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Conserved domains on  [gi|915492495|ref|WP_050822663|]
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MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Bacillus]

Protein Classification

NAD(P)/FAD-dependent oxidoreductase( domain architecture ID 11441266)

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; belongs to the pyridine nucleotide-disulfide oxidoreductase superfamily

CATH:  3.30.390.30
EC:  1.-.-.-
Gene Ontology:  GO:0016491|GO:0000166
PubMed:  38537870
SCOP:  4000121

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
3-394 1.53e-129

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


:

Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 378.33  E-value: 1.53e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495   3 KNFVIIGSGVAAVNAAKTIREYDKGSNIFIFGEEPSLPYKRIKLSKDLYSDLHSEKVLIKKKKWYQDNHISVFINTKVVK 82
Cdd:COG1251    2 MRIVIIGAGMAGVRAAEELRKLDPDGEITVIGAEPHPPYNRPPLSKVLAGETDEEDLLLRPADFYEENGIDLRLGTRVTA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  83 INTDEQFIVTSNEAVFSYHKLLICTGANNRRLEINGINKKNIFTIRDMKEADELKGHLEDKESVVTIGGGVQGLETAWSI 162
Cdd:COG1251   82 IDRAARTVTLADGETLPYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRAALAPGKRVVVIGGGLIGLEAAAAL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 163 LKAGKKVSIVEVAPLLMRRQLDTKSSLLLKRRIEKEGVKVYLNTSIDSILGKESVTGIKMNDNSQINCDSIVYSIGVTPN 242
Cdd:COG1251  162 RKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRLADGEELPADLVVVAIGVRPN 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 243 TKLVHDTAIKLNRGIVVDEEMRTNIDSVYAAGDVAEVNNEIEG-----LWGTALEQGRVAGSNMVSKTAIYKKEIPTTIF 317
Cdd:COG1251  242 TELARAAGLAVDRGIVVDDYLRTSDPDIYAAGDCAEHPGPVYGrrvleLVAPAYEQARVAAANLAGGPAAYEGSVPSTKL 321

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 915492495 318 NAFNVSLFSIGVVNEEqcDTTIVEED-GKEKYTRLFIKDNKIVGVISLEGVAASISYKSAIEKHVSLEGIDLLNTNIS 394
Cdd:COG1251  322 KVFGVDVASAGDAEGD--EEVVVRGDpARGVYKKLVLRDGRLVGAVLVGDTSDAGALRQLIKNGRPLPPRALLDAALP 397
 
Name Accession Description Interval E-value
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
3-394 1.53e-129

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 378.33  E-value: 1.53e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495   3 KNFVIIGSGVAAVNAAKTIREYDKGSNIFIFGEEPSLPYKRIKLSKDLYSDLHSEKVLIKKKKWYQDNHISVFINTKVVK 82
Cdd:COG1251    2 MRIVIIGAGMAGVRAAEELRKLDPDGEITVIGAEPHPPYNRPPLSKVLAGETDEEDLLLRPADFYEENGIDLRLGTRVTA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  83 INTDEQFIVTSNEAVFSYHKLLICTGANNRRLEINGINKKNIFTIRDMKEADELKGHLEDKESVVTIGGGVQGLETAWSI 162
Cdd:COG1251   82 IDRAARTVTLADGETLPYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRAALAPGKRVVVIGGGLIGLEAAAAL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 163 LKAGKKVSIVEVAPLLMRRQLDTKSSLLLKRRIEKEGVKVYLNTSIDSILGKESVTGIKMNDNSQINCDSIVYSIGVTPN 242
Cdd:COG1251  162 RKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRLADGEELPADLVVVAIGVRPN 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 243 TKLVHDTAIKLNRGIVVDEEMRTNIDSVYAAGDVAEVNNEIEG-----LWGTALEQGRVAGSNMVSKTAIYKKEIPTTIF 317
Cdd:COG1251  242 TELARAAGLAVDRGIVVDDYLRTSDPDIYAAGDCAEHPGPVYGrrvleLVAPAYEQARVAAANLAGGPAAYEGSVPSTKL 321

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 915492495 318 NAFNVSLFSIGVVNEEqcDTTIVEED-GKEKYTRLFIKDNKIVGVISLEGVAASISYKSAIEKHVSLEGIDLLNTNIS 394
Cdd:COG1251  322 KVFGVDVASAGDAEGD--EEVVVRGDpARGVYKKLVLRDGRLVGAVLVGDTSDAGALRQLIKNGRPLPPRALLDAALP 397
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
 6-362 8.02e-73

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


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 242.43  E-value: 8.02e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495    6 VIIGSGVAAVNAAKTIREYDKGS-NIFIFGEEPSLPYKRIKLSKDLYSDLHSEKVLIKKKKWYQDNHISVFINTKVVKIN 84
Cdd:TIGR02374   2 VLVGNGMAGHRCIEEVLKLNRHMfEITIFGEEPHPNYNRILLSSVLQGEADLDDITLNSKDWYEKHGITLYTGETVIQID 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495   85 TDEQFIVTSNEAVFSYHKLLICTGANNRRLEINGINKKNIFTIRDMKEADELKGHLEDKESVVTIGGGVQGLETAWSILK 164
Cdd:TIGR02374  82 TDQKQVITDAGRTLSYDKLILATGSYPFILPIPGADKKGVYVFRTIEDLDAIMAMAQRFKKAAVIGGGLLGLEAAVGLQN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  165 AGKKVSIVEVAPLLMRRQLDTKSSLLLKRRIEKEGVKVYLNTSIDSILGKESVTGIKMNDNSQINCDSIVYSIGVTPNTK 244
Cdd:TIGR02374 162 LGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVGATKADRIRFKDGSSLEADLIVMAAGIRPNDE 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  245 LVHDTAIKLNRGIVVDEEMRTNIDSVYAAGDVAEVNNEIEGLWGTALEQGRVAGSNMV-SKTAIYKKEIPTTIFNAFNVS 323
Cdd:TIGR02374 242 LAVSAGIKVNRGIIVNDSMQTSDPDIYAVGECAEHNGRVYGLVAPLYEQAKVLADHICgVECEEYEGSDLSAKLKLLGVD 321

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 915492495  324 LFSIGVVNE-EQCDTTIVEEDGKEKYTRLFIKDNKIVGVI 362
Cdd:TIGR02374 322 VWSAGDAQEtERTTSIKIYDEQKGIYKKLVLSDDKLLGAV 361
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 6-294 1.12e-54

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: 182.90  E-value: 1.12e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495    6 VIIGSGVAAVNAAKTIREYdkGSNIFIFGEEPSLPYKRIKLSKDLYSDLHSEKVLIKKKKWYQD---------NHISVFI 76
Cdd:pfam07992   4 VVIGGGPAGLAAALTLAQL--GGKVTLIEDEGTCPYGGCVLSKALLGAAEAPEIASLWADLYKRkeevvkklnNGIEVLL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495   77 NTKVVKINTDEQFI-----VTSNEAVFSYHKLLICTGANNRRLEINGINKKNIFTIRDMKEADELKgHLEDKESVVTIGG 151
Cdd:pfam07992  82 GTEVVSIDPGAKKVvleelVDGDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALR-LKLLPKRVVVVGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  152 GVQGLETAWSILKAGKKVSIVEVAPLLMRrQLDTKSSLLLKRRIEKEGVKVYLNTSIDSILGKESVTGIKMNDNSQINCD 231
Cdd:pfam07992 161 GYIGVELAAALAKLGKEVTLIEALDRLLR-AFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVILKDGTEIDAD 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 915492495  232 SIVYSIGVTPNTKLVHDTAIKLNR--GIVVDEEMRTNIDSVYAAGDVAEVnneIEGLWGTALEQG 294
Cdd:pfam07992 240 LVVVAIGRRPNTELLEAAGLELDErgGIVVDEYLRTSVPGIYAAGDCRVG---GPELAQNAVAQG 301
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
 2-302 1.95e-47

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 166.64  E-value: 1.95e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495   2 EKNFVIIGSGVAAVNAAKTIREYDKGSNIFIFGEEPSLPYKRIKLSKDLYSDLHSEKVLIKKKKWYQDNHISVFINTKVV 81
Cdd:PRK09754   3 EKTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPQLQQVLPANWWQENNVHLHSGVTIK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  82 KINTDEQFIVTSNEAVFSYHKLLICTGANNRRLEINGINKKNIFTIRDMKEADELKGHLEDKESVVTIGGGVQGLETAWS 161
Cdd:PRK09754  83 TLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELAAS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 162 ILKAGKKVSIVEVAPLLMRRQLDTKSSLLLKRRIEKEGVKVYLNTSIDSILGKESVTgIKMNDNSQINCDSIVYSIGVTP 241
Cdd:PRK09754 163 ATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVE-LTLQSGETLQADVVIYGIGISA 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 915492495 242 NTKLVHDTAIKLNRGIVVDEEMRTNIDSVYAAGDVA---EVNNEIE--GLWGTALEQGRVAGSNMV 302
Cdd:PRK09754 242 NDQLAREANLDTANGIVIDEACRTCDPAIFAGGDVAitrLDNGALHrcESWENANNQAQIAAAAML 307
 
