
Cdd:TIGR01350 310 ---GG--PMLAHVASHEGIVAAENIA----GKEPAHIDYD 340
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
 50-361 3.18e-16

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


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 81.03  E-value: 3.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814  50 LLHEVATGSLDEGVDALSYLAHARNHDFQFQLG-SVIDLNRESKTLTLAElrdekgellvpERKLPYDKLIMALGSTSND 128
Cdd:TIGR02374  42 LLSSVLQGEADLDDITLNSKDWYEKHGITLYTGeTVIQIDTDQKQVITDA-----------GRTLSYDKLILATGSYPFI 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 129 FNTPGV-KDHCifldnpHQARRFH--QEMLNlflkfsanlGASGKVNIAIVGGGATGVELSaelhnavkqlhsygyKGLT 205
Cdd:TIGR02374 111 LPIPGAdKKGV------YVFRTIEdlDAIMA---------MAQRFKKAAVIGGGLLGLEAA---------------VGLQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 206 NEALNVTLVEAGERILPALPPRISGAA-HNELTKLGVRVLT-KTMVTSADEG---GLHTKEGEYIQADLMVWAAGIKAPD 280
Cdd:TIGR02374 161 NLGMDVSVIHHAPGLMAKQLDQTAGRLlQRELEQKGLTFLLeKDTVEIVGATkadRIRFKDGSSLEADLIVMAAGIRPND 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 281 FMKDLGGLETNRinQLVVEPTLQTTrDADIYAIGDCASCARPEGGFVPPraqaAHQMATCALHNILaqrkGKPLKAYQYK 360
Cdd:TIGR02374 241 ELAVSAGIKVNR--GIIVNDSMQTS-DPDIYAVGECAEHNGRVYGLVAP----LYEQAKVLADHIC----GVECEEYEGS 309


                  .
gi 1340728814 361 D 361
Cdd:TIGR02374 310 D 310
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 84-318 3.01e-14

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 74.31  E-value: 3.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814  84 VIDLNRESKTLTLAELRDEKgellvpERKLPYDKLIMALGSTSNDFNTPGVKdhcifLDNPHQARRFH--QEMLNLFLKf 161
Cdd:PRK09564   79 VVKVDAKNKTITVKNLKTGS------IFNDTYDKLMIATGARPIIPPIKNIN-----LENVYTLKSMEdgLALKELLKD- 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 162 sanlgaSGKVNIAIVGGGATGVELSAELHNAVKqlhsygykgltnealNVTLVEAGERILP-ALPPRISGAAHNELTKLG 240
Cdd:PRK09564  147 ------EEIKNIVIIGAGFIGLEAVEAAKHLGK---------------NVRIIQLEDRILPdSFDKEITDVMEEELRENG 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 241 VRVLTKTMVTSAD-EG---GLHTKEGEYiQADLMVWAAGIK-APDFMKDlGGLETNRINQLVVEPTLQTTrDADIYAIGD 315
Cdd:PRK09564  206 VELHLNEFVKSLIgEDkveGVVTDKGEY-EADVVIVATGVKpNTEFLED-TGLKTLKNGAIIVDEYGETS-IENIYAAGD 282


                  ...
gi 1340728814 316 CAS 318
Cdd:PRK09564  283 CAT 285
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 173-315 8.41e-13

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 69.79  E-value: 8.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 173 IAIVGGGATGVEL-SAelhnavkqlhsygYKGLTNEalnVTLVEAGERILPALPPRISGAAHNELTKLGVRVLTKTMVTS 251
Cdd:PRK06416  175 LVVIGGGYIGVEFaSA-------------YASLGAE---VTIVEALPRILPGEDKEISKLAERALKKRGIKIKTGAKAKK 238

