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Conserved domains on  [gi|1039431258|ref|WP_064795031|]
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MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Klebsiella]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
19-398 1.33e-109

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


:

Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 327.48  E-value: 1.33e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  19 KTLRDEGFSGEICVVAEEQWDFYERPPLSKAALLEAEPALPRLFSAEAQQALNLRWYRPLRADSIDRQNKTVALSNGETL 98
Cdd:COG1251    18 EELRKLDPDGEITVIGAEPHPPYNRPPLSKVLAGETDEEDLLLRPADFYEENGIDLRLGTRVTAIDRAARTVTLADGETL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  99 AYDQLLIATGGRARLPSEGWAQHPQVYTLRHWQDAQRLKQRLASATRLAIVGGGWIGLEIAASARKSDVAVTLYEQQPAL 178
Cdd:COG1251    98 PYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRAALAPGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRL 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 179 CMRSVSMEVSQALAQLHRQQGVEIRGGCGALELEDDNGLPTLHC-DGQRETFDAVVVGIGVDLNLELARDAGLTVDRGIV 257
Cdd:COG1251   178 LPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRLaDGEELPADLVVVAIGVRPNTELARAAGLAVDRGIV 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 258 VNAQGRSNDPAIFAAGDVAQHHQ--YG-LCIQSWAFAQNQAIATAKAMLDPQASGYDEAPWLWSDQYDRNIQILGIPQAG 334
Cdd:COG1251   258 VDDYLRTSDPDIYAAGDCAEHPGpvYGrRVLELVAPAYEQARVAAANLAGGPAAYEGSVPSTKLKVFGVDVASAGDAEGD 337

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039431258 335 SRTIVRDEPQGAIYFSLN-ADGRLTQLVAFNNARIVKLAKRWMAAGRDLSNVPLADPTFSLMSLR 398
Cdd:COG1251   338 EEVVVRGDPARGVYKKLVlRDGRLVGAVLVGDTSDAGALRQLIKNGRPLPPRALLDAALPLKELK 402
 
Name Accession Description Interval E-value
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
19-398 1.33e-109

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 327.48  E-value: 1.33e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  19 KTLRDEGFSGEICVVAEEQWDFYERPPLSKAALLEAEPALPRLFSAEAQQALNLRWYRPLRADSIDRQNKTVALSNGETL 98
Cdd:COG1251    18 EELRKLDPDGEITVIGAEPHPPYNRPPLSKVLAGETDEEDLLLRPADFYEENGIDLRLGTRVTAIDRAARTVTLADGETL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  99 AYDQLLIATGGRARLPSEGWAQHPQVYTLRHWQDAQRLKQRLASATRLAIVGGGWIGLEIAASARKSDVAVTLYEQQPAL 178
Cdd:COG1251    98 PYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRAALAPGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRL 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 179 CMRSVSMEVSQALAQLHRQQGVEIRGGCGALELEDDNGLPTLHC-DGQRETFDAVVVGIGVDLNLELARDAGLTVDRGIV 257
Cdd:COG1251   178 LPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRLaDGEELPADLVVVAIGVRPNTELARAAGLAVDRGIV 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 258 VNAQGRSNDPAIFAAGDVAQHHQ--YG-LCIQSWAFAQNQAIATAKAMLDPQASGYDEAPWLWSDQYDRNIQILGIPQAG 334
Cdd:COG1251   258 VDDYLRTSDPDIYAAGDCAEHPGpvYGrRVLELVAPAYEQARVAAANLAGGPAAYEGSVPSTKLKVFGVDVASAGDAEGD 337

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039431258 335 SRTIVRDEPQGAIYFSLN-ADGRLTQLVAFNNARIVKLAKRWMAAGRDLSNVPLADPTFSLMSLR 398
Cdd:COG1251   338 EEVVVRGDPARGVYKKLVlRDGRLVGAVLVGDTSDAGALRQLIKNGRPLPPRALLDAALPLKELK 402
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
 5-380 2.83e-69

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 223.65  E-value: 2.83e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258   5 IVIIGGGQAGGWAAKTLRDEGFSGEICVVAEEQWDFYERPPLSKAALLEAEPALPRLFSAEAQQALNLRWYRPLRADSID 84
Cdd:PRK09754    6 IIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPQLQQVLPANWWQENNVHLHSGVTIKTLG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  85 RQNKTVALSNGETLAYDQLLIATGGRARLPSEGWAQHPQVYTLRHWQDAQRLKQRLASATRLAIVGGGWIGLEIAASARK 164
Cdd:PRK09754   86 RDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELAASATQ 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 165 SDVAVTLYEQQPALCMRSVSMEVSQALAQLHRQQGVEIRGGCGALELEDDNGLPTLHCDGQRETFDAVVVGIGVDLNLEL 244
Cdd:PRK09754  166 RRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVELTLQSGETLQADVVIYGIGISANDQL 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 245 ARDAGLTVDRGIVVNAQGRSNDPAIFAAGDVAQHHQYGLCIQ---SWAFAQNQAIATAKAMLD---PQASgydeAPWLWS 318
Cdd:PRK09754  246 AREANLDTANGIVIDEACRTCDPAIFAGGDVAITRLDNGALHrceSWENANNQAQIAAAAMLGlplPLLP----PPWFWS 321

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039431258 319 DQYDRNIQILGIPQAGSRTIVRD-EPQGAIYFSLNaDGRLTQLVAFNNARIVKLAKRWMAAGR 380
Cdd:PRK09754  322 DQYSDNLQFIGDMRGDDWLCRGNpETQKAIWFNLQ-NGVLIGAVTLNQGREIRPIRKWIQSGK 383
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 19-295 9.87e-52

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: 175.20  E-value: 9.87e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  19 KTLRDEGfsGEICVVAEEQWDFYERPPLSKAALLEAEPALPRLFSAEAQQ---------ALNLRWYRPLRADSIDRQNKT 89
Cdd:pfam07992  17 LTLAQLG--GKVTLIEDEGTCPYGGCVLSKALLGAAEAPEIASLWADLYKrkeevvkklNNGIEVLLGTEVVSIDPGAKK 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  90 VALS-----NGETLAYDQLLIATGGRARLPS-EGwAQHPQVYTLRHWQDAQRLKQRLASAtRLAIVGGGWIGLEIAASAR 163
Cdd:pfam07992  95 VVLEelvdgDGETITYDRLVIATGARPRLPPiPG-VELNVGFLVRTLDSAEALRLKLLPK-RVVVVGGGYIGVELAAALA 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 164 KSDVAVTLYEQQPALcMRSVSMEVSQALAQLHRQQGVEIRGGCGALELEDDNGLPTLHC-DGQRETFDAVVVGIGVDLNL 242
Cdd:pfam07992 173 KLGKEVTLIEALDRL-LRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVILkDGTEIDADLVVVAIGRRPNT 251

