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Conserved domains on  [gi|1169125346|ref|WP_080467367|]
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NAD(P)/FAD-dependent oxidoreductase [Bacillus subtilis]

Protein Classification

NAD(P)/FAD-dependent oxidoreductase( domain architecture ID 12044987)

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:  1.14.13.-
Gene Ontology:  GO:0050660|GO:0050661
SCOP:  4000073

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HI0933_like pfam03486
HI0933-like protein;
4-413 0e+00

HI0933-like protein;


:

Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 591.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   4 YDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGNKLGRKLAISGGGRCNVTN-RLPVEEIIKHIPGNGRFLYSAFSEFNNE 82
Cdd:pfam03486   1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLGRKILISGGGRCNVTNlSEEPDNFLSRYPGNPKFLKSALSRFTPW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  83 DIIKFFENLGIQLKEEDHGRMFPVTDKAQSVVDALLNRLKQLRVTIRTNEKIKSVLYEDGQAAGIVTNNGEmIHSQSVII 162
Cdd:pfam03486  81 DFIAFFESLGVPLKEEDHGRLFPDSDKASDIVDALLNELKELGVKIRLRTRVLSVEKDDDGRFRVKTGGEE-LEADSLVL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 163 AVGGKSVPHTGSTGDGYEWAEAAGHTITELFPTEVPVTSGEPFIKQKTLQGLSLRDVAVSvlnkKGKPIITHKMDMLFTH 242
Cdd:pfam03486 160 ATGGLSWPKTGSTGFGYPLAEQFGHTIIPLRPALVPFTIDEPFLFLKRLSGISLKNVVLS----NGKGGITFRGELLFTH 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 243 FGLSGPAILRCSQFVVKELKKQPQVPIRIDLYPDINEETLFQKMYKELKEAPKKTIKNVLKPWMQERYLLFLLEKNGISP 322
Cdd:pfam03486 236 RGLSGPAILQLSSYWRRAILKKGGVTLSIDLLPDLDAEELAARLEKPRGAHPKKSLKNSLAGLLPKRLAEFLLEQAGIEP 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 323 NVSFSELPKDPFRQFVRDCKQFTVLANGTLSLDKAFVTGGGVSVKEIDPKKMASKKMEGLYFCGEILDIHGYTGGYNITS 402
Cdd:pfam03486 316 DKKLAQLSKKELAALAQLLKAWTFTPNGTEGYRTAEVTAGGVDTKELSSKTMESKKVPGLFFAGEVLDVDGWTGGYNLQW 395

                         410
                  ....*....|.
gi 1169125346 403 ALVTGRLAGLN 413
Cdd:pfam03486 396 AWSSGYAAGQG 406
 
Name Accession Description Interval E-value
HI0933_like pfam03486
HI0933-like protein;
4-413 0e+00

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 591.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   4 YDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGNKLGRKLAISGGGRCNVTN-RLPVEEIIKHIPGNGRFLYSAFSEFNNE 82
Cdd:pfam03486   1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLGRKILISGGGRCNVTNlSEEPDNFLSRYPGNPKFLKSALSRFTPW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  83 DIIKFFENLGIQLKEEDHGRMFPVTDKAQSVVDALLNRLKQLRVTIRTNEKIKSVLYEDGQAAGIVTNNGEmIHSQSVII 162
Cdd:pfam03486  81 DFIAFFESLGVPLKEEDHGRLFPDSDKASDIVDALLNELKELGVKIRLRTRVLSVEKDDDGRFRVKTGGEE-LEADSLVL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 163 AVGGKSVPHTGSTGDGYEWAEAAGHTITELFPTEVPVTSGEPFIKQKTLQGLSLRDVAVSvlnkKGKPIITHKMDMLFTH 242
Cdd:pfam03486 160 ATGGLSWPKTGSTGFGYPLAEQFGHTIIPLRPALVPFTIDEPFLFLKRLSGISLKNVVLS----NGKGGITFRGELLFTH 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 243 FGLSGPAILRCSQFVVKELKKQPQVPIRIDLYPDINEETLFQKMYKELKEAPKKTIKNVLKPWMQERYLLFLLEKNGISP 322
Cdd:pfam03486 236 RGLSGPAILQLSSYWRRAILKKGGVTLSIDLLPDLDAEELAARLEKPRGAHPKKSLKNSLAGLLPKRLAEFLLEQAGIEP 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 323 NVSFSELPKDPFRQFVRDCKQFTVLANGTLSLDKAFVTGGGVSVKEIDPKKMASKKMEGLYFCGEILDIHGYTGGYNITS 402
Cdd:pfam03486 316 DKKLAQLSKKELAALAQLLKAWTFTPNGTEGYRTAEVTAGGVDTKELSSKTMESKKVPGLFFAGEVLDVDGWTGGYNLQW 395

                         410
                  ....*....|.
gi 1169125346 403 ALVTGRLAGLN 413
Cdd:pfam03486 396 AWSSGYAAGQG 406
YhiN COG2081
Predicted flavoprotein YhiN [General function prediction only];
7-417 0e+00

Predicted flavoprotein YhiN [General function prediction only];


Pssm-ID: 441684 [Multi-domain]  Cd Length: 402  Bit Score: 570.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   7 IVIGGGPSGLMAAIAAGEQGAGVLLIDKGNKLGRKLAISGGGRCNVTNRLPVEEIIKHIPGNGRFLYSAFSEFNNEDIIK 86
Cdd:COG2081     1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVGRKILISGGGRCNFTNSEPLPEFLNYYGGNPHFLKSALSRFTPEDLIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  87 FFENLGIQLKEEDHGRMFPVTDKAQSVVDALLNRLKQLRVTIRTNEKIKSVLYEDGqAAGIVTNNGEMIHSQSVIIAVGG 166
Cdd:COG2081    81 FFEGLGIETKEESSGRVFPDSSKASDILRALLAELREAGVEIRLRTRVTGIEKEDG-GFGVETPDGETVRADAVVLATGG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 167 KSVPHTGSTGDGYEWAEAAGHTITELFPTEVPVTSGEPFIKQktLQGLSLRDVAVSVlnkKGKPIITHKMDMLFTHFGLS 246
Cdd:COG2081   160 LSYPKLGSTGDGYRLAEQFGHTITPLRPALVPLTLSEHFFKR--LAGLSLKNVALSV---GGKKIASFRGELLFTHRGLS 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 247 GPAILRCSQFVVKELKKqPQVPIRIDLYPDINEETLFQKMYKELKEAPKKTIKNVLKPWMQERYLLFLLEKNGisPNVSF 326
Cdd:COG2081   235 GPAILQLSSYWRDALKK-GGATLTIDLLPDLDLEELDARLARPREKNGKKSLKNVLRGLLPKRLAALLLELAD--PDKPL 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 327 SELPKDPFRQFVRDCKQFTVLANGTLSLDKAFVTGGGVSVKEIDPKKMASKKMEGLYFCGEILDIHGYTGGYNITSALVT 406
Cdd:COG2081   312 AQLSKKEREALAALLKAWPLTPTGTRGYDEAIVTAGGVDTKELDPKTMESKKVPGLYFAGEVLDVDGPTGGYNLQWAWSS 391

                         410
                  ....*....|.
gi 1169125346 407 GRLAGLNAGQY 417
Cdd:COG2081   392 GYAAGQAAAAW 402
TIGR00275 TIGR00275
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ...
 7-412 0e+00

flavoprotein, HI0933 family; The model when searched with a partial length search brings in proteins with a dinucleotide-binding motif (Rossman fold) over the initial 40 residues of the model, including oxidoreductases and dehydrogenases. Partially characterized members include an FAD-binding protein from Bacillus cereus and flavoprotein HI0933 from Haemophilus influenzae. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272992 [Multi-domain]  Cd Length: 400  Bit Score: 533.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   7 IVIGGGPSGLMAAIAAGEQGAGVLLIDKGNKLGRKLAISGGGRCNVTNRLPVEEIIKHIPGNGRFLYSAFSEFNNEDIIK 86
Cdd:TIGR00275   1 IIIGGGAAGLMAAITAARAGLSVLLLEKNKKIGKKLLISGGGRCNLTNSCPTPEFVAYYPRNGKFLRSALSRFSNKDLID 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  87 FFENLGIQLKEEDHGRMFPVTDKAQSVVDALLNRLKQLRVTIRTNEKIKSVlYEDGQAAGIVTNNGEmIHSQSVIIAVGG 166
Cdd:TIGR00275  81 FFESLGLELKVEEDGRVFPCSDSAADVLDALLNELKELGVEILTNSKVKSI-EKEDGGFGVETSGGE-YEADKVIIATGG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 167 KSVPHTGSTGDGYEWAEAAGHTITELFPTEVPVTSGEPFIKQktLQGLSLRDVAVSVLNkkGKPIITHKMDMLFTHFGLS 246
Cdd:TIGR00275 159 LSYPQLGSTGDGYEIAESLGHTIVPPVPALVPLTLDESFLKE--LSGISLDGVVLSLVN--GKKVLEEFGELLFTHFGLS 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 247 GPAILRCSQFVVKELKKQPQVPIRIDLYPDINEETLFQKMYKELKEAPKKTIKNVLKPWMQERYLLFLLEKNGISPNVSF 326
Cdd:TIGR00275 235 GPAILDLSAFAARALLKHKGVELEIDLLPDLSEEELEQRLKRLRKSNPKKTVKNILKGLLPKRLAELLLEQLGIDPDLPA 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 327 SELPKDPFRQFVRDCKQFTVLANGTLSLDKAFVTGGGVSVKEIDPKKMASKKMEGLYFCGEILDIHGYTGGYNITSALVT 406
Cdd:TIGR00275 315 AQLSKKEIKKLVQLLKNWPFTISGTRGFKEAEVTAGGVSLKEINPKTMESKLVPGLYFAGEVLDIDGDTGGYNLQWAWSS 394


                  ....*.
gi 1169125346 407 GRLAGL 412
Cdd:TIGR00275 395 GYLAGK 400
PRK08274 PRK08274
FAD-dependent tricarballylate dehydrogenase TcuA;
1-420 2.78e-11

FAD-dependent tricarballylate dehydrogenase TcuA;


Pssm-ID: 236214 [Multi-domain]  Cd Length: 466  Bit Score: 64.90  E-value: 2.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   1 MKQYDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGNK--LGRKLAISGGGRCN-------VTNRLPVEE----IIKHIPG 67
Cdd:PRK08274    2 ASMVDVLVIGGGNAALCAALAAREAGASVLLLEAAPRewRGGNSRHTRNLRCMhdapqdvLVGAYPEEEfwqdLLRVTGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  68 NG-----RFLYSAFSefnneDIIKFFENLGIQLKEEDHGRMFPVTDKAQ------SVVDALLNRLKQLRVTIRTNEKIKS 136
Cdd:PRK08274   82 RTdealaRLLIRESS-----DCRDWMRKHGVRFQPPLSGALHVARTNAFfwgggkALVNALYRSAERLGVEIRYDAPVTA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 137 VLYEDGQAAGIVTNNG----EMIHSQSVIIAVGG---------------------KSVPHtgSTGDGYEW-----AEAAG 186
Cdd:PRK08274  157 LELDDGRFVGARAGSAaggaERIRAKAVVLAAGGfesnrewlreawgqpadnflvRGTPY--NQGDLLKAlldagADRIG 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 187 HtitelfPTE---VPVTSGEPfikqKTLQGLSLRDVAVS---VLNKKGKPIITHKMDMLFTHFGLSGPAILRCSQ---FV 257
Cdd:PRK08274  235 D------PSQchaVAIDARAP----LYDGGICTRIDCVPlgiVVNRDGERFYDEGEDFWPKRYAIWGRLVAQQPGqiaYQ 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 258 VKELKKQPQVPIRidLYPDINEETLfqkmyKELKEA----PKKTIKNVlkpwmqERYllfllekngispNVSFSELPKDP 333
Cdd:PRK08274  305 IFDAKAIGRFMPP--VFPPIQADTL-----EELAEKlgldPAAFLRTV------AAF------------NAAVRPGPFDP 359

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 334 frqFVRDCKQFTVLA----NGTLSLDKA-FV----------TGGGVSVKEIDPKKMASKK-MEGLYFCGEIL--DI--HG 393
Cdd:PRK08274  360 ---TVLDDCGTEGLTppksHWARPIDTPpFYaypvrpgitfTYLGLKVDEDARVRFADGRpSPNLFAAGEMMagNVlgKG 436

                         490       500
                  ....*....|....*....|....*..
gi 1169125346 394 YTGGYNITSALVTGRLAGLNAGQYARS 420
Cdd:PRK08274  437 YPAGVGLTIGAVFGRIAGEEAARHAQH 463
PFDH_like cd08282
Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde ...
 6-67 5.10e-03

Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. Unlike typical FDH, Pseudomonas putida aldehyde-dismutating FDH (PFDH) is glutathione-independent. PFDH converts 2 molecules of aldehydes to corresponding carboxylic acid and alcohol. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like the zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. Unlike ADH, where NAD(P)(H) acts as a cofactor, NADH in FDH is a tightly bound redox cofactor (similar to nicotinamide proteins). The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176242 [Multi-domain]  Cd Length: 375  Bit Score: 38.73  E-value: 5.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169125346   6 VIVIGGGPSGLMAAIAAGEQGAG-VLLIDKgNKLGRKLAISGGgrC---NVTNRLPVEEIIKHIPG 67
Cdd:cd08282   180 VAVFGAGPVGLMAAYSAILRGASrVYVVDH-VPERLDLAESIG--AipiDFSDGDPVEQILGLEPG 242
 
Name Accession Description Interval E-value
HI0933_like pfam03486
HI0933-like protein;
4-413 0e+00

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 591.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   4 YDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGNKLGRKLAISGGGRCNVTN-RLPVEEIIKHIPGNGRFLYSAFSEFNNE 82
Cdd:pfam03486   1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLGRKILISGGGRCNVTNlSEEPDNFLSRYPGNPKFLKSALSRFTPW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  83 DIIKFFENLGIQLKEEDHGRMFPVTDKAQSVVDALLNRLKQLRVTIRTNEKIKSVLYEDGQAAGIVTNNGEmIHSQSVII 162
Cdd:pfam03486  81 DFIAFFESLGVPLKEEDHGRLFPDSDKASDIVDALLNELKELGVKIRLRTRVLSVEKDDDGRFRVKTGGEE-LEADSLVL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 163 AVGGKSVPHTGSTGDGYEWAEAAGHTITELFPTEVPVTSGEPFIKQKTLQGLSLRDVAVSvlnkKGKPIITHKMDMLFTH 242
Cdd:pfam03486 160 ATGGLSWPKTGSTGFGYPLAEQFGHTIIPLRPALVPFTIDEPFLFLKRLSGISLKNVVLS----NGKGGITFRGELLFTH 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 243 FGLSGPAILRCSQFVVKELKKQPQVPIRIDLYPDINEETLFQKMYKELKEAPKKTIKNVLKPWMQERYLLFLLEKNGISP 322
Cdd:pfam03486 236 RGLSGPAILQLSSYWRRAILKKGGVTLSIDLLPDLDAEELAARLEKPRGAHPKKSLKNSLAGLLPKRLAEFLLEQAGIEP 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 323 NVSFSELPKDPFRQFVRDCKQFTVLANGTLSLDKAFVTGGGVSVKEIDPKKMASKKMEGLYFCGEILDIHGYTGGYNITS 402
Cdd:pfam03486 316 DKKLAQLSKKELAALAQLLKAWTFTPNGTEGYRTAEVTAGGVDTKELSSKTMESKKVPGLFFAGEVLDVDGWTGGYNLQW 395

                         410
                  ....*....|.
gi 1169125346 403 ALVTGRLAGLN 413
Cdd:pfam03486 396 AWSSGYAAGQG 406
YhiN COG2081
Predicted flavoprotein YhiN [General function prediction only];
7-417 0e+00

Predicted flavoprotein YhiN [General function prediction only];


Pssm-ID: 441684 [Multi-domain]  Cd Length: 402  Bit Score: 570.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   7 IVIGGGPSGLMAAIAAGEQGAGVLLIDKGNKLGRKLAISGGGRCNVTNRLPVEEIIKHIPGNGRFLYSAFSEFNNEDIIK 86
Cdd:COG2081     1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVGRKILISGGGRCNFTNSEPLPEFLNYYGGNPHFLKSALSRFTPEDLIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  87 FFENLGIQLKEEDHGRMFPVTDKAQSVVDALLNRLKQLRVTIRTNEKIKSVLYEDGqAAGIVTNNGEMIHSQSVIIAVGG 166
Cdd:COG2081    81 FFEGLGIETKEESSGRVFPDSSKASDILRALLAELREAGVEIRLRTRVTGIEKEDG-GFGVETPDGETVRADAVVLATGG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 167 KSVPHTGSTGDGYEWAEAAGHTITELFPTEVPVTSGEPFIKQktLQGLSLRDVAVSVlnkKGKPIITHKMDMLFTHFGLS 246
Cdd:COG2081   160 LSYPKLGSTGDGYRLAEQFGHTITPLRPALVPLTLSEHFFKR--LAGLSLKNVALSV---GGKKIASFRGELLFTHRGLS 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 247 GPAILRCSQFVVKELKKqPQVPIRIDLYPDINEETLFQKMYKELKEAPKKTIKNVLKPWMQERYLLFLLEKNGisPNVSF 326
Cdd:COG2081   235 GPAILQLSSYWRDALKK-GGATLTIDLLPDLDLEELDARLARPREKNGKKSLKNVLRGLLPKRLAALLLELAD--PDKPL 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 327 SELPKDPFRQFVRDCKQFTVLANGTLSLDKAFVTGGGVSVKEIDPKKMASKKMEGLYFCGEILDIHGYTGGYNITSALVT 406
Cdd:COG2081   312 AQLSKKEREALAALLKAWPLTPTGTRGYDEAIVTAGGVDTKELDPKTMESKKVPGLYFAGEVLDVDGPTGGYNLQWAWSS 391

                         410
                  ....*....|.
gi 1169125346 407 GRLAGLNAGQY 417
Cdd:COG2081   392 GYAAGQAAAAW 402
TIGR00275 TIGR00275
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ...
 7-412 0e+00

flavoprotein, HI0933 family; The model when searched with a partial length search brings in proteins with a dinucleotide-binding motif (Rossman fold) over the initial 40 residues of the model, including oxidoreductases and dehydrogenases. Partially characterized members include an FAD-binding protein from Bacillus cereus and flavoprotein HI0933 from Haemophilus influenzae. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272992 [Multi-domain]  Cd Length: 400  Bit Score: 533.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   7 IVIGGGPSGLMAAIAAGEQGAGVLLIDKGNKLGRKLAISGGGRCNVTNRLPVEEIIKHIPGNGRFLYSAFSEFNNEDIIK 86
Cdd:TIGR00275   1 IIIGGGAAGLMAAITAARAGLSVLLLEKNKKIGKKLLISGGGRCNLTNSCPTPEFVAYYPRNGKFLRSALSRFSNKDLID 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  87 FFENLGIQLKEEDHGRMFPVTDKAQSVVDALLNRLKQLRVTIRTNEKIKSVlYEDGQAAGIVTNNGEmIHSQSVIIAVGG 166
Cdd:TIGR00275  81 FFESLGLELKVEEDGRVFPCSDSAADVLDALLNELKELGVEILTNSKVKSI-EKEDGGFGVETSGGE-YEADKVIIATGG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 167 KSVPHTGSTGDGYEWAEAAGHTITELFPTEVPVTSGEPFIKQktLQGLSLRDVAVSVLNkkGKPIITHKMDMLFTHFGLS 246
Cdd:TIGR00275 159 LSYPQLGSTGDGYEIAESLGHTIVPPVPALVPLTLDESFLKE--LSGISLDGVVLSLVN--GKKVLEEFGELLFTHFGLS 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 247 GPAILRCSQFVVKELKKQPQVPIRIDLYPDINEETLFQKMYKELKEAPKKTIKNVLKPWMQERYLLFLLEKNGISPNVSF 326
Cdd:TIGR00275 235 GPAILDLSAFAARALLKHKGVELEIDLLPDLSEEELEQRLKRLRKSNPKKTVKNILKGLLPKRLAELLLEQLGIDPDLPA 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 327 SELPKDPFRQFVRDCKQFTVLANGTLSLDKAFVTGGGVSVKEIDPKKMASKKMEGLYFCGEILDIHGYTGGYNITSALVT 406
Cdd:TIGR00275 315 AQLSKKEIKKLVQLLKNWPFTISGTRGFKEAEVTAGGVSLKEINPKTMESKLVPGLYFAGEVLDIDGDTGGYNLQWAWSS 394


                  ....*.
gi 1169125346 407 GRLAGL 412
Cdd:TIGR00275 395 GYLAGK 400
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 1-420 3.45e-23

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


Pssm-ID: 440673 [Multi-domain]  Cd Length: 443  Bit Score: 101.06  E-value: 3.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   1 MKQYDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGNKLGRKLAISGGGrCNVTN------------RLPVEEIIKhipgN 68
Cdd:COG1053     1 DHEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGGHTAAAQGG-INAAGtnvqkaagedspEEHFYDTVK----G 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  69 GRFLYS-----AFSEfNNEDIIKFFENLGIQLKEEDHG-----------RMFPVTDKA-QSVVDALLNRLKQLRVTIRTN 131
Cdd:COG1053    76 GDGLADqdlveALAE-EAPEAIDWLEAQGVPFSRTPDGrlpqfgghsvgRTCYAGDGTgHALLATLYQAALRLGVEIFTE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 132 EKIKSVLYEDGQAAGIVTNNGEM----IHSQSVIIAVGG------------------KSVPHTGSTGDGYEWAEAAG--- 186
Cdd:COG1053   155 TEVLDLIVDDGRVVGVVARDRTGeivrIRAKAVVLATGGfgrnyemraeylpeaegaLSTNAPGNTGDGIAMALRAGaal 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 187 --------HtitelfPTEVPVTSGepfikqktLQGLSLRDVAVSVL-NKKGK---------PIITHKMdmlFTHFGlsGP 248
Cdd:COG1053   235 admefvqfH------PTGLPGDGG--------LISEGARGKPGGILvNKEGErfmneyaprDVVSRAI---LEEID--EP 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 249 AILRCSQFVVKELKKQPQVPiridlyPDINEETLfqkmyKELKEA---PKKTIKNVLkpwmqERYLLFllEKNGISPNVS 325
Cdd:COG1053   296 AYLVLDLRHRRRLEEYLEAG------YLVKADTI-----EELAAKlgiDAAELAATV-----ARYNAA--AKAGVDPRGT 357

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 326 F----SELPKDPFRqfVRDCKQFTVlangtlsldkafvtgGGVsvkEIDPKKMASKK----MEGLYFCGEIL-DIHG--Y 394
Cdd:COG1053   358 ClgpiKEGPFYAIP--VRPGVHYTM---------------GGL---RVDADARVLDAdgtpIPGLYAAGEAAgSVHGanR 417

                         490       500
                  ....*....|....*....|....*.
gi 1169125346 395 TGGYNITSALVTGRLAGLNAGQYARS 420
Cdd:COG1053   418 LGGNSLGDALVFGRIAGRHAAEYAKA 443
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 5-198 5.98e-16

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


Pssm-ID: 395718 [Multi-domain]  Cd Length: 398  Bit Score: 78.87  E-value: 5.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   5 DVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGNKLGRKLAISGGGRC--NVTNRLPVEEIIKHIpgngRFLYSAFSEFNNE 82
Cdd:pfam00890   1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGATAWSSGGIDalGNPPQGGIDSPELHP----TDTLKGLDELADH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  83 DIIK-----------FFENLGIQLKEEDHG-----------------------RMFPVTDKAqsVVDALLNRLKQLRVTI 128
Cdd:pfam00890  77 PYVEafveaapeavdWLEALGVPFSRTEDGhldlrplgglsatwrtphdaadrRRGLGTGHA--LLARLLEGLRKAGVDF 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 129 RTNEKIKSVLYEDGQAAGIV---TNNGEM--IHSQS-VIIAVGGKSVPHT---------------GSTGDGYEWAEAAGH 187
Cdd:pfam00890 155 QPRTAADDLIVEDGRVTGAVvenRRNGREvrIRAIAaVLLATGGFGRLAElllpaagyadttnppANTGDGLALALRAGA 234

                         250
                  ....*....|.
gi 1169125346 188 TITELFPTEVP 198
Cdd:pfam00890 235 ALTDDLMEFVQ 245
GIDA pfam01134
Glucose inhibited division protein A;
5-419 2.42e-14

Glucose inhibited division protein A;


Pssm-ID: 250388 [Multi-domain]  Cd Length: 391  Bit Score: 74.12  E-value: 2.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   5 DVIVIGGGPSGLMAAIAAGEQGAGVLLID-KGNKLGRkLAisgggrCNVTNRLP-----VEEIikhipgngRFLYSafse 78
Cdd:pfam01134   1 DVIVIGGGHAGCEAALAAARMGAKVLLIThNTDTIAE-LS------CNPSIGGIakghlVREI--------DALGG---- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  79 fnneDIIKFFENLGIQLKEEDHGRMFPV------TDK---AQSVVDALLNrlkQLRVTIRTNEkIKSVLYEDGQAAGIