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Conserved domains on  [gi|16129072|ref|NP_415627|]
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NADH:quinone oxidoreductase II [Escherichia coli str. K-12 substr. MG1655]

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];
18-416 5.30e-157

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


:

Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 448.81  E-value: 5.30e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  18 LEMATQLGHKLGrkKKAKITLVDRNHSHLWKPLLHEVATGSLDEGVDALSYLAHARNHGFQFQLGSVIDIDREAKTITIA 97
Cdd:COG1252  14 LEAARRLRKKLG--GDAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRAGVRFIQGEVTGIDPEARTVTLA 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  98 ElrdekgellvpERKIAYDTLVMALGSTSNDFNTPGVKENCIFLDNPHQARRFHQEMLNLFLKYSANlganGKVNIAIVG 177
Cdd:COG1252  92 D-----------GRTLSYDYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAFERAERR----RLLTIVVVG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072 178 GGATGVELSAELHNAVKQLHSYgyKGLTNEALNVTLVEAGERILPALPPRISAAAHNELTKLGVRVLTQTMVTSADEGGL 257
Cdd:COG1252 157 GGPTGVELAGELAELLRKLLRY--PGIDPDKVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDADGV 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072 258 HTKDGEYIEADLMVWAAGIKAPDFLKDIGgLETNRINQLVVEPTLQTTRDPDIYAIGDCASCPRPEGGFVPPRAQAAHQM 337
Cdd:COG1252 235 TLEDGEEIPADTVIWAAGVKAPPLLADLG-LPTDRRGRVLVDPTLQVPGHPNVFAIGDCAAVPDPDGKPVPKTAQAAVQQ 313
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129072 338 ATCAMNNILAQMNGKPLKNYQYKDHGSLVSLSNFSTVGSLMGnltrgsMMIEGRIARFVYISLYRMHQIALHGYFKTGL 416
Cdd:COG1252 314 AKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVGG------LKLSGFLAWLLKRAIHLYFLPGFRGRLRVLL 386
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
18-416 5.30e-157

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 448.81  E-value: 5.30e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  18 LEMATQLGHKLGrkKKAKITLVDRNHSHLWKPLLHEVATGSLDEGVDALSYLAHARNHGFQFQLGSVIDIDREAKTITIA 97
Cdd:COG1252  14 LEAARRLRKKLG--GDAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRAGVRFIQGEVTGIDPEARTVTLA 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  98 ElrdekgellvpERKIAYDTLVMALGSTSNDFNTPGVKENCIFLDNPHQARRFHQEMLNLFLKYSANlganGKVNIAIVG 177
Cdd:COG1252  92 D-----------GRTLSYDYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAFERAERR----RLLTIVVVG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072 178 GGATGVELSAELHNAVKQLHSYgyKGLTNEALNVTLVEAGERILPALPPRISAAAHNELTKLGVRVLTQTMVTSADEGGL 257
Cdd:COG1252 157 GGPTGVELAGELAELLRKLLRY--PGIDPDKVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDADGV 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072 258 HTKDGEYIEADLMVWAAGIKAPDFLKDIGgLETNRINQLVVEPTLQTTRDPDIYAIGDCASCPRPEGGFVPPRAQAAHQM 337
Cdd:COG1252 235 TLEDGEEIPADTVIWAAGVKAPPLLADLG-LPTDRRGRVLVDPTLQVPGHPNVFAIGDCAAVPDPDGKPVPKTAQAAVQQ 313
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129072 338 ATCAMNNILAQMNGKPLKNYQYKDHGSLVSLSNFSTVGSLMGnltrgsMMIEGRIARFVYISLYRMHQIALHGYFKTGL 416
Cdd:COG1252 314 AKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVGG------LKLSGFLAWLLKRAIHLYFLPGFRGRLRVLL 386
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
30-338 5.53e-62

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: 202.93  E-value: 5.53e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072    30 RKKKAKITLV-DRNHSHLWKPLLHEVATGSLDEGVDAL---SYLAHARNHGFQFQLG-------SVIDIDREAKTITIAE 98
Cdd:pfam07992  20 AQLGGKVTLIeDEGTCPYGGCVLSKALLGAAEAPEIASlwaDLYKRKEEVVKKLNNGievllgtEVVSIDPGAKKVVLEE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072    99 LRDEKGEllvperKIAYDTLVMALGSTSNDFNTPGVKENCIFL-DNPHQARRFHQEMLNLflkysanlgangkvNIAIVG 177
Cdd:pfam07992 100 LVDGDGE------TITYDRLVIATGARPRLPPIPGVELNVGFLvRTLDSAEALRLKLLPK--------------RVVVVG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072   178 GGATGVELSAELHNAVKQlhsygykgltnealnVTLVEAGERILPALPPRISAAAHNELTKLGVRVLTQTMVTSADEGG- 256
Cdd:pfam07992 160 GGYIGVELAAALAKLGKE---------------VTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGd 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072   257 ---LHTKDGEYIEADLMVWAAGIKAPDFLKDIGGLETNRINQLVVEPTLQTTrDPDIYAIGDCascprpeGGFVPPRAQA 333
Cdd:pfam07992 225 gveVILKDGTEIDADLVVVAIGRRPNTELLEAAGLELDERGGIVVDEYLRTS-VPGIYAAGDC-------RVGGPELAQN 296

                  ....*
gi 16129072   334 AHQMA 338
Cdd:pfam07992 297 AVAQG 301
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
32-401 9.01e-46