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039431258 243 ELARDAGLTVDR--GIVVNAQGRSNDPAIFAAGDVAQHHqyglcIQSWAFAQNQA 295
Cdd:pfam07992 252 ELLEAAGLELDErgGIVVDEYLRTSVPGIYAAGDCRVGG-----PELAQNAVAQG 301
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
 29-347 7.48e-30

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


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 121.86  E-value: 7.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  29 EICVVAEEQWDFYERPPLSKAALLEAEPALPRLFSAEAQQALNLRWYRPLRADSIDRQNKTVALSNGETLAYDQLLIATG 108
Cdd:TIGR02374  26 EITIFGEEPHPNYNRILLSSVLQGEADLDDITLNSKDWYEKHGITLYTGETVIQIDTDQKQVITDAGRTLSYDKLILATG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 109 GRARLPSEGWAQHPQVYTLRHWQDAQRLKQRLASATRLAIVGGGWIGLEIAASARKSDVAVTLYEQQPALCMRSVSMEVS 188
Cdd:TIGR02374 106 SYPFILPIPGADKKGVYVFRTIEDLDAIMAMAQRFKKAAVIGGGLLGLEAAVGLQNLGMDVSVIHHAPGLMAKQLDQTAG 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 189 QALAQLHRQQGVEIRGGCGALELEDDNGLPTLH-CDGQRETFDAVVVGIGVDLNLELARDAGLTVDRGIVVNAQGRSNDP 267
Cdd:TIGR02374 186 RLLQRELEQKGLTFLLEKDTVEIVGATKADRIRfKDGSSLEADLIVMAAGIRPNDELAVSAGIKVNRGIIVNDSMQTSDP 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 268 AIFAAGDVAQHHQ--YGLCiqswAFAQNQAIATAKAMLDPQASGYDEApwlwsdQYDRNIQILGIPQAGSRTIVRDEPQG 345
Cdd:TIGR02374 266 DIYAVGECAEHNGrvYGLV----APLYEQAKVLADHICGVECEEYEGS------DLSAKLKLLGVDVWSAGDAQETERTT 335


                  ..
gi 1039431258 346 AI 347
Cdd:TIGR02374 336 SI 337
 
Name Accession Description Interval E-value
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
19-398 1.33e-109

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 327.48  E-value: 1.33e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  19 KTLRDEGFSGEICVVAEEQWDFYERPPLSKAALLEAEPALPRLFSAEAQQALNLRWYRPLRADSIDRQNKTVALSNGETL 98
Cdd:COG1251    18 EELRKLDPDGEITVIGAEPHPPYNRPPLSKVLAGETDEEDLLLRPADFYEENGIDLRLGTRVTAIDRAARTVTLADGETL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  99 AYDQLLIATGGRARLPSEGWAQHPQVYTLRHWQDAQRLKQRLASATRLAIVGGGWIGLEIAASARKSDVAVTLYEQQPAL 178
Cdd:COG1251    98 PYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRAALAPGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRL 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 179 CMRSVSMEVSQALAQLHRQQGVEIRGGCGALELEDDNGLPTLHC-DGQRETFDAVVVGIGVDLNLELARDAGLTVDRGIV 257
Cdd:COG1251   178 LPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRLaDGEELPADLVVVAIGVRPNTELARAAGLAVDRGIV 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 258 VNAQGRSNDPAIFAAGDVAQHHQ--YG-LCIQSWAFAQNQAIATAKAMLDPQASGYDEAPWLWSDQYDRNIQILGIPQAG 334
Cdd:COG1251   258 VDDYLRTSDPDIYAAGDCAEHPGpvYGrRVLELVAPAYEQARVAAANLAGGPAAYEGSVPSTKLKVFGVDVASAGDAEGD 337

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039431258 335 SRTIVRDEPQGAIYFSLN-ADGRLTQLVAFNNARIVKLAKRWMAAGRDLSNVPLADPTFSLMSLR 398
Cdd:COG1251   338 EEVVVRGDPARGVYKKLVlRDGRLVGAVLVGDTSDAGALRQLIKNGRPLPPRALLDAALPLKELK 402
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 24-329 1.23e-78

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: 245.11  E-value: 1.23e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  24 EGFSGEICVVAEEQWDFYERPPLSKAALLE-AEPALPRLFSAEAQQALNLRWYRPLRADSIDRQNKTVALSNGETLAYDQ 102
Cdd:COG0446     2 LGPDAEITVIEKGPHHSYQPCGLPYYVGGGiKDPEDLLVRTPESFERKGIDVRTGTEVTAIDPEAKTVTLRDGETLSYDK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 103 LLIATGGRARLPS-EGWaQHPQVYTLRHWQDAQRLKQRLAS--ATRLAIVGGGWIGLEIAASARKSDVAVTLYEQQPALc 179
Cdd:COG0446    82 LVLATGARPRPPPiPGL-DLPGVFTLRTLDDADALREALKEfkGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRL- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 180 MRSVSMEVSQALAQLHRQQGVEIRGGCGALELEDDNGLpTLHC-DGQRETFDAVVVGIGVDLNLELARDAGLTVDR--GI 256
Cdd:COG0446   160 LGVLDPEMAALLEEELREHGVELRLGETVVAIDGDDKV-AVTLtDGEEIPADLVVVAPGVRPNTELAKDAGLALGErgWI 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039431258 257 VVNAQGRSNDPAIFAAGDVAQHHQYGLC----IQSWAFAQNQAIATAKAMLDpQASGYDEAPWLWSDQYDRNIQILG 329
Cdd:COG0446   239 KVDETLQTSDPDVYAAGDCAEVPHPVTGktvyIPLASAANKQGRVAAENILG-GPAPFPGLGTFISKVFDLCIASTG 314
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
 5-380 2.83e-69

