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Conserved domains on  [gi|495128029|ref|WP_007852840|]
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MULTISPECIES: glutathione-disulfide reductase [Cronobacter]

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
1-450 0e+00

glutathione reductase; Validated


:

Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 911.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029   1 MTRHYDYLAIGGGSGGIASVNRAAMYGQKCALIEAKALGGTCVNVGCVPKKIMWHAAQIAEAIHLYGPDYGFDTTVNHFD 80
Cdd:PRK06116   1 MTKDYDLIVIGGGSGGIASANRAAMYGAKVALIEAKRLGGTCVNVGCVPKKLMWYGAQIAEAFHDYAPGYGFDVTENKFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  81 WQKLVASRTAYIDRIHTSYDNVLGKNNVDVIQGFARFVDAHTVEVNGERITADHILIATGGRPSHPDIPGAEYGIDSDGF 160
Cdd:PRK06116  81 WAKLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNGERYTADHILIATGGRPSIPDIPGAEYGITSDGF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 161 FALSAMPQRVAVVGAGYIAVELAGVINALGAKTHLFVRKHAPLRTFDPMLSETLVEVMQAEGPQLHTHATPKAVEKNSDG 240
Cdd:PRK06116 161 FALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 241 SLTLHLEDGRSETVDALIWAIGREPETDNFNLAATGVKTNEKGYIVVDKYQNTNVPGIYAVGDNTGAVELTPVAVAAGRR 320
Cdd:PRK06116 241 SLTLTLEDGETLTVDCLIWAIGREPNTDGLGLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGDVTGRVELTPVAIAAGRR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 321 LSERLFNNKPDEHLDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDANVKIYKSSFTAMYTAVTTHRQPCRMKLVCVGPEE 400
Cdd:PRK06116 321 LSERLFNNKPDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVKVYRSSFTPMYTALTGHRQPCLMKLVVVGKEE 400
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 495128029 401 KIVGIHGIGFGMDEMLQGFAVALKMGATKKDFDNTVAIHPTAAEEFVTMR 450
Cdd:PRK06116 401 KVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFVTMR 450
 
Name Accession Description Interval E-value
PRK06116 PRK06116
glutathione reductase; Validated
1-450 0e+00

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 911.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029   1 MTRHYDYLAIGGGSGGIASVNRAAMYGQKCALIEAKALGGTCVNVGCVPKKIMWHAAQIAEAIHLYGPDYGFDTTVNHFD 80
Cdd:PRK06116   1 MTKDYDLIVIGGGSGGIASANRAAMYGAKVALIEAKRLGGTCVNVGCVPKKLMWYGAQIAEAFHDYAPGYGFDVTENKFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  81 WQKLVASRTAYIDRIHTSYDNVLGKNNVDVIQGFARFVDAHTVEVNGERITADHILIATGGRPSHPDIPGAEYGIDSDGF 160
Cdd:PRK06116  81 WAKLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNGERYTADHILIATGGRPSIPDIPGAEYGITSDGF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 161 FALSAMPQRVAVVGAGYIAVELAGVINALGAKTHLFVRKHAPLRTFDPMLSETLVEVMQAEGPQLHTHATPKAVEKNSDG 240
Cdd:PRK06116 161 FALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 241 SLTLHLEDGRSETVDALIWAIGREPETDNFNLAATGVKTNEKGYIVVDKYQNTNVPGIYAVGDNTGAVELTPVAVAAGRR 320
Cdd:PRK06116 241 SLTLTLEDGETLTVDCLIWAIGREPNTDGLGLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGDVTGRVELTPVAIAAGRR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 321 LSERLFNNKPDEHLDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDANVKIYKSSFTAMYTAVTTHRQPCRMKLVCVGPEE 400
Cdd:PRK06116 321 LSERLFNNKPDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVKVYRSSFTPMYTALTGHRQPCLMKLVVVGKEE 400
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 495128029 401 KIVGIHGIGFGMDEMLQGFAVALKMGATKKDFDNTVAIHPTAAEEFVTMR 450
Cdd:PRK06116 401 KVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFVTMR 450
gluta_reduc_1 TIGR01421
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ...
3-450 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: 685.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029    3 RHYDYLAIGGGSGGIASVNRAAMYGQKCALIEAKALGGTCVNVGCVPKKIMWHAAQIAEAIHlYGPDYGFDTTV-NHFDW 81
Cdd:TIGR01421   1 KHYDYLVIGGGSGGIASARRAAEHGAKALLVEAKKLGGTCVNVGCVPKKVMWYASDLAERMH-DAADYGFYQNDeNTFNW 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029   82 QKLVASRTAYIDRIHTSYDNVLGKNNVDVIQGFARFVDAHTVEVNGERITADHILIATGGRPSHPD-IPGAEYGIDSDGF 160
Cdd:TIGR01421  80 PELKEKRDAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVNGRDYTAPHILIATGGKPSFPEnIPGAELGTDSDGF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  161 FALSAMPQRVAVVGAGYIAVELAGVINALGAKTHLFVRKHAPLRTFDPMLSETLVEVMQAEGPQLHTHATPKAVEKNSDG 240
Cdd:TIGR01421 160 FALEELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRHERVLRSFDSMISETITEEYEKEGINVHKLSKPVKVEKTVEG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  241 SLTLHLEDGR-SETVDALIWAIGREPETDNFNLAATGVKTNEKGYIVVDKYQNTNVPGIYAVGDNTGAVELTPVAVAAGR 319
Cdd:TIGR01421 240 KLVIHFEDGKsIDDVDELIWAIGRKPNTKGLGLENVGIKLNEKGQIIVDEYQNTNVPGIYALGDVVGKVELTPVAIAAGR 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  320 RLSERLFNNKPDEHLDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDANVKIYKSSFTAMYTAVTTHRQPCRMKLVCVGPE 399
Cdd:TIGR01421 320 KLSERLFNGKTDDKLDYNNVPTVVFSHPPIGTIGLTEKEAIEKYGKENIKVYNSSFTPMYYAMTSEKQKCRMKLVCAGKE 399
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 495128029  400 EKIVGIHGIGFGMDEMLQGFAVALKMGATKKDFDNTVAIHPTAAEEFVTMR 450
Cdd:TIGR01421 400 EKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEELVTMR 450
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
22-450 1.10e-180

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: 512.32  E-value: 1.10e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  22 RAAMYGQKCALIEAKALGGTCVNVGCVPKKIMWHAAQIAEAIHlYGPDYGFDTTVNHFDWQKLVASRTAYIDRIHTSYDN 101
Cdd:COG1249   21 RAAQLGLKVALVEKGRLGGTCLNVGCIPSKALLHAAEVAHEAR-HAAEFGISAGAPSVDWAALMARKDKVVDRLRGGVEE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 102 VLGKNNVDVIQGFARFVDAHTVEVNG-ERITADHILIATGGRPSHPDIPGA--EYGIDSDGFFALSAMPQRVAVVGAGYI 178
Cdd:COG1249  100 LLKKNGVDVIRGRARFVDPHTVEVTGgETLTADHIVIATGSRPRVPPIPGLdeVRVLTSDEALELEELPKSLVVIGGGYI 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 179 AVELAGVINALGAKTHLFVRKHAPLRTFDPMLSETLVEVMQAEGPQLHTHATPKAVEKNSDGsLTLHLEDGRSET---VD 255
Cdd:COG1249  180 GLEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDG-VTVTLEDGGGEEaveAD 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 256 ALIWAIGREPETDNFNLAATGVKTNEKGYIVVDKYQNTNVPGIYAVGDNTGAVELTPVAVAAGRRLSERLFNNKPdEHLD 335
Cdd:COG1249  259 KVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRTSVPGIYAIGDVTGGPQLAHVASAEGRVAAENILGKKP-RPVD 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 336 YSNIPTVVFSHPPIGTVGLTEPQAREQYGDanVKIYKSSFTAMYTAVTTHRQPCRMKLVCVGPEEKIVGIHGIGFGMDEM 415
Cdd:COG1249  338 YRAIPSVVFTDPEIASVGLTEEEAREAGID--VKVGKFPFAANGRALALGETEGFVKLIADAETGRILGAHIVGPHAGEL 415
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 495128029 416 LQGFAVALKMGATKKDFDNTVAIHPTAAEEFVTMR 450
Cdd:COG1249  416 IHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAA 450
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
22-318 5.62e-76

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: 239.53  E-value: 5.62e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029   22 RAAMYGQKCALIEakaLGGTCVNVGCVPKKIMWHAAQIAEAIHLygpdygfdttvnhfdWQKLVASRTAYIDRIHTSYDN 101
Cdd:pfam07992  18 TLAQLGGKVTLIE---DEGTCPYGGCVLSKALLGAAEAPEIASL---------------WADLYKRKEEVVKKLNNGIEV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  102 VLGKNNVDVIQGFARFVDAHTVEVNGERITADHILIATGGRPSHPDIPGAEYG-------IDSDGFFALSAMPQRVAVVG 174
Cdd:pfam07992  80 LLGTEVVSIDPGAKKVVLEELVDGDGETITYDRLVIATGARPRLPPIPGVELNvgflvrtLDSAEALRLKLLPKRVVVVG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  175 AGYIAVELAGVINALGAKTHLFVRKHAPLRTFDPMLSETLVEVMQAEGPQLHTHATPKAVEKNSDGsLTLHLEDGRSETV 254
Cdd:pfam07992 160 GGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDG-VEVILKDGTEIDA 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495128029  255 DALIWAIGREPETDnfNLAATGVKTNEKGYIVVDKYQNTNVPGIYAVGDNT-GAVELTPVAVAAG 318
Cdd:pfam07992 239 DLVVVAIGRRPNTE--LLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDCRvGGPELAQNAVAQG 301
 
Name Accession Description Interval E-value
PRK06116 PRK06116
glutathione reductase; Validated
1-450 0e+00

