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Conserved domains on  [gi|500021004|ref|WP_011701722|]
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glutathione-disulfide reductase [Listeria welshimeri]

Protein Classification

glutathione-disulfide reductase( domain architecture ID 11482057)

glutathione-disulfide reductase catalyzes the reduction of glutathione disulfide (GSSG) to form two molecules of glutathione (GSH); functions in the maintenance of high levels of reduced glutathione in the cytosol

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK06116 PRK06116
glutathione reductase; Validated
1-449 0e+00

glutathione reductase; Validated


:

Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 833.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004   1 MEKHYDYIAIGGGSGGIASINRAAMHGAKCALIEPKFLGGTCVNVGCVPKKVMWYGAQIKEAMDLYADAYGYQVD-ASFN 79
Cdd:PRK06116   1 MTKDYDLIVIGGGSGGIASANRAAMYGAKVALIEAKRLGGTCVNVGCVPKKLMWYGAQIAEAFHDYAPGYGFDVTeNKFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  80 FQKLVENREAYIERIRGSYKNGLDNNKVEWIKGYAEFVDEKTLRVNGEIVTADHILIATGGEPVLPSIPGAEYGITSDGF 159
Cdd:PRK06116  81 WAKLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNGERYTADHILIATGGRPSIPDIPGAEYGITSDGF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 160 FALKELPKKVAVIGAGYIAVELAGVLQQLGSETHLFVRKHAPLRNFDPLLTDTLTEIIEQSDMMLHKHAVPQKVEKNSDG 239
Cdd:PRK06116 161 FALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 240 SLTLSLEDGRTETVDTIIWAIGRKPVITGLQIEKAGVELLESGHIAVDKFQNTNVEGIYAVGDVTGHYELTPVAIAAGRR 319
Cdd:PRK06116 241 SLTLTLEDGETLTVDCLIWAIGREPNTDGLGLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGDVTGRVELTPVAIAAGRR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 320 LSERLFNNKKDAHLSYENIPTVVFSHPAIGTVGLTEPEAIEKYGKENIKIYTSSFTSMYTAITDHREPCRMKLICEGNTE 399
Cdd:PRK06116 321 LSERLFNNKPDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVKVYRSSFTPMYTALTGHRQPCLMKLVVVGKEE 400
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 500021004 400 RVIGLHGIGYGVDEMIQGFAVAINMGATKSDFDNTVAIHPTGSEEFVTMK 449
Cdd:PRK06116 401 KVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFVTMR 450
 
Name Accession Description Interval E-value
PRK06116 PRK06116
glutathione reductase; Validated
1-449 0e+00

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 833.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004   1 MEKHYDYIAIGGGSGGIASINRAAMHGAKCALIEPKFLGGTCVNVGCVPKKVMWYGAQIKEAMDLYADAYGYQVD-ASFN 79
Cdd:PRK06116   1 MTKDYDLIVIGGGSGGIASANRAAMYGAKVALIEAKRLGGTCVNVGCVPKKLMWYGAQIAEAFHDYAPGYGFDVTeNKFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  80 FQKLVENREAYIERIRGSYKNGLDNNKVEWIKGYAEFVDEKTLRVNGEIVTADHILIATGGEPVLPSIPGAEYGITSDGF 159
Cdd:PRK06116  81 WAKLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNGERYTADHILIATGGRPSIPDIPGAEYGITSDGF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 160 FALKELPKKVAVIGAGYIAVELAGVLQQLGSETHLFVRKHAPLRNFDPLLTDTLTEIIEQSDMMLHKHAVPQKVEKNSDG 239
Cdd:PRK06116 161 FALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 240 SLTLSLEDGRTETVDTIIWAIGRKPVITGLQIEKAGVELLESGHIAVDKFQNTNVEGIYAVGDVTGHYELTPVAIAAGRR 319
Cdd:PRK06116 241 SLTLTLEDGETLTVDCLIWAIGREPNTDGLGLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGDVTGRVELTPVAIAAGRR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 320 LSERLFNNKKDAHLSYENIPTVVFSHPAIGTVGLTEPEAIEKYGKENIKIYTSSFTSMYTAITDHREPCRMKLICEGNTE 399
Cdd:PRK06116 321 LSERLFNNKPDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVKVYRSSFTPMYTALTGHRQPCLMKLVVVGKEE 400
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 500021004 400 RVIGLHGIGYGVDEMIQGFAVAINMGATKSDFDNTVAIHPTGSEEFVTMK 449
Cdd:PRK06116 401 KVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFVTMR 450
gluta_reduc_1 TIGR01421
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ...
3-449 0e+00

glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important reductant, e.g., for maintaining the cellular thiol/disulfide status and for protecting against reactive oxygen species such as hydrogen peroxide. Glutathione-disulfide reductase regenerates reduced glutathione from oxidized glutathione (glutathione disulfide) + NADPH. This model represents one of two closely related subfamilies of glutathione-disulfide reductase. Both are closely related to trypanothione reductase, and separate models are built so each of the three can describe proteins with conserved function. This model describes glutathione-disulfide reductases of animals, yeast, and a number of animal-resident bacteria. [Energy metabolism, Electron transport]


Pssm-ID: 273614 [Multi-domain]  Cd Length: 450  Bit Score: 654.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004    3 KHYDYIAIGGGSGGIASINRAAMHGAKCALIEPKFLGGTCVNVGCVPKKVMWYGAQIKEAMDLYADaYGYQVDA--SFNF 80
Cdd:TIGR01421   1 KHYDYLVIGGGSGGIASARRAAEHGAKALLVEAKKLGGTCVNVGCVPKKVMWYASDLAERMHDAAD-YGFYQNDenTFNW 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004   81 QKLVENREAYIERIRGSYKNGLDNNKVEWIKGYAEFVDEKTLRVNGEIVTADHILIATGGEPVLPS-IPGAEYGITSDGF 159
Cdd:TIGR01421  80 PELKEKRDAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVNGRDYTAPHILIATGGKPSFPEnIPGAELGTDSDGF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  160 FALKELPKKVAVIGAGYIAVELAGVLQQLGSETHLFVRKHAPLRNFDPLLTDTLTEIIEQSDMMLHKHAVPQKVEKNSDG 239
Cdd:TIGR01421 160 FALEELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRHERVLRSFDSMISETITEEYEKEGINVHKLSKPVKVEKTVEG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  240 SLTLSLEDGRT-ETVDTIIWAIGRKPVITGLQIEKAGVELLESGHIAVDKFQNTNVEGIYAVGDVTGHYELTPVAIAAGR 318
Cdd:TIGR01421 240 KLVIHFEDGKSiDDVDELIWAIGRKPNTKGLGLENVGIKLNEKGQIIVDEYQNTNVPGIYALGDVVGKVELTPVAIAAGR 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  319 RLSERLFNNKKDAHLSYENIPTVVFSHPAIGTVGLTEPEAIEKYGKENIKIYTSSFTSMYTAITDHREPCRMKLICEGNT 398
Cdd:TIGR01421 320 KLSERLFNGKTDDKLDYNNVPTVVFSHPPIGTIGLTEKEAIEKYGKENIKVYNSSFTPMYYAMTSEKQKCRMKLVCAGKE 399
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 500021004  399 ERVIGLHGIGYGVDEMIQGFAVAINMGATKSDFDNTVAIHPTGSEEFVTMK 449
Cdd:TIGR01421 400 EKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEELVTMR 450
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
22-448 2.37e-172

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: 491.14  E-value: 2.37e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  22 RAAMHGAKCALIEPKFLGGTCVNVGCVPKKVMWYGAQIKEAMDlYADAYGYQV-DASFNFQKLVENREAYIERIRGSYKN 100
Cdd:COG1249   21 RAAQLGLKVALVEKGRLGGTCLNVGCIPSKALLHAAEVAHEAR-HAAEFGISAgAPSVDWAALMARKDKVVDRLRGGVEE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 101 GLDNNKVEWIKGYAEFVDEKTLRVNG-EIVTADHILIATGGEPVLPSIPGA--EYGITSDGFFALKELPKKVAVIGAGYI 177
Cdd:COG1249  100 LLKKNGVDVIRGRARFVDPHTVEVTGgETLTADHIVIATGSRPRVPPIPGLdeVRVLTSDEALELEELPKSLVVIGGGYI 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 178 AVELAGVLQQLGSETHLFVRKHAPLRNFDPLLTDTLTEIIEQSDMMLHKHAVPQKVEKNSDGsLTLSLEDGRTET---VD 254
Cdd:COG1249  180 GLEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDG-VTVTLEDGGGEEaveAD 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 255 TIIWAIGRKPVITGLQIEKAGVELLESGHIAVDKFQNTNVEGIYAVGDVTGHYELTPVAIAAGRRLSERLFNNKKdAHLS 334
Cdd:COG1249  259 KVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRTSVPGIYAIGDVTGGPQLAHVASAEGRVAAENILGKKP-RPVD 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 335 YENIPTVVFSHPAIGTVGLTEPEAIEKygKENIKIYTSSFTSMYTAITDHREPCRMKLICEGNTERVIGLHGIGYGVDEM 414
Cdd:COG1249  338 YRAIPSVVFTDPEIASVGLTEEEAREA--GIDVKVGKFPFAANGRALALGETEGFVKLIADAETGRILGAHIVGPHAGEL 415
                        410       420       430
                 ....*....|....*....|....*....|....
gi 500021004 415 IQGFAVAINMGATKSDFDNTVAIHPTGSEEFVTM 448
Cdd:COG1249  416 IHEAALAMEMGLTVEDLADTIHAHPTLSEALKEA 449
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
22-317 2.11e-70

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: 224.89  E-value: 2.11e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004   22 RAAMHGAKCALIEpkfLGGTCVNVGCVPKKVMWYGAQIKEAMdlyadaygyqvdasFNFQKLVENREAYIERIRGSYKNG 101
Cdd:pfam07992  18 TLAQLGGKVTLIE---DEGTCPYGGCVLSKALLGAAEAPEIA--------------SLWADLYKRKEEVVKKLNNGIEVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  102 LDNNKVEWIKGYAEFVDEKTLRVNGEIVTADHILIATGGEPVLPSIPGAEYG-------ITSDGFFALKELPKKVAVIGA 174
Cdd:pfam07992  81 LGTEVVSIDPGAKKVVLEELVDGDGETITYDRLVIATGARPRLPPIPGVELNvgflvrtLDSAEALRLKLLPKRVVVVGG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  175 GYIAVELAGVLQQLGSETHLFVRKHAPLRNFDPLLTDTLTEIIEQSDMMLHKHAVPQKVEKNSDGsLTLSLEDGRTETVD 254
Cdd:pfam07992 161 GYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDG-VEVILKDGTEIDAD 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500021004  255 TIIWAIGRKPVITGLqiEKAGVELLESGHIAVDKFQNTNVEGIYAVGDVT-GHYELTPVAIAAG 317
Cdd:pfam07992 240 LVVVAIGRRPNTELL--EAAGLELDERGGIVVDEYLRTSVPGIYAAGDCRvGGPELAQNAVAQG 301
 
Name Accession Description Interval E-value
PRK06116 PRK06116
glutathione reductase; Validated
1-449 0e+00

