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Conserved domains on  [gi|186509939|ref|NP_001118607|]
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monodehydroascorbate reductase [Arabidopsis thaliana]

Protein Classification

NAD(P)/FAD-dependent oxidoreductase( domain architecture ID 11441266)

NAD(P)/FAD-dependent oxidoreductase catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant; belongs to the pyridine nucleotide-disulfide oxidoreductase superfamily

CATH:  3.30.390.30
EC:  1.-.-.-
Gene Ontology:  GO:0016491|GO:0000166
PubMed:  38537870
SCOP:  4000121

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
33-396 2.46e-74

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


:

Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 238.12  E-value: 2.46e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  33 GELAIISKEPVPPFERPELTKVYidlevnptlaniyvcAGTGEAKQY----PNWYKEKEI--------VKADLASKTLVS 100
Cdd:COG1251   27 GEITVIGAEPHPPYNRPPLSKVL---------------AGETDEEDLllrpADFYEENGIdlrlgtrvTAIDRAARTVTL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 101 DDGKIYKYQTLLIATGSTNIRLSEIGvqeADVKNIFYLREIEDsdelALAMELYVQRGK-AVIIGGGFLGLEISSALRAN 179
Cdd:COG1251   92 ADGETLPYDKLVLATGSRPRVPPIPG---ADLPGVFTLRTLDD----ADALRAALAPGKrVVVIGGGLIGLEAAAALRKR 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 180 NHEVTMVFPEPWLVHRFFTAEIASFYESYYANKGIKIIKGTVATGFstNSDGEVTEVKLEDGRTLEANIVVAGVGARPAT 259
Cdd:COG1251  165 GLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEI--EGDDRVTGVRLADGEELPADLVVVAIGVRPNT 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 260 SLFKG-QLEEEkGGIKTDGFFKTSVPDVYALGDVATFPMKMYGGtRRVEHADNARKSAAQAVKAIkAGEEgktIPDYDYL 338
Cdd:COG1251  243 ELARAaGLAVD-RGIVVDDYLRTSDPDIYAAGDCAEHPGPVYGR-RVLELVAPAYEQARVAAANL-AGGP---AAYEGSV 316

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 186509939 339 PYFYSRFFKLSWEFYGENVG--ESVLFGDndpkspkPKFGTY---WVKDGKVVGVFLEGGTQE 396
Cdd:COG1251  317 PSTKLKVFGVDVASAGDAEGdeEVVVRGD-------PARGVYkklVLRDGRLVGAVLVGDTSD 372
 
Name Accession Description Interval E-value
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
33-396 2.46e-74

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 238.12  E-value: 2.46e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  33 GELAIISKEPVPPFERPELTKVYidlevnptlaniyvcAGTGEAKQY----PNWYKEKEI--------VKADLASKTLVS 100
Cdd:COG1251   27 GEITVIGAEPHPPYNRPPLSKVL---------------AGETDEEDLllrpADFYEENGIdlrlgtrvTAIDRAARTVTL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 101 DDGKIYKYQTLLIATGSTNIRLSEIGvqeADVKNIFYLREIEDsdelALAMELYVQRGK-AVIIGGGFLGLEISSALRAN 179
Cdd:COG1251   92 ADGETLPYDKLVLATGSRPRVPPIPG---ADLPGVFTLRTLDD----ADALRAALAPGKrVVVIGGGLIGLEAAAALRKR 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 180 NHEVTMVFPEPWLVHRFFTAEIASFYESYYANKGIKIIKGTVATGFstNSDGEVTEVKLEDGRTLEANIVVAGVGARPAT 259
Cdd:COG1251  165 GLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEI--EGDDRVTGVRLADGEELPADLVVVAIGVRPNT 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 260 SLFKG-QLEEEkGGIKTDGFFKTSVPDVYALGDVATFPMKMYGGtRRVEHADNARKSAAQAVKAIkAGEEgktIPDYDYL 338
Cdd:COG1251  243 ELARAaGLAVD-RGIVVDDYLRTSDPDIYAAGDCAEHPGPVYGR-RVLELVAPAYEQARVAAANL-AGGP---AAYEGSV 316

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 186509939 339 PYFYSRFFKLSWEFYGENVG--ESVLFGDndpkspkPKFGTY---WVKDGKVVGVFLEGGTQE 396
Cdd:COG1251  317 PSTKLKVFGVDVASAGDAEGdeEVVVRGD-------PARGVYkklVLRDGRLVGAVLVGDTSD 372
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 31-316 1.27e-47

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: 165.18  E-value: 1.27e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939   31 KPGELAIISKEPVPPFERPELTKVYI----DLEVNPTLANIYVCAgTGEAKQYPN---WYKEKEIVKADLASKTL----- 98
Cdd:pfam07992  22 LGGKVTLIEDEGTCPYGGCVLSKALLgaaeAPEIASLWADLYKRK-EEVVKKLNNgieVLLGTEVVSIDPGAKKVvleel 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939   99 VSDDGKIYKYQTLLIATGSTNIRLSEIGVQEadvKNIFYLREIEDSDELALAMelyvQRGKAVIIGGGFLGLEISSALRA 178
Cdd:pfam07992 101 VDGDGETITYDRLVIATGARPRLPPIPGVEL---NVGFLVRTLDSAEALRLKL----LPKRVVVVGGGYIGVELAAALAK 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  179 NNHEVTMVFPEPWLVhRFFTAEIASFYESYYANKGIKIIKGTVATGFstNSDGEVTEVKLEDGRTLEANIVVAGVGARPA 258
Cdd:pfam07992 174 LGKEVTLIEALDRLL-RAFDEEISAALEKALEKNGVEVRLGTSVKEI--IGDGDGVEVILKDGTEIDADLVVVAIGRRPN 250

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  259 TSLFK--GQLEEEKGGIKTDGFFKTSVPDVYALGDVatfpmkmygGTRRVEHADNARKSA 316
Cdd:pfam07992 251 TELLEaaGLELDERGGIVVDEYLRTSVPGIYAAGDC---------RVGGPELAQNAVAQG 301
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
 34-301 2.00e-27

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


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 115.31  E-value: 2.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939   34 ELAIISKEPVPPFERPELTKVyidLEVNPTLANIYVCAGTGEAKQYPNWYKEKEIVKADLASKTLVSDDGKIYKYQTLLI 113
Cdd:TIGR02374  26 EITIFGEEPHPNYNRILLSSV---LQGEADLDDITLNSKDWYEKHGITLYTGETVIQIDTDQKQVITDAGRTLSYDKLIL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  114 ATGSTNIRLSeigVQEADVKNIFYLREIEDSDelalAMELYVQRG-KAVIIGGGFLGLEISSALRANNHEVTMVFPEPWL 192
Cdd:TIGR02374 103 ATGSYPFILP---IPGADKKGVYVFRTIEDLD----AIMAMAQRFkKAAVIGGGLLGLEAAVGLQNLGMDVSVIHHAPGL 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  193 VHRFFTAEIASFYESYYANKGIKIIKGTvaTGFSTNSDGEVTEVKLEDGRTLEANIVVAGVGARPATSLFKGQLEEEKGG 272
Cdd:TIGR02374 176 MAKQLDQTAGRLLQRELEQKGLTFLLEK--DTVEIVGATKADRIRFKDGSSLEADLIVMAAGIRPNDELAVSAGIKVNRG 253

                         250       260
                  ....*....|....*....|....*....
gi 186509939  273 IKTDGFFKTSVPDVYALGDVATFPMKMYG 301
Cdd:TIGR02374 254 IIVNDSMQTSDPDIYAVGECAEHNGRVYG 282
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
 33-372 1.59e-23