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 223.65  E-value: 2.83e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258   5 IVIIGGGQAGGWAAKTLRDEGFSGEICVVAEEQWDFYERPPLSKAALLEAEPALPRLFSAEAQQALNLRWYRPLRADSID 84
Cdd:PRK09754    6 IIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPQLQQVLPANWWQENNVHLHSGVTIKTLG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  85 RQNKTVALSNGETLAYDQLLIATGGRARLPSEGWAQHPQVYTLRHWQDAQRLKQRLASATRLAIVGGGWIGLEIAASARK 164
Cdd:PRK09754   86 RDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELAASATQ 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 165 SDVAVTLYEQQPALCMRSVSMEVSQALAQLHRQQGVEIRGGCGALELEDDNGLPTLHCDGQRETFDAVVVGIGVDLNLEL 244
Cdd:PRK09754  166 RRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVELTLQSGETLQADVVIYGIGISANDQL 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 245 ARDAGLTVDRGIVVNAQGRSNDPAIFAAGDVAQHHQYGLCIQ---SWAFAQNQAIATAKAMLD---PQASgydeAPWLWS 318
Cdd:PRK09754  246 AREANLDTANGIVIDEACRTCDPAIFAGGDVAITRLDNGALHrceSWENANNQAQIAAAAMLGlplPLLP----PPWFWS 321

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039431258 319 DQYDRNIQILGIPQAGSRTIVRD-EPQGAIYFSLNaDGRLTQLVAFNNARIVKLAKRWMAAGR 380
Cdd:PRK09754  322 DQYSDNLQFIGDMRGDDWLCRGNpETQKAIWFNLQ-NGVLIGAVTLNQGREIRPIRKWIQSGK 383
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 19-295 9.87e-52

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: 175.20  E-value: 9.87e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  19 KTLRDEGfsGEICVVAEEQWDFYERPPLSKAALLEAEPALPRLFSAEAQQ---------ALNLRWYRPLRADSIDRQNKT 89
Cdd:pfam07992  17 LTLAQLG--GKVTLIEDEGTCPYGGCVLSKALLGAAEAPEIASLWADLYKrkeevvkklNNGIEVLLGTEVVSIDPGAKK 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  90 VALS-----NGETLAYDQLLIATGGRARLPS-EGwAQHPQVYTLRHWQDAQRLKQRLASAtRLAIVGGGWIGLEIAASAR 163
Cdd:pfam07992  95 VVLEelvdgDGETITYDRLVIATGARPRLPPiPG-VELNVGFLVRTLDSAEALRLKLLPK-RVVVVGGGYIGVELAAALA 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 164 KSDVAVTLYEQQPALcMRSVSMEVSQALAQLHRQQGVEIRGGCGALELEDDNGLPTLHC-DGQRETFDAVVVGIGVDLNL 242
Cdd:pfam07992 173 KLGKEVTLIEALDRL-LRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVILkDGTEIDADLVVVAIGRRPNT 251

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039431258 243 ELARDAGLTVDR--GIVVNAQGRSNDPAIFAAGDVAQHHqyglcIQSWAFAQNQA 295
Cdd:pfam07992 252 ELLEAAGLELDErgGIVVDEYLRTSVPGIYAAGDCRVGG-----PELAQNAVAQG 301
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
1-277 5.54e-35

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 132.73  E-value: 5.54e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258   1 MTARIVIIGGGQAGGWAAKTLRDEGFSGEICVVAEEQWDFYERPPLSKAALLEAEPA-LPRLFSAEAQQALNLRWYRPLR 79
Cdd:PRK04965    1 MSNGIVIIGSGFAARQLVKNIRKQDAHIPITLITADSGDEYNKPDLSHVFSQGQRADdLTRQSAGEFAEQFNLRLFPHTW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  80 ADSIDRQNKTVaLSNGETLAYDQLLIATGGRARLPS-EGwaqHPQVYTLRHWQDAQRLKQRLASATRLAIVGGGWIGLEI 158
Cdd:PRK04965   81 VTDIDAEAQVV-KSQGNQWQYDKLVLATGASAFVPPiPG---RELMLTLNSQQEYRAAETQLRDAQRVLVVGGGLIGTEL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 159 A---ASARKsdvAVTLYEQQPALCMRSVSMEVSQALAQLHRQQGVEIRGGCG--ALELEDDNGLPTLHcDGQRETFDAVV 233
Cdd:PRK04965  157 AmdlCRAGK---AVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQlqGLEKTDSGIRATLD-SGRSIEVDAVI 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1039431258 234 VGIGVDLNLELARDAGLTVDRGIVVNAQGRSNDPAIFAAGDVAQ 277
Cdd:PRK04965  233 AAAGLRPNTALARRAGLAVNRGIVVDSYLQTSAPDIYALGDCAE 276
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 82-276 7.19e-30

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 119.76  E-value: 7.19e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  82 SIDRQNKTVALSNGET-----LAYDQLLIATGGRARLPSEGWAQHPQVYTLRHWQDAQRLKQRL--ASATRLAIVGGGWI 154
Cdd:PRK09564   81 KVDAKNKTITVKNLKTgsifnDTYDKLMIATGARPIIPPIKNINLENVYTLKSMEDGLALKELLkdEEIKNIVIIGAGFI 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 155 GLEIAASARKSDVAVTLYEQQPALCMRSVSMEVSQALAQLHRQQGVEIRGGCGALELEDDNGLPTLHCDGQRETFDAVVV 234
Cdd:PRK09564  161 GLEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEGVVTDKGEYEADVVIV 240

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1039431258 235 GIGVDLNLELARDAGL-TVDRG-IVVNAQGRSNDPAIFAAGDVA 276
Cdd:PRK09564  241 ATGVKPNTEFLEDTGLkTLKNGaIIVDEYGETSIENIYAAGDCA 284
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
 29-347 7.48e-30

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


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 121.86  E-value: 7.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  29 EICVVAEEQWDFYERPPLSKAALLEAEPALPRLFSAEAQQALNLRWYRPLRADSIDRQNKTVALSNGETLAYDQLLIATG 108
Cdd:TIGR02374  26 EITIFGEEPHPNYNRILLSSVLQGEADLDDITLNSKDWYEKHGITLYTGETVIQIDTDQKQVITDAGRTLSYDKLILATG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 109 GRARLPSEGWAQHPQVYTLRHWQDAQRLKQRLASATRLAIVGGGWIGLEIAASARKSDVAVTLYEQQPALCMRSVSMEVS 188
Cdd:TIGR02374 106 SYPFILPIPGADKKGVYVFRTIEDLDAIMAMAQRFKKAAVIGGGLLGLEAAVGLQNLGMDVSVIHHAPGLMAKQLDQTAG 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 189 QALAQLHRQQGVEIRGGCGALELEDDNGLPTLH-CDGQRETFDAVVVGIGVDLNLELARDAGLTVDRGIVVNAQGRSNDP 267
Cdd:TIGR02374 186 RLLQRELEQKGLTFLLEKDTVEIVGATKADRIRfKDGSSLEADLIVMAAGIRPNDELAVSAGIKVNRGIIVNDSMQTSDP 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 268 AIFAAGDVAQHHQ--YGLCiqswAFAQNQAIATAKAMLDPQASGYDEApwlwsdQYDRNIQILGIPQAGSRTIVRDEPQG 345
Cdd:TIGR02374 266 DIYAVGECAEHNGrvYGLV----APLYEQAKVLADHICGVECEEYEGS------DLSAKLKLLGVDVWSAGDAQETERTT 335


