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Conserved domains on  [gi|447001026|ref|WP_001078282|]
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MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Bacillus]

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];
7-321 4.89e-87

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


:

Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 264.29  E-value: 4.89e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026   7 FDVTVIGGGPAGLYSAFYSGLREMKTKIIEfQPQLGGKIHVYpeKMIWDVGGL-LPVTGDKLIEQLVQQGLTFKPEVVLD 85
Cdd:COG0492    1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIE-GGEPGGQLATT--KEIENYPGFpEGISGPELAERLREQAERFGAEILLE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026  86 TkVESIIRnEDGTFTLKTSNGAEHFSKTVIVATGSGilkPQKLSIEGAERFEVSNLNYTVKS-LKRFKDKTVIISGGGNS 164
Cdd:COG0492   78 E-VTSVDK-DDGPFRVTTDDGTEYEAKAVIIATGAG---PRKLGLPGEEEFEGRGVSYCATCdGFFFRGKDVVVVGGGDS 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026 165 AVDWANELEPIAKKVYVTYRKEELSGHEAQVKQLL-NSSADCFFNTSITKLIaGDNHeaIEYVELTNHETGEVSHLSIDE 243
Cdd:COG0492  153 ALEEALYLTKFASKVTLIHRRDELRASKILVERLRaNPKIEVLWNTEVTEIE-GDGR--VEGVTLKNVKTGEEKELEVDG 229

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447001026 244 VIINHGYERDITLLENseLDVAIIDNYYIAGNANSESSVDGLYAAGDILKHegKLHLIAGAFQDAGNAVNKAKQFIQP 321
Cdd:COG0492  230 VFVAIGLKPNTELLKG--LGLELDEDGYIVVDEDMETSVPGVFAAGDVRDY--KYRQAATAAGEGAIAALSAARYLEP 303
 
Name Accession Description Interval E-value
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
7-321 4.89e-87

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 264.29  E-value: 4.89e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026   7 FDVTVIGGGPAGLYSAFYSGLREMKTKIIEfQPQLGGKIHVYpeKMIWDVGGL-LPVTGDKLIEQLVQQGLTFKPEVVLD 85
Cdd:COG0492    1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIE-GGEPGGQLATT--KEIENYPGFpEGISGPELAERLREQAERFGAEILLE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026  86 TkVESIIRnEDGTFTLKTSNGAEHFSKTVIVATGSGilkPQKLSIEGAERFEVSNLNYTVKS-LKRFKDKTVIISGGGNS 164
Cdd:COG0492   78 E-VTSVDK-DDGPFRVTTDDGTEYEAKAVIIATGAG---PRKLGLPGEEEFEGRGVSYCATCdGFFFRGKDVVVVGGGDS 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026 165 AVDWANELEPIAKKVYVTYRKEELSGHEAQVKQLL-NSSADCFFNTSITKLIaGDNHeaIEYVELTNHETGEVSHLSIDE 243
Cdd:COG0492  153 ALEEALYLTKFASKVTLIHRRDELRASKILVERLRaNPKIEVLWNTEVTEIE-GDGR--VEGVTLKNVKTGEEKELEVDG 229

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447001026 244 VIINHGYERDITLLENseLDVAIIDNYYIAGNANSESSVDGLYAAGDILKHegKLHLIAGAFQDAGNAVNKAKQFIQP 321
Cdd:COG0492  230 VFVAIGLKPNTELLKG--LGLELDEDGYIVVDEDMETSVPGVFAAGDVRDY--KYRQAATAAGEGAIAALSAARYLEP 303
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 7-304 1.86e-21

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: 92.77  E-value: 1.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026    7 FDVTVIGGGPAGLYSAFYSGLREMKTKIIEFqpqlgGKIHVY----PEKMIWDVGGLLPV--TGDKLIEQL--VQQGLTF 78
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIED-----EGTCPYggcvLSKALLGAAEAPEIasLWADLYKRKeeVVKKLNN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026   79 KPEVVLDTKVESIIRNEdGTFTLKTSNGAEHFS---KTVIVATGSgilKPQKLSIEGAER---FEVSNLNYTVKSLKRFK 152
Cdd:pfam07992  76 GIEVLLGTEVVSIDPGA-KKVVLEELVDGDGETityDRLVIATGA---RPRLPPIPGVELnvgFLVRTLDSAEALRLKLL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026  153 DKTVIISGGGNSAVDWANELEPIAKKVYVTYRKEEL-SGHEAQV-----KQLLNSSADCFFNTSITKLIagDNHEAIEYV 226
Cdd:pfam07992 152 PKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLlRAFDEEIsaaleKALEKNGVEVRLGTSVKEII--GDGDGVEVI 229

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447001026  227 eltnheTGEVSHLSIDEVIINHGYERDITLLEnsELDVAIIDNYYIAGNANSESSVDGLYAAGDILKHEGKLHLIAGA 304
Cdd:pfam07992 230 ------LKDGTEIDADLVVVAIGRRPNTELLE--AAGLELDERGGIVVDEYLRTSVPGIYAAGDCRVGGPELAQNAVA 299
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 1-290 9.67e-15

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 74.81  E-value: 9.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026   1 MNREELFDVTVIGGGPAGLYSAFYS---GLRemkTKII--EFqpqlGGKIH--VYPEKMIwdvgGLLPVTGDKLIEQLVQ 73
Cdd:PRK15317 206 LNAKDPYDVLVVGGGPAGAAAAIYAarkGIR---TGIVaeRF----GGQVLdtMGIENFI----SVPETEGPKLAAALEE 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026  74 QGLTFKPEVVLDTKVESIIRNeDGTFTLKTSNGAEHFSKTVIVATGSgilKPQKLSIEGAERFevsnlnytvkslkR--- 150
Cdd:PRK15317 275 HVKEYDVDIMNLQRASKLEPA-AGLIEVELANGAVLKAKTVILATGA---RWRNMNVPGEDEY-------------Rnkg 337