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 911.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029   1 MTRHYDYLAIGGGSGGIASVNRAAMYGQKCALIEAKALGGTCVNVGCVPKKIMWHAAQIAEAIHLYGPDYGFDTTVNHFD 80
Cdd:PRK06116   1 MTKDYDLIVIGGGSGGIASANRAAMYGAKVALIEAKRLGGTCVNVGCVPKKLMWYGAQIAEAFHDYAPGYGFDVTENKFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  81 WQKLVASRTAYIDRIHTSYDNVLGKNNVDVIQGFARFVDAHTVEVNGERITADHILIATGGRPSHPDIPGAEYGIDSDGF 160
Cdd:PRK06116  81 WAKLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNGERYTADHILIATGGRPSIPDIPGAEYGITSDGF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 161 FALSAMPQRVAVVGAGYIAVELAGVINALGAKTHLFVRKHAPLRTFDPMLSETLVEVMQAEGPQLHTHATPKAVEKNSDG 240
Cdd:PRK06116 161 FALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 241 SLTLHLEDGRSETVDALIWAIGREPETDNFNLAATGVKTNEKGYIVVDKYQNTNVPGIYAVGDNTGAVELTPVAVAAGRR 320
Cdd:PRK06116 241 SLTLTLEDGETLTVDCLIWAIGREPNTDGLGLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGDVTGRVELTPVAIAAGRR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 321 LSERLFNNKPDEHLDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDANVKIYKSSFTAMYTAVTTHRQPCRMKLVCVGPEE 400
Cdd:PRK06116 321 LSERLFNNKPDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVKVYRSSFTPMYTALTGHRQPCLMKLVVVGKEE 400
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 495128029 401 KIVGIHGIGFGMDEMLQGFAVALKMGATKKDFDNTVAIHPTAAEEFVTMR 450
Cdd:PRK06116 401 KVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFVTMR 450
gluta_reduc_1 TIGR01421
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ...
3-450 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: 685.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029    3 RHYDYLAIGGGSGGIASVNRAAMYGQKCALIEAKALGGTCVNVGCVPKKIMWHAAQIAEAIHlYGPDYGFDTTV-NHFDW 81
Cdd:TIGR01421   1 KHYDYLVIGGGSGGIASARRAAEHGAKALLVEAKKLGGTCVNVGCVPKKVMWYASDLAERMH-DAADYGFYQNDeNTFNW 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029   82 QKLVASRTAYIDRIHTSYDNVLGKNNVDVIQGFARFVDAHTVEVNGERITADHILIATGGRPSHPD-IPGAEYGIDSDGF 160
Cdd:TIGR01421  80 PELKEKRDAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVNGRDYTAPHILIATGGKPSFPEnIPGAELGTDSDGF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  161 FALSAMPQRVAVVGAGYIAVELAGVINALGAKTHLFVRKHAPLRTFDPMLSETLVEVMQAEGPQLHTHATPKAVEKNSDG 240
Cdd:TIGR01421 160 FALEELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRHERVLRSFDSMISETITEEYEKEGINVHKLSKPVKVEKTVEG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  241 SLTLHLEDGR-SETVDALIWAIGREPETDNFNLAATGVKTNEKGYIVVDKYQNTNVPGIYAVGDNTGAVELTPVAVAAGR 319
Cdd:TIGR01421 240 KLVIHFEDGKsIDDVDELIWAIGRKPNTKGLGLENVGIKLNEKGQIIVDEYQNTNVPGIYALGDVVGKVELTPVAIAAGR 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  320 RLSERLFNNKPDEHLDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDANVKIYKSSFTAMYTAVTTHRQPCRMKLVCVGPE 399
Cdd:TIGR01421 320 KLSERLFNGKTDDKLDYNNVPTVVFSHPPIGTIGLTEKEAIEKYGKENIKVYNSSFTPMYYAMTSEKQKCRMKLVCAGKE 399
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 495128029  400 EKIVGIHGIGFGMDEMLQGFAVALKMGATKKDFDNTVAIHPTAAEEFVTMR 450
Cdd:TIGR01421 400 EKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEELVTMR 450
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
22-450 1.10e-180

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: 512.32  E-value: 1.10e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  22 RAAMYGQKCALIEAKALGGTCVNVGCVPKKIMWHAAQIAEAIHlYGPDYGFDTTVNHFDWQKLVASRTAYIDRIHTSYDN 101
Cdd:COG1249   21 RAAQLGLKVALVEKGRLGGTCLNVGCIPSKALLHAAEVAHEAR-HAAEFGISAGAPSVDWAALMARKDKVVDRLRGGVEE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 102 VLGKNNVDVIQGFARFVDAHTVEVNG-ERITADHILIATGGRPSHPDIPGA--EYGIDSDGFFALSAMPQRVAVVGAGYI 178
Cdd:COG1249  100 LLKKNGVDVIRGRARFVDPHTVEVTGgETLTADHIVIATGSRPRVPPIPGLdeVRVLTSDEALELEELPKSLVVIGGGYI 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 179 AVELAGVINALGAKTHLFVRKHAPLRTFDPMLSETLVEVMQAEGPQLHTHATPKAVEKNSDGsLTLHLEDGRSET---VD 255
Cdd:COG1249  180 GLEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDG-VTVTLEDGGGEEaveAD 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 256 ALIWAIGREPETDNFNLAATGVKTNEKGYIVVDKYQNTNVPGIYAVGDNTGAVELTPVAVAAGRRLSERLFNNKPdEHLD 335
Cdd:COG1249  259 KVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRTSVPGIYAIGDVTGGPQLAHVASAEGRVAAENILGKKP-RPVD 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 336 YSNIPTVVFSHPPIGTVGLTEPQAREQYGDanVKIYKSSFTAMYTAVTTHRQPCRMKLVCVGPEEKIVGIHGIGFGMDEM 415
Cdd:COG1249  338 YRAIPSVVFTDPEIASVGLTEEEAREAGID--VKVGKFPFAANGRALALGETEGFVKLIADAETGRILGAHIVGPHAGEL 415
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 495128029 416 LQGFAVALKMGATKKDFDNTVAIHPTAAEEFVTMR 450
Cdd:COG1249  416 IHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAA 450
PTZ00058 PTZ00058
glutathione reductase; Provisional
5-449 2.59e-154

glutathione reductase; Provisional


Pssm-ID: 185420 [Multi-domain]  Cd Length: 561  Bit Score: 449.07  E-value: 2.59e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029   5 YDYLAIGGGSGGIASVNRAAMYGQKCALIEAKALGGTCVNVGCVPKKIMWHAAQIAEAIHLYGpDYGFDTTVNhFDWQKL 84
Cdd:PTZ00058  49 YDLIVIGGGSGGMAAARRAARNKAKVALVEKDYLGGTCVNVGCVPKKIMFNAASIHDILENSR-HYGFDTQFS-FNLPLL 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  85 VASRTAYIDRIHTSYDNVLGKNNVDVIQGFARFVDAHTVEV-----------------------------NGERITADHI 135
Cdd:PTZ00058 127 VERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLIkkvsqvdgeadesdddevtivsagvsqldDGQVIEGKNI 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 136 LIATGGRPSHPDIPGAEYGIDSDGFFALSAmPQRVAVVGAGYIAVELAGVINALGAKTHLFVRKHAPLRTFDPMLSETLV 215
Cdd:PTZ00058 207 LIAVGNKPIFPDVKGKEFTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLRKFDETIINELE 285
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 216 EVMQAEGPQLHTHATPKAVEKNSDGSLTLHLEDGRS-ETVDALIWAIGREPETDNFNLAATGVKTnEKGYIVVDKYQNTN 294
Cdd:PTZ00058 286 NDMKKNNINIITHANVEEIEKVKEKNLTIYLSDGRKyEHFDYVIYCVGRSPNTEDLNLKALNIKT-PKGYIKVDDNQRTS 364
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 295 VPGIYAVGDNTGA----------------------------------VELTPVAVAAGRRLSERLFNNKPDEHlDYSNIP 340
Cdd:PTZ00058 365 VKHIYAVGDCCMVkknqeiedlnllklyneepylkkkentsgesyynVQLTPVAINAGRLLADRLFGPFSRTT-NYKLIP 443
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 341 TVVFSHPPIGTVGLTEPQAREQYGDANVKIYKSSFTAMYTAV----TTHRQPCRMKLVCVGPEEKIVGIHGIGFGMDEML 416
Cdd:PTZ00058 444 SVIFSHPPIGTIGLSEQEAIDIYGKENVKIYESRFTNLFFSVydmdPAQKEKTYLKLVCVGKEELIKGLHIVGLNADEIL 523
                        490       500       510
                 ....*....|....*....|....*....|...
gi 495128029 417 QGFAVALKMGATKKDFDNTVAIHPTAAEEFVTM 449
Cdd:PTZ00058 524 QGFAVALKMNATKADFDETIPIHPTAAEEFVTM 556
PLN02546 PLN02546
glutathione reductase
3-450 1.63e-138

glutathione reductase


Pssm-ID: 215301 [Multi-domain]  Cd Length: 558  Bit Score: 408.88  E-value: 1.63e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029   3 RHYDY-LAIGGGSGGIASVNR-AAMYGQKCALIE----------AKALGGTCVNVGCVPKKIMWHAAQIAeaiHLYGPDY 70
Cdd:PLN02546  76 RHYDFdLFTIGAGSGGVRASRfASNFGASAAVCElpfatissdtLGGVGGTCVLRGCVPKKLLVYASKYS---HEFEESR 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  71 GF----DTTVNHfDWQKLVASRTAYIDRIHTSYDNVLGKNNVDVIQGFARFVDAHTVEVNGERITADHILIATGGRPSHP 146
Cdd:PLN02546 153 GFgwkyETEPKH-DWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDVDGKLYTARNILIAVGGRPFIP 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 147 DIPGAEYGIDSDGFFALSAMPQRVAVVGAGYIAVELAGVINALGAKTHLFVRKHAPLRTFDPMLSETLVEVMQAEGPQLH 226
Cdd:PLN02546 232 DIPGIEHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKKVLRGFDEEVRDFVAEQMSLRGIEFH 311
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 227 THATPKAVEKNSDGSLTLHLEDGRSETVDALIWAIGREPETDNFNLAATGVKTNEKGYIVVDKYQNTNVPGIYAVGDNTG 306
Cdd:PLN02546 312 TEESPQAIIKSADGSLSLKTNKGTVEGFSHVMFATGRKPNTKNLGLEEVGVKMDKNGAIEVDEYSRTSVPSIWAVGDVTD 391
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 307 AVELTPVAVAAGRRLSERLFNNKPDEHlDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDanVKIYKSSFTAMYTAVTTHR 386
Cdd:PLN02546 392 RINLTPVALMEGGALAKTLFGNEPTKP-DYRAVPSAVFSQPPIGQVGLTEEQAIEEYGD--VDVFTANFRPLKATLSGLP 468
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495128029 387 QPCRMKLVCVGPEEKIVGIHGIGFGMDEMLQGFAVALKMGATKKDFDNTVAIHPTAAEEFVTMR 450
Cdd:PLN02546 469 DRVFMKLIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEEFVTMR 532
gluta_reduc_2 TIGR01424
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ...
22-450 1.22e-137

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: 402.65  E-value: 1.22e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029   22 RAAMYGQKCALIEAKALGGTCVNVGCVPKKIMWHAAQIAEAIHlYGPDYGFDTTVNHFDWQKLVASRTAYIDRIHTSYDN 101
Cdd:TIGR01424  20 LAAALGAKVAIAEEFRVGGTCVIRGCVPKKLMVYASQFAEHFE-DAAGYGWTVGKARFDWKKLLAAKDQEIARLSGLYRK 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  102 VLGKNNVDVIQGFARFVDAHTVEV--NGERITADHILIATGGRPSHPDIPGAEYGIDSDGFFALSAMPQRVAVVGAGYIA 179
Cdd:TIGR01424  99 GLANAGAELLDGRAELVGPNTVEVlaSGKTYTAEKILIAVGGRPPKPALPGHELGITSNEAFHLPTLPKSILIAGGGYIA 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  180 VELAGVINALGAKTHLFVRKHAPLRTFDPMLSETLVEVMQAEGPQLHTHATPKAVEKNSDGSLTLHLEDGRSETVDALIW 259
Cdd:TIGR01424 179 VEFAGIFRGLGVQTTLIYRGKEILRGFDDDMRRGLAAALEERGIRILPEDSITSISKDDDGRLKATLSKHEEIVADVVLF 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  260 AIGREPETDNFNLAATGVKTNEKGYIVVDKYQNTNVPGIYAVGDNTGAVELTPVAVAAGRRLSERLFNNKPDEhLDYSNI 339
Cdd:TIGR01424 259 ATGRSPNTNGLGLEAAGVRLNDLGAIAVDEYSRTSTPSIYAVGDVTDRINLTPVAIHEATCFAETEFGNNPTS-FDHDLI 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  340 PTVVFSHPPIGTVGLTEPQAREQYGDanVKIYKSSFTAMYTAVTTHRQPCRMKLVCVGPEEKIVGIHGIGFGMDEMLQGF 419
Cdd:TIGR01424 338 ATAVFSQPPIGTVGLTEEEARRKFGD--IEVYRAEFRPMKATFSGRQEKTLMKLVVDAKDDKVLGAHMVGPDAAEIIQGL 415
                         410       420       430
                  ....*....|....*....|....*....|.
gi 495128029  420 AVALKMGATKKDFDNTVAIHPTAAEEFVTMR 450
Cdd:TIGR01424 416 AIALKMGATKDDFDSTVAVHPTSAEELVTMR 446
TGR TIGR01438
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ...
5-449 6.48e-118