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 833.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004   1 MEKHYDYIAIGGGSGGIASINRAAMHGAKCALIEPKFLGGTCVNVGCVPKKVMWYGAQIKEAMDLYADAYGYQVD-ASFN 79
Cdd:PRK06116   1 MTKDYDLIVIGGGSGGIASANRAAMYGAKVALIEAKRLGGTCVNVGCVPKKLMWYGAQIAEAFHDYAPGYGFDVTeNKFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  80 FQKLVENREAYIERIRGSYKNGLDNNKVEWIKGYAEFVDEKTLRVNGEIVTADHILIATGGEPVLPSIPGAEYGITSDGF 159
Cdd:PRK06116  81 WAKLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNGERYTADHILIATGGRPSIPDIPGAEYGITSDGF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 160 FALKELPKKVAVIGAGYIAVELAGVLQQLGSETHLFVRKHAPLRNFDPLLTDTLTEIIEQSDMMLHKHAVPQKVEKNSDG 239
Cdd:PRK06116 161 FALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 240 SLTLSLEDGRTETVDTIIWAIGRKPVITGLQIEKAGVELLESGHIAVDKFQNTNVEGIYAVGDVTGHYELTPVAIAAGRR 319
Cdd:PRK06116 241 SLTLTLEDGETLTVDCLIWAIGREPNTDGLGLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGDVTGRVELTPVAIAAGRR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 320 LSERLFNNKKDAHLSYENIPTVVFSHPAIGTVGLTEPEAIEKYGKENIKIYTSSFTSMYTAITDHREPCRMKLICEGNTE 399
Cdd:PRK06116 321 LSERLFNNKPDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVKVYRSSFTPMYTALTGHRQPCLMKLVVVGKEE 400
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 500021004 400 RVIGLHGIGYGVDEMIQGFAVAINMGATKSDFDNTVAIHPTGSEEFVTMK 449
Cdd:PRK06116 401 KVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFVTMR 450
gluta_reduc_1 TIGR01421
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ...
3-449 0e+00

glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important reductant, e.g., for maintaining the cellular thiol/disulfide status and for protecting against reactive oxygen species such as hydrogen peroxide. Glutathione-disulfide reductase regenerates reduced glutathione from oxidized glutathione (glutathione disulfide) + NADPH. This model represents one of two closely related subfamilies of glutathione-disulfide reductase. Both are closely related to trypanothione reductase, and separate models are built so each of the three can describe proteins with conserved function. This model describes glutathione-disulfide reductases of animals, yeast, and a number of animal-resident bacteria. [Energy metabolism, Electron transport]


Pssm-ID: 273614 [Multi-domain]  Cd Length: 450  Bit Score: 654.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004    3 KHYDYIAIGGGSGGIASINRAAMHGAKCALIEPKFLGGTCVNVGCVPKKVMWYGAQIKEAMDLYADaYGYQVDA--SFNF 80
Cdd:TIGR01421   1 KHYDYLVIGGGSGGIASARRAAEHGAKALLVEAKKLGGTCVNVGCVPKKVMWYASDLAERMHDAAD-YGFYQNDenTFNW 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004   81 QKLVENREAYIERIRGSYKNGLDNNKVEWIKGYAEFVDEKTLRVNGEIVTADHILIATGGEPVLPS-IPGAEYGITSDGF 159
Cdd:TIGR01421  80 PELKEKRDAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVNGRDYTAPHILIATGGKPSFPEnIPGAELGTDSDGF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  160 FALKELPKKVAVIGAGYIAVELAGVLQQLGSETHLFVRKHAPLRNFDPLLTDTLTEIIEQSDMMLHKHAVPQKVEKNSDG 239
Cdd:TIGR01421 160 FALEELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRHERVLRSFDSMISETITEEYEKEGINVHKLSKPVKVEKTVEG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  240 SLTLSLEDGRT-ETVDTIIWAIGRKPVITGLQIEKAGVELLESGHIAVDKFQNTNVEGIYAVGDVTGHYELTPVAIAAGR 318
Cdd:TIGR01421 240 KLVIHFEDGKSiDDVDELIWAIGRKPNTKGLGLENVGIKLNEKGQIIVDEYQNTNVPGIYALGDVVGKVELTPVAIAAGR 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  319 RLSERLFNNKKDAHLSYENIPTVVFSHPAIGTVGLTEPEAIEKYGKENIKIYTSSFTSMYTAITDHREPCRMKLICEGNT 398
Cdd:TIGR01421 320 KLSERLFNGKTDDKLDYNNVPTVVFSHPPIGTIGLTEKEAIEKYGKENIKVYNSSFTPMYYAMTSEKQKCRMKLVCAGKE 399
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 500021004  399 ERVIGLHGIGYGVDEMIQGFAVAINMGATKSDFDNTVAIHPTGSEEFVTMK 449
Cdd:TIGR01421 400 EKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEELVTMR 450
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
22-448 2.37e-172

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: 491.14  E-value: 2.37e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  22 RAAMHGAKCALIEPKFLGGTCVNVGCVPKKVMWYGAQIKEAMDlYADAYGYQV-DASFNFQKLVENREAYIERIRGSYKN 100
Cdd:COG1249   21 RAAQLGLKVALVEKGRLGGTCLNVGCIPSKALLHAAEVAHEAR-HAAEFGISAgAPSVDWAALMARKDKVVDRLRGGVEE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 101 GLDNNKVEWIKGYAEFVDEKTLRVNG-EIVTADHILIATGGEPVLPSIPGA--EYGITSDGFFALKELPKKVAVIGAGYI 177
Cdd:COG1249  100 LLKKNGVDVIRGRARFVDPHTVEVTGgETLTADHIVIATGSRPRVPPIPGLdeVRVLTSDEALELEELPKSLVVIGGGYI 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 178 AVELAGVLQQLGSETHLFVRKHAPLRNFDPLLTDTLTEIIEQSDMMLHKHAVPQKVEKNSDGsLTLSLEDGRTET---VD 254
Cdd:COG1249  180 GLEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDG-VTVTLEDGGGEEaveAD 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 255 TIIWAIGRKPVITGLQIEKAGVELLESGHIAVDKFQNTNVEGIYAVGDVTGHYELTPVAIAAGRRLSERLFNNKKdAHLS 334
Cdd:COG1249  259 KVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRTSVPGIYAIGDVTGGPQLAHVASAEGRVAAENILGKKP-RPVD 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 335 YENIPTVVFSHPAIGTVGLTEPEAIEKygKENIKIYTSSFTSMYTAITDHREPCRMKLICEGNTERVIGLHGIGYGVDEM 414
Cdd:COG1249  338 YRAIPSVVFTDPEIASVGLTEEEAREA--GIDVKVGKFPFAANGRALALGETEGFVKLIADAETGRILGAHIVGPHAGEL 415
                        410       420       430
                 ....*....|....*....|....*....|....
gi 500021004 415 IQGFAVAINMGATKSDFDNTVAIHPTGSEEFVTM 448
Cdd:COG1249  416 IHEAALAMEMGLTVEDLADTIHAHPTLSEALKEA 449
PTZ00058 PTZ00058
glutathione reductase; Provisional
5-448 7.62e-144

glutathione reductase; Provisional


Pssm-ID: 185420 [Multi-domain]  Cd Length: 561  Bit Score: 422.49  E-value: 7.62e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004   5 YDYIAIGGGSGGIASINRAAMHGAKCALIEPKFLGGTCVNVGCVPKKVMWYGAQIKEAMDlYADAYGYQVDASFNFQKLV 84
Cdd:PTZ00058  49 YDLIVIGGGSGGMAAARRAARNKAKVALVEKDYLGGTCVNVGCVPKKIMFNAASIHDILE-NSRHYGFDTQFSFNLPLLV 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  85 ENREAYIERIRGSYKNGLDNNKVEWIKGYAEFVDEKTLRV-----------------------------NGEIVTADHIL 135
Cdd:PTZ00058 128 ERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLIkkvsqvdgeadesdddevtivsagvsqldDGQVIEGKNIL 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 136 IATGGEPVLPSIPGAEYGITSDGFFALKElPKKVAVIGAGYIAVELAGVLQQLGSETHLFVRKHAPLRNFDPLLTDTLTE 215
Cdd:PTZ00058 208 IAVGNKPIFPDVKGKEFTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLRKFDETIINELEN 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 216 IIEQSDMMLHKHAVPQKVEKNSDGSLTLSLEDGRT-ETVDTIIWAIGRKPVITGLQIeKAGVELLESGHIAVDKFQNTNV 294
Cdd:PTZ00058 287 DMKKNNINIITHANVEEIEKVKEKNLTIYLSDGRKyEHFDYVIYCVGRSPNTEDLNL-KALNIKTPKGYIKVDDNQRTSV 365
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 295 EGIYAVGDVTG----------------------------------HYELTPVAIAAGRRLSERLFNNKKDAHlSYENIPT 340
Cdd:PTZ00058 366 KHIYAVGDCCMvkknqeiedlnllklyneepylkkkentsgesyyNVQLTPVAINAGRLLADRLFGPFSRTT-NYKLIPS 444
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 341 VVFSHPAIGTVGLTEPEAIEKYGKENIKIYTSSFTSMYTAITD----HREPCRMKLICEGNTERVIGLHGIGYGVDEMIQ 416
Cdd:PTZ00058 445 VIFSHPPIGTIGLSEQEAIDIYGKENVKIYESRFTNLFFSVYDmdpaQKEKTYLKLVCVGKEELIKGLHIVGLNADEILQ 524
                        490       500       510
                 ....*....|....*....|....*....|..
gi 500021004 417 GFAVAINMGATKSDFDNTVAIHPTGSEEFVTM 448
Cdd:PTZ00058 525 GFAVALKMNATKADFDETIPIHPTAAEEFVTM 556
gluta_reduc_2 TIGR01424
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ...
22-449 3.41e-135

glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, e.g., for maintaining the cellular thiol/disulfide status and for protecting against reactive oxygen species such as hydrogen peroxide. Glutathione-disulfide reductase regenerates reduced glutathione from oxidized glutathione (glutathione disulfide) + NADPH. This model represents one of two closely related subfamilies of glutathione-disulfide reductase. Both are closely related to trypanothione reductase, and separate models are built so each of the three can describe proteins with conserved function. This model describes glutathione-disulfide reductases of plants and some bacteria, including cyanobacteria. [Energy metabolism, Electron transport]


Pssm-ID: 213618 [Multi-domain]  Cd Length: 446  Bit Score: 396.10  E-value: 3.41e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004   22 RAAMHGAKCALIEPKFLGGTCVNVGCVPKKVMWYGAQIKEAMDlYADAYGYQV-DASFNFQKLVENREAYIERIRGSYKN 100
Cdd:TIGR01424  20 LAAALGAKVAIAEEFRVGGTCVIRGCVPKKLMVYASQFAEHFE-DAAGYGWTVgKARFDWKKLLAAKDQEIARLSGLYRK 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  101 GLDNNKVEWIKGYAEFVDEKTLRV--NGEIVTADHILIATGGEPVLPSIPGAEYGITSDGFFALKELPKKVAVIGAGYIA 178
Cdd:TIGR01424  99 GLANAGAELLDGRAELVGPNTVEVlaSGKTYTAEKILIAVGGRPPKPALPGHELGITSNEAFHLPTLPKSILIAGGGYIA 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  179 VELAGVLQQLGSETHLFVRKHAPLRNFDPLLTDTLTEIIEQSDMMLHKHAVPQKVEKNSDGSLTLSLEDGRTETVDTIIW 258
Cdd:TIGR01424 179 VEFAGIFRGLGVQTTLIYRGKEILRGFDDDMRRGLAAALEERGIRILPEDSITSISKDDDGRLKATLSKHEEIVADVVLF 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  259 AIGRKPVITGLQIEKAGVELLESGHIAVDKFQNTNVEGIYAVGDVTGHYELTPVAIAAGRRLSERLFNNKKdAHLSYENI 338
Cdd:TIGR01424 259 ATGRSPNTNGLGLEAAGVRLNDLGAIAVDEYSRTSTPSIYAVGDVTDRINLTPVAIHEATCFAETEFGNNP-TSFDHDLI 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  339 PTVVFSHPAIGTVGLTEPEAIEKYGKenIKIYTSSFTSMYTAITDHREPCRMKLICEGNTERVIGLHGIGYGVDEMIQGF 418
Cdd:TIGR01424 338 ATAVFSQPPIGTVGLTEEEARRKFGD--IEVYRAEFRPMKATFSGRQEKTLMKLVVDAKDDKVLGAHMVGPDAAEIIQGL 415
                         410       420       430
                  ....*....|....*....|....*....|.
gi 500021004  419 AVAINMGATKSDFDNTVAIHPTGSEEFVTMK 449
Cdd:TIGR01424 416 AIALKMGATKDDFDSTVAVHPTSAEELVTMR 446
PLN02546 PLN02546
glutathione reductase
23-449 8.06e-124