                  ..
gi 1039431258 346 AI 347
Cdd:TIGR02374 336 SI 337
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
79-276 2.21e-28

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 114.46  E-value: 2.21e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  79 RADSIDRQNKTVALSNGETLAYDQLLIATGGRARLPS-EGWAQHpqVYTLRHWQDAQRLKQRLASA---------TRLAI 148
Cdd:COG1252    77 EVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGiPGLAEH--ALPLKTLEDALALRERLLAAferaerrrlLTIVV 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 149 VGGGWIGLEIAASA-------------RKSDVAVTLYEQQPALcMRSVSMEVSQALAQLHRQQGVEIRGGCGALELEDDn 215
Cdd:COG1252   155 VGGGPTGVELAGELaellrkllrypgiDPDKVRITLVEAGPRI-LPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDAD- 232

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039431258 216 glpTLHC-DGQRETFDAVVVGIGVDLNlELARDAGLTVDRG--IVVNAQGRS-NDPAIFAAGDVA 276
Cdd:COG1252   233 ---GVTLeDGEEIPADTVIWAAGVKAP-PLLADLGLPTDRRgrVLVDPTLQVpGHPNVFAIGDCA 293
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 87-276 6.99e-28

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: 114.03  E-value: 6.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  87 NKTVALSNGETLAYDQLLIATGGRAR-LPSEGwAQHPQVYTlrhWQDAQRLKQRLAsatRLAIVGGGWIGLEIAASARKS 165
Cdd:COG1249   118 PHTVEVTGGETLTADHIVIATGSRPRvPPIPG-LDEVRVLT---SDEALELEELPK---SLVVIGGGYIGLEFAQIFARL 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 166 DVAVTLYEQQPALcMRSVSMEVSQALAQLHRQQGVEIRGGCGALELEDDNGLPTLHCDGQRE----TFDAVVVGIGV--- 238
Cdd:COG1249   191 GSEVTLVERGDRL-LPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDGVTVTLEDGGGeeavEADKVLVATGRrpn 269

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1039431258 239 --DLNLElarDAGLTVDR--GIVVNAQGRSNDPAIFAAGDVA 276
Cdd:COG1249   270 tdGLGLE---AAGVELDErgGIKVDEYLRTSVPGIYAIGDVT 308
PRK06370 PRK06370
FAD-containing oxidoreductase;
94-304 7.78e-22

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 96.81  E-value: 7.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  94 NGETLAYDQLLIATGGRARLPS-EGWAQHPqvYtlrhwqdaqrlkqrLASAT---------RLAIVGGGWIGLEIAASAR 163
Cdd:PRK06370  128 GGETLRAKRIFINTGARAAIPPiPGLDEVG--Y--------------LTNETifsldelpeHLVIIGGGYIGLEFAQMFR 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 164 KSDVAVTLYEQQPALCMRSvSMEVSQALAQLHRQQGVEIRGGCGALELEDDNGLPTLH--CDGQRE--TFDAVVVGIGV- 238
Cdd:PRK06370  192 RFGSEVTVIERGPRLLPRE-DEDVAAAVREILEREGIDVRLNAECIRVERDGDGIAVGldCNGGAPeiTGSHILVAVGRv 270

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039431258 239 ----DLNLElarDAGLTVDR--GIVVNAQGRSNDPAIFAAGDvaqhhqyglCIQSWAF---AQNQAIATAKAMLD 304
Cdd:PRK06370  271 pntdDLGLE---AAGVETDArgYIKVDDQLRTTNPGIYAAGD---------CNGRGAFthtAYNDARIVAANLLD 333
PRK14989 PRK14989
nitrite reductase subunit NirD; Provisional
 79-292 2.06e-17

nitrite reductase subunit NirD; Provisional


Pssm-ID: 184951 [Multi-domain]  Cd Length: 847  Bit Score: 84.40  E-value: 2.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  79 RADSIDRQNKTVALSNGETLAYDQLLIATGGRARLPSEGWAQHPQVYTLRHWQDAQRLKQRLASATRLAIVGGGWIGLEI 158
Cdd:PRK14989   81 RAITINRQEKVIHSSAGRTVFYDKLIMATGSYPWIPPIKGSETQDCFVYRTIEDLNAIEACARRSKRGAVVGGGLLGLEA 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 159 AASARKSDVAVTLYEQQPALCMRSVSMEVSQALAQLHRQQGVEIRGGCGALEL--EDDNGLPTLH-CDGQRETFDAVVVG 235
Cdd:PRK14989  161 AGALKNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSKNTLEIvqEGVEARKTMRfADGSELEVDFIVFS 240

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039431258 236 IGVDLNLELARDAGLTVDR--GIVVNAQGRSNDPAIFAAGDVAQHHQ--YGLCIQSWAFAQ 292
Cdd:PRK14989  241 TGIRPQDKLATQCGLAVAPrgGIVINDSCQTSDPDIYAIGECASWNNrvFGLVAPGYKMAQ 301
Reductase_C pfam14759
Reductase C-terminal; This domain occurs at the C-terminus of various reductase enzymes, ...
 315-396 2.43e-17

Reductase C-terminal; This domain occurs at the C-terminus of various reductase enzymes, including putidaredoxin reductase, ferredoxin reductase, 3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase component, benzene 1,2-dioxygenase system ferredoxin--NAD(+) reductase subunit, rhodocoxin reductase, biphenyl dioxygenase system ferredoxin--NAD(+) reductase component, rubredoxin-NAD(+) reductase and toluene 1,2-dioxygenase system ferredoxin--NAD(+) reductase component. In putidaredoxin reductase this domain is involved in dimerization. In the FAD-containing NADH-ferredoxin reductase (BphA4) it is responsible for interaction with the Rieske-type [2Fe-2S] ferredoxin (BphA3).


