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Conserved domains on  [gi|851901822|ref|WP_048211961|]
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MULTISPECIES: NADH-quinone dehydrogenase [Citrobacter]

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];
36-416 3.77e-150

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


:

Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 431.48  E-value: 3.77e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822  36 ITLVDRNHSHLWKPLLHEVATGSLDEGVDALSYLAHARNHGFQFQLGSVMDIDREAKTITIAElrdekgdllvpERKVPY 115
Cdd:COG1252   30 VTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRAGVRFIQGEVTGIDPEARTVTLAD-----------GRTLSY 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 116 DTLVMALGSTSNDFNTPGVKENCIFLDNPHQARRFHQEMLNLFLKYSANlganGKVNIAIVGGGATGVELSAELHNAVKQ 195
Cdd:COG1252   99 DYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAFERAERR----RLLTIVVVGGGPTGVELAGELAELLRK 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 196 LHSYgyKGLTNEALNVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTMVTSADEGGLHTKDGEYIKADLMVWAAG 275
Cdd:COG1252  175 LLRY--PGIDPDKVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDADGVTLEDGEEIPADTVIWAAG 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 276 IKAPDFMKEIGgLETNRINQLVVEPTLQTSRDPDIYAIGDCASCARPEGGFVPPRAQAAHQMASCAMNNILAQMNGKPLK 355
Cdd:COG1252  253 VKAPPLLADLG-LPTDRRGRVLVDPTLQVPGHPNVFAIGDCAAVPDPDGKPVPKTAQAAVQQAKVLAKNIAALLRGKPLK 331
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 851901822 356 AYQYKDHGSLVSLSNFSTVGSLMGnltrgsMMVEGRIARFVYISLYRMHQIALHGYFKTGL 416
Cdd:COG1252  332 PFRYRDKGCLASLGRGAAVADVGG------LKLSGFLAWLLKRAIHLYFLPGFRGRLRVLL 386
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
36-416 3.77e-150

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 431.48  E-value: 3.77e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822  36 ITLVDRNHSHLWKPLLHEVATGSLDEGVDALSYLAHARNHGFQFQLGSVMDIDREAKTITIAElrdekgdllvpERKVPY 115
Cdd:COG1252   30 VTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRAGVRFIQGEVTGIDPEARTVTLAD-----------GRTLSY 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 116 DTLVMALGSTSNDFNTPGVKENCIFLDNPHQARRFHQEMLNLFLKYSANlganGKVNIAIVGGGATGVELSAELHNAVKQ 195
Cdd:COG1252   99 DYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAFERAERR----RLLTIVVVGGGPTGVELAGELAELLRK 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 196 LHSYgyKGLTNEALNVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTMVTSADEGGLHTKDGEYIKADLMVWAAG 275
Cdd:COG1252  175 LLRY--PGIDPDKVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDADGVTLEDGEEIPADTVIWAAG 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 276 IKAPDFMKEIGgLETNRINQLVVEPTLQTSRDPDIYAIGDCASCARPEGGFVPPRAQAAHQMASCAMNNILAQMNGKPLK 355
Cdd:COG1252  253 VKAPPLLADLG-LPTDRRGRVLVDPTLQVPGHPNVFAIGDCAAVPDPDGKPVPKTAQAAVQQAKVLAKNIAALLRGKPLK 331
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 851901822 356 AYQYKDHGSLVSLSNFSTVGSLMGnltrgsMMVEGRIARFVYISLYRMHQIALHGYFKTGL 416
Cdd:COG1252  332 PFRYRDKGCLASLGRGAAVADVGG------LKLSGFLAWLLKRAIHLYFLPGFRGRLRVLL 386
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
36-338 8.81e-58

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: 191.76  E-value: 8.81e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822   36 ITLV-DRNHSHLWKPLLHEVATGSLDEGVDAL---SYLAHARNHGFQFQLG-------SVMDIDREAKTITIAELRDEKG 104
Cdd:pfam07992  26 VTLIeDEGTCPYGGCVLSKALLGAAEAPEIASlwaDLYKRKEEVVKKLNNGievllgtEVVSIDPGAKKVVLEELVDGDG 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822  105 dllvpeRKVPYDTLVMALGSTSNDFNTPGVKENCIFL-DNPHQARRFHQEMLNLflkysanlgangkvNIAIVGGGATGV 183
Cdd:pfam07992 106 ------ETITYDRLVIATGARPRLPPIPGVELNVGFLvRTLDSAEALRLKLLPK--------------RVVVVGGGYIGV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822  184 ELSAELHNAVKQlhsygykgltnealnVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTMVTSADEGG----LHT 259
Cdd:pfam07992 166 ELAAALAKLGKE---------------VTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGdgveVIL 230
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 851901822  260 KDGEYIKADLMVWAAGIKAPDFMKEIGGLETNRINQLVVEPTLQTSrDPDIYAIGDCascarpeGGFVPPRAQAAHQMA 338
Cdd:pfam07992 231 KDGTEIDADLVVVAIGRRPNTELLEAAGLELDERGGIVVDEYLRTS-VPGIYAAGDC-------RVGGPELAQNAVAQG 301
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
41-401 1.19e-44