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: 353.39  E-value: 6.48e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029    5 YDYLAIGGGSGGIASVNRAAMYGQKCALIEAK---------ALGGTCVNVGCVPKKIMWHAAQIAEAIHlYGPDYG--FD 73
Cdd:TIGR01438   3 YDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVtptplgtrwGIGGTCVNVGCIPKKLMHQAALLGQALK-DSRNYGwkVE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029   74 TTVNHfDWQKLVASRTAYIDRIHTSYDNVLGKNNVDVIQGFARFVDAHTVEV---NG--ERITADHILIATGGRPSHPDI 148
Cdd:TIGR01438  82 ETVKH-DWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKAtnkKGkeKIYSAERFLIATGERPRYPGI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  149 PGA-EYGIDSDGFFALSAMPQRVAVVGAGYIAVELAGVINALGAKTHLFVRKhAPLRTFDPMLSETLVEVMQAEGPQLHT 227
Cdd:TIGR01438 161 PGAkELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRS-ILLRGFDQDCANKVGEHMEEHGVKFKR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  228 HATPKAVEKNSDGSLT--LHLEDGRSETVDALIWAIGREPETDNFNLAATGVKTNEK-GYIVVDKYQNTNVPGIYAVGD- 303
Cdd:TIGR01438 240 QFVPIKVEQIEAKVLVefTDSTNGIEEEYDTVLLAIGRDACTRKLNLENVGVKINKKtGKIPADEEEQTNVPYIYAVGDi 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  304 NTGAVELTPVAVAAGRRLSERLFNNKpDEHLDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDANVKIYKSSFTAM-YTAV 382
Cdd:TIGR01438 320 LEDKPELTPVAIQAGRLLAQRLFKGS-TVICDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENVEVFHSYFWPLeWTIP 398
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495128029  383 ttHRQP---CRMKLVCVGPE-EKIVGIHGIGFGMDEMLQGFAVALKMGATKKDFDNTVAIHPTAAEEFVTM 449
Cdd:TIGR01438 399 --SRDNhnkCYAKLVCNKKEnERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTL 467
PLN02507 PLN02507
glutathione reductase
23-450 1.17e-116

glutathione reductase


Pssm-ID: 215281 [Multi-domain]  Cd Length: 499  Bit Score: 350.66  E-value: 1.17e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  23 AAMYGQKCALIE----------AKALGGTCVNVGCVPKKIMWHAAQIAEAIHlYGPDYGFDttVNH---FDWQKLVASRT 89
Cdd:PLN02507  44 SANFGAKVGICElpfhpissesIGGVGGTCVIRGCVPKKILVYGATFGGEFE-DAKNYGWE--INEkvdFNWKKLLQKKT 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  90 AYIDRIHTSYDNVLGKNNVDVIQGFARFVDAHTVEV---NGE--RITADHILIATGGRPSHPDIPGAEYGIDSDGFFALS 164
Cdd:PLN02507 121 DEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVtqlDGTklRYTAKHILIATGSRAQRPNIPGKELAITSDEALSLE 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 165 AMPQRVAVVGAGYIAVELAGVINALGAKTHLFVRKHAPLRTFDPMLSETLVEVMQAEGPQLHTHATPKAVEKNSDGsLTL 244
Cdd:PLN02507 201 ELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRAVVARNLEGRGINLHPRTNLTQLTKTEGG-IKV 279
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 245 HLEDGRSETVDALIWAIGREPETDNFNLAATGVKTNEKGYIVVDKYQNTNVPGIYAVGDNTGAVELTPVAVAAGRRLSER 324
Cdd:PLN02507 280 ITDHGEEFVADVVLFATGRAPNTKRLNLEAVGVELDKAGAVKVDEYSRTNIPSIWAIGDVTNRINLTPVALMEGTCFAKT 359
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 325 LFNNKPDEHlDYSNIPTVVFSHPPIGTVGLTEPQAREQyGDANVKIYKSSFTAMYTAVTTHRQPCRMKLVCVGPEEKIVG 404
Cdd:PLN02507 360 VFGGQPTKP-DYENVACAVFCIPPLSVVGLSEEEAVEQ-AKGDILVFTSSFNPMKNTISGRQEKTVMKLIVDAETDKVLG 437
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 495128029 405 IHGIGFGMDEMLQGFAVALKMGATKKDFDNTVAIHPTAAEEFVTMR 450
Cdd:PLN02507 438 ASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEFVTMR 483
PTZ00052 PTZ00052
thioredoxin reductase; Provisional
5-446 2.47e-114

thioredoxin reductase; Provisional


Pssm-ID: 185416 [Multi-domain]  Cd Length: 499  Bit Score: 344.88  E-value: 2.47e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029   5 YDYLAIGGGSGGIASVNRAAMYGQKCALIE---------AKALGGTCVNVGCVPKKIMWHAAQIAEAIHLYGPDYGFDTT 75
Cdd:PTZ00052   6 YDLVVIGGGSGGMAAAKEAAAHGKKVALFDyvkpstqgtKWGLGGTCVNVGCVPKKLMHYAANIGSIFHHDSQMYGWKTS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  76 vNHFDWQKLVASRTAYIDRIHTSYDNVLGKNNVDVIQGFARFVDAHTVEVNG----ERITADHILIATGGRPSHP-DIPG 150
Cdd:PTZ00052  86 -SSFNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTVSYGDnsqeETITAKYILIATGGRPSIPeDVPG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 151 A-EYGIDSDGFFALSAMPQRVAVVGAGYIAVELAGVINALGAKTHLFVRKhAPLRTFDPMLSETLVEVMQAEGPQLHTHA 229
Cdd:PTZ00052 165 AkEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRS-IPLRGFDRQCSEKVVEYMKEQGTLFLEGV 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 230 TPKAVEKNSDgSLTLHLEDGRSETVDALIWAIGREPETDNFNLAATGVKTNEKGYIVVDKyQNTNVPGIYAVGD-NTGAV 308
Cdd:PTZ00052 244 VPINIEKMDD-KIKVLFSDGTTELFDTVLYATGRKPDIKGLNLNAIGVHVNKSNKIIAPN-DCTNIPNIFAVGDvVEGRP 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 309 ELTPVAVAAGRRLSERLFNNKpDEHLDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDANVKIYKSSFTAMYTAvTTHRQP 388
Cdd:PTZ00052 322 ELTPVAIKAGILLARRLFKQS-NEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQEFNTLEIA-AVHREK 399
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495128029 389 ----------------CRMKLVCVGPE-EKIVGIHGIGFGMDEMLQGFAVALKMGATKKDFDNTVAIHPTAAEEF 446
Cdd:PTZ00052 400 herarkdeydfdvssnCLAKLVCVKSEdNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHPTDAEVF 474
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
21-450 1.04e-108

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: 330.01  E-value: 1.04e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029   21 NRAAMYGQKCALIEAK---------ALGGTCVNVGCVPKKIMWHAAQIAEAI-HLYGPDYGFDTTVNHFDWQKLVASRTA 90
Cdd:TIGR01423  21 NAATLYKKRVAVVDVQthhgppfyaALGGTCVNVGCVPKKLMVTGAQYMDTLrESAGFGWEFDRSSVKANWKALIAAKNK 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029   91 YIDRIHTSYDNVLGKNN-VDVIQGFARFVDAHTVEVNG---------ERITADHILIATGGRPSHPDIPGAEYGIDSDGF 160
Cdd:TIGR01423 101 AVLDINKSYEGMFADTEgLTFFLGWGALEDKNVVLVREsadpksavkERLQAEHILLATGSWPQMLGIPGIEHCISSNEA 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  161 FALSAMPQRVAVVGAGYIAVELAGVINA---LGAKTHLFVRKHAPLRTFDPMLSETLVEVMQAEGPQLHTHATPKAVEKN 237
Cdd:TIGR01423 181 FYLDEPPRRVLTVGGGFISVEFAGIFNAykpRGGKVTLCYRNNMILRGFDSTLRKELTKQLRANGINIMTNENPAKVTLN 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  238 SDGSLTLHLEDGRSETVDALIWAIGREPETDNFNLAATGVKTNEKGYIVVDKYQNTNVPGIYAVGDNTGAVELTPVAVAA 317
Cdd:TIGR01423 261 ADGSKHVTFESGKTLDVDVVMMAIGRVPRTQTLQLDKVGVELTKKGAIQVDEFSRTNVPNIYAIGDVTDRVMLTPVAINE 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  318 GRRLSERLFNNKPdEHLDYSNIPTVVFSHPPIGTVGLTEPQAREQYgdANVKIYKSSFTA-MYTAVTTHRQPCRMKLVCV 396
Cdd:TIGR01423 341 GAAFVDTVFGNKP-RKTDHTRVASAVFSIPPIGTCGLVEEDAAKKF--EKVAVYESSFTPlMHNISGSKYKKFVAKIVTN 417
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 495128029  397 GPEEKIVGIHGIGFGMDEMLQGFAVALKMGATKKDFDNTVAIHPTAAEEFVTMR 450
Cdd:TIGR01423 418 HADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAEELCSMR 471
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
22-444 4.74e-100

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 306.72  E-value: 4.74e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  22 RAAMYGQKCALIEAKALGGTCVNVGCVPKKIMWHAAQIAEAIHlYGPDYGFDTTVNHFDWQKLVASRTAYIDRIHTS-YD 100
Cdd:PRK06292  21 RAAKLGKKVALIEKGPLGGTCLNVGCIPSKALIAAAEAFHEAK-HAEEFGIHADGPKIDFKKVMARVRRERDRFVGGvVE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 101 NVLGKNNVDVIQGFARFVDAHTVEVNGERITADHILIATGGRPshPDIPGAEYG-----IDSDGFFALSAMPQRVAVVGA 175
Cdd:PRK06292 100 GLEKKPKIDKIKGTARFVDPNTVEVNGERIEAKNIVIATGSRV--PPIPGVWLIlgdrlLTSDDAFELDKLPKSLAVIGG 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 176 GYIAVELAGVINALGAKTHLFVRKHAPLRTFDPMLSETLVEVMQAEGPqLHTHATPKAVEKNSDGSLTLHLEDG--RSET 253
Cdd:PRK06292 178 GVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILSKEFK-IKLGAKVTSVEKSGDEKVEELEKGGktETIE 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 254 VDALIWAIGREPETDNFNLAATGVKTNEKGYIVVDKYQNTNVPGIYAVGDNTGAVELTPVAVAAGRRLSERLFNNKPDeH 333
Cdd:PRK06292 257 ADYVLVATGRRPNTDGLGLENTGIELDERGRPVVDEHTQTSVPGIYAAGDVNGKPPLLHEAADEGRIAAENAAGDVAG-G 335
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 334 LDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDANVKIYksSFTAMYTAVTTHRQPCRMKLVCVGPEEKIVGIHGIGFGMD 413
Cdd:PRK06292 336 VRYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEV--PFEAQGRARVMGKNDGFVKVYADKKTGRLLGAHIIGPDAE 413
                        410       420       430
                 ....*....|....*....|....*....|.
gi 495128029 414 EMLQGFAVALKMGATKKDFDNTVAIHPTAAE 444
Cdd:PRK06292 414 HLIHLLAWAMQQGLTVEDLLRMPFYHPTLSE 444
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
22-444 4.92e-100