Name Accession Description Interval E-value
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
3-394 1.53e-129

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 378.33  E-value: 1.53e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495   3 KNFVIIGSGVAAVNAAKTIREYDKGSNIFIFGEEPSLPYKRIKLSKDLYSDLHSEKVLIKKKKWYQDNHISVFINTKVVK 82
Cdd:COG1251    2 MRIVIIGAGMAGVRAAEELRKLDPDGEITVIGAEPHPPYNRPPLSKVLAGETDEEDLLLRPADFYEENGIDLRLGTRVTA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  83 INTDEQFIVTSNEAVFSYHKLLICTGANNRRLEINGINKKNIFTIRDMKEADELKGHLEDKESVVTIGGGVQGLETAWSI 162
Cdd:COG1251   82 IDRAARTVTLADGETLPYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRAALAPGKRVVVIGGGLIGLEAAAAL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 163 LKAGKKVSIVEVAPLLMRRQLDTKSSLLLKRRIEKEGVKVYLNTSIDSILGKESVTGIKMNDNSQINCDSIVYSIGVTPN 242
Cdd:COG1251  162 RKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRLADGEELPADLVVVAIGVRPN 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 243 TKLVHDTAIKLNRGIVVDEEMRTNIDSVYAAGDVAEVNNEIEG-----LWGTALEQGRVAGSNMVSKTAIYKKEIPTTIF 317
Cdd:COG1251  242 TELARAAGLAVDRGIVVDDYLRTSDPDIYAAGDCAEHPGPVYGrrvleLVAPAYEQARVAAANLAGGPAAYEGSVPSTKL 321

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 915492495 318 NAFNVSLFSIGVVNEEqcDTTIVEED-GKEKYTRLFIKDNKIVGVISLEGVAASISYKSAIEKHVSLEGIDLLNTNIS 394
Cdd:COG1251  322 KVFGVDVASAGDAEGD--EEVVVRGDpARGVYKKLVLRDGRLVGAVLVGDTSDAGALRQLIKNGRPLPPRALLDAALP 397
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
 6-362 8.02e-73

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


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 242.43  E-value: 8.02e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495    6 VIIGSGVAAVNAAKTIREYDKGS-NIFIFGEEPSLPYKRIKLSKDLYSDLHSEKVLIKKKKWYQDNHISVFINTKVVKIN 84
Cdd:TIGR02374   2 VLVGNGMAGHRCIEEVLKLNRHMfEITIFGEEPHPNYNRILLSSVLQGEADLDDITLNSKDWYEKHGITLYTGETVIQID 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495   85 TDEQFIVTSNEAVFSYHKLLICTGANNRRLEINGINKKNIFTIRDMKEADELKGHLEDKESVVTIGGGVQGLETAWSILK 164
Cdd:TIGR02374  82 TDQKQVITDAGRTLSYDKLILATGSYPFILPIPGADKKGVYVFRTIEDLDAIMAMAQRFKKAAVIGGGLLGLEAAVGLQN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  165 AGKKVSIVEVAPLLMRRQLDTKSSLLLKRRIEKEGVKVYLNTSIDSILGKESVTGIKMNDNSQINCDSIVYSIGVTPNTK 244
Cdd:TIGR02374 162 LGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVGATKADRIRFKDGSSLEADLIVMAAGIRPNDE 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  245 LVHDTAIKLNRGIVVDEEMRTNIDSVYAAGDVAEVNNEIEGLWGTALEQGRVAGSNMV-SKTAIYKKEIPTTIFNAFNVS 323
Cdd:TIGR02374 242 LAVSAGIKVNRGIIVNDSMQTSDPDIYAVGECAEHNGRVYGLVAPLYEQAKVLADHICgVECEEYEGSDLSAKLKLLGVD 321

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 915492495  324 LFSIGVVNE-EQCDTTIVEEDGKEKYTRLFIKDNKIVGVI 362
Cdd:TIGR02374 322 VWSAGDAQEtERTTSIKIYDEQKGIYKKLVLSDDKLLGAV 361
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 25-328 2.08e-69

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: 221.61  E-value: 2.08e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  25 DKGSNIFIFGEEPSLPYKRIKLSKDLYSDLHS-EKVLIKKKKWYQDNHISVFINTKVVKINTDEQFIVTSNEAVFSYHKL 103
Cdd:COG0446    3 GPDAEITVIEKGPHHSYQPCGLPYYVGGGIKDpEDLLVRTPESFERKGIDVRTGTEVTAIDPEAKTVTLRDGETLSYDKL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 104 LICTGANNRRLEINGINKKNIFTIRDMKEADELKGHLEDKE--SVVTIGGGVQGLETAWSILKAGKKVSIVEVAPLLMRR 181
Cdd:COG0446   83 VLATGARPRPPPIPGLDLPGVFTLRTLDDADALREALKEFKgkRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 182 qLDTKSSLLLKRRIEKEGVKVYLNTSIDSILGKESVTgIKMNDNSQINCDSIVYSIGVTPNTKLVHDTAIKLNR--GIVV 259
Cdd:COG0446  163 -LDPEMAALLEEELREHGVELRLGETVVAIDGDDKVA-VTLTDGEEIPADLVVVAPGVRPNTELAKDAGLALGErgWIKV 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 915492495 260 DEEMRTNIDSVYAAGDVAEVNNEIEG------LWGTALEQGRVAGSNMVSKTAIYkKEIPTTIFNAFNVSLFSIG 328
Cdd:COG0446  241 DETLQTSDPDVYAAGDCAEVPHPVTGktvyipLASAANKQGRVAAENILGGPAPF-PGLGTFISKVFDLCIASTG 314
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 6-294 1.12e-54

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: 182.90  E-value: 1.12e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495    6 VIIGSGVAAVNAAKTIREYdkGSNIFIFGEEPSLPYKRIKLSKDLYSDLHSEKVLIKKKKWYQD---------NHISVFI 76
Cdd:pfam07992   4 VVIGGGPAGLAAALTLAQL--GGKVTLIEDEGTCPYGGCVLSKALLGAAEAPEIASLWADLYKRkeevvkklnNGIEVLL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495   77 NTKVVKINTDEQFI-----VTSNEAVFSYHKLLICTGANNRRLEINGINKKNIFTIRDMKEADELKgHLEDKESVVTIGG 151
Cdd:pfam07992  82 GTEVVSIDPGAKKVvleelVDGDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALR-LKLLPKRVVVVGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  152 GVQGLETAWSILKAGKKVSIVEVAPLLMRrQLDTKSSLLLKRRIEKEGVKVYLNTSIDSILGKESVTGIKMNDNSQINCD 231
Cdd:pfam07992 161 GYIGVELAAALAKLGKEVTLIEALDRLLR-AFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVILKDGTEIDAD 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 915492495  232 SIVYSIGVTPNTKLVHDTAIKLNR--GIVVDEEMRTNIDSVYAAGDVAEVnneIEGLWGTALEQG 294
Cdd:pfam07992 240 LVVVAIGRRPNTELLEAAGLELDErgGIVVDEYLRTSVPGIYAAGDCRVG---GPELAQNAVAQG 301
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
 2-302 1.95e-47

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 166.64  E-value: 1.95e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495   2 EKNFVIIGSGVAAVNAAKTIREYDKGSNIFIFGEEPSLPYKRIKLSKDLYSDLHSEKVLIKKKKWYQDNHISVFINTKVV 81
Cdd:PRK09754   3 EKTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPQLQQVLPANWWQENNVHLHSGVTIK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  82 KINTDEQFIVTSNEAVFSYHKLLICTGANNRRLEINGINKKNIFTIRDMKEADELKGHLEDKESVVTIGGGVQGLETAWS 161
Cdd:PRK09754  83 TLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELAAS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 162 ILKAGKKVSIVEVAPLLMRRQLDTKSSLLLKRRIEKEGVKVYLNTSIDSILGKESVTgIKMNDNSQINCDSIVYSIGVTP 241
Cdd:PRK09754 163 ATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVE-LTLQSGETLQADVVIYGIGISA 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 915492495 242 NTKLVHDTAIKLNRGIVVDEEMRTNIDSVYAAGDVA---EVNNEIE--GLWGTALEQGRVAGSNMV 302
Cdd:PRK09754 242 NDQLAREANLDTANGIVIDEACRTCDPAIFAGGDVAitrLDNGALHrcESWENANNQAQIAAAAML 307
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 6-355 1.36e-46

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 165.60  E-value: 1.36e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495   6 VIIGSGVAAVNAAKTIREYDKGSNIFI--------FGEePSLPYkrikLSKDLYSDlhSEKVLIKKKKWYQDNHISVFIN 77
Cdd:PRK09564   4 IIIGGTAAGMSAAAKAKRLNKELEITVyektdivsFGA-CGLPY----FVGGFFDD--PNTMIARTPEEFIKSGIDVKTE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  78 TKVVKINTDEQFIVTSN---EAVF--SYHKLLICTGANNRRLEINGINKKNIFTIRDMKEADELKGHLEDKE--SVVTIG 150
Cdd:PRK09564  77 HEVVKVDAKNKTITVKNlktGSIFndTYDKLMIATGARPIIPPIKNINLENVYTLKSMEDGLALKELLKDEEikNIVIIG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 151 GGVQGLETAWSILKAGKKVSIVEVAPLLMRRQLDTKSSLLLKRRIEKEGVKVYLNTSIDSILGKESVTGIKmNDNSQINC 230
Cdd:PRK09564 157 AGFIGLEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEGVV-TDKGEYEA 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 231 DSIVYSIGVTPNTKLVHDTAIKL--NRGIVVDEEMRTNIDSVYAAGDVAEVNNEIEG------LWGTALEQGRVAGSNMV 302
Cdd:PRK09564 236 DVVIVATGVKPNTEFLEDTGLKTlkNGAIIVDEYGETSIENIYAAGDCATIYNIVSNknvyvpLATTANKLGRMVGENLA 315

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 915492495 303 SKtaiyKKEIPTTIFNAfnvslfSIGVVNEEQCDTTIVEEDGKE---KYTRLFIKD 355
Cdd:PRK09564 316 GR----HVSFKGTLGSA------CIKVLDLEAARTGLTEEEAKKlgiDYKTVFIKD 361
PRK14989 PRK14989
nitrite reductase subunit NirD; Provisional
 6-357 5.86e-37

nitrite reductase subunit NirD; Provisional


Pssm-ID: 184951 [Multi-domain]  Cd Length: 847  Bit Score: 142.95  E-value: 5.86e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495   6 VIIGSGVAAvnaAKTIREY-DKGS----NIFIFGEEPSLPYKRIKLSKdLYSDLHSEKVLIKKKKWYQDNHISVFINTKV 80
Cdd:PRK14989   7 AIIGNGMVG---HRFIEDLlDKADaanfDITVFCEEPRIAYDRVHLSS-YFSHHTAEELSLVREGFYEKHGIKVLVGERA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  81 VKINTDEQFIVTSNEAVFSYHKLLICTGANNRRLEINGINKKNIFTIRDMKEADELKGHLEDKESVVTIGGGVQGLETAW 160
Cdd:PRK14989  83 ITINRQEKVIHSSAGRTVFYDKLIMATGSYPWIPPIKGSETQDCFVYRTIEDLNAIEACARRSKRGAVVGGGLLGLEAAG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 161 SILKAGKKVSIVEVAPLLMRRQLDTKSSLLLKRRIEKEGVKVYLNTSIDSIL--GKESVTGIKMNDNSQINCDSIVYSIG 238
Cdd:PRK14989 163 ALKNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSKNTLEIVqeGVEARKTMRFADGSELEVDFIVFSTG 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 239 VTPNTKLVHDTAIKLNR--GIVVDEEMRTNIDSVYAAGDVAEVNNEIEGLWGTALEQGRVAGSNMVSKTAIYKKEIPTTI 316
Cdd:PRK14989 243 IRPQDKLATQCGLAVAPrgGIVINDSCQTSDPDIYAIGECASWNNRVFGLVAPGYKMAQVAVDHLLGSENAFEGADLSAK 322

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 915492495 317 FNAFNVSLFSIGVVN--EEQCDTTIVEEDGKEKYTRLFI-KDNK 357
Cdd:PRK14989 323 LKLLGVDVGGIGDAHgrTPGARSYVYLDESKEIYKRLIVsEDNK 366
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
1-280 6.01e-37

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 138.13  E-value: 6.01e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495   1 MEKNFVIIGSGVAAVNAAKTIREYDKGSNIFIF----GEEpslpYKRIKLSKdLYSDLHSEKVLIKKK--KWYQDNHISV 74
Cdd:PRK04965   1 MSNGIVIIGSGFAARQLVKNIRKQDAHIPITLItadsGDE----YNKPDLSH-VFSQGQRADDLTRQSagEFAEQFNLRL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  75 FINTKVVKINTDEQfIVTSNEAVFSYHKLLICTGANNRRLEINGinKKNIFTIRDMKEADELKGHLEDKESVVTIGGGVQ 154
Cdd:PRK04965  76 FPHTWVTDIDAEAQ-VVKSQGNQWQYDKLVLATGASAFVPPIPG--RELMLTLNSQQEYRAAETQLRDAQRVLVVGGGLI 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 155 GLETAWSILKAGKKVSIVEVAPLLMRRQLDTKSSLLLKRRIEKEGVKVYLNTSIDSILGKESVTGIKMNDNSQINCDSIV 234
Cdd:PRK04965 153 GTELAMDLCRAGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRATLDSGRSIEVDAVI 232

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 915492495 235 YSIGVTPNTKLVHDTAIKLNRGIVVDEEMRTNIDSVYAAGDVAEVN 280
Cdd:PRK04965 233 AAAGLRPNTALARRAGLAVNRGIVVDSYLQTSAPDIYALGDCAEIN 278
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 15-317 6.64e-31

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: 122.89  E-value: 6.64e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  15 VNAAKTIREYDKGSNIFIFGEEPSLPYKRIKLSKDLYSDLHSEKVlikkKKWYQDNHISV------FINTKVVKINTDEq 88
Cdd:COG1249   53 LHAAEVAHEARHAAEFGISAGAPSVDWAALMARKDKVVDRLRGGV----EELLKKNGVDVirgrarFVDPHTVEVTGGE- 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  89 fivtsneaVFSYHKLLICTGANNRRLEINGINKKNIFTIRDMKEADELKGHLedkesVVtIGGGVQGLETAwSILKA-GK 167
Cdd:COG1249  128 --------TLTADHIVIATGSRPRVPPIPGLDEVRVLTSDEALELEELPKSL-----VV-IGGGYIGLEFA-QIFARlGS 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 168 KVSIVEVAPLLMRRqLDTKSSLLLKRRIEKEGVKVYLNTSIDSILGKESVTGIKMNDNS---QINCDSIVYSIGVTPNTK 244
Cdd:COG1249  193 EVTLVERGDRLLPG-EDPEISEALEKALEKEGIDILTGAKVTSVEKTGDGVTVTLEDGGgeeAVEADKVLVATGRRPNTD 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 245 LVH-DTA-IKLNR--GIVVDEEMRTNIDSVYAAGDVAevnneieglwG------TALEQGRVAGSNMV---SKTAIYKKe 311
Cdd:COG1249  272 GLGlEAAgVELDErgGIKVDEYLRTSVPGIYAIGDVT----------GgpqlahVASAEGRVAAENILgkkPRPVDYRA- 340


                 ....*.
gi 915492495 312 IPTTIF 317
Cdd:COG1249  341 IPSVVF 346
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
75-277 8.92e-29

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 114.06  E-value: 8.92e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  75 FINTKVVKIN-TDEQFIV-TSNEAVFSYHKLLICTGANNRRLEINGInkkniftirdmkeaDELKGH------------L 140
Cdd:COG0492   74 ILLEEVTSVDkDDGPFRVtTDDGTEYEAKAVIIATGAGPRKLGLPGE--------------EEFEGRgvsycatcdgffF 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 141 EDKEsVVTIGGGVQGLETAWSILKAGKKVSIVevapllMRRQlDTKSSLLLKRRIEK-EGVKVYLNTSIDSILGKESVTG 219
Cdd:COG0492  140 RGKD-VVVVGGGDSALEEALYLTKFASKVTLI------HRRD-ELRASKILVERLRAnPKIEVLWNTEVTEIEGDGRVEG 211

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 915492495 220 IKMNDN-----SQINCDSIVYSIGVTPNTKLVHDTAIKLNRG--IVVDEEMRTNIDSVYAAGDVA 277
Cdd:COG0492  212 VTLKNVktgeeKELEVDGVFVAIGLKPNTELLKGLGLELDEDgyIVVDEDMETSVPGVFAAGDVR 276
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
6-300 5.89e-24