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 160.70  E-value: 1.19e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822  41 RNHsHLWKPLLHEVATGSLdEGVDALSYLAHARNH-GFQFQLGSVMDIDREAKTITIaELRDEKGDLLVPERKVPYDTLV 119
Cdd:PTZ00318  42 RNH-MLFTPLLPQTTTGTL-EFRSICEPVRPALAKlPNRYLRAVVYDVDFEEKRVKC-GVVSKSNNANVNTFSVPYDKLV 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 120 MALGSTSNDFNTPGVKENCIFLDNPHQARRFHQEMLNLFLKysANLG------ANGKVNIAIVGGGATGVELSAELHNAV 193
Cdd:PTZ00318 119 VAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIVQCIER--ASLPttsveeRKRLLHFVVVGGGPTGVEFAAELADFF 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 194 KQLHSYGYKGLTNEAlNVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTMVTSADEGGLHTKDGEYIKADLMVWA 273
Cdd:PTZ00318 197 RDDVRNLNPELVEEC-KVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEVLDKEVVLKDGEVIPTGLVVWS 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 274 AGIKAPDFMKEIGGLETNRiNQLVVEPTLQTSRDPDIYAIGDCASCarpEGGFVPPRAQAAHQMASCAMNNILAQMNGKP 353
Cdd:PTZ00318 276 TGVGPGPLTKQLKVDKTSR-GRISVDDHLRVKPIPNVFALGDCAAN---EERPLPTLAQVASQQGVYLAKEFNNELKGKP 351
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 851901822 354 L-KAYQYKDHGSLVSLSNFSTVGSLmgnltrGSMMVEGRIARFVYISLY 401
Cdd:PTZ00318 352 MsKPFVYRSLGSLAYLGNYSAIVQL------GAFDLSGFKALLFWRSAY 394
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
50-361 7.66e-21

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


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 95.28  E-value: 7.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822   50 LLHEVATGSLDEGVDALSYLAHARNHGFQFQLG-SVMDIDREAKTITIAElrdekgdllvpERKVPYDTLVMALGSTSND 128
Cdd:TIGR02374  42 LLSSVLQGEADLDDITLNSKDWYEKHGITLYTGeTVIQIDTDQKQVITDA-----------GRTLSYDKLILATGSYPFI 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822  129 FNTPGV-KENCifldnpHQARRFH--QEMLNlflkysanlGANGKVNIAIVGGGATGVELSAELHNAVKQLHSYGYK-GL 204
Cdd:TIGR02374 111 LPIPGAdKKGV------YVFRTIEdlDAIMA---------MAQRFKKAAVIGGGLLGLEAAVGLQNLGMDVSVIHHApGL 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822  205 TNEALNvtlvEAGERILpalpprissaaHNELTKLGVRVLTQT----MVTSADEGGLHTKDGEYIKADLMVWAAGIKAPD 280
Cdd:TIGR02374 176 MAKQLD----QTAGRLL-----------QRELEQKGLTFLLEKdtveIVGATKADRIRFKDGSSLEADLIVMAAGIRPND 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822  281 FMKEIGGLETNRinQLVVEPTLQTSrDPDIYAIGDCASCARPEGGFVPPraqaAHQMASCAMNNILaqmnGKPLKAYQYK 360
Cdd:TIGR02374 241 ELAVSAGIKVNR--GIIVNDSMQTS-DPDIYAVGECAEHNGRVYGLVAP----LYEQAKVLADHIC----GVECEEYEGS 309

                  .
gi 851901822  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];
36-416 3.77e-150

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 431.48  E-value: 3.77e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822  36 ITLVDRNHSHLWKPLLHEVATGSLDEGVDALSYLAHARNHGFQFQLGSVMDIDREAKTITIAElrdekgdllvpERKVPY 115
Cdd:COG1252   30 VTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRAGVRFIQGEVTGIDPEARTVTLAD-----------GRTLSY 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 116 DTLVMALGSTSNDFNTPGVKENCIFLDNPHQARRFHQEMLNLFLKYSANlganGKVNIAIVGGGATGVELSAELHNAVKQ 195
Cdd:COG1252   99 DYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAFERAERR----RLLTIVVVGGGPTGVELAGELAELLRK 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 196 LHSYgyKGLTNEALNVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTMVTSADEGGLHTKDGEYIKADLMVWAAG 275
Cdd:COG1252  175 LLRY--PGIDPDKVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDADGVTLEDGEEIPADTVIWAAG 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 276 IKAPDFMKEIGgLETNRINQLVVEPTLQTSRDPDIYAIGDCASCARPEGGFVPPRAQAAHQMASCAMNNILAQMNGKPLK 355
Cdd:COG1252  253 VKAPPLLADLG-LPTDRRGRVLVDPTLQVPGHPNVFAIGDCAAVPDPDGKPVPKTAQAAVQQAKVLAKNIAALLRGKPLK 331
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 851901822 356 AYQYKDHGSLVSLSNFSTVGSLMGnltrgsMMVEGRIARFVYISLYRMHQIALHGYFKTGL 416
Cdd:COG1252  332 PFRYRDKGCLASLGRGAAVADVGG------LKLSGFLAWLLKRAIHLYFLPGFRGRLRVLL 386
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
36-338 8.81e-58