Pssm-ID: 434185 [Multi-domain]  Cd Length: 83  Bit Score: 76.06  E-value: 2.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 315 WLWSDQYDRNIQILGIPQAGSRTIVRDEPQG----AIYFslnADGRLTQLVAFNNARIVKLAKRWMAAGRDLSNVPLADP 390
Cdd:pfam14759   1 WFWSDQYDLKLQIAGLPTGADEVVLRGDPEDgafsVFYL---RDGRLVAVDAVNRPRDFMAARRLIARGASVDPAALADP 77


                  ....*.
gi 1039431258 391 TFSLMS 396
Cdd:pfam14759  78 AVDLKA 83
PRK07251 PRK07251
FAD-containing oxidoreductase;
87-275 4.11e-16

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 79.41  E-value: 4.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  87 NKTVALSNGE---TLAYDQLLIATGGRA-RLPSEGWAQHPQVYtlrhwqDAQRLKQRLASATRLAIVGGGWIGLEIAASA 162
Cdd:PRK07251  103 NKVIEVQAGDekiELTAETIVINTGAVSnVLPIPGLADSKHVY------DSTGIQSLETLPERLGIIGGGNIGLEFAGLY 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 163 RKSDVAVTLYEQQPALCMRsVSMEVSQALAQLHRQQGVEIRGGCGALELEDDNGLPTLHCDGQRETFDAVVVGIG----- 237
Cdd:PRK07251  177 NKLGSKVTVLDAASTILPR-EEPSVAALAKQYMEEDGITFLLNAHTTEVKNDGDQVLVVTEDETYRFDALLYATGrkpnt 255

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1039431258 238 VDLNLElARDAGLTvDRG-IVVNAQGRSNDPAIFAAGDV 275
Cdd:PRK07251  256 EPLGLE-NTDIELT-ERGaIKVDDYCQTSVPGVFAVGDV 292
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
 82-279 3.58e-15

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 76.75  E-value: 3.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  82 SIDRQNKTVALSNGET-----LAYDQLLIATGGRA-RLPSEgwaqHPQVYTLRHWQDAQRLKQRLAS--ATRLAIVGGGW 153
Cdd:PRK13512   83 AINDERQTVTVLNRKTneqfeESYDKLILSPGASAnSLGFE----SDITFTLRNLEDTDAIDQFIKAnqVDKALVVGAGY 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 154 IGLEIAASARKSDVAVTLYEQQPALcMRSVSMEVSQALAQLHRQQGVEIRGGcgaLELEDDNGLPTLHCDGQRETFDAVV 233
Cdd:PRK13512  159 ISLEVLENLYERGLHPTLIHRSDKI-NKLMDADMNQPILDELDKREIPYRLN---EEIDAINGNEVTFKSGKVEHYDMII 234

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1039431258 234 VGIGVDLNLELARDAGLTVDRG--IVVNAQGRSNDPAIFAAGDVAQHH 279
Cdd:PRK13512  235 EGVGTHPNSKFIESSNIKLDDKgfIPVNDKFETNVPNIYAIGDIITSH 282
PRK06116 PRK06116
glutathione reductase; Validated
 79-275 3.61e-15

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 76.73  E-value: 3.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  79 RADSIDrqNKTVALsNGETLAYDQLLIATGGRARLP----------SEG---WAQHPQvytlrhwqdaqrlkqrlasatR 145
Cdd:PRK06116  114 FARFVD--AHTVEV-NGERYTADHILIATGGRPSIPdipgaeygitSDGffaLEELPK---------------------R 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 146 LAIVGGGWIGLEIAASARKSDVAVTLYEQQPALcMRSVSMEVSQALAQLHRQQGVEIRGGC--GALELEDDNGLpTLHC- 222
Cdd:PRK06116  170 VAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAP-LRGFDPDIRETLVEEMEKKGIRLHTNAvpKAVEKNADGSL-TLTLe 247

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 223 DGQRETFDAVVVGIG-----VDLNLElarDAGLTVD-RG-IVVNAQGRSNDPAIFAAGDV 275
Cdd:PRK06116  248 DGETLTVDCLIWAIGrepntDGLGLE---NAGVKLNeKGyIIVDEYQNTNVPGIYAVGDV 304
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
79-279 4.39e-15

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 75.16  E-value: 4.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  79 RADSIDRQN--KTVALSNGETLAYDQLLIATGGRAR-LPSEGWAQhpqvYTLR--HW---QDAQRLKQRlasatRLAIVG 150
Cdd:COG0492    78 EVTSVDKDDgpFRVTTDDGTEYEAKAVIIATGAGPRkLGLPGEEE----FEGRgvSYcatCDGFFFRGK-----DVVVVG 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 151 GGWIGLEIAAS----ARKsdvaVTLYeqqpalcMRSVSMEVSQALAQ-LHRQQGVEIRGGCGALELEDDNGLPTLHC--- 222
Cdd:COG0492   149 GGDSALEEALYltkfASK----VTLI-------HRRDELRASKILVErLRANPKIEVLWNTEVTEIEGDGRVEGVTLknv 217

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039431258 223 -DGQRETF--DAVVVGIGVDLNLELARDAGLTVDRG--IVVNAQGRSNDPAIFAAGDVAQHH 279
Cdd:COG0492   218 kTGEEKELevDGVFVAIGLKPNTELLKGLGLELDEDgyIVVDEDMETSVPGVFAAGDVRDYK 279
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 95-276 7.26e-15

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 75.95  E-value: 7.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  95 GETLAYDQLLIATGGRAR-LPS-EgwAQHPQVYTLRHwqdAQRLKqRLASatRLAIVGGGWIGLEIAASARKSDVAVTLY 172
Cdd:PRK06416  130 EQTYTAKNIILATGSRPReLPGiE--IDGRVIWTSDE---ALNLD-EVPK--SLVVIGGGYIGVEFASAYASLGAEVTIV 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 173 EQQPALcMRSVSMEVSQALAQLHRQQGVEIRGGCGALELE-DDNGLpTLHC--DGQRETF--DAVVVGIGV-----DLNL 242
Cdd:PRK06416  202 EALPRI-LPGEDKEISKLAERALKKRGIKIKTGAKAKKVEqTDDGV-TVTLedGGKEETLeaDYVLVAVGRrpnteNLGL 279

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1039431258 243 ElarDAGLTVDRG-IVVNAQGRSNDPAIFAAGDVA 276
Cdd:PRK06416  280 E---ELGVKTDRGfIEVDEQLRTNVPNIYAIGDIV 311
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
96-275 1.10e-14

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


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 75.19  E-value: 1.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  96 ETLAYDQLLIATGGRARLPSEGWAQHPQVY------TLRHwqdaqrlkqrlaSATRLAIVGGGWIGLEIAASARKSDVAV 169
Cdd:PRK05249  134 ETLTADKIVIATGSRPYRPPDVDFDHPRIYdsdsilSLDH------------LPRSLIIYGAGVIGCEYASIFAALGVKV 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 170 TLYEQQPALcMRSVSMEVSQALAQLHRQQGVEIRGGCGALELEDDNGLPTLHC-DGQRETFDAVVVGIG----VD-LNLE 243
Cdd:PRK05249  202 TLINTRDRL-LSFLDDEISDALSYHLRDSGVTIRHNEEVEKVEGGDDGVIVHLkSGKKIKADCLLYANGrtgnTDgLNLE 280