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1340728814 252 ADEGG----LH---TKEGEYIQADLMVWAAGIkAPDfMKDLG----GLETNRiNQLVVEPTLQTTrDADIYAIGD 315
Cdd:PRK06416  239 VEQTDdgvtVTledGGKEETLEADYVLVAVGR-RPN-TENLGleelGVKTDR-GFIEVDEQLRTN-VPNIYAIGD 309
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 173-352 2.13e-12

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 68.67  E-value: 2.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 173 IAIVGGGATGVEL-SAelhnavkqLHSYGYKgltnealnVTLVEAGERILPALPPRISGAAHNELTKlGVRVLTKTMVTS 251
Cdd:PRK06292  172 LAVIGGGVIGLELgQA--------LSRLGVK--------VTVFERGDRILPLEDPEVSKQAQKILSK-EFKIKLGAKVTS 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 252 ADEGG-----LHTKEGE--YIQADLMVWAAGIKApdFMKDLG----GLETNRINQLVVEPTLQTTrDADIYAIGDCAsca 320
Cdd:PRK06292  235 VEKSGdekveELEKGGKteTIEADYVLVATGRRP--NTDGLGlentGIELDERGRPVVDEHTQTS-VPGIYAAGDVN--- 308

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1340728814 321 rpegGFVPPRAQAAHQmATCALHNILAQRKGK 352
Cdd:PRK06292  309 ----GKPPLLHEAADE-GRIAAENAAGDVAGG 335
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 172-256 4.07e-11

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: 58.75  E-value: 4.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 172 NIAIVGGGATGVELSAELHNavkqlhsYGYKgltnealnVTLVEAGERILPALPPRISGAAHNELTKLGVRVLTKTMVTS 251
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALAR-------LGSK--------VTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEA 65


                  ....*
gi 1340728814 252 ADEGG 256
Cdd:pfam00070  66 IEGNG 70
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
 99-380 2.68e-10

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 61.86  E-value: 2.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814  99 LRDEKGELLVPERKLPYDKLIMALGSTSNDFNT-PGVKDHCIFLDNPHQARRFHQEMlnlflkfsanlgASGKvNIAIVG 177
Cdd:PRK09754   85 GRDTRELVLTNGESWHWDQLFIATGAAARPLPLlDALGERCFTLRHAGDAARLREVL------------QPER-SVVIVG 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 178 GGATGVELSAELhnavkqlhsygykglTNEALNVTLVEAGERIL-PALPPRISGAAHNELTKLGVRVLTKTMVTSADEGG 256
Cdd:PRK09754  152 AGTIGLELAASA---------------TQRRCKVTVIELAATVMgRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGE 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 257 ---LHTKEGEYIQADLMVWAAGIKAPDFMKDLGGLETNriNQLVVEPTLQTTrDADIYAIGDCASCARPEGGFVPPRA-Q 332
Cdd:PRK09754  217 kveLTLQSGETLQADVVIYGIGISANDQLAREANLDTA--NGIVIDEACRTC-DPAIFAGGDVAITRLDNGALHRCESwE 293

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1340728814 333 AAHQMATCALHNILAQRKGKPLKAYQYKDHGSLvslsNFSTVGSLMGN 380
Cdd:PRK09754  294 NANNQAQIAAAAMLGLPLPLLPPPWFWSDQYSD----NLQFIGDMRGD 337
PRK14989 PRK14989
nitrite reductase subunit NirD; Provisional
 84-348 5.99e-10

