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Conserved domains on  [gi|1298151778|gb|AUC62135|]
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NADH dehydrogenase [Cyanobacterium sp. HL-69]

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

 Zoom to residue level

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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];
16-380 5.44e-117

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


:

Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 345.58  E-value: 5.44e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778  16 YTALRLQELdWEGDFpEITLVDKGDRFLFSPLLYELITEEMQSWEVAPYYTELLEDSKINFIQDTVTGINLENKTVSLES 95
Cdd:COG1252    15 EAARRLRKK-LGGDA-EVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRAGVRFIQGEVTGIDPEARTVTLAD 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778  96 NSTLEYDRLVVAFGGTTPSQTVAGAKEYAIPFRTLNDAYTLKERLRQL--ENSDQEKIRVAIVGGGYSGVELAVKIGDRL 173
Cdd:COG1252    93 GRTLSYDYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAfeRAERRRLLTIVVVGGGPTGVELAGELAELL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 174 Q----------ERGKIRIIDRGDQILKKSPEFNRKTAEKALRDRKIWLDLDTEITSIEENQISLQYKnivDTIPVDLVLW 243
Cdd:COG1252   173 RkllrypgidpDKVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDADGVTLEDG---EEIPADTVIW 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 244 TVGTKPVKILDGLSLPQNEQGKLTINQELQVENYPEIFALGDLVESLDKDGNILPSTAQVAFQQSDYCAWNIWASLQEKP 323
Cdd:COG1252   250 AAGVKAPPLLADLGLPTDRRGRVLVDPTLQVPGHPNVFAIGDCAAVPDPDGKPVPKTAQAAVQQAKVLAKNIAALLRGKP 329

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1298151778 324 LLPFRYQPLGEMIALGIDNATLSGLGVSLDGGLAYLARRFVYLYRLPTPKHQLKVGL 380
Cdd:COG1252   330 LKPFRYRDKGCLASLGRGAAVADVGGLKLSGFLAWLLKRAIHLYFLPGFRGRLRVLL 386
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
16-380 5.44e-117

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 345.58  E-value: 5.44e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778  16 YTALRLQELdWEGDFpEITLVDKGDRFLFSPLLYELITEEMQSWEVAPYYTELLEDSKINFIQDTVTGINLENKTVSLES 95
Cdd:COG1252    15 EAARRLRKK-LGGDA-EVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRAGVRFIQGEVTGIDPEARTVTLAD 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778  96 NSTLEYDRLVVAFGGTTPSQTVAGAKEYAIPFRTLNDAYTLKERLRQL--ENSDQEKIRVAIVGGGYSGVELAVKIGDRL 173
Cdd:COG1252    93 GRTLSYDYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAfeRAERRRLLTIVVVGGGPTGVELAGELAELL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 174 Q----------ERGKIRIIDRGDQILKKSPEFNRKTAEKALRDRKIWLDLDTEITSIEENQISLQYKnivDTIPVDLVLW 243
Cdd:COG1252   173 RkllrypgidpDKVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDADGVTLEDG---EEIPADTVIW 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 244 TVGTKPVKILDGLSLPQNEQGKLTINQELQVENYPEIFALGDLVESLDKDGNILPSTAQVAFQQSDYCAWNIWASLQEKP 323
Cdd:COG1252   250 AAGVKAPPLLADLGLPTDRRGRVLVDPTLQVPGHPNVFAIGDCAAVPDPDGKPVPKTAQAAVQQAKVLAKNIAALLRGKP 329

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1298151778 324 LLPFRYQPLGEMIALGIDNATLSGLGVSLDGGLAYLARRFVYLYRLPTPKHQLKVGL 380
Cdd:COG1252   330 LKPFRYRDKGCLASLGRGAAVADVGGLKLSGFLAWLLKRAIHLYFLPGFRGRLRVLL 386
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 32-387 3.49e-40

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 147.61  E-value: 3.49e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778  32 EITLVDKGDRFLFSPLLYELITEEMQSWEVAPYYTELLEDSKINFIQDTVTGINLENKTV----------SLESNSTLEY 101
Cdd:PTZ00318   35 NITVISPRNHMLFTPLLPQTTTGTLEFRSICEPVRPALAKLPNRYLRAVVYDVDFEEKRVkcgvvsksnnANVNTFSVPY 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 102 DRLVVAFGGTTPSQTVAGAKEYAIPFRTLNDAYTLKERLRQ-LENSD------QEKIR---VAIVGGGYSGVELAVKIGD 171
Cdd:PTZ00318  115 DKLVVAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIVQcIERASlpttsvEERKRllhFVVVGGGPTGVEFAAELAD 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 172 -----------RLQERGKIRIIDRGDQILKKSPEFNRKTAEKALRDRKIWLDLDTEITSIEENQISLQYKNIvdtIPVDL 240
Cdd:PTZ00318  195 ffrddvrnlnpELVEECKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEVLDKEVVLKDGEV---IPTGL 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 241 VLWTVGTKPVKILDGLSLPQNEQGKLTINQELQVENYPEIFALGDLVESldkDGNILPSTAQVAFQQSDYCAWNIWASLQ 320
Cdd:PTZ00318  272 VVWSTGVGPGPLTKQLKVDKTSRGRISVDDHLRVKPIPNVFALGDCAAN---EERPLPTLAQVASQQGVYLAKEFNNELK 348

