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Conserved domains on  [gi|1371933378|ref|WP_106835705|]
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NAD(P)/FAD-dependent oxidoreductase [Brevibacillus porteri]

Protein Classification

NAD(P)/FAD-dependent oxidoreductase( domain architecture ID 11422994)

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

CATH:  3.50.50.60
EC:  1.-.-.-
Gene Ontology:  GO:0050660|GO:0016491
PubMed:  33684359

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
6-297 8.13e-55

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


:

Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 180.32  E-value: 8.13e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSCLLIEKtDRLGGQLHhIYNEITDFPPLVYD-QGAALVKVLIAH--PFiqQPNIRLnE 82
Cdd:COG0492     3 VVIIGAGPAGLTAAIYAARAGLKTLVIEG-GEPGGQLA-TTKEIENYPGFPEGiSGPELAERLREQaeRF--GAEILL-E 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378  83 AILSIDRE--TKQVITSK-SVYRVDYLLIATGVGWNEIPaladCPSVLSPW-----FSTTAQAHTIAGQDIAVIGGGDRA 154
Cdd:COG0492    78 EVTSVDKDdgPFRVTTDDgTEYEAKAVIIATGAGPRKLG----LPGEEEFEgrgvsYCATCDGFFFRGKDVVVVGGGDSA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 155 LESAANLSFHARQVYLLVRSSEWRARPEWQKKITGLPNIQVLWETQVSDYQHEEARTVLTLTSTRTGNPETIVVDWILPR 234
Cdd:COG0492   154 LEEALYLTKFASKVTLIHRRDELRASKILVERLRANPKIEVLWNTEVTEIEGDGRVEGVTLKNVKTGEEKELEVDGVFVA 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371933378 235 IGVHGNTAGFD--GLDMFGDDYLQTDSSQRVNSPWIYAVGDVNNGaAYASLSLAVGQAMKAVKHI 297
Cdd:COG0492   234 IGLKPNTELLKglGLELDEDGYIVVDEDMETSVPGVFAAGDVRDY-KYRQAATAAGEGAIAALSA 297
 
Name Accession Description Interval E-value
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
6-297 8.13e-55

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 180.32  E-value: 8.13e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSCLLIEKtDRLGGQLHhIYNEITDFPPLVYD-QGAALVKVLIAH--PFiqQPNIRLnE 82
Cdd:COG0492     3 VVIIGAGPAGLTAAIYAARAGLKTLVIEG-GEPGGQLA-TTKEIENYPGFPEGiSGPELAERLREQaeRF--GAEILL-E 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378  83 AILSIDRE--TKQVITSK-SVYRVDYLLIATGVGWNEIPaladCPSVLSPW-----FSTTAQAHTIAGQDIAVIGGGDRA 154
Cdd:COG0492    78 EVTSVDKDdgPFRVTTDDgTEYEAKAVIIATGAGPRKLG----LPGEEEFEgrgvsYCATCDGFFFRGKDVVVVGGGDSA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 155 LESAANLSFHARQVYLLVRSSEWRARPEWQKKITGLPNIQVLWETQVSDYQHEEARTVLTLTSTRTGNPETIVVDWILPR 234
Cdd:COG0492   154 LEEALYLTKFASKVTLIHRRDELRASKILVERLRANPKIEVLWNTEVTEIEGDGRVEGVTLKNVKTGEEKELEVDGVFVA 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371933378 235 IGVHGNTAGFD--GLDMFGDDYLQTDSSQRVNSPWIYAVGDVNNGaAYASLSLAVGQAMKAVKHI 297
Cdd:COG0492   234 IGLKPNTELLKglGLELDEDGYIVVDEDMETSVPGVFAAGDVRDY-KYRQAATAAGEGAIAALSA 297
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
5-274 1.40e-28

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: 111.64  E-value: 1.40e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378   5 QVLIAGGGIAGLSAAIWCHRLGLSCLLIE-KTDRLGGQ--LHHIYNEITDFPPLVYDqGAALVKVLIAHPFIQQPNIR-- 79
Cdd:pfam07992   2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEdEGTCPYGGcvLSKALLGAAEAPEIASL-WADLYKRKEEVVKKLNNGIEvl 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378  80 LNEAILSIDRETKQVITSKSV------YRVDYLLIATGVGWN--EIPALAD-CPSVLSPWFSTTAQAHTIAGQDIAVIGG 150
Cdd:pfam07992  81 LGTEVVSIDPGAKKVVLEELVdgdgetITYDRLVIATGARPRlpPIPGVELnVGFLVRTLDSAEALRLKLLPKRVVVVGG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 151 GDRALESAANLSFHARQVYLLVRSSEW------RARPEWQKKITGLpNIQVLWETQVSDYQHEEarTVLTLTstrTGNPE 224
Cdd:pfam07992 161 GYIGVELAAALAKLGKEVTLIEALDRLlrafdeEISAALEKALEKN-GVEVRLGTSVKEIIGDG--DGVEVI---LKDGT 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1371933378 225 TIVVDWILPRIGVHGNTAGFD--GLDMFGDDYLQTDSSQRVNSPWIYAVGDV 274
Cdd:pfam07992 235 EIDADLVVVAIGRRPNTELLEaaGLELDERGGIVVDEYLRTSVPGIYAAGDC 286
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
6-293 7.48e-16

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 77.51  E-value: 7.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSCLLIekTDRLGGQLhhiyNE---ITDFPPLVYDQGAALVKVLIAHpfIQQPNIRL-- 80
Cdd:PRK15317  214 VLVVGGGPAGAAAAIYAARKGIRTGIV--AERFGGQV----LDtmgIENFISVPETEGPKLAAALEEH--VKEYDVDImn 285
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378  81 ---------NEAILSIDRETKQVITSKSVyrvdylLIATGVGWNEI--P--------ALADCPSVLSPWFSttaqahtia 141
Cdd:PRK15317  286 lqrasklepAAGLIEVELANGAVLKAKTV------ILATGARWRNMnvPgedeyrnkGVAYCPHCDGPLFK--------- 350
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 142 GQDIAVIGGGDRALESAANLSFHARQVYLLVRSSEWRARPEWQKKITGLPNIQVLWETQVSDYQHEEAR-TVLTLTSTRT 220
Cdd:PRK15317  351 GKRVAVIGGGNSGVEAAIDLAGIVKHVTVLEFAPELKADQVLQDKLRSLPNVTIITNAQTTEVTGDGDKvTGLTYKDRTT 430
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371933378 221 GNPETIVVDWILPRIGVHGNTAGFDG---LDMFGDdyLQTDSSQRVNSPWIYAVGDVNNgAAYASLSLAVGQAMKA 293
Cdd:PRK15317  431 GEEHHLELEGVFVQIGLVPNTEWLKGtveLNRRGE--IIVDARGATSVPGVFAAGDCTT-VPYKQIIIAMGEGAKA 503
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
6-297 4.27e-14