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 163.78  E-value: 9.01e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072   32 KKAKITLVD-RNHsHLWKPLLHEVATGSLdEGVDALSYLAHARNH-GFQFQLGSVIDIDREAKTITIAELRDEKGELlVP 109
Cdd:PTZ00318  32 KKYNITVISpRNH-MLFTPLLPQTTTGTL-EFRSICEPVRPALAKlPNRYLRAVVYDVDFEEKRVKCGVVSKSNNAN-VN 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  110 ERKIAYDTLVMALGSTSNDFNTPGVKENCIFLDNPHQARRFHQEMLNLFLKysANLG------ANGKVNIAIVGGGATGV 183
Cdd:PTZ00318 109 TFSVPYDKLVVAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIVQCIER--ASLPttsveeRKRLLHFVVVGGGPTGV 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  184 ELSAELHNAVKQLHSYGYKGLTNEAlNVTLVEAGERILPALPPRISAAAHNELTKLGVRVLTQTMVTSADEGGLHTKDGE 263
Cdd:PTZ00318 187 EFAAELADFFRDDVRNLNPELVEEC-KVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEVLDKEVVLKDGE 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  264 YIEADLMVWAAGIKAPDFLKDIGGLETNRiNQLVVEPTLQTTRDPDIYAIGDCASCprpEGGFVPPRAQAAHQMATCAMN 343
Cdd:PTZ00318 266 VIPTGLVVWSTGVGPGPLTKQLKVDKTSR-GRISVDDHLRVKPIPNVFALGDCAAN---EERPLPTLAQVASQQGVYLAK 341
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 16129072  344 NILAQMNGKPL-KNYQYKDHGSLVSLSNFSTVGSLmgnltrGSMMIEGRIARFVYISLY 401
Cdd:PTZ00318 342 EFNNELKGKPMsKPFVYRSLGSLAYLGNYSAIVQL------GAFDLSGFKALLFWRSAY 394
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
50-361 6.41e-20

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


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 92.58  E-value: 6.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072    50 LLHEVATGSLDEGVDALSYLAHARNHGFQFQLG-SVIDIDREAKTITIAElrdekgellvpERKIAYDTLVMALGSTSND 128
Cdd:TIGR02374  42 LLSSVLQGEADLDDITLNSKDWYEKHGITLYTGeTVIQIDTDQKQVITDA-----------GRTLSYDKLILATGSYPFI 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072   129 FNTPGV-KENCifldnpHQARRFH--QEMLNlflkysanlGANGKVNIAIVGGGATGVELSAELHNAVKQLHSYGYK-GL 204
Cdd:TIGR02374 111 LPIPGAdKKGV------YVFRTIEdlDAIMA---------MAQRFKKAAVIGGGLLGLEAAVGLQNLGMDVSVIHHApGL 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072   205 TNEALNvtlvEAGERILpalpprisaaaHNELTKLGVRVLTQT----MVTSADEGGLHTKDGEYIEADLMVWAAGIKAPD 280
Cdd:TIGR02374 176 MAKQLD----QTAGRLL-----------QRELEQKGLTFLLEKdtveIVGATKADRIRFKDGSSLEADLIVMAAGIRPND 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072   281 FLKDIGGLETNRinQLVVEPTLQTTrDPDIYAIGDCASCPRPEGGFVPPraqaAHQMATCAMNNILaqmnGKPLKNYQYK 360
Cdd:TIGR02374 241 ELAVSAGIKVNR--GIIVNDSMQTS-DPDIYAVGECAEHNGRVYGLVAP----LYEQAKVLADHIC----GVECEEYEGS 309

                  .
gi 16129072   361 D 361
Cdd:TIGR02374 310 D 310
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
18-416 5.30e-157

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 448.81  E-value: 5.30e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  18 LEMATQLGHKLGrkKKAKITLVDRNHSHLWKPLLHEVATGSLDEGVDALSYLAHARNHGFQFQLGSVIDIDREAKTITIA 97
Cdd:COG1252  14 LEAARRLRKKLG--GDAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRAGVRFIQGEVTGIDPEARTVTLA 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  98 ElrdekgellvpERKIAYDTLVMALGSTSNDFNTPGVKENCIFLDNPHQARRFHQEMLNLFLKYSANlganGKVNIAIVG 177
Cdd:COG1252  92 D-----------GRTLSYDYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAFERAERR----RLLTIVVVG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072 178 GGATGVELSAELHNAVKQLHSYgyKGLTNEALNVTLVEAGERILPALPPRISAAAHNELTKLGVRVLTQTMVTSADEGGL 257
Cdd:COG1252 157 GGPTGVELAGELAELLRKLLRY--PGIDPDKVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDADGV 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072 258 HTKDGEYIEADLMVWAAGIKAPDFLKDIGgLETNRINQLVVEPTLQTTRDPDIYAIGDCASCPRPEGGFVPPRAQAAHQM 337
Cdd:COG1252 235 TLEDGEEIPADTVIWAAGVKAPPLLADLG-LPTDRRGRVLVDPTLQVPGHPNVFAIGDCAAVPDPDGKPVPKTAQAAVQQ 313
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129072 338 ATCAMNNILAQMNGKPLKNYQYKDHGSLVSLSNFSTVGSLMGnltrgsMMIEGRIARFVYISLYRMHQIALHGYFKTGL 416
Cdd:COG1252 314 AKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVGG------LKLSGFLAWLLKRAIHLYFLPGFRGRLRVLL 386
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
30-338 5.53e-62