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: 191.76  E-value: 8.81e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822   36 ITLV-DRNHSHLWKPLLHEVATGSLDEGVDAL---SYLAHARNHGFQFQLG-------SVMDIDREAKTITIAELRDEKG 104
Cdd:pfam07992  26 VTLIeDEGTCPYGGCVLSKALLGAAEAPEIASlwaDLYKRKEEVVKKLNNGievllgtEVVSIDPGAKKVVLEELVDGDG 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822  105 dllvpeRKVPYDTLVMALGSTSNDFNTPGVKENCIFL-DNPHQARRFHQEMLNLflkysanlgangkvNIAIVGGGATGV 183
Cdd:pfam07992 106 ------ETITYDRLVIATGARPRLPPIPGVELNVGFLvRTLDSAEALRLKLLPK--------------RVVVVGGGYIGV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822  184 ELSAELHNAVKQlhsygykgltnealnVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTMVTSADEGG----LHT 259
Cdd:pfam07992 166 ELAAALAKLGKE---------------VTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGdgveVIL 230
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 851901822  260 KDGEYIKADLMVWAAGIKAPDFMKEIGGLETNRINQLVVEPTLQTSrDPDIYAIGDCascarpeGGFVPPRAQAAHQMA 338
Cdd:pfam07992 231 KDGTEIDADLVVVAIGRRPNTELLEAAGLELDERGGIVVDEYLRTS-VPGIYAAGDC-------RVGGPELAQNAVAQG 301
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
41-401 1.19e-44

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 160.70  E-value: 1.19e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822  41 RNHsHLWKPLLHEVATGSLdEGVDALSYLAHARNH-GFQFQLGSVMDIDREAKTITIaELRDEKGDLLVPERKVPYDTLV 119
Cdd:PTZ00318  42 RNH-MLFTPLLPQTTTGTL-EFRSICEPVRPALAKlPNRYLRAVVYDVDFEEKRVKC-GVVSKSNNANVNTFSVPYDKLV 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 120 MALGSTSNDFNTPGVKENCIFLDNPHQARRFHQEMLNLFLKysANLG------ANGKVNIAIVGGGATGVELSAELHNAV 193
Cdd:PTZ00318 119 VAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIVQCIER--ASLPttsveeRKRLLHFVVVGGGPTGVEFAAELADFF 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 194 KQLHSYGYKGLTNEAlNVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTMVTSADEGGLHTKDGEYIKADLMVWA 273
Cdd:PTZ00318 197 RDDVRNLNPELVEEC-KVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEVLDKEVVLKDGEVIPTGLVVWS 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 274 AGIKAPDFMKEIGGLETNRiNQLVVEPTLQTSRDPDIYAIGDCASCarpEGGFVPPRAQAAHQMASCAMNNILAQMNGKP 353
Cdd:PTZ00318 276 TGVGPGPLTKQLKVDKTSR-GRISVDDHLRVKPIPNVFALGDCAAN---EERPLPTLAQVASQQGVYLAKEFNNELKGKP 351
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 851901822 354 L-KAYQYKDHGSLVSLSNFSTVGSLmgnltrGSMMVEGRIARFVYISLY 401
Cdd:PTZ00318 352 MsKPFVYRSLGSLAYLGNYSAIVQL------GAFDLSGFKALLFWRSAY 394
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
36-355 1.75e-38

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: 141.49  E-value: 1.75e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822  36 ITLVDRNHSH------LWKPLLHEVATgsldegVDALSYLAHA--RNHGFQFQLGS-VMDIDREAKTITIAElrdekgdl 106
Cdd:COG0446    8 ITVIEKGPHHsyqpcgLPYYVGGGIKD------PEDLLVRTPEsfERKGIDVRTGTeVTAIDPEAKTVTLRD-------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 107 lvpERKVPYDTLVMALGSTSNDFNTPGVKENCIF-LDNPHQARRFHQEMLNlflkysanlgANGKvNIAIVGGGATGVEL 185
Cdd:COG0446   74 ---GETLSYDKLVLATGARPRPPPIPGLDLPGVFtLRTLDDADALREALKE----------FKGK-RAVVIGGGPIGLEL 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 186 SAELHNAvkqlhsygykGLtnealNVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTMVTSADEGG---LHTKDG 262
Cdd:COG0446  140 AEALRKR----------GL-----KVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAIDGDDkvaVTLTDG 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 263 EYIKADLMVWAAGIkAPDFmkEIG---GLETNRINQLVVEPTLQTSrDPDIYAIGDCASCARPEGG--FVPPRAQAAHQM 337
Cdd:COG0446  205 EEIPADLVVVAPGV-RPNT--ELAkdaGLALGERGWIKVDETLQTS-DPDVYAAGDCAEVPHPVTGktVYIPLASAANKQ 280
                        330
                 ....*....|....*...
gi 851901822 338 ASCAMNNILaqmnGKPLK 355
Cdd:COG0446  281 GRVAAENIL----GGPAP 294
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
48-346 1.47e-36

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 138.35  E-value: 1.47e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822  48 KPLLHEVATGSLDEGVDALSYLAHARNHGFQFQLGS-VMDIDREAKTITiaelrDEKGdllvpeRKVPYDTLVMALGSTS 126
Cdd:COG1251   42 RPPLSKVLAGETDEEDLLLRPADFYEENGIDLRLGTrVTAIDRAARTVT-----LADG------ETLPYDKLVLATGSRP 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 127 NDFNTPGV-KENCIFLDNPHQARRFHQEMlnlflkysanlgANGKvNIAIVGGGATGVELSAELHNAvkqlhsyGYKglt 205
Cdd:COG1251  111 RVPPIPGAdLPGVFTLRTLDDADALRAAL------------APGK-RVVVIGGGLIGLEAAAALRKR-------GLE--- 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 206 nealnVTLVEAGERILP-ALPPRISSAAHNELTKLGVRVLTQTMVTS--ADEG--GLHTKDGEYIKADLMVWAAGIKaP- 279
Cdd:COG1251  168 -----VTVVERAPRLLPrQLDEEAGALLQRLLEALGVEVRLGTGVTEieGDDRvtGVRLADGEELPADLVVVAIGVR-Pn 241
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 280 -DFMKEIGgLETNR-InqlVVEPTLQTSrDPDIYAIGDCASCA-RPEGGFVPPRAQAAHQMASCAMNNIL 346
Cdd:COG1251  242 tELARAAG-LAVDRgI---VVDDYLRTS-DPDIYAAGDCAEHPgPVYGRRVLELVAPAYEQARVAAANLA 306
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
84-348 2.53e-22

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 97.68  E-value: 2.53e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822  84 VMDIDREAKTITiaelrdekgdllVPERKVPYDTLVMALGSTSndFNTPGVKENCIFLDNPHQARRFHQEMLnlflkysa 163
Cdd:PRK04965  81 VTDIDAEAQVVK------------SQGNQWQYDKLVLATGASA--FVPPIPGRELMLTLNSQQEYRAAETQL-------- 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 164 nlgANGKvNIAIVGGGATGVELSAELHNAVKQlhsygykgltnealnVTLVEAGERILPAL-PPRISSAAHNELTKLGVR 242
Cdd:PRK04965 139 ---RDAQ-RVLVVGGGLIGTELAMDLCRAGKA---------------VTLVDNAASLLASLmPPEVSSRLQHRLTEMGVH 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 243 VLTQTMVTSAD--EGGLH--TKDGEYIKADLMVWAAGIKAPDFMKEIGGLETNRinQLVVEPTLQTSrDPDIYAIGDCAS 318
Cdd:PRK04965 200 LLLKSQLQGLEktDSGIRatLDSGRSIEVDAVIAAAGLRPNTALARRAGLAVNR--GIVVDSYLQTS-APDIYALGDCAE 276
                        250       260       270
                 ....*....|....*....|....*....|
gi 851901822 319 CarpeGGFVPPRAQAAHQMASCAMNNILAQ 348
Cdd:PRK04965 277 I----NGQVLPFLQPIQLSAMALAKNLLGQ 302
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
173-359 2.02e-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: 95.92  E-value: 2.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 173 IAIVGGGATGVEL-SAelhnavkqLHSYGYKgltnealnVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTMVTS 251
Cdd:COG1249  171 LVVIGGGYIGLEFaQI--------FARLGSE--------VTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTS 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 252 ADEGG----LHTKDG---EYIKADLMVWAAGIKApdFMKEIG----GLETNRINQLVVEPTLQTSrDPDIYAIGDCAsca 320
Cdd:COG1249  235 VEKTGdgvtVTLEDGggeEAVEADKVLVATGRRP--NTDGLGleaaGVELDERGGIKVDEYLRTS-VPGIYAIGDVT--- 308
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 851901822 321 rpeGGfvPPRAQAAHQMASCAMNNILaqmnGKPLKAYQY 359
Cdd:COG1249  309 ---GG--PQLAHVASAEGRVAAENIL----GKKPRPVDY 338
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
50-361 7.66e-21