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 101.54  E-value: 1.59e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  33 GELAIISKEPVPPFERPELTKVYIdleVNPTLANIYVCAgtgeakqyPNWYKEKEI-------VKADLASK-TLVSDDGK 104
Cdd:PRK09754  29 GELHLFSDERHLPYERPPLSKSML---LEDSPQLQQVLP--------ANWWQENNVhlhsgvtIKTLGRDTrELVLTNGE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 105 IYKYQTLLIATGSTNIR---LSEIGvqeadvKNIFYLREIEDSDELALAmelyVQRGKAV-IIGGGFLGLEI---SSALR 177
Cdd:PRK09754  98 SWHWDQLFIATGAAARPlplLDALG------ERCFTLRHAGDAARLREV----LQPERSVvIVGAGTIGLELaasATQRR 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 178 ANnheVTMVFPEPWLVHRFFTAEIASFYESYYANKGIKIIkgtVATGFSTNSDGEVTEVKLEDGRTLEANIVVAGVGARp 257
Cdd:PRK09754 168 CK---VTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRIL---LNNAIEHVVDGEKVELTLQSGETLQADVVIYGIGIS- 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 258 atslFKGQLEEE-----KGGIKTDGFFKTSVPDVYALGDVAtFPMKMYGGTRRVEHADNARKSAAQAVKAIKAGEEGKTI 332
Cdd:PRK09754 241 ----ANDQLAREanldtANGIVIDEACRTCDPAIFAGGDVA-ITRLDNGALHRCESWENANNQAQIAAAAMLGLPLPLLP 315

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 186509939 333 PdydylPYFYSRFFKLSWEFYGENVGESVLFgDNDPKSPK 372
Cdd:PRK09754 316 P-----PWFWSDQYSDNLQFIGDMRGDDWLC-RGNPETQK 349
 
Name Accession Description Interval E-value
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
33-396 2.46e-74

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 238.12  E-value: 2.46e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  33 GELAIISKEPVPPFERPELTKVYidlevnptlaniyvcAGTGEAKQY----PNWYKEKEI--------VKADLASKTLVS 100
Cdd:COG1251   27 GEITVIGAEPHPPYNRPPLSKVL---------------AGETDEEDLllrpADFYEENGIdlrlgtrvTAIDRAARTVTL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 101 DDGKIYKYQTLLIATGSTNIRLSEIGvqeADVKNIFYLREIEDsdelALAMELYVQRGK-AVIIGGGFLGLEISSALRAN 179
Cdd:COG1251   92 ADGETLPYDKLVLATGSRPRVPPIPG---ADLPGVFTLRTLDD----ADALRAALAPGKrVVVIGGGLIGLEAAAALRKR 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 180 NHEVTMVFPEPWLVHRFFTAEIASFYESYYANKGIKIIKGTVATGFstNSDGEVTEVKLEDGRTLEANIVVAGVGARPAT 259
Cdd:COG1251  165 GLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEI--EGDDRVTGVRLADGEELPADLVVVAIGVRPNT 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 260 SLFKG-QLEEEkGGIKTDGFFKTSVPDVYALGDVATFPMKMYGGtRRVEHADNARKSAAQAVKAIkAGEEgktIPDYDYL 338
Cdd:COG1251  243 ELARAaGLAVD-RGIVVDDYLRTSDPDIYAAGDCAEHPGPVYGR-RVLELVAPAYEQARVAAANL-AGGP---AAYEGSV 316

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 186509939 339 PYFYSRFFKLSWEFYGENVG--ESVLFGDndpkspkPKFGTY---WVKDGKVVGVFLEGGTQE 396
Cdd:COG1251  317 PSTKLKVFGVDVASAGDAEGdeEVVVRGD-------PARGVYkklVLRDGRLVGAVLVGDTSD 372
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 33-348 6.40e-55

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: 185.01  E-value: 6.40e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  33 GELAIISKEPVPPFERPELTKVYidLEVNPTLANIYVcagtgeakQYPNWYKEK--------EIVKADLASKTLVSDDGK 104
Cdd:COG0446    6 AEITVIEKGPHHSYQPCGLPYYV--GGGIKDPEDLLV--------RTPESFERKgidvrtgtEVTAIDPEAKTVTLRDGE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 105 IYKYQTLLIATGSTNIRLSEIGVqeaDVKNIFYLREIEDSDELALAMElYVQRGKAVIIGGGFLGLEISSALRANNHEVT 184
Cdd:COG0446   76 TLSYDKLVLATGARPRPPPIPGL---DLPGVFTLRTLDDADALREALK-EFKGKRAVVIGGGPIGLELAEALRKRGLKVT 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 185 MVFPEPwLVHRFFTAEIASFYESYYANKGIKIIKGTVATGFstNSDGEVTeVKLEDGRTLEANIVVAGVGARPATSLFKG 264
Cdd:COG0446  152 LVERAP-RLLGVLDPEMAALLEEELREHGVELRLGETVVAI--DGDDKVA-VTLTDGEEIPADLVVVAPGVRPNTELAKD 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 265 -QLE-EEKGGIKTDGFFKTSVPDVYALGDVATFPMKMYGGTRRVEHADNARKSAAQAVKAIkAGEEgktiPDYDYLPYFY 342
Cdd:COG0446  228 aGLAlGERGWIKVDETLQTSDPDVYAAGDCAEVPHPVTGKTVYIPLASAANKQGRVAAENI-LGGP----APFPGLGTFI 302


                 ....*.
gi 186509939 343 SRFFKL 348
Cdd:COG0446  303 SKVFDL 308
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 31-316 1.27e-47

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: 165.18  E-value: 1.27e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939   31 KPGELAIISKEPVPPFERPELTKVYI----DLEVNPTLANIYVCAgTGEAKQYPN---WYKEKEIVKADLASKTL----- 98
Cdd:pfam07992  22 LGGKVTLIEDEGTCPYGGCVLSKALLgaaeAPEIASLWADLYKRK-EEVVKKLNNgieVLLGTEVVSIDPGAKKVvleel 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939   99 VSDDGKIYKYQTLLIATGSTNIRLSEIGVQEadvKNIFYLREIEDSDELALAMelyvQRGKAVIIGGGFLGLEISSALRA 178
Cdd:pfam07992 101 VDGDGETITYDRLVIATGARPRLPPIPGVEL---NVGFLVRTLDSAEALRLKL----LPKRVVVVGGGYIGVELAAALAK 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  179 NNHEVTMVFPEPWLVhRFFTAEIASFYESYYANKGIKIIKGTVATGFstNSDGEVTEVKLEDGRTLEANIVVAGVGARPA 258
Cdd:pfam07992 174 LGKEVTLIEALDRLL-RAFDEEISAALEKALEKNGVEVRLGTSVKEI--IGDGDGVEVILKDGTEIDADLVVVAIGRRPN 250

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  259 TSLFK--GQLEEEKGGIKTDGFFKTSVPDVYALGDVatfpmkmygGTRRVEHADNARKSA 316
Cdd:pfam07992 251 TELLEaaGLELDERGGIVVDEYLRTSVPGIYAAGDC---------RVGGPELAQNAVAQG 301
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
 34-301 2.00e-27