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 306.69  E-value: 4.92e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  22 RAAMYGQKCALIEAKALGGTCVNVGCVPKKIMWHAAQIA-EAIHLygPDYGFDTTVNHFDWQKLVASRTAYIDRIHTSYD 100
Cdd:PRK06416  22 RAAQLGLKVAIVEKEKLGGTCLNRGCIPSKALLHAAERAdEARHS--EDFGIKAENVGIDFKKVQEWKNGVVNRLTGGVE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 101 NVLGKNNVDVIQGFARFVDAHTVEVN----GERITADHILIATGGRPShpDIPGAEYG----IDSDGFFALSAMPQRVAV 172
Cdd:PRK06416 100 GLLKKNKVDIIRGEAKLVDPNTVRVMtedgEQTYTAKNIILATGSRPR--ELPGIEIDgrviWTSDEALNLDEVPKSLVV 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 173 VGAGYIAVELAGVINALGAKT-------HLfvrkhapLRTFDPMLSETLVEVMQAEGPQLHTHATPKAVEKNSDGsLTLH 245
Cdd:PRK06416 178 IGGGYIGVEFASAYASLGAEVtivealpRI-------LPGEDKEISKLAERALKKRGIKIKTGAKAKKVEQTDDG-VTVT 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 246 LEDGRSE---TVDALIWAIGREPETDNFNLAATGVKTnEKGYIVVDKYQNTNVPGIYAVGDNTGAVELTPVAVAAGRRLS 322
Cdd:PRK06416 250 LEDGGKEetlEADYVLVAVGRRPNTENLGLEELGVKT-DRGFIEVDEQLRTNVPNIYAIGDIVGGPMLAHKASAEGIIAA 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 323 ERLFNNkpDEHLDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDanVKIYKSSFTAMYTAVTTHRQPCRMKLVCVGPEEKI 402
Cdd:PRK06416 329 EAIAGN--PHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFD--VKVVKFPFAGNGKALALGETDGFVKLIFDKKDGEV 404
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 495128029 403 VGIHGIGFGMDEMLQGFAVALKMGATKKDFDNTVAIHPTAAE 444
Cdd:PRK06416 405 LGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSE 446
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
22-444 3.83e-99

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: 304.57  E-value: 3.83e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029   22 RAAMYGQKCALIEAKALGGTCVNVGCVPKKIMWHAAQIAEAI-HLygPDYGFDTTVNHFDWQKLVASRTAYIDRIHTSYD 100
Cdd:TIGR01350  19 RAAQLGLKVALVEKEYLGGTCLNVGCIPTKALLHSAEVYDEIkHA--KDLGIEVENVSVDWEKMQKRKNKVVKKLVGGVS 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  101 NVLGKNNVDVIQGFARFVDAHTVEVNGER----ITADHILIATGGRPSHPDIP---GAEYGIDSDGFFALSAMPQRVAVV 173
Cdd:TIGR01350  97 GLLKKNKVTVIKGEAKFLDPGTVSVTGENgeetLEAKNIIIATGSRPRSLPGPfdfDGKVVITSTGALNLEEVPESLVII 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  174 GAGYIAVELAGVINALGAKTHLFVRKHAPLRTFDPMLSETLVEVMQAEGPQLHTHATPKAVEKNsDGSLTLHLEDGRSET 253
Cdd:TIGR01350 177 GGGVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEKN-DDQVTYENKGGETET 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  254 VDA---LIwAIGREPETDNFNLAATGVKTNEKGYIVVDKYQNTNVPGIYAVGDNTGAVELTPVAVAAGRRLSERLFnNKP 330
Cdd:TIGR01350 256 LTGekvLV-AVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDVIGGPMLAHVASHEGIVAAENIA-GKE 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  331 DEHLDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDanVKIYKSSFTAMYTAVTTHRQPCRMKLVcVGPE-EKIVGIHGIG 409
Cdd:TIGR01350 334 PAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGYD--VKIGKFPFAANGKALALGETDGFVKII-ADKKtGEILGAHIIG 410
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 495128029  410 FGMDEMLQGFAVALKMGATKKDFDNTVAIHPTAAE 444
Cdd:TIGR01350 411 PHATELISEAALAMELEGTVEELARTIHPHPTLSE 445
PRK06370 PRK06370
FAD-containing oxidoreductase;
22-444 5.03e-94

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 291.34  E-value: 5.03e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  22 RAAMYGQKCALIEAKALGGTCVNVGCVPKKIM---WHAAQIAEAIHLYGPDYGFDTTVnhfDWQKLVASRTAYIDRIHTS 98
Cdd:PRK06370  23 RAAGLGMKVALIERGLLGGTCVNTGCVPTKTLiasARAAHLARRAAEYGVSVGGPVSV---DFKAVMARKRRIRARSRHG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  99 YDNVL-GKNNVDVIQGFARFVDAHTVEVNGERITADHILIATGGRPSHPDIPG-AEYG-IDSDGFFALSAMPQRVAVVGA 175
Cdd:PRK06370 100 SEQWLrGLEGVDVFRGHARFESPNTVRVGGETLRAKRIFINTGARAAIPPIPGlDEVGyLTNETIFSLDELPEHLVIIGG 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 176 GYIAVELAGVINALGAKTHLFVRKHAPLRTFDPMLSETLVEVMQAEGPQLHTHATPKAVEKNSDG-SLTLHLEDGRSE-T 253
Cdd:PRK06370 180 GYIGLEFAQMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILEREGIDVRLNAECIRVERDGDGiAVGLDCNGGAPEiT 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 254 VDALIWAIGREPETDNFNLAATGVKTNEKGYIVVDKYQNTNVPGIYAVGDNTGAVELTPVAVAAGRRLSERLFNNKPdEH 333
Cdd:PRK06370 260 GSHILVAVGRVPNTDDLGLEAAGVETDARGYIKVDDQLRTTNPGIYAAGDCNGRGAFTHTAYNDARIVAANLLDGGR-RK 338
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 334 LDYSNIPTVVFSHPPIGTVGLTEPQAREQygDANVKIYKSSFTAMYTAVTTHRQPCRMKLVCVGPEEKIVGIHGIGFGMD 413
Cdd:PRK06370 339 VSDRIVPYATYTDPPLARVGMTEAEARKS--GRRVLVGTRPMTRVGRAVEKGETQGFMKVVVDADTDRILGATILGVHGD 416
                        410       420       430
                 ....*....|....*....|....*....|.
gi 495128029 414 EMLQGFAVALKMGATKKDFDNTVAIHPTAAE 444
Cdd:PRK06370 417 EMIHEILDAMYAGAPYTTLSRAIHIHPTVSE 447
MerA TIGR02053
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ...
22-444 3.74e-89

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: 278.92  E-value: 3.74e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029   22 RAAMYGQKCALIEAKALGGTCVNVGCVPKKIMWHAAQIAEAIHlyGPDYGFDTTVNHFDWQKLVASRTAYIDRI-HTSYD 100
Cdd:TIGR02053  18 KAAELGASVAMVERGPLGGTCVNVGCVPSKMLLRAAEVAHYAR--KPPFGGLAATVAVDFGELLEGKREVVEELrHEKYE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  101 NVLGKNNVDVIQGFARFVDAHTVEVNGERIT--ADHILIATGGRPSHPDIPG---AEYgIDSDGFFALSAMPQRVAVVGA 175
Cdd:TIGR02053  96 DVLSSYGVDYLRGRARFKDPKTVKVDLGREVrgAKRFLIATGARPAIPPIPGlkeAGY-LTSEEALALDRIPESLAVIGG 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  176 GYIAVELAGVINALGAKTHLFVRKHAPLRTFDPMLSETLVEVMQAEGPQLHTHATPKAVEKNSDGSL-TLHLEDGRSET- 253
Cdd:TIGR02053 175 GAIGVELAQAFARLGSEVTILQRSDRLLPREEPEISAAVEEALAEEGIEVVTSAQVKAVSVRGGGKIiTVEKPGGQGEVe 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  254 VDALIWAIGREPETDNFNLAATGVKTNEKGYIVVDKYQNTNVPGIYAVGDNTGAVELTPVAVAAGRRLSERLFNNkPDEH 333
Cdd:TIGR02053 255 ADELLVATGRRPNTDGLGLEKAGVKLDERGGILVDETLRTSNPGIYAAGDVTGGLQLEYVAAKEGVVAAENALGG-ANAK 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  334 LDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDANVKiykssfTAMYTAVT---THRQPCRM-KLVCVGPEEKIVGIHGIG 409
Cdd:TIGR02053 334 LDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCR------TLPLTNVPrarINRDTRGFiKLVAEPGTGKVLGVQVVA 407
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 495128029  410 FGMDEMLQGFAVALKMGATKKDFDNTVAIHPTAAE 444
Cdd:TIGR02053 408 PEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAE 442
PRK07846 PRK07846
mycothione reductase; Reviewed
27-444 7.91e-78

mycothione reductase; Reviewed


Pssm-ID: 181142 [Multi-domain]  Cd Length: 451  Bit Score: 249.10  E-value: 7.91e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  27 GQKCALIEAKALGGTCVNVGCVPKKIMWHAAQIAEAIHlYGPDYGFDTTVNHFDWQKLVaSRT-AYIDRIHTS---YdNV 102
Cdd:PRK07846  22 DKRIAIVEKGTFGGTCLNVGCIPTKMFVYAADVARTIR-EAARLGVDAELDGVRWPDIV-SRVfGRIDPIAAGgeeY-RG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 103 LGKNNVDVIQGFARFVDAHTVEV-NGERITADHILIATGGRPSHPDIPGAEyGID---SDGFFALSAMPQRVAVVGAGYI 178
Cdd:PRK07846  99 RDTPNIDVYRGHARFIGPKTLRTgDGEEITADQVVIAAGSRPVIPPVIADS-GVRyhtSDTIMRLPELPESLVIVGGGFI 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 179 AVELAGVINALGAKTHLFVRKHAPLRTFDPMLSETLVEVMQAEGpQLHTHATPKAVEKNSDGsLTLHLEDGRSETVDALI 258
Cdd:PRK07846 178 AAEFAHVFSALGVRVTVVNRSGRLLRHLDDDISERFTELASKRW-DVRLGRNVVGVSQDGSG-VTLRLDDGSTVEADVLL 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 259 WAIGREPETDNFNLAATGVKTNEKGYIVVDKYQNTNVPGIYAVGDNTGAVELTPVAVAAGRRLSERLFNNKPDEHLDYSN 338
Cdd:PRK07846 256 VATGRVPNGDLLDAAAAGVDVDEDGRVVVDEYQRTSAEGVFALGDVSSPYQLKHVANHEARVVQHNLLHPDDLIASDHRF 335
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 339 IPTVVFSHPPIGTVGLTEPQAREQYGDANVKIYKSSFTAMYTAV--TTHrqpcRMKLVCVGPEEKIVGIHGIGFGMDEML 416
Cdd:PRK07846 336 VPAAVFTHPQIASVGLTENEARAAGLDITVKVQNYGDVAYGWAMedTTG----FVKLIADRDTGRLLGAHIIGPQASTLI 411
                        410       420
                 ....*....|....*....|....*....
gi 495128029 417 QGFAVALKMGATKKDF-DNTVAIHPTAAE 444
Cdd:PRK07846 412 QPLIQAMSFGLDAREMaRGQYWIHPALPE 440
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
22-318 5.62e-76