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


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 95.28  E-value: 7.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822   50 LLHEVATGSLDEGVDALSYLAHARNHGFQFQLG-SVMDIDREAKTITIAElrdekgdllvpERKVPYDTLVMALGSTSND 128
Cdd:TIGR02374  42 LLSSVLQGEADLDDITLNSKDWYEKHGITLYTGeTVIQIDTDQKQVITDA-----------GRTLSYDKLILATGSYPFI 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822  129 FNTPGV-KENCifldnpHQARRFH--QEMLNlflkysanlGANGKVNIAIVGGGATGVELSAELHNAVKQLHSYGYK-GL 204
Cdd:TIGR02374 111 LPIPGAdKKGV------YVFRTIEdlDAIMA---------MAQRFKKAAVIGGGLLGLEAAVGLQNLGMDVSVIHHApGL 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822  205 TNEALNvtlvEAGERILpalpprissaaHNELTKLGVRVLTQT----MVTSADEGGLHTKDGEYIKADLMVWAAGIKAPD 280
Cdd:TIGR02374 176 MAKQLD----QTAGRLL-----------QRELEQKGLTFLLEKdtveIVGATKADRIRFKDGSSLEADLIVMAAGIRPND 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822  281 FMKEIGGLETNRinQLVVEPTLQTSrDPDIYAIGDCASCARPEGGFVPPraqaAHQMASCAMNNILaqmnGKPLKAYQYK 360
Cdd:TIGR02374 241 ELAVSAGIKVNR--GIIVNDSMQTS-DPDIYAVGECAEHNGRVYGLVAP----LYEQAKVLADHIC----GVECEEYEGS 309

                  .
gi 851901822  361 D 361
Cdd:TIGR02374 310 D 310
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
172-360 3.27e-18

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: 86.54  E-value: 3.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822  172 NIAIVGGGATGVELSAelhnavkQLHSYGYKgltnealnVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTMVT- 250
Cdd:TIGR01350 172 SLVIIGGGVIGIEFAS-------IFASLGSK--------VTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTa 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822  251 -SADEGGLHTK----DGEYIKADLMVWAAGIKaPDFmKEIG----GLETNRINQLVVEPTLQTSrDPDIYAIGDCAscar 321
Cdd:TIGR01350 237 vEKNDDQVTYEnkggETETLTGEKVLVAVGRK-PNT-EGLGleklGVELDERGRIVVDEYMRTN-VPGIYAIGDVI---- 309
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 851901822  322 peGGfvPPRAQAAHQMASCAMNNILaqmnGKPLKAYQYK 360
Cdd:TIGR01350 310 --GG--PMLAHVASHEGIVAAENIA----GKEPAHIDYD 340
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
84-318 3.41e-16

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 80.08  E-value: 3.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822  84 VMDIDREAKTITIAELRDEKgdllvpERKVPYDTLVMALGSTSNdfnTPGVKEncIFLDNPHQARRFH--QEMLNLFLKY 161
Cdd:PRK09564  79 VVKVDAKNKTITVKNLKTGS------IFNDTYDKLMIATGARPI---IPPIKN--INLENVYTLKSMEdgLALKELLKDE 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 162 SanlgangKVNIAIVGGGATGVELSAELHNAVKqlhsygykgltnealNVTLVEAGERILP-ALPPRISSAAHNELTKLG 240
Cdd:PRK09564 148 E-------IKNIVIIGAGFIGLEAVEAAKHLGK---------------NVRIIQLEDRILPdSFDKEITDVMEEELRENG 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 241 VRVLTQTMVTSAD-EG---GLHTKDGEYiKADLMVWAAGIK-APDFMKEiGGLETNRINQLVVEPTLQTSrDPDIYAIGD 315
Cdd:PRK09564 206 VELHLNEFVKSLIgEDkveGVVTDKGEY-EADVVIVATGVKpNTEFLED-TGLKTLKNGAIIVDEYGETS-IENIYAAGD 282

                 ...
gi 851901822 316 CAS 318
Cdd:PRK09564 283 CAT 285
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
173-315 3.21e-14

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 74.03  E-value: 3.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 173 IAIVGGGATGVEL-SAelhnavkqlhsygYKGLTNEalnVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTMVTS 251
Cdd:PRK06416 175 LVVIGGGYIGVEFaSA-------------YASLGAE---VTIVEALPRILPGEDKEISKLAERALKKRGIKIKTGAKAKK 238
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 851901822 252 ADEGG----LHTKDG---EYIKADLMVWAAGIkAPDfMKEIG----GLETNRiNQLVVEPTLQTSrDPDIYAIGD 315
Cdd:PRK06416 239 VEQTDdgvtVTLEDGgkeETLEADYVLVAVGR-RPN-TENLGleelGVKTDR-GFIEVDEQLRTN-VPNIYAIGD 309
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
173-316 1.57e-12