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1298151778 321 EKPLL-PFRYQPLGEMIALGIDNATLSGLGVSLDGGLAYLARRFVYLYRLPTPKHQLKVGLSWLSTPF 387
Cdd:PTZ00318  349 GKPMSkPFVYRSLGSLAYLGNYSAIVQLGAFDLSGFKALLFWRSAYLTILGSWRSKLYVLVNWAGTAI 416
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 32-307 1.07e-35

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: 132.44  E-value: 1.07e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778  32 EITLVDKGDRFLFS-PLLYELITEEMQSWEVAPYYTELLEDSK----------INFIQDTVTGINLENKTVSLESNS--- 97
Cdd:pfam07992  25 KVTLIEDEGTCPYGgCVLSKALLGAAEAPEIASLWADLYKRKEevvkklnngiEVLLGTEVVSIDPGAKKVVLEELVdgd 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778  98 --TLEYDRLVVAFGGTTPSQTVAGAKEYAIPF-RTLNDAYTLKERLRQLensdqekiRVAIVGGGYSGVELA---VKIGD 171
Cdd:pfam07992 105 geTITYDRLVIATGARPRLPPIPGVELNVGFLvRTLDSAEALRLKLLPK--------RVVVVGGGYIGVELAaalAKLGK 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 172 rlqergKIRIIDRGDQILKKSPEFNRKTAEKALRDRKIWLDLDTEITSIEENQISLQYK-NIVDTIPVDLVLWTVGTKP- 249
Cdd:pfam07992 177 ------EVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVIlKDGTEIDADLVVVAIGRRPn 250

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1298151778 250 VKILDGLSLPQNEQGKLTINQELQVeNYPEIFALGDlvesLDKDGnilPSTAQVAFQQ 307
Cdd:pfam07992 251 TELLEAAGLELDERGGIVVDEYLRT-SVPGIYAAGD----CRVGG---PELAQNAVAQ 300
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
 98-290 5.08e-05

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: 45.35  E-value: 5.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778  98 TLEYDRLVVAfGGTTPSQTVAGAKEYAIpfrTLNDAYTLKERLRqlensdqekiRVAIVGGGYSGVELAVKIGDRLQERG 177
Cdd:TIGR01423 149 RLQAEHILLA-TGSWPQMLGIPGIEHCI---SSNEAFYLDEPPR----------RVLTVGGGFISVEFAGIFNAYKPRGG 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 178 KIRIIDRGDQILKKSPEFNRKTAEKALRDRKIWLDLDTEITSIEENQISLQYKNIVD--TIPVDLVLWTVGTKPVKilDG 255
Cdd:TIGR01423 215 KVTLCYRNNMILRGFDSTLRKELTKQLRANGINIMTNENPAKVTLNADGSKHVTFESgkTLDVDVVMMAIGRVPRT--QT 292

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1298151778 256 LSLpQNEQGKLTINQELQVE-----NYPEIFALGDLVESL 290
Cdd:TIGR01423 293 LQL-DKVGVELTKKGAIQVDefsrtNVPNIYAIGDVTDRV 331
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
16-380 5.44e-117

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 345.58  E-value: 5.44e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778  16 YTALRLQELdWEGDFpEITLVDKGDRFLFSPLLYELITEEMQSWEVAPYYTELLEDSKINFIQDTVTGINLENKTVSLES 95
Cdd:COG1252    15 EAARRLRKK-LGGDA-EVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRAGVRFIQGEVTGIDPEARTVTLAD 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778  96 NSTLEYDRLVVAFGGTTPSQTVAGAKEYAIPFRTLNDAYTLKERLRQL--ENSDQEKIRVAIVGGGYSGVELAVKIGDRL 173
Cdd:COG1252    93 GRTLSYDYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAfeRAERRRLLTIVVVGGGPTGVELAGELAELL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 174 Q----------ERGKIRIIDRGDQILKKSPEFNRKTAEKALRDRKIWLDLDTEITSIEENQISLQYKnivDTIPVDLVLW 243
Cdd:COG1252   173 RkllrypgidpDKVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDADGVTLEDG---EEIPADTVIW 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 244 TVGTKPVKILDGLSLPQNEQGKLTINQELQVENYPEIFALGDLVESLDKDGNILPSTAQVAFQQSDYCAWNIWASLQEKP 323
Cdd:COG1252   250 AAGVKAPPLLADLGLPTDRRGRVLVDPTLQVPGHPNVFAIGDCAAVPDPDGKPVPKTAQAAVQQAKVLAKNIAALLRGKP 329