nitrite reductase subunit NirD; Provisional


Pssm-ID: 184951 [Multi-domain]  Cd Length: 847  Bit Score: 61.29  E-value: 5.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814  84 VIDLNRESKTLtlaelRDEKGellvpeRKLPYDKLIMALGSTSNDFNTPGVKDHCIFLdnphqARRFhqEMLNLfLKFSA 163
Cdd:PRK14989   82 AITINRQEKVI-----HSSAG------RTVFYDKLIMATGSYPWIPPIKGSETQDCFV-----YRTI--EDLNA-IEACA 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 164 NLGASGkvniAIVGGGATGVELSAelhnAVKQLhsygykGLTNEALNVTLVEAGERilpaLPPRISGAAHNELTKLGVRV 243
Cdd:PRK14989  143 RRSKRG----AVVGGGLLGLEAAG----ALKNL------GVETHVIEFAPMLMAEQ----LDQMGGEQLRRKIESMGVRV 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 244 LT-KTMVTSADEGG-----LHTKEGEYIQADLMVWAAGIKAPDFMKDLGGLETNRINQLVVEPTLQTTrDADIYAIGDCA 317
Cdd:PRK14989  205 HTsKNTLEIVQEGVearktMRFADGSELEVDFIVFSTGIRPQDKLATQCGLAVAPRGGIVINDSCQTS-DPDIYAIGECA 283

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1340728814 318 SCARPEGGFVPPraqaAHQMATCALHNILAQ 348
Cdd:PRK14989  284 SWNNRVFGLVAP----GYKMAQVAVDHLLGS 310
MerA TIGR02053
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ...
 173-316 3.96e-09

mercury(II) reductase; This model represents the mercuric reductase found in the mer operon for the detoxification of mercury compounds. MerA is a FAD-containing flavoprotein which reduces Hg(II) to Hg(0) utilizing NADPH. [Cellular processes, Detoxification]


Pssm-ID: 273944 [Multi-domain]  Cd Length: 463  Bit Score: 58.20  E-value: 3.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 173 IAIVGGGATGVELSAELHNAvkqlhsygykgltneALNVTLVEAGERILPALPPRISGAAHNELTKLGVRVLTKTMVT-- 250
Cdd:TIGR02053 169 LAVIGGGAIGVELAQAFARL---------------GSEVTILQRSDRLLPREEPEISAAVEEALAEEGIEVVTSAQVKav 233

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1340728814 251 SADEGG----LHTKEGEY-IQADLMVWAAGiKAPDfMKDLG----GLETNRINQLVVEPTLQTTrDADIYAIGDC 316
Cdd:TIGR02053 234 SVRGGGkiitVEKPGGQGeVEADELLVATG-RRPN-TDGLGlekaGVKLDERGGILVDETLRTS-NPGIYAAGDV 305
PRK06116 PRK06116
glutathione reductase; Validated
 173-316 3.67e-08

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 55.16  E-value: 3.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 173 IAIVGGGATGVELSAELHnavkqlhsygykGLTNEalnVTLVEAGERILPALPPRISGAAHNELTKLGVRVLTKTMVTS- 251
Cdd:PRK06116  170 VAVVGAGYIAVEFAGVLN------------GLGSE---THLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAv 234

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1340728814 252 --ADEGGL--HTKEGEYIQADLMVWAAGiKAPDfMKDLG----GLETNRINQLVVEpTLQTTRDADIYAIGDC 316
Cdd:PRK06116  235 ekNADGSLtlTLEDGETLTVDCLIWAIG-REPN-TDGLGlenaGVKLNEKGYIIVD-EYQNTNVPGIYAVGDV 304
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
173-353 4.46e-08

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


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 55.16  E-value: 4.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 173 IAIVGGGATGVElsaelhnavkqlhsY-------GYKgltnealnVTLVEAGERILPALPPRISGAAHNELTKLGVRVLT 245
Cdd:PRK05249  178 LIIYGAGVIGCE--------------YasifaalGVK--------VTLINTRDRLLSFLDDEISDALSYHLRDSGVTIRH 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 246 KTMVTS--ADEGG--LHTKEGEYIQADLMVWAAGIKAPdfMKDLG----GLETNRINQLVVEPTLQTTRDaDIYAIGDCA 317
Cdd:PRK05249  236 NEEVEKveGGDDGviVHLKSGKKIKADCLLYANGRTGN--TDGLNlenaGLEADSRGQLKVNENYQTAVP-HIYAVGDVI 312