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


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 115.31  E-value: 2.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939   34 ELAIISKEPVPPFERPELTKVyidLEVNPTLANIYVCAGTGEAKQYPNWYKEKEIVKADLASKTLVSDDGKIYKYQTLLI 113
Cdd:TIGR02374  26 EITIFGEEPHPNYNRILLSSV---LQGEADLDDITLNSKDWYEKHGITLYTGETVIQIDTDQKQVITDAGRTLSYDKLIL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  114 ATGSTNIRLSeigVQEADVKNIFYLREIEDSDelalAMELYVQRG-KAVIIGGGFLGLEISSALRANNHEVTMVFPEPWL 192
Cdd:TIGR02374 103 ATGSYPFILP---IPGADKKGVYVFRTIEDLD----AIMAMAQRFkKAAVIGGGLLGLEAAVGLQNLGMDVSVIHHAPGL 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  193 VHRFFTAEIASFYESYYANKGIKIIKGTvaTGFSTNSDGEVTEVKLEDGRTLEANIVVAGVGARPATSLFKGQLEEEKGG 272
Cdd:TIGR02374 176 MAKQLDQTAGRLLQRELEQKGLTFLLEK--DTVEIVGATKADRIRFKDGSSLEADLIVMAAGIRPNDELAVSAGIKVNRG 253

                         250       260
                  ....*....|....*....|....*....
gi 186509939  273 IKTDGFFKTSVPDVYALGDVATFPMKMYG 301
Cdd:TIGR02374 254 IIVNDSMQTSDPDIYAVGECAEHNGRVYG 282
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 93-340 9.76e-26

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: 108.64  E-value: 9.76e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  93 LASKTLVSDDGKIYKYQTLLIATGSTNIRLSEIGVQEADVKnifylreieDSDElalAMELYVQRGKAVIIGGGFLGLEI 172
Cdd:COG1249  116 VDPHTVEVTGGETLTADHIVIATGSRPRVPPIPGLDEVRVL---------TSDE---ALELEELPKSLVVIGGGYIGLEF 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 173 SSALRANNHEVTMVFPEPWLVhRFFTAEIASFYESYYANKGIKIIKGTVATGFSTNSDGevTEVKLEDGR---TLEANIV 249
Cdd:COG1249  184 AQIFARLGSEVTLVERGDRLL-PGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDG--VTVTLEDGGgeeAVEADKV 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 250 VAGVGARPATSLFKgqLEE------EKGGIKTDGFFKTSVPDVYALGDVATFPMkmyggtrrvehadNARKSAAQAVKAI 323
Cdd:COG1249  261 LVATGRRPNTDGLG--LEAagveldERGGIKVDEYLRTSVPGIYAIGDVTGGPQ-------------LAHVASAEGRVAA 325

                        250
                 ....*....|....*....
gi 186509939 324 K--AGEEGKTIpDYDYLPY 340
Cdd:COG1249  326 EniLGKKPRPV-DYRAIPS 343
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
 33-372 1.59e-23

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 101.54  E-value: 1.59e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  33 GELAIISKEPVPPFERPELTKVYIdleVNPTLANIYVCAgtgeakqyPNWYKEKEI-------VKADLASK-TLVSDDGK 104
Cdd:PRK09754  29 GELHLFSDERHLPYERPPLSKSML---LEDSPQLQQVLP--------ANWWQENNVhlhsgvtIKTLGRDTrELVLTNGE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 105 IYKYQTLLIATGSTNIR---LSEIGvqeadvKNIFYLREIEDSDELALAmelyVQRGKAV-IIGGGFLGLEI---SSALR 177
Cdd:PRK09754  98 SWHWDQLFIATGAAARPlplLDALG------ERCFTLRHAGDAARLREV----LQPERSVvIVGAGTIGLELaasATQRR 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 178 ANnheVTMVFPEPWLVHRFFTAEIASFYESYYANKGIKIIkgtVATGFSTNSDGEVTEVKLEDGRTLEANIVVAGVGARp 257
Cdd:PRK09754 168 CK---VTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRIL---LNNAIEHVVDGEKVELTLQSGETLQADVVIYGIGIS- 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 258 atslFKGQLEEE-----KGGIKTDGFFKTSVPDVYALGDVAtFPMKMYGGTRRVEHADNARKSAAQAVKAIKAGEEGKTI 332
Cdd:PRK09754 241 ----ANDQLAREanldtANGIVIDEACRTCDPAIFAGGDVA-ITRLDNGALHRCESWENANNQAQIAAAAMLGLPLPLLP 315

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 186509939 333 PdydylPYFYSRFFKLSWEFYGENVGESVLFgDNDPKSPK 372
Cdd:PRK09754 316 P-----PWFWSDQYSDNLQFIGDMRGDDWLC-RGNPETQK 349
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 87-297 3.01e-23

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 101.38  E-value: 3.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  87 EIVK--ADLASKTLVS----DDGKIYKYQTLLIATGSTNIRLSEIgvqEADVKNIFylreieDSDElALAMElYVQRgKA 160
Cdd:PRK06416 108 DIIRgeAKLVDPNTVRvmteDGEQTYTAKNIILATGSRPRELPGI---EIDGRVIW------TSDE-ALNLD-EVPK-SL 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 161 VIIGGGFLGLEISSALRANNHEVTMVFPEPWLVHRFfTAEIASFYESYYANKGIKIIKGTVATGFSTNSDGeVTeVKLED 240
Cdd:PRK06416 176 VVIGGGYIGVEFASAYASLGAEVTIVEALPRILPGE-DKEISKLAERALKKRGIKIKTGAKAKKVEQTDDG-VT-VTLED 252

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 186509939 241 G---RTLEANIVVAGVGARPATSLFkGqLEE-----EKGGIKTDGFFKTSVPDVYALGDVATFPM 297
Cdd:PRK06416 253 GgkeETLEADYVLVAVGRRPNTENL-G-LEElgvktDRGFIEVDEQLRTNVPNIYAIGDIVGGPM 315
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
87-337 3.02e-23

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 100.59  E-value: 3.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  87 EIVKADLASKTLVSDDGKIYKYQTLLIATGSTNiRLSEI-GVQEadvkNIFYLREIEDS----DELALAMELYVQR--GK 159
Cdd:COG1252   77 EVTGIDPEARTVTLADGRTLSYDYLVIATGSVT-NFFGIpGLAE----HALPLKTLEDAlalrERLLAAFERAERRrlLT 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 160 AVIIGGGFLGLEISSAL-------------RANNHEVTMVFPEPWLVHRfFTAEIASFYESYYANKGIKIIKGTVATgfs 226
Cdd:COG1252  152 IVVVGGGPTGVELAGELaellrkllrypgiDPDKVRITLVEAGPRILPG-LGEKLSEAAEKELEKRGVEVHTGTRVT--- 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 227 tnsdgEVTE--VKLEDGRTLEANIVV--AGVGARPATSLFKGQLeEEKGGIKTDGFFKT-SVPDVYALGDVATFPMKMYG 301
Cdd:COG1252  228 -----EVDAdgVTLEDGEEIPADTVIwaAGVKAPPLLADLGLPT-DRRGRVLVDPTLQVpGHPNVFAIGDCAAVPDPDGK 301

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 186509939 302 GTRRVEHAdnARKSAAQAVKAIKAGEEGKTIPDYDY 337
Cdd:COG1252  302 PVPKTAQA--AVQQAKVLAKNIAALLRGKPLKPFRY 335
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 100-340 2.10e-21

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: 96.17  E-value: 2.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  100 SDDGKIYKYQTLLIATGSTNIRLSeiGVQEADVKNIFylreieDSDElalAMELYVQRGKAVIIGGGFLGLEISSALRAN 179
Cdd:TIGR01350 124 ENGEETLEAKNIIIATGSRPRSLP--GPFDFDGKVVI------TSTG---ALNLEEVPESLVIIGGGVIGIEFASIFASL 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  180 NHEVTMVFPEPWLVHrFFTAEIASFYESYYANKGIKIIKGTVATGFSTNSDGEVTEVKLEDGRTLEANIVVAGVGARPAT 259
Cdd:TIGR01350 193 GSKVTVIEMLDRILP-GEDAEVSKVLQKALKKKGVKILTNTKVTAVEKNDDQVTYENKGGETETLTGEKVLVAVGRKPNT 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  260 S---LFKGQLE-EEKGGIKTDGFFKTSVPDVYALGDVATFPMKmyggtrrvehadnARKSAAQAVKAIK--AGEEGKTIp 333
Cdd:TIGR01350 272 EglgLEKLGVElDERGRIVVDEYMRTNVPGIYAIGDVIGGPML-------------AHVASHEGIVAAEniAGKEPAHI- 337


                  ....*..
gi 186509939  334 DYDYLPY 340
Cdd:TIGR01350 338 DYDAVPS 344
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 85-294 1.45e-20

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 93.57  E-value: 1.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  85 EKEIVKADLASKTLVSDD---GKIY--KYQTLLIATGSTNIrLSEIGvqEADVKNIFYLREIEDSDELALAMElYVQRGK 159
Cdd:PRK09564  76 EHEVVKVDAKNKTITVKNlktGSIFndTYDKLMIATGARPI-IPPIK--NINLENVYTLKSMEDGLALKELLK-DEEIKN 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 160 AVIIGGGFLGLEISSALRANNHEVTMVFPEPWLVHRFFTAEIASFYESYYANKGIKIIKGTVATgfSTNSDGEVTEVKLE 239
Cdd:PRK09564 152 IVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHLNEFVK--SLIGEDKVEGVVTD 229

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 186509939 240 DGRtLEANIVVAGVGARPATSLFKGQLEE--EKGGIKTDGFFKTSVPDVYALGDVAT 294
Cdd:PRK09564 230 KGE-YEADVVIVATGVKPNTEFLEDTGLKtlKNGAIIVDEYGETSIENIYAAGDCAT 285
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
83-298 5.40e-20

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 89.79  E-value: 5.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  83 YKEKEIVKADLAS--KTLVSDDGKIYKYQTLLIATGSTNIRLSEIGVQEADVKNIFYlreiedsdelALAMELYVQRGKA 160
Cdd:COG0492   74 ILLEEVTSVDKDDgpFRVTTDDGTEYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSY----------CATCDGFFFRGKD 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 161 V-IIGGGFLGLEISSALRANNHEVTmvfpepwLVHRF--FTAEIASFyESYYANKGIKIIKGTVATGFstNSDGEVTEVK 237
Cdd:COG0492  144 VvVVGGGDSALEEALYLTKFASKVT-------LIHRRdeLRASKILV-ERLRANPKIEVLWNTEVTEI--EGDGRVEGVT 213

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 186509939 238 LEDGRT-----LEANIVVAGVGARPATSLFKGQ-LE-EEKGGIKTDGFFKTSVPDVYALGDVATFPMK 298
Cdd:COG0492  214 LKNVKTgeekeLEVDGVFVAIGLKPNTELLKGLgLElDEDGYIVVDEDMETSVPGVFAAGDVRDYKYR 281
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 90-297 5.83e-17

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 82.53  E-value: 5.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  90 KADLASKTLVSDDGKIYKYQTLLIATGSTNIRLSeiGVQEADVKNIFylreieDSDElalAMELYVQRGKAVIIGGGFLG 169
Cdd:PRK06292 113 TARFVDPNTVEVNGERIEAKNIVIATGSRVPPIP--GVWLILGDRLL------TSDD---AFELDKLPKSLAVIGGGVIG 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 170 LEISSALRANNHEVTM------VFPepwlvhrFFTAEIASFYESYYAnKGIKIIKGTVATGFSTNSDGEVTEVKLEDG-R 242
Cdd:PRK06292 182 LELGQALSRLGVKVTVfergdrILP-------LEDPEVSKQAQKILS-KEFKIKLGAKVTSVEKSGDEKVEELEKGGKtE 253

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 186509939 243 TLEANIVVAGVGARPAT---SLFKGQLE-EEKGGIKTDGFFKTSVPDVYALGDVATFPM 297
Cdd:PRK06292 254 TIEADYVLVATGRRPNTdglGLENTGIElDERGRPVVDEHTQTSVPGIYAAGDVNGKPP 312
PRK06116 PRK06116
glutathione reductase; Validated
 102-292 2.49e-16

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 80.59  E-value: 2.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 102 DGKIYKYQTLLIATGST----NIRLSEIGVqeadvknifylreieDSDElalAMELYVQRGKAVIIGGGFLGLEISSALR 177
Cdd:PRK06116 126 NGERYTADHILIATGGRpsipDIPGAEYGI---------------TSDG---FFALEELPKRVAVVGAGYIAVEFAGVLN 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 178 ANNHEVTMVF--PEPWlvhRFFTAEIASFYESYYANKGIKIIKGTVATGFSTNSDGEVTeVKLEDGRTLEANIVVAGVGA 255
Cdd:PRK06116 188 GLGSETHLFVrgDAPL---RGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADGSLT-LTLEDGETLTVDCLIWAIGR 263

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 186509939 256 RPATSLFkgQLE------EEKGGIKTDGFFKTSVPDVYALGDV 292
Cdd:PRK06116 264 EPNTDGL--GLEnagvklNEKGYIIVDEYQNTNVPGIYAVGDV 304
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
89-293 1.11e-14

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 74.95  E-value: 1.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  89 VKADLASKTLVSDDGKIYKYQTLLIATGSTnirlseigvqeADVKNIfylreieDSDELAL---------AMELYVQRGK 159
Cdd:PRK04965  81 VTDIDAEAQVVKSQGNQWQYDKLVLATGAS-----------AFVPPI-------PGRELMLtlnsqqeyrAAETQLRDAQ 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 160 AV-IIGGGFLGLEISSALRANNHEVTMVFPEPWLVHRFFTAEIASFYESYYANKGIKIIKGTVATGFSTNSDGEVteVKL 238
Cdd:PRK04965 143 RVlVVGGGLIGTELAMDLCRAGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIR--ATL 220

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 239 EDGRTLEANIVVAGVGARPATslfkgQLEEEKG-----GIKTDGFFKTSVPDVYALGDVA 293
Cdd:PRK04965 221 DSGRSIEVDAVIAAAGLRPNT-----ALARRAGlavnrGIVVDSYLQTSAPDIYALGDCA 275
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 159-241 3.18e-13

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: 64.53  E-value: 3.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  159 KAVIIGGGFLGLEISSALRANNHEVTMVFPEPWLVhRFFTAEIASFYESYYANKGIKIIKGTVATGFSTNSDGEVteVKL 238
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLL-PGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVV--VVL 77


                  ...
gi 186509939  239 EDG 241
Cdd:pfam00070  78 TDG 80
PLN02507 PLN02507
glutathione reductase
 102-340 3.58e-13

glutathione reductase


Pssm-ID: 215281 [Multi-domain]  Cd Length: 499  Bit Score: 71.00  E-value: 3.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 102 DGKIYKYQT--LLIATGSTNIRLSEIGvQEADVKnifylreiedSDElALAMELYVQRgkAVIIGGGFLGLEISSALRAN 179
Cdd:PLN02507 160 DGTKLRYTAkhILIATGSRAQRPNIPG-KELAIT----------SDE-ALSLEELPKR--AVVLGGGYIAVEFASIWRGM 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 180 NHEVTMVFPEPwLVHRFFTAEIASFYESYYANKGIKIIKGTVATGFSTNSDGevTEVKLEDGRTLEANIVVAGVGARPAT 259
Cdd:PLN02507 226 GATVDLFFRKE-LPLRGFDDEMRAVVARNLEGRGINLHPRTNLTQLTKTEGG--IKVITDHGEEFVADVVLFATGRAPNT 302