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: 72.29  E-value: 4.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSCLLIEKtDRLGGQ------------LH--HIYNEIT--------------DFPPLVy 57
Cdd:TIGR01350   4 VIVIGGGPGGYVAAIRAAQLGLKVALVEK-EYLGGTclnvgciptkalLHsaEVYDEIKhakdlgievenvsvDWEKMQ- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378  58 DQGAALVKVLIA--HPFIQQPNIRL--NEAILSIDRETKqVITSKS--VYRVDYLLIATGVGWNEIPAL--ADCPSVLSp 129
Cdd:TIGR01350  82 KRKNKVVKKLVGgvSGLLKKNKVTVikGEAKFLDPGTVS-VTGENGeeTLEAKNIIIATGSRPRSLPGPfdFDGKVVIT- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 130 wfSTTAQAHTIAGQDIAVIGGGDRALESAanLSFHARQVYLLVRSSEWRARPEWQKKITGL-------PNIQVLWETQVS 202
Cdd:TIGR01350 160 --STGALNLEEVPESLVIIGGGVIGIEFA--SIFASLGSKVTVIEMLDRILPGEDAEVSKVlqkalkkKGVKILTNTKVT 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 203 DYQHEEARTVLtltSTRTGNPETIVVDWILPRIGVHGNTAGFD----GLDMFGDDYLQTDSSQRVNSPWIYAVGDVNNGA 278
Cdd:TIGR01350 236 AVEKNDDQVTY---ENKGGETETLTGEKVLVAVGRKPNTEGLGleklGVELDERGRIVVDEYMRTNVPGIYAIGDVIGGP 312
                         330
                  ....*....|....*....
gi 1371933378 279 AYAslSLAVGQAMKAVKHI 297
Cdd:TIGR01350 313 MLA--HVASHEGIVAAENI 329
 
Name Accession Description Interval E-value
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
6-297 8.13e-55

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 180.32  E-value: 8.13e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSCLLIEKtDRLGGQLHhIYNEITDFPPLVYD-QGAALVKVLIAH--PFiqQPNIRLnE 82
Cdd:COG0492     3 VVIIGAGPAGLTAAIYAARAGLKTLVIEG-GEPGGQLA-TTKEIENYPGFPEGiSGPELAERLREQaeRF--GAEILL-E 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378  83 AILSIDRE--TKQVITSK-SVYRVDYLLIATGVGWNEIPaladCPSVLSPW-----FSTTAQAHTIAGQDIAVIGGGDRA 154
Cdd:COG0492    78 EVTSVDKDdgPFRVTTDDgTEYEAKAVIIATGAGPRKLG----LPGEEEFEgrgvsYCATCDGFFFRGKDVVVVGGGDSA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 155 LESAANLSFHARQVYLLVRSSEWRARPEWQKKITGLPNIQVLWETQVSDYQHEEARTVLTLTSTRTGNPETIVVDWILPR 234
Cdd:COG0492   154 LEEALYLTKFASKVTLIHRRDELRASKILVERLRANPKIEVLWNTEVTEIEGDGRVEGVTLKNVKTGEEKELEVDGVFVA 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371933378 235 IGVHGNTAGFD--GLDMFGDDYLQTDSSQRVNSPWIYAVGDVNNGaAYASLSLAVGQAMKAVKHI 297
Cdd:COG0492   234 IGLKPNTELLKglGLELDEDGYIVVDEDMETSVPGVFAAGDVRDY-KYRQAATAAGEGAIAALSA 297
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
5-274 1.40e-28

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: 111.64  E-value: 1.40e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378   5 QVLIAGGGIAGLSAAIWCHRLGLSCLLIE-KTDRLGGQ--LHHIYNEITDFPPLVYDqGAALVKVLIAHPFIQQPNIR-- 79
Cdd:pfam07992   2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEdEGTCPYGGcvLSKALLGAAEAPEIASL-WADLYKRKEEVVKKLNNGIEvl 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378  80 LNEAILSIDRETKQVITSKSV------YRVDYLLIATGVGWN--EIPALAD-CPSVLSPWFSTTAQAHTIAGQDIAVIGG 150
Cdd:pfam07992  81 LGTEVVSIDPGAKKVVLEELVdgdgetITYDRLVIATGARPRlpPIPGVELnVGFLVRTLDSAEALRLKLLPKRVVVVGG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 151 GDRALESAANLSFHARQVYLLVRSSEW------RARPEWQKKITGLpNIQVLWETQVSDYQHEEarTVLTLTstrTGNPE 224
Cdd:pfam07992 161 GYIGVELAAALAKLGKEVTLIEALDRLlrafdeEISAALEKALEKN-GVEVRLGTSVKEIIGDG--DGVEVI---LKDGT 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1371933378 225 TIVVDWILPRIGVHGNTAGFD--GLDMFGDDYLQTDSSQRVNSPWIYAVGDV 274
Cdd:pfam07992 235 EIDADLVVVAIGRRPNTELLEaaGLELDERGGIVVDEYLRTSVPGIYAAGDC 286
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
6-293 7.48e-16

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 77.51  E-value: 7.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSCLLIekTDRLGGQLhhiyNE---ITDFPPLVYDQGAALVKVLIAHpfIQQPNIRL-- 80
Cdd:PRK15317  214 VLVVGGGPAGAAAAIYAARKGIRTGIV--AERFGGQV----LDtmgIENFISVPETEGPKLAAALEEH--VKEYDVDImn 285
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378  81 ---------NEAILSIDRETKQVITSKSVyrvdylLIATGVGWNEI--P--------ALADCPSVLSPWFSttaqahtia 141
Cdd:PRK15317  286 lqrasklepAAGLIEVELANGAVLKAKTV------ILATGARWRNMnvPgedeyrnkGVAYCPHCDGPLFK--------- 350
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 142 GQDIAVIGGGDRALESAANLSFHARQVYLLVRSSEWRARPEWQKKITGLPNIQVLWETQVSDYQHEEAR-TVLTLTSTRT 220
Cdd:PRK15317  351 GKRVAVIGGGNSGVEAAIDLAGIVKHVTVLEFAPELKADQVLQDKLRSLPNVTIITNAQTTEVTGDGDKvTGLTYKDRTT 430
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371933378 221 GNPETIVVDWILPRIGVHGNTAGFDG---LDMFGDdyLQTDSSQRVNSPWIYAVGDVNNgAAYASLSLAVGQAMKA 293
Cdd:PRK15317  431 GEEHHLELEGVFVQIGLVPNTEWLKGtveLNRRGE--IIVDARGATSVPGVFAAGDCTT-VPYKQIIIAMGEGAKA 503
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
1-297 1.78e-15

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: 76.28  E-value: 1.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378   1 MEHIQVLIAGGGIAGLSAAIWCHRLGLSCLLIEKtDRLGGQ------------LH--HIYNEITDFPPLVYDQGAALV-- 64
Cdd:COG1249     1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEK-GRLGGTclnvgcipskalLHaaEVAHEARHAAEFGISAGAPSVdw 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378  65 KVLIAH---------PFIQQ----PNIRLNEAILSIDRETKQVITSKSVYRVDYLLIATGVGWNEIPAL-ADCPSVLSpw 130
Cdd:COG1249    80 AALMARkdkvvdrlrGGVEEllkkNGVDVIRGRARFVDPHTVEVTGGETLTADHIVIATGSRPRVPPIPgLDEVRVLT-- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 131 fSTTAQAHTIAGQDIAVIGGGDRALESAanlSFHAR---QVYLLVRSSewR--------ARPEWQKKITGLpNIQVLWET 199
Cdd:COG1249   158 -SDEALELEELPKSLVVIGGGYIGLEFA---QIFARlgsEVTLVERGD--RllpgedpeISEALEKALEKE-GIDILTGA 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 200 QVSDYQHEEARTVLTLTSTRTgnPETIVVDWILPRIGVHGNTAGFD----GLDMFGDDYLQTDSSQRVNSPWIYAVGDVN 275
Cdd:COG1249   231 KVTSVEKTGDGVTVTLEDGGG--EEAVEADKVLVATGRRPNTDGLGleaaGVELDERGGIKVDEYLRTSVPGIYAIGDVT 308
                         330       340
                  ....*....|....*....|..
gi 1371933378 276 NGAAYASLSLAvgQAMKAVKHI 297
Cdd:COG1249   309 GGPQLAHVASA--EGRVAAENI 328
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
6-297 4.27e-14