glutathione reductase


Pssm-ID: 215301 [Multi-domain]  Cd Length: 558  Bit Score: 371.13  E-value: 8.06e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  23 AAMHGAKCALIEPKF----------LGGTCVNVGCVPKKVMWYGAQIKEAMDlyaDAYG----YQVDASFNFQKLVENRE 88
Cdd:PLN02546  98 ASNFGASAAVCELPFatissdtlggVGGTCVLRGCVPKKLLVYASKYSHEFE---ESRGfgwkYETEPKHDWNTLIANKN 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  89 AYIERIRGSYKNGLDNNKVEWIKGYAEFVDEKTLRVNGEIVTADHILIATGGEPVLPSIPGAEYGITSDGFFALKELPKK 168
Cdd:PLN02546 175 AELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDVDGKLYTARNILIAVGGRPFIPDIPGIEHAIDSDAALDLPSKPEK 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 169 VAVIGAGYIAVELAGVLQQLGSETHLFVRKHAPLRNFDPLLTDTLTEIIEQSDMMLHKHAVPQKVEKNSDGSLTLSLEDG 248
Cdd:PLN02546 255 IAIVGGGYIALEFAGIFNGLKSDVHVFIRQKKVLRGFDEEVRDFVAEQMSLRGIEFHTEESPQAIIKSADGSLSLKTNKG 334
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 249 RTETVDTIIWAIGRKPVITGLQIEKAGVELLESGHIAVDKFQNTNVEGIYAVGDVTGHYELTPVAIAAGRRLSERLFNN- 327
Cdd:PLN02546 335 TVEGFSHVMFATGRKPNTKNLGLEEVGVKMDKNGAIEVDEYSRTSVPSIWAVGDVTDRINLTPVALMEGGALAKTLFGNe 414
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 328 --KKDahlsYENIPTVVFSHPAIGTVGLTEPEAIEKYGkeNIKIYTSSFTSMYTAITDHREPCRMKLICEGNTERVIGLH 405
Cdd:PLN02546 415 ptKPD----YRAVPSAVFSQPPIGQVGLTEEQAIEEYG--DVDVFTANFRPLKATLSGLPDRVFMKLIVCAKTNKVLGVH 488
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 500021004 406 GIGYGVDEMIQGFAVAINMGATKSDFDNTVAIHPTGSEEFVTMK 449
Cdd:PLN02546 489 MCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEEFVTMR 532
TGR TIGR01438
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ...
22-448 8.06e-120

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


Pssm-ID: 273624 [Multi-domain]  Cd Length: 484  Bit Score: 358.40  E-value: 8.06e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004   22 RAAMHGAKCALI---EPK------FLGGTCVNVGCVPKKVMWYGAQIKEAMDlYADAYGYQVDASF--NFQKLVENREAY 90
Cdd:TIGR01438  20 EAAAYGAKVMLLdfvTPTplgtrwGIGGTCVNVGCIPKKLMHQAALLGQALK-DSRNYGWKVEETVkhDWKRLVEAVQNH 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004   91 IERIRGSYKNGLDNNKVEWIKGYAEFVDEKTLRVNG-----EIVTADHILIATGGEPVLPSIPGA-EYGITSDGFFALKE 164
Cdd:TIGR01438  99 IGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNkkgkeKIYSAERFLIATGERPRYPGIPGAkELCITSDDLFSLPY 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  165 LPKKVAVIGAGYIAVELAGVLQQLGSETHLFVRKhAPLRNFDPLLTDTLTEIIEQSDMMLHKHAVPQKVEKNSDGSLTLS 244
Cdd:TIGR01438 179 CPGKTLVVGASYVALECAGFLAGIGLDVTVMVRS-ILLRGFDQDCANKVGEHMEEHGVKFKRQFVPIKVEQIEAKVLVEF 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  245 --LEDGRTETVDTIIWAIGRKPVITGLQIEKAGVELLE-SGHIAVDKFQNTNVEGIYAVGDVT-GHYELTPVAIAAGRRL 320
Cdd:TIGR01438 258 tdSTNGIEEEYDTVLLAIGRDACTRKLNLENVGVKINKkTGKIPADEEEQTNVPYIYAVGDILeDKPELTPVAIQAGRLL 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  321 SERLFNNKKDAhLSYENIPTVVFSHPAIGTVGLTEPEAIEKYGKENIKIYTSSFTSM-YTAIT-DHREPCRMKLICEGN- 397
Cdd:TIGR01438 338 AQRLFKGSTVI-CDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENVEVFHSYFWPLeWTIPSrDNHNKCYAKLVCNKKe 416
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 500021004  398 TERVIGLHGIGYGVDEMIQGFAVAINMGATKSDFDNTVAIHPTGSEEFVTM 448
Cdd:TIGR01438 417 NERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTL 467
PTZ00052 PTZ00052
thioredoxin reductase; Provisional
5-445 3.33e-113

thioredoxin reductase; Provisional


Pssm-ID: 185416 [Multi-domain]  Cd Length: 499  Bit Score: 341.80  E-value: 3.33e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004   5 YDYIAIGGGSGGIASINRAAMHGAKCAL---IEPKF------LGGTCVNVGCVPKKVMWYGAQIKEAMDLYADAYGYQVD 75
Cdd:PTZ00052   6 YDLVVIGGGSGGMAAAKEAAAHGKKVALfdyVKPSTqgtkwgLGGTCVNVGCVPKKLMHYAANIGSIFHHDSQMYGWKTS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  76 ASFNFQKLVENREAYIERIRGSYKNGLDNNKVEWIKGYAEFVDEKTLRV--NGEI--VTADHILIATGGEPVLP-SIPGA 150
Cdd:PTZ00052  86 SSFNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTVSYgdNSQEetITAKYILIATGGRPSIPeDVPGA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 151 -EYGITSDGFFALKELPKKVAVIGAGYIAVELAGVLQQLGSETHLFVRKhAPLRNFDPLLTDTLTEIIEQSDMMLHKHAV 229
Cdd:PTZ00052 166 kEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRS-IPLRGFDRQCSEKVVEYMKEQGTLFLEGVV 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 230 PQKVEKNSDgSLTLSLEDGRTETVDTIIWAIGRKPVITGLQIEKAGVELLESGHIAVDKfQNTNVEGIYAVGDVT-GHYE 308
Cdd:PTZ00052 245 PINIEKMDD-KIKVLFSDGTTELFDTVLYATGRKPDIKGLNLNAIGVHVNKSNKIIAPN-DCTNIPNIFAVGDVVeGRPE 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 309 LTPVAIAAGRRLSERLFNNKKDAhLSYENIPTVVFSHPAIGTVGLTEPEAIEKYGKENIKIYTSSFTSMYTAITdHREP- 387
Cdd:PTZ00052 323 LTPVAIKAGILLARRLFKQSNEF-IDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQEFNTLEIAAV-HREKh 400
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500021004 388 ---------------CRMKLICEGNT-ERVIGLHGIGYGVDEMIQGFAVAINMGATKSDFDNTVAIHPTGSEEF 445
Cdd:PTZ00052 401 erarkdeydfdvssnCLAKLVCVKSEdNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHPTDAEVF 474
PLN02507 PLN02507
glutathione reductase
23-449 3.57e-113

glutathione reductase


Pssm-ID: 215281 [Multi-domain]  Cd Length: 499  Bit Score: 341.80  E-value: 3.57e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  23 AAMHGAKCALIEPKF----------LGGTCVNVGCVPKKVMWYGAQIK-EAMDlyADAYGYQV--DASFNFQKLVENREA 89
Cdd:PLN02507  44 SANFGAKVGICELPFhpissesiggVGGTCVIRGCVPKKILVYGATFGgEFED--AKNYGWEIneKVDFNWKKLLQKKTD 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  90 YIERIRGSYKNGLDNNKVEWIKGYAEFVDEKTLRV---NGEIV--TADHILIATGGEPVLPSIPGAEYGITSDGFFALKE 164
Cdd:PLN02507 122 EILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVtqlDGTKLryTAKHILIATGSRAQRPNIPGKELAITSDEALSLEE 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 165 LPKKVAVIGAGYIAVELAGVLQQLGSETHLFVRKHAPLRNFDPLLTDTLTEIIEQSDMMLHKHAVPQKVEKNSDGsLTLS 244
Cdd:PLN02507 202 LPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRAVVARNLEGRGINLHPRTNLTQLTKTEGG-IKVI 280
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 245 LEDGRTETVDTIIWAIGRKPVITGLQIEKAGVELLESGHIAVDKFQNTNVEGIYAVGDVTGHYELTPVAIAAGRRLSERL 324
Cdd:PLN02507 281 TDHGEEFVADVVLFATGRAPNTKRLNLEAVGVELDKAGAVKVDEYSRTNIPSIWAIGDVTNRINLTPVALMEGTCFAKTV 360
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 325 FNNKKdAHLSYENIPTVVFSHPAIGTVGLTEPEAIEKyGKENIKIYTSSFTSMYTAITDHREPCRMKLICEGNTERVIGL 404
Cdd:PLN02507 361 FGGQP-TKPDYENVACAVFCIPPLSVVGLSEEEAVEQ-AKGDILVFTSSFNPMKNTISGRQEKTVMKLIVDAETDKVLGA 438
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 500021004 405 HGIGYGVDEMIQGFAVAINMGATKSDFDNTVAIHPTGSEEFVTMK 449
Cdd:PLN02507 439 SMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEFVTMR 483
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
22-443 2.81e-101

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 309.80  E-value: 2.81e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  22 RAAMHGAKCALIEPKFLGGTCVNVGCVPKKVMWYGAQIKEAMDlYADAYGYQVD-ASFNFQKLVENREAYIERIRGS-YK 99
Cdd:PRK06292  21 RAAKLGKKVALIEKGPLGGTCLNVGCIPSKALIAAAEAFHEAK-HAEEFGIHADgPKIDFKKVMARVRRERDRFVGGvVE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 100 NGLDNNKVEWIKGYAEFVDEKTLRVNGEIVTADHILIATGGEpvLPSIPGAEYG-----ITSDGFFALKELPKKVAVIGA 174
Cdd:PRK06292 100 GLEKKPKIDKIKGTARFVDPNTVEVNGERIEAKNIVIATGSR--VPPIPGVWLIlgdrlLTSDDAFELDKLPKSLAVIGG 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 175 GYIAVELAGVLQQLGSETHLFVRKHAPLRNFDPLLTDTLTEIIEQSdMMLHKHAVPQKVEKNSDGSLTLSLEDG--RTET 252
Cdd:PRK06292 178 GVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILSKE-FKIKLGAKVTSVEKSGDEKVEELEKGGktETIE 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 253 VDTIIWAIGRKPVITGLQIEKAGVELLESGHIAVDKFQNTNVEGIYAVGDVTGHYELTPVAIAAGRRLSERLFNNKKDaH 332
Cdd:PRK06292 257 ADYVLVATGRRPNTDGLGLENTGIELDERGRPVVDEHTQTSVPGIYAAGDVNGKPPLLHEAADEGRIAAENAAGDVAG-G 335
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 333 LSYENIPTVVFSHPAIGTVGLTEPEAIEKYGkeNIKIYTSSFTSMYTAITDHREPCRMKLICEGNTERVIGLHGIGYGVD 412
Cdd:PRK06292 336 VRYHPIPSVVFTDPQIASVGLTEEELKAAGI--DYVVGEVPFEAQGRARVMGKNDGFVKVYADKKTGRLLGAHIIGPDAE 413
                        410       420       430
                 ....*....|....*....|....*....|.
gi 500021004 413 EMIQGFAVAINMGATKSDFDNTVAIHPTGSE 443
Cdd:PRK06292 414 HLIHLLAWAMQQGLTVEDLLRMPFYHPTLSE 444
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
21-449 1.34e-98