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 102.13  E-value: 5.89e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495   6 VIIGSGVAAVNAAKTIREYDKG---------SNIFIFGeePSLPY---KRIKLSKDLYsDLhsEKVLikkkkwyQDNHIS 73
Cdd:COG1252    5 VIVGGGFAGLEAARRLRKKLGGdaevtlidpNPYHLFQ--PLLPEvaaGTLSPDDIAI-PL--RELL-------RRAGVR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  74 vFINTKVVKINTDEQFIVTSNEAVFSYHKLLICTGANNRRLEINGInKKNIFTIRDMKEADELKGHLED---------KE 144
Cdd:COG1252   73 -FIQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGIPGL-AEHALPLKTLEDALALRERLLAaferaerrrLL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 145 SVVTIGGGVQGLETA------------WSILKAGK-KVSIVEVAPLLMRRqLDTKSSLLLKRRIEKEGVKVYLNTSIDSI 211
Cdd:COG1252  151 TIVVVGGGPTGVELAgelaellrkllrYPGIDPDKvRITLVEAGPRILPG-LGEKLSEAAEKELEKRGVEVHTGTRVTEV 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 212 LGkesvTGIKMNDNSQINCDSIVYSIGVTPNtKLVHDTAIKLNRG--IVVDEEMRT-NIDSVYAAGDVAEVNNEIEGLWG 288
Cdd:COG1252  230 DA----DGVTLEDGEEIPADTVIWAAGVKAP-PLLADLGLPTDRRgrVLVDPTLQVpGHPNVFAIGDCAAVPDPDGKPVP 304

                        330
                 ....*....|....*.
gi 915492495 289 ----TALEQGRVAGSN 300
Cdd:COG1252  305 ktaqAAVQQAKVLAKN 320
TRX_reduct TIGR01292
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ...
 75-276 3.20e-22

thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a member of the pyridine nucleotide-disulphide oxidoreductases (pfam00070). [Energy metabolism, Electron transport]


Pssm-ID: 273540 [Multi-domain]  Cd Length: 299  Bit Score: 95.77  E-value: 3.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495   75 FINTKVVKI-NTDEQFIV-TSNEAVFSYHKLLICTGANNRRLEINGINKkniFTIRDMKEADELKGHL-EDKEsVVTIGG 151
Cdd:TIGR01292  73 IIYEEVIKVdKSDRPFKVyTGDGKEYTAKAVIIATGASARKLGIPGEDE---FWGRGVSYCATCDGPFfKNKE-VAVVGG 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  152 GVQGLETAWSILKAGKKVSIVEvapllmRRQLDTKSSLLLKRRIEKEGVKVYLNTSIDSILGKESVTGIKMNDN-----S 226
Cdd:TIGR01292 149 GDSAIEEALYLTRIAKKVTLVH------RRDKFRAEKILLDRLKKNPKIEFLWNSTVEEIVGDNKVEGVKIKNTvtgeeE 222

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 915492495  227 QINCDSIVYSIGVTPNTKLVHDtAIKLNRG--IVVDEEMRTNIDSVYAAGDV 276
Cdd:TIGR01292 223 ELEVDGVFIAIGHEPNTELLKG-LLELDENgyIVTDEGMRTSVPGVFAAGDV 273
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 75-335 3.34e-22

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: 98.10  E-value: 3.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495   75 FINTKVVKINTdeqfivTSNEAVFSYHKLLICTGANNRrlEINGINKKNIFTIRDMKEADELKghlEDKESVVTIGGGVQ 154
Cdd:TIGR01350 113 FLDPGTVSVTG------ENGEETLEAKNIIIATGSRPR--SLPGPFDFDGKVVITSTGALNLE---EVPESLVIIGGGVI 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  155 GLETAWSILKAGKKVSIVEVAPLLMRrQLDTKSSLLLKRRIEKEGVKVYLNTSIDSILGKESVTGIKMNDNSQ--INCDS 232
Cdd:TIGR01350 182 GIEFASIFASLGSKVTVIEMLDRILP-GEDAEVSKVLQKALKKKGVKILTNTKVTAVEKNDDQVTYENKGGETetLTGEK 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  233 IVYSIGVTPNTKL--VHDTAIKLN-RG-IVVDEEMRTNIDSVYAAGDVaevnneIEG--LWGTALEQGRVAGSNMV--SK 304
Cdd:TIGR01350 261 VLVAVGRKPNTEGlgLEKLGVELDeRGrIVVDEYMRTNVPGIYAIGDV------IGGpmLAHVASHEGIVAAENIAgkEP 334

                         250       260       270
                  ....*....|....*....|....*....|.
gi 915492495  305 TAIYKKEIPTTIFNAFNVSlfSIGvVNEEQC 335
Cdd:TIGR01350 335 AHIDYDAVPSVIYTDPEVA--SVG-LTEEQA 362
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 75-317 4.61e-21

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 94.47  E-value: 4.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  75 FINTKVVKINtdEQFIVTSNeavfsyhkLLICTGAnnRRLEING---INKKNIFTIRDMKEADELKghledkESVVTIGG 151
Cdd:PRK06292 116 FVDPNTVEVN--GERIEAKN--------IVIATGS--RVPPIPGvwlILGDRLLTSDDAFELDKLP------KSLAVIGG 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 152 GVQGLETA--WSILkaGKKVSIVEVAPLLMRRQlDTKSSLLLKRRIEKEgVKVYLNTSIDSI--LGKESVTGIKMNDNSQ 227
Cdd:PRK06292 178 GVIGLELGqaLSRL--GVKVTVFERGDRILPLE-DPEVSKQAQKILSKE-FKIKLGAKVTSVekSGDEKVEELEKGGKTE 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 228 -INCDSIVYSIGVTPNTKLVH--DTAIKL-NRG-IVVDEEMRTNIDSVYAAGDvaeVNNEIEgLWGTALEQGRVAGSNMV 302
Cdd:PRK06292 254 tIEADYVLVATGRRPNTDGLGleNTGIELdERGrPVVDEHTQTSVPGIYAAGD---VNGKPP-LLHEAADEGRIAAENAA 329

                        250
                 ....*....|....*..
gi 915492495 303 SKTAIY--KKEIPTTIF 317
Cdd:PRK06292 330 GDVAGGvrYHPIPSVVF 346
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
 6-347 4.65e-20

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 91.38  E-value: 4.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495   6 VIIGSGVAAVNAAKTIREYDKGSNIFIFGEEPSLPYKRIKLSKDLYSDLHSEK--VLIKKKKWYQDNHISVFINTKVVKI 83
Cdd:PRK13512   5 IVVGAVAGGATCASQIRRLDKESDIIIFEKDRDMSFANCALPYYIGEVVEDRKyaLAYTPEKFYDRKQITVKTYHEVIAI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  84 NTDEQFIVTSN---EAVF--SYHKLLICTGANNRRLeinGINKKNIFTIRDMKEADELKGHLE--DKESVVTIGGGVQGL 156
Cdd:PRK13512  85 NDERQTVTVLNrktNEQFeeSYDKLILSPGASANSL---GFESDITFTLRNLEDTDAIDQFIKanQVDKALVVGAGYISL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 157 ETAWSILKAGKKVSIVEVAPLLMRrQLDTKSSLLLKRRIEKEGVKVYLNTSIDSILGKEsvtgIKMNDNSQINCDSIVYS 236
Cdd:PRK13512 162 EVLENLYERGLHPTLIHRSDKINK-LMDADMNQPILDELDKREIPYRLNEEIDAINGNE----VTFKSGKVEHYDMIIEG 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 237 IGVTPNTKLVHDTAIKLNRG--IVVDEEMRTNIDSVYAAGDVAE-------VNNEIEGLWGTALEQGRVAGSNMVSKTAI 307
Cdd:PRK13512 237 VGTHPNSKFIESSNIKLDDKgfIPVNDKFETNVPNIYAIGDIITshyrhvdLPASVPLAWGAHRAASIVAEQIAGNDTIE 316

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 915492495 308 YKKEIPTTIFNAFNVSLFSIGVVNEE--QCDTTIVEEDGKEK 347
Cdd:PRK13512 317 FKGFLGNNIVKFFDYTFASVGVKPNElkQFDYKMVEVTQGAH 358
PRK06370 PRK06370
FAD-containing oxidoreductase;
91-276 1.05e-18

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 87.57  E-value: 1.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  91 VTSNEAVFSYHKLLICTGANNRRLEINGINKKNIFTIRDMKEADELKGHLedkesvVTIGGGVQGLETAWSILKAGKKVS 170
Cdd:PRK06370 125 VRVGGETLRAKRIFINTGARAAIPPIPGLDEVGYLTNETIFSLDELPEHL------VIIGGGYIGLEFAQMFRRFGSEVT 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 171 IVEVAPLLMRRQlDTKSSLLLKRRIEKEGVKVYLNTSIDSILGKESVTGIKMN---DNSQINCDSIVYSIGVTPNT-KLV 246
Cdd:PRK06370 199 VIERGPRLLPRE-DEDVAAAVREILEREGIDVRLNAECIRVERDGDGIAVGLDcngGAPEITGSHILVAVGRVPNTdDLG 277