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: 239.53  E-value: 5.62e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029   22 RAAMYGQKCALIEakaLGGTCVNVGCVPKKIMWHAAQIAEAIHLygpdygfdttvnhfdWQKLVASRTAYIDRIHTSYDN 101
Cdd:pfam07992  18 TLAQLGGKVTLIE---DEGTCPYGGCVLSKALLGAAEAPEIASL---------------WADLYKRKEEVVKKLNNGIEV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  102 VLGKNNVDVIQGFARFVDAHTVEVNGERITADHILIATGGRPSHPDIPGAEYG-------IDSDGFFALSAMPQRVAVVG 174
Cdd:pfam07992  80 LLGTEVVSIDPGAKKVVLEELVDGDGETITYDRLVIATGARPRLPPIPGVELNvgflvrtLDSAEALRLKLLPKRVVVVG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  175 AGYIAVELAGVINALGAKTHLFVRKHAPLRTFDPMLSETLVEVMQAEGPQLHTHATPKAVEKNSDGsLTLHLEDGRSETV 254
Cdd:pfam07992 160 GGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDG-VEVILKDGTEIDA 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495128029  255 DALIWAIGREPETDnfNLAATGVKTNEKGYIVVDKYQNTNVPGIYAVGDNT-GAVELTPVAVAAG 318
Cdd:pfam07992 239 DLVVVAIGRRPNTE--LLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDCRvGGPELAQNAVAQG 301
PRK13748 PRK13748
putative mercuric reductase; Provisional
22-362 4.18e-73

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 240.05  E-value: 4.18e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  22 RAAMYGQKCALIEAKALGGTCVNVGCVPKKIMWHAAQIAeaiHLY--GP-DYGFDTTVNHFDWQKLVASRTAYIDRI-HT 97
Cdd:PRK13748 116 KAVEQGARVTLIERGTIGGTCVNVGCVPSKIMIRAAHIA---HLRreSPfDGGIAATVPTIDRSRLLAQQQARVDELrHA 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  98 SYDNVLGKN-NVDVIQGFARFVDAHTVEV----NGER-ITADHILIATGGRPSHPDIPG---AEYGIDSDGFFAlSAMPQ 168
Cdd:PRK13748 193 KYEGILDGNpAITVLHGEARFKDDQTLIVrlndGGERvVAFDRCLIATGASPAVPPIPGlkeTPYWTSTEALVS-DTIPE 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 169 RVAVVGAGYIAVELAGVINALGAKTHLFVRKHAPLRTfDPMLSETLVEVMQAEGPQLHTHATPKAVeKNSDGSLTLHLED 248
Cdd:PRK13748 272 RLAVIGSSVVALELAQAFARLGSKVTILARSTLFFRE-DPAIGEAVTAAFRAEGIEVLEHTQASQV-AHVDGEFVLTTGH 349
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 249 GrSETVDALIWAIGREPETDNFNLAATGVKTNEKGYIVVDKYQNTNVPGIYAVGDNTGAVELTPVAVAAGRRLSERLFNN 328
Cdd:PRK13748 350 G-ELRADKLLVATGRAPNTRSLALDAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQPQFVYVAAAAGTRAAINMTGG 428
                        330       340       350
                 ....*....|....*....|....*....|....
gi 495128029 329 kpDEHLDYSNIPTVVFSHPPIGTVGLTEPQAREQ 362
Cdd:PRK13748 429 --DAALDLTAMPAVVFTDPQVATVGYSEAEAHHD 460
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
22-444 7.71e-66

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 218.64  E-value: 7.71e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  22 RAAMYGQKCALIEA-------KALGGTCVNVGCVPKKIMWHAAQIAEAIHLYGPDYGFDTTVNHFDWQKLVASRTAYIDR 94
Cdd:PRK06327  22 RAAQLGLKVACIEAwknpkgkPALGGTCLNVGCIPSKALLASSEEFENAGHHFADHGIHVDGVKIDVAKMIARKDKVVKK 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  95 IHTSYDNVLGKNNVDVIQGFARFV----DAHTVEVNGER---ITADHILIATGGRPSHpdIPGAEYG----IDSDGFFAL 163
Cdd:PRK06327 102 MTGGIEGLFKKNKITVLKGRGSFVgktdAGYEIKVTGEDetvITAKHVIIATGSEPRH--LPGVPFDnkiiLDNTGALNF 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 164 SAMPQRVAVVGAGYIAVELAGVINALGAktHLFVRKHAP--LRTFDPMLSETLVEVMQAEGPQLHTHATPKAVEKNSDG- 240
Cdd:PRK06327 180 TEVPKKLAVIGAGVIGLELGSVWRRLGA--EVTILEALPafLAAADEQVAKEAAKAFTKQGLDIHLGVKIGEIKTGGKGv 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 241 SLTLHLEDGRSET--VDALIWAIGREPETDNFNLAATGVKTNEKGYIVVDKYQNTNVPGIYAVGDNTGAVELTPVAVAAG 318
Cdd:PRK06327 258 SVAYTDADGEAQTleVDKLIVSIGRVPNTDGLGLEAVGLKLDERGFIPVDDHCRTNVPNVYAIGDVVRGPMLAHKAEEEG 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 319 RRLSERLFNNKPdeHLDYSNIPTVVFSHPPIGTVGLTEPQAREQygDANVKIYKSSFTAMYTAVTTHRQPCRMKLVCVGP 398
Cdd:PRK06327 338 VAVAERIAGQKG--HIDYNTIPWVIYTSPEIAWVGKTEQQLKAE--GVEYKAGKFPFMANGRALAMGEPDGFVKIIADAK 413
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 495128029 399 EEKIVGIHGIGFGMDEMLQGFAVALKMGATKKDFDNTVAIHPTAAE 444
Cdd:PRK06327 414 TDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSE 459
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
22-444 3.80e-64

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


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 213.86  E-value: 3.80e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  22 RAAM----YGQKCALIEAK-ALGGTCVNVGCVPKKIMWHAA-QIAE--AIHLYGpDYGFdttVNHFDWQKLVASRTAYID 93
Cdd:PRK05249  19 GAAMqaakLGKRVAVIERYrNVGGGCTHTGTIPSKALREAVlRLIGfnQNPLYS-SYRV---KLRITFADLLARADHVIN 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  94 R---IHTSYdnvLGKNNVDVIQGFARFVDAHTVEVNG-----ERITADHILIATGGRPSHP-DIP-GAEYGIDSDGFFAL 163
Cdd:PRK05249  95 KqveVRRGQ---YERNRVDLIQGRARFVDPHTVEVECpdgevETLTADKIVIATGSRPYRPpDVDfDHPRIYDSDSILSL 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 164 SAMPQRVAVVGAGYIAVELAGVINALGAKTHLFVRKHAPLRTFDPMLSETLVEVMQAEGPQLHTHATPKAVEKNSDGSLT 243
Cdd:PRK05249 172 DHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSFLDDEISDALSYHLRDSGVTIRHNEEVEKVEGGDDGVIV 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 244 lHLEDGRSETVDALIWAIGREPETDNFNLAATGVKTNEKGYIVVDKYQNTNVPGIYAVGDNTGAVELTPVAVAAGRRLSE 323
Cdd:PRK05249 252 -HLKSGKKIKADCLLYANGRTGNTDGLNLENAGLEADSRGQLKVNENYQTAVPHIYAVGDVIGFPSLASASMDQGRIAAQ 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 324 RLFNNkPDEHLdYSNIPTVVFSHPPIGTVGLTEPQAREQYGDANVKIykSSFTAMYTAVTTHRQPCRMKLVCVGPEEKIV 403
Cdd:PRK05249 331 HAVGE-ATAHL-IEDIPTGIYTIPEISSVGKTEQELTAAKVPYEVGR--ARFKELARAQIAGDNVGMLKILFHRETLEIL 406
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 495128029 404 GIHGIGFGMDEMLQ-GFAVaLKMGATKKDFDNTVAIHPTAAE 444
Cdd:PRK05249 407 GVHCFGERATEIIHiGQAI-MEQKGTIEYFVNTTFNYPTMAE 447
PRK07251 PRK07251
FAD-containing oxidoreductase;
27-446 1.09e-62

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 209.22  E-value: 1.09e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  27 GQKCALIEAKAL--GGTCVNVGCVPKKIMWHAAQiaeaihlygpdygfdttvNHFDWQKLVASRTAYIDRIHTSYDNVLG 104
Cdd:PRK07251  26 GKKVALVEESKAmyGGTCINIGCIPTKTLLVAAE------------------KNLSFEQVMATKNTVTSRLRGKNYAMLA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 105 KNNVDVIQGFARFVDAHTVEVNG----ERITADHILIATGGRPSHPDIPG---AEYGIDSDGFFALSAMPQRVAVVGAGY 177
Cdd:PRK07251  88 GSGVDLYDAEAHFVSNKVIEVQAgdekIELTAETIVINTGAVSNVLPIPGladSKHVYDSTGIQSLETLPERLGIIGGGN 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 178 IAVELAGVINALGAKTHLFVRKHAPLRTFDPMLSETLVEVMQAEGPQLHTHATPKAVEknSDGSLTLHLEDGRSETVDAL 257
Cdd:PRK07251 168 IGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYMEEDGITFLLNAHTTEVK--NDGDQVLVVTEDETYRFDAL 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 258 IWAIGREPETDNFNLAATGVKTNEKGYIVVDKYQNTNVPGIYAVGDNTGAVELTPVAVAAGRRLSERLFNNKPDEHLDYS 337
Cdd:PRK07251 246 LYATGRKPNTEPLGLENTDIELTERGAIKVDDYCQTSVPGVFAVGDVNGGPQFTYISLDDFRIVFGYLTGDGSYTLEDRG 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 338 NIPTVVFSHPPIGTVGLTEPQAREQYGDanVKIYKSSFTAMYTAVTTHRQPCRMKLVcVGPEEK-IVGIHGIGFGMDEML 416
Cdd:PRK07251 326 NVPTTMFITPPLSQVGLTEKEAKEAGLP--YAVKELLVAAMPRAHVNNDLRGAFKVV-VNTETKeILGATLFGEGSQEII 402
                        410       420       430
                 ....*....|....*....|....*....|
gi 495128029 417 QGFAVALKMGATKKDFDNTVAIHPTAAEEF 446
Cdd:PRK07251 403 NLITMAMDNKIPYTYFKKQIFTHPTMAENL 432
PRK08010 PRK08010
pyridine nucleotide-disulfide oxidoreductase; Provisional
24-444 1.96e-53