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1298151778 324 LLPFRYQPLGEMIALGIDNATLSGLGVSLDGGLAYLARRFVYLYRLPTPKHQLKVGL 380
Cdd:COG1252   330 LKPFRYRDKGCLASLGRGAAVADVGGLKLSGFLAWLLKRAIHLYFLPGFRGRLRVLL 386
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 32-387 3.49e-40

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 147.61  E-value: 3.49e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778  32 EITLVDKGDRFLFSPLLYELITEEMQSWEVAPYYTELLEDSKINFIQDTVTGINLENKTV----------SLESNSTLEY 101
Cdd:PTZ00318   35 NITVISPRNHMLFTPLLPQTTTGTLEFRSICEPVRPALAKLPNRYLRAVVYDVDFEEKRVkcgvvsksnnANVNTFSVPY 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 102 DRLVVAFGGTTPSQTVAGAKEYAIPFRTLNDAYTLKERLRQ-LENSD------QEKIR---VAIVGGGYSGVELAVKIGD 171
Cdd:PTZ00318  115 DKLVVAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIVQcIERASlpttsvEERKRllhFVVVGGGPTGVEFAAELAD 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 172 -----------RLQERGKIRIIDRGDQILKKSPEFNRKTAEKALRDRKIWLDLDTEITSIEENQISLQYKNIvdtIPVDL 240
Cdd:PTZ00318  195 ffrddvrnlnpELVEECKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEVLDKEVVLKDGEV---IPTGL 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 241 VLWTVGTKPVKILDGLSLPQNEQGKLTINQELQVENYPEIFALGDLVESldkDGNILPSTAQVAFQQSDYCAWNIWASLQ 320
Cdd:PTZ00318  272 VVWSTGVGPGPLTKQLKVDKTSRGRISVDDHLRVKPIPNVFALGDCAAN---EERPLPTLAQVASQQGVYLAKEFNNELK 348

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1298151778 321 EKPLL-PFRYQPLGEMIALGIDNATLSGLGVSLDGGLAYLARRFVYLYRLPTPKHQLKVGLSWLSTPF 387
Cdd:PTZ00318  349 GKPMSkPFVYRSLGSLAYLGNYSAIVQLGAFDLSGFKALLFWRSAYLTILGSWRSKLYVLVNWAGTAI 416
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 32-291 2.38e-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: 137.64  E-value: 2.38e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778  32 EITLVDKGDRFLFSP--LLYELITEEMQSWEVAPYYTELLEDSKINFI-QDTVTGINLENKTVSLESNSTLEYDRLVVAF 108
Cdd:COG0446     7 EITVIEKGPHHSYQPcgLPYYVGGGIKDPEDLLVRTPESFERKGIDVRtGTEVTAIDPEAKTVTLRDGETLSYDKLVLAT 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 109 GGT--TPSqtVAGAKEYAI-PFRTLNDAYTLKERLRQLENSdqekiRVAIVGGGYSGVELAvkigDRLQERG-KIRIIDR 184
Cdd:COG0446    87 GARprPPP--IPGLDLPGVfTLRTLDDADALREALKEFKGK-----RAVVIGGGPIGLELA----EALRKRGlKVTLVER 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 185 GDQILKK-SPEFNRKtAEKALRDRKIWLDLDTEITSIE-ENQISLQYKNiVDTIPVDLVLWTVGTKP-VKILDGLSLPQN 261
Cdd:COG0446   156 APRLLGVlDPEMAAL-LEEELREHGVELRLGETVVAIDgDDKVAVTLTD-GEEIPADLVVVAPGVRPnTELAKDAGLALG 233

                         250       260       270
                  ....*....|....*....|....*....|
gi 1298151778 262 EQGKLTINQELQVeNYPEIFALGDLVESLD 291
Cdd:COG0446   234 ERGWIKVDETLQT-SDPDVYAAGDCAEVPH 262
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 32-307 1.07e-35

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: 132.44  E-value: 1.07e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778  32 EITLVDKGDRFLFS-PLLYELITEEMQSWEVAPYYTELLEDSK----------INFIQDTVTGINLENKTVSLESNS--- 97
Cdd:pfam07992  25 KVTLIEDEGTCPYGgCVLSKALLGAAEAPEIASLWADLYKRKEevvkklnngiEVLLGTEVVSIDPGAKKVVLEELVdgd 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778  98 --TLEYDRLVVAFGGTTPSQTVAGAKEYAIPF-RTLNDAYTLKERLRQLensdqekiRVAIVGGGYSGVELA---VKIGD 171
Cdd:pfam07992 105 geTITYDRLVIATGARPRLPPIPGVELNVGFLvRTLDSAEALRLKLLPK--------RVVVVGGGYIGVELAaalAKLGK 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 172 rlqergKIRIIDRGDQILKKSPEFNRKTAEKALRDRKIWLDLDTEITSIEENQISLQYK-NIVDTIPVDLVLWTVGTKP- 249
Cdd:pfam07992 177 ------EVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVIlKDGTEIDADLVVVAIGRRPn 250