                        170       180       190
                 ....*....|....*....|....*....|...
gi 915492495 247 HDTA-IKLNR--GIVVDEEMRTNIDSVYAAGDV 276
Cdd:PRK06370 278 LEAAgVETDArgYIKVDDQLRTTNPGIYAAGDC 310
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 103-277 3.52e-18

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 85.97  E-value: 3.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 103 LLICTGANNRrlEINGIN--KKNIFTIRDMKEADELKghledkESVVTIGGGVQGLE--TAWSILkaGKKVSIVEVAPLL 178
Cdd:PRK06416 138 IILATGSRPR--ELPGIEidGRVIWTSDEALNLDEVP------KSLVVIGGGYIGVEfaSAYASL--GAEVTIVEALPRI 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 179 MRRQlDTKSSLLLKRRIEKEGVKVYLNTSIDSIlgKESVTGIKMND-----NSQINCDSIVYSIGVTPNTKLV--HDTAI 251
Cdd:PRK06416 208 LPGE-DKEISKLAERALKKRGIKIKTGAKAKKV--EQTDDGVTVTLedggkEETLEADYVLVAVGRRPNTENLglEELGV 284

                        170       180
                 ....*....|....*....|....*..
gi 915492495 252 KLNRG-IVVDEEMRTNIDSVYAAGDVA 277
Cdd:PRK06416 285 KTDRGfIEVDEQLRTNVPNIYAIGDIV 311
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
6-317 4.30e-18

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


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 85.59  E-value: 4.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495   6 VIIGSG----VAAVNAA---------------------------KTIREydKGSNIFIFGEEPSlpYKRIKLSKDL-YSD 53
Cdd:PRK05249   9 VVIGSGpageGAAMQAAklgkrvavieryrnvgggcthtgtipsKALRE--AVLRLIGFNQNPL--YSSYRVKLRItFAD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  54 L--HSEKVLIK----KKKWYQDNHISVFI--------NTKVVKINTDEQFIVTSNeavfsyhKLLICTGANNRRLEINGI 119
Cdd:PRK05249  85 LlaRADHVINKqvevRRGQYERNRVDLIQgrarfvdpHTVEVECPDGEVETLTAD-------KIVIATGSRPYRPPDVDF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 120 NKKNIF---TIRDMKEadelkghleDKESVVTIGGGVQGLETAwSILKA-GKKVSIVEvapllmRRQ-----LDTKSSLL 190
Cdd:PRK05249 158 DHPRIYdsdSILSLDH---------LPRSLIIYGAGVIGCEYA-SIFAAlGVKVTLIN------TRDrllsfLDDEISDA 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 191 LKRRIEKEGVKVYLNTSIDSILGKESVTGIKMNDNSQINCDSIVYSIGVTPNTKLVHDTAIKL---NRG-IVVDEEMRTN 266
Cdd:PRK05249 222 LSYHLRDSGVTIRHNEEVEKVEGGDDGVIVHLKSGKKIKADCLLYANGRTGNTDGLNLENAGLeadSRGqLKVNENYQTA 301

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 915492495 267 IDSVYAAGDVaevnneI--EGLWGTALEQGRVAGSNMV-SKTAIYKKEIPTTIF 317
Cdd:PRK05249 302 VPHIYAVGDV------IgfPSLASASMDQGRIAAQHAVgEATAHLIEDIPTGIY 349
MerA TIGR02053
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ...
 74-391 9.32e-17

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: 81.70  E-value: 9.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495   74 VFINTKVVKINtdeqfivtSNEAVFSYHKLLICTGANNRRLEINGINKKNIFTIRDMKEADELKghledkESVVTIGGGV 153
Cdd:TIGR02053 111 RFKDPKTVKVD--------LGREVRGAKRFLIATGARPAIPPIPGLKEAGYLTSEEALALDRIP------ESLAVIGGGA 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  154 QGLETAWSILKAGKKVSIVEVAPLLMRRQlDTKSSLLLKRRIEKEGVKVYLNTSIDSI---LGKESVTGIKMNDNSQINC 230
Cdd:TIGR02053 177 IGVELAQAFARLGSEVTILQRSDRLLPRE-EPEISAAVEEALAEEGIEVVTSAQVKAVsvrGGGKIITVEKPGGQGEVEA 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  231 DSIVYSIGVTPNTKLV--HDTAIKLNR--GIVVDEEMRTNIDSVYAAGDVAEvNNEIEGLwgtALEQGRVAGSNMV--SK 304
Cdd:TIGR02053 256 DELLVATGRRPNTDGLglEKAGVKLDErgGILVDETLRTSNPGIYAAGDVTG-GLQLEYV---AAKEGVVAAENALggAN 331

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  305 TAIYKKEIPTTIFNAFNVSlfSIGVVNEE------QCDTTIVEEDGKEK-----YTRLFIKDN------KIVGVISLEGV 367
Cdd:TIGR02053 332 AKLDLLVIPRVVFTDPAVA--SVGLTEAEaqkagiECDCRTLPLTNVPRarinrDTRGFIKLVaepgtgKVLGVQVVAPE 409

                         330       340
                  ....*....|....*....|....
gi 915492495  368 AASISYKSAIEKHVSLEGIDLLNT 391
Cdd:TIGR02053 410 AAEVINEAALAIRAGMTVDDLIDT 433
PRK07251 PRK07251
FAD-containing oxidoreductase;
75-276 1.85e-14

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 74.40  E-value: 1.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  75 FINTKVVKINTDEQFIVTSNEAVfsyhklLICTGANNRRLEINGI-NKKNIFTIRDMKEADELKGHLEdkesvvTIGGGV 153
Cdd:PRK07251 100 FVSNKVIEVQAGDEKIELTAETI------VINTGAVSNVLPIPGLaDSKHVYDSTGIQSLETLPERLG------IIGGGN 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 154 QGLETAWSILKAGKKVSIVEVAPLLMRRQLDTKSSLLlKRRIEKEGVKVYLNTSIDSILGKESVTGIKMNDNSQInCDSI 233
Cdd:PRK07251 168 IGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALA-KQYMEEDGITFLLNAHTTEVKNDGDQVLVVTEDETYR-FDAL 245

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 915492495 234 VYSIGVTPNTKLVH--DTAIKLN-RG-IVVDEEMRTNIDSVYAAGDV 276
Cdd:PRK07251 246 LYATGRKPNTEPLGleNTDIELTeRGaIKVDDYCQTSVPGVFAVGDV 292
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 75-281 9.60e-14

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 72.49  E-value: 9.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  75 FINTKVVKINTDEQFI----------VTSNEAVFSYHKLLICTGANNRRLEINGInKKNIFTIRDMKEADELKGHL---- 140
Cdd:PTZ00318  79 YLRAVVYDVDFEEKRVkcgvvsksnnANVNTFSVPYDKLVVAHGARPNTFNIPGV-EERAFFLKEVNHARGIRKRIvqci 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 141 ----------EDKE---SVVTIGGGVQGLETAWSI--------------LKAGKKVSIVEVAPLLMRrQLDTKSSLLLKR 193
Cdd:PTZ00318 158 eraslpttsvEERKrllHFVVVGGGPTGVEFAAELadffrddvrnlnpeLVEECKVTVLEAGSEVLG-SFDQALRKYGQR 236

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 194 RIEKEGVKVYLNTSIDSILGKESVTgikmNDNSQINCDSIVYSIGVTPNTKLVHDTAIKLNRG-IVVDEEMRT-NIDSVY 271
Cdd:PTZ00318 237 RLRRLGVDIRTKTAVKEVLDKEVVL----KDGEVIPTGLVVWSTGVGPGPLTKQLKVDKTSRGrISVDDHLRVkPIPNVF 312

                        250
                 ....*....|
gi 915492495 272 AAGDVAEVNN 281
Cdd:PTZ00318 313 ALGDCAANEE 322
PRK08010 PRK08010
pyridine nucleotide-disulfide oxidoreductase; Provisional
 75-276 1.51e-12

pyridine nucleotide-disulfide oxidoreductase; Provisional


Pssm-ID: 181196 [Multi-domain]  Cd Length: 441  Bit Score: 68.89  E-value: 1.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  75 FINTKVVKINTDEQFIVTSNEAVFsyhkllICTGANNRRLEINGINKK-NIFTIRDMKEADELKGHLEdkesvvTIGGGV 153
Cdd:PRK08010 101 FINNHSLRVHRPEGNLEIHGEKIF------INTGAQTVVPPIPGITTTpGVYDSTGLLNLKELPGHLG------ILGGGY 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 154 QGLETAWSILKAGKKVSIVEVAPLLMRRQlDTKSSLLLKRRIEKEGVKVYLNTSIDSILGKESVTGIKmNDNSQINCDSI 233
Cdd:PRK08010 169 IGVEFASMFANFGSKVTILEAASLFLPRE-DRDIADNIATILRDQGVDIILNAHVERISHHENQVQVH-SEHAQLAVDAL 246