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026 151 -----------FKDKTVIISGGGNSAVDWANELEPIAKKVYVTYRKEELSGHEAQVKQlLNSSAdcffNTSI-----TKL 214
Cdd:PRK15317 338 vaycphcdgplFKGKRVAVIGGGNSGVEAAIDLAGIVKHVTVLEFAPELKADQVLQDK-LRSLP----NVTIitnaqTTE 412

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026 215 IAGDNHE--AIEYvelTNHETGEVSHLSIDEVIINhgyerdITLLENSE-LDVAIIDNYY--IAGNANSESSVDGLYAAG 289
Cdd:PRK15317 413 VTGDGDKvtGLTY---KDRTTGEEHHLELEGVFVQ------IGLVPNTEwLKGTVELNRRgeIIVDARGATSVPGVFAAG 483


                 .
gi 447001026 290 D 290
Cdd:PRK15317 484 D 484
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 7-323 8.38e-09

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: 56.50  E-value: 8.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026    7 FDVTVIGGGPAGLYSAFYSGLREMKTKIIEfQPQLGGK-IHV--YPEKmiwdvgGLLPVTgdKLIEQLVQ--------QG 75
Cdd:TIGR01350   2 YDVIVIGGGPGGYVAAIRAAQLGLKVALVE-KEYLGGTcLNVgcIPTK------ALLHSA--EVYDEIKHakdlgievEN 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026   76 LTFKPEVVLDTKVESIIRNEDGTFTLKTSNGAEHFS------------------------KTVIVATGSgilKPQKLSIE 131
Cdd:TIGR01350  73 VSVDWEKMQKRKNKVVKKLVGGVSGLLKKNKVTVIKgeakfldpgtvsvtgengeetleaKNIIIATGS---RPRSLPGP 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026  132 GAERFEVSNLNYTVKSLKRFKDKTVIIsGGGNSAVDWANELEPIAKKVYVT-YRKEELSGHEAQV-----KQLLNSSADC 205
Cdd:TIGR01350 150 FDFDGKVVITSTGALNLEEVPESLVII-GGGVIGIEFASIFASLGSKVTVIeMLDRILPGEDAEVskvlqKALKKKGVKI 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026  206 FFNTSITKLIAGDNheaieYVELTNhETGEVSHLSIDEVIINHGYERDITLLENSELDVAIIDNYYIAGNANSESSVDGL 285
Cdd:TIGR01350 229 LTNTKVTAVEKNDD-----QVTYEN-KGGETETLTGEKVLVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRTNVPGI 302

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 447001026  286 YAAGDILkheGKLHLIAGAFQD----AGNAVNKAKQFIQPDA 323
Cdd:TIGR01350 303 YAIGDVI---GGPMLAHVASHEgivaAENIAGKEPAHIDYDA 341
 
Name Accession Description Interval E-value
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
7-321 4.89e-87

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 264.29  E-value: 4.89e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026   7 FDVTVIGGGPAGLYSAFYSGLREMKTKIIEfQPQLGGKIHVYpeKMIWDVGGL-LPVTGDKLIEQLVQQGLTFKPEVVLD 85
Cdd:COG0492    1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIE-GGEPGGQLATT--KEIENYPGFpEGISGPELAERLREQAERFGAEILLE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026  86 TkVESIIRnEDGTFTLKTSNGAEHFSKTVIVATGSGilkPQKLSIEGAERFEVSNLNYTVKS-LKRFKDKTVIISGGGNS 164
Cdd:COG0492   78 E-VTSVDK-DDGPFRVTTDDGTEYEAKAVIIATGAG---PRKLGLPGEEEFEGRGVSYCATCdGFFFRGKDVVVVGGGDS 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026 165 AVDWANELEPIAKKVYVTYRKEELSGHEAQVKQLL-NSSADCFFNTSITKLIaGDNHeaIEYVELTNHETGEVSHLSIDE 243
Cdd:COG0492  153 ALEEALYLTKFASKVTLIHRRDELRASKILVERLRaNPKIEVLWNTEVTEIE-GDGR--VEGVTLKNVKTGEEKELEVDG 229

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447001026 244 VIINHGYERDITLLENseLDVAIIDNYYIAGNANSESSVDGLYAAGDILKHegKLHLIAGAFQDAGNAVNKAKQFIQP 321
Cdd:COG0492  230 VFVAIGLKPNTELLKG--LGLELDEDGYIVVDEDMETSVPGVFAAGDVRDY--KYRQAATAAGEGAIAALSAARYLEP 303
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 7-304 1.86e-21

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: 92.77  E-value: 1.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026    7 FDVTVIGGGPAGLYSAFYSGLREMKTKIIEFqpqlgGKIHVY----PEKMIWDVGGLLPV--TGDKLIEQL--VQQGLTF 78
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIED-----EGTCPYggcvLSKALLGAAEAPEIasLWADLYKRKeeVVKKLNN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026   79 KPEVVLDTKVESIIRNEdGTFTLKTSNGAEHFS---KTVIVATGSgilKPQKLSIEGAER---FEVSNLNYTVKSLKRFK 152
Cdd:pfam07992  76 GIEVLLGTEVVSIDPGA-KKVVLEELVDGDGETityDRLVIATGA---RPRLPPIPGVELnvgFLVRTLDSAEALRLKLL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026  153 DKTVIISGGGNSAVDWANELEPIAKKVYVTYRKEEL-SGHEAQV-----KQLLNSSADCFFNTSITKLIagDNHEAIEYV 226
Cdd:pfam07992 152 PKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLlRAFDEEIsaaleKALEKNGVEVRLGTSVKEII--GDGDGVEVI 229