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: 72.29  E-value: 4.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSCLLIEKtDRLGGQ------------LH--HIYNEIT--------------DFPPLVy 57
Cdd:TIGR01350   4 VIVIGGGPGGYVAAIRAAQLGLKVALVEK-EYLGGTclnvgciptkalLHsaEVYDEIKhakdlgievenvsvDWEKMQ- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378  58 DQGAALVKVLIA--HPFIQQPNIRL--NEAILSIDRETKqVITSKS--VYRVDYLLIATGVGWNEIPAL--ADCPSVLSp 129
Cdd:TIGR01350  82 KRKNKVVKKLVGgvSGLLKKNKVTVikGEAKFLDPGTVS-VTGENGeeTLEAKNIIIATGSRPRSLPGPfdFDGKVVIT- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 130 wfSTTAQAHTIAGQDIAVIGGGDRALESAanLSFHARQVYLLVRSSEWRARPEWQKKITGL-------PNIQVLWETQVS 202
Cdd:TIGR01350 160 --STGALNLEEVPESLVIIGGGVIGIEFA--SIFASLGSKVTVIEMLDRILPGEDAEVSKVlqkalkkKGVKILTNTKVT 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 203 DYQHEEARTVLtltSTRTGNPETIVVDWILPRIGVHGNTAGFD----GLDMFGDDYLQTDSSQRVNSPWIYAVGDVNNGA 278
Cdd:TIGR01350 236 AVEKNDDQVTY---ENKGGETETLTGEKVLVAVGRKPNTEGLGleklGVELDERGRIVVDEYMRTNVPGIYAIGDVIGGP 312
                         330
                  ....*....|....*....
gi 1371933378 279 AYAslSLAVGQAMKAVKHI 297
Cdd:TIGR01350 313 MLA--HVASHEGIVAAENI 329
Pyr_redox_3 pfam13738
Pyridine nucleotide-disulphide oxidoreductase;
14-180 5.42e-14

Pyridine nucleotide-disulphide oxidoreductase;


Pssm-ID: 404603 [Multi-domain]  Cd Length: 296  Bit Score: 71.10  E-value: 5.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378  14 AGLSAAIWCHRLGLSCLLI-EKtdrlgGQL-HHIYN-----------------EITDFP-------P------------- 54
Cdd:pfam13738   2 AGIGCAIALKKAGLEDYLIlEK-----GNIgNSFYRypthmtffspsftsngfGIPDLNaispgtsPaftfnrehpsgne 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378  55 -LVYDQGAALVKVLiahpfiqqpNIRLNEAILSIDRETK--QVITSKSVYRVDYLLIATGV----GWNEIPALADCPSVL 127
Cdd:pfam13738  77 yAEYLRRVADHFEL---------PINLFEEVTSVKKEDDgfVVTTSKGTYQARYVIIATGEfdfpNKLGVPELPKHYSYV 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1371933378 128 SPWfsttaqaHTIAGQDIAVIGGGDRALESAANLSFHARQVYLLVRSSEWRAR 180
Cdd:pfam13738 148 KDF-------HPYAGQKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDR 193
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
31-297 2.10e-13

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: 69.45  E-value: 2.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378  31 LIEKTDRLGGQLhhiyneitdfPPLVYDQGAALVKV--LIAHP--FIQQPNI--RLNEAILSIDRETKQVITSK-SVYRV 103
Cdd:COG0446    10 VIEKGPHHSYQP----------CGLPYYVGGGIKDPedLLVRTpeSFERKGIdvRTGTEVTAIDPEAKTVTLRDgETLSY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 104 DYLLIATGVG--WNEIPALaDCPSVLSpwFSTTAQAHTI-------AGQDIAVIGGGDRALESAANLSFHARQVYLLVRS 174
Cdd:COG0446    80 DKLVLATGARprPPPIPGL-DLPGVFT--LRTLDDADALrealkefKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 175 -----------SEWrARPEWQKKitglpNIQVLWETQVSDYqHEEARTVLTLTSTrtgnpETIVVDWILPRIGVHGNTAG 243
Cdd:COG0446   157 prllgvldpemAAL-LEEELREH-----GVELRLGETVVAI-DGDDKVAVTLTDG-----EEIPADLVVVAPGVRPNTEL 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1371933378 244 FD--GLDMFGDDYLQTDSSQRVNSPWIYAVGD-------VNNGAAYASL-SLAVGQAMKAVKHI 297
Cdd:COG0446   225 AKdaGLALGERGWIKVDETLQTSDPDVYAAGDcaevphpVTGKTVYIPLaSAANKQGRVAAENI 288
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
1-177 4.88e-13

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: 69.12  E-value: 4.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378   1 MEHIQVLIAGGGIAGLSAAIWCHRLGLSCLLIEKTDRLGGQ-LHHIYNEIT-DFPPLVYD----QGAALVKVLIAHPFIQ 74
Cdd:COG2072     4 TEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGTwRDNRYPGLRlDTPSHLYSlpffPNWSDDPDFPTGDEIL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378  75 Q------------PNIRLNEAILSI--DRETK--QVITSK-SVYRVDYLLIATGVGWN----EIPALADcpsvlspwFS- 132
Cdd:COG2072    84 AyleayadkfglrRPIRFGTEVTSArwDEADGrwTVTTDDgETLTARFVVVATGPLSRpkipDIPGLED--------FAg 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1371933378 133 ---TTAQ---AHTIAGQDIAVIGGGDRALESAANLSFHARQVYLLVRSSEW 177
Cdd:COG2072   156 eqlHSADwrnPVDLAGKRVLVVGTGASAVQIAPELARVAAHVTVFQRTPPW 206
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
6-274 6.05e-13

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 68.63  E-value: 6.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSC-LLIektdrLGGQLHHIYNEitdfPPLVYD-QGAALVKVLIAHP--FIQQPNI--R 79
Cdd:COG1251     4 IVIIGAGMAGVRAAEELRKLDPDGeITV-----IGAEPHPPYNR----PPLSKVlAGETDEEDLLLRPadFYEENGIdlR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378  80 LNEAILSIDRETKQVITSK-SVYRVDYLLIATGvGWNEIPAL--ADCPSVLSpwFSTTAQAHTI-----AGQDIAVIGGG 151
Cdd:COG1251    75 LGTRVTAIDRAARTVTLADgETLPYDKLVLATG-SRPRVPPIpgADLPGVFT--LRTLDDADALraalaPGKRVVVIGGG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 152 DRALESAANLSFHARQVYLLVRSSEWRAR---PE----WQKKITGLpNIQVLWETQVSDYQHEEARTVLTLTStrtGnpE 224
Cdd:COG1251   152 LIGLEAAAALRKRGLEVTVVERAPRLLPRqldEEagalLQRLLEAL-GVEVRLGTGVTEIEGDDRVTGVRLAD---G--E 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1371933378 225 TIVVDWILPRIGVHGNTAGFD--GLDMFG----DDYLQTdssqrvNSPWIYAVGDV 274
Cdd:COG1251   226 ELPADLVVVAIGVRPNTELARaaGLAVDRgivvDDYLRT------SDPDIYAAGDC 275
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
6-274 1.16e-11

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 64.77  E-value: 1.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378   6 VLIAGGGIAGLSAAI-WCHRL--GLSCLLIEKTDrlggqlHHIyneitdFPPLVYDQGAALVKV-LIAHPF---IQQPNI 78
Cdd:COG1252     4 IVIVGGGFAGLEAARrLRKKLggDAEVTLIDPNP------YHL------FQPLLPEVAAGTLSPdDIAIPLrelLRRAGV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378  79 R-LNEAILSIDRETKQVITSK-SVYRVDYLLIATGVGWN--EIPALAD-CPSVLSP---------WFSTTAQAHTIAGQD 144
Cdd:COG1252    72 RfIQGEVTGIDPEARTVTLADgRTLSYDYLVIATGSVTNffGIPGLAEhALPLKTLedalalrerLLAAFERAERRRLLT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 145 IAVIGGGDRALESAANLSFHARQVY------------LLV------------RSSEWrARPEWQKKitglpNIQVLWETQ 200
Cdd:COG1252   152 IVVVGGGPTGVELAGELAELLRKLLrypgidpdkvriTLVeagprilpglgeKLSEA-AEKELEKR-----GVEVHTGTR 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 201 VSDYQHEEartvLTLTSTRTGNPETIVvdWilprigvhgnTAGFDGLDMFGDDYLQTDSSQRV---------NSPWIYAV 271
Cdd:COG1252   226 VTEVDADG----VTLEDGEEIPADTVI--W----------AAGVKAPPLLADLGLPTDRRGRVlvdptlqvpGHPNVFAI 289

                  ...
gi 1371933378 272 GDV 274
Cdd:COG1252   290 GDC 292
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
77-297 1.05e-10

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


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 62.54  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378  77 NIRL--NEAILSIDRETKQVITS-KSVYRVDYLLIATG-VGWneIPAL--ADCPSVLSpwFSTTAQAHTIAG-----QDI 145
Cdd:TIGR02374  68 GITLytGETVIQIDTDQKQVITDaGRTLSYDKLILATGsYPF--ILPIpgADKKGVYV--FRTIEDLDAIMAmaqrfKKA 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 146 AVIGGGDRALESAANLSFHARQVY-------LLVRSSEWRARPEWQKKITGLpNIQVLWETQ-VSDYQHEEARTVltlts 217
Cdd:TIGR02374 144 AVIGGGLLGLEAAVGLQNLGMDVSvihhapgLMAKQLDQTAGRLLQRELEQK-GLTFLLEKDtVEIVGATKADRI----- 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 218 tRTGNPETIVVDWILPRIGVHGNT--AGFDGLDMFG----DDYLQTdssqrvNSPWIYAVGDV--NNGAAYASLSLAVGQ 289
Cdd:TIGR02374 218 -RFKDGSSLEADLIVMAAGIRPNDelAVSAGIKVNRgiivNDSMQT------SDPDIYAVGECaeHNGRVYGLVAPLYEQ 290

                  ....*...
gi 1371933378 290 AMKAVKHI 297
Cdd:TIGR02374 291 AKVLADHI 298
PRK13748 PRK13748
putative mercuric reductase; Provisional
104-288 1.05e-10

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 62.09  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 104 DYLLIATGVGWN--EIPALADCPSvlspWFSTTAQAHTIAGQDIAVIGGGDRALESAANLSFHARQVYLLVRSSE-WRAR 180
Cdd:PRK13748  234 DRCLIATGASPAvpPIPGLKETPY----WTSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILARSTLfFRED 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 181 PEWQKKITG---LPNIQVLWETQVSDYQHEEARTVLTltsTRTGnpeTIVVDWILPRIGVHGNTAGFD----GLDMFGDD 253
Cdd:PRK13748  310 PAIGEAVTAafrAEGIEVLEHTQASQVAHVDGEFVLT---TGHG---ELRADKLLVATGRAPNTRSLAldaaGVTVNAQG 383
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1371933378 254 YLQTDSSQRVNSPWIYAVGDVNNGAAYASLSLAVG 288
Cdd:PRK13748  384 AIVIDQGMRTSVPHIYAAGDCTDQPQFVYVAAAAG 418
PRK10262 PRK10262
thioredoxin reductase; Provisional
2-274 2.33e-09

thioredoxin reductase; Provisional


Pssm-ID: 182343 [Multi-domain]  Cd Length: 321  Bit Score: 57.38  E-value: 2.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378   2 EHIQVLIAGGGIAGLSAAIWCHRLGLSCLLIEKTDRlGGQLhHIYNEITDFPPLVYD-QGAALVKVLIAHPFIQQPNIrL 80
Cdd:PRK10262    5 KHSKLLILGSGPAGYTAAVYAARANLQPVLITGMEK-GGQL-TTTTEVENWPGDPNDlTGPLLMERMHEHATKFETEI-I 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378  81 NEAILSIDRETK--QVITSKSVYRVDYLLIATGVGWNEIpalaDCPSVLSPWFSTTAQAHTIAG-----QDIAVIGGGDR 153
Cdd:PRK10262   82 FDHINKVDLQNRpfRLTGDSGEYTCDALIIATGASARYL----GLPSEEAFKGRGVSACATCDGffyrnQKVAVIGGGNT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 154 ALESAANLSFHARQVYLLVRSSEWRARPEWQKKITG-LPNIQVLWETQVSDYQ---HEEARTVLTLTSTR-TGNPETIVV 228
Cdd:PRK10262  158 AVEEALYLSNIASEVHLIHRRDGFRAEKILIKRLMDkVENGNIILHTNRTLEEvtgDQMGVTGVRLRDTQnSDNIESLDV 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1371933378 229 DWILPRIGVHGNTAGFDGLDMFGDDYLQTDSSQRVNS-----PWIYAVGDV 274
Cdd:PRK10262  238 AGLFVAIGHSPNTAIFEGQLELENGYIKVQSGIHGNAtqtsiPGVFAAGDV 288
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
1-281 1.58e-08

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 55.18  E-value: 1.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378   1 MEHIQVLIAGGGIAGLSAAIWCHRLGLSCLLIEKtDRLGGQ------------LH--HIYNEITDFPPLvydqGAALVKV 66
Cdd:PRK06292    1 MEKYDVIVIGAGPAGYVAARRAAKLGKKVALIEK-GPLGGTclnvgcipskalIAaaEAFHEAKHAEEF----GIHADGP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378  67 LIAHPFIQQpNIR---------LNEAILSIDRETK-----------QVITSKSVYRVDYLLIATGvgwneipalADCPSV 126
Cdd:PRK06292   76 KIDFKKVMA-RVRrerdrfvggVVEGLEKKPKIDKikgtarfvdpnTVEVNGERIEAKNIVIATG---------SRVPPI 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 127 LSPWF--------STTAQAHTIAGQDIAVIGGGDRALESAanlSFHAR---QVYLLVRSSewRARPEWQKKITGL----- 190
Cdd:PRK06292  146 PGVWLilgdrlltSDDAFELDKLPKSLAVIGGGVIGLELG---QALSRlgvKVTVFERGD--RILPLEDPEVSKQaqkil 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 191 -PNIQVLWETQVSDYqhEEARTVLTLTSTRTGNPETIVVDWILPRIGVHGNTAGFdGLDMFG-----------DDYLQTd 258
Cdd:PRK06292  221 sKEFKIKLGAKVTSV--EKSGDEKVEELEKGGKTETIEADYVLVATGRRPNTDGL-GLENTGieldergrpvvDEHTQT- 296
                         330       340
                  ....*....|....*....|...
gi 1371933378 259 ssqrvNSPWIYAVGDVNNGAAYA 281
Cdd:PRK06292  297 -----SVPGIYAAGDVNGKPPLL 314
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
6-45 1.70e-08

Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440845 [Multi-domain]  Cd Length: 443  Bit Score: 55.22  E-value: 1.70e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSCLLIEKTDRLGGQLHHI 45
Cdd:COG1232     4 VAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIRTV 43
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
6-43 3.83e-08

FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.


Pssm-ID: 395718 [Multi-domain]  Cd Length: 398  Bit Score: 54.22  E-value: 3.83e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSCLLIEKTDRLGGQLH 43
Cdd:pfam00890   2 VLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGATA 39
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
6-43 5.24e-08

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 53.70  E-value: 5.24e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLS--CLLIEKTDRLGGQLH 43
Cdd:PRK11883    3 VAIIGGGITGLSAAYRLHKKGPDadITLLEASDRLGGKIQ 42
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
6-42 1.07e-07

FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 52.61  E-value: 1.07e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSCLLIEKTDRLGGQL 42
Cdd:pfam12831   2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGML 38
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
1-44 1.13e-07

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 52.25  E-value: 1.13e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1371933378   1 MEHIQVLIAGGGIAGLSAAIWCHRLGLSCLLIEKTDRL-----GGQLHH 44
Cdd:COG0654     1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPrpdgrGIALSP 49
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
6-40 1.75e-07

Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440673 [Multi-domain]  Cd Length: 443  Bit Score: 52.14  E-value: 1.75e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSCLLIEKTDRLGG 40
Cdd:COG1053     6 VVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
8-61 3.11e-07

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 46.76  E-value: 3.11e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1371933378   8 IAGGGIAGLSAAIWCHRLGLSCLLIEKTDRLGGQLHHIyneitDFPPLVYDQGA 61
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAYSY-----RVPGYVFDYGA 49
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
59-273 3.20e-07

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 51.07  E-value: 3.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378  59 QGAALVKVLIAHPFIQQPNIRL--NEAILSIDRETKQVITSKSVYRVDYLLIATGvgwneipALADCPSVL-SPWFST-- 133
Cdd:PRK04965   54 QRADDLTRQSAGEFAEQFNLRLfpHTWVTDIDAEAQVVKSQGNQWQYDKLVLATG-------ASAFVPPIPgRELMLTln 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 134 ------TAQAHTIAGQDIAVIGGGDRALESAANLSFHARQVYLLVRSS---------EWRARPEWQKKITGlpnIQVLWE 198
Cdd:PRK04965  127 sqqeyrAAETQLRDAQRVLVVGGGLIGTELAMDLCRAGKAVTLVDNAAsllaslmppEVSSRLQHRLTEMG---VHLLLK 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 199 TQVSDYQHEEARTVLTLTSTRtgnpeTIVVDWILPRIGVHGNT--AGFDGLD----MFGDDYLQTdssqrvNSPWIYAVG 272
Cdd:PRK04965  204 SQLQGLEKTDSGIRATLDSGR-----SIEVDAVIAAAGLRPNTalARRAGLAvnrgIVVDSYLQT------SAPDIYALG 272

                  .
gi 1371933378 273 D 273
Cdd:PRK04965  273 D 273
MerA TIGR02053
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ...
6-288 3.54e-07

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: 51.27  E-value: 3.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSCLLIEkTDRLGG-----------------QLHHiYNEITDFPPLvydqgAALVKVLI 68
Cdd:TIGR02053   3 LVIIGSGAAAFAAAIKAAELGASVAMVE-RGPLGGtcvnvgcvpskmllraaEVAH-YARKPPFGGL-----AATVAVDF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378  69 AhPFIQQPNIRLNE-------AILS-------------IDRETKQVITSKSVYRVDYLLIATGVGWN--EIPALADCPSv 126
Cdd:TIGR02053  76 G-ELLEGKREVVEElrhekyeDVLSsygvdylrgrarfKDPKTVKVDLGREVRGAKRFLIATGARPAipPIPGLKEAGY- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 127 lspWFSTTAQAHTIAGQDIAVIGGGDRALESAANLSFHARQVYLLVRSSewRARPEWQKKIT-GLPN------IQVLWET 199
Cdd:TIGR02053 154 ---LTSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSD--RLLPREEPEISaAVEEalaeegIEVVTSA 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 200 QVSDYQHEEARTVLTLTstRTGNPETIVVDWILPRIGVHGNTAGFD----GLDMFGDDYLQTDSSQRVNSPWIYAVGDVN 275
Cdd:TIGR02053 229 QVKAVSVRGGGKIITVE--KPGGQGEVEADELLVATGRRPNTDGLGlekaGVKLDERGGILVDETLRTSNPGIYAAGDVT 306
                         330
                  ....*....|...
gi 1371933378 276 NGAAYASLSLAVG 288
Cdd:TIGR02053 307 GGLQLEYVAAKEG 319
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
1-64 9.47e-07

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 49.92  E-value: 9.47e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1371933378   1 MEHIQVLIAGGGIAGLSAAIWCHRLGLSCLLIEKTDRLGGqlhHIYNEITDFPPLVYDQGAALV 64
Cdd:COG1231     5 ARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGG---RVWTLRFGDDGLYAELGAMRI 65
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
6-113 1.69e-06

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: 48.65  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSCLLIEKTDRLggqlhhiyneitdFPPLVYDQGAALVKVLIAHPfIqqpNIRLNEAIL 85
Cdd:COG0446   127 AVVIGGGPIGLELAEALRKRGLKVTLVERAPRL-------------LGVLDPEMAALLEEELREHG-V---ELRLGETVV 189
                          90       100       110
                  ....*....|....*....|....*....|
gi 1371933378  86 SIDRETKQVI--TSKSVYRVDYLLIATGVG 113
Cdd:COG0446   190 AIDGDDKVAVtlTDGEEIPADLVVVAPGVR 219
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
140-304 2.30e-06

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


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 48.97  E-value: 2.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 140 IAGQDIAVIGGGDRALESAAN-LSFHARQVYLLVRSSEWR--ARPEWQK--KITGlpnIQVLWETQVSDYQHEEARTV-- 212
Cdd:PRK12778  568 KFGKKVAVVGGGNTAMDSARTaKRLGAERVTIVYRRSEEEmpARLEEVKhaKEEG---IEFLTLHNPIEYLADEKGWVkq 644
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 213 LTLTSTRTGNP---------------ETIVVDWILPRIGVHGN---TAGFDGLDMFGDDYLQTDSSQRVNSPWIYAVGDV 274
Cdd:PRK12778  645 VVLQKMELGEPdasgrrrpvaipgstFTVDVDLVIVSVGVSPNplvPSSIPGLELNRKGTIVVDEEMQSSIPGIYAGGDI 724
                         170       180       190
                  ....*....|....*....|....*....|
gi 1371933378 275 NNGAayASLSLAVGQAMKAVKHISLQIQNN 304
Cdd:PRK12778  725 VRGG--ATVILAMGDGKRAAAAIDEYLSSK 752
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
6-112 3.24e-06

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 48.11  E-value: 3.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSCLLIEKTDR-LGGQLHhiyNEITDfpplvydqgaalvkVLIAHPFIQQPNIRLNEAI 84
Cdd:PRK09564  152 IVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRiLPDSFD---KEITD--------------VMEEELRENGVELHLNEFV 214
                          90       100       110
                  ....*....|....*....|....*....|
gi 1371933378  85 LSIDRETK--QVITSKSVYRVDYLLIATGV 112
Cdd:PRK09564  215 KSLIGEDKveGVVTDKGEYEADVVIVATGV 244
PRK07251 PRK07251
FAD-containing oxidoreductase;
104-285 5.11e-06