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: 202.93  E-value: 5.53e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072    30 RKKKAKITLV-DRNHSHLWKPLLHEVATGSLDEGVDAL---SYLAHARNHGFQFQLG-------SVIDIDREAKTITIAE 98
Cdd:pfam07992  20 AQLGGKVTLIeDEGTCPYGGCVLSKALLGAAEAPEIASlwaDLYKRKEEVVKKLNNGievllgtEVVSIDPGAKKVVLEE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072    99 LRDEKGEllvperKIAYDTLVMALGSTSNDFNTPGVKENCIFL-DNPHQARRFHQEMLNLflkysanlgangkvNIAIVG 177
Cdd:pfam07992 100 LVDGDGE------TITYDRLVIATGARPRLPPIPGVELNVGFLvRTLDSAEALRLKLLPK--------------RVVVVG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072   178 GGATGVELSAELHNAVKQlhsygykgltnealnVTLVEAGERILPALPPRISAAAHNELTKLGVRVLTQTMVTSADEGG- 256
Cdd:pfam07992 160 GGYIGVELAAALAKLGKE---------------VTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGd 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072   257 ---LHTKDGEYIEADLMVWAAGIKAPDFLKDIGGLETNRINQLVVEPTLQTTrDPDIYAIGDCascprpeGGFVPPRAQA 333
Cdd:pfam07992 225 gveVILKDGTEIDADLVVVAIGRRPNTELLEAAGLELDERGGIVVDEYLRTS-VPGIYAAGDC-------RVGGPELAQN 296

                  ....*
gi 16129072   334 AHQMA 338
Cdd:pfam07992 297 AVAQG 301
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
32-401 9.01e-46

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 163.78  E-value: 9.01e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072   32 KKAKITLVD-RNHsHLWKPLLHEVATGSLdEGVDALSYLAHARNH-GFQFQLGSVIDIDREAKTITIAELRDEKGELlVP 109
Cdd:PTZ00318  32 KKYNITVISpRNH-MLFTPLLPQTTTGTL-EFRSICEPVRPALAKlPNRYLRAVVYDVDFEEKRVKCGVVSKSNNAN-VN 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  110 ERKIAYDTLVMALGSTSNDFNTPGVKENCIFLDNPHQARRFHQEMLNLFLKysANLG------ANGKVNIAIVGGGATGV 183
Cdd:PTZ00318 109 TFSVPYDKLVVAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIVQCIER--ASLPttsveeRKRLLHFVVVGGGPTGV 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  184 ELSAELHNAVKQLHSYGYKGLTNEAlNVTLVEAGERILPALPPRISAAAHNELTKLGVRVLTQTMVTSADEGGLHTKDGE 263
Cdd:PTZ00318 187 EFAAELADFFRDDVRNLNPELVEEC-KVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEVLDKEVVLKDGE 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  264 YIEADLMVWAAGIKAPDFLKDIGGLETNRiNQLVVEPTLQTTRDPDIYAIGDCASCprpEGGFVPPRAQAAHQMATCAMN 343
Cdd:PTZ00318 266 VIPTGLVVWSTGVGPGPLTKQLKVDKTSR-GRISVDDHLRVKPIPNVFALGDCAAN---EERPLPTLAQVASQQGVYLAK 341
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 16129072  344 NILAQMNGKPL-KNYQYKDHGSLVSLSNFSTVGSLmgnltrGSMMIEGRIARFVYISLY 401
Cdd:PTZ00318 342 EFNNELKGKPMsKPFVYRSLGSLAYLGNYSAIVQL------GAFDLSGFKALLFWRSAY 394
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
30-355 1.37e-41

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: 149.96  E-value: 1.37e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  30 RKKKAKITLVDRNHSH------LWKPLLHEVATgsldegVDALSYLAHA--RNHGFQFQLGS-VIDIDREAKTITIAElr 100
Cdd:COG0446   2 LGPDAEITVIEKGPHHsyqpcgLPYYVGGGIKD------PEDLLVRTPEsfERKGIDVRTGTeVTAIDPEAKTVTLRD-- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072 101 dekgellvpERKIAYDTLVMALGSTSNDFNTPGVKENCIF-LDNPHQARRFHQEMLNlflkysanlgANGKvNIAIVGGG 179
Cdd:COG0446  74 ---------GETLSYDKLVLATGARPRPPPIPGLDLPGVFtLRTLDDADALREALKE----------FKGK-RAVVIGGG 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072 180 ATGVELSAELHNAvkqlhsygykGLtnealNVTLVEAGERILPALPPRISAAAHNELTKLGVRVLTQTMVTSADEGG--- 256
Cdd:COG0446 134 PIGLELAEALRKR----------GL-----KVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAIDGDDkva 198
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072 257 LHTKDGEYIEADLMVWAAGIkAPDF-LKDIGGLETNRINQLVVEPTLQtTRDPDIYAIGDCASCPRPEGG--FVPPRAQA 333
Cdd:COG0446 199 VTLTDGEEIPADLVVVAPGV-RPNTeLAKDAGLALGERGWIKVDETLQ-TSDPDVYAAGDCAEVPHPVTGktVYIPLASA 276
                       330       340
                ....*....|....*....|..
gi 16129072 334 AHQMATCAMNNILaqmnGKPLK 355
Cdd:COG0446 277 ANKQGRVAAENIL----GGPAP 294
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
48-346 1.14e-38

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 143.74  E-value: 1.14e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  48 KPLLHEVATGSLDEGVDALSYLAHARNHGFQFQLGS-VIDIDREAKTITiaelrDEKGEllvperKIAYDTLVMALGSTS 126
Cdd:COG1251  42 RPPLSKVLAGETDEEDLLLRPADFYEENGIDLRLGTrVTAIDRAARTVT-----LADGE------TLPYDKLVLATGSRP 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072 127 NDFNTPGV-KENCIFLDNPHQARRFHQEMlnlflkysanlgANGKvNIAIVGGGATGVELSAELHNAvkqlhsyGYKglt 205
Cdd:COG1251 111 RVPPIPGAdLPGVFTLRTLDDADALRAAL------------APGK-RVVVIGGGLIGLEAAAALRKR-------GLE--- 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072 206 nealnVTLVEAGERILP-ALPPRISAAAHNELTKLGVRVLTQTMVTS--ADEG--GLHTKDGEYIEADLMVWAAGIKaP- 279
Cdd:COG1251 168 -----VTVVERAPRLLPrQLDEEAGALLQRLLEALGVEVRLGTGVTEieGDDRvtGVRLADGEELPADLVVVAIGVR-Pn 241
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072 280 -DFLKDIGgLETNR-InqlVVEPTLQTTrDPDIYAIGDCASCP-RPEGGFVPPRAQAAHQMATCAMNNIL 346
Cdd:COG1251 242 tELARAAG-LAVDRgI---VVDDYLRTS-DPDIYAAGDCAEHPgPVYGRRVLELVAPAYEQARVAAANLA 306
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
173-348 2.39e-23

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


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 101.70  E-value: 2.39e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072 173 IAIVGGGATGVEL-SAelhnavkqLHSYGYKgltnealnVTLVEAGERILPALPPRISAAAHNELTKLGVRVLTQTMVTS 251
Cdd:COG1249 171 LVVIGGGYIGLEFaQI--------FARLGSE--------VTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTS 234
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072 252 ADEGG----LHTKDG---EYIEADLMVWAAGIKApdFLKDIG----GLETNRINQLVVEPTLQTTrDPDIYAIGDCAscp 320
Cdd:COG1249 235 VEKTGdgvtVTLEDGggeEAVEADKVLVATGRRP--NTDGLGleaaGVELDERGGIKVDEYLRTS-VPGIYAIGDVT--- 308
                       170       180
                ....*....|....*....|....*...
gi 16129072 321 rpeGGfvPPRAQAAHQMATCAMNNILAQ 348
Cdd:COG1249 309 ---GG--PQLAHVASAEGRVAAENILGK 331
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
84-348 9.73e-23

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 98.84  E-value: 9.73e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072   84 VIDIDREAKTITiaelrdekgellVPERKIAYDTLVMALGSTSndFNTPGVKENCIFLDNPHQARRFHQEMLnlflkysa 163
Cdd:PRK04965  81 VTDIDAEAQVVK------------SQGNQWQYDKLVLATGASA--FVPPIPGRELMLTLNSQQEYRAAETQL-------- 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  164 nlgANGKvNIAIVGGGATGVELSAELHNAVKQlhsygykgltnealnVTLVEAGERILPAL-PPRISAAAHNELTKLGVR 242
Cdd:PRK04965 139 ---RDAQ-RVLVVGGGLIGTELAMDLCRAGKA---------------VTLVDNAASLLASLmPPEVSSRLQHRLTEMGVH 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  243 VLTQTMVTSAD--EGGLH--TKDGEYIEADLMVWAAGIKAPDFLKDIGGLETNRinQLVVEPTLQTTrDPDIYAIGDCAS 318
Cdd:PRK04965 200 LLLKSQLQGLEktDSGIRatLDSGRSIEVDAVIAAAGLRPNTALARRAGLAVNR--GIVVDSYLQTS-APDIYALGDCAE 276
                        250       260       270
                 ....*....|....*....|....*....|
gi 16129072  319 CprpeGGFVPPRAQAAHQMATCAMNNILAQ 348
Cdd:PRK04965 277 I----NGQVLPFLQPIQLSAMALAKNLLGQ 302
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
50-361 6.41e-20

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


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 92.58  E-value: 6.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072    50 LLHEVATGSLDEGVDALSYLAHARNHGFQFQLG-SVIDIDREAKTITIAElrdekgellvpERKIAYDTLVMALGSTSND 128
Cdd:TIGR02374  42 LLSSVLQGEADLDDITLNSKDWYEKHGITLYTGeTVIQIDTDQKQVITDA-----------GRTLSYDKLILATGSYPFI 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072   129 FNTPGV-KENCifldnpHQARRFH--QEMLNlflkysanlGANGKVNIAIVGGGATGVELSAELHNAVKQLHSYGYK-GL 204
Cdd:TIGR02374 111 LPIPGAdKKGV------YVFRTIEdlDAIMA---------MAQRFKKAAVIGGGLLGLEAAVGLQNLGMDVSVIHHApGL 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072   205 TNEALNvtlvEAGERILpalpprisaaaHNELTKLGVRVLTQT----MVTSADEGGLHTKDGEYIEADLMVWAAGIKAPD 280
Cdd:TIGR02374 176 MAKQLD----QTAGRLL-----------QRELEQKGLTFLLEKdtveIVGATKADRIRFKDGSSLEADLIVMAAGIRPND 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072   281 FLKDIGGLETNRinQLVVEPTLQTTrDPDIYAIGDCASCPRPEGGFVPPraqaAHQMATCAMNNILaqmnGKPLKNYQYK 360
Cdd:TIGR02374 241 ELAVSAGIKVNR--GIIVNDSMQTS-DPDIYAVGECAEHNGRVYGLVAP----LYEQAKVLADHIC----GVECEEYEGS 309