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447001026  227 eltnheTGEVSHLSIDEVIINHGYERDITLLEnsELDVAIIDNYYIAGNANSESSVDGLYAAGDILKHEGKLHLIAGA 304
Cdd:pfam07992 230 ------LKDGTEIDADLVVVAIGRRPNTELLE--AAGLELDERGGIVVDEYLRTSVPGIYAAGDCRVGGPELAQNAVA 299
Pyr_redox_3 pfam13738
Pyridine nucleotide-disulphide oxidoreductase;
78-289 2.10e-17

Pyridine nucleotide-disulphide oxidoreductase;


Pssm-ID: 404603 [Multi-domain]  Cd Length: 296  Bit Score: 81.12  E-value: 2.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026   78 FKPEVVLDTKVESIIRNEDGtFTLKTSNGaEHFSKTVIVATGsGILKPQKLSIEgaerfEVSNLNYTVKSLKRFKDKTVI 157
Cdd:pfam13738  88 FELPINLFEEVTSVKKEDDG-FVVTTSKG-TYQARYVIIATG-EFDFPNKLGVP-----ELPKHYSYVKDFHPYAGQKVV 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026  158 ISGGGNSAVDWANELEPIAKKVYVTYRKEELSGHEAQVKQLL-------------NSSADCFFNTSITKLiagDNHEAIE 224
Cdd:pfam13738 160 VIGGYNSAVDAALELVRKGARVTVLYRGSEWEDRDSDPSYSLspdtlnrleelvkNGKIKAHFNAEVKEI---TEVDVSY 236

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447001026  225 YVELTNHETGEVShlsiDEVIINHGYERDITLLENSELDVAiiDNYYIAGNANSESS-VDGLYAAG 289
Cdd:pfam13738 237 KVHTEDGRKVTSN----DDPILATGYHPDLSFLKKGLFELD--EDGRPVLTEETESTnVPGLFLAG 296
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 9-291 4.14e-15

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: 75.94  E-value: 4.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026   9 VTVIGGGPAGLYSAFYsgLRemktkiiefqpQLGGKIHVYpEKMiwD-VGGLLpVTG-----------DKLIEQLVQQGL 76
Cdd:COG0493  124 VAVVGSGPAGLAAAYQ--LA-----------RAGHEVTVF-EAL--DkPGGLL-RYGipefrlpkdvlDREIELIEALGV 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026  77 TFKPEVVL--DTKVESIIRNEDgtftlktsngAehfsktVIVATGSGilKPQKLSIEGAE------------RFEVSNLN 142
Cdd:COG0493  187 EFRTNVEVgkDITLDELLEEFD----------A------VFLATGAG--KPRDLGIPGEDlkgvhsamdfltAVNLGEAP 248

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026 143 YTVKslkrFKDKTVIISGGGNSAVD---WANELEpiAKKVYVTYR--KEELSGHEAQVKQLLNSSADCFFNTSITKLIAG 217
Cdd:COG0493  249 DTIL----AVGKRVVVIGGGNTAMDcarTALRLG--AESVTIVYRrtREEMPASKEEVEEALEEGVEFLFLVAPVEIIGD 322

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026 218 DNH--EAIEYVELTNHE------------TGEVSHLSIDEVIINHGYERDITLLEnSELDVAIIDNYYIAGNANS-ESSV 282
Cdd:COG0493  323 ENGrvTGLECVRMELGEpdesgrrrpvpiEGSEFTLPADLVILAIGQTPDPSGLE-EELGLELDKRGTIVVDEETyQTSL 401


                 ....*....
gi 447001026 283 DGLYAAGDI 291
Cdd:COG0493  402 PGVFAGGDA 410
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 1-290 9.67e-15

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 74.81  E-value: 9.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026   1 MNREELFDVTVIGGGPAGLYSAFYS---GLRemkTKII--EFqpqlGGKIH--VYPEKMIwdvgGLLPVTGDKLIEQLVQ 73
Cdd:PRK15317 206 LNAKDPYDVLVVGGGPAGAAAAIYAarkGIR---TGIVaeRF----GGQVLdtMGIENFI----SVPETEGPKLAAALEE 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026  74 QGLTFKPEVVLDTKVESIIRNeDGTFTLKTSNGAEHFSKTVIVATGSgilKPQKLSIEGAERFevsnlnytvkslkR--- 150
Cdd:PRK15317 275 HVKEYDVDIMNLQRASKLEPA-AGLIEVELANGAVLKAKTVILATGA---RWRNMNVPGEDEY-------------Rnkg 337

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026 151 -----------FKDKTVIISGGGNSAVDWANELEPIAKKVYVTYRKEELSGHEAQVKQlLNSSAdcffNTSI-----TKL 214
Cdd:PRK15317 338 vaycphcdgplFKGKRVAVIGGGNSGVEAAIDLAGIVKHVTVLEFAPELKADQVLQDK-LRSLP----NVTIitnaqTTE 412

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026 215 IAGDNHE--AIEYvelTNHETGEVSHLSIDEVIINhgyerdITLLENSE-LDVAIIDNYY--IAGNANSESSVDGLYAAG 289
Cdd:PRK15317 413 VTGDGDKvtGLTY---KDRTTGEEHHLELEGVFVQ------IGLVPNTEwLKGTVELNRRgeIIVDARGATSVPGVFAAG 483


                 .
gi 447001026 290 D 290
Cdd:PRK15317 484 D 484
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 9-291 1.55e-13