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 47.44  E-value: 5.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 104 DYLLIATGVGWNE--IPALADCPSVLSpwfSTTAQAHTIAGQDIAVIGGGDRALESAANLSFHARQVYLLVRSSEWRARP 181
Cdd:PRK07251  120 ETIVINTGAVSNVlpIPGLADSKHVYD---STGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPRE 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 182 EwqKKITGLPN-------IQVLWETQVSDYQHEEARTVLTLtstrtgNPETIVVDWILPRIGVHGNTAGFdGLD------ 248
Cdd:PRK07251  197 E--PSVAALAKqymeedgITFLLNAHTTEVKNDGDQVLVVT------EDETYRFDALLYATGRKPNTEPL-GLEntdiel 267
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1371933378 249 -----MFGDDYLQTdssqrvNSPWIYAVGDVNNGAAYASLSL 285
Cdd:PRK07251  268 tergaIKVDDYCQT------SVPGVFAVGDVNGGPQFTYISL 303
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
6-80 7.46e-06

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 47.16  E-value: 7.46e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSCLLIEKTDRLGGQLHHIYneiTDFPPLvyDQGAALVKVLIAHpfIQQ-PNIRL 80
Cdd:COG1148   143 ALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAQLH---KTFPGL--DCPQCILEPLIAE--VEAnPNITV 211
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
6-297 8.15e-06

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 47.18  E-value: 8.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSCLLIEKTDRLGGQLHH-IyneitdfpplvydqgaalvkvliahpfiqqPNIRLNEAI 84
Cdd:PRK12771  140 VAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMRYgI------------------------------PAYRLPREV 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378  85 LS--IDRETKQVITSKSVYRV-------------DYLLIATG--VGWN-EIPAlADCPSVLSPW-----FSTTAQAHTia 141
Cdd:PRK12771  190 LDaeIQRILDLGVEVRLGVRVgeditleqlegefDAVFVAIGaqLGKRlPIPG-EDAAGVLDAVdflraVGEGEPPFL-- 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 142 GQDIAVIGGGDRALEsAANLsfhARQ--------VYllvrssewRARPEwqkKITGLPN---------IQVLWETQ---- 200
Cdd:PRK12771  267 GKRVVVIGGGNTAMD-AART---ARRlgaeevtiVY--------RRTRE---DMPAHDEeieealregVEINWLRTpvei 331
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 201 VSDYQHEEARTVLTLT----------STRTGNPETIVVDWILPRIGVHGNTAGFDGLDM--FGDDYLQTDSSQRV-NSPW 267
Cdd:PRK12771  332 EGDENGATGLRVITVEkmeldedgrpSPVTGEEETLEADLVVLAIGQDIDSAGLESVPGveVGRGVVQVDPNFMMtGRPG 411
                         330       340       350
                  ....*....|....*....|....*....|
gi 1371933378 268 IYAVGDVNNGAayASLSLAVGQAMKAVKHI 297
Cdd:PRK12771  412 VFAGGDMVPGP--RTVTTAIGHGKKAARNI 439
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
145-218 3.09e-05

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: 41.42  E-value: 3.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 145 IAVIGGGDRALESAANLSFHARQVYLLVRSSEWR------ARPEWQKKITGLpNIQVLWETQVSDYQHEEARTVLTLTST 218
Cdd:pfam00070   2 VVVVGGGYIGLELAGALARLGSKVTVVERRDRLLpgfdpeIAKILQEKLEKN-GIEFLLNTTVEAIEGNGDGVVVVLTDG 80
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
1-40 4.75e-05

Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];


Pssm-ID: 442577 [Multi-domain]  Cd Length: 445  Bit Score: 44.46  E-value: 4.75e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1371933378   1 MEHIQVLIAGGGIAGLSAAIWCHRLGLSCLLIEKTDRLGG 40
Cdd:COG3349     1 MMPPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG 40
PRK06116 PRK06116
glutathione reductase; Validated
101-277 6.78e-05

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 43.99  E-value: 6.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 101 YRVDYLLIATGvGW---------------NEIPALADCPsvlspwfsttaqahtiagQDIAVIGGGDRALESAANLSFHA 165
Cdd:PRK06116  130 YTADHILIATG-GRpsipdipgaeygitsDGFFALEELP------------------KRVAVVGAGYIAVEFAGVLNGLG 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 166 RQVYLLVRssewRARP--------------EWQKKitglpNIQVLWETQVSDYqHEEARTVLTLTstrTGNPETIVVDWI 231
Cdd:PRK06116  191 SETHLFVR----GDAPlrgfdpdiretlveEMEKK-----GIRLHTNAVPKAV-EKNADGSLTLT---LEDGETLTVDCL 257
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1371933378 232 LPRIGVHGNTAGFdGLDMFG---DD--YLQTDSSQRVNSPWIYAVGDVNNG 277
Cdd:PRK06116  258 IWAIGREPNTDGL-GLENAGvklNEkgYIIVDEYQNTNVPGIYAVGDVTGR 307
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
1-40 6.93e-05

Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 44.07  E-value: 6.93e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1371933378   1 MEHIQVLIAGGGIAGLSAAIWCHRLGLSCLLIEKTDRLGG 40
Cdd:COG1233     1 MMMYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
6-51 1.05e-04

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 43.36  E-value: 1.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSCLLIEK-------TDRLGGQLHHIYNEITD 51
Cdd:COG0665     5 VVVIGGGIAGLSTAYHLARRGLDVTVLERgrpgsgaSGRNAGQLRPGLAALAD 57
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
6-46 1.21e-04

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 43.16  E-value: 1.21e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSCLLIEKTDRLG--------GQLHHIY 46
Cdd:pfam01266   2 VVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGsgasgrnaGLIHPGL 50
PRK12842 PRK12842
putative succinate dehydrogenase; Reviewed
6-40 1.80e-04

putative succinate dehydrogenase; Reviewed


Pssm-ID: 237224 [Multi-domain]  Cd Length: 574  Bit Score: 42.76  E-value: 1.80e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSCLLIEKTDRLGG 40
Cdd:PRK12842   12 VLVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGG 46
PLN02268 PLN02268
probable polyamine oxidase
6-62 1.85e-04

probable polyamine oxidase


Pssm-ID: 177909 [Multi-domain]  Cd Length: 435  Bit Score: 42.75  E-value: 1.85e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSCLLIEKTDRLGGQLHHIYNeiTDFPplvYDQGAA 62
Cdd:PLN02268    3 VIVIGGGIAGIAAARALHDASFKVTLLESRDRIGGRVHTDYS--FGFP---VDMGAS 54
PRK07538 PRK07538
hypothetical protein; Provisional
5-38 2.33e-04

hypothetical protein; Provisional


Pssm-ID: 236046 [Multi-domain]  Cd Length: 413  Bit Score: 42.58  E-value: 2.33e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1371933378   5 QVLIAGGGIAGLSAAIWCHRLGLSCLLIEKTDRL 38
Cdd:PRK07538    2 KVLIAGGGIGGLTLALTLHQRGIEVVVFEAAPEL 35
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
207-281 2.38e-04

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 42.44  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 207 EEARTVLTLTSTRTGNPETIVVDWILPRIGVHGNTAGFdGLDMFG----------DDYLQTdssqrvNSPWIYAVGDVNN 276
Cdd:PRK06416  240 EQTDDGVTVTLEDGGKEETLEADYVLVAVGRRPNTENL-GLEELGvktdrgfievDEQLRT------NVPNIYAIGDIVG 312

                  ....*
gi 1371933378 277 GAAYA 281
Cdd:PRK06416  313 GPMLA 317
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
81-274 3.47e-04