pyridine nucleotide-disulfide oxidoreductase; Provisional


Pssm-ID: 181196 [Multi-domain]  Cd Length: 441  Bit Score: 184.83  E-value: 1.96e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  24 AMYGQKCALIEAKA--LGGTCVNVGCVPKKIMWHAAQiaeaihlygpdygfdttvNHFDWQKLVASRTAYIDRIHT-SYD 100
Cdd:PRK08010  23 AKAGWRVALIEQSNamYGGTCINIGCIPTKTLVHDAQ------------------QHTDFVRAIQRKNEVVNFLRNkNFH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 101 NVLGKNNVDVIQGFARFVDAHTVEV---NGER-ITADHILIATGGRPSHPDIPG--AEYGI-DSDGFFALSAMPQRVAVV 173
Cdd:PRK08010  85 NLADMPNIDVIDGQAEFINNHSLRVhrpEGNLeIHGEKIFINTGAQTVVPPIPGitTTPGVyDSTGLLNLKELPGHLGIL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 174 GAGYIAVELAGVINALGAKTHLFVRKHAPLRTFDPMLSETLVEVMQAEGPQLHTHATPKAVEkNSDGSLTLHLEDGrSET 253
Cdd:PRK08010 165 GGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVERIS-HHENQVQVHSEHA-QLA 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 254 VDALIWAIGREPETDNFNLAATGVKTNEKGYIVVDKYQNTNVPGIYAVGDNTGAVELTPVAVAAGRRLSERLFNNKPDEH 333
Cdd:PRK08010 243 VDALLIASGRQPATASLHPENAGIAVNERGAIVVDKYLHTTADNIWAMGDVTGGLQFTYISLDDYRIVRDELLGEGKRST 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 334 LDYSNIPTVVFSHPPIGTVGLTEPQAREQygDANVKIYKSSFTAMYTAVTTHRQPCRMKLVCVGPEEKIVGIHGIGFGMD 413
Cdd:PRK08010 323 DDRKNVPYSVFMTPPLSRVGMTEEQARES--GADIQVVTLPVAAIPRARVMNDTRGVLKAIVDNKTQRILGASLLCVDSH 400
                        410       420       430
                 ....*....|....*....|....*....|.
gi 495128029 414 EMLQGFAVALKMGATKKDFDNTVAIHPTAAE 444
Cdd:PRK08010 401 EMINIVKMVMDAGLPYSILRDQIFTHPSMSE 431
Pyr_redox_dim pfam02852
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ...
339-449 5.48e-44

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: 149.63  E-value: 5.48e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  339 IPTVVFSHPPIGTVGLTEPQAREQYGDanVKIYKSSFTAMYTAVTTHRQPCRMKLVCVGPEEKIVGIHGIGFGMDEMLQG 418
Cdd:pfam02852   1 IPSVVFTDPEIASVGLTEEEAKEKGGE--VKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQE 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 495128029  419 FAVALKMGATKKDFDNTVAIHPTAAEEFVTM 449
Cdd:pfam02852  79 AALAIKMGATVEDLANTIHIHPTLSEALVEA 109
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
119-330 1.21e-40

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: 147.65  E-value: 1.21e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 119 DAHTVEV-NGERITADHILIATGGRPSHPDIPGaeygIDSDGFFALSAM--------------PQRVAVVGAGYIAVELA 183
Cdd:COG0446   65 EAKTVTLrDGETLSYDKLVLATGARPRPPPIPG----LDLPGVFTLRTLddadalrealkefkGKRAVVIGGGPIGLELA 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 184 GVINALGAKTHLFVRKHAPLRTFDPMLSETLVEVMQAEGPQLHTHATPKAVEknSDGSLTLHLEDGRSETVDALIWAIGR 263
Cdd:COG0446  141 EALRKRGLKVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAID--GDDKVAVTLTDGEEIPADLVVVAPGV 218
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495128029 264 EPETDnfnLA-ATGVKTNEKGYIVVDKYQNTNVPGIYAVGDNTGA----------VELTPVAVAAGRRLSERLFNNKP 330
Cdd:COG0446  219 RPNTE---LAkDAGLALGERGWIKVDETLQTSDPDVYAAGDCAEVphpvtgktvyIPLASAANKQGRVAAENILGGPA 293
PRK07845 PRK07845
flavoprotein disulfide reductase; Reviewed
23-368 2.44e-35

flavoprotein disulfide reductase; Reviewed


Pssm-ID: 236112 [Multi-domain]  Cd Length: 466  Bit Score: 136.53  E-value: 2.44e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  23 AAMYGQKCALIEAKALGGTCVNVGCVPKKIMWHAAQIAEAIHlYGPDYGfdttVNHFDWQKLVASrtayIDRIHT----- 97
Cdd:PRK07845  20 AAQLGADVTVIERDGLGGAAVLTDCVPSKTLIATAEVRTELR-RAAELG----IRFIDDGEARVD----LPAVNArvkal 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  98 ----SYD--NVLGKNNVDVIQGFARFVDA----HTVEVNG-----ERITADHILIATGGRPShpDIPGAEygidSDG--- 159
Cdd:PRK07845  91 aaaqSADirARLEREGVRVIAGRGRLIDPglgpHRVKVTTadggeETLDADVVLIATGASPR--ILPTAE----PDGeri 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 160 -----FFALSAMPQRVAVVGAGYIAVELAGVINALGAKTHLFVRKHAPLRTFDPMLSETLVEVMQAEGPQLHTHATPKAV 234
Cdd:PRK07845 165 ltwrqLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPGEDADAAEVLEEVFARRGMTVLKRSRAESV 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 235 EKNSDGsLTLHLEDGRSETVDALIWAIGREPETDNFNLAATGVKTNEKGYIVVDKYQNTNVPGIYAVGDNTGAVELTPVA 314
Cdd:PRK07845 245 ERTGDG-VVVTLTDGRTVEGSHALMAVGSVPNTAGLGLEEAGVELTPSGHITVDRVSRTSVPGIYAAGDCTGVLPLASVA 323
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 495128029 315 VAAGR-----RLSERLfnnKPdehLDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDANV 368
Cdd:PRK07845 324 AMQGRiamyhALGEAV---SP---LRLKTVASNVFTRPEIATVGVSQAAIDSGEVPART 376
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
105-372 3.40e-33

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 129.11  E-value: 3.40e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 105 KNNVDVIQGfARFV----DAHTVEV-NGERITADHILIATGGRPSHPDIPGAE----YGI----DSDGFFALSAMPQRVA 171
Cdd:COG1251   68 ENGIDLRLG-TRVTaidrAARTVTLaDGETLPYDKLVLATGSRPRVPPIPGADlpgvFTLrtldDADALRAALAPGKRVV 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 172 VVGAGYIAVELAGVINALGAKTHLFVRKHAPL-RTFDPMLSETLVEVMQAEGPQLHTHATPKAVEKNSDGsLTLHLEDGR 250
Cdd:COG1251  147 VIGGGLIGLEAAAALRKRGLEVTVVERAPRLLpRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRV-TGVRLADGE 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 251 SETVDALIWAIGREPETDnfnLA-ATGVKTNeKGyIVVDKYQNTNVPGIYAVGD---------NTGAVELTPVAVAAGRR 320
Cdd:COG1251  226 ELPADLVVVAIGVRPNTE---LArAAGLAVD-RG-IVVDDYLRTSDPDIYAAGDcaehpgpvyGRRVLELVAPAYEQARV 300
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 495128029 321 LSERLfNNKPDEHLDYSNIPTVVFSHPPIGTVGLTEPQARE-QYGDANVKIYK 372
Cdd:COG1251  301 AAANL-AGGPAAYEGSVPSTKLKVFGVDVASAGDAEGDEEVvVRGDPARGVYK 352
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
23-318 1.67e-30

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 119.84  E-value: 1.67e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  23 AAMYGQKCALIEAKALGG-----TCV-NVGCVPKKIMwhaaqiaeaihlyGPDYGfdttvnhfdwQKLVASRTAYidrih 96
Cdd:COG0492   19 AARAGLKTLVIEGGEPGGqlattKEIeNYPGFPEGIS-------------GPELA----------ERLREQAERF----- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  97 tsydnvlgknNVDVIQGFARFVDA----HTVEV-NGERITADHILIATGGRPSHPDIPGAE--------YGIDSDGFFal 163
Cdd:COG0492   71 ----------GAEILLEEVTSVDKddgpFRVTTdDGTEYEAKAVIIATGAGPRKLGLPGEEefegrgvsYCATCDGFF-- 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 164 saMP-QRVAVVGAGYIAVELAGVINALGAKTHLFVRKHaplrtfDPMLSETLVE-VMQAEGPQLHTHATPKAVEKnsDGS 241
Cdd:COG0492  139 --FRgKDVVVVGGGDSALEEALYLTKFASKVTLIHRRD------ELRASKILVErLRANPKIEVLWNTEVTEIEG--DGR 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 242 LT-LHLEDGRSET-----VDALIWAIGREPETDNFnlAATGVKTNEKGYIVVDKYQNTNVPGIYAVGD-NTGAVELtpVA 314
Cdd:COG0492  209 VEgVTLKNVKTGEekeleVDGVFVAIGLKPNTELL--KGLGLELDEDGYIVVDEDMETSVPGVFAAGDvRDYKYRQ--AA 284

                 ....
gi 495128029 315 VAAG 318
Cdd:COG0492  285 TAAG 288
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
77-343 3.80e-28

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 114.84  E-value: 3.80e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  77 NHFDWQKL---VASRTAYIDRIHTSYDNVLGKNNVDVIQGFARFVD--AHTVEV-NGERITADHILIATGGRPSHPDIPG 150
Cdd:COG1252   37 PYHLFQPLlpeVAAGTLSPDDIAIPLRELLRRAGVRFIQGEVTGIDpeARTVTLaDGRTLSYDYLVIATGSVTNFFGIPG 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 151 AE---YGIDS-----------DGFFALSAMPQ--RVAVVGAGYIAVELAGVINALGAKTHLFVRKHA------------- 201
Cdd:COG1252  117 LAehaLPLKTledalalrerlLAAFERAERRRllTIVVVGGGPTGVELAGELAELLRKLLRYPGIDPdkvritlveagpr 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 202 PLRTFDPMLSETLVEVMQAEGPQLHTHATPKAVEKNsdgslTLHLEDGRSETVDALIWAIG-REPETdnfnLAATGVKTN 280
Cdd:COG1252  197 ILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDAD-----GVTLEDGEEIPADTVIWAAGvKAPPL----LADLGLPTD 267
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495128029 281 EKGYIVVDKY-QNTNVPGIYAVGDnTGAVE------LTPVAVAA---GRRLSE---RLFNNKPDEHLDYSNIPTVV 343
Cdd:COG1252  268 RRGRVLVDPTlQVPGHPNVFAIGD-CAAVPdpdgkpVPKTAQAAvqqAKVLAKniaALLRGKPLKPFRYRDKGCLA 342
PTZ00153 PTZ00153
lipoamide dehydrogenase; Provisional
37-444 7.74e-28