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 70.98  E-value: 1.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026   9 VTVIGGGPAGLYSAFYsgLRemktkiiefqpQLGGKIHVY---PEkmiwdVGGLLpVTG-----------DKLIEQLVQQ 74
Cdd:PRK11749 143 VAVIGAGPAGLTAAHR--LA-----------RKGYDVTIFearDK-----AGGLL-RYGipefrlpkdivDREVERLLKL 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026  75 GLTFKPEVVLdtkvesiirneDGTFTLktsngAEHFS--KTVIVATGSGilKPQKLSIEGAERFEV-SNLNYtVKSLKRF 151
Cdd:PRK11749 204 GVEIRTNTEV-----------GRDITL-----DELRAgyDAVFIGTGAG--LPRFLGIPGENLGGVySAVDF-LTRVNQA 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026 152 KD-------KTVIISGGGNSAVDWANELepI---AKKVYVTYR--KEELSG--------HEAQVKQLLNSSadcffntsi 211
Cdd:PRK11749 265 VAdydlpvgKRVVVIGGGNTAMDAARTA--KrlgAESVTIVYRrgREEMPAseeevehaKEEGVEFEWLAA--------- 333

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026 212 TKLIAGDN--HEAIEYVELTNHE-----------TGEVSHLSIDEVIINHGYERDITLLENS-ELDVAiIDNYYIAGNAN 277
Cdd:PRK11749 334 PVEILGDEgrVTGVEFVRMELGEpdasgrrrvpiEGSEFTLPADLVIKAIGQTPNPLILSTTpGLELN-RWGTIIADDET 412

                        330
                 ....*....|....
gi 447001026 278 SESSVDGLYAAGDI 291
Cdd:PRK11749 413 GRTSLPGVFAGGDI 426
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 5-184 2.23e-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: 70.66  E-value: 2.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026   5 ELFDVTVIGGGPAGLYSAFYsgLREM--KTKIIEFQPQLGG----------------KIHVYPEKMIWDVGGLLPvTGDK 66
Cdd:COG2072    5 EHVDVVVIGAGQAGLAAAYH--LRRAgiDFVVLEKADDVGGtwrdnrypglrldtpsHLYSLPFFPNWSDDPDFP-TGDE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026  67 L---IEQLVQQ-GLTfkPEVVLDTKVESI-IRNEDGTFTLKTSNGAEHFSKTVIVATGsgIL-KPQKLSIEGAERFEV-- 138
Cdd:COG2072   82 IlayLEAYADKfGLR--RPIRFGTEVTSArWDEADGRWTVTTDDGETLTARFVVVATG--PLsRPKIPDIPGLEDFAGeq 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 447001026 139 ---SNLNYTVkslkRFKDKTVIISGGGNSAVDWANELEPIAKKVYVTYR 184
Cdd:COG2072  158 lhsADWRNPV----DLAGKRVLVVGTGASAVQIAPELARVAAHVTVFQR 202
PRK10262 PRK10262
thioredoxin reductase; Provisional
 11-294 1.60e-12

thioredoxin reductase; Provisional


Pssm-ID: 182343 [Multi-domain]  Cd Length: 321  Bit Score: 67.39  E-value: 1.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026  11 VIGGGPAGLYSAFYSGLREMKTKIIEFQPQlGGKIHVYPEKMIWDvGGLLPVTGDKLIEQLVQQGLTFKPEVVLDTKVES 90
Cdd:PRK10262  11 ILGSGPAGYTAAVYAARANLQPVLITGMEK-GGQLTTTTEVENWP-GDPNDLTGPLLMERMHEHATKFETEIIFDHINKV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026  91 IIRNEdgTFTLkTSNGAEHFSKTVIVATGSgilKPQKLSIEGAERFEVSNLNYTVKSLKRF-KDKTVIISGGGNSAVDWA 169
Cdd:PRK10262  89 DLQNR--PFRL-TGDSGEYTCDALIIATGA---SARYLGLPSEEAFKGRGVSACATCDGFFyRNQKVAVIGGGNTAVEEA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026 170 NELEPIAKKVYVTYRKEELSGHEAQVKQLLN--SSADCFFNTSIT-KLIAGDNHEAIEYVELTNHETGEVSHLSIDEVII 246
Cdd:PRK10262 163 LYLSNIASEVHLIHRRDGFRAEKILIKRLMDkvENGNIILHTNRTlEEVTGDQMGVTGVRLRDTQNSDNIESLDVAGLFV 242

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 447001026 247 NHGYERDITLLENS-ELDVAIID-NYYIAGNAnSESSVDGLYAAGDILKH 294
Cdd:PRK10262 243 AIGHSPNTAIFEGQlELENGYIKvQSGIHGNA-TQTSIPGVFAAGDVMDH 291
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
 9-292 2.08e-10

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 61.16  E-value: 2.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026   9 VTVIGGGPAGLYSAFYSGLRemktkiiefqpqlGGKIHVY---PEKmiwdvGGLL---------PVTGDKL-IEQLVQQG 75
Cdd:PRK12770  21 VAIIGAGPAGLAAAGYLACL-------------GYEVHVYdklPEP-----GGLMlfgipefriPIERVREgVKELEEAG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026  76 LTFKPevvlDTKV--ESIIRNEDGtftlktsngaEHFSK-------------TVIVATGSgiLKPQKLSIEGAE------ 134
Cdd:PRK12770  83 VVFHT----RTKVccGEPLHEEEG----------DEFVErivsleelvkkydAVLIATGT--WKSRKLGIPGEDlpgvys 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026 135 ------RFEVSNLNYTVK-SLKRFKDKTVIISGGGNSAVDWANE-LEPIAKKVYVTYR--KEELSGHEAQVKQLLNSSAD 204
Cdd:PRK12770 147 aleylfRIRAAKLGYLPWeKVPPVEGKKVVVVGAGLTAVDAALEaVLLGAEKVYLAYRrtINEAPAGKYEIERLIARGVE 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026 205 CFFNTSITKLIAGDNHEAIEYVELTNHE------------TGEVSHLSIDEVIINHGyERDITLLENSELDVAIIDNYYI 272
Cdd:PRK12770 227 FLELVTPVRIIGEGRVEGVELAKMRLGEpdesgrprpvpiPGSEFVLEADTVVFAIG-EIPTPPFAKECLGIELNRKGEI 305