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 915492495 234 VYSIGVTPNTKLVH--DTAIKLNR--GIVVDEEMRTNIDSVYAAGDV 276
Cdd:PRK08010 247 LIASGRQPATASLHpeNAGIAVNErgAIVVDKYLHTTADNIWAMGDV 293
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
 7-297 5.30e-12

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 66.55  E-value: 5.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495   7 IIGSGVAAVNAAKTIR-------EYDK---GSNIFIFG-EEPSLPYKRIKLS-KDLysdlhsekvlikkkkwyQDNHISV 74
Cdd:PRK12770  23 IIGAGPAGLAAAGYLAclgyevhVYDKlpePGGLMLFGiPEFRIPIERVREGvKEL-----------------EEAGVVF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  75 FINTKVV------KINTDE--QFIVTSNEAVFSYHKLLICTGA-NNRRLEINGINKKNI-------FTIRDMKeadelKG 138
Cdd:PRK12770  86 HTRTKVCcgeplhEEEGDEfvERIVSLEELVKKYDAVLIATGTwKSRKLGIPGEDLPGVysaleylFRIRAAK-----LG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 139 HLeDKES--------VVTIGGGVQGLETAWSILKAGkkvsiVEVAPLLMRRQLD----TKSSLllkRRIEKEGVKVYLNT 206
Cdd:PRK12770 161 YL-PWEKvppvegkkVVVVGAGLTAVDAALEAVLLG-----AEKVYLAYRRTINeapaGKYEI---ERLIARGVEFLELV 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 207 SIDSILGKESVTGIKM--------------------NDNSQINCDSIVYSIGVTPNTKL-VHDTAIKLNRG--IVVDEEM 263
Cdd:PRK12770 232 TPVRIIGEGRVEGVELakmrlgepdesgrprpvpipGSEFVLEADTVVFAIGEIPTPPFaKECLGIELNRKgeIVVDEKH 311

                        330       340       350
                 ....*....|....*....|....*....|....
gi 915492495 264 RTNIDSVYAAGDVAEVNNEIeglwGTALEQGRVA 297
Cdd:PRK12770 312 MTSREGVFAAGDVVTGPSKI----GKAIKSGLRA 341
PRK06116 PRK06116
glutathione reductase; Validated
 71-354 1.02e-11

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 66.33  E-value: 1.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  71 HISVFINTKVVKINTDEQFI----VTSNEAVFSYHKLLICTGANNRRLEINGINkkniFTIrDMKEADELKghlEDKESV 146
Cdd:PRK06116  99 YRNGLENNGVDLIEGFARFVdahtVEVNGERYTADHILIATGGRPSIPDIPGAE----YGI-TSDGFFALE---ELPKRV 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 147 VTIGGGVQGLETAwSILKA-GKKVSivevapLLMRRQL-----DTKSSLLLKRRIEKEGVKVYLNTSIDSI--LGKESVT 218
Cdd:PRK06116 171 AVVGAGYIAVEFA-GVLNGlGSETH------LFVRGDAplrgfDPDIRETLVEEMEKKGIRLHTNAVPKAVekNADGSLT 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 219 gIKMNDNSQINCDSIVYSIGVTPNTKLV--HDTAIKLN-RG-IVVDEEMRTNIDSVYAAGDvaeVNNEIEgLWGTALEQG 294
Cdd:PRK06116 244 -LTLEDGETLTVDCLIWAIGREPNTDGLglENAGVKLNeKGyIIVDEYQNTNVPGIYAVGD---VTGRVE-LTPVAIAAG 318

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 915492495 295 RVagsnmVSKTAIYKKE--------IPTTIFnafnvSLFSIGVVNeeqcdttIVEEDGKEKYTRLFIK 354
Cdd:PRK06116 319 RR-----LSERLFNNKPdekldysnIPTVVF-----SHPPIGTVG-------LTEEEAREQYGEDNVK 369
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
 80-317 1.26e-11

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 66.10  E-value: 1.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  80 VVKINTDEQFIVTSneavfsyHKLLICTGANNRRLEINGINKKNIFTIRDMKEADELKGHLedkesvVTIGGGVQGLETA 159
Cdd:PRK06327 133 EIKVTGEDETVITA-------KHVIIATGSEPRHLPGVPFDNKIILDNTGALNFTEVPKKL------AVIGAGVIGLELG 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 160 --WSILkaGKKVSIVEVAPLLMRRQLDTKSSLLLKRrIEKEGVKVYLNTSIDSI-LGKESVTgIKMND---NSQ-INCDS 232
Cdd:PRK06327 200 svWRRL--GAEVTILEALPAFLAAADEQVAKEAAKA-FTKQGLDIHLGVKIGEIkTGGKGVS-VAYTDadgEAQtLEVDK 275

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 233 IVYSIGVTPNTK-LVHDTA-IKLN-RG-IVVDEEMRTNIDSVYAAGDVaevnneIEG--LWGTALEQGRVAGSNMVSKTA 306
Cdd:PRK06327 276 LIVSIGRVPNTDgLGLEAVgLKLDeRGfIPVDDHCRTNVPNVYAIGDV------VRGpmLAHKAEEEGVAVAERIAGQKG 349

                        250
                 ....*....|..
gi 915492495 307 -IYKKEIPTTIF 317
Cdd:PRK06327 350 hIDYNTIPWVIY 361
Rubredoxin_C pfam18267
Rubredoxin NAD+ reductase C-terminal domain; This is the C-terminal domain of NADH rubredoxin ...
 313-379 1.41e-11

Rubredoxin NAD+ reductase C-terminal domain; This is the C-terminal domain of NADH rubredoxin oxidoreductase present in Clostridium acetobutylicum. The majority of obligatory anaerobes detoxify micro-aerobic environments by consuming O2 via H2O-forming NADH oxidase. This enzyme offers an alternate reaction pathway for scavenging of O2 and reactive oxygen species, wherein the reducing equivalent is obtained from NADH.


Pssm-ID: 408082 [Multi-domain]  Cd Length: 70  Bit Score: 59.49  E-value: 1.41e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 915492495  313 PTTIFNAFNVSLFSIGVVNE-EQCDTTIVEEDGKEKYTRLFIKDNKIVGVISLEGVAASISYKSAIEK 379
Cdd:pfam18267   1 PSTILKVFGIDLFSMGDIEEnDNAEEIVKVDASNGIYKKLFIRDGKLVGAILIGDTSESPKLKKAIEK 68
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 95-277 7.94e-11

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: 63.23  E-value: 7.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  95 EAVFsyhkllICTGA-NNRRLEINGINKKNIFT----IRDMKEADELKGHLEDKESVVTIGGGVQGLETAWSILKAG-KK 168
Cdd:COG0493  208 DAVF------LATGAgKPRDLGIPGEDLKGVHSamdfLTAVNLGEAPDTILAVGKRVVVIGGGNTAMDCARTALRLGaES 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 169 VSIVEvapllmRRQLDTKSSLllKRRIE---KEGVKVYLNTSIDSILGKES--VTGIKM-------NDNS---------- 226
Cdd:COG0493  282 VTIVY------RRTREEMPAS--KEEVEealEEGVEFLFLVAPVEIIGDENgrVTGLECvrmelgePDESgrrrpvpieg 353

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 915492495 227 ---QINCDSIVYSIGVTPNTKLVHDTA-IKLNRG--IVVDEE-MRTNIDSVYAAGDVA 277
Cdd:COG0493  354 sefTLPADLVILAIGQTPDPSGLEEELgLELDKRgtIVVDEEtYQTSLPGVFAGGDAV 411
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 145-224 1.01e-10

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: 57.60  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  145 SVVTIGGGVQGLETAWSILKAGKKVSIVEVAPLLMrRQLDTKSSLLLKRRIEKEGVKVYLNTSIDSILGKESVTGIKMND 224
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLL-PGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLTD 79
PRK13748 PRK13748
putative mercuric reductase; Provisional
 95-275 1.54e-10

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 62.86  E-value: 1.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  95 EAVFSYHKLLICTGANNRRLEINGINKKNIFTIRDMKEADELKGHLedkesvVTIGGGVQGLETAWSILKAGKKVSIVEV 174
Cdd:PRK13748 228 ERVVAFDRCLIATGASPAVPPIPGLKETPYWTSTEALVSDTIPERL------AVIGSSVVALELAQAFARLGSKVTILAR 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 175 APLLMRRqlDTKSSLLLKRRIEKEGVKVYLNTSIDSI--LGKESV--TGikmndNSQINCDSIVYSIGVTPNT-KLVHDT 249
Cdd:PRK13748 302 STLFFRE--DPAIGEAVTAAFRAEGIEVLEHTQASQVahVDGEFVltTG-----HGELRADKLLVATGRAPNTrSLALDA 374