                  .
gi 16129072   361 D 361
Cdd:TIGR02374 310 D 310
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
172-360 5.17e-17

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


Pssm-ID: 273568 [Multi-domain]  Cd Length: 460  Bit Score: 82.69  E-value: 5.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072   172 NIAIVGGGATGVELSAelhnavkQLHSYGYKgltnealnVTLVEAGERILPALPPRISAAAHNELTKLGVRVLTQTMVT- 250
Cdd:TIGR01350 172 SLVIIGGGVIGIEFAS-------IFASLGSK--------VTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTa 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072   251 -SADEGGLHTK----DGEYIEADLMVWAAGIKAPdfLKDIG----GLETNRINQLVVEPTLQTTrDPDIYAIGDCAscpr 321
Cdd:TIGR01350 237 vEKNDDQVTYEnkggETETLTGEKVLVAVGRKPN--TEGLGleklGVELDERGRIVVDEYMRTN-VPGIYAIGDVI---- 309
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 16129072   322 peGGfvPPRAQAAHQMATCAMNNILaqmnGKPLKNYQYK 360
Cdd:TIGR01350 310 --GG--PMLAHVASHEGIVAAENIA----GKEPAHIDYD 340
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
84-318 1.37e-16

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 81.24  E-value: 1.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072   84 VIDIDREAKTITIAELRDEKgellvpERKIAYDTLVMALGSTSNdfnTPGVKEncIFLDNPHQARRFH--QEMLNLFLKY 161
Cdd:PRK09564  79 VVKVDAKNKTITVKNLKTGS------IFNDTYDKLMIATGARPI---IPPIKN--INLENVYTLKSMEdgLALKELLKDE 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  162 SanlgangKVNIAIVGGGATGVELSAELHNAVKqlhsygykgltnealNVTLVEAGERILP-ALPPRISAAAHNELTKLG 240
Cdd:PRK09564 148 E-------IKNIVIIGAGFIGLEAVEAAKHLGK---------------NVRIIQLEDRILPdSFDKEITDVMEEELRENG 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  241 VRVLTQTMVTSAD-EG---GLHTKDGEYiEADLMVWAAGIK-APDFLKDiGGLETNRINQLVVEPTLQTTrDPDIYAIGD 315
Cdd:PRK09564 206 VELHLNEFVKSLIgEDkveGVVTDKGEY-EADVVIVATGVKpNTEFLED-TGLKTLKNGAIIVDEYGETS-IENIYAAGD 282

                 ...
gi 16129072  316 CAS 318
Cdd:PRK09564 283 CAT 285
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
173-315 1.65e-14

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 75.18  E-value: 1.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  173 IAIVGGGATGVEL-SAelhnavkqlhsygYKGLTNEalnVTLVEAGERILPALPPRISAAAHNELTKLGVRVLTQTMVTS 251
Cdd:PRK06416 175 LVVIGGGYIGVEFaSA-------------YASLGAE---VTIVEALPRILPGEDKEISKLAERALKKRGIKIKTGAKAKK 238
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129072  252 ADEGG----LHTKDG---EYIEADLMVWAAGIkAPDfLKDIG----GLETNRiNQLVVEPTLQTTrDPDIYAIGD 315
Cdd:PRK06416 239 VEQTDdgvtVTLEDGgkeETLEADYVLVAVGR-RPN-TENLGleelGVKTDR-GFIEVDEQLRTN-VPNIYAIGD 309
PRK14989 PRK14989
nitrite reductase subunit NirD; Provisional
75-350 2.54e-13

nitrite reductase subunit NirD; Provisional


Pssm-ID: 184951 [Multi-domain]  Cd Length: 847  Bit Score: 72.07  E-value: 2.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072   75 HGFQFQLGS-VIDIDREAKTItiaelRDEKGellvpeRKIAYDTLVMALGSTSNdfnTPGVKenciflDNPHQARRFHQE 153
Cdd:PRK14989  72 HGIKVLVGErAITINRQEKVI-----HSSAG------RTVFYDKLIMATGSYPW---IPPIK------GSETQDCFVYRT 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  154 MLNL-FLKYSANLGANGkvniAIVGGGATGVELSAelhnAVKQLhsygykGLTNEALNVTLVEAGERilpaLPPRISAAA 232
Cdd:PRK14989 132 IEDLnAIEACARRSKRG----AVVGGGLLGLEAAG----ALKNL------GVETHVIEFAPMLMAEQ----LDQMGGEQL 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  233 HNELTKLGVRVLT----QTMVTSADEGG--LHTKDGEYIEADLMVWAAGIKAPDFLKDIGGLETNRINQLVVEPTLQTTr 306
Cdd:PRK14989 194 RRKIESMGVRVHTskntLEIVQEGVEARktMRFADGSELEVDFIVFSTGIRPQDKLATQCGLAVAPRGGIVINDSCQTS- 272
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 16129072  307 DPDIYAIGDCASCPRPEGGFVPPraqaAHQMATCAMNNILAQMN 350
Cdd:PRK14989 273 DPDIYAIGECASWNNRVFGLVAP----GYKMAQVAVDHLLGSEN 312
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
173-316 9.61e-13