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 42.08  E-value: 3.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378  81 NEAILSIDRETKQVITSKsvyrVDYLLIATGVGWNEIPALADCPSVLSPWFSTTAQAHTIAGQDIA---VIGGGDRALES 157
Cdd:PRK13512   88 RQTVTVLNRKTNEQFEES----YDKLILSPGASANSLGFESDITFTLRNLEDTDAIDQFIKANQVDkalVVGAGYISLEV 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 158 AANLSFHARQVYLLVRSSewrarpewqkKITGL-------PNIQVLWETQVsDYQHEE--ARTVLTLTSTRTGNPETIvv 228
Cdd:PRK13512  164 LENLYERGLHPTLIHRSD----------KINKLmdadmnqPILDELDKREI-PYRLNEeiDAINGNEVTFKSGKVEHY-- 230
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1371933378 229 DWILPRIGVHGNTAGFDGLDMFGDD--YLQTDSSQRVNSPWIYAVGDV 274
Cdd:PRK13512  231 DMIIEGVGTHPNSKFIESSNIKLDDkgFIPVNDKFETNVPNIYAIGDI 278
PRK06847 PRK06847
hypothetical protein; Provisional
5-34 3.56e-04

hypothetical protein; Provisional


Pssm-ID: 235874 [Multi-domain]  Cd Length: 375  Bit Score: 41.78  E-value: 3.56e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1371933378   5 QVLIAGGGIAGLSAAIWCHRLGLSCLLIEK 34
Cdd:PRK06847    6 KVLIVGGGIGGLSAAIALRRAGIAVDLVEI 35
PRK12843 PRK12843
FAD-dependent oxidoreductase;
6-40 5.33e-04

FAD-dependent oxidoreductase;


Pssm-ID: 237225 [Multi-domain]  Cd Length: 578  Bit Score: 41.65  E-value: 5.33e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSCLLIEKTDRLGG 40
Cdd:PRK12843   19 VIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGG 53
PRK06134 PRK06134
putative FAD-binding dehydrogenase; Reviewed
6-40 6.74e-04

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 180419 [Multi-domain]  Cd Length: 581  Bit Score: 41.24  E-value: 6.74e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSCLLIEKTDRLGG 40
Cdd:PRK06134   15 VLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGG 49
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
5-40 7.72e-04

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 41.30  E-value: 7.72e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1371933378    5 QVLIAGGGIAGLSAAIWCHRLGLSCLLIEKTDRLGG 40
Cdd:PTZ00306   411 RVIVVGGGLAGCSAAIEAASCGAQVILLEKEAKLGG 446
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
6-306 8.45e-04

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 40.55  E-value: 8.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSCLLIEKTDRLGGQLhhIYNeITDFPpLVYDQGAALVKVLIAhpfiQQPNIRLNEAI- 84
Cdd:PRK11749  143 VAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGGLL--RYG-IPEFR-LPKDIVDREVERLLK----LGVEIRTNTEVg 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378  85 --LSID--REtkqvitsksvyRVDYLLIATGVGwneipaladcpsvlSPWF----------------------STTAQAH 138
Cdd:PRK11749  215 rdITLDelRA-----------GYDAVFIGTGAG--------------LPRFlgipgenlggvysavdfltrvnQAVADYD 269
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 139 TIAGQDIAVIGGGDRALESA--AnLSFHARQVYLLVRSS--EWRARPEWQK--KITGlpnIQVLWETQ-VSDYQHEEART 211
Cdd:PRK11749  270 LPVGKRVVVIGGGNTAMDAArtA-KRLGAESVTIVYRRGreEMPASEEEVEhaKEEG---VEFEWLAApVEILGDEGRVT 345
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 212 VLTLTSTRTGNPE--------------TIVVDWILPRIGVHGNT---AGFDGLDMFGDDYLQTD-SSQRVNSPWIYAVGD 273
Cdd:PRK11749  346 GVEFVRMELGEPDasgrrrvpiegsefTLPADLVIKAIGQTPNPlilSTTPGLELNRWGTIIADdETGRTSLPGVFAGGD 425
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1371933378 274 VNNGAayASLSLAVGQAMKAVKHISLQIQNNRS 306
Cdd:PRK11749  426 IVTGA--ATVVWAVGDGKDAAEAIHEYLEGAAS 456
PRK05329 PRK05329
glycerol-3-phosphate dehydrogenase subunit GlpB;
6-72 9.29e-04

glycerol-3-phosphate dehydrogenase subunit GlpB;


Pssm-ID: 235412  Cd Length: 422  Bit Score: 40.60  E-value: 9.29e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSCLLIEKT-----------DRLGgqlhhiYNEITDFPPLVYDQGAALVKVLIAHPF 72
Cdd:PRK05329    5 VLVIGGGLAGLTAALAAAEAGKRVALVAKGqgalhfssgsiDLLG------YLPDGQPVSDPFEALAALAEQAPEHPY 76
GlpB COG3075
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
6-32 1.25e-03

Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];


Pssm-ID: 442309  Cd Length: 415  Bit Score: 40.16  E-value: 1.25e-03
                          10        20
                  ....*....|....*....|....*..
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSCLLI 32
Cdd:COG3075     5 VVVIGGGLAGLTAAIRAAEAGLRVAIV 31
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
5-34 1.49e-03

FAD binding domain; This domain is involved in FAD binding in a number of enzymes.


Pssm-ID: 396193 [Multi-domain]  Cd Length: 348  Bit Score: 39.62  E-value: 1.49e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1371933378   5 QVLIAGGGIAGLSAAIWCHRLGLSCLLIEK 34
Cdd:pfam01494   3 DVLIVGGGPAGLMLALLLARAGVRVVLVER 32
PRK12844 PRK12844
3-ketosteroid-delta-1-dehydrogenase; Reviewed
6-40 1.56e-03

3-ketosteroid-delta-1-dehydrogenase; Reviewed


Pssm-ID: 183787 [Multi-domain]  Cd Length: 557  Bit Score: 40.12  E-value: 1.56e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSCLLIEKTDRLGG 40
Cdd:PRK12844    9 VVVVGSGGGGMCAALAAADSGLEPLIVEKQDKVGG 43
HI0933_like pfam03486
HI0933-like protein;
5-111 1.81e-03

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 39.49  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378   5 QVLIAGGGIAGLSAAIWCHRLGLSCLLIEKTDRLG--------GQLH--HIYNEITD------------------FPP-- 54
Cdd:pfam03486   2 DVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLGrkilisggGRCNvtNLSEEPDNflsrypgnpkflksalsrFTPwd 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378  55 ---LVYDQGAAL------------------VKVLIAHPFIQQPNIRLNEAILSIDRET---KQVITSKSVYRVDYLLIAT 110
Cdd:pfam03486  82 fiaFFESLGVPLkeedhgrlfpdsdkasdiVDALLNELKELGVKIRLRTRVLSVEKDDdgrFRVKTGGEELEADSLVLAT 161

                  .
gi 1371933378 111 G 111
Cdd:pfam03486 162 G 162
PRK06370 PRK06370
FAD-containing oxidoreductase;
107-281 1.89e-03

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 39.80  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 107 LIATGV--GWNEIPALADCP-----SVLSpwfSTTAQAHtiagqdIAVIGGGDRALESAANLSFHARQVYLLVRSSEWRA 179
Cdd:PRK06370  138 FINTGAraAIPPIPGLDEVGyltneTIFS---LDELPEH------LVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLP 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 180 R-----PEWQKKITGLPNIQVLWETQVSDYQHEEARTVLTLTSTrtGNPETIVVDWILPRIGVHGNTAGFdGLDMFG--- 251
Cdd:PRK06370  209 RededvAAAVREILEREGIDVRLNAECIRVERDGDGIAVGLDCN--GGAPEITGSHILVAVGRVPNTDDL-GLEAAGvet 285
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1371933378 252 --------DDYLQTdssqrvNSPWIYAVGDVNNG-----AAYA 281
Cdd:PRK06370  286 dargyikvDDQLRT------TNPGIYAAGDCNGRgafthTAYN 322
PRK12839 PRK12839
FAD-dependent oxidoreductase;
6-40 2.06e-03