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 69.05  E-value: 1.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 173 IAIVGGGATGVEL-SAelhnavkqLHSYGYKgltnealnVTLVEAGERILPALPPRISSAAHNELTKlGVRVLTQTMVTS 251
Cdd:PRK06292 172 LAVIGGGVIGLELgQA--------LSRLGVK--------VTVFERGDRILPLEDPEVSKQAQKILSK-EFKIKLGAKVTS 234
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 851901822 252 ADEGG-----LHTKDGE--YIKADLMVWAAGIKA--PDFMKEIGGLETNRINQLVVEPTLQTSrDPDIYAIGDC 316
Cdd:PRK06292 235 VEKSGdekveELEKGGKteTIEADYVLVATGRRPntDGLGLENTGIELDERGRPVVDEHTQTS-VPGIYAAGDV 307
PRK14989 PRK14989
nitrite reductase subunit NirD; Provisional
75-350 3.80e-12

nitrite reductase subunit NirD; Provisional


Pssm-ID: 184951 [Multi-domain]  Cd Length: 847  Bit Score: 68.22  E-value: 3.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822  75 HGFQFQLGS-VMDIDREAKTItiaelRDEKGdllvpeRKVPYDTLVMALGSTSNdfnTPGVKenciflDNPHQARRFHQE 153
Cdd:PRK14989  72 HGIKVLVGErAITINRQEKVI-----HSSAG------RTVFYDKLIMATGSYPW---IPPIK------GSETQDCFVYRT 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 154 MLNL-FLKYSANLGANGkvniAIVGGGATGVELSAelhnAVKQLhsygykGLTNEALNVTLVEAGERilpaLPPRISSAA 232
Cdd:PRK14989 132 IEDLnAIEACARRSKRG----AVVGGGLLGLEAAG----ALKNL------GVETHVIEFAPMLMAEQ----LDQMGGEQL 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 233 HNELTKLGVRVLT----QTMVTSADEGG--LHTKDGEYIKADLMVWAAGIKAPDFMKEIGGLETNRINQLVVEPTLQTSr 306
Cdd:PRK14989 194 RRKIESMGVRVHTskntLEIVQEGVEARktMRFADGSELEVDFIVFSTGIRPQDKLATQCGLAVAPRGGIVINDSCQTS- 272
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 851901822 307 DPDIYAIGDCASCARPEGGFVPPraqaAHQMASCAMNNILAQMN 350
Cdd:PRK14989 273 DPDIYAIGECASWNNRVFGLVAP----GYKMAQVAVDHLLGSEN 312
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
172-256 1.09e-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: 60.30  E-value: 1.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822  172 NIAIVGGGATGVELSAELHNavkqlhsYGYKgltnealnVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTMVTS 251
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALAR-------LGSK--------VTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEA 65

                  ....*
gi 851901822  252 ADEGG 256
Cdd:pfam00070  66 IEGNG 70
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
99-324 3.06e-11

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 64.56  E-value: 3.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822  99 LRDEKGDLLVPERKVPYDTLVMALGSTSNDFNT-PGVKENCIFLDNPHQARRFHQEMlnlflkysanlgANGKvNIAIVG 177
Cdd:PRK09754  85 GRDTRELVLTNGESWHWDQLFIATGAAARPLPLlDALGERCFTLRHAGDAARLREVL------------QPER-SVVIVG 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 178 GGATGVELSAElhnavkqlhsygykgLTNEALNVTLVEAGERIL-PALPPRISSAAHNELTKLGVRVLTQTMVTSADEGG 256
Cdd:PRK09754 152 AGTIGLELAAS---------------ATQRRCKVTVIELAATVMgRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGE 216
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 851901822 257 ---LHTKDGEYIKADLMVWAAGIKAPDFMKEIGGLETNriNQLVVEPTLQTSrDPDIYAIGDCASCARPEG 324
Cdd:PRK09754 217 kveLTLQSGETLQADVVIYGIGISANDQLAREANLDTA--NGIVIDEACRTC-DPAIFAGGDVAITRLDNG 284
MerA TIGR02053
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ...
173-316 7.58e-11

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: 63.60  E-value: 7.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822  173 IAIVGGGATGVELSAELHNAvkqlhsygykgltneALNVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTMVT-- 250
Cdd:TIGR02053 169 LAVIGGGAIGVELAQAFARL---------------GSEVTILQRSDRLLPREEPEISAAVEEALAEEGIEVVTSAQVKav 233
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 851901822  251 SADEGG----LHTKDGEY-IKADLMVWAAGiKAPDFMK---EIGGLETNRINQLVVEPTLQTSrDPDIYAIGDC 316
Cdd:TIGR02053 234 SVRGGGkiitVEKPGGQGeVEADELLVATG-RRPNTDGlglEKAGVKLDERGGILVDETLRTS-NPGIYAAGDV 305
PRK06116 PRK06116
glutathione reductase; Validated
173-316 8.27e-10

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 60.56  E-value: 8.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 173 IAIVGGGATGVELSAELHnavkqlhsygykGLTNEalnVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTMVTS- 251
Cdd:PRK06116 170 VAVVGAGYIAVEFAGVLN------------GLGSE---THLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAv 234
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 851901822 252 --ADEGGL--HTKDGEYIKADLMVWAAGiKAP---DFMKEIGGLETNRINQLVVEPTLQTSrDPDIYAIGDC 316
Cdd:PRK06116 235 ekNADGSLtlTLEDGETLTVDCLIWAIG-REPntdGLGLENAGVKLNEKGYIIVDEYQNTN-VPGIYAVGDV 304
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
173-353 2.14e-09

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


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 59.01  E-value: 2.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 173 IAIVGGGATGVElsaelhnavkqlhsY-------GYKgltnealnVTLVEAGERILPALPPRISSAAHNELTKLGVRVLT 245
Cdd:PRK05249 178 LIIYGAGVIGCE--------------YasifaalGVK--------VTLINTRDRLLSFLDDEISDALSYHLRDSGVTIRH 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 246 QTMVTS--ADEGG--LHTKDGEYIKADLMVWAAG-IKAPDFMK-EIGGLETNRINQLVVEPTLQTSRdPDIYAIGDCAsc 319
Cdd:PRK05249 236 NEEVEKveGGDDGviVHLKSGKKIKADCLLYANGrTGNTDGLNlENAGLEADSRGQLKVNENYQTAV-PHIYAVGDVI-- 312
                        170       180       190
                 ....*....|....*....|....*....|....
gi 851901822 320 arpegGFvPPRAQAAHQMASCAMNNILAQMNGKP 353
Cdd:PRK05249 313 -----GF-PSLASASMDQGRIAAQHAVGEATAHL 340
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
73-318 3.46e-09

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: 58.61  E-value: 3.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822  73 RNHGFQFQLGSVMDidreaKTITIAELRDEkgdllvperkvpYDTLVMALGST-SNDFNTPGvkENcifLDNPHQArrfh 151
Cdd:COG0493  182 EALGVEFRTNVEVG-----KDITLDELLEE------------FDAVFLATGAGkPRDLGIPG--ED---LKGVHSA---- 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 152 qemlNLFLKySANLG-------ANGKvNIAIVGGGATGVelsaelhNAVKQLHSYGykgltneALNVTLVE-AGERILPA 223
Cdd:COG0493  236 ----MDFLT-AVNLGeapdtilAVGK-RVVVIGGGNTAM-------DCARTALRLG-------AESVTIVYrRTREEMPA 295
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 224 LPPRISSaAHNEltklGVRVLTQTMVTS--ADEGG----LHT---------KDG-----------EYIKADLMVWAAGIK 277
Cdd:COG0493  296 SKEEVEE-ALEE----GVEFLFLVAPVEiiGDENGrvtgLECvrmelgepdESGrrrpvpiegseFTLPADLVILAIGQT 370
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 851901822 278 A-PDFMKEIGGLETNRINQLVVEP-TLQTSRdPDIYAIGDCAS 318
Cdd:COG0493  371 PdPSGLEEELGLELDKRGTIVVDEeTYQTSL-PGVFAGGDAVR 412
PRK06370 PRK06370
FAD-containing oxidoreductase;
173-316 2.35e-07

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 52.90  E-value: 2.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 173 IAIVGGGATGVELSaelhnavkqlhsYGYKGLTNEalnVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTMVTSA 252
Cdd:PRK06370 174 LVIIGGGYIGLEFA------------QMFRRFGSE---VTVIERGPRLLPREDEDVAAAVREILEREGIDVRLNAECIRV 238
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 851901822 253 ----DEGGLHTK---DGEYIKADLMVWAAGiKAP---DFMKEIGGLETNRINQLVVEPTLQTSrDPDIYAIGDC 316
Cdd:PRK06370 239 erdgDGIAVGLDcngGAPEITGSHILVAVG-RVPntdDLGLEAAGVETDARGYIKVDDQLRTT-NPGIYAAGDC 310
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
70-318 1.35e-05

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 46.65  E-value: 1.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822  70 AHARNHGFQFQLGSVMDIDREAKTITIaelRDEKGDLLVPerkvpyDTLVMALGSTSNDFNTPGVKE-------NCIFLD 142
Cdd:COG0492   65 EQAERFGAEILLEEVTSVDKDDGPFRV---TTDDGTEYEA------KAVIIATGAGPRKLGLPGEEEfegrgvsYCATCD 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 143 NPhqarrfhqemlnlFLKysanlganGKvNIAIVGGGATGVELSAElhnavkqlhsygykgLTNEALNVTLVEAGERIlp 222
Cdd:COG0492  136 GF-------------FFR--------GK-DVVVVGGGDSALEEALY---------------LTKFASKVTLIHRRDEL-- 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 223 alpprisSAAHNELTKL----GVRVLTQTMVTSAD-EGGL------HTKDGE--YIKADLMVWAAGIKAP-DFMKEIgGL 288
Cdd:COG0492  177 -------RASKILVERLranpKIEVLWNTEVTEIEgDGRVegvtlkNVKTGEekELEVDGVFVAIGLKPNtELLKGL-GL 248
                        250       260       270
                 ....*....|....*....|....*....|
gi 851901822 289 ETNRINQLVVEPTLQTSRdPDIYAIGDCAS 318
Cdd:COG0492  249 ELDEDGYIVVDEDMETSV-PGVFAAGDVRD 277
PRK13748 PRK13748
putative mercuric reductase; Provisional
222-316 2.02e-05