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 69.44  E-value: 9.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  173 IAIVGGGATGVEL-SAelhnavkqLHSYGYKgltnealnVTLVEAGERILPALPPRISAAAHNELTKlGVRVLTQTMVTS 251
Cdd:PRK06292 172 LAVIGGGVIGLELgQA--------LSRLGVK--------VTVFERGDRILPLEDPEVSKQAQKILSK-EFKIKLGAKVTS 234
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129072  252 ADEGG-----LHTKDGE--YIEADLMVWAAGIKApdFLKDIG----GLETNRINQLVVEPTLQTTrDPDIYAIGDC 316
Cdd:PRK06292 235 VEKSGdekveELEKGGKteTIEADYVLVATGRRP--NTDGLGlentGIELDERGRPVVDEHTQTS-VPGIYAAGDV 307
MerA TIGR02053
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ...
173-350 4.65e-12

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: 67.45  E-value: 4.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072   173 IAIVGGGATGVELSAELHNAvkqlhsygykgltneALNVTLVEAGERILPALPPRISAAAHNELTKLGVRVLTQTMVT-- 250
Cdd:TIGR02053 169 LAVIGGGAIGVELAQAFARL---------------GSEVTILQRSDRLLPREEPEISAAVEEALAEEGIEVVTSAQVKav 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072   251 SADEGG----LHTKDGEY-IEADLMVWAAGiKAP--DFLK-DIGGLETNRINQLVVEPTLQTTrDPDIYAIGDCASCPRp 322
Cdd:TIGR02053 234 SVRGGGkiitVEKPGGQGeVEADELLVATG-RRPntDGLGlEKAGVKLDERGGILVDETLRTS-NPGIYAAGDVTGGLQ- 310
                         170       180
                  ....*....|....*....|....*...
gi 16129072   323 eggFVPPRAQAAHQMATCAMNNILAQMN 350
Cdd:TIGR02053 311 ---LEYVAAKEGVVAAENALGGANAKLD 335
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
172-256 1.42e-11

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


Pssm-ID: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 59.91  E-value: 1.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072   172 NIAIVGGGATGVELSAELHNavkqlhsYGYKgltnealnVTLVEAGERILPALPPRISAAAHNELTKLGVRVLTQTMVTS 251
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALAR-------LGSK--------VTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEA 65

                  ....*
gi 16129072   252 ADEGG 256
Cdd:pfam00070  66 IEGNG 70
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
99-324 5.67e-11

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 63.79  E-value: 5.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072   99 LRDEKGELLVPERKIAYDTLVMALGSTSNDFNT-PGVKENCIFLDNPHQARRFHQEMlnlflkysanlgANGKvNIAIVG 177
Cdd:PRK09754  85 GRDTRELVLTNGESWHWDQLFIATGAAARPLPLlDALGERCFTLRHAGDAARLREVL------------QPER-SVVIVG 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  178 GGATGVELSAElhnavkqlhsygykgLTNEALNVTLVEAGERIL-PALPPRISAAAHNELTKLGVRVLTQTMVTSADEGG 256
Cdd:PRK09754 152 AGTIGLELAAS---------------ATQRRCKVTVIELAATVMgRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGE 216
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129072  257 ---LHTKDGEYIEADLMVWAAGIKAPDFLKDIGGLETNriNQLVVEPTLQTTrDPDIYAIGDCASCPRPEG 324
Cdd:PRK09754 217 kveLTLQSGETLQADVVIYGIGISANDQLAREANLDTA--NGIVIDEACRTC-DPAIFAGGDVAITRLDNG 284
PRK06116 PRK06116
glutathione reductase; Validated
173-316 7.47e-11

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 63.64  E-value: 7.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  173 IAIVGGGATGVELSAELHnavkqlhsygykGLTNEalnVTLVEAGERILPALPPRISAAAHNELTKLGVRVLTQTMVTS- 251
Cdd:PRK06116 170 VAVVGAGYIAVEFAGVLN------------GLGSE---THLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAv 234
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129072  252 --ADEGGL--HTKDGEYIEADLMVWAAGiKAPDfLKDIG----GLETNRINQLVVEpTLQTTRDPDIYAIGDC 316
Cdd:PRK06116 235 ekNADGSLtlTLEDGETLTVDCLIWAIG-REPN-TDGLGlenaGVKLNEKGYIIVD-EYQNTNVPGIYAVGDV 304
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
73-321 6.96e-10

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: 60.53  E-value: 6.96e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  73 RNHGFQFQLGSVIDidreaKTITIAELRDEkgellvperkiaYDTLVMALGST-SNDFNTPGvkENcifLDNPHQArrfh 151
Cdd:COG0493 182 EALGVEFRTNVEVG-----KDITLDELLEE------------FDAVFLATGAGkPRDLGIPG--ED---LKGVHSA---- 235
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072 152 qemlNLFLKySANLG-------ANGKvNIAIVGGGATGVelsaelhNAVKQLHSYGykgltneALNVTLV---------- 214
Cdd:COG0493 236 ----MDFLT-AVNLGeapdtilAVGK-RVVVIGGGNTAM-------DCARTALRLG-------AESVTIVyrrtreempa 295
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072 215 ----------EAGERILPALPPRISAAAHNELTklGVRVLTQTMVTSADEGGLHTKDGE----YIEADLMVWAAGIKA-P 279
Cdd:COG0493 296 skeeveealeEGVEFLFLVAPVEIIGDENGRVT--GLECVRMELGEPDESGRRRPVPIEgsefTLPADLVILAIGQTPdP 373
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 16129072 280 DFLKDIGGLETNRINQLVVEP-TLQTTRdPDIYAIGDCASCPR 321
Cdd:COG0493 374 SGLEEELGLELDKRGTIVVDEeTYQTSL-PGVFAGGDAVRGPS 415
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
173-359 4.54e-09

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


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 58.24  E-value: 4.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  173 IAIVGGGATGVELsAELHNAVkqlhsyGYKgltnealnVTLVEAGERILPALPPRISAAAHNELTKLGVRVLTQTMVTS- 251
Cdd:PRK05249 178 LIIYGAGVIGCEY-ASIFAAL------GVK--------VTLINTRDRLLSFLDDEISDALSYHLRDSGVTIRHNEEVEKv 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  252 -ADEGG--LHTKDGEYIEADLMVWAAG----IKAPDfLKDIgGLETNRINQLVVEPTLQTTRdPDIYAIGDCAscprpeg 324
Cdd:PRK05249 243 eGGDDGviVHLKSGKKIKADCLLYANGrtgnTDGLN-LENA-GLEADSRGQLKVNENYQTAV-PHIYAVGDVI------- 312
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 16129072  325 GFvPPRAQAAHQMATCAMNNILAQMNGKPLKNYQY 359
Cdd:PRK05249 313 GF-PSLASASMDQGRIAAQHAVGEATAHLIEDIPT 346
PRK06370 PRK06370
FAD-containing oxidoreductase;
173-316 2.32e-08

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 55.98  E-value: 2.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  173 IAIVGGGATGVELSaelhnavkqlhsYGYKGLTNEalnVTLVEAGERILPALPPRISAAAHNELTKLGVRVLTQTMVTSA 252
Cdd:PRK06370 174 LVIIGGGYIGLEFA------------QMFRRFGSE---VTVIERGPRLLPREDEDVAAAVREILEREGIDVRLNAECIRV 238
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129072  253 ----DEGGLHTK---DGEYIEADLMVWAAGiKAPDfLKDIG----GLETNRINQLVVEPTLQTTrDPDIYAIGDC 316
Cdd:PRK06370 239 erdgDGIAVGLDcngGAPEITGSHILVAVG-RVPN-TDDLGleaaGVETDARGYIKVDDQLRTT-NPGIYAAGDC 310
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
70-318 1.35e-06

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 49.73  E-value: 1.35e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  70 AHARNHGFQFQLGSVIDIDREAKTITIaelRDEKGELLVPerkiayDTLVMALGSTSNDFNTPGVKE-------NCIFLD 142
Cdd:COG0492  65 EQAERFGAEILLEEVTSVDKDDGPFRV---TTDDGTEYEA------KAVIIATGAGPRKLGLPGEEEfegrgvsYCATCD 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072 143 NPhqarrfhqemlnlFLKysanlganGKvNIAIVGGGATGVELSAElhnavkqlhsygykgLTNEALNVTLVEAGERIlp 222
Cdd:COG0492 136 GF-------------FFR--------GK-DVVVVGGGDSALEEALY---------------LTKFASKVTLIHRRDEL-- 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072 223 alpprisAAAHNELTKL----GVRVLTQTMVTSAD-EGGL------HTKDGE--YIEADLMVWAAGIKAP-DFLKDIgGL 288
Cdd:COG0492 177 -------RASKILVERLranpKIEVLWNTEVTEIEgDGRVegvtlkNVKTGEekELEVDGVFVAIGLKPNtELLKGL-GL 248
                       250       260       270
                ....*....|....*....|....*....|
gi 16129072 289 ETNRINQLVVEPTLQTTRdPDIYAIGDCAS 318
Cdd:COG0492 249 ELDEDGYIVVDEDMETSV-PGVFAAGDVRD 277
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
84-318 5.95e-06

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 48.24  E-value: 5.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072   84 VIDIDREAKTITIAELR-DEKGEllvperkIAYDTLVMalgstsndfnTPGVKENCIFLDNPH--QARRFHQ-EMLNLFL 159
Cdd:PRK13512  81 VIAINDERQTVTVLNRKtNEQFE-------ESYDKLIL----------SPGASANSLGFESDItfTLRNLEDtDAIDQFI 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  160 KysanlgANGKVNIAIVGGGATGVELSAELHNavkqlhsygykgltnEALNVTLVEAGERILPALPPRISAAAHNELTKL 239
Cdd:PRK13512 144 K------ANQVDKALVVGAGYISLEVLENLYE---------------RGLHPTLIHRSDKINKLMDADMNQPILDELDKR 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  240 GVRVLTQTMVTSADEGGLHTKDGEYIEADLMVWAAGIKA-PDFLKDiGGLETNRINQLVVEPTLQTTrDPDIYAIGDCAS 318
Cdd:PRK13512 203 EIPYRLNEEIDAINGNEVTFKSGKVEHYDMIIEGVGTHPnSKFIES-SNIKLDDKGFIPVNDKFETN-VPNIYAIGDIIT 280
PRK13748 PRK13748
putative mercuric reductase; Provisional
222-321 1.27e-05

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 47.45  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  222 PALPPRISAAAHNEltklGVRVLTQTMVTS-ADEGG---LHTKDGEyIEADLMVWAAGiKAPDFLK---DIGGLETNRIN 294
Cdd:PRK13748 310 PAIGEAVTAAFRAE----GIEVLEHTQASQvAHVDGefvLTTGHGE-LRADKLLVATG-RAPNTRSlalDAAGVTVNAQG 383
                         90       100
                 ....*....|....*....|....*..
gi 16129072  295 QLVVEPTLQTTRdPDIYAIGDCASCPR 321
Cdd:PRK13748 384 AIVIDQGMRTSV-PHIYAAGDCTDQPQ 409
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
187-327 1.45e-04