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1039431258 244 larDAGLTVD-RG-IVVNAQGRSNDPAIFAAGDV 275
Cdd:PRK05249  281 ---NAGLEADsRGqLKVNENYQTAVPHIYAVGDV 311
PRK07846 PRK07846
mycothione reductase; Reviewed
 75-280 1.89e-14

mycothione reductase; Reviewed


Pssm-ID: 181142 [Multi-domain]  Cd Length: 451  Bit Score: 74.61  E-value: 1.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  75 YRPLRADSID--RQN------KTVALSNGETLAYDQLLIATGGRARLPSEGWAQHPQVYTLrhwQDAQRLKQRlasATRL 146
Cdd:PRK07846   96 YRGRDTPNIDvyRGHarfigpKTLRTGDGEEITADQVVIAAGSRPVIPPVIADSGVRYHTS---DTIMRLPEL---PESL 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 147 AIVGGGWIGLEIAASARKSDVAVTLYEQQPALcMRSVSMEVSQALAQLHRQQgVEIRGGCGALELEDDNGLPTLHCD-GQ 225
Cdd:PRK07846  170 VIVGGGFIAAEFAHVFSALGVRVTVVNRSGRL-LRHLDDDISERFTELASKR-WDVRLGRNVVGVSQDGSGVTLRLDdGS 247

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039431258 226 RETFDAVVVGIGVDLNLEL--ARDAGLTVDRG--IVVNAQGRSNDPAIFAAGDVAQHHQ 280
Cdd:PRK07846  248 TVEADVLLVATGRVPNGDLldAAAAGVDVDEDgrVVVDEYQRTSAEGVFALGDVSSPYQ 306
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
 90-276 1.95e-12

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 68.41  E-value: 1.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  90 VALSNGETLAYDQLLIATGGRAR-LP-----------SEGwaqhpqvytlrhwqdAQRLKqrlASATRLAIVGGGWIGLE 157
Cdd:PRK06327  136 VTGEDETVITAKHVIIATGSEPRhLPgvpfdnkiildNTG---------------ALNFT---EVPKKLAVIGAGVIGLE 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 158 IAASARKSDVAVTLYEQQPALCMrSVSMEVSQALAQLHRQQGVEIRGGCGALELED-DNGLPTLHCDG----QRETFDAV 232
Cdd:PRK06327  198 LGSVWRRLGAEVTILEALPAFLA-AADEQVAKEAAKAFTKQGLDIHLGVKIGEIKTgGKGVSVAYTDAdgeaQTLEVDKL 276

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039431258 233 VVGIG-----VDLNLElarDAGLTVD-RG-IVVNAQGRSNDPAIFAAGDVA 276
Cdd:PRK06327  277 IVSIGrvpntDGLGLE---AVGLKLDeRGfIPVDDHCRTNVPNVYAIGDVV 324
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 87-275 2.99e-12

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 67.90  E-value: 2.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  87 NKTVALsNGETLAYDQLLIATGGR-ARLPSEGWAQHPQVYTLRhwqDAQRLkQRLASatRLAIVGGGWIGLEIAASARKS 165
Cdd:PRK06292  119 PNTVEV-NGERIEAKNIVIATGSRvPPIPGVWLILGDRLLTSD---DAFEL-DKLPK--SLAVIGGGVIGLELGQALSRL 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 166 DVAVTLYEQQPALCMRSvSMEVSQALAQLHRQQgVEIRGGCGALELEDDNGLP----TLHCDGQRETFDAVVVGIG---- 237
Cdd:PRK06292  192 GVKVTVFERGDRILPLE-DPEVSKQAQKILSKE-FKIKLGAKVTSVEKSGDEKveelEKGGKTETIEADYVLVATGrrpn 269

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1039431258 238 VD-LNLElarDAGLTVD-RG-IVVNAQGRSNDPAIFAAGDV 275
Cdd:PRK06292  270 TDgLGLE---NTGIELDeRGrPVVDEHTQTSVPGIYAAGDV 307
PRK08010 PRK08010
pyridine nucleotide-disulfide oxidoreductase; Provisional
 79-281 1.09e-09

pyridine nucleotide-disulfide oxidoreductase; Provisional


Pssm-ID: 181196 [Multi-domain]  Cd Length: 441  Bit Score: 59.64  E-value: 1.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  79 RADSIDRQNKTVALSNGE-TLAYDQLLIATGGRARLPS-EGWAQHPQVYtlrhwqDAQRLKQRLASATRLAIVGGGWIGL 156
Cdd:PRK08010   98 QAEFINNHSLRVHRPEGNlEIHGEKIFINTGAQTVVPPiPGITTTPGVY------DSTGLLNLKELPGHLGILGGGYIGV 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 157 EIAASARKSDVAVTLYEQQPALCMRSvSMEVSQALAQLHRQQGVEIRGGCGALELEDDNGLPTLHCDGQRETFDAVVVGI 236
Cdd:PRK08010  172 EFASMFANFGSKVTILEAASLFLPRE-DRDIADNIATILRDQGVDIILNAHVERISHHENQVQVHSEHAQLAVDALLIAS 250

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039431258 237 G-----VDLNLElarDAGLTVDR--GIVVNAQGRSNDPAIFAAGDVAQHHQY 281
Cdd:PRK08010  251 GrqpatASLHPE---NAGIAVNErgAIVVDKYLHTTADNIWAMGDVTGGLQF 299
PRK13748 PRK13748
putative mercuric reductase; Provisional
 84-281 2.11e-09

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 59.01  E-value: 2.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  84 DRQNKTVALSNG--ETLAYDQLLIATGGRARLPS-EGWAQHPqvytlrHWQDAQRLkqrlASAT---RLAIVGGGWIGLE 157
Cdd:PRK13748  215 DDQTLIVRLNDGgeRVVAFDRCLIATGASPAVPPiPGLKETP------YWTSTEAL----VSDTipeRLAVIGSSVVALE 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 158 IA-ASAR-KSDVAVT-----LYEQQPALcmrsvsmevSQALAQLHRQQGVEIRGGCGALELEDDNGLPTLHCDGQRETFD 230
Cdd:PRK13748  285 LAqAFARlGSKVTILarstlFFREDPAI---------GEAVTAAFRAEGIEVLEHTQASQVAHVDGEFVLTTGHGELRAD 355