FAD-dependent oxidoreductase;


Pssm-ID: 237223 [Multi-domain]  Cd Length: 572  Bit Score: 39.81  E-value: 2.06e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSCLLIEKTDRLGG 40
Cdd:PRK12839   11 VVVVGSGAGGLSAAVAAAYGGAKVLVVEKASTCGG 45
PLN02676 PLN02676
polyamine oxidase
6-43 3.63e-03

polyamine oxidase


Pssm-ID: 215362 [Multi-domain]  Cd Length: 487  Bit Score: 38.93  E-value: 3.63e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSCLLI-EKTDRLGGQLH 43
Cdd:PLN02676   29 VIIVGAGMSGISAAKTLSEAGIEDILIlEATDRIGGRMR 67
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
1-277 3.72e-03

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 38.75  E-value: 3.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378   1 MEHIQVLIAGGGIAGLSAAIWCHRLGLSCLLIEKTD------RLGG---------------------QLHHIYNE--IT- 50
Cdd:PRK06327    2 SKQFDVVVIGAGPGGYVAAIRAAQLGLKVACIEAWKnpkgkpALGGtclnvgcipskallasseefeNAGHHFADhgIHv 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378  51 -----DFPPL------VYDQGAALVKVLIAH----------PFIQQPNirlNEAILSIDRETKQVITSKSVyrvdylLIA 109
Cdd:PRK06327   82 dgvkiDVAKMiarkdkVVKKMTGGIEGLFKKnkitvlkgrgSFVGKTD---AGYEIKVTGEDETVITAKHV------IIA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 110 TGVGWNEIPALA-DCPSVLSpwfSTTAQAHTIAGQDIAVIGGGDRALESAanlsfharqvyllvrsSEWR---------- 178
Cdd:PRK06327  153 TGSEPRHLPGVPfDNKIILD---NTGALNFTEVPKKLAVIGAGVIGLELG----------------SVWRrlgaevtile 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933378 179 ARP------------EWQKKIT--GLpNIQVlwETQVSDYQHEEARTVLTLTStRTGNPETIVVDWILPRIGVHGNTAGF 244
Cdd:PRK06327  214 ALPaflaaadeqvakEAAKAFTkqGL-DIHL--GVKIGEIKTGGKGVSVAYTD-ADGEAQTLEVDKLIVSIGRVPNTDGL 289
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1371933378 245 dGLDMFG---DD--YLQTDSSQRVNSPWIYAVGDVNNG 277
Cdd:PRK06327  290 -GLEAVGlklDErgFIPVDDHCRTNVPNVYAIGDVVRG 326
PRK08274 PRK08274
FAD-dependent tricarballylate dehydrogenase TcuA;
1-44 3.82e-03

FAD-dependent tricarballylate dehydrogenase TcuA;


Pssm-ID: 236214 [Multi-domain]  Cd Length: 466  Bit Score: 38.70  E-value: 3.82e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1371933378   1 MEHIQVLIAGGGIAGLSAAIWCHRLGLSCLLIEKTDR--LGGQLHH 44
Cdd:PRK08274    2 ASMVDVLVIGGGNAALCAALAAREAGASVLLLEAAPRewRGGNSRH 47
glycerol3P_GlpB TIGR03378
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are ...
6-32 4.21e-03

glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are the B subunit, product of the glpB gene, of a three-subunit, membrane-anchored, FAD-dependent anaerobic glycerol-3-phosphate dehydrogenase. [Energy metabolism, Anaerobic]


Pssm-ID: 213807  Cd Length: 419  Bit Score: 38.46  E-value: 4.21e-03
                          10        20
                  ....*....|....*....|....*..
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSCLLI 32
Cdd:TIGR03378   3 VIIIGGGLAGLSCALRLAEAGKKCAII 29
PRK08163 PRK08163
3-hydroxybenzoate 6-monooxygenase;
6-39 4.51e-03

3-hydroxybenzoate 6-monooxygenase;


Pssm-ID: 181262 [Multi-domain]  Cd Length: 396  Bit Score: 38.48  E-value: 4.51e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSCLLIEKTDRLG 39
Cdd:PRK08163    7 VLIVGGGIGGLAAALALARQGIKVKLLEQAAEIG 40
PRK07588 PRK07588
FAD-binding domain;
5-40 4.92e-03

FAD-binding domain;


Pssm-ID: 169028 [Multi-domain]  Cd Length: 391  Bit Score: 38.18  E-value: 4.92e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1371933378   5 QVLIAGGGIAGLSAAIWCHRLGLSCLLIEKTDRL--GG 40
Cdd:PRK07588    2 KVAISGAGIAGPTLAYWLRRYGHEPTLIERAPELrtGG 39
PRK12416 PRK12416
protoporphyrinogen oxidase; Provisional
6-47 5.00e-03

protoporphyrinogen oxidase; Provisional


Pssm-ID: 183516  Cd Length: 463  Bit Score: 38.27  E-value: 5.00e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1371933378   6 VLIAGGGIAGLSAAIWC------HRLGLSCLLIEKTDRLGGQLHHIYN 47
Cdd:PRK12416    4 VVVIGGGITGLSTMFYLeklkkdYNIDLNLILVEKEEYLGGKIHSVEE 51
YhiN COG2081
Predicted flavoprotein YhiN [General function prediction only];
7-39 7.40e-03

Predicted flavoprotein YhiN [General function prediction only];


Pssm-ID: 441684 [Multi-domain]  Cd Length: 402  Bit Score: 37.72  E-value: 7.40e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1371933378   7 LIAGGGIAGLSAAIWCHRLGLSCLLIEKTDRLG 39
Cdd:COG2081     1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVG 33
PRK07208 PRK07208
hypothetical protein; Provisional
1-40 7.55e-03

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 37.95  E-value: 7.55e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1371933378   1 MEHIQVLIAGGGIAGLSAAIWCHRLGLSCLLIEKTDRLGG 40
Cdd:PRK07208    2 TNKKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGG 41
COG3573 COG3573
Predicted oxidoreductase [General function prediction only];
6-41 8.00e-03

Predicted oxidoreductase [General function prediction only];


Pssm-ID: 442794 [Multi-domain]  Cd Length: 551  Bit Score: 37.85  E-value: 8.00e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1371933378   6 VLIAGGGIAGLSAAIWCHRLGLSCLLI--EKTDRLGGQ 41
Cdd:COG3573     8 VIVVGAGLAGLVAAAELADAGRRVLLLdqEPEANLGGQ 45
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
11-34 8.08e-03

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 37.25  E-value: 8.08e-03
                          10        20
                  ....*....|....*....|....
gi 1371933378  11 GGIAGLSAAIWCHRLGLSCLLIEK 34
Cdd:COG0644     1 AGPAGSAAARRLARAGLSVLLLEK 24
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
1-39 8.56e-03

L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 37.43  E-value: 8.56e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1371933378   1 MEHIQVLIAGGGIAGLSAAIWCHRL-GLSCLLIEKTDRLG 39
Cdd:COG0579     2 MEMYDVVIIGAGIVGLALARELSRYeDLKVLVLEKEDDVA 41
 
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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