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 46.68  E-value: 2.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 222 PALPPRISSAAHNEltklGVRVLTQTMVTS-ADEGG---LHTKDGEyIKADLMVWAAGiKAPDFMK---EIGGLETNRIN 294
Cdd:PRK13748 310 PAIGEAVTAAFRAE----GIEVLEHTQASQvAHVDGefvLTTGHGE-LRADKLLVATG-RAPNTRSlalDAAGVTVNAQG 383
                         90       100
                 ....*....|....*....|..
gi 851901822 295 QLVVEPTLQTSRdPDIYAIGDC 316
Cdd:PRK13748 384 AIVIDQGMRTSV-PHIYAAGDC 404
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
84-318 2.34e-05

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 46.31  E-value: 2.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822  84 VMDIDREAKTITIaelRDEKGDLLVPERkvpYDTLVMalgstsndfnTPGVKENCIFLDNPH--QARRFHQ-EMLNLFLK 160
Cdd:PRK13512  81 VIAINDERQTVTV---LNRKTNEQFEES---YDKLIL----------SPGASANSLGFESDItfTLRNLEDtDAIDQFIK 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 161 ysanlgANGKVNIAIVGGGATGVELSAELHNavkqlhsygykgltnEALNVTLVEAGERILPALPPRISSAAHNELTKLG 240
Cdd:PRK13512 145 ------ANQVDKALVVGAGYISLEVLENLYE---------------RGLHPTLIHRSDKINKLMDADMNQPILDELDKRE 203
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 851901822 241 VRVLTQTMVTSADEGGLHTKDGEYIKADLMVWAAGIKAPDFMKEIGGLETNRINQLVVEPTLQTSrDPDIYAIGDCAS 318
Cdd:PRK13512 204 IPYRLNEEIDAINGNEVTFKSGKVEHYDMIIEGVGTHPNSKFIESSNIKLDDKGFIPVNDKFETN-VPNIYAIGDIIT 280
PTZ00058 PTZ00058
glutathione reductase; Provisional
173-316 8.73e-04

glutathione reductase; Provisional


Pssm-ID: 185420 [Multi-domain]  Cd Length: 561  Bit Score: 41.52  E-value: 8.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 173 IAIVGGGATGVELSaelhNAVKQLhsygykgltneALNVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTM---V 249
Cdd:PTZ00058 240 IGIAGSGYIAVELI----NVVNRL-----------GAESYIFARGNRLLRKFDETIINELENDMKKNNINIITHANveeI 304
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 851901822 250 TSADEGGLHT---KDGEYIKADLMVWAAGiKAPDfMKEIGGLETNRINQ---LVVEPTLQTSRdPDIYAIGDC 316
Cdd:PTZ00058 305 EKVKEKNLTIylsDGRKYEHFDYVIYCVG-RSPN-TEDLNLKALNIKTPkgyIKVDDNQRTSV-KHIYAVGDC 374
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
174-318 1.40e-03

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 40.68  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 174 AIVGGGATGVELSAElhnavkqlhsygYKGLTNEalnVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTMVTSAD 253
Cdd:PRK06327 187 AVIGAGVIGLELGSV------------WRRLGAE---VTILEALPAFLAAADEQVAKEAAKAFTKQGLDIHLGVKIGEIK 251
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 851901822 254 EGG------LHTKDGEY--IKADLMVWAAGIKA--PDFMKEIGGLETNRINQLVVEPTLQTSRdPDIYAIGDCAS 318
Cdd:PRK06327 252 TGGkgvsvaYTDADGEAqtLEVDKLIVSIGRVPntDGLGLEAVGLKLDERGFIPVDDHCRTNV-PNVYAIGDVVR 325
PRK08010 PRK08010
pyridine nucleotide-disulfide oxidoreductase; Provisional
173-315 3.54e-03

pyridine nucleotide-disulfide oxidoreductase; Provisional


Pssm-ID: 181196 [Multi-domain]  Cd Length: 441  Bit Score: 39.61  E-value: 3.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901822 173 IAIVGGGATGVELSAELHNavkqlhsYGYKgltnealnVTLVEAGERILPALPPRISSAAHNELTKLGVRVLTQTMV--T 250
Cdd:PRK08010 161 LGILGGGYIGVEFASMFAN-------FGSK--------VTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVerI 225
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 851901822 251 SADEGG--LHTKDGEYIkADLMVWAAGIK--APDFMKEIGGLETNRINQLVVEPTLQTSRDpDIYAIGD 315
Cdd:PRK08010 226 SHHENQvqVHSEHAQLA-VDALLIASGRQpaTASLHPENAGIAVNERGAIVVDKYLHTTAD-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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