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039431258 231 AVVVGIG-----VDLNLElarDAGLTVDRG--IVVNAQGRSNDPAIFAAGDVAQHHQY 281
Cdd:PRK13748  356 KLLVATGrapntRSLALD---AAGVTVNAQgaIVIDQGMRTSVPHIYAAGDCTDQPQF 410
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 145-216 5.50e-09

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: 52.59  E-value: 5.50e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039431258 145 RLAIVGGGWIGLEIAASARKSDVAVTLYEQQPALcMRSVSMEVSQALAQLHRQQGVEIRGGCGALELEDDNG 216
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRL-LPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGD 71
PLN02507 PLN02507
glutathione reductase
 90-275 1.02e-07

glutathione reductase


Pssm-ID: 215281 [Multi-domain]  Cd Length: 499  Bit Score: 53.67  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  90 VALSNGETLAY--DQLLIATGGRARLPSegWAQHPQVYTLRHWQDAQRLKQRLAsatrlaIVGGGWIGLEIAASARKSDV 167
Cdd:PLN02507  156 VTQLDGTKLRYtaKHILIATGSRAQRPN--IPGKELAITSDEALSLEELPKRAV------VLGGGYIAVEFASIWRGMGA 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 168 AVTLYEQQPaLCMRSVSMEVSQALAQLHRQQGVEIRGGCGALELED-DNGLPTLHCDGQRETFDAVVVGIG-----VDLN 241
Cdd:PLN02507  228 TVDLFFRKE-LPLRGFDDEMRAVVARNLEGRGINLHPRTNLTQLTKtEGGIKVITDHGEEFVADVVLFATGrapntKRLN 306

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1039431258 242 LElarDAGLTVDR--GIVVNAQGRSNDPAIFAAGDV 275
Cdd:PLN02507  307 LE---AVGVELDKagAVKVDEYSRTNIPSIWAIGDV 339
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
 96-275 4.49e-07

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: 51.90  E-value: 4.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  96 ETLAYDQLLIATGGrarlpsegWAQHPQVYTLRHWQDAQRLKQRLASATRLAIVGGGWIGLEIAA---SARKSDVAVTL- 171
Cdd:TIGR01423 148 ERLQAEHILLATGS--------WPQMLGIPGIEHCISSNEAFYLDEPPRRVLTVGGGFISVEFAGifnAYKPRGGKVTLc 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 172 YEQQPALcmRSVSMEVSQALAQLHRQQGVEIRG--GCGALELEDDNGLPTLHCDGQRETFDAVVVGIGV-----DLNLEL 244
Cdd:TIGR01423 220 YRNNMIL--RGFDSTLRKELTKQLRANGINIMTneNPAKVTLNADGSKHVTFESGKTLDVDVVMMAIGRvprtqTLQLDK 297

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1039431258 245 ArDAGLTVDRGIVVNAQGRSNDPAIFAAGDV 275
Cdd:TIGR01423 298 V-GVELTKKGAIQVDEFSRTNVPNIYAIGDV 327
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 95-276 3.16e-06

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: 48.98  E-value: 3.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  95 GETLAYDQLL-------IATG-GRAR-LPSEGwAQHPQVYT----LRHWQDAQRLKQRLASATRLAIVGGGWIGLEIAAS 161
Cdd:COG0493   195 GKDITLDELLeefdavfLATGaGKPRdLGIPG-EDLKGVHSamdfLTAVNLGEAPDTILAVGKRVVVIGGGNTAMDCART 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 162 ARKSDVA-VTLYEQQPALCMRSVSMEVSQALAQlhrqqGVEIRGGCGALELE-DDNG-LPTLHC----------DGQR-- 226
Cdd:COG0493   274 ALRLGAEsVTIVYRRTREEMPASKEEVEEALEE-----GVEFLFLVAPVEIIgDENGrVTGLECvrmelgepdeSGRRrp 348

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039431258 227 -----ETF----DAVVVGIGVDLNLE-LARDAGLTVDRG--IVVNAQ-GRSNDPAIFAAGDVA 276
Cdd:COG0493   349 vpiegSEFtlpaDLVILAIGQTPDPSgLEEELGLELDKRgtIVVDEEtYQTSLPGVFAGGDAV 411
PLN02546 PLN02546
glutathione reductase
 94-275 4.28e-06

glutathione reductase


Pssm-ID: 215301 [Multi-domain]  Cd Length: 558  Bit Score: 48.72  E-value: 4.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  94 NGETLAYDQLLIATGGRarlPSEgwaqhPQVYTLRHWQDAQRLKQRLASATRLAIVGGGWIGLEIAA--SARKSDVAVTL 171
Cdd:PLN02546  211 DGKLYTARNILIAVGGR---PFI-----PDIPGIEHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGifNGLKSDVHVFI 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 172 YEQQpalCMRSVSMEVSQALAQLHRQQGVE----------IRGGCGALELEDDNGlpTLhcdgqrETFDAVVVGIG---- 237
Cdd:PLN02546  283 RQKK---VLRGFDEEVRDFVAEQMSLRGIEfhteespqaiIKSADGSLSLKTNKG--TV------EGFSHVMFATGrkpn 351

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1039431258 238 -VDLNLElarDAGLTVDR--GIVVNAQGRSNDPAIFAAGDV 275
Cdd:PLN02546  352 tKNLGLE---EVGVKMDKngAIEVDEYSRTSVPSIWAVGDV 389
PTZ00052 PTZ00052
thioredoxin reductase; Provisional
 68-276 1.00e-05

thioredoxin reductase; Provisional


Pssm-ID: 185416 [Multi-domain]  Cd Length: 499  Bit Score: 47.51  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  68 QALNLRWYRPLRADSIDRQNKTVALSNGETLAYDQL-----------LIATGGRARLPS--EGWAQhpqvYTLRHwQDAQ 134
Cdd:PTZ00052  102 RSLNFSYRTGLRSSKVEYINGLAKLKDEHTVSYGDNsqeetitakyiLIATGGRPSIPEdvPGAKE----YSITS-DDIF 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 135 RLKQrlaSATRLAIVGGGWIGLEIAA--SARKSDVAVTLYeqqpALCMRSVSMEVSQALAQLHRQQGVEIRGGCGALELE 212
Cdd:PTZ00052  177 SLSK---DPGKTLIVGASYIGLETAGflNELGFDVTVAVR----SIPLRGFDRQCSEKVVEYMKEQGTLFLEGVVPINIE 249