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


Pssm-ID: 200098 [Multi-domain]  Cd Length: 486  Bit Score: 303.82  E-value: 1.34e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004   21 NRAAMHGAKCALIE------PKF---LGGTCVNVGCVPKKVMWYGAQIKEAMDLYAdAYGYQVDASF---NFQKLVENRE 88
Cdd:TIGR01423  21 NAATLYKKRVAVVDvqthhgPPFyaaLGGTCVNVGCVPKKLMVTGAQYMDTLRESA-GFGWEFDRSSvkaNWKALIAAKN 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004   89 AYIERIRGSYKNGL-DNNKVEWIKGYAEFVDEKTLRVNG---------EIVTADHILIATGGEPVLPSIPGAEYGITSDG 158
Cdd:TIGR01423 100 KAVLDINKSYEGMFaDTEGLTFFLGWGALEDKNVVLVREsadpksavkERLQAEHILLATGSWPQMLGIPGIEHCISSNE 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  159 FFALKELPKKVAVIGAGYIAVELAGVL---QQLGSETHLFVRKHAPLRNFDPLLTDTLTEIIEQSDMMLHKHAVPQKVEK 235
Cdd:TIGR01423 180 AFYLDEPPRRVLTVGGGFISVEFAGIFnayKPRGGKVTLCYRNNMILRGFDSTLRKELTKQLRANGINIMTNENPAKVTL 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  236 NSDGSLTLSLEDGRTETVDTIIWAIGRKPVITGLQIEKAGVELLESGHIAVDKFQNTNVEGIYAVGDVTGHYELTPVAIA 315
Cdd:TIGR01423 260 NADGSKHVTFESGKTLDVDVVMMAIGRVPRTQTLQLDKVGVELTKKGAIQVDEFSRTNVPNIYAIGDVTDRVMLTPVAIN 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  316 AGRRLSERLFNNKKDAhLSYENIPTVVFSHPAIGTVGLTEPEAIEKYgkENIKIYTSSFTSMYTAITDHREPCRM-KLIC 394
Cdd:TIGR01423 340 EGAAFVDTVFGNKPRK-TDHTRVASAVFSIPPIGTCGLVEEDAAKKF--EKVAVYESSFTPLMHNISGSKYKKFVaKIVT 416
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 500021004  395 EGNTERVIGLHGIGYGVDEMIQGFAVAINMGATKSDFDNTVAIHPTGSEEFVTMK 449
Cdd:TIGR01423 417 NHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAEELCSMR 471
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
22-443 6.98e-93

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: 288.39  E-value: 6.98e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004   22 RAAMHGAKCALIEPKFLGGTCVNVGCVPKKVMWYGAQIKEAMDlYADAYGYQVD-ASFNFQKLVENREAYIERIRGSYKN 100
Cdd:TIGR01350  19 RAAQLGLKVALVEKEYLGGTCLNVGCIPTKALLHSAEVYDEIK-HAKDLGIEVEnVSVDWEKMQKRKNKVVKKLVGGVSG 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  101 GLDNNKVEWIKGYAEFVDEKTLRVNGE----IVTADHILIATGGEPVLPSIP---GAEYGITSDGFFALKELPKKVAVIG 173
Cdd:TIGR01350  98 LLKKNKVTVIKGEAKFLDPGTVSVTGEngeeTLEAKNIIIATGSRPRSLPGPfdfDGKVVITSTGALNLEEVPESLVIIG 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  174 AGYIAVELAGVLQQLGSETHLFVRKHAPLRNFDPLLTDTLTEIIEQSDMMLHKHAVPQKVEKNsDGSLTLSLEDGRTETV 253
Cdd:TIGR01350 178 GGVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEKN-DDQVTYENKGGETETL 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  254 --DTIIWAIGRKPVITGLQIEKAGVELLESGHIAVDKFQNTNVEGIYAVGDVTGHYELTPVAIAAGRRLSERLFnNKKDA 331
Cdd:TIGR01350 257 tgEKVLVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDVIGGPMLAHVASHEGIVAAENIA-GKEPA 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  332 HLSYENIPTVVFSHPAIGTVGLTEPEAIEKYGkeNIKIYTSSFTSMYTAITDHREPCRMKLICEGNTERVIGLHGIGYGV 411
Cdd:TIGR01350 336 HIDYDAVPSVIYTDPEVASVGLTEEQAKEAGY--DVKIGKFPFAANGKALALGETDGFVKIIADKKTGEILGAHIIGPHA 413
                         410       420       430
                  ....*....|....*....|....*....|..
gi 500021004  412 DEMIQGFAVAINMGATKSDFDNTVAIHPTGSE 443
Cdd:TIGR01350 414 TELISEAALAMELEGTVEELARTIHPHPTLSE 445
PRK06370 PRK06370
FAD-containing oxidoreductase;
22-443 9.06e-89

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 277.85  E-value: 9.06e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  22 RAAMHGAKCALIEPKFLGGTCVNVGCVPKKVMWYGAQ-IKEAMDlyADAYGYQVDA--SFNFQKLVenreAYIERIRGSY 98
Cdd:PRK06370  23 RAAGLGMKVALIERGLLGGTCVNTGCVPTKTLIASARaAHLARR--AAEYGVSVGGpvSVDFKAVM----ARKRRIRARS 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  99 KNGLdnnkVEWIKGY---------AEFVDEKTLRVNGEIVTADHILIATGGEPVLPSIPG-AEYG-ITSDGFFALKELPK 167
Cdd:PRK06370  97 RHGS----EQWLRGLegvdvfrghARFESPNTVRVGGETLRAKRIFINTGARAAIPPIPGlDEVGyLTNETIFSLDELPE 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 168 KVAVIGAGYIAVELAGVLQQLGSETHLFVRKHAPLRNFDPLLTDTLTEIIEQSDMMLHKHAVPQKVEKNSDG-SLTLSLE 246
Cdd:PRK06370 173 HLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILEREGIDVRLNAECIRVERDGDGiAVGLDCN 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 247 DGRTE-TVDTIIWAIGRKPVITGLQIEKAGVELLESGHIAVDKFQNTNVEGIYAVGDVTGHYELTPVAIAAGRRLSERLF 325
Cdd:PRK06370 253 GGAPEiTGSHILVAVGRVPNTDDLGLEAAGVETDARGYIKVDDQLRTTNPGIYAAGDCNGRGAFTHTAYNDARIVAANLL 332
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 326 NNkKDAHLSYENIPTVVFSHPAIGTVGLTEPEAiEKYGKeNIKIYTSSFTSMYTAITDHREPCRMKLICEGNTERVIGLH 405
Cdd:PRK06370 333 DG-GRRKVSDRIVPYATYTDPPLARVGMTEAEA-RKSGR-RVLVGTRPMTRVGRAVEKGETQGFMKVVVDADTDRILGAT 409
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 500021004 406 GIGYGVDEMIQGFAVAINMGATKSDFDNTVAIHPTGSE 443
Cdd:PRK06370 410 ILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSE 447
MerA TIGR02053
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ...
22-443 1.26e-86

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: 272.37  E-value: 1.26e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004   22 RAAMHGAKCALIEPKFLGGTCVNVGCVPKKVMWYGAQIKEamdlYADAYGYQVDAS---FNFQKLVENREAYIERIRGS- 97
Cdd:TIGR02053  18 KAAELGASVAMVERGPLGGTCVNVGCVPSKMLLRAAEVAH----YARKPPFGGLAAtvaVDFGELLEGKREVVEELRHEk 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004   98 YKNGLDNNKVEWIKGYAEFVDEKTLRVNG--EIVTADHILIATGGEPVLPSIPG---AEYgITSDGFFALKELPKKVAVI 172
Cdd:TIGR02053  94 YEDVLSSYGVDYLRGRARFKDPKTVKVDLgrEVRGAKRFLIATGARPAIPPIPGlkeAGY-LTSEEALALDRIPESLAVI 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  173 GAGYIAVELAGVLQQLGSETHLFVRKHAPLRNFDPLLTDTLTEIIEQSDMMLHKHAVPQKVEKNSDGSL-TLSLEDGRTE 251
Cdd:TIGR02053 173 GGGAIGVELAQAFARLGSEVTILQRSDRLLPREEPEISAAVEEALAEEGIEVVTSAQVKAVSVRGGGKIiTVEKPGGQGE 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  252 T-VDTIIWAIGRKPVITGLQIEKAGVELLESGHIAVDKFQNTNVEGIYAVGDVTGHYELTPVAIAAGRRLSERLFNNkKD 330
Cdd:TIGR02053 253 VeADELLVATGRRPNTDGLGLEKAGVKLDERGGILVDETLRTSNPGIYAAGDVTGGLQLEYVAAKEGVVAAENALGG-AN 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  331 AHLSYENIPTVVFSHPAIGTVGLTEPEAIEKYGkeNIKIYTSSFTSMYTAITDHREPCRMKLICEGNTERVIGLHGIGYG 410
Cdd:TIGR02053 332 AKLDLLVIPRVVFTDPAVASVGLTEAEAQKAGI--ECDCRTLPLTNVPRARINRDTRGFIKLVAEPGTGKVLGVQVVAPE 409
                         410       420       430
                  ....*....|....*....|....*....|...
gi 500021004  411 VDEMIQGFAVAINMGATKSDFDNTVAIHPTGSE 443
Cdd:TIGR02053 410 AAEVINEAALAIRAGMTVDDLIDTLHPFPTMAE 442
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
22-443 5.19e-86

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 270.48  E-value: 5.19e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  22 RAAMHGAKCALIEPKFLGGTCVNVGCVPKKVMWYGAQIKEAMdLYADAYGYQVD-ASFNFQKLVENREAYIERIRGSYKN 100
Cdd:PRK06416  22 RAAQLGLKVAIVEKEKLGGTCLNRGCIPSKALLHAAERADEA-RHSEDFGIKAEnVGIDFKKVQEWKNGVVNRLTGGVEG 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 101 GLDNNKVEWIKGYAEFVDEKTLRVN----GEIVTADHILIATGGEPVlpSIPGAEYG----ITSDGFFALKELPKKVAVI 172
Cdd:PRK06416 101 LLKKNKVDIIRGEAKLVDPNTVRVMtedgEQTYTAKNIILATGSRPR--ELPGIEIDgrviWTSDEALNLDEVPKSLVVI 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 173 GAGYIAVELAGVLQQLGSET-------HLfvrkhapLRNFDPLLTDTLTEIIEQSDMMLHKHAVPQKVEKNSDGsLTLSL 245
Cdd:PRK06416 179 GGGYIGVEFASAYASLGAEVtivealpRI-------LPGEDKEISKLAERALKKRGIKIKTGAKAKKVEQTDDG-VTVTL 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 246 EDGRTE---TVDTIIWAIGRKPVITGLQIEKAGVElLESGHIAVDKFQNTNVEGIYAVGDVTGHYELTPVAIAAGRRLSE 322
Cdd:PRK06416 251 EDGGKEetlEADYVLVAVGRRPNTENLGLEELGVK-TDRGFIEVDEQLRTNVPNIYAIGDIVGGPMLAHKASAEGIIAAE 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 323 RLFNNkkDAHLSYENIPTVVFSHPAIGTVGLTEPEAIEKYGkeNIKIYTSSFTSMYTAITDHREPCRMKLICEGNTERVI 402
Cdd:PRK06416 330 AIAGN--PHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEGF--DVKVVKFPFAGNGKALALGETDGFVKLIFDKKDGEVL 405
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 500021004 403 GLHGIGYGVDEMIQGFAVAINMGATKSDFDNTVAIHPTGSE 443
Cdd:PRK06416 406 GAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSE 446
PRK07846 PRK07846
mycothione reductase; Reviewed
29-443 1.30e-71