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 260 SLFkgQLEE------EKGGIKTDGFFKTSVPDVYALGDVatfpmkmyggTRRVEHADNARKSAAQAVKAIKAGEEGKtiP 333
Cdd:PLN02507 303 KRL--NLEAvgveldKAGAVKVDEYSRTNIPSIWAIGDV----------TNRINLTPVALMEGTCFAKTVFGGQPTK--P 368


                 ....*..
gi 186509939 334 DYDYLPY 340
Cdd:PLN02507 369 DYENVAC 375
PRK06370 PRK06370
FAD-containing oxidoreductase;
99-292 6.68e-13

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 70.23  E-value: 6.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  99 VSDDGKIYKYQTLLIATGSTNIRLSEIGVQEADvknifYLreieDSDELalaMELYVQRGKAVIIGGGFLGLEISSALRA 178
Cdd:PRK06370 125 VRVGGETLRAKRIFINTGARAAIPPIPGLDEVG-----YL----TNETI---FSLDELPEHLVIIGGGYIGLEFAQMFRR 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 179 NNHEVTMVFPEPWLVHRFfTAEIASFYESYYANKGIKIIKGTVATGFSTNSDGEVTEVKLEDGR-TLEANIVVAGVGARP 257
Cdd:PRK06370 193 FGSEVTVIERGPRLLPRE-DEDVAAAVREILEREGIDVRLNAECIRVERDGDGIAVGLDCNGGApEITGSHILVAVGRVP 271

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 186509939 258 ATSLFkgQLEE------EKGGIKTDGFFKTSVPDVYALGDV 292
Cdd:PRK06370 272 NTDDL--GLEAagvetdARGYIKVDDQLRTTNPGIYAAGDC 310
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
 108-294 2.71e-12

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 68.27  E-value: 2.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 108 YQTLLIATGSTNIRLSeigvqeADVKNIFYLREIEDSDelalAMELYVQRG---KAVIIGGGFLGLEISSALRANNHEVT 184
Cdd:PRK13512 106 YDKLILSPGASANSLG------FESDITFTLRNLEDTD----AIDQFIKANqvdKALVVGAGYISLEVLENLYERGLHPT 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 185 mvfpepwLVHR--------------FFTAEIASFYESYYANKGIKIIKGTvatgfstnsdgevtEVKLEDGRTLEANIVV 250
Cdd:PRK13512 176 -------LIHRsdkinklmdadmnqPILDELDKREIPYRLNEEIDAINGN--------------EVTFKSGKVEHYDMII 234

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 186509939 251 AGVGARPATSLFKGQ--LEEEKGGIKTDGFFKTSVPDVYALGDVAT 294
Cdd:PRK13512 235 EGVGTHPNSKFIESSniKLDDKGFIPVNDKFETNVPNIYAIGDIIT 280
PRK14989 PRK14989
nitrite reductase subunit NirD; Provisional
 92-301 4.01e-12

nitrite reductase subunit NirD; Provisional


Pssm-ID: 184951 [Multi-domain]  Cd Length: 847  Bit Score: 68.22  E-value: 4.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  92 DLASKTLVSDDGKIYKYQTLLIATGS----TNIRLSEigvqeadVKNIFYLREIEDSDelalAMELYVQRGK-AVIIGGG 166
Cdd:PRK14989  86 NRQEKVIHSSAGRTVFYDKLIMATGSypwiPPIKGSE-------TQDCFVYRTIEDLN----AIEACARRSKrGAVVGGG 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 167 FLGLEISSALRANNHEVTMVFPEPWLVhrfftAEIASFYESYYANKGIKIIKGTVATGFSTN---SDGEVTE--VKLEDG 241
Cdd:PRK14989 155 LLGLEAAGALKNLGVETHVIEFAPMLM-----AEQLDQMGGEQLRRKIESMGVRVHTSKNTLeivQEGVEARktMRFADG 229

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 186509939 242 RTLEANIVVAGVGARPATSLFK--GQLEEEKGGIKTDGFFKTSVPDVYALGDVATFPMKMYG 301
Cdd:PRK14989 230 SELEVDFIVFSTGIRPQDKLATqcGLAVAPRGGIVINDSCQTSDPDIYAIGECASWNNRVFG 291
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
 111-292 7.02e-12

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: 66.92  E-value: 7.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  111 LLIATGSTNIRLSEIGVQEADVKN-IFYLREIEDsdelalamelyvqrgKAVIIGGGFLGLE---ISSALRANNHEVTMV 186
Cdd:TIGR01423 155 ILLATGSWPQMLGIPGIEHCISSNeAFYLDEPPR---------------RVLTVGGGFISVEfagIFNAYKPRGGKVTLC 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  187 FPEPwLVHRFFTAEIASFYESYYANKGIKIIKGTVATGFSTNSDGEvTEVKLEDGRTLEANIVVAGVGARPATSLFkgQL 266
Cdd:TIGR01423 220 YRNN-MILRGFDSTLRKELTKQLRANGINIMTNENPAKVTLNADGS-KHVTFESGKTLDVDVVMMAIGRVPRTQTL--QL 295

                         170       180       190
                  ....*....|....*....|....*....|..
gi 186509939  267 EE------EKGGIKTDGFFKTSVPDVYALGDV 292
Cdd:TIGR01423 296 DKvgveltKKGAIQVDEFSRTNVPNIYAIGDV 327
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
98-296 9.79e-12

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


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 66.33  E-value: 9.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  98 LVSDDGKIYKYQ--TLLIATGSTNIRLSEIgvqEADVKNIFylreieDSDELaLAMElYVQRgKAVIIGGGFLGLEISSA 175
Cdd:PRK05249 126 VECPDGEVETLTadKIVIATGSRPYRPPDV---DFDHPRIY------DSDSI-LSLD-HLPR-SLIIYGAGVIGCEYASI 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 176 LRANNHEVTMVFPEPWLVHrFFTAEIA-SFyeSY-YANKGIKIIKGTVATGFSTNSDGevTEVKLEDGRTLEANIVVAGV 253
Cdd:PRK05249 194 FAALGVKVTLINTRDRLLS-FLDDEISdAL--SYhLRDSGVTIRHNEEVEKVEGGDDG--VIVHLKSGKKIKADCLLYAN 268

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 186509939 254 GARPAT-SLfkgQLEE------EKGGIKTDGFFKTSVPDVYALGDVATFP 296
Cdd:PRK05249 269 GRTGNTdGL---NLENagleadSRGQLKVNENYQTAVPHIYAVGDVIGFP 315
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 112-294 5.95e-11

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


Pssm-ID: 440259 [Multi-domain]  Cd Length: 434  Bit Score: 64.00  E-value: 5.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 112 LIATGSTNIRlsEIGVQEADVKNIF----YLREIEdsdeLALAMELYVQRGK-AVIIGGGFLGLE-ISSALRANNHEVTM 185
Cdd:COG0493  211 FLATGAGKPR--DLGIPGEDLKGVHsamdFLTAVN----LGEAPDTILAVGKrVVVIGGGNTAMDcARTALRLGAESVTI 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 186 VFPEPwlvhrffTAEI-ASFYESYYA-NKGIKIIKGTVATGFSTNSDGEVTEVKL---------EDGR-----------T 243
Cdd:COG0493  285 VYRRT-------REEMpASKEEVEEAlEEGVEFLFLVAPVEIIGDENGRVTGLECvrmelgepdESGRrrpvpiegsefT 357