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1340728814 318 scarpegGFvPPRAQAAHQMATCALHNILAQRKGKP 353
Cdd:PRK05249  313 -------GF-PSLASASMDQGRIAAQHAVGEATAHL 340
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 79-318 5.92e-08

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: 54.76  E-value: 5.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814  79 FQLGSVIDlnresKTLTLAELRDEkgellvperklpYDKLIMALGST-SNDFNTPGVKdhcifLDNPHQArrfhqemlNL 157
Cdd:COG0493   188 FRTNVEVG-----KDITLDELLEE------------FDAVFLATGAGkPRDLGIPGED-----LKGVHSA--------MD 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 158 FLKfSANLG-------ASGKvNIAIVGGGATGVelsaelhNAVKQLHSYGykgltneALNVTLV---------------- 214
Cdd:COG0493   238 FLT-AVNLGeapdtilAVGK-RVVVIGGGNTAM-------DCARTALRLG-------AESVTIVyrrtreempaskeeve 301

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 215 ----EAGERILPALPPRISGAAHNELTklGVRVlTKTMVTSADEGG---LHTKEGEY--IQADLMVWAAGIKA-PDFMKD 284
Cdd:COG0493   302 ealeEGVEFLFLVAPVEIIGDENGRVT--GLEC-VRMELGEPDESGrrrPVPIEGSEftLPADLVILAIGQTPdPSGLEE 378

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1340728814 285 LGGLETNRINQLVVEP-TLQTTRDaDIYAIGDCAS 318
Cdd:COG0493   379 ELGLELDKRGTIVVDEeTYQTSLP-GVFAGGDAVR 412
PRK06370 PRK06370
FAD-containing oxidoreductase;
173-322 2.61e-07

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 52.51  E-value: 2.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 173 IAIVGGGATGVELSaelhnavkqlhsYGYKGLTNEalnVTLVEAGERILPALPPRISGAAHNELTKLGVRVLTKTMVTSA 252
Cdd:PRK06370  174 LVIIGGGYIGLEFA------------QMFRRFGSE---VTVIERGPRLLPREDEDVAAAVREILEREGIDVRLNAECIRV 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 253 ----DEGGLHTK---EGEYIQADLMVWAAGiKAPDfMKDLG----GLETNRINQLVVEPTLQTTRDaDIYAIGDCasCAR 321
Cdd:PRK06370  239 erdgDGIAVGLDcngGAPEITGSHILVAVG-RVPN-TDDLGleaaGVETDARGYIKVDDQLRTTNP-GIYAAGDC--NGR 313


                  .
gi 1340728814 322 P 322
Cdd:PRK06370  314 G 314
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
 84-357 2.51e-04

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 43.23  E-value: 2.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814  84 VIDLNRESKTLTLAELR-DEKGELlvperklPYDKLIMALGSTSNDFNTPgvKDHCIFLDNPHQARRFHQEMLNLFLKfs 162
Cdd:PRK13512   81 VIAINDERQTVTVLNRKtNEQFEE-------SYDKLILSPGASANSLGFE--SDITFTLRNLEDTDAIDQFIKANQVD-- 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 163 anlgasgkvNIAIVGGGATGVELSAELHnavkqlhsygykgltNEALNVTLVEAGERILPALPPRISGAAHNELTKLGVR 242
Cdd:PRK13512  150 ---------KALVVGAGYISLEVLENLY---------------ERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIP 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 243 VLTKTMVTSADEGGLHTKEGEYIQADLMVWAAGIKA-PDFMKDlGGLETNRINQLVVEPTLQTTrDADIYAIGDCASCAR 321
Cdd:PRK13512  206 YRLNEEIDAINGNEVTFKSGKVEHYDMIIEGVGTHPnSKFIES-SNIKLDDKGFIPVNDKFETN-VPNIYAIGDIITSHY 283