                        170       180
                 ....*....|....*....|....*....
gi 915492495 250 A-IKLN-RG-IVVDEEMRTNIDSVYAAGD 275
Cdd:PRK13748 375 AgVTVNaQGaIVIDQGMRTSVPHIYAAGD 403
PRK07846 PRK07846
mycothione reductase; Reviewed
 144-276 2.50e-10

mycothione reductase; Reviewed


Pssm-ID: 181142 [Multi-domain]  Cd Length: 451  Bit Score: 61.89  E-value: 2.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 144 ESVVTIGGGVQGLETAWSILKAGKKVSIVEVAPLLMRRQLDTKSSLLLkrRIEKEGVKVYLNTSIDSILGKESVTGIKMN 223
Cdd:PRK07846 167 ESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLDDDISERFT--ELASKRWDVRLGRNVVGVSQDGSGVTLRLD 244

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 915492495 224 DNSQINCDSIVYSIGVTPNTKL--VHDTAIKLNRG--IVVDEEMRTNIDSVYAAGDV 276
Cdd:PRK07846 245 DGSTVEADVLLVATGRVPNGDLldAAAAGVDVDEDgrVVVDEYQRTSAEGVFALGDV 301
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 69-279 2.99e-10

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 61.71  E-value: 2.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  69 DNHISVFINTKVVKINTDEQFIV--TSNEAVFSYHKLLICTGANNRRLEINGinkkniftirdmkeADELKGH------- 139
Cdd:PRK15317 278 EYDVDIMNLQRASKLEPAAGLIEveLANGAVLKAKTVILATGARWRNMNVPG--------------EDEYRNKgvaycph 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 140 -----LEDKEsVVTIGGGVQGLETAwsILKAG--KKVSIVEVAPLLmrrqldtKSSLLLKRRIEK-EGVKVYLNTSIDSI 211
Cdd:PRK15317 344 cdgplFKGKR-VAVIGGGNSGVEAA--IDLAGivKHVTVLEFAPEL-------KADQVLQDKLRSlPNVTIITNAQTTEV 413

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 915492495 212 LGKES-VTGIKMNDNS-----QINCDSIVYSIGVTPNTKLVHDTaIKLN-RG-IVVDEEMRTNIDSVYAAGDVAEV 279
Cdd:PRK15317 414 TGDGDkVTGLTYKDRTtgeehHLELEGVFVQIGLVPNTEWLKGT-VELNrRGeIIVDARGATSVPGVFAAGDCTTV 488
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 96-277 3.93e-10

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 61.35  E-value: 3.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  96 AVFsyhkllICTGANN-RRLEINGINKKNIF-------TIRDMKEADEL-KGhledkESVVTIGGGvqglETAW-----S 161
Cdd:PRK11749 228 AVF------IGTGAGLpRFLGIPGENLGGVYsavdfltRVNQAVADYDLpVG-----KRVVVIGGG----NTAMdaartA 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 162 ILKAGKKVSIVevapllMRRQLDTKSSlllkRRIE-----KEGVKVYLNTSIDSILGKE----SVTGIKMNDNSQ----- 227
Cdd:PRK11749 293 KRLGAESVTIV------YRRGREEMPA----SEEEvehakEEGVEFEWLAAPVEILGDEgrvtGVEFVRMELGEPdasgr 362

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 915492495 228 -----------INCDSIVYSIGVTPNTKLVHDT-AIKLNR--GIVVDEE-MRTNIDSVYAAGDVA 277
Cdd:PRK11749 363 rrvpiegseftLPADLVIKAIGQTPNPLILSTTpGLELNRwgTIIADDEtGRTSLPGVFAGGDIV 427
Pyr_redox_3 pfam13738
Pyridine nucleotide-disulphide oxidoreductase;
70-274 4.71e-10

Pyridine nucleotide-disulphide oxidoreductase;


Pssm-ID: 404603 [Multi-domain]  Cd Length: 296  Bit Score: 60.32  E-value: 4.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495   70 NHISVFINTKVVKIN-TDEQFIVTSNEAVFSYHKLLICTG--ANNRRLEINGINKKNiftiRDMKEADELKGhledkESV 146
Cdd:pfam13738  88 FELPINLFEEVTSVKkEDDGFVVTTSKGTYQARYVIIATGefDFPNKLGVPELPKHY----SYVKDFHPYAG-----QKV 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  147 VTIGGGVQGLETAWSILKAGKKVSIVEVAPLLMRRQLDTKSSL------LLKRRIEKEGVKVYLNTSIDSILGKESVTGI 220
Cdd:pfam13738 159 VVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDRDSDPSYSLspdtlnRLEELVKNGKIKAHFNAEVKEITEVDVSYKV 238

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 915492495  221 KMNDNSQINCDSI-VYSIGVTPNTKLVHDTAIKLNRG--IVVDEE-MRTNIDSVYAAG 274
Cdd:pfam13738 239 HTEDGRKVTSNDDpILATGYHPDLSFLKKGLFELDEDgrPVLTEEtESTNVPGLFLAG 296
TGR TIGR01438
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ...
 58-346 1.69e-09

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


Pssm-ID: 273624 [Multi-domain]  Cd Length: 484  Bit Score: 59.48  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495   58 KVLIKKKKWYQDNHISVFINTKVVKiNTDEQfivtSNEAVFSYHKLLICTGANNRRLEINGINKKNIftirdmkEADELK 137
Cdd:TIGR01438 107 RVALREKKVKYENAYAEFVDKHRIK-ATNKK----GKEKIYSAERFLIATGERPRYPGIPGAKELCI-------TSDDLF 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  138 GHLEDKESVVTIGGGVQGLETAWSILKAGKKVSIVEVAPLLmrRQLDTKSSLLLKRRIEKEGVKVYLNTSIDSILGKESV 217
Cdd:TIGR01438 175 SLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILL--RGFDQDCANKVGEHMEEHGVKFKRQFVPIKVEQIEAK 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  218 TGIKMNDNSQINC---DSIVYSIGVTPNTKLVH--DTAIKLNRG---IVVDEEMRTNIDSVYAAGDVAEVNNEIEGLwgt 289
Cdd:TIGR01438 253 VLVEFTDSTNGIEeeyDTVLLAIGRDACTRKLNleNVGVKINKKtgkIPADEEEQTNVPYIYAVGDILEDKPELTPV--- 329

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 915492495  290 ALEQGRVAGSNMV--SKTAIYKKEIPTTIFNAFNVSlfSIGVVNEEQcdttiVEEDGKE 346
Cdd:TIGR01438 330 AIQAGRLLAQRLFkgSTVICDYENVPTTVFTPLEYG--ACGLSEEKA-----VEKFGEE 381
PLN02507 PLN02507
glutathione reductase
 79-276 3.72e-09

glutathione reductase


Pssm-ID: 215281 [Multi-domain]  Cd Length: 499  Bit Score: 58.29  E-value: 3.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  79 KVVKINTDEQFIVTSNEAVFSYHKLLICTGANNRRLEINGinkKNIFTIRDmkEADELKghlEDKESVVTIGGGVQGLET 158
Cdd:PLN02507 147 KIVGPNEVEVTQLDGTKLRYTAKHILIATGSRAQRPNIPG---KELAITSD--EALSLE---ELPKRAVVLGGGYIAVEF 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 159 AwSILKA-GKKVSIVEVAPLLMRrQLDTKSSLLLKRRIEKEGVKVYLNTSIDSILGKESVTGIKMNDNSQINCDSIVYSI 237
Cdd:PLN02507 219 A-SIWRGmGATVDLFFRKELPLR-GFDDEMRAVVARNLEGRGINLHPRTNLTQLTKTEGGIKVITDHGEEFVADVVLFAT 296

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 915492495 238 GVTPNTKLVH--DTAIKLNR--GIVVDEEMRTNIDSVYAAGDV 276
Cdd:PLN02507 297 GRAPNTKRLNleAVGVELDKagAVKVDEYSRTNIPSIWAIGDV 339
PRK12831 PRK12831
putative oxidoreductase; Provisional
 72-275 7.01e-07

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 51.17  E-value: 7.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  72 ISVFINTKVV---KINTDEQFIVTSNEAVFsyhkllICTGANNRR-LEINGINKKNIFTirdmkeADE-------LKGHL 140
Cdd:PRK12831 204 LGVKIETNVVvgkTVTIDELLEEEGFDAVF------IGSGAGLPKfMGIPGENLNGVFS------ANEfltrvnlMKAYK 271

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 141 EDKES-------VVTIGGGVQGLETAWSILKAGKKVSIVevapllMRRqldtkSSLLLKRRIE------KEGVKVYLNTS 207
Cdd:PRK12831 272 PEYDTpikvgkkVAVVGGGNVAMDAARTALRLGAEVHIV------YRR-----SEEELPARVEevhhakEEGVIFDLLTN 340