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 186509939 244 LEANIVVAGVGARPATSLFKGQLE---EEKGGIKTD-GFFKTSVPDVYALGDVAT 294
Cdd:COG0493  358 LPADLVILAIGQTPDPSGLEEELGlelDKRGTIVVDeETYQTSLPGVFAGGDAVR 412
PRK07846 PRK07846
mycothione reductase; Reviewed
 94-298 8.05e-11

mycothione reductase; Reviewed


Pssm-ID: 181142 [Multi-domain]  Cd Length: 451  Bit Score: 63.43  E-value: 8.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  94 ASKTLVSDDGKIYKYQTLLIATGSTNIRLSEIGvqEADVKnifylreIEDSDELalaMELYVQRGKAVIIGGGFLGLEIS 173
Cdd:PRK07846 115 GPKTLRTGDGEEITADQVVIAAGSRPVIPPVIA--DSGVR-------YHTSDTI---MRLPELPESLVIVGGGFIAAEFA 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 174 SALRANNHEVTMVFPEPWLVhRFFTAEIA-SFYEsyYANKGIKIIKGTVATGFSTNSDGevTEVKLEDGRTLEANIVVAG 252
Cdd:PRK07846 183 HVFSALGVRVTVVNRSGRLL-RHLDDDISeRFTE--LASKRWDVRLGRNVVGVSQDGSG--VTLRLDDGSTVEADVLLVA 257

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 186509939 253 VGARPATSLF---KGQLE-EEKGGIKTDGFFKTSVPDVYALGDVAT-FPMK 298
Cdd:PRK07846 258 TGRVPNGDLLdaaAAGVDvDEDGRVVVDEYQRTSAEGVFALGDVSSpYQLK 308
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
 101-297 9.45e-10

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 60.32  E-value: 9.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 101 DDGKIYKYQTLLIATGSTNIRLSEIGVQEadvknifylREIEDSDElALAMElyVQRGKAVIIGGGFLGLEISSALRANN 180
Cdd:PRK06327 139 EDETVITAKHVIIATGSEPRHLPGVPFDN---------KIILDNTG-ALNFT--EVPKKLAVIGAGVIGLELGSVWRRLG 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 181 HEVTMVFPEPwlvhRFFTA---EIASFYESYYANKGIKIIKGtVATGFSTNSDGEVTeVKLEDG----RTLEANIVVAGV 253
Cdd:PRK06327 207 AEVTILEALP----AFLAAadeQVAKEAAKAFTKQGLDIHLG-VKIGEIKTGGKGVS-VAYTDAdgeaQTLEVDKLIVSI 280

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 186509939 254 GARPATSLFK----GQLEEEKGGIKTDGFFKTSVPDVYALGDVATFPM 297
Cdd:PRK06327 281 GRVPNTDGLGleavGLKLDERGFIPVDDHCRTNVPNVYAIGDVVRGPM 328
PRK07251 PRK07251
FAD-containing oxidoreductase;
101-292 2.10e-09

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 58.99  E-value: 2.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 101 DDGKIYKYQTLLIATGSTNIRLSEIGVqeADVKNIFylreieDSDELalaMELYVQRGKAVIIGGGFLGLEISSALRANN 180
Cdd:PRK07251 112 DEKIELTAETIVINTGAVSNVLPIPGL--ADSKHVY------DSTGI---QSLETLPERLGIIGGGNIGLEFAGLYNKLG 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 181 HEVTMVFPEPWLVHRFfTAEIASFYESYYANKGIKIIKGtvATGFSTNSDGEVTEVKLEDGrTLEANIVVAGVGARPATS 260
Cdd:PRK07251 181 SKVTVLDAASTILPRE-EPSVAALAKQYMEEDGITFLLN--AHTTEVKNDGDQVLVVTEDE-TYRFDALLYATGRKPNTE 256

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 186509939 261 LFkgQLEE------EKGGIKTDGFFKTSVPDVYALGDV 292
Cdd:PRK07251 257 PL--GLENtdieltERGAIKVDDYCQTSVPGVFAVGDV 292
PLN02546 PLN02546
glutathione reductase
 99-339 6.12e-09

glutathione reductase


Pssm-ID: 215301 [Multi-domain]  Cd Length: 558  Bit Score: 57.96  E-value: 6.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  99 VSDDGKIYKYQTLLIATGStnirlseigvqEADVKNIFYLREIEDSDElalAMELYVQRGKAVIIGGGFLGLEISSALRA 178
Cdd:PLN02546 208 VDVDGKLYTARNILIAVGG-----------RPFIPDIPGIEHAIDSDA---ALDLPSKPEKIAIVGGGYIALEFAGIFNG 273

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 179 NNHEVtMVFPEPWLVHRFFTAEIASFYESYYANKGIKIIKGTVATGFSTNSDGEVTeVKLEDGRTLEANIVVAGVGARPA 258
Cdd:PLN02546 274 LKSDV-HVFIRQKKVLRGFDEEVRDFVAEQMSLRGIEFHTEESPQAIIKSADGSLS-LKTNKGTVEGFSHVMFATGRKPN 351

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 259 TSLFKgqLEE------EKGGIKTDGFFKTSVPDVYALGDVatfpmkmyggTRRVEHADNARKSAAQAVKAIKAGEEGKti 332
Cdd:PLN02546 352 TKNLG--LEEvgvkmdKNGAIEVDEYSRTSVPSIWAVGDV----------TDRINLTPVALMEGGALAKTLFGNEPTK-- 417


                 ....*..
gi 186509939 333 PDYDYLP 339
Cdd:PLN02546 418 PDYRAVP 424
PRK07845 PRK07845
flavoprotein disulfide reductase; Reviewed
 87-292 2.10e-08

flavoprotein disulfide reductase; Reviewed


Pssm-ID: 236112 [Multi-domain]  Cd Length: 466  Bit Score: 56.02  E-value: 2.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  87 EIVKADLASKTLVSDdgkiykyqTLLIATGSTNIRLSEigvQEADVKNIFYLREIEDSDELAlaMELyvqrgkaVIIGGG 166
Cdd:PRK07845 127 KVTTADGGEETLDAD--------VVLIATGASPRILPT---AEPDGERILTWRQLYDLDELP--EHL-------IVVGSG 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 167 FLGLEISSALRANNHEVTMV------FP-EpwlvhrffTAEIASFYESYYANKGIKIIKGTVATGFSTNSDGevTEVKLE 239
Cdd:PRK07845 187 VTGAEFASAYTELGVKVTLVssrdrvLPgE--------DADAAEVLEEVFARRGMTVLKRSRAESVERTGDG--VVVTLT 256

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 186509939 240 DGRTLEANIVVAGVGARPATS---LFKGQLEEEKGG-IKTDGFFKTSVPDVYALGDV 292
Cdd:PRK07845 257 DGRTVEGSHALMAVGSVPNTAglgLEEAGVELTPSGhITVDRVSRTSVPGIYAAGDC 313
TGR TIGR01438
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ...
 79-339 2.80e-07

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: 52.55  E-value: 2.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939   79 YPNWYKEkeIVKADLASKTLVSDDGKIYKYQTLLIATGstnIRLSEIGVQEADVKNIfylreieDSDELalaMELYVQRG 158
Cdd:TIGR01438 117 YENAYAE--FVDKHRIKATNKKGKEKIYSAERFLIATG---ERPRYPGIPGAKELCI-------TSDDL---FSLPYCPG 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  159 KAVIIGGGFLGLEISSALRANNHEVTMVFPEpwLVHRFFTAEIASFYESYYANKGIKIIKGTVATGFST-NSDGEVTEVK 237
Cdd:TIGR01438 182 KTLVVGASYVALECAGFLAGIGLDVTVMVRS--ILLRGFDQDCANKVGEHMEEHGVKFKRQFVPIKVEQiEAKVLVEFTD 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  238 LEDGRTLEANIVVAGVGARPATSlfKGQLE-------EEKGGIKTDGFFKTSVPDVYALGDVAtfpmkmyggTRRVEHAD 310
Cdd:TIGR01438 260 STNGIEEEYDTVLLAIGRDACTR--KLNLEnvgvkinKKTGKIPADEEEQTNVPYIYAVGDIL---------EDKPELTP 328