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1298151778 250 VKILDGLSLPQNEQGKLTINQELQVeNYPEIFALGDlvesLDKDGnilPSTAQVAFQQ 307
Cdd:pfam07992 251 TELLEAAGLELDERGGIVVDEYLRT-SVPGIYAAGD----CRVGG---PELAQNAVAQ 300
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
17-288 2.30e-21

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 94.82  E-value: 2.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778  17 TALRLQELDWEGdfpEITLVDKGDRFLFS-PLLYELITEEMQSWEVAPYYTELLEDSKINFIQDT-VTGINLENKTVSLE 94
Cdd:COG1251    16 AAEELRKLDPDG---EITVIGAEPHPPYNrPPLSKVLAGETDEEDLLLRPADFYEENGIDLRLGTrVTAIDRAARTVTLA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778  95 SNSTLEYDRLVVAFGGT--TPSqtVAGA-KEYAIPFRTLNDAYTLKERLRQLEnsdqekiRVAIVGGGYSGVELAvkigD 171
Cdd:COG1251    93 DGETLPYDKLVLATGSRprVPP--IPGAdLPGVFTLRTLDDADALRAALAPGK-------RVVVIGGGLIGLEAA----A 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 172 RLQERG-KIRIIDRGDQILkkSPEFNRKTAE---KALRDRKIWLDLDTEITSIE--ENQISLQYKNiVDTIPVDLVLWTV 245
Cdd:COG1251   160 ALRKRGlEVTVVERAPRLL--PRQLDEEAGAllqRLLEALGVEVRLGTGVTEIEgdDRVTGVRLAD-GEELPADLVVVAI 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1298151778 246 GTKP-VKILD--GLSLpqnEQGkLTINQELQVeNYPEIFALGDLVE 288
Cdd:COG1251   237 GVRPnTELARaaGLAV---DRG-IVVDDYLRT-SDPDIYAAGDCAE 277
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 65-315 2.71e-21

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: 95.15  E-value: 2.71e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778  65 YTELLEDSKINFIQDT--VTGinleNKTVSLESNSTLEYDRLVVAfGGTTPSQ-TVAGAKEyaIPFRTLNDAYTLKERLR 141
Cdd:COG1249    97 VEELLKKNGVDVIRGRarFVD----PHTVEVTGGETLTADHIVIA-TGSRPRVpPIPGLDE--VRVLTSDEALELEELPK 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 142 qlensdqekiRVAIVGGGYSGVELA-------VkigdrlqergKIRIIDRGDQILKKSPEFNRKTAEKALRDRKIWLDLD 214
Cdd:COG1249   170 ----------SLVVIGGGYIGLEFAqifarlgS----------EVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTG 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 215 TEITSIE--ENQISLQYKN--IVDTIPVDLVLWTVGTKPVkiLDGLSLPQ-----NEQGKLTINQELQVeNYPEIFALGD 285
Cdd:COG1249   230 AKVTSVEktGDGVTVTLEDggGEEAVEADKVLVATGRRPN--TDGLGLEAagvelDERGGIKVDEYLRT-SVPGIYAIGD 306

                         250       260       270
                  ....*....|....*....|....*....|
gi 1298151778 286 LVesldkdGNilPSTAQVAFQQSDYCAWNI 315
Cdd:COG1249   307 VT------GG--PQLAHVASAEGRVAAENI 328
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
 81-289 1.36e-16

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 80.98  E-value: 1.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778  81 VTGINLENKTVSL---ESNSTLE--YDRLVVAfggttpsqtvAGAKEYAIPFRTlNDAYTLkerlRQLENSDQ------- 148
Cdd:PRK13512   81 VIAINDERQTVTVlnrKTNEQFEesYDKLILS----------PGASANSLGFES-DITFTL----RNLEDTDAidqfika 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 149 -EKIRVAIVGGGYSGVELAvkigDRLQERG-KIRIIDRGDQILKKSPEFNRKTAEKALRDRKIWLDLDTEITSIEENQIS 226
Cdd:PRK13512  146 nQVDKALVVGAGYISLEVL----ENLYERGlHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDAINGNEVT 221

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1298151778 227 LQYKNIVDtipVDLVLWTVGTKP-VKILDGLSLPQNEQGKLTINQELQVeNYPEIFALGDLVES 289
Cdd:PRK13512  222 FKSGKVEH---YDMIIEGVGTHPnSKFIESSNIKLDDKGFIPVNDKFET-NVPNIYAIGDIITS 281
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 67-285 3.27e-14

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 73.54  E-value: 3.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778  67 ELLEDSKIN-FIQDTVTGINLENKTV---SLESNSTLE--YDRLVVAfggttpsqtvAGAKEYAIPFRTLN--DAYTLK- 137
Cdd:PRK09564   64 EEFIKSGIDvKTEHEVVKVDAKNKTItvkNLKTGSIFNdtYDKLMIA----------TGARPIIPPIKNINleNVYTLKs 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 138 ----ERLRQLENsDQEKIRVAIVGGGYSGVELAvkigDRLQERGK-IRIIDRGDQILKKS--PEFNRkTAEKALRDRKIW 210
Cdd:PRK09564  134 medgLALKELLK-DEEIKNIVIIGAGFIGLEAV----EAAKHLGKnVRIIQLEDRILPDSfdKEITD-VMEEELRENGVE 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 211 LDLDTEITSIEENQISlqYKNIVD--TIPVDLVLWTVGTKP-VKILDGLSLPQNEQGKLTINQ--ELQVENypeIFALGD 285
Cdd:PRK09564  208 LHLNEFVKSLIGEDKV--EGVVTDkgEYEADVVIVATGVKPnTEFLEDTGLKTLKNGAIIVDEygETSIEN---IYAAGD 282
PRK06116 PRK06116
glutathione reductase; Validated
 65-285 1.86e-12

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 68.26  E-value: 1.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778  65 YTELLEDSKINFIQDTVTGINleNKTVSLeSNSTLEYDRLVVAFGGTTPSQTVAGAkEYAIpfrTLNDAYTLKErlrqle 144
Cdd:PRK06116   99 YRNGLENNGVDLIEGFARFVD--AHTVEV-NGERYTADHILIATGGRPSIPDIPGA-EYGI---TSDGFFALEE------ 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 145 nsdQEKiRVAIVGGGYSGVELA-VkigdrLQERG-KIRIIDRGDQILKKSPEFNRKTAEKALRDRKIWLDLDTEITSIEE 222
Cdd:PRK06116  166 ---LPK-RVAVVGAGYIAVEFAgV-----LNGLGsETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEK 236

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1298151778 223 N---QISLQYKNiVDTIPVDLVLWTVGTKPVkiLDGLSLPQ-----NEQGKLTINqELQVENYPEIFALGD 285
Cdd:PRK06116  237 NadgSLTLTLED-GETLTVDCLIWAIGREPN--TDGLGLENagvklNEKGYIIVD-EYQNTNVPGIYAVGD 303
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 67-332 3.85e-12

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 67.51  E-value: 3.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778  67 ELLEDSKINFIQDTvtGINLENKTVSLEsNSTLEYDRLVVAFGGTTPSqtVAGAkeyaipFRTLNDAY-TLKERLrqlen 145
Cdd:PRK06292  100 GLEKKPKIDKIKGT--ARFVDPNTVEVN-GERIEAKNIVIATGSRVPP--IPGV------WLILGDRLlTSDDAF----- 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 146 sDQEKI--RVAIVGGGYSGVELAVKIGdRLqerG-KIRIIDRGDQILK-KSPEFnRKTAEKALrDRKIWLDLDTEITSIE 221
Cdd:PRK06292  164 -ELDKLpkSLAVIGGGVIGLELGQALS-RL---GvKVTVFERGDRILPlEDPEV-SKQAQKIL-SKEFKIKLGAKVTSVE 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 222 ENQISLQYKNIVD----TIPVDLVLWTVGTKPVkiLDGLSLPQ-----NEQGKLTINQELQvENYPEIFALGDLVesldk 292
Cdd:PRK06292  237 KSGDEKVEELEKGgkteTIEADYVLVATGRRPN--TDGLGLENtgielDERGRPVVDEHTQ-TSVPGIYAAGDVN----- 308

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1298151778 293 dgNILPsTAQVAFQQSDYCAWNIWASLQEKpllpFRYQPL 332
Cdd:PRK06292  309 --GKPP-LLHEAADEGRIAAENAAGDVAGG----VRYHPI 341
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
67-287 1.85e-11

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 64.37  E-value: 1.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778  67 ELLEDSKINFIQDTVTGINLEN--KTVSLESNSTLEYDRLVVAFGgttpsqtvAGAKEYAIP----FRTLN-------DA 133
Cdd:COG0492    65 EQAERFGAEILLEEVTSVDKDDgpFRVTTDDGTEYEAKAVIIATG--------AGPRKLGLPgeeeFEGRGvsycatcDG 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 134 YTLKERlrqlensdqekiRVAIVGGGYSGVELAV---KIGDrlqergKIRIIDRGDQiLKKSPEfnrkTAEKALRDRKIW 210
Cdd:COG0492   137 FFFRGK------------DVVVVGGGDSALEEALyltKFAS------KVTLIHRRDE-LRASKI----LVERLRANPKIE 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 211 LDLDTEITSIE-ENQI-SLQYKNIVD----TIPVDLVLWTVGTKP-VKILDGLSLPQNEQGKLTINQELQVeNYPEIFAL 283
Cdd:COG0492   194 VLWNTEVTEIEgDGRVeGVTLKNVKTgeekELEVDGVFVAIGLKPnTELLKGLGLELDEDGYIVVDEDMET-SVPGVFAA 272