lipoamide dehydrogenase; Provisional


Pssm-ID: 173442 [Multi-domain]  Cd Length: 659  Bit Score: 116.55  E-value: 7.74e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  37 ALGGTCVNVGCVPKKIMWHAA----QIAEAIHLYGpdYGFDTTVN------------------HFDWQKLVASRTAYIDR 94
Cdd:PTZ00153 151 SIGGTCVNVGCIPSKALLYATgkyrELKNLAKLYT--YGIYTNAFkngkndpvernqlvadtvQIDITKLKEYTQSVIDK 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  95 IHTSYDNVLGKN-------NVDVIQGFARFVDAHTV--EVNGERITADHILIATGGRPSHPDipgaeyGIDSDGF----- 160
Cdd:PTZ00153 229 LRGGIENGLKSKkfcknseHVQVIYERGHIVDKNTIksEKSGKEFKVKNIIIATGSTPNIPD------NIEVDQKsvfts 302
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 161 ---FALSAMPQRVAVVGAGYIAVELAGVINALGAKTHLF-------------VRKHAPlRTF---DPMLSETLVEVMQAE 221
Cdd:PTZ00153 303 dtaVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFeyspqllplldadVAKYFE-RVFlksKPVRVHLNTLIEYVR 381
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 222 GPQ-------LHTHATpkavEKNSDGSLTlHLEDGRSETVDALIWAIGREPETDNFNLAATGVKTNeKGYIVVD------ 288
Cdd:PTZ00153 382 AGKgnqpviiGHSERQ----TGESDGPKK-NMNDIKETYVDSCLVATGRKPNTNNLGLDKLKIQMK-RGFVSVDehlrvl 455
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 289 KYQNTNVPGIYAVGDNTGAVELTPVAVAAGRRLSERLFNNKPDEH-----------LDYSNIPTVVFSHPPIGTVGLTEP 357
Cdd:PTZ00153 456 REDQEVYDNIFCIGDANGKQMLAHTASHQALKVVDWIEGKGKENVninvenwaskpIIYKNIPSVCYTTPELAFIGLTEK 535
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 358 QAREQYGDANVKIYKSSFTAMYTAVTTHRQPCR----------------------MKLVCVGPEEKIVGIHGIGFGMDEM 415
Cdd:PTZ00153 536 EAKELYPPDNVGVEISFYKANSKVLCENNISFPnnsknnsynkgkyntvdntegmVKIVYLKDTKEILGMFIVGSYASIL 615
                        490       500
                 ....*....|....*....|....*....
gi 495128029 416 LQGFAVALKMGATKKDFDNTVAIHPTAAE 444
Cdd:PTZ00153 616 IHEGVLAINLKLSVKDLAHMVHSHPTISE 644
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
169-249 2.14e-20

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: 84.95  E-value: 2.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  169 RVAVVGAGYIAVELAGVINALGAKTHLFVRKHAPLRTFDPMLSETLVEVMQAEGPQLHTHATPKAVEKNSDGSlTLHLED 248
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGV-VVVLTD 79

                  .
gi 495128029  249 G 249
Cdd:pfam00070  80 G 80
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
131-325 4.56e-20

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 92.03  E-value: 4.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 131 TADHILIATGGRPSHPDIPGaeygIDSDGFFALSAMP--------------QRVAVVGAGYIAVELAGVINALGAKTHLF 196
Cdd:PRK09564 103 TYDKLMIATGARPIIPPIKN----INLENVYTLKSMEdglalkellkdeeiKNIVIIGAGFIGLEAVEAAKHLGKNVRII 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 197 VR-KHAPLRTFDPMLSETLVEVMQAEGPQLHTHATPKAV--EKNSDGSLTlhlEDGRSETvDALIWAIGREPETDnFnLA 273
Cdd:PRK09564 179 QLeDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSLigEDKVEGVVT---DKGEYEA-DVVIVATGVKPNTE-F-LE 252
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495128029 274 ATGVKTNEKGYIVVDKYQNTNVPGIYAVGDN-------TGAVELTPVAVAA---GRRLSERL 325
Cdd:PRK09564 253 DTGLKTLKNGAIIVDEYGETSIENIYAAGDCatiynivSNKNVYVPLATTAnklGRMVGENL 314
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
133-320 1.72e-19

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: 90.19  E-value: 1.72e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 133 DHILIATG-GRPSHPDIPGAE-----YGID-------SDGFFALSAMPQRVAVVGAGYIAVELAGVINALGAKT-HLFVR 198
Cdd:COG0493  208 DAVFLATGaGKPRDLGIPGEDlkgvhSAMDfltavnlGEAPDTILAVGKRVVVIGGGNTAMDCARTALRLGAESvTIVYR 287
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 199 khaplRTFDPMlSETLVEVMQA--EGPQLHTHATPKAVEKNSDGSLT-LHL---------EDGR--------SETV---D 255
Cdd:COG0493  288 -----RTREEM-PASKEEVEEAleEGVEFLFLVAPVEIIGDENGRVTgLECvrmelgepdESGRrrpvpiegSEFTlpaD 361
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 256 ALIWAIGREPETDNFnLAATGVKTNEKGYIVVDK-YQNTNVPGIYAVGDN-TGA---VEltpvAVAAGRR 320
Cdd:COG0493  362 LVILAIGQTPDPSGL-EEELGLELDKRGTIVVDEeTYQTSLPGVFAGGDAvRGPslvVW----AIAEGRK 426
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
118-303 6.99e-19

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 88.05  E-value: 6.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 118 VDAHTVEVNGERITADHILIATGGRPSHPDIPGAEYGI--DSDGFFALS----AMPQRVAVVGAGYIAVELAGVINALGA 191
Cdd:PRK04965  86 AEAQVVKSQGNQWQYDKLVLATGASAFVPPIPGRELMLtlNSQQEYRAAetqlRDAQRVLVVGGGLIGTELAMDLCRAGK 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 192 KTHLFVRKHAPLRTFDP-MLSETLVEVMQAEGPQLHTHATPKAVEKNSDG-SLTLHleDGRSETVDALIWAIGREPETdn 269
Cdd:PRK04965 166 AVTLVDNAASLLASLMPpEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGiRATLD--SGRSIEVDAVIAAAGLRPNT-- 241
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 495128029 270 fNLA-ATGVKTNeKGyIVVDKYQNTNVPGIYAVGD 303
Cdd:PRK04965 242 -ALArRAGLAVN-RG-IVVDSYLQTSAPDIYALGD 273
Pyr_redox_3 pfam13738
Pyridine nucleotide-disulphide oxidoreductase;
99-302 2.75e-16

Pyridine nucleotide-disulphide oxidoreductase;


Pssm-ID: 404603 [Multi-domain]  Cd Length: 296  Bit Score: 79.19  E-value: 2.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029   99 YDNVLGKNNVDV-----IQGFARFVDAHTVEVNGERITADHILIATG--GRPSHPDIPgaEYGIDSDGFFALSAMP-QRV 170
Cdd:pfam13738  81 LRRVADHFELPInlfeeVTSVKKEDDGFVVTTSKGTYQARYVIIATGefDFPNKLGVP--ELPKHYSYVKDFHPYAgQKV 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  171 AVVGAGYIAVELAGVINALGAKTHLFVRkHAPLRTFDPMLSETLV--------EVMQAEGPQLHTHATPKAVEKNsDGSL 242
Cdd:pfam13738 159 VVIGGYNSAVDAALELVRKGARVTVLYR-GSEWEDRDSDPSYSLSpdtlnrleELVKNGKIKAHFNAEVKEITEV-DVSY 236
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495128029  243 TLHLEDGRSETV-DALIWAIGREPETDnFnLAATGVKTNEKGYIVVDK-YQNTNVPGIYAVG 302
Cdd:pfam13738 237 KVHTEDGRKVTSnDDPILATGYHPDLS-F-LKKGLFELDEDGRPVLTEeTESTNVPGLFLAG 296
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
127-303 6.76e-15

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


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 77.18  E-value: 6.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  127 GERITADHILIATGGRPSHPDIPGAE----YGI----DSDGFFALSAMPQRVAVVGAGYIAVELAGVINALGAKTHlfVR 198
Cdd:TIGR02374  92 GRTLSYDKLILATGSYPFILPIPGADkkgvYVFrtieDLDAIMAMAQRFKKAAVIGGGLLGLEAAVGLQNLGMDVS--VI 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  199 KHAPL---RTFDPMLSETLVEVMQAEGPQLHthatpkaVEKNSDGSL------TLHLEDGRSETVDALIWAIGREPetdN 269
Cdd:TIGR02374 170 HHAPGlmaKQLDQTAGRLLQRELEQKGLTFL-------LEKDTVEIVgatkadRIRFKDGSSLEADLIVMAAGIRP---N 239
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 495128029  270 FNLA-ATGVKTNekGYIVVDKYQNTNVPGIYAVGD 303
Cdd:TIGR02374 240 DELAvSAGIKVN--RGIIVNDSMQTSDPDIYAVGE 272
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
133-320 5.71e-14

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 73.67  E-value: 5.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 133 DHILIATG-GRPSHPDIPGAEYG-----ID-------SDGFFALSAmPQRVAVVGAGYIAVELAGVINALGAK-THLFVR 198
Cdd:PRK11749 227 DAVFIGTGaGLPRFLGIPGENLGgvysaVDfltrvnqAVADYDLPV-GKRVVVIGGGNTAMDAARTAKRLGAEsVTIVYR 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 199 khaplRTFDPMlSETLVEVMQA--EGPQLHTHATPKAVEKNSDGSLTLHLE---------DGR-------SE---TVDAL 257
Cdd:PRK11749 306 -----RGREEM-PASEEEVEHAkeEGVEFEWLAAPVEILGDEGRVTGVEFVrmelgepdaSGRrrvpiegSEftlPADLV 379
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495128029 258 IWAIGREPEtDNFNLAATGVKTNEKGYIVVD-KYQNTNVPGIYAVGDNTGAVELTPVAVAAGRR 320
Cdd:PRK11749 380 IKAIGQTPN-PLILSTTPGLELNRWGTIIADdETGRTSLPGVFAGGDIVTGAATVVWAVGDGKD 442
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
133-325 4.88e-13

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 70.02  E-value: 4.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 133 DHILIATGG-RPSHPDIPGAE-----------YGIDSD--GFFALSAMP----QRVAVVGAGYIAVELAGVINALGAK-- 192
Cdd:PRK12770 120 DAVLIATGTwKSRKLGIPGEDlpgvysaleylFRIRAAklGYLPWEKVPpvegKKVVVVGAGLTAVDAALEAVLLGAEkv 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 193 THLFVR--KHAPLRTFDpmlsetlVEVMQAEGPQLHTHATPKAVE--------KNSDGSLTLHLEDGRSETV-------- 254
Cdd:PRK12770 200 YLAYRRtiNEAPAGKYE-------IERLIARGVEFLELVTPVRIIgegrvegvELAKMRLGEPDESGRPRPVpipgsefv 272
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495128029 255 ---DALIWAIGREPeTDNFNLAATGVKTNEKGYIVVDKYQNTNVPGIYAVGDNTGAVELTPVAVAAGRRLSERL 325
Cdd:PRK12770 273 leaDTVVFAIGEIP-TPPFAKECLGIELNRKGEIVVDEKHMTSREGVFAAGDVVTGPSKIGKAIKSGLRAAQSI 345
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
168-303 1.19e-12