                         250       260
                  ....*....|....*....|....*....
gi 186509939  311 NARKSAAQAVKAIKAGEegKTIPDYDYLP 339
Cdd:TIGR01438 329 VAIQAGRLLAQRLFKGS--TVICDYENVP 355
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
161-268 2.48e-06

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 49.36  E-value: 2.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 161 VIIGGGFLGLEISSALR---ANNHEVTMVFPEPW-----LVHRFFTA-----EIASFYESYYANKGIKIIKGTVaTGFST 227
Cdd:COG1252    5 VIVGGGFAGLEAARRLRkklGGDAEVTLIDPNPYhlfqpLLPEVAAGtlspdDIAIPLRELLRRAGVRFIQGEV-TGIDP 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 186509939 228 NSDgevtEVKLEDGRTLEANIVVAGVGARPATSLFKGqLEE 268
Cdd:COG1252   84 EAR----TVTLADGRTLSYDYLVIATGSVTNFFGIPG-LAE 119
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 107-333 8.71e-06

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 47.84  E-value: 8.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 107 KYQTLLIATGSTNIRLSEIGVQEadvkNIFYLREIEDSDEL--------------ALAMELYVQRGKAVIIGGGFLGLEI 172
Cdd:PTZ00318 113 PYDKLVVAHGARPNTFNIPGVEE----RAFFLKEVNHARGIrkrivqcieraslpTTSVEERKRLLHFVVVGGGPTGVEF 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 173 SSAL--------RANNHEVTmvfPEPWLVHRFFTAEIASFYESYYANKGIKIIKgtvATGFSTNSDGEVTEVK-----LE 239
Cdd:PTZ00318 189 AAELadffrddvRNLNPELV---EECKVTVLEAGSEVLGSFDQALRKYGQRRLR---RLGVDIRTKTAVKEVLdkevvLK 262

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 240 DGRTLEANIVV--AGVGARPATSLFKGQlEEEKGGIKTDGFFKTS-VPDVYALGDVATFPMKMYGGTRRVehadnARKSA 316
Cdd:PTZ00318 263 DGEVIPTGLVVwsTGVGPGPLTKQLKVD-KTSRGRISVDDHLRVKpIPNVFALGDCAANEERPLPTLAQV-----ASQQG 336

                        250
                 ....*....|....*..
gi 186509939 317 AQAVKAIKAGEEGKTIP 333
Cdd:PTZ00318 337 VYLAKEFNNELKGKPMS 353
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 107-294 9.92e-06

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 47.48  E-value: 9.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 107 KYQTLLIATGSTNIRlsEIGVQEADVKNIF----YLREIEDSDELAlamELYVQRgKAVIIGGGFLGLE-ISSALRANNH 181
Cdd:PRK11749 225 GYDAVFIGTGAGLPR--FLGIPGENLGGVYsavdFLTRVNQAVADY---DLPVGK-RVVVIGGGNTAMDaARTAKRLGAE 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 182 EVTMVFpepwlvhRFFTAEI-ASFYESYYA-NKGIKIIKGTVATGFSTNSDGeVTEVKLE---------DGR-------- 242
Cdd:PRK11749 299 SVTIVY-------RRGREEMpASEEEVEHAkEEGVEFEWLAAPVEILGDEGR-VTGVEFVrmelgepdaSGRrrvpiegs 370

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 186509939 243 --TLEANIVVAGVGARPATSLFKGQLEEE---KGGIKTD-GFFKTSVPDVYALGDVAT 294
Cdd:PRK11749 371 efTLPADLVIKAIGQTPNPLILSTTPGLElnrWGTIIADdETGRTSLPGVFAGGDIVT 428
PRK08010 PRK08010
pyridine nucleotide-disulfide oxidoreductase; Provisional
 158-292 2.76e-05

pyridine nucleotide-disulfide oxidoreductase; Provisional


Pssm-ID: 181196 [Multi-domain]  Cd Length: 441  Bit Score: 46.16  E-value: 2.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 158 GKAVIIGGGFLGLEISSALRANNHEVTMVFPEPWLVHRFfTAEIASFYESYYANKGIKIIKGTVATGFSTNsDGEVtEVK 237
Cdd:PRK08010 159 GHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPRE-DRDIADNIATILRDQGVDIILNAHVERISHH-ENQV-QVH 235

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 186509939 238 LEDGRTLEANIVVAGvGARPATSLFK----GQLEEEKGGIKTDGFFKTSVPDVYALGDV 292
Cdd:PRK08010 236 SEHAQLAVDALLIAS-GRQPATASLHpenaGIAVNERGAIVVDKYLHTTADNIWAMGDV 293
PRK13984 PRK13984
putative oxidoreductase; Provisional
 107-296 4.33e-05

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 45.91  E-value: 4.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 107 KYQTLLIATGSTNIRLSEI-GVQEADVKN-IFYLREIEDSDElALAMELYVQRgKAVIIGGGFLGLEIS-SALRANNHE- 182
Cdd:PRK13984 368 KHDAVFLSTGFTLGRSTRIpGTDHPDVIQaLPLLREIRDYLR-GEGPKPKIPR-SLVVIGGGNVAMDIArSMARLQKMEy 445

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 183 ----VTMVFPEPWLVHrfFTAEIASFYESyyANKGIKIIKGTVATGFSTNSDG-------EVTEVKLEDGR--------- 242
Cdd:PRK13984 446 gevnVKVTSLERTFEE--MPADMEEIEEG--LEEGVVIYPGWGPMEVVIENDKvkgvkfkKCVEVFDEEGRfnpkfdesd 521

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 243 --TLEANIVVAGVGARPATSLF----KGQLEEEKGGIKTDGFFKTSVPDVYALGDVATFP 296
Cdd:PRK13984 522 qiIVEADMVVEAIGQAPDYSYLpeelKSKLEFVRGRILTNEYGQTSIPWLFAGGDIVHGP 581
PTZ00058 PTZ00058
glutathione reductase; Provisional
 101-291 8.54e-05

glutathione reductase; Provisional


Pssm-ID: 185420 [Multi-domain]  Cd Length: 561  Bit Score: 44.99  E-value: 8.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 101 DDGKIYKYQTLLIATGSTNIRLSEIGVQEA-DVKNIFYLREIEdsdelalamelyvqrgKAVIIGGGFLGLEISSALRAN 179
Cdd:PTZ00058 196 DDGQVIEGKNILIAVGNKPIFPDVKGKEFTiSSDDFFKIKEAK----------------RIGIAGSGYIAVELINVVNRL 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 180 NHEvTMVFPEPWLVHRFFTAEIASFYESYYANKGIKIIKGTVATGFSTNSDGEVTEVKLEDGRTLEANIVVAGVGARPAT 259
Cdd:PTZ00058 260 GAE-SYIFARGNRLLRKFDETIINELENDMKKNNINIITHANVEEIEKVKEKNLTIYLSDGRKYEHFDYVIYCVGRSPNT 338