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 43.74  E-value: 1.45e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072 187 AELHNAVKQLHSYGYKgltnealnVTLVEAGE--RILPAL------------------PPRISAAAHNELTKLGVRVLTQ 246
Cdd:COG0665 100 AALRAEAEALRALGLP--------VELLDAAElrEREPGLgspdyagglydpddghvdPAKLVRALARAARAAGVRIREG 171
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072 247 TMVTSADEGG-----LHTKDGEyIEADLMVWAAGIKAPDFLKDIGG---LETNRINQLVVEP-----TLQTTRDPDIYAI 313
Cdd:COG0665 172 TPVTGLEREGgrvtgVRTERGT-VRADAVVLAAGAWSARLLPMLGLrlpLRPVRGYVLVTEPlpdlpLRPVLDDTGVYLR 250
                       170
                ....*....|....
gi 16129072 314 gdcascPRPEGGFV 327
Cdd:COG0665 251 ------PTADGRLL 258
PTZ00058 PTZ00058
glutathione reductase; Provisional
173-316 2.05e-04

glutathione reductase; Provisional


Pssm-ID: 185420 [Multi-domain]  Cd Length: 561  Bit Score: 43.45  E-value: 2.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  173 IAIVGGGATGVELSaelhNAVKQLhsygykgltneALNVTLVEAGERILPALPPRISAAAHNELTKLGVRVLTQTM---V 249
Cdd:PTZ00058 240 IGIAGSGYIAVELI----NVVNRL-----------GAESYIFARGNRLLRKFDETIINELENDMKKNNINIITHANveeI 304
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129072  250 TSADEGGLHT---KDGEYIEADLMVWAAGiKAPDfLKDIG--GLETNRINQLVVEPTLQTTRDPDIYAIGDC 316
Cdd:PTZ00058 305 EKVKEKNLTIylsDGRKYEHFDYVIYCVG-RSPN-TEDLNlkALNIKTPKGYIKVDDNQRTSVKHIYAVGDC 374
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
174-320 2.74e-04

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 42.99  E-value: 2.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  174 AIVGGGATGVELSAElhnavkqlhsygYKGLTNEalnVTLVEAGERILPALPPRISAAAHNELTKLGVRVLTQTMVTSAD 253
Cdd:PRK06327 187 AVIGAGVIGLELGSV------------WRRLGAE---VTILEALPAFLAAADEQVAKEAAKAFTKQGLDIHLGVKIGEIK 251
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129072  254 EGG------LHTKDGEY--IEADLMVWAAGIKAPdfLKDIG----GLETNRINQLVVEPTLQTTRdPDIYAIGDCASCP 320
Cdd:PRK06327 252 TGGkgvsvaYTDADGEAqtLEVDKLIVSIGRVPN--TDGLGleavGLKLDERGFIPVDDHCRTNV-PNVYAIGDVVRGP 327
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
92-321 7.55e-04

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 41.51  E-value: 7.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072   92 KTITIAELRDEKGELLVpERKI-------AYDTLVMALGS-TSNDFNTPGvkENcifLDNPHQARRFhqemlnLFLKYSA 163
Cdd:PRK12770  90 KVCCGEPLHEEEGDEFV-ERIVsleelvkKYDAVLIATGTwKSRKLGIPG--ED---LPGVYSALEY------LFRIRAA 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  164 NLG--ANGKV------NIAIVGGGATGVE--LSAELHNAVKQLHSYgyKGLTNEA------LNvTLVEAG----ERILPA 223
Cdd:PRK12770 158 KLGylPWEKVppvegkKVVVVGAGLTAVDaaLEAVLLGAEKVYLAY--RRTINEApagkyeIE-RLIARGveflELVTPV 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  224 lppRISAaahnELTKLGVRvLTQTMVTSADEGGLH----TKDGEY-IEADLMVWAAG-IKAPDFLKDIGGLETNRINQLV 297
Cdd:PRK12770 235 ---RIIG----EGRVEGVE-LAKMRLGEPDESGRPrpvpIPGSEFvLEADTVVFAIGeIPTPPFAKECLGIELNRKGEIV 306
                        250       260
                 ....*....|....*....|....
gi 16129072  298 VEPTLQTTRdPDIYAIGDCASCPR 321
Cdd:PRK12770 307 VDEKHMTSR-EGVFAAGDVVTGPS 329
PRK08010 PRK08010
pyridine nucleotide-disulfide oxidoreductase; Provisional
173-315 6.03e-03

pyridine nucleotide-disulfide oxidoreductase; Provisional


Pssm-ID: 181196 [Multi-domain]  Cd Length: 441  Bit Score: 38.84  E-value: 6.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129072  173 IAIVGGGATGVELSAELHNavkqlhsYGYKgltnealnVTLVEAGERILPALPPRISAAAHNELTKLGVRVLTQTMV--T 250
Cdd:PRK08010 161 LGILGGGYIGVEFASMFAN-------FGSK--------VTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVerI 225
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129072  251 SADEGG--LHTKDGEYIEADLMVWAAGIKAPDFLK-DIGGLETNRINQLVVEPTLQTTRDpDIYAIGD 315
Cdd:PRK08010 226 SHHENQvqVHSEHAQLAVDALLIASGRQPATASLHpENAGIAVNERGAIVVDKYLHTTAD-NIWAMGD 292
 
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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