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 69.43  E-value: 1.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 168 QRVAVVGAGYIAVELAGVINALGAKTHLFVRKHAPLRTFDPMLSETLVEVMQAEGPQLHTHATPKAVEKNsdgslTLHLE 247
Cdd:PRK13512 149 DKALVVGAGYISLEVLENLYERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDAINGN-----EVTFK 223
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 495128029 248 DGRSETVDALIWAIGREPETDnFnLAATGVKTNEKGYIVVDKYQNTNVPGIYAVGD 303
Cdd:PRK13512 224 SGKVEHYDMIIEGVGTHPNSK-F-IESSNIKLDDKGFIPVNDKFETNVPNIYAIGD 277
PRK14989 PRK14989
nitrite reductase subunit NirD; Provisional
88-303 5.26e-11

nitrite reductase subunit NirD; Provisional


Pssm-ID: 184951 [Multi-domain]  Cd Length: 847  Bit Score: 64.75  E-value: 5.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029  88 RTAYiDRIH-TSY-------------DNVLGKNNVDVIQG-FARFVDAHTVEV---NGERITADHILIATGGRPSHPDIP 149
Cdd:PRK14989  41 RIAY-DRVHlSSYfshhtaeelslvrEGFYEKHGIKVLVGeRAITINRQEKVIhssAGRTVFYDKLIMATGSYPWIPPIK 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 150 GAE------YGI--DSDGFFALSAMPQRVAVVGAGYIAVELAGVINALGAKTHlfVRKHAPL---RTFDPMLSETLVEVM 218
Cdd:PRK14989 120 GSEtqdcfvYRTieDLNAIEACARRSKRGAVVGGGLLGLEAAGALKNLGVETH--VIEFAPMlmaEQLDQMGGEQLRRKI 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 219 QAEGPQLHTHA-TPKAVEKNSDGSLTLHLEDGRSETVDALIWAIGREPETdnfNLAA-TGVKTNEKGYIVVDKYQNTNVP 296
Cdd:PRK14989 198 ESMGVRVHTSKnTLEIVQEGVEARKTMRFADGSELEVDFIVFSTGIRPQD---KLATqCGLAVAPRGGIVINDSCQTSDP 274

                 ....*..
gi 495128029 297 GIYAVGD 303
Cdd:PRK14989 275 DIYAIGE 281
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
133-330 6.50e-10

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 61.28  E-value: 6.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 133 DHILIATGG-RPSHPDIPGAEY-----GIDSDGFFALSAMP---QRVAVVGAGYIAVELAGVINALGAK--THLFVRKHA 201
Cdd:PRK12814 280 DAVLLAVGAqKASKMGIPGEELpgvisGIDFLRNVALGTALhpgKKVVVIGGGNTAIDAARTALRLGAEsvTILYRRTRE 359
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 202 PLRTFDPMLSETLvevmqAEGPQLHTHATPKAVEKnSDGSLTLHL---------EDGRSETV-----------DALIWAI 261
Cdd:PRK12814 360 EMPANRAEIEEAL-----AEGVSLRELAAPVSIER-SEGGLELTAikmqqgepdESGRRRPVpvegseftlqaDTVISAI 433
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495128029 262 GREpeTDNFNLAATGVKTNEKGYIVVDK-YQNTNVPGIYAVGDNTGAVELTPVAVAAGRRLSE---RLFNNKP 330
Cdd:PRK12814 434 GQQ--VDPPIAEAAGIGTSRNGTVKVDPeTLQTSVAGVFAGGDCVTGADIAINAVEQGKRAAHaidLFLNGKP 504
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
122-306 8.05e-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: 60.26  E-value: 8.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 122 TVEV-NGERITADHILIATGG--RPSHPDIPG-----------AEYGIDSDgfFAlsamPQRVAVVGAGY----IAVELA 183
Cdd:COG2072  118 TVTTdDGETLTARFVVVATGPlsRPKIPDIPGledfageqlhsADWRNPVD--LA----GKRVLVVGTGAsavqIAPELA 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 184 GVinalGAKTHLFVRKH---APLRTFDPMLSETLVEVMQAEGPQLHTHATPKAVEKNSDGSL------------------ 242
Cdd:COG2072  192 RV----AAHVTVFQRTPpwvLPRPNYDPERGRPANYLGLEAPPALNRRDARAWLRRLLRAQVkdpelglltpdyppgckr 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 243 -----------------------------TLHLEDGRSETVDALIWAIGREPETDnfNLAATGVkTNEKGYIVVDKYQNT 293
Cdd:COG2072  268 pllstdyyealrrgnvelvtggieritedGVVFADGTEHEVDVIVWATGFRADLP--WLAPLDV-RGRDGRSGPRAYLGV 344
                        250
                 ....*....|....*.
gi 495128029 294 ---NVPGIYAVGDNTG 306
Cdd:COG2072  345 vvpGFPNLFFLGPNSP 360
PRK10262 PRK10262
thioredoxin reductase; Provisional
131-303 1.50e-09

thioredoxin reductase; Provisional


Pssm-ID: 182343 [Multi-domain]  Cd Length: 321  Bit Score: 59.30  E-value: 1.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 131 TADHILIATGGRPSHPDIPGAE----YGIDS----DGFFALSampQRVAVVGAGYIAVELAGVINALGAKTHLFVRKHAp 202
Cdd:PRK10262 105 TCDALIIATGASARYLGLPSEEafkgRGVSAcatcDGFFYRN---QKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDG- 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 203 LRTfDPMLSETLVEVMQAEGPQLHTHATPKAVEKNSDGSLTLHLEDGRS----ETVD--ALIWAIGREPETDNFNlaatG 276
Cdd:PRK10262 181 FRA-EKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQNsdniESLDvaGLFVAIGHSPNTAIFE----G 255
                        170       180       190
                 ....*....|....*....|....*....|..
gi 495128029 277 VKTNEKGYIVVD-----KYQNTNVPGIYAVGD 303
Cdd:PRK10262 256 QLELENGYIKVQsgihgNATQTSIPGVFAAGD 287
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
169-334 2.55e-09

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 59.12  E-value: 2.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 169 RVAVVGAGYIAVELAGVINALGAKTHLFVRkhapLRTFDPM-LSETLVEVMQAEGPQLHTHATPKAVEKNSDGSLTLHL- 246
Cdd:PRK12771 269 RVVVIGGGNTAMDAARTARRLGAEEVTIVY----RRTREDMpAHDEEIEEALREGVEINWLRTPVEIEGDENGATGLRVi 344
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 247 --------EDGR-------SETV--DALIWAIGREPETDNFNlAATGVkTNEKGYIVVDK-YQNTNVPGIYAVGDNTGAV 308
Cdd:PRK12771 345 tvekmeldEDGRpspvtgeEETLeaDLVVLAIGQDIDSAGLE-SVPGV-EVGRGVVQVDPnFMMTGRPGVFAGGDMVPGP 422
                        170       180       190
                 ....*....|....*....|....*....|....
gi 495128029 309 ELTPVAVAAGRR--------LSERLFNNKPDEHL 334
Cdd:PRK12771 423 RTVTTAIGHGKKaarnidafLGGEPYEHRPKREI 456
PRK12831 PRK12831
putative oxidoreductase; Provisional
133-320 6.56e-08

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 54.64  E-value: 6.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 133 DHILIATG-GRPSHPDIPGaeygIDSDGFFALS--------------------AMPQRVAVVGAGYIAVELAGVINALGA 191
Cdd:PRK12831 230 DAVFIGSGaGLPKFMGIPG----ENLNGVFSANefltrvnlmkaykpeydtpiKVGKKVAVVGGGNVAMDAARTALRLGA 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 192 KTHLFVRkhaplRTFDPMLSEtLVEVMQA--EGPQLHTHATPKAVEKNSDGSLT------LHLED----GR--------S 251
Cdd:PRK12831 306 EVHIVYR-----RSEEELPAR-VEEVHHAkeEGVIFDLLTNPVEILGDENGWVKgmkcikMELGEpdasGRrrpveiegS 379
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495128029 252 E---TVDALIWAIGREPetdN--FNLAATGVKTNEKGYIVVDKYQN-TNVPGIYAVGDN-TGAVELTpVAVAAGRR 320
Cdd:PRK12831 380 EfvlEVDTVIMSLGTSP---NplISSTTKGLKINKRGCIVADEETGlTSKEGVFAGGDAvTGAATVI-LAMGAGKK 451
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
119-305 2.62e-07

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 52.85  E-value: 2.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 119 DAHTVEV-NGERITADHILIATGGRPSHPDIPG-AEY---GI----DSDG-FFAlsamPQRVAVVGAGYIAVE----LAG 184
Cdd:PRK15317 297 GLIEVELaNGAVLKAKTVILATGARWRNMNVPGeDEYrnkGVaycpHCDGpLFK----GKRVAVIGGGNSGVEaaidLAG 372
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 185 VINalgaktHLFVRKHAP-LRTfDPMLSETL-----VEVmqaegpqlHTHATPKAVEKNSDGSLTLHLED---GRSETV- 254
Cdd:PRK15317 373 IVK------HVTVLEFAPeLKA-DQVLQDKLrslpnVTI--------ITNAQTTEVTGDGDKVTGLTYKDrttGEEHHLe 437
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 495128029 255 -DALIWAIGREPETDNFNLAatgVKTNEKGYIVVDKYQNTNVPGIYAVGDNT 305
Cdd:PRK15317 438 lEGVFVQIGLVPNTEWLKGT---VELNRRGEIIVDARGATSVPGVFAAGDCT 486
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
123-303 1.35e-06

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 50.31  E-value: 1.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 123 VEVNGERITADHILIATGGR----PSHPDIPGAEYGI----DSDGFFALSAMPQRVAVVGAGYIAVELAGVINALGAKTH 194
Cdd:PRK09754  92 VLTNGESWHWDQLFIATGAAarplPLLDALGERCFTLrhagDAARLREVLQPERSVVIVGAGTIGLELAASATQRRCKVT 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 195 LFVRKHAPL-RTFDPMLSETLVEVMQAEGPQLHTHATPKAVEKNSDgsLTLHLEDGRSETVDALIWAIGREPetdNFNLA 273
Cdd:PRK09754 172 VIELAATVMgRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEK--VELTLQSGETLQADVVIYGIGISA---NDQLA 246
                        170       180       190
                 ....*....|....*....|....*....|.
gi 495128029 274 A-TGVKTNekGYIVVDKYQNTNVPGIYAVGD 303
Cdd:PRK09754 247 ReANLDTA--NGIVIDEACRTCDPAIFAGGD 275
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
103-320 1.54e-06

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


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 50.51  E-value: 1.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 103 LGKNNVDV-IQGFARF-VDAHTVEVNGERITADH--------ILIATG-GRPSHPDIPGAEY-GIDS-----------DG 159
Cdd:PRK12778 479 LPKKIVDVeIENLKKLgVKFETDVIVGKTITIEEleeegfkgIFIASGaGLPNFMNIPGENSnGVMSsneyltrvnlmDA 558
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 160 FFALSAMP----QRVAVVGAGYIAVELAGVINALGAKTHLFVRKhaplRTFDPMLSEtLVEVMQA--EGPQLHTHATPKA 233
Cdd:PRK12778 559 ASPDSDTPikfgKKVAVVGGGNTAMDSARTAKRLGAERVTIVYR----RSEEEMPAR-LEEVKHAkeEGIEFLTLHNPIE 633
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128029 234 VEKNSDGSLT-LHLE------------------DGRSETVDA--LIWAIGREPetdNFNLAAT--GVKTNEKGYIVVDKY 290
Cdd:PRK12778 634 YLADEKGWVKqVVLQkmelgepdasgrrrpvaiPGSTFTVDVdlVIVSVGVSP---NPLVPSSipGLELNRKGTIVVDEE 710
                        250       260       270
                 ....*....|....*....|....*....|.
gi 495128029 291 QNTNVPGIYAVGDN-TGAVELTpVAVAAGRR 320
Cdd:PRK12778 711 MQSSIPGIYAGGDIvRGGATVI-LAMGDGKR 740
 
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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