                  ....
gi 1298151778 284 GDLV 287
Cdd:COG0492   273 GDVR 276
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
81-288 2.18e-11

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 64.55  E-value: 2.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778  81 VTGINLENKTVsLESNSTLEYDRLVVAfggttpsqtvAGAKEYAIPFR------TLNdayTLKErLRQLENSDQEKIRVA 154
Cdd:PRK04965   81 VTDIDAEAQVV-KSQGNQWQYDKLVLA----------TGASAFVPPIPgrelmlTLN---SQQE-YRAAETQLRDAQRVL 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 155 IVGGGYSGVELAVKigdrLQERGK-IRIIDRGDQILKK-SPEFNRKTAEKALRDRKIWLDLDTEITSIEENQISLQYKNI 232
Cdd:PRK04965  146 VVGGGLIGTELAMD----LCRAGKaVTLVDNAASLLASlMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRATLD 221

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1298151778 233 VD-TIPVDLVLWTVGTKPvkildGLSLPQneQGKLTINQELQVENY-----PEIFALGDLVE 288
Cdd:PRK04965  222 SGrSIEVDAVIAAAGLRP-----NTALAR--RAGLAVNRGIVVDSYlqtsaPDIYALGDCAE 276
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 152-315 3.24e-11

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 64.40  E-value: 3.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 152 RVAIVGGGYSGVELA---VKIGdrlqerGKIRIIDRGDQILkksPEFNR---KTAEKALRDRKIWLDLDTEITSIEENQ- 224
Cdd:PRK06416  174 SLVVIGGGYIGVEFAsayASLG------AEVTIVEALPRIL---PGEDKeisKLAERALKKRGIKIKTGAKAKKVEQTDd 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 225 ---ISLQYKNIVDTIPVDLVLWTVGTKPVkiLDGLSLpqNEQG-KLT-----INQELQvENYPEIFALGDLVESldkdgn 295
Cdd:PRK06416  245 gvtVTLEDGGKEETLEADYVLVAVGRRPN--TENLGL--EELGvKTDrgfieVDEQLR-TNVPNIYAIGDIVGG------ 313

                         170       180
                  ....*....|....*....|
gi 1298151778 296 ilPSTAQVAFQQSDYCAWNI 315
Cdd:PRK06416  314 --PMLAHKASAEGIIAAEAI 331
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 152-224 3.36e-09

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: 52.98  E-value: 3.36e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1298151778 152 RVAIVGGGYSGVELAVKigdrLQERG-KIRIIDRGDQILKKSPEFNRKTAEKALRDRKIWLDLDTEITSIEENQ 224
Cdd:pfam00070   1 RVVVVGGGYIGLELAGA----LARLGsKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNG 70
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
 80-286 6.25e-08

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 54.16  E-value: 6.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778  80 TVTGINLENKTVSLESNSTLEYDRLVVAFGGTT---PSQTVAGAKEYAIpfRTLNDAytlkERLRQLEnsdQEKIRVAIV 156
Cdd:PRK09754   80 TIKTLGRDTRELVLTNGESWHWDQLFIATGAAArplPLLDALGERCFTL--RHAGDA----ARLREVL---QPERSVVIV 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 157 GGGYSGVELAvkiGDRLQERGKIRIIDRGDQIL-KKSPEFNRKTAEKALRDRKIWLDLDTEITSIEENQISLQYKNIVDT 235
Cdd:PRK09754  151 GAGTIGLELA---ASATQRRCKVTVIELAATVMgRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVELTLQSGET 227

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1298151778 236 IPVDLVLWTVGtkpVKILDGLSLPQN--EQGKLTINQELQVENyPEIFALGDL 286
Cdd:PRK09754  228 LQADVVIYGIG---ISANDQLAREANldTANGIVIDEACRTCD-PAIFAGGDV 276
PRK06370 PRK06370
FAD-containing oxidoreductase;
89-285 1.11e-07

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 53.67  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778  89 KTVSLeSNSTLEYDRLVVAFGG--TTPSqtVAGAKEyaIPFRTLNDAYTLKERLRQLensdqekirvAIVGGGYSGVELA 166
Cdd:PRK06370  123 NTVRV-GGETLRAKRIFINTGAraAIPP--IPGLDE--VGYLTNETIFSLDELPEHL----------VIIGGGYIGLEFA 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 167 vKIGDRLqerG-KIRIIDRGDQILKKSPEFNRKTAEKALRDRKIWLDLDTEITSIE--ENQISLQY--KNIVDTIPVDLV 241
Cdd:PRK06370  188 -QMFRRF---GsEVTVIERGPRLLPREDEDVAAAVREILEREGIDVRLNAECIRVErdGDGIAVGLdcNGGAPEITGSHI 263

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1298151778 242 LWTVGTKPVkiLDGLSLPQ-----NEQGKLTINQELQVENyPEIFALGD 285
Cdd:PRK06370  264 LVAVGRVPN--TDDLGLEAagvetDARGYIKVDDQLRTTN-PGIYAAGD 309
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
 98-290 5.08e-05