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1340728814 322 PEGGfVP---PRAQAAHQMATCALHNIlAQRKGKPLKAY 357
Cdd:PRK13512  284 RHVD-LPasvPLAWGAHRAASIVAEQI-AGNDTIEFKGF 320
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
173-318 3.57e-04

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 42.41  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 173 IAIVGGGATGVELSAElhnavkqlhsygykgLTNEALNVTLVEAGERIlpalpprisGAAHNELTKL----GVRVLTKTM 248
Cdd:COG0492   144 VVVVGGGDSALEEALY---------------LTKFASKVTLIHRRDEL---------RASKILVERLranpKIEVLWNTE 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 249 VTSAD-EGGL--------HTKEGEYIQADLMVWAAGIKAP-DFMKDLgGLETNRINQLVVEPTLQTTRDAdIYAIGDCAS 318
Cdd:COG0492   200 VTEIEgDGRVegvtlknvKTGEEKELEVDGVFVAIGLKPNtELLKGL-GLELDEDGYIVVDEDMETSVPG-VFAAGDVRD 277
PRK13748 PRK13748
putative mercuric reductase; Provisional
 222-316 1.38e-03

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 40.91  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 222 PALPPRISGAAHNEltklGVRVLTKTMVTS-ADEGG---LHTKEGEyIQADLMVWAAGiKAPDFMK---DLGGLETNRIN 294
Cdd:PRK13748  310 PAIGEAVTAAFRAE----GIEVLEHTQASQvAHVDGefvLTTGHGE-LRADKLLVATG-RAPNTRSlalDAAGVTVNAQG 383

                          90       100
                  ....*....|....*....|..
gi 1340728814 295 QLVVEPTLQTTRdADIYAIGDC 316
Cdd:PRK13748  384 AIVIDQGMRTSV-PHIYAAGDC 404
PRK08010 PRK08010
pyridine nucleotide-disulfide oxidoreductase; Provisional
 173-315 1.73e-03

pyridine nucleotide-disulfide oxidoreductase; Provisional


Pssm-ID: 181196 [Multi-domain]  Cd Length: 441  Bit Score: 40.38  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 173 IAIVGGGATGVELSAELHNavkqlhsYGYKgltnealnVTLVEAGERILPALPPRISGAAHNELTKLGVRVLTKTMV--T 250
Cdd:PRK08010  161 LGILGGGYIGVEFASMFAN-------FGSK--------VTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVerI 225

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1340728814 251 SADEGG--LHTKEGEYIqADLMVWAAGIK--APDFMKDLGGLETNRINQLVVEPTLQTTRDaDIYAIGD 315
Cdd:PRK08010  226 SHHENQvqVHSEHAQLA-VDALLIASGRQpaTASLHPENAGIAVNERGAIVVDKYLHTTAD-NIWAMGD 292
PRK12779 PRK12779
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ...
 259-338 3.56e-03

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


Pssm-ID: 183740 [Multi-domain]  Cd Length: 944  Bit Score: 39.82  E-value: 3.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 259 TKEGEYIQADLMVWAAGIKAPDFMKDLG-GLETNRINQLVVEPTLQTTRDADIYAIGDCAscarpEGGFVPPRAQAAHQM 337
Cdd:PRK12779  543 TGEIERVPVDLVIMALGNTANPIMKDAEpGLKTNKWGTIEVEKGSQRTSIKGVYSGGDAA-----RGGSTAIRAAGDGQA 617


                  .
gi 1340728814 338 A 338
Cdd:PRK12779  618 A 618
PTZ00058 PTZ00058
glutathione reductase; Provisional
 173-316 3.62e-03

glutathione reductase; Provisional


Pssm-ID: 185420 [Multi-domain]  Cd Length: 561  Bit Score: 39.60  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 173 IAIVGGGATGVELSaelhNAVKQLhsygykgltneALNVTLVEAGERILPALPPRISGAAHNELTKLGVRVLTKTM---V 249
Cdd:PTZ00058  240 IGIAGSGYIAVELI----NVVNRL-----------GAESYIFARGNRLLRKFDETIINELENDMKKNNINIITHANveeI 304

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1340728814 250 TSADEGGLHT---KEGEYIQADLMVWAAGiKAPDfMKDLG--GLETNRINQLVVEPTLQTTRDADIYAIGDC 316
Cdd:PTZ00058  305 EKVKEKNLTIylsDGRKYEHFDYVIYCVG-RSPN-TEDLNlkALNIKTPKGYIKVDDNQRTSVKHIYAVGDC 374
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
173-278 4.99e-03

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 38.56  E-value: 4.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 173 IAIVGGGATGveLSAelhnAVkqlhsygYKGLTNeaLNVTLVEAGE---------RI--LPALPPRISGA-----AHNEL 236
Cdd:COG0492     3 VVIIGAGPAG--LTA----AI-------YAARAG--LKTLVIEGGEpggqlattkEIenYPGFPEGISGPelaerLREQA 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1340728814 237 TKLGVRVLTkTMVTSADEGG----LHTKEGEYIQADLMVWAAGIKA 278
Cdd:COG0492    68 ERFGAEILL-EEVTSVDKDDgpfrVTTDDGTEYEAKAVIIATGAGP 112
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
 173-315 5.92e-03

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 38.82  E-value: 5.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 173 IAIVGGGATGVE--LSAELHNAVKQLHSYgyKGLTNEA------LNvTLVEAG----ERILPAlppRISGaahnELTKLG 240
Cdd:PRK12770  175 VVVVGAGLTAVDaaLEAVLLGAEKVYLAY--RRTINEApagkyeIE-RLIARGveflELVTPV---RIIG----EGRVEG 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 241 VRvLTKTMVTSADEGGLH-----TKEGEYIQADLMVWAAG-IKAPDFMKDLGGLETNRINQLVVEPTLQTTRdADIYAIG 314
Cdd:PRK12770  245 VE-LAKMRLGEPDESGRPrpvpiPGSEFVLEADTVVFAIGeIPTPPFAKECLGIELNRKGEIVVDEKHMTSR-EGVFAAG 322


                  .
gi 1340728814 315 D 315
Cdd:PRK12770  323 D 323
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
 174-318 7.84e-03

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 38.37  E-value: 7.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 174 AIVGGGATGVELSAElhnavkqlhsygYKGLTNEalnVTLVEAGERILPALPPRISGAAHNELTKLGVRVLTKTMVTSAD 253
Cdd:PRK06327  187 AVIGAGVIGLELGSV------------WRRLGAE---VTILEALPAFLAAADEQVAKEAAKAFTKQGLDIHLGVKIGEIK 251

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1340728814 254 EGG------LHTKEGEY--IQADLMVWAAGIKAPdfMKDLG----GLETNRINQLVVEPTLQTTRDaDIYAIGDCAS 318
Cdd:PRK06327  252 TGGkgvsvaYTDADGEAqtLEVDKLIVSIGRVPN--TDGLGleavGLKLDERGFIPVDDHCRTNVP-NVYAIGDVVR 325
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
187-311 9.19e-03

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 37.96  E-value: 9.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340728814 187 AELHNAVKQLHSYGYKgltnealnVTLVEAGE--RILPAL-PPRISGAAHNE-----------------LTKLGVRVLTK 246
Cdd:COG0665   100 AALRAEAEALRALGLP--------VELLDAAElrEREPGLgSPDYAGGLYDPddghvdpaklvralaraARAAGVRIREG 171

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1340728814 247 TMVTSADEGG-----LHTKEGEyIQADLMVWAAGIKAPDFMKDLGG---LETNRINQLVVEP-----TLQTTRDADIY 311
Cdd:COG0665   172 TPVTGLEREGgrvtgVRTERGT-VRADAVVLAAGAWSARLLPMLGLrlpLRPVRGYVLVTEPlpdlpLRPVLDDTGVY 248
 
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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