mycothione reductase; Reviewed


Pssm-ID: 181142 [Multi-domain]  Cd Length: 451  Bit Score: 232.92  E-value: 1.30e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  29 KCALIEPKFLGGTCVNVGCVPKKVMWYGAQIKEAMdlyADAYGYQVDASFN---FQKLVENREAYIERIRGS---YKnGL 102
Cdd:PRK07846  24 RIAIVEKGTFGGTCLNVGCIPTKMFVYAADVARTI---REAARLGVDAELDgvrWPDIVSRVFGRIDPIAAGgeeYR-GR 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 103 DNNKVEWIKGYAEFVDEKTLRV-NGEIVTADHILIATGGEPVLPSIP---GAEYGiTSDGFFALKELPKKVAVIGAGYIA 178
Cdd:PRK07846 100 DTPNIDVYRGHARFIGPKTLRTgDGEEITADQVVIAAGSRPVIPPVIadsGVRYH-TSDTIMRLPELPESLVIVGGGFIA 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 179 VELAGVLQQLGSETHLFVRKHAPLRNFDPLLTDTLTEIIEQSdMMLHKHAVPQKVEKNSDGsLTLSLEDGRTETVDTIIW 258
Cdd:PRK07846 179 AEFAHVFSALGVRVTVVNRSGRLLRHLDDDISERFTELASKR-WDVRLGRNVVGVSQDGSG-VTLRLDDGSTVEADVLLV 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 259 AIGRKPVITGLQIEKAGVELLESGHIAVDKFQNTNVEGIYAVGDVTGHYELTPVAIAAGRRLSERLFNNKKDAHLSYENI 338
Cdd:PRK07846 257 ATGRVPNGDLLDAAAAGVDVDEDGRVVVDEYQRTSAEGVFALGDVSSPYQLKHVANHEARVVQHNLLHPDDLIASDHRFV 336
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 339 PTVVFSHPAIGTVGLTEPEAIEKYGKENIKIYTSSFTSMYTAITDHREPCrmKLICEGNTERVIGLHGIGYGVDEMIQGF 418
Cdd:PRK07846 337 PAAVFTHPQIASVGLTENEARAAGLDITVKVQNYGDVAYGWAMEDTTGFV--KLIADRDTGRLLGAHIIGPQASTLIQPL 414
                        410       420
                 ....*....|....*....|....*.
gi 500021004 419 AVAINMGATKSDF-DNTVAIHPTGSE 443
Cdd:PRK07846 415 IQAMSFGLDAREMaRGQYWIHPALPE 440
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
22-317 2.11e-70

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: 224.89  E-value: 2.11e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004   22 RAAMHGAKCALIEpkfLGGTCVNVGCVPKKVMWYGAQIKEAMdlyadaygyqvdasFNFQKLVENREAYIERIRGSYKNG 101
Cdd:pfam07992  18 TLAQLGGKVTLIE---DEGTCPYGGCVLSKALLGAAEAPEIA--------------SLWADLYKRKEEVVKKLNNGIEVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  102 LDNNKVEWIKGYAEFVDEKTLRVNGEIVTADHILIATGGEPVLPSIPGAEYG-------ITSDGFFALKELPKKVAVIGA 174
Cdd:pfam07992  81 LGTEVVSIDPGAKKVVLEELVDGDGETITYDRLVIATGARPRLPPIPGVELNvgflvrtLDSAEALRLKLLPKRVVVVGG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  175 GYIAVELAGVLQQLGSETHLFVRKHAPLRNFDPLLTDTLTEIIEQSDMMLHKHAVPQKVEKNSDGsLTLSLEDGRTETVD 254
Cdd:pfam07992 161 GYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDG-VEVILKDGTEIDAD 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500021004  255 TIIWAIGRKPVITGLqiEKAGVELLESGHIAVDKFQNTNVEGIYAVGDVT-GHYELTPVAIAAG 317
Cdd:pfam07992 240 LVVVAIGRRPNTELL--EAAGLELDERGGIVVDEYLRTSVPGIYAAGDCRvGGPELAQNAVAQG 301
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
22-443 6.24e-64

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 213.63  E-value: 6.24e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  22 RAAMHGAKCALIEPKF-------LGGTCVNVGCVPKKVMWYGAQIKEAMDLYADAYGYQVD-ASFNFQKLVENREAYIER 93
Cdd:PRK06327  22 RAAQLGLKVACIEAWKnpkgkpaLGGTCLNVGCIPSKALLASSEEFENAGHHFADHGIHVDgVKIDVAKMIARKDKVVKK 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  94 IRGSYKNGLDNNKVEWIKGYAEFV----DEKTLRVNGE---IVTADHILIATGGEPV-LPSIPGAEYGI-TSDGFFALKE 164
Cdd:PRK06327 102 MTGGIEGLFKKNKITVLKGRGSFVgktdAGYEIKVTGEdetVITAKHVIIATGSEPRhLPGVPFDNKIIlDNTGALNFTE 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 165 LPKKVAVIGAGYIAVELAGVLQQLGSETHLFVRKHAPLRNFDPLLTDTLTEIIEQSDMMLHKHAVPQKVEKNSDGsLTLS 244
Cdd:PRK06327 182 VPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAAADEQVAKEAAKAFTKQGLDIHLGVKIGEIKTGGKG-VSVA 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 245 LEDG----RTETVDTIIWAIGRKPVITGLQIEKAGVELLESGHIAVDKFQNTNVEGIYAVGDVTGHYELTPVAIAAGRRL 320
Cdd:PRK06327 261 YTDAdgeaQTLEVDKLIVSIGRVPNTDGLGLEAVGLKLDERGFIPVDDHCRTNVPNVYAIGDVVRGPMLAHKAEEEGVAV 340
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 321 SERLFNNKkdAHLSYENIPTVVFSHPAIGTVGLTEPEAIEkygkENIKIYTSSFTSMytAITDHR---EPCRM-KLICEG 396
Cdd:PRK06327 341 AERIAGQK--GHIDYNTIPWVIYTSPEIAWVGKTEQQLKA----EGVEYKAGKFPFM--ANGRALamgEPDGFvKIIADA 412
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 500021004 397 NTERVIGLHGIGYGVDEMIQGFAVAINMGATKSDFDNTVAIHPTGSE 443
Cdd:PRK06327 413 KTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSE 459
PRK07251 PRK07251
FAD-containing oxidoreductase;
27-445 3.67e-60

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 202.67  E-value: 3.67e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  27 GAKCALIE--PKFLGGTCVNVGCVPKKVMWYGAqikeamdlyadaygyqvDASFNFQKLVENREAYIERIRGSYKNGLDN 104
Cdd:PRK07251  26 GKKVALVEesKAMYGGTCINIGCIPTKTLLVAA-----------------EKNLSFEQVMATKNTVTSRLRGKNYAMLAG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 105 NKVEWIKGYAEFVDEKTLRVNG----EIVTADHILIATGGEPVLPSIPG---AEYGITSDGFFALKELPKKVAVIGAGYI 177
Cdd:PRK07251  89 SGVDLYDAEAHFVSNKVIEVQAgdekIELTAETIVINTGAVSNVLPIPGladSKHVYDSTGIQSLETLPERLGIIGGGNI 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 178 AVELAGVLQQLGSETHLFVRKHAPLRNFDPLLTDTLTEIIEQSDMMLHKHAVPQKVeKNSDGSLTLSLEDGrTETVDTII 257
Cdd:PRK07251 169 GLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYMEEDGITFLLNAHTTEV-KNDGDQVLVVTEDE-TYRFDALL 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 258 WAIGRKPVITGLQIEKAGVELLESGHIAVDKFQNTNVEGIYAVGDVTGHYELTPVAIAAGRRLSERLFNNKKDAHLSYEN 337
Cdd:PRK07251 247 YATGRKPNTEPLGLENTDIELTERGAIKVDDYCQTSVPGVFAVGDVNGGPQFTYISLDDFRIVFGYLTGDGSYTLEDRGN 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 338 IPTVVFSHPAIGTVGLTEPEAIEKygKENIKIYTSSFTSMYTAITDHREPCRMKLICEGNTERVIGLHGIGYGVDEMIQG 417
Cdd:PRK07251 327 VPTTMFITPPLSQVGLTEKEAKEA--GLPYAVKELLVAAMPRAHVNNDLRGAFKVVVNTETKEILGATLFGEGSQEIINL 404
                        410       420
                 ....*....|....*....|....*...
gi 500021004 418 FAVAINMGATKSDFDNTVAIHPTGSEEF 445
Cdd:PRK07251 405 ITMAMDNKIPYTYFKKQIFTHPTMAENL 432
PRK13748 PRK13748
putative mercuric reductase; Provisional
22-422 3.94e-60

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 205.77  E-value: 3.94e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  22 RAAMHGAKCALIEPKFLGGTCVNVGCVPKKVMWYGAQIKE-----AMDLYADAYGYQVDASfnfqKLVENREAYIERIR- 95
Cdd:PRK13748 116 KAVEQGARVTLIERGTIGGTCVNVGCVPSKIMIRAAHIAHlrresPFDGGIAATVPTIDRS----RLLAQQQARVDELRh 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  96 GSYKNGLDNN-KVEWIKGYAEFVDEKTLRV----NGE-IVTADHILIATGGEPVLPSIPG---AEYGITSDGFFAlKELP 166
Cdd:PRK13748 192 AKYEGILDGNpAITVLHGEARFKDDQTLIVrlndGGErVVAFDRCLIATGASPAVPPIPGlkeTPYWTSTEALVS-DTIP 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 167 KKVAVIGAGYIAVELAGVLQQLGSETHLFVRKHAPLRNfDPLLTDTLTEIIEQSDMMLHKHAVPQKVeKNSDGSLTLSLE 246
Cdd:PRK13748 271 ERLAVIGSSVVALELAQAFARLGSKVTILARSTLFFRE-DPAIGEAVTAAFRAEGIEVLEHTQASQV-AHVDGEFVLTTG 348
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 247 DGrTETVDTIIWAIGRKPVITGLQIEKAGVELLESGHIAVDKFQNTNVEGIYAVGDVTGHYELTPVAIAAGRRLSERLFN 326
Cdd:PRK13748 349 HG-ELRADKLLVATGRAPNTRSLALDAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQPQFVYVAAAAGTRAAINMTG 427
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 327 NkkDAHLSYENIPTVVFSHPAIGTVGLTEPEAiekygkENIKIYTSSFT----SMYTAITDHREPCRMKLICEGNTERVI 402
Cdd:PRK13748 428 G--DAALDLTAMPAVVFTDPQVATVGYSEAEA------HHDGIETDSRTltldNVPRALANFDTRGFIKLVIEEGSGRLI 499
                        410       420
                 ....*....|....*....|
gi 500021004 403 GLHGIGYGVDEMIQGFAVAI 422
Cdd:PRK13748 500 GVQAVAPEAGELIQTAALAI 519
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
22-443 3.58e-52