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: 45.35  E-value: 5.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778  98 TLEYDRLVVAfGGTTPSQTVAGAKEYAIpfrTLNDAYTLKERLRqlensdqekiRVAIVGGGYSGVELAVKIGDRLQERG 177
Cdd:TIGR01423 149 RLQAEHILLA-TGSWPQMLGIPGIEHCI---SSNEAFYLDEPPR----------RVLTVGGGFISVEFAGIFNAYKPRGG 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 178 KIRIIDRGDQILKKSPEFNRKTAEKALRDRKIWLDLDTEITSIEENQISLQYKNIVD--TIPVDLVLWTVGTKPVKilDG 255
Cdd:TIGR01423 215 KVTLCYRNNMILRGFDSTLRKELTKQLRANGINIMTNENPAKVTLNADGSKHVTFESgkTLDVDVVMMAIGRVPRT--QT 292

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1298151778 256 LSLpQNEQGKLTINQELQVE-----NYPEIFALGDLVESL 290
Cdd:TIGR01423 293 LQL-DKVGVELTKKGAIQVDefsrtNVPNIYAIGDVTDRV 331
PRK08010 PRK08010
pyridine nucleotide-disulfide oxidoreductase; Provisional
 143-290 9.23e-05

pyridine nucleotide-disulfide oxidoreductase; Provisional


Pssm-ID: 181196 [Multi-domain]  Cd Length: 441  Bit Score: 44.23  E-value: 9.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 143 LENSDQEKIRVAIVGGGYSGVELAVKIGDRlqeRGKIRIIDRGDQILkksPEFNRKTAE---KALRDRKIWLDLDTEITS 219
Cdd:PRK08010  151 LLNLKELPGHLGILGGGYIGVEFASMFANF---GSKVTILEAASLFL---PREDRDIADniaTILRDQGVDIILNAHVER 224

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1298151778 220 IEENQISLQYKNIVDTIPVDLVLWTVGTKPVKI---LDGLSLPQNEQGKLTINQELQVeNYPEIFALGDLVESL 290
Cdd:PRK08010  225 ISHHENQVQVHSEHAQLAVDALLIASGRQPATAslhPENAGIAVNERGAIVVDKYLHT-TADNIWAMGDVTGGL 297
PTZ00052 PTZ00052
thioredoxin reductase; Provisional
 65-331 9.82e-05

thioredoxin reductase; Provisional


Pssm-ID: 185416 [Multi-domain]  Cd Length: 499  Bit Score: 44.43  E-value: 9.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778  65 YTELLEDSKINFIQDTVtgiNLENK-TVSLESNS-----TLEYdrLVVAFGGTtPS--QTVAGAKEYAIpfrTLNDAYTL 136
Cdd:PTZ00052  108 YRTGLRSSKVEYINGLA---KLKDEhTVSYGDNSqeetiTAKY--ILIATGGR-PSipEDVPGAKEYSI---TSDDIFSL 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 137 KerlrqlensdQEKIRVAIVGGGYSGVELAvkigDRLQERG-----KIR-IIDRGdqilkkspeFNRKTAEKAlrdrKIW 210
Cdd:PTZ00052  179 S----------KDPGKTLIVGASYIGLETA----GFLNELGfdvtvAVRsIPLRG---------FDRQCSEKV----VEY 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 211 LD----------LDTEITSIEENqISLQYKNIVdTIPVDLVLWTVGTKPvkILDGLSLPQ-----NEQGKLTINQElqVE 275
Cdd:PTZ00052  232 MKeqgtlflegvVPINIEKMDDK-IKVLFSDGT-TELFDTVLYATGRKP--DIKGLNLNAigvhvNKSNKIIAPND--CT 305

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1298151778 276 NYPEIFALGDLVESldkdgniLPSTAQVAFQQSDYCAWNIWASLQEkpLLPFRYQP 331
Cdd:PTZ00052  306 NIPNIFAVGDVVEG-------RPELTPVAIKAGILLARRLFKQSNE--FIDYTFIP 352
YdhS COG4529
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
58-184 3.57e-04

Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];


Pssm-ID: 443597 [Multi-domain]  Cd Length: 466  Bit Score: 42.63  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778  58 SWEVAPYYTELLEDSKINFIQDTVTGINLENK--TVSLESNSTLEYDRLVVAFGG---TTPSQTVAGAKEYaipfrtLND 132
Cdd:COG4529   106 RERLAEALARAPAGVRLRHIRAEVVDLERDDGgyRVTLADGETLRADAVVLATGHpppAPPPGLAAGSPRY------IAD 179

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1298151778 133 AYTLkERLRQLENSDqekiRVAIVGGGYSGVELAVKIGDRlQERGKIRIIDR 184
Cdd:COG4529   180 PWPP-GALARIPPDA----RVLIIGTGLTAIDVVLSLAAR-GHRGPITALSR 225
PRK15182 PRK15182
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;
149-304 9.64e-04

Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;


Pssm-ID: 185104 [Multi-domain]  Cd Length: 425  Bit Score: 41.21  E-value: 9.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 149 EKIRVAIVGGGYSGVELAVKIGDRLQERG----KIRIIDrgdqiLKKSPEFNRKTAEKALRDRKiWLDLDTEITSIEENQ 224
Cdd:PRK15182    5 DEVKIAIIGLGYVGLPLAVEFGKSRQVVGfdvnKKRILE-----LKNGVDVNLETTEEELREAR-YLKFTSEIEKIKECN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 225 ISL--------QYKNiVDTIPVDLVLWTVGT----KPVKILDGLSLPQNEQGK----------LTINQELQVENYPEIFA 282
Cdd:PRK15182   79 FYIitvptpinTYKQ-PDLTPLIKASETVGTvlnrGDIVVYESTVYPGCTEEEcvpilarmsgMTFNQDFYVGYSPERIN 157

                         170       180
                  ....*....|....*....|...
gi 1298151778 283 LGDLVESLDKDGNILP-STAQVA 304
Cdd:PRK15182  158 PGDKKHRLTNIKKITSgSTAQIA 180
PRK07251 PRK07251
FAD-containing oxidoreductase;
152-286 1.46e-03

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 40.50  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 152 RVAIVGGGYSGVELA---VKIGdrlqerGKIRIIDRGDQILKKSPEFNRKTAEKALRDRKIWLDLDTEITSI--EENQIS 226
Cdd:PRK07251  159 RLGIIGGGNIGLEFAglyNKLG------SKVTVLDAASTILPREEPSVAALAKQYMEEDGITFLLNAHTTEVknDGDQVL 232

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1298151778 227 LQYKNivDTIPVDLVLWTVGTKPVkiLDGLSLpQNEQGKLTINQELQVENY-----PEIFALGDL 286
Cdd:PRK07251  233 VVTED--ETYRFDALLYATGRKPN--TEPLGL-ENTDIELTERGAIKVDDYcqtsvPGVFAVGDV 292
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
 152-287 1.66e-03

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 40.29  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 152 RVAIVGGGYSGVELA---VKIGdrlqerGKIRIIDRGDQILKKSPEFNRKTAEKALRDRKIWLDLDTEITSIE--ENQIS 226
Cdd:PRK06327  185 KLAVIGAGVIGLELGsvwRRLG------AEVTILEALPAFLAAADEQVAKEAAKAFTKQGLDIHLGVKIGEIKtgGKGVS 258

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1298151778 227 LQY---KNIVDTIPVDLVLWTVGTKPVKI---LDGLSLPQNEQGKLTINQELQVeNYPEIFALGDLV 287
Cdd:PRK06327  259 VAYtdaDGEAQTLEVDKLIVSIGRVPNTDglgLEAVGLKLDERGFIPVDDHCRT-NVPNVYAIGDVV 324
PLN02507 PLN02507
glutathione reductase
 65-323 5.17e-03

glutathione reductase


Pssm-ID: 215281 [Multi-domain]  Cd Length: 499  Bit Score: 39.03  E-value: 5.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778  65 YTELLEDSKINFIQDTVTGINLENKTVSLESNSTLEY--DRLVVAFGGTTPSQTVAGaKEYAIpfrTLNDAYTLKERLRq 142
Cdd:PLN02507  130 YKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRYtaKHILIATGSRAQRPNIPG-KELAI---TSDEALSLEELPK- 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 143 lensdqekiRVAIVGGGYSGVELAVKIgdrlqeRG---KIRIIDRGDQILKKSPEFNRKTAEKALRDRKIWLDLDTEITS 219
Cdd:PLN02507  205 ---------RAVVLGGGYIAVEFASIW------RGmgaTVDLFFRKELPLRGFDDEMRAVVARNLEGRGINLHPRTNLTQ 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1298151778 220 IEENQISLqyKNIVD---TIPVDLVLWTVGTKPVKI---LDGLSLPQNEQGKLTINqELQVENYPEIFALGDLVESLdkd 293
Cdd:PLN02507  270 LTKTEGGI--KVITDhgeEFVADVVLFATGRAPNTKrlnLEAVGVELDKAGAVKVD-EYSRTNIPSIWAIGDVTNRI--- 343

                         250       260       270
                  ....*....|....*....|....*....|
gi 1298151778 294 gNILPstaqVAFQQSDYCAWNIWASLQEKP 323
Cdd:PLN02507  344 -NLTP----VALMEGTCFAKTVFGGQPTKP 368
YdhS COG4529
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
152-188 6.36e-03

Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];


Pssm-ID: 443597 [Multi-domain]  Cd Length: 466  Bit Score: 38.40  E-value: 6.36e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1298151778 152 RVAIVGGGYSGVELAVKIGDRLQERGKIRIIDRGDQI 188
Cdd:COG4529     7 RIAIIGGGASGTALAIHLLRRAPEPLRITLFEPRPEL 43
 
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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