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 186509939 260 SLFKGQ---LEEEKGGIKTDGFFKTSVPDVYALGD 291
Cdd:PTZ00058 339 EDLNLKalnIKTPKGYIKVDDNQRTSVKHIYAVGD 373
PTZ00052 PTZ00052
thioredoxin reductase; Provisional
 91-339 1.01e-04

thioredoxin reductase; Provisional


Pssm-ID: 185416 [Multi-domain]  Cd Length: 499  Bit Score: 44.43  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  91 ADLASKTLVS--DDGKIYKYQT--LLIATGS-TNIRLSEIGVQEADVK--NIFYLREIEdsdelalamelyvqrGKAVII 163
Cdd:PTZ00052 124 AKLKDEHTVSygDNSQEETITAkyILIATGGrPSIPEDVPGAKEYSITsdDIFSLSKDP---------------GKTLIV 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 164 GGGFLGLEISSALRANNHEVTMVFPEpwLVHRFFTAEIASFYESYYANKGIKIIKGTVATGFSTNSDGevTEVKLEDGRT 243
Cdd:PTZ00052 189 GASYIGLETAGFLNELGFDVTVAVRS--IPLRGFDRQCSEKVVEYMKEQGTLFLEGVVPINIEKMDDK--IKVLFSDGTT 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 244 LEANIVVAGVGARPATSLFKGQ---LEEEKGGIKTDGFFKTSVPDVYALGDVATFPMKMyggtrrvehadnarksaaqAV 320
Cdd:PTZ00052 265 ELFDTVLYATGRKPDIKGLNLNaigVHVNKSNKIIAPNDCTNIPNIFAVGDVVEGRPEL-------------------TP 325

                        250       260
                 ....*....|....*....|....*..
gi 186509939 321 KAIKAGE--------EGKTIPDYDYLP 339
Cdd:PTZ00052 326 VAIKAGIllarrlfkQSNEFIDYTFIP 352
PRK07333 PRK07333
ubiquinone biosynthesis hydroxylase;
213-278 7.25e-04

ubiquinone biosynthesis hydroxylase;


Pssm-ID: 180935 [Multi-domain]  Cd Length: 403  Bit Score: 41.50  E-value: 7.25e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 186509939 213 GIKIIKGTVATGFSTNSDGevTEVKLEDGRTLEANIVVAGVGARPATslfkgqleEEKGGIKTDGF 278
Cdd:PRK07333 125 GIDLREATSVTDFETRDEG--VTVTLSDGSVLEARLLVAADGARSKL--------RELAGIKTVGW 180
PTZ00153 PTZ00153
lipoamide dehydrogenase; Provisional
 103-332 8.10e-04

lipoamide dehydrogenase; Provisional


Pssm-ID: 173442 [Multi-domain]  Cd Length: 659  Bit Score: 41.82  E-value: 8.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 103 GKIYKYQTLLIATGSTNIRLSEIgvqEADVKNIFylreieDSDElalAMELYVQRGKAVIIGGGFLGLEISSALRANNHE 182
Cdd:PTZ00153 270 GKEFKVKNIIIATGSTPNIPDNI---EVDQKSVF------TSDT---AVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSE 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 183 VTMVFPEPWLVhRFFTAEIASFYE---------SYYANKGIKIIKGT-----VATGFSTNSDGEVTEVK--LEDGRTLEA 246
Cdd:PTZ00153 338 VVSFEYSPQLL-PLLDADVAKYFErvflkskpvRVHLNTLIEYVRAGkgnqpVIIGHSERQTGESDGPKknMNDIKETYV 416

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 247 NIVVAGVGARPATS---LFKGQLEEEKGGIKTDGFFKTSVPD------VYALGDVatfpmkmyGGTRRVEHAdnarkSAA 317
Cdd:PTZ00153 417 DSCLVATGRKPNTNnlgLDKLKIQMKRGFVSVDEHLRVLREDqevydnIFCIGDA--------NGKQMLAHT-----ASH 483

                        250
                 ....*....|....*..
gi 186509939 318 QAVKAIK--AGEEGKTI 332
Cdd:PTZ00153 484 QALKVVDwiEGKGKENV 500
PRK12831 PRK12831
putative oxidoreductase; Provisional
 155-320 9.45e-04

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 41.54  E-value: 9.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 155 VQRGKAV-IIGGGFLGLEIS-SALRANnhevtmvfPEPWLVHRFFTAEIASFYESYYANK--GIKIIKGTVATGFSTNSD 230
Cdd:PRK12831 278 IKVGKKVaVVGGGNVAMDAArTALRLG--------AEVHIVYRRSEEELPARVEEVHHAKeeGVIFDLLTNPVEILGDEN 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 231 GEVTEVKLE---------DGR-----------TLEANIVVAGVGARP---ATSLFKGQLEEEKGGIKTD-GFFKTSVPDV 286
Cdd:PRK12831 350 GWVKGMKCIkmelgepdaSGRrrpveiegsefVLEVDTVIMSLGTSPnplISSTTKGLKINKRGCIVADeETGLTSKEGV 429

                        170       180       190
                 ....*....|....*....|....*....|....
gi 186509939 287 YALGDVATfpmkmygGTRRVEHADNARKSAAQAV 320
Cdd:PRK12831 430 FAGGDAVT-------GAATVILAMGAGKKAAKAI 456
PRK10262 PRK10262
thioredoxin reductase; Provisional
 88-292 1.13e-03

thioredoxin reductase; Provisional


Pssm-ID: 182343 [Multi-domain]  Cd Length: 321  Bit Score: 40.82  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939  88 IVKADLASKT--LVSDDGKiYKYQTLLIATGSTnIRLSEIGVQEAdvkniFYLREIEdsdELALAMELYVQRGKAVIIGG 165
Cdd:PRK10262  85 INKVDLQNRPfrLTGDSGE-YTCDALIIATGAS-ARYLGLPSEEA-----FKGRGVS---ACATCDGFFYRNQKVAVIGG 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 166 GFLGLEisSALRANNhevtmVFPEPWLVHRfftaeiasfYESYYANK-GIKIIKGTVATG---FSTNSDGE--------V 233
Cdd:PRK10262 155 GNTAVE--EALYLSN-----IASEVHLIHR---------RDGFRAEKiLIKRLMDKVENGniiLHTNRTLEevtgdqmgV 218

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 234 TEVKLEDGR------TLEANIVVAGVGARPATSLFKGQLEEEKGGIKTDGFF-----KTSVPDVYALGDV 292
Cdd:PRK10262 219 TGVRLRDTQnsdnieSLDVAGLFVAIGHSPNTAIFEGQLELENGYIKVQSGIhgnatQTSIPGVFAAGDV 288
PRK13748 PRK13748
putative mercuric reductase; Provisional
 161-304 2.20e-03

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 40.13  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 161 VIIGGGFLGLEISSALRANNHEVTMVfpepwLVHRFFTAEIASFYESYYA---NKGIKIIKGTVATGFStNSDGEVTevk 237
Cdd:PRK13748 274 AVIGSSVVALELAQAFARLGSKVTIL-----ARSTLFFREDPAIGEAVTAafrAEGIEVLEHTQASQVA-HVDGEFV--- 344

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 186509939 238 LEDGR-TLEANIVVAGVGARPATSLFK----GQLEEEKGGIKTDGFFKTSVPDVYALGDVATFPMKMY----GGTR 304
Cdd:PRK13748 345 LTTGHgELRADKLLVATGRAPNTRSLAldaaGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQPQFVYvaaaAGTR 420
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 214-298 5.46e-03

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 38.99  E-value: 5.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509939 214 IKIIKGtVATGFSTNSDGEVTEVKLEDGRTLEANIV-VAGV----GARPATSLFKGQLE-EEKGGIKTDGFFKTSVPDVY 287
Cdd:PRK15317 402 VTIITN-AQTTEVTGDGDKVTGLTYKDRTTGEEHHLeLEGVfvqiGLVPNTEWLKGTVElNRRGEIIVDARGATSVPGVF 480

                         90
                 ....*....|.
gi 186509939 288 ALGDVATFPMK 298
Cdd:PRK15317 481 AAGDCTTVPYK 491
 
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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