                        330       340
                 ....*....|....*....|
gi 447001026 273 AGNANSESSVDGLYAAGDIL 292
Cdd:PRK12770 306 VVDEKHMTSREGVFAAGDVV 325
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 7-323 8.38e-09

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: 56.50  E-value: 8.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026    7 FDVTVIGGGPAGLYSAFYSGLREMKTKIIEfQPQLGGK-IHV--YPEKmiwdvgGLLPVTgdKLIEQLVQ--------QG 75
Cdd:TIGR01350   2 YDVIVIGGGPGGYVAAIRAAQLGLKVALVE-KEYLGGTcLNVgcIPTK------ALLHSA--EVYDEIKHakdlgievEN 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026   76 LTFKPEVVLDTKVESIIRNEDGTFTLKTSNGAEHFS------------------------KTVIVATGSgilKPQKLSIE 131
Cdd:TIGR01350  73 VSVDWEKMQKRKNKVVKKLVGGVSGLLKKNKVTVIKgeakfldpgtvsvtgengeetleaKNIIIATGS---RPRSLPGP 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026  132 GAERFEVSNLNYTVKSLKRFKDKTVIIsGGGNSAVDWANELEPIAKKVYVT-YRKEELSGHEAQV-----KQLLNSSADC 205
Cdd:TIGR01350 150 FDFDGKVVITSTGALNLEEVPESLVII-GGGVIGIEFASIFASLGSKVTVIeMLDRILPGEDAEVskvlqKALKKKGVKI 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026  206 FFNTSITKLIAGDNheaieYVELTNhETGEVSHLSIDEVIINHGYERDITLLENSELDVAIIDNYYIAGNANSESSVDGL 285
Cdd:TIGR01350 229 LTNTKVTAVEKNDD-----QVTYEN-KGGETETLTGEKVLVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRTNVPGI 302

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 447001026  286 YAAGDILkheGKLHLIAGAFQD----AGNAVNKAKQFIQPDA 323
Cdd:TIGR01350 303 YAIGDVI---GGPMLAHVASHEgivaAENIAGKEPAHIDYDA 341
HI0933_like pfam03486
HI0933-like protein;
7-119 6.05e-08

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 53.74  E-value: 6.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026    7 FDVTVIGGGPAGLYSAFYSGLREMKTKIIEFQPQLGGKI-----------HVY-------------------------PE 50
Cdd:pfam03486   1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLGRKIlisgggrcnvtNLSeepdnflsrypgnpkflksalsrftPW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026   51 KMI-W-----------DVGGLLPVTG------DKLIEQLVQQGLTFKpevvLDTKVESIIRNEDGTFTLKTSNGAEHFSK 112
Cdd:pfam03486  81 DFIaFfeslgvplkeeDHGRLFPDSDkasdivDALLNELKELGVKIR----LRTRVLSVEKDDDGRFRVKTGGEELEADS 156


                  ....*..
gi 447001026  113 tVIVATG 119
Cdd:pfam03486 157 -LVLATG 162
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
 9-290 6.63e-08

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 53.96  E-value: 6.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026   9 VTVIGGGPAGLYSAFYSGLREMKTKIIEFQPQLGGKIHvY-------PEKMIwdvggllpvtgDKLIEQLVQQGLTFKPE 81
Cdd:PRK12814 196 VAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMR-YgiprfrlPESVI-----------DADIAPLRAMGAEFRFN 263

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026  82 VVL--DTKVESIIRNEDGTFtlktsngaehfsktviVATGSGilKPQKLSIEGAERFEV-SNLNYtvksLKRFKD----- 153
Cdd:PRK12814 264 TVFgrDITLEELQKEFDAVL----------------LAVGAQ--KASKMGIPGEELPGViSGIDF----LRNVALgtalh 321

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026 154 --KTVIISGGGNSAVDWA-NELEPIAKKVYVTYR--KEELSGHEAQVKQLLNS--SADCF-FNTSITKLIAGDNHEAIEY 225
Cdd:PRK12814 322 pgKKVVVIGGGNTAIDAArTALRLGAESVTILYRrtREEMPANRAEIEEALAEgvSLRELaAPVSIERSEGGLELTAIKM 401

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447001026 226 VELTNHETG-------EVSHLSI--DEVIINHGYERDITLLENSELDVAiiDNYYIAGNANS-ESSVDGLYAAGD 290
Cdd:PRK12814 402 QQGEPDESGrrrpvpvEGSEFTLqaDTVISAIGQQVDPPIAEAAGIGTS--RNGTVKVDPETlQTSVAGVFAGGD 474
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 9-314 3.45e-07

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


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 52.05  E-value: 3.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026   9 VTVIGGGPAGLYSAFYSGLREMKTKIIEFQPQLGGkIHVY--PE----KMIWDVGgllpvtgdklIEQLVQQGLTFKPEV 82
Cdd:PRK12778 434 VAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGG-VLKYgiPEfrlpKKIVDVE----------IENLKKLGVKFETDV 502

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026  83 VLDTkvesiirnedgTFTLKTSnGAEHFsKTVIVATGSGIlkPQKLSIEGAERFEV--SNLNYT-VKSLKRFKD------ 153
Cdd:PRK12778 503 IVGK-----------TITIEEL-EEEGF-KGIFIASGAGL--PNFMNIPGENSNGVmsSNEYLTrVNLMDAASPdsdtpi 567