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


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 181.89  E-value: 3.58e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  22 RAAM----HGAKCALIEPKF-LGGTCVNVGCVPKKVMWYGA-QIKEAM--DLYADaygYQVDASFNFQKL------VENR 87
Cdd:PRK05249  19 GAAMqaakLGKRVAVIERYRnVGGGCTHTGTIPSKALREAVlRLIGFNqnPLYSS---YRVKLRITFADLlaradhVINK 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  88 EayIERIRGSYknglDNNKVEWIKGYAEFVDEKTLRVNG-----EIVTADHILIATGGEPVLPsipgAEYGIT------S 156
Cdd:PRK05249  96 Q--VEVRRGQY----ERNRVDLIQGRARFVDPHTVEVECpdgevETLTADKIVIATGSRPYRP----PDVDFDhpriydS 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 157 DGFFALKELPKKVAVIGAGYIAVELAGVLQQLGSETHLFVRKHAPLRNFDPLLTDTLTEIIEQSDMMLHKHAVPQKVEKN 236
Cdd:PRK05249 166 DSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSFLDDEISDALSYHLRDSGVTIRHNEEVEKVEGG 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 237 SDGSLTlSLEDGRTETVDTIIWAIGRKPVITGLQIEKAGVELLESGHIAVDK-FQnTNVEGIYAVGDVTGHYELTPVAIA 315
Cdd:PRK05249 246 DDGVIV-HLKSGKKIKADCLLYANGRTGNTDGLNLENAGLEADSRGQLKVNEnYQ-TAVPHIYAVGDVIGFPSLASASMD 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 316 AGRRLSERLFNNkKDAHLSyENIPTVVFSHPAIGTVGLTEPEAIEKY-----GKenikiytSSFTSMYTA-ITDHREPCr 389
Cdd:PRK05249 324 QGRIAAQHAVGE-ATAHLI-EDIPTGIYTIPEISSVGKTEQELTAAKvpyevGR-------ARFKELARAqIAGDNVGM- 393
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 500021004 390 MKLICEGNTERVIGLHGIGYGVDEMIQ-GFAVaINMGATKSDFDNTVAIHPTGSE 443
Cdd:PRK05249 394 LKILFHRETLEILGVHCFGERATEIIHiGQAI-MEQKGTIEYFVNTTFNYPTMAE 447
PRK08010 PRK08010
pyridine nucleotide-disulfide oxidoreductase; Provisional
24-443 1.69e-51

pyridine nucleotide-disulfide oxidoreductase; Provisional


Pssm-ID: 181196 [Multi-domain]  Cd Length: 441  Bit Score: 179.82  E-value: 1.69e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  24 AMHGAKCALIEPK--FLGGTCVNVGCVPKKVMWYGAQikeamdlyadaygyqvdASFNFQKLVENREAYIERIRG-SYKN 100
Cdd:PRK08010  23 AKAGWRVALIEQSnaMYGGTCINIGCIPTKTLVHDAQ-----------------QHTDFVRAIQRKNEVVNFLRNkNFHN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 101 GLDNNKVEWIKGYAEFVDEKTLRV---NGEIVT-ADHILIATGGEPVLPSIPG--AEYGI-TSDGFFALKELPKKVAVIG 173
Cdd:PRK08010  86 LADMPNIDVIDGQAEFINNHSLRVhrpEGNLEIhGEKIFINTGAQTVVPPIPGitTTPGVyDSTGLLNLKELPGHLGILG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 174 AGYIAVELAGVLQQLGSETHLFVRKHAPLRNFDPLLTDTLTEIIEQS--DMMLHKHAvpQKVEkNSDGSLTLSLEDGRtE 251
Cdd:PRK08010 166 GGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQgvDIILNAHV--ERIS-HHENQVQVHSEHAQ-L 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 252 TVDTIIWAIGRKPVITGLQIEKAGVELLESGHIAVDKFQNTNVEGIYAVGDVTGHYELTPVAIAAGRRLSERLFNNKKDA 331
Cdd:PRK08010 242 AVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKYLHTTADNIWAMGDVTGGLQFTYISLDDYRIVRDELLGEGKRS 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 332 HLSYENIPTVVFSHPAIGTVGLTEPEAIEKygKENIKIYTSSFTSMYTAITDHREPCRMKLICEGNTERVIGLHGIGYGV 411
Cdd:PRK08010 322 TDDRKNVPYSVFMTPPLSRVGMTEEQARES--GADIQVVTLPVAAIPRARVMNDTRGVLKAIVDNKTQRILGASLLCVDS 399
                        410       420       430
                 ....*....|....*....|....*....|..
gi 500021004 412 DEMIQGFAVAINMGATKSDFDNTVAIHPTGSE 443
Cdd:PRK08010 400 HEMINIVKMVMDAGLPYSILRDQIFTHPSMSE 431
Pyr_redox_dim pfam02852
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ...
338-448 3.21e-47

Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases.


Pssm-ID: 427019 [Multi-domain]  Cd Length: 109  Bit Score: 158.10  E-value: 3.21e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  338 IPTVVFSHPAIGTVGLTEPEAIEKYGKenIKIYTSSFTSMYTAITDHREPCRMKLICEGNTERVIGLHGIGYGVDEMIQG 417
Cdd:pfam02852   1 IPSVVFTDPEIASVGLTEEEAKEKGGE--VKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQE 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 500021004  418 FAVAINMGATKSDFDNTVAIHPTGSEEFVTM 448
Cdd:pfam02852  79 AALAIKMGATVEDLANTIHIHPTLSEALVEA 109
PRK07845 PRK07845
flavoprotein disulfide reductase; Reviewed
23-442 5.28e-39

flavoprotein disulfide reductase; Reviewed


Pssm-ID: 236112 [Multi-domain]  Cd Length: 466  Bit Score: 146.54  E-value: 5.28e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  23 AAMHGAKCALIEPKFLGGTCVNVGCVPKKVMWYGAQIKEAMDlYADAYGYQVD----ASFNFQKLveNReayieRIRG-- 96
Cdd:PRK07845  20 AAQLGADVTVIERDGLGGAAVLTDCVPSKTLIATAEVRTELR-RAAELGIRFIddgeARVDLPAV--NA-----RVKAla 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  97 -----SYKNGLDNNKVEWIKGYAEFVDEK----TLRVNG-----EIVTADHILIATGGEP-VLPS-IPGAEYGITSDGFF 160
Cdd:PRK07845  92 aaqsaDIRARLEREGVRVIAGRGRLIDPGlgphRVKVTTadggeETLDADVVLIATGASPrILPTaEPDGERILTWRQLY 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 161 ALKELPKKVAVIGAGYIAVELAGVLQQLGSETHLFVRKHAPLRNFDPLLTDTLTEIIEQSDMMLHKHAVPQKVEKNSDGs 240
Cdd:PRK07845 172 DLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPGEDADAAEVLEEVFARRGMTVLKRSRAESVERTGDG- 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 241 LTLSLEDGRTETVDTIIWAIGRKPVITGLQIEKAGVELLESGHIAVDKFQNTNVEGIYAVGDVTGHYELTPVAIAAGR-- 318
Cdd:PRK07845 251 VVVTLTDGRTVEGSHALMAVGSVPNTAGLGLEEAGVELTPSGHITVDRVSRTSVPGIYAAGDCTGVLPLASVAAMQGRia 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 319 ---RLSERLfnnkkdAHLSYENIPTVVFSHPAIGTVGLTEpEAIEKyGKENIKIYTSSFTSMYTAitdhrepcRM----- 390
Cdd:PRK07845 331 myhALGEAV------SPLRLKTVASNVFTRPEIATVGVSQ-AAIDS-GEVPARTVMLPLATNPRA--------KMsglrd 394
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500021004 391 ---KLICEGNTERVIGlhgigyGV------DEMIQGFAVAINMGATKSDFDNTVAIHP--TGS 442
Cdd:PRK07845 395 gfvKLFCRPGTGVVIG------GVvvapraSELILPIALAVQNRLTVDDLAQTFTVYPslSGS 451
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
118-307 8.53e-37

NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];


Pssm-ID: 440215 [Multi-domain]  Cd Length: 322  Bit Score: 137.25  E-value: 8.53e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 118 DEKTLRV-NGEIVTADHILIATGGEPVLPSIPGaeygITSDGFFALKEL--------------PKKVAVIGAGYIAVELA 182
Cdd:COG0446   65 EAKTVTLrDGETLSYDKLVLATGARPRPPPIPG----LDLPGVFTLRTLddadalrealkefkGKRAVVIGGGPIGLELA 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 183 GVLQQLGSETHLFVRKHAPLRNFDPLLTDTLTEIIEQSDMMLHKHAVPQKVEknSDGSLTLSLEDGRTETVDTIIWAIGR 262
Cdd:COG0446  141 EALRKRGLKVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAID--GDDKVAVTLTDGEEIPADLVVVAPGV 218
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 500021004 263 KPViTGLqIEKAGVELLESGHIAVDKFQNTNVEGIYAVGDVTGHY 307
Cdd:COG0446  219 RPN-TEL-AKDAGLALGERGWIKVDETLQTSDPDVYAAGDCAEVP 261
PTZ00153 PTZ00153
lipoamide dehydrogenase; Provisional
38-443 5.84e-36

lipoamide dehydrogenase; Provisional


Pssm-ID: 173442 [Multi-domain]  Cd Length: 659  Bit Score: 140.43  E-value: 5.84e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  38 LGGTCVNVGCVPKKVMWYGA----QIKEAMDLYAdaYGYQVDASFNFQ-------------------KLVENREAYIERI 94
Cdd:PTZ00153 152 IGGTCVNVGCIPSKALLYATgkyrELKNLAKLYT--YGIYTNAFKNGKndpvernqlvadtvqiditKLKEYTQSVIDKL 229
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  95 RGSYKNGLDNNK-------VEWIKGYAEFVDEKTLR--VNGEIVTADHILIATGGEPVLPS-IPGAEYGI-TSDGFFALK 163
Cdd:PTZ00153 230 RGGIENGLKSKKfcknsehVQVIYERGHIVDKNTIKseKSGKEFKVKNIIIATGSTPNIPDnIEVDQKSVfTSDTAVKLE 309
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 164 ELPKKVAVIGAGYIAVELAGVLQQLGSE------------------THLFVR---KHAPLRnfdpLLTDTLTEII----- 217
Cdd:PTZ00153 310 GLQNYMGIVGMGIIGLEFMDIYTALGSEvvsfeyspqllplldadvAKYFERvflKSKPVR----VHLNTLIEYVragkg 385
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 218 EQSDMMLHKHAVpqkvEKNSDGSLTlSLEDGRTETVDTIIWAIGRKPVITGLQIEKAGVELlESGHIAVD------KFQN 291
Cdd:PTZ00153 386 NQPVIIGHSERQ----TGESDGPKK-NMNDIKETYVDSCLVATGRKPNTNNLGLDKLKIQM-KRGFVSVDehlrvlREDQ 459
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 292 TNVEGIYAVGDVTGHYELTPVAIAAGRRLSERLFNNKKDAHLS-----------YENIPTVVFSHPAIGTVGLTEPEAIE 360
Cdd:PTZ00153 460 EVYDNIFCIGDANGKQMLAHTASHQALKVVDWIEGKGKENVNInvenwaskpiiYKNIPSVCYTTPELAFIGLTEKEAKE 539
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 361 KYGKENIKIYTSSFTSMYTAITDHREPCR----------------------MKLICEGNTERVIGLHGIGYGVDEMIQGF 418
Cdd:PTZ00153 540 LYPPDNVGVEISFYKANSKVLCENNISFPnnsknnsynkgkyntvdntegmVKIVYLKDTKEILGMFIVGSYASILIHEG 619
                        490       500
                 ....*....|....*....|....*
gi 500021004 419 AVAINMGATKSDFDNTVAIHPTGSE 443
Cdd:PTZ00153 620 VLAINLKLSVKDLAHMVHSHPTISE 644
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
23-317 1.87e-27

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 111.37  E-value: 1.87e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  23 AAMHGAKCALIEPKFLGG-----TCV-NVGCVPKKVMwyGAQIKEAMDLYADAYGyqvdasfnfqklVENREAYIERIRg 96
Cdd:COG0492   19 AARAGLKTLVIEGGEPGGqlattKEIeNYPGFPEGIS--GPELAERLREQAERFG------------AEILLEEVTSVD- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  97 sykngldnnkvewikgyaefVDEKTLRV---NGEIVTADHILIATGGEPVLPSIPGAE--------YGITSDGFFALKel 165
Cdd:COG0492   84 --------------------KDDGPFRVttdDGTEYEAKAVIIATGAGPRKLGLPGEEefegrgvsYCATCDGFFFRG-- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 166 pKKVAVIGAGYIAVELAGVLQQLGSETHLFVRKHApLRNFDPLLTdtltEIIEQSDMMLHKHAVPQKVEKnsDGSLT-LS 244
Cdd:COG0492  142 -KDVVVVGGGDSALEEALYLTKFASKVTLIHRRDE-LRASKILVE----RLRANPKIEVLWNTEVTEIEG--DGRVEgVT 213
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500021004 245 LEDGRTET-----VDTIIWAIGRKPvITGLqIEKAGVELLESGHIAVDKFQNTNVEGIYAVGDVTGH-YELtpVAIAAG 317
Cdd:COG0492  214 LKNVKTGEekeleVDGVFVAIGLKP-NTEL-LKGLGLELDEDGYIVVDEDMETSVPGVFAAGDVRDYkYRQ--AATAAG 288
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
118-324 3.50e-26