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 208 IDSILGKES--VTG---IKMN----DNS-------------QINCDSIVYSIGVTPNtKLVHDTA--IKLNRG--IVVDE 261
Cdd:PRK12831 341 PVEILGDENgwVKGmkcIKMElgepDASgrrrpveiegsefVLEVDTVIMSLGTSPN-PLISSTTkgLKINKRgcIVADE 419

                        250
                 ....*....|....*
gi 915492495 262 EM-RTNIDSVYAAGD 275
Cdd:PRK12831 420 ETgLTSKEGVFAGGD 434
PRK07845 PRK07845
flavoprotein disulfide reductase; Reviewed
 104-297 1.17e-06

flavoprotein disulfide reductase; Reviewed


Pssm-ID: 236112 [Multi-domain]  Cd Length: 466  Bit Score: 50.24  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 104 LICTGANNRRL---EINGinkKNIFTIRDMKEADELKGHLedkesvVTIGGGVQGLETAWSILKAGKKVSIV----EVAP 176
Cdd:PRK07845 144 LIATGASPRILptaEPDG---ERILTWRQLYDLDELPEHL------IVVGSGVTGAEFASAYTELGVKVTLVssrdRVLP 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 177 llmrrQLDTKSSLLLKRRIEKEGVKVYLNTSIDSIlgkeSVTG----IKMNDNSQINCDSIVYSIGVTPNTK-LVHDTA- 250
Cdd:PRK07845 215 -----GEDADAAEVLEEVFARRGMTVLKRSRAESV----ERTGdgvvVTLTDGRTVEGSHALMAVGSVPNTAgLGLEEAg 285

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 915492495 251 IKLNRG--IVVDEEMRTNIDSVYAAGDVAEVNneieGLWGTALEQGRVA 297
Cdd:PRK07845 286 VELTPSghITVDRVSRTSVPGIYAAGDCTGVL----PLASVAAMQGRIA 330
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 117-276 5.08e-06

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


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 48.58  E-value: 5.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 117 NGINKKNIFTIRD--MKEADEL-KGHLEDKESVVTIGGGVQGLETAWSILKAGkkvsiVEVAPLLMRRqldtkSSLLLKR 193
Cdd:PRK12778 541 NGVMSSNEYLTRVnlMDAASPDsDTPIKFGKKVAVVGGGNTAMDSARTAKRLG-----AERVTIVYRR-----SEEEMPA 610

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 194 RIE------KEGVKVYLNTSIDSILGKE-----SVTGIKMN----DNS-------------QINCDSIVYSIGVTPNtKL 245
Cdd:PRK12778 611 RLEevkhakEEGIEFLTLHNPIEYLADEkgwvkQVVLQKMElgepDASgrrrpvaipgstfTVDVDLVIVSVGVSPN-PL 689

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 915492495 246 VHDT--AIKLNR--GIVVDEEMRTNIDSVYAAGDV 276
Cdd:PRK12778 690 VPSSipGLELNRkgTIVVDEEMQSSIPGIYAGGDI 724
PTZ00052 PTZ00052
thioredoxin reductase; Provisional
 149-317 3.21e-05

thioredoxin reductase; Provisional


Pssm-ID: 185416 [Multi-domain]  Cd Length: 499  Bit Score: 45.97  E-value: 3.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 149 IGGGVQGLETAWSILKAGKKVSI-VEVAPLlmrRQLDTKSSLLLKRRIEKEGVKvYLNTSIDSILGK-ESVTGIKMNDNS 226
Cdd:PTZ00052 188 VGASYIGLETAGFLNELGFDVTVaVRSIPL---RGFDRQCSEKVVEYMKEQGTL-FLEGVVPINIEKmDDKIKVLFSDGT 263

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 227 QINCDSIVYSIGVTPNTKLVHDTAIKL-----NRGIVVDEEmrTNIDSVYAAGDVAEVNNEiegLWGTALEQGRVAGSNM 301
Cdd:PTZ00052 264 TELFDTVLYATGRKPDIKGLNLNAIGVhvnksNKIIAPNDC--TNIPNIFAVGDVVEGRPE---LTPVAIKAGILLARRL 338

                        170
                 ....*....|....*...
gi 915492495 302 V--SKTAIYKKEIPTTIF 317
Cdd:PTZ00052 339 FkqSNEFIDYTFIPTTIF 356
PTZ00058 PTZ00058
glutathione reductase; Provisional
 140-286 6.34e-05

glutathione reductase; Provisional


Pssm-ID: 185420 [Multi-domain]  Cd Length: 561  Bit Score: 44.99  E-value: 6.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 140 LEDKESVVTIGGGVQGLETAwSILKAGKKVSIVEVAPLLMRRQLDTKSSLLLKRRIEKEGVKVYLNTSIDSILGKES--V 217
Cdd:PTZ00058 234 IKEAKRIGIAGSGYIAVELI-NVVNRLGAESYIFARGNRLLRKFDETIINELENDMKKNNINIITHANVEEIEKVKEknL 312

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 915492495 218 TGIKMNDNSQINCDSIVYSIGVTPNTKLVHDTAI--KLNRG-IVVDEEMRTNIDSVYAAGDVAEV--NNEIEGL 286
Cdd:PTZ00058 313 TIYLSDGRKYEHFDYVIYCVGRSPNTEDLNLKALniKTPKGyIKVDDNQRTSVKHIYAVGDCCMVkkNQEIEDL 386
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
 141-278 1.14e-04

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


Pssm-ID: 200098 [Multi-domain]  Cd Length: 486  Bit Score: 44.19  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495  141 EDKESVVTIGGGVQGLETAwSILKA----GKKVSIVEVAPLLMRrQLDTKSSLLLKRRIEKEGVKVYLNTSIDSI-LGKE 215
Cdd:TIGR01423 185 EPPRRVLTVGGGFISVEFA-GIFNAykprGGKVTLCYRNNMILR-GFDSTLRKELTKQLRANGINIMTNENPAKVtLNAD 262

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 915492495  216 SVTGIKMNDNSQINCDSIVYSIGVTPNTKLVH--DTAIKL--NRGIVVDEEMRTNIDSVYAAGDVAE 278
Cdd:TIGR01423 263 GSKHVTFESGKTLDVDVVMMAIGRVPRTQTLQldKVGVELtkKGAIQVDEFSRTNVPNIYAIGDVTD 329
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
145-241 2.11e-04

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 43.31  E-value: 2.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 145 SVVTIGGGVQGLETAWSILKAGKKVSIVEVAPLL--MRRQLDTK-------SSLL--LKRRIEK-EGVKVYLNTSIDSIL 212
Cdd:COG1148  142 RALVIGGGIAGMTAALELAEQGYEVYLVEKEPELggRAAQLHKTfpgldcpQCILepLIAEVEAnPNITVYTGAEVEEVS 221

                         90       100       110
                 ....*....|....*....|....*....|....
gi 915492495 213 GKE---SVTgIKMNDNS--QINCDSIVYSIGVTP 241
Cdd:COG1148  222 GYVgnfTVT-IKKGPREeiEIEVGAIVLATGFKP 254
PLN02546 PLN02546
glutathione reductase
 144-361 3.20e-04

glutathione reductase


Pssm-ID: 215301 [Multi-domain]  Cd Length: 558  Bit Score: 42.94  E-value: 3.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 144 ESVVTIGGGVQGLETA--WSILKAGKKVSIVEVAPLlmrRQLDTKSSLLLKRRIEKEGVKVYLNTSIDSIL-GKESVTGI 220
Cdd:PLN02546 253 EKIAIVGGGYIALEFAgiFNGLKSDVHVFIRQKKVL---RGFDEEVRDFVAEQMSLRGIEFHTEESPQAIIkSADGSLSL 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 221 KMNDNSQINCDSIVYSIGVTPNTKLV--HDTAIKLNR--GIVVDEEMRTNIDSVYAAGDVAEVNNeiegLWGTALEQGrv 296
Cdd:PLN02546 330 KTNKGTVEGFSHVMFATGRKPNTKNLglEEVGVKMDKngAIEVDEYSRTSVPSIWAVGDVTDRIN----LTPVALMEG-- 403

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915492495 297 agsNMVSKTaIYKKEIPTTIFNAFNVSLFS---IGVV--NEEQCdttiVEEDGK-EKYT---------------RLFIK- 354
Cdd:PLN02546 404 ---GALAKT-LFGNEPTKPDYRAVPSAVFSqppIGQVglTEEQA----IEEYGDvDVFTanfrplkatlsglpdRVFMKl 475

                        250
                 ....*....|..
gi 915492495 355 -----DNKIVGV 361
Cdd:PLN02546 476 ivcakTNKVLGV 487
 
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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