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026 154 ---KTVIISGGGNSAVDWANELEPI-AKKVYVTYRK--EELSGHEAQVKQLLNSSADcfFNTSITKL-IAGDNHEAIEYV 226
Cdd:PRK12778 568 kfgKKVAVVGGGNTAMDSARTAKRLgAERVTIVYRRseEEMPARLEEVKHAKEEGIE--FLTLHNPIeYLADEKGWVKQV 645

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026 227 ELTNHETGE---------------VSHLSIDEVIINHGYERDiTLLENSELDVAIIDNYYIAGNANSESSVDGLYAAGDI 291
Cdd:PRK12778 646 VLQKMELGEpdasgrrrpvaipgsTFTVDVDLVIVSVGVSPN-PLVPSSIPGLELNRKGTIVVDEEMQSSIPGIYAGGDI 724

                        330       340
                 ....*....|....*....|...
gi 447001026 292 LKHEGKLHLIAGAFQDAGNAVNK 314
Cdd:PRK12778 725 VRGGATVILAMGDGKRAAAAIDE 747
PRK12831 PRK12831
putative oxidoreductase; Provisional
 9-314 5.22e-07

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 51.17  E-value: 5.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026   9 VTVIGGGPAGLYSAFYSGLREMKTKIIEFQPQLGGkIHVY--PEKMiwdvgglLPVTG--DKLIEQLVQQGLTFKPEVVL 84
Cdd:PRK12831 143 VAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGG-VLVYgiPEFR-------LPKETvvKKEIENIKKLGVKIETNVVV 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026  85 --DTKVESIIrnEDGTFtlktsngaehfsKTVIVATGSGIlkPQKLSIEGaerfevSNLN--YT-------VKSLKRFKD 153
Cdd:PRK12831 215 gkTVTIDELL--EEEGF------------DAVFIGSGAGL--PKFMGIPG------ENLNgvFSanefltrVNLMKAYKP 272

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026 154 ---------KTVIISGGGNSAVDWANELEPIAKKVYVTYRK--EELSGHEAQVKQLLNSSADCFFNTSITKLIAGDNH-- 220
Cdd:PRK12831 273 eydtpikvgKKVAVVGGGNVAMDAARTALRLGAEVHIVYRRseEELPARVEEVHHAKEEGVIFDLLTNPVEILGDENGwv 352

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026 221 EAIEYVELTNHE------------TGEVSHLSIDEVIINHGYERDITLLENSE-LDVAiIDNYYIAGNANSESSVDGLYA 287
Cdd:PRK12831 353 KGMKCIKMELGEpdasgrrrpveiEGSEFVLEVDTVIMSLGTSPNPLISSTTKgLKIN-KRGCIVADEETGLTSKEGVFA 431

                        330       340
                 ....*....|....*....|....*..
gi 447001026 288 AGDILKHEGKLHLIAGAFQDAGNAVNK 314
Cdd:PRK12831 432 GGDAVTGAATVILAMGAGKKAAKAIDE 458
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 7-291 1.23e-06

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: 50.09  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026   7 FDVTVIGGGPAGLYSAFYSGLREMKTKIIEfQPQLGGK-IHV--YPEKMIWDVGGLLpvtgdKLIEQLVQQGLTFKP--- 80
Cdd:COG1249    4 YDLVVIGAGPGGYVAAIRAAQLGLKVALVE-KGRLGGTcLNVgcIPSKALLHAAEVA-----HEARHAAEFGISAGApsv 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026  81 ----------EVV--LDTKVESIIRNED-------GTF----TLKTSNGAEHFSKTVIVATGSgilKPQKLSIEGA--ER 135
Cdd:COG1249   78 dwaalmarkdKVVdrLRGGVEELLKKNGvdvirgrARFvdphTVEVTGGETLTADHIVIATGS---RPRVPPIPGLdeVR 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026 136 FEVSNlnyTVKSLKRFKDKTVIIsGGGNSAVdwanELEPIAK----KVYVTYRKEE-LSGHEAQV-----KQLLNSSADC 205
Cdd:COG1249  155 VLTSD---EALELEELPKSLVVI-GGGYIGL----EFAQIFArlgsEVTLVERGDRlLPGEDPEIsealeKALEKEGIDI 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026 206 FFNTSITKLIAGDNHeaieyVELTNHETGEVSHLSIDEVII---------NHGYErditllensELDVAIIDNYYIAGNA 276
Cdd:COG1249  227 LTGAKVTSVEKTGDG-----VTVTLEDGGGEEAVEADKVLVatgrrpntdGLGLE---------AAGVELDERGGIKVDE 292

                        330
                 ....*....|....*
gi 447001026 277 NSESSVDGLYAAGDI 291
Cdd:COG1249  293 YLRTSVPGIYAIGDV 307
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 9-295 1.93e-06

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 49.49  E-value: 1.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026   9 VTVIGGGPAGLYSAFYSGLREMKTKIIEFQPQLGGKIHvY-------PEKMIwdvggllpvtgDKLIEQLVQQGLtfkpE 81
Cdd:PRK12771 140 VAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMR-YgipayrlPREVL-----------DAEIQRILDLGV----E 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026  82 VVLDTKVESIIRNEDgtftLKTSNGAehfsktVIVATGSGILKpqKLSIEGAerfEVSNLNYTVKSLKRFKD-------K 154
Cdd:PRK12771 204 VRLGVRVGEDITLEQ----LEGEFDA------VFVAIGAQLGK--RLPIPGE---DAAGVLDAVDFLRAVGEgeppflgK 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026 155 TVIISGGGNSAVDWANELEPI-AKKVYVTYR--KEELSGHEAQVKQLLNSSADCFFNTSITKLIAGDNH---------EA 222
Cdd:PRK12771 269 RVVVIGGGNTAMDAARTARRLgAEEVTIVYRrtREDMPAHDEEIEEALREGVEINWLRTPVEIEGDENGatglrvitvEK 348