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 109.46  E-value: 3.50e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 118 DEKTLRV-NGEIVTADHILIATGGEPVLPSIPGAEygitSDGFFALKEL------------PKKVAVIGAGYIAVELAGV 184
Cdd:COG1251   85 AARTVTLaDGETLPYDKLVLATGSRPRVPPIPGAD----LPGVFTLRTLddadalraalapGKRVVVIGGGLIGLEAAAA 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 185 LQQLGSETHLFVRKHAPL-RNFDPLLTDTLTEIIEQSDMMLHKHAVPQKVEKNSDGsLTLSLEDGRTETVDTIIWAIGRK 263
Cdd:COG1251  161 LRKRGLEVTVVERAPRLLpRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRV-TGVRLADGEELPADLVVVAIGVR 239
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 264 PViTGLqIEKAGVElLESGhIAVDKFQNTNVEGIYAVGDVTGHY---------ELTPVAIAAGRRLSERL 324
Cdd:COG1251  240 PN-TEL-ARAAGLA-VDRG-IVVDDYLRTSDPDIYAAGDCAEHPgpvygrrvlELVAPAYEQARVAAANL 305
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
118-427 4.55e-24

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 103.97  E-value: 4.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 118 DEKTLRV----NGEIVTA--DHILIATGGEPVLPSIPGAE----YGITS--DGFfALKELPKK-----VAVIGAGYIAVE 180
Cdd:PRK09564  85 KNKTITVknlkTGSIFNDtyDKLMIATGARPIIPPIKNINlenvYTLKSmeDGL-ALKELLKDeeiknIVIIGAGFIGLE 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 181 LAGVLQQLGSETHLFVR-KHAPLRNFDPLLTDTLTEIIEQSDMMLHKHAVPQKVEknSDGSLTLSLEDGRTETVDTIIWA 259
Cdd:PRK09564 164 AVEAAKHLGKNVRIIQLeDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSLI--GEDKVEGVVTDKGEYEADVVIVA 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 260 IGRKPVITGLqiEKAGVELLESGHIAVDKFQNTNVEGIYAVGD-------VTGHYELTPVAIAA---GRRLSERLFNNKK 329
Cdd:PRK09564 242 TGVKPNTEFL--EDTGLKTLKNGAIIVDEYGETSIENIYAAGDcatiyniVSNKNVYVPLATTAnklGRMVGENLAGRHV 319
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 330 DAHLSYENIPTVVFSHPAiGTVGLTEPEAIekygKENIKIYTSSFTSM-YTAITDHREPCRMKLICEGNTERVIGLHGIG 408
Cdd:PRK09564 320 SFKGTLGSACIKVLDLEA-ARTGLTEEEAK----KLGIDYKTVFIKDKnHTNYYPGQEDLYVKLIYEADTKVILGGQIIG 394
                        330       340
                 ....*....|....*....|
gi 500021004 409 Y-GVDEMIQGFAVAINMGAT 427
Cdd:PRK09564 395 KkGAVLRIDALAVAIYAKLT 414
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
102-342 2.65e-18

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 86.34  E-value: 2.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 102 LDNNKVEWIKGYAEFVD--EKTLRV-NGEIVTADHILIATGGEPVLPSIPG-AEYGI---TSDGFFALKEL--------- 165
Cdd:COG1252   66 LRRAGVRFIQGEVTGIDpeARTVTLaDGRTLSYDYLVIATGSVTNFFGIPGlAEHALplkTLEDALALRERllaaferae 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 166 ---PKKVAVIGAGYIAVELAGVLQQLGSETHLFVRKHA-------------PLRNFDPLLTDTLTEIIEQSDMMLHKHAV 229
Cdd:COG1252  146 rrrLLTIVVVGGGPTGVELAGELAELLRKLLRYPGIDPdkvritlveagprILPGLGEKLSEAAEKELEKRGVEVHTGTR 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 230 PQKVEKNsdgslTLSLEDGRTETVDTIIWAIGrkpvITGLQ-IEKAGVELLESGHIAVDKF-QNTNVEGIYAVGDVTG-- 305
Cdd:COG1252  226 VTEVDAD-----GVTLEDGEEIPADTVIWAAG----VKAPPlLADLGLPTDRRGRVLVDPTlQVPGHPNVFAIGDCAAvp 296
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 500021004 306 HYELTPV------AIAAGRRLSE---RLFNNKKDAHLSYENIPTVV 342
Cdd:COG1252  297 DPDGKPVpktaqaAVQQAKVLAKniaALLRGKPLKPFRYRDKGCLA 342
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
168-248 1.05e-16

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: 74.55  E-value: 1.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  168 KVAVIGAGYIAVELAGVLQQLGSETHLFVRKHAPLRNFDPLLTDTLTEIIEQSDMMLHKHAVPQKVEKNSDGSLTLsLED 247
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVV-LTD 79

                  .
gi 500021004  248 G 248
Cdd:pfam00070  80 G 80
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
126-306 3.77e-15

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


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 77.95  E-value: 3.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  126 GEIVTADHILIATGGEPVLPSIPGAE----YGITS----DGFFALKELPKKVAVIGAGYIAVELAGVLQQLGSETHlfVR 197
Cdd:TIGR02374  92 GRTLSYDKLILATGSYPFILPIPGADkkgvYVFRTiedlDAIMAMAQRFKKAAVIGGGLLGLEAAVGLQNLGMDVS--VI 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  198 KHAPL---RNFDPLLTDTLTEIIEQSDMMLHkhavpqkVEKNSDGSL------TLSLEDGRTETVDTIIWAIGRKPVITg 268
Cdd:TIGR02374 170 HHAPGlmaKQLDQTAGRLLQRELEQKGLTFL-------LEKDTVEIVgatkadRIRFKDGSSLEADLIVMAAGIRPNDE- 241
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 500021004  269 LQIEkAGVELleSGHIAVDKFQNTNVEGIYAVGDVTGH 306
Cdd:TIGR02374 242 LAVS-AGIKV--NRGIIVNDSMQTSDPDIYAVGECAEH 276
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
167-439 5.18e-15

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 76.75  E-value: 5.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 167 KKVAVIGAGYIAVELAGVLQQLGSETHLFVRKHAPLRNFDPLLTDTLTEIIEQSDMMLHKHAVPQKVEKNsdgslTLSLE 246
Cdd:PRK13512 149 DKALVVGAGYISLEVLENLYERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDAINGN-----EVTFK 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 247 DGRTETVDTIIWAIGRKPviTGLQIEKAGVELLESGHIAV-DKFQnTNVEGIYAVGDV-TGHYE------LTPVAIAAGR 318
Cdd:PRK13512 224 SGKVEHYDMIIEGVGTHP--NSKFIESSNIKLDDKGFIPVnDKFE-TNVPNIYAIGDIiTSHYRhvdlpaSVPLAWGAHR 300
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 319 RLS---ERLFNNKKDAHLSYENIPTVVFSHPAIGTVGLtEPEAIEKYGKENIKIYTSSFTSMYTAitdhREPCRMKLICE 395
Cdd:PRK13512 301 AASivaEQIAGNDTIEFKGFLGNNIVKFFDYTFASVGV-KPNELKQFDYKMVEVTQGAHANYYPG----NSPLHLRVYYD 375
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 500021004 396 GNTERVIGLHGIG-YGVDEMIQGFAVAINMGATKSDF-DNTVAIHP 439
Cdd:PRK13512 376 TSNRKILRAAAVGkEGADKRIDVLSMAMMNQLTVDELtEFEVAYAP 421
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
117-302 2.62e-14

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 74.18  E-value: 2.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 117 VDEKTLRVNGEIVTADHILIATGGEPVLPSIPGAEYGIT--SDGFFALKELP----KKVAVIGAGYIAVELAGVLQQLGS 190
Cdd:PRK04965  86 AEAQVVKSQGNQWQYDKLVLATGASAFVPPIPGRELMLTlnSQQEYRAAETQlrdaQRVLVVGGGLIGTELAMDLCRAGK 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 191 ETHLFVRKHAPLRNfdpLLTDTLTEIIEQS--DMMLH---KHAVpQKVEKNSDGsLTLSLEDGRTETVDTIIWAIGRKPV 265
Cdd:PRK04965 166 AVTLVDNAASLLAS---LMPPEVSSRLQHRltEMGVHlllKSQL-QGLEKTDSG-IRATLDSGRSIEVDAVIAAAGLRPN 240
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 500021004 266 I-----TGLQIEKAgvellesghIAVDKFQNTNVEGIYAVGD 302
Cdd:PRK04965 241 TalarrAGLAVNRG---------IVVDSYLQTSAPDIYALGD 273
Pyr_redox_3 pfam13738
Pyridine nucleotide-disulphide oxidoreductase;
121-301 5.09e-12

Pyridine nucleotide-disulphide oxidoreductase;


Pssm-ID: 404603 [Multi-domain]  Cd Length: 296  Bit Score: 66.48  E-value: 5.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  121 TLRVNGEIVTADHILIATG--GEPVLPSIPgaEYGITSDGFFALKELP-KKVAVIGAGYIAVELAGVLQQLGSETHLFVR 197
Cdd:pfam13738 109 VVTTSKGTYQARYVIIATGefDFPNKLGVP--ELPKHYSYVKDFHPYAgQKVVVIGGYNSAVDAALELVRKGARVTVLYR 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  198 kHAPLRNFDP-----LLTDT---LTEIIEQSDMMLHKHAVPQKVEKNsDGSLTLSLEDGRTETVDTI-IWAIGRKPviTG 268
Cdd:pfam13738 187 -GSEWEDRDSdpsysLSPDTlnrLEELVKNGKIKAHFNAEVKEITEV-DVSYKVHTEDGRKVTSNDDpILATGYHP--DL 262
                         170       180       190
                  ....*....|....*....|....*....|....
gi 500021004  269 LQIEKAGVELLESGHIAVDKF-QNTNVEGIYAVG 301
Cdd:pfam13738 263 SFLKKGLFELDEDGRPVLTEEtESTNVPGLFLAG 296
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
132-319 2.97e-11

NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440259 [Multi-domain]  Cd Length: 434  Bit Score: 65.16  E-value: 2.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 132 DHILIATG-GEPVLPSIPGAEY-GITS-----------DGFFALKELPKKVAVIGAGYIAVELAGVLQQLGSET-HLFVR 197
Cdd:COG0493  208 DAVFLATGaGKPRDLGIPGEDLkGVHSamdfltavnlgEAPDTILAVGKRVVVIGGGNTAMDCARTALRLGAESvTIVYR 287
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 198 ---KHAPLRNFDplLTDTLTEIIEqsdmmLHKHAVPQKVEKNSDGSLT----------LSLEDGR-----------TETV 253
Cdd:COG0493  288 rtrEEMPASKEE--VEEALEEGVE-----FLFLVAPVEIIGDENGRVTglecvrmelgEPDESGRrrpvpiegsefTLPA 360
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500021004 254 DTIIWAIGRKPVITGLQiEKAGVELLESGHIAVDKF-QNTNVEGIYAVGD-VTGhYELTPVAIAAGRR 319
Cdd:COG0493  361 DLVILAIGQTPDPSGLE-EELGLELDKRGTIVVDEEtYQTSLPGVFAGGDaVRG-PSLVVWAIAEGRK 426
PRK14989 PRK14989
nitrite reductase subunit NirD; Provisional
118-302 5.61e-11

nitrite reductase subunit NirD; Provisional


Pssm-ID: 184951 [Multi-domain]  Cd Length: 847  Bit Score: 64.75  E-value: 5.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 118 DEKTLRVN-GEIVTADHILIATGGEPVLPSIPGAEygiTSDGFF-----------ALKELPKKVAVIGAGYIAVELAGVL 185
Cdd:PRK14989  88 QEKVIHSSaGRTVFYDKLIMATGSYPWIPPIKGSE---TQDCFVyrtiedlnaieACARRSKRGAVVGGGLLGLEAAGAL 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 186 QQLGSETHlfVRKHAPL---RNFDPLLTDTLTEIIEQSDMMLHKHAVPQK-VEKNSDGSLTLSLEDGRTETVDTIIWAIG 261
Cdd:PRK14989 165 KNLGVETH--VIEFAPMlmaEQLDQMGGEQLRRKIESMGVRVHTSKNTLEiVQEGVEARKTMRFADGSELEVDFIVFSTG 242
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 500021004 262 RKPVITglQIEKAGVELLESGHIAVDKFQNTNVEGIYAVGD 302
Cdd:PRK14989 243 IRPQDK--LATQCGLAVAPRGGIVINDSCQTSDPDIYAIGE 281
PRK10262 PRK10262
thioredoxin reductase; Provisional
130-306 3.29e-10

thioredoxin reductase; Provisional


Pssm-ID: 182343 [Multi-domain]  Cd Length: 321  Bit Score: 61.23  E-value: 3.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 130 TADHILIATGGEPVLPSIPGAE----YGI----TSDGFFALKElpkKVAVIGAGYIAVELAGVLQQLGSETHLFVRKHAp 201
Cdd:PRK10262 105 TCDALIIATGASARYLGLPSEEafkgRGVsacaTCDGFFYRNQ---KVAVIGGGNTAVEEALYLSNIASEVHLIHRRDG- 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 202 lRNFDPLLTDTLTEIIEQSDMMLHKHAVPQKVEKNSDGSLTLSLEDGRT----ETVDT--IIWAIGRKP--VITGLQIEk 273
Cdd:PRK10262 181 -FRAEKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQNsdniESLDVagLFVAIGHSPntAIFEGQLE- 258
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 500021004 274 agvelLESGHIAVD-----KFQNTNVEGIYAVGDVTGH 306
Cdd:PRK10262 259 -----LENGYIKVQsgihgNATQTSIPGVFAAGDVMDH 291
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
126-324 5.51e-10

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 60.77  E-value: 5.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 126 GEIVTA-DHILIATGG-EPVLPSIPGAE-----------YGITSD--GFFALKELP----KKVAVIGAGYIAVELAGVLQ 186
Cdd:PRK12770 113 EELVKKyDAVLIATGTwKSRKLGIPGEDlpgvysaleylFRIRAAklGYLPWEKVPpvegKKVVVVGAGLTAVDAALEAV 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 187 QLGSE--THLFVR--KHAPLRNFDplltdtlTEIIEQSDMMLHKHAVPqkVEKNSDGS----------LTLSLEDGRTET 252
Cdd:PRK12770 193 LLGAEkvYLAYRRtiNEAPAGKYE-------IERLIARGVEFLELVTP--VRIIGEGRvegvelakmrLGEPDESGRPRP 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 253 V-----------DTIIWAIGRKPViTGLQIEKAGVELLESGHIAVDKFQNTNVEGIYAVGDVTGHYELTPVAIAAGRRLS 321
Cdd:PRK12770 264 VpipgsefvleaDTVVFAIGEIPT-PPFAKECLGIELNRKGEIVVDEKHMTSREGVFAAGDVVTGPSKIGKAIKSGLRAA 342

                 ...
gi 500021004 322 ERL 324
Cdd:PRK12770 343 QSI 345
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
125-261 5.97e-10

Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];


Pssm-ID: 441675 [Multi-domain]  Cd Length: 414  Bit Score: 61.03  E-value: 5.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 125 NGEIVTADHILIATGG--EPVLPSIPGAE-YGITS------DGFFALKElpKKVAVIGAGYIAVELAGVLQQLGSETHLF 195
Cdd:COG2072  123 DGETLTARFVVVATGPlsRPKIPDIPGLEdFAGEQlhsadwRNPVDLAG--KRVLVVGTGASAVQIAPELARVAAHVTVF 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 196 VRKH---APLRNFDPLLTDTLTEIIEQSDMMLHKHAVPQKVEKNSDGSL------------------------------- 241
Cdd:COG2072  201 QRTPpwvLPRPNYDPERGRPANYLGLEAPPALNRRDARAWLRRLLRAQVkdpelglltpdyppgckrpllstdyyealrr 280
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 500021004 242 ----------------TLSLEDGRTETVDTIIWAIG 261
Cdd:COG2072  281 gnvelvtggieritedGVVFADGTEHEVDVIVWATG 316
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
132-319 6.59e-07

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 51.65  E-value: 6.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 132 DHILIATGGEPV-LPSIPGAEY-GITSD-GFFA------LKELPKKVAVIGAGYIAVELAGVLQQLGSE--THLFVRKHA 200
Cdd:PRK12814 280 DAVLLAVGAQKAsKMGIPGEELpGVISGiDFLRnvalgtALHPGKKVVVIGGGNTAIDAARTALRLGAEsvTILYRRTRE 359
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 201 PLRNFDPLLTDTLTEIIEqsdmmLHKHAVPQKVEKnSDGSLTLSL---------EDGR-----------TETVDTIIWAI 260
Cdd:PRK12814 360 EMPANRAEIEEALAEGVS-----LRELAAPVSIER-SEGGLELTAikmqqgepdESGRrrpvpvegsefTLQADTVISAI 433
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500021004 261 GRKPVITGLqiEKAGVELLESGHIAVD-KFQNTNVEGIYAVGD-VTGHyELTPVAIAAGRR 319
Cdd:PRK12814 434 GQQVDPPIA--EAAGIGTSRNGTVKVDpETLQTSVAGVFAGGDcVTGA-DIAINAVEQGKR 491
PRK12775 PRK12775
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ...
132-329 1.92e-06

putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional


Pssm-ID: 183738 [Multi-domain]  Cd Length: 1006  Bit Score: 50.32  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  132 DHILIATG-GEPVLPSIPGAEYG--ITSDGF-----------FALKELP----KKVAVIGAGYIAVELAGVLQQLGSETh 193
Cdd:PRK12775  519 DAVFLGVGaGAPTFLGIPGEFAGqvYSANEFltrvnlmggdkFPFLDTPislgKSVVVIGAGNTAMDCLRVAKRLGAPT- 597
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  194 lfVR-----------------KHAPLRNFDPLLTDTLTEIIEQSDMMLHKHAVPQKVEKNSDgsltlslEDGRTETV--- 253
Cdd:PRK12775  598 --VRcvyrrseaeaparieeiRHAKEEGIDFFFLHSPVEIYVDAEGSVRGMKVEEMELGEPD-------EKGRRKPMptg 668
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004  254 -------DTIIWAIGRK--PVITGlqiEKAGVELLESGHIAVDKF-----QNTNVEGIYAVGDVTGHYELTPVAIAAGRR 319
Cdd:PRK12775  669 efkdlecDTVIYALGTKanPIITQ---STPGLALNKWGNIAADDGklestQSTNLPGVFAGGDIVTGGATVILAMGAGRR 745
                         250
                  ....*....|....
gi 500021004  320 ----LSERLFNNKK 329
Cdd:PRK12775  746 aarsIATYLRLGKK 759
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
125-303 1.62e-05

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 46.84  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 125 NGEIVTADHILIATGGE----PVLPSIPGAEYGI-TSDGFFALKELPKK---VAVIGAGYIAVELAGVLQQLGSETHLFV 196
Cdd:PRK09754  95 NGESWHWDQLFIATGAAarplPLLDALGERCFTLrHAGDAARLREVLQPersVVIVGAGTIGLELAASATQRRCKVTVIE 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 197 RKHAPL-RNFDPLLTDTLTEIIEQSDMMLHkhaVPQKVEKNSDGS-LTLSLEDGRTETVDTIIWAIGrkpvITGLQIEKA 274
Cdd:PRK09754 175 LAATVMgRNAPPPVQRYLLQRHQQAGVRIL---LNNAIEHVVDGEkVELTLQSGETLQADVVIYGIG----ISANDQLAR 247
                        170       180
                 ....*....|....*....|....*....
gi 500021004 275 GVELLESGHIAVDKFQNTNVEGIYAVGDV 303
Cdd:PRK09754 248 EANLDTANGIVIDEACRTCDPAIFAGGDV 276
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
132-319 1.86e-05

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


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 47.04  E-value: 1.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 132 DHILIATG-GEPVLPSIPGAEY-GITS-----------DGFFALKELP----KKVAVIGAGYIAVELAGVLQQLGSETHL 194
Cdd:PRK12778 519 KGIFIASGaGLPNFMNIPGENSnGVMSsneyltrvnlmDAASPDSDTPikfgKKVAVVGGGNTAMDSARTAKRLGAERVT 598
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 195 FVR--------------KHAPLRNFDPLLTDTLTEIIEQSDMMLhKHAVPQKV---EKNSDGSLTLSLEDGRTETV--DT 255
Cdd:PRK12778 599 IVYrrseeemparleevKHAKEEGIEFLTLHNPIEYLADEKGWV-KQVVLQKMelgEPDASGRRRPVAIPGSTFTVdvDL 677
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500021004 256 IIWAIGRK--PVITGlqiEKAGVELLESGHIAVDKFQNTNVEGIYAVGD-VTGHYELTpVAIAAGRR 319
Cdd:PRK12778 678 VIVSVGVSpnPLVPS---SIPGLELNRKGTIVVDEEMQSSIPGIYAGGDiVRGGATVI-LAMGDGKR 740
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
132-319 4.78e-05

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 45.56  E-value: 4.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 132 DHILIATG-GEPVLPSIPGAEYG--------ITS----DGFFALkELPKKVAVIGAGYIAVELAGVLQQLGSE-THLFVR 197
Cdd:PRK11749 227 DAVFIGTGaGLPRFLGIPGENLGgvysavdfLTRvnqaVADYDL-PVGKRVVVIGGGNTAMDAARTAKRLGAEsVTIVYR 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 198 K---HAPLRNFDplltdtlTEIIEQSDMMLHKHAVPQKVEKNSDGS---------LTLSLEDGR----------TETVDT 255
Cdd:PRK11749 306 RgreEMPASEEE-------VEHAKEEGVEFEWLAAPVEILGDEGRVtgvefvrmeLGEPDASGRrrvpiegsefTLPADL 378
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500021004 256 IIWAIGRKPVITGLQ-IEKAGVELlESGHIAVDKFQNTNVEGIYAVGDVTGHYELTPVAIAAGRR 319
Cdd:PRK11749 379 VIKAIGQTPNPLILStTPGLELNR-WGTIIADDETGRTSLPGVFAGGDIVTGAATVVWAVGDGKD 442
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
125-304 2.68e-04

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 43.22  E-value: 2.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 125 NGEIVTADHILIATGGEPVLPSIPG-AEY---GIT----SDG-FFAlkelPKKVAVIGAGYIAVE----LAGVLqqlgse 191
Cdd:PRK15317 305 NGAVLKAKTVILATGARWRNMNVPGeDEYrnkGVAycphCDGpLFK----GKRVAVIGGGNSGVEaaidLAGIV------ 374
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500021004 192 thlfvrKHAPLRNFDP------LLTDTL-----TEIIeqsdmmlhKHAVPQKVEKNSDGSLTLSLEDGRTETVDTIIWA- 259
Cdd:PRK15317 375 ------KHVTVLEFAPelkadqVLQDKLrslpnVTII--------TNAQTTEVTGDGDKVTGLTYKDRTTGEEHHLELEg 440
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 500021004 260 ----IGRKPVITGLqieKAGVELLESGHIAVDKFQNTNVEGIYAVGDVT 304
Cdd:PRK15317 441 vfvqIGLVPNTEWL---KGTVELNRRGEIIVDARGATSVPGVFAAGDCT 486
 
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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