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039431258 213 D-DNGLPTLHCDGQRETFDAVVVGIGVDLNLelardAGLTVDR-GIVVNAQGR-------SNDPAIFAAGDVA 276
Cdd:PTZ00052  250 KmDDKIKVLFSDGTTELFDTVLYATGRKPDI-----KGLNLNAiGVHVNKSNKiiapndcTNIPNIFAVGDVV 317
PTZ00058 PTZ00058
glutathione reductase; Provisional
 91-274 5.52e-05

glutathione reductase; Provisional


Pssm-ID: 185420 [Multi-domain]  Cd Length: 561  Bit Score: 45.38  E-value: 5.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  91 ALSNGETLAYDQLLIATGGRArlpsegwaQHPQVYTLRHWQDAQRLKQrLASATRLAIVGGGWIGLEIAASARKSDVAVT 170
Cdd:PTZ00058  194 QLDDGQVIEGKNILIAVGNKP--------IFPDVKGKEFTISSDDFFK-IKEAKRIGIAGSGYIAVELINVVNRLGAESY 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 171 LYEQQPALcMRSVSMEVSQALAQLHRQQGVEIRGGCGALELEDD--NGLPTLHCDGQR-ETFDAVVVGIG-----VDLNL 242
Cdd:PTZ00058  265 IFARGNRL-LRKFDETIINELENDMKKNNINIITHANVEEIEKVkeKNLTIYLSDGRKyEHFDYVIYCVGrspntEDLNL 343

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1039431258 243 ELARDagLTVDRGIVVNAQGRSNDPAIFAAGD 274
Cdd:PTZ00058  344 KALNI--KTPKGYIKVDDNQRTSVKHIYAVGD 373
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
 145-314 1.83e-04

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 43.56  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 145 RLAIVGGGWIGLEIAASA-RKSDVAVT-LY----EQQPAlcmrsVSMEVSQALAQlhrqqGVE---------IRGGCGAL 209
Cdd:PRK12814  325 KVVVIGGGNTAIDAARTAlRLGAESVTiLYrrtrEEMPA-----NRAEIEEALAE-----GVSlrelaapvsIERSEGGL 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 210 ELE---------DDNG----LP------TLHCDgqretfdAVVVGIGVDLNLELARDAGLTVDR-GIVVNAQG--RSNDP 267
Cdd:PRK12814  395 ELTaikmqqgepDESGrrrpVPvegsefTLQAD-------TVISAIGQQVDPPIAEAAGIGTSRnGTVKVDPEtlQTSVA 467

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039431258 268 AIFAAGD-----------VAQHHQYGLCIQSwaFAQNQAIATAKAMLDPQASGYDEAP 314
Cdd:PRK12814  468 GVFAGGDcvtgadiainaVEQGKRAAHAIDL--FLNGKPVTAPVQPFNSSYGPRDKAP 523
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 209-277 2.33e-04

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 43.24  E-value: 2.33e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039431258 209 LELEDDNGLPTLHCDGQRETF--DAVVVGIGVDLN---LELARDAGLTVDRGIVVN-AQGRSNDPAIFAAGDVAQ 277
Cdd:PRK11749  354 LGEPDASGRRRVPIEGSEFTLpaDLVIKAIGQTPNpliLSTTPGLELNRWGTIIADdETGRTSLPGVFAGGDIVT 428
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 79-275 2.40e-03

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 39.76  E-value: 2.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258  79 RADSIDR--QNKTVALSNGETLAYDQLLIATGGRAR---LPSEgwaqhpqvytlrhwqdaQRLKQR-----------LAS 142
Cdd:PRK15317  288 RASKLEPaaGLIEVELANGAVLKAKTVILATGARWRnmnVPGE-----------------DEYRNKgvaycphcdgpLFK 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 143 ATRLAIVGGGWIGLEIAAsarksDVA-----VTLYEQQPALCMRSVSMEVSQALAQ---LHRQQGVEIRGGCG---ALEL 211
Cdd:PRK15317  351 GKRVAVIGGGNSGVEAAI-----DLAgivkhVTVLEFAPELKADQVLQDKLRSLPNvtiITNAQTTEVTGDGDkvtGLTY 425

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039431258 212 EDDNglptlhcDGQRETF--DAVVVGIGVDLNLELARDAGLTVDRG-IVVNAQGRSNDPAIFAAGDV 275
Cdd:PRK15317  426 KDRT-------TGEEHHLelEGVFVQIGLVPNTEWLKGTVELNRRGeIIVDARGATSVPGVFAAGDC 485
PRK13984 PRK13984
putative oxidoreductase; Provisional
 100-275 3.36e-03

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 39.75  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 100 YDQLLIATG---GRA-RLPSegwAQHPQVYT----LRHWQDAQRLK-QRLASATRLAIVGGGWIGLEIAAS-AR------ 163
Cdd:PRK13984  369 HDAVFLSTGftlGRStRIPG---TDHPDVIQalplLREIRDYLRGEgPKPKIPRSLVVIGGGNVAMDIARSmARlqkmey 445

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039431258 164 -KSDVAVT----LYEQQPAlcmrsvSM-EVSQALaqlhrQQGVEIRGGCGALELEDDN----GLPTLHC----DGQRE-- 227
Cdd:PRK13984  446 gEVNVKVTslerTFEEMPA------DMeEIEEGL-----EEGVVIYPGWGPMEVVIENdkvkGVKFKKCvevfDEEGRfn 514

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039431258 228 -TFDA----------VVVGIGVDLNLELARD---AGLTVDRG-IVVNAQGRSNDPAIFAAGDV 275
Cdd:PRK13984  515 pKFDEsdqiiveadmVVEAIGQAPDYSYLPEelkSKLEFVRGrILTNEYGQTSIPWLFAGGDI 577
PRK05732 PRK05732
2-octaprenyl-6-methoxyphenyl hydroxylase; Validated
 60-122 4.62e-03

2-octaprenyl-6-methoxyphenyl hydroxylase; Validated


Pssm-ID: 235584 [Multi-domain]  Cd Length: 395  Bit Score: 39.07  E-value: 4.62e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039431258  60 RLFSAeAQQALNLRWYRPLRADSIDR--QNKTVALSNGETLAYDQLLIATGGRARLPSE---GWAQHP 122
Cdd:PRK05732  117 RLFAL-LDKAPGVTLHCPARVANVERtqGSVRVTLDDGETLTGRLLVAADGSHSALREAlgiDWQQHP 183
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
148-184 6.80e-03

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 34.81  E-value: 6.80e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1039431258 148 IVGGGWIGLEIAASARKSDVAVTLYEQQPALCMRSVS 184
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAYS 37
 
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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