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447001026 223 IEYVE-LTNH-ETGEVSHLSIDEVIINHGYERDITLLEnsELDVAIIDNYYIAGNANSE-SSVDGLYAAGDILKHE 295
Cdd:PRK12771 349 MELDEdGRPSpVTGEEETLEADLVVLAIGQDIDSAGLE--SVPGVEVGRGVVQVDPNFMmTGRPGVFAGGDMVPGP 422
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 9-290 5.91e-06

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 47.85  E-value: 5.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026   9 VTVIGGGPAGLYSAfysglremktkiiEFQPQLGGKIHVY---PEkmiwdVGGLL----P--------VtgDKLIEQLVQ 73
Cdd:PRK12810 146 VAVVGSGPAGLAAA-------------DQLARAGHKVTVFeraDR-----IGGLLrygiPdfklekevI--DRRIELMEA 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026  74 QGLTFKPEVVL--DTKVESIIRNEDGtftlktsngaehfsktVIVATGSGilKPQKLSIEGAERFEV------------S 139
Cdd:PRK12810 206 EGIEFRTNVEVgkDITAEELLAEYDA----------------VFLGTGAY--KPRDLGIPGRDLDGVhfamdfliqntrR 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026 140 NLNYTVKSLKRFKDKTVIISGGGNSAVD--------------------------WANELEPIAKKVY-VTYRKEElsghe 192
Cdd:PRK12810 268 VLGDETEPFISAKGKHVVVIGGGDTGMDcvgtairqgaksvtqrdimpmppsrrNKNNPWPYWPMKLeVSNAHEE----- 342

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026 193 aqvkqllnssADCF-FNTSITKLIAGDNH-EAIEYVELTNHE------TGEVSHLSIDEVIINHGYE-RDITLLEnsELD 263
Cdd:PRK12810 343 ----------GVEReFNVQTKEFEGENGKvTGVKVVRTELGEgdfepvEGSEFVLPADLVLLAMGFTgPEAGLLA--QFG 410

                        330       340
                 ....*....|....*....|....*...
gi 447001026 264 VAIIDNYYI-AGNANSESSVDGLYAAGD 290
Cdd:PRK12810 411 VELDERGRVaAPDNAYQTSNPKVFAAGD 438
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 69-290 6.60e-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: 47.11  E-value: 6.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026  69 EQLVQQGLtfkpEVVLDTKVESIIRnEDGTFTLKTsNGAEHFSKtVIVATGSgilKPQKLSIEGAER---FEVSNLN--- 142
Cdd:COG0446   44 ESFERKGI----DVRTGTEVTAIDP-EAKTVTLRD-GETLSYDK-LVLATGA---RPRPPPIPGLDLpgvFTLRTLDdad 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026 143 YTVKSLKRFKDKTVIISGGGnsavdwanelePIA-----------KKVYVTYRK--------EELSgheAQVKQLLNSS- 202
Cdd:COG0446  114 ALREALKEFKGKRAVVIGGG-----------PIGlelaealrkrgLKVTLVERAprllgvldPEMA---ALLEEELREHg 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026 203 ADCFFNTSITKlIAGDNHEAieyVELTNHETgevshLSIDEVIINHGYERDITLLENSELdvAIIDNYYIAGNANSESSV 282
Cdd:COG0446  180 VELRLGETVVA-IDGDDKVA---VTLTDGEE-----IPADLVVVAPGVRPNTELAKDAGL--ALGERGWIKVDETLQTSD 248


                 ....*...
gi 447001026 283 DGLYAAGD 290
Cdd:COG0446  249 PDVYAAGD 256
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
 7-291 4.37e-05

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: 44.96  E-value: 4.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026    7 FDVTVIGGGPAGLYSAFYSG-LREMKTKIIEFQPQ--------LGG---KIHVYPEKMIwdvggllpVTGDKLIEQLVQQ 74
Cdd:TIGR01423   4 FDLVVIGAGSGGLEAGWNAAtLYKKRVAVVDVQTHhgppfyaaLGGtcvNVGCVPKKLM--------VTGAQYMDTLRES 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026   75 --------GLTFKP----------EVVLDTK--VESIIRNEDG-TF-----TLKTSN------GAEHFSKT--------V 114
Cdd:TIGR01423  76 agfgwefdRSSVKAnwkaliaaknKAVLDINksYEGMFADTEGlTFflgwgALEDKNvvlvreSADPKSAVkerlqaehI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026  115 IVATGSGilkPQKLSIEGAERFEVSNLNYTVKSLKRfkdkTVIISGGGNSAVDWA---NELEPIAKKVYVTYRKEE-LSG 190
Cdd:TIGR01423 156 LLATGSW---PQMLGIPGIEHCISSNEAFYLDEPPR----RVLTVGGGFISVEFAgifNAYKPRGGKVTLCYRNNMiLRG 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026  191 HEAQV-----KQLLNSSADCFFNTSITKLIAgdNHEAIEYVELtnhETGEVshLSIDEVIINHGYERDITLLENSELDVA 265
Cdd:TIGR01423 229 FDSTLrkeltKQLRANGINIMTNENPAKVTL--NADGSKHVTF---ESGKT--LDVDVVMMAIGRVPRTQTLQLDKVGVE 301

                         330       340
                  ....*....|....*....|....*.
gi 447001026  266 IIDNYYIAGNANSESSVDGLYAAGDI 291
Cdd:TIGR01423 302 LTKKGAIQVDEFSRTNVPNIYAIGDV 327
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 8-58 7.49e-05

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: 44.44  E-value: 7.49e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 447001026   8 DVTVIGGGPAGLYSAFYSGLREMKTKIIEFQPQLGGKIHVYPEK-MIWDVGG 58
Cdd:COG1232    3 RVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIRTVEVDgFRIDRGP 54
TGR TIGR01438
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ...
 7-306 8.71e-05

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: 44.07  E-value: 8.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026    7 FDVTVIGGGPAGLYSAFYSGLREMKTKIIEF---QPQ-----LGG---KIHVYPEKMI-----------------WDVGG 58
Cdd:TIGR01438   3 YDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFvtpTPLgtrwgIGGtcvNVGCIPKKLMhqaallgqalkdsrnygWKVEE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026   59 LLPVTGDKLIEQlVQ---QGLTFKPEVVLDtkvESIIRNEDG--------TFTLKTSNGAEHF--SKTVIVATGsgiLKP 125
Cdd:TIGR01438  83 TVKHDWKRLVEA-VQnhiGSLNWGYRVALR---EKKVKYENAyaefvdkhRIKATNKKGKEKIysAERFLIATG---ERP 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026  126 QKLSIEGAERFEVSNLNytVKSLKRFKDKTVIIsGGGNSAVDWANELEPIAKKVYVTYRKEELSGHEAQ----VKQLLNS 201
Cdd:TIGR01438 156 RYPGIPGAKELCITSDD--LFSLPYCPGKTLVV-GASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDcankVGEHMEE 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026  202 SADCFFNTSITKLIagdnhEAIE---YVELTNHETGEVSHLsiDEVIINHGYERDITLLENSELDVAIID-NYYIAGNAN 277
Cdd:TIGR01438 233 HGVKFKRQFVPIKV-----EQIEakvLVEFTDSTNGIEEEY--DTVLLAIGRDACTRKLNLENVGVKINKkTGKIPADEE 305

                         330       340
                  ....*....|....*....|....*....
gi 447001026  278 SESSVDGLYAAGDILkhEGKLHLIAGAFQ 306
Cdd:TIGR01438 306 EQTNVPYIYAVGDIL--EDKPELTPVAIQ 332
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
1-119 1.18e-04

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 43.58  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026   1 MNREELFDVTVIGGGPAGLYSAFysGLREMKTKIIEFQPQLGGKIHVY---PEKMIwdVGGLLPVTGDKLIEQLVQQGLt 77
Cdd:COG1252  144 AERRRLLTIVVVGGGPTGVELAG--ELAELLRKLLRYPGIDPDKVRITlveAGPRI--LPGLGEKLSEAAEKELEKRGV- 218

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 447001026  78 fkpEVVLDTKVESIirnEDGTFTLKtsNGAEHFSKTVIVATG 119
Cdd:COG1252  219 ---EVHTGTRVTEV---DADGVTLE--DGEEIPADTVIWAAG 252
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 9-119 5.53e-04

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: 41.34  E-value: 5.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026   9 VTVIGGGPAGLYSAFYSGLREMKTKIIEFQPQLGGkihVYPEKMiwdvggllpvtGDKLIEQLVQQGLtfkpEVVLDTKV 88
Cdd:COG0446  127 AVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLG---VLDPEM-----------AALLEEELREHGV----ELRLGETV 188

                         90       100       110
                 ....*....|....*....|....*....|.
gi 447001026  89 ESIirNEDGTFTLKTSNGAEHFSKTVIVATG 119
Cdd:COG0446  189 VAI--DGDDKVAVTLTDGEEIPADLVVVAPG 217
carotene-cycl TIGR01790
lycopene cyclase family protein; This family includes lycopene beta and epsilion cyclases ...
 8-129 1.37e-03

lycopene cyclase family protein; This family includes lycopene beta and epsilion cyclases (which form beta and delta carotene, respectively) from bacteria and plants as well as the plant capsanthin/capsorubin and neoxanthin cyclases which appear to have evolved from the plant lycopene cyclases. The plant lycopene epsilon cyclases also transform neurosporene to alpha zeacarotene.


Pssm-ID: 130850 [Multi-domain]  Cd Length: 388  Bit Score: 40.11  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026    8 DVTVIGGGPAGLYSAFYSGLREMKTKIIEFQPQLGGKiHVY----PEKMIWDVGGLL--------PVTGDK--------- 66
Cdd:TIGR01790   1 DLAVIGGGPAGLAIALELARPGLRVQLIEPHPPIPGN-HTYgvwdDDLSDLGLADCVehvwpdvyEYRFPKqprklgtay 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447001026   67 -----------LIEQLVQQGLTFkpevvLDTKVESIIRNEDGTFTLKTSNGAEHFSKTVIVATGSGILKPQKLS 129
Cdd:TIGR01790  80 gsvdstrlheeLLQKCPEGGVLW-----LERKAIHAEADGVALSTVYCAGGQRIQARLVIDARGFGPLVQYVRF 148
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
8-128 2.29e-03

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 39.84  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447001026   8 DVTVIGGGPAGLYSAFysGLREM--KTKIIEFQPQLGGKI----HVYPekmiwdvgGLLPVTgdKLIEQLVQQgLTFKP- 80
Cdd:COG1148  142 RALVIGGGIAGMTAAL--ELAEQgyEVYLVEKEPELGGRAaqlhKTFP--------GLDCPQ--CILEPLIAE-VEANPn 208

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 447001026  81 -EVVLDTKVESiIRNEDGTFTLKTSNGAEHFSK----TVIVATGSGILKPQKL 128
Cdd:COG1148  209 iTVYTGAEVEE-VSGYVGNFTVTIKKGPREEIEievgAIVLATGFKPYDPTKL 260
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
11-46 6.79e-03

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 34.81  E-value: 6.79e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 447001026   11 VIGGGPAGLYSAFYSGLREMKTKIIEFQPQLGGKIH 46
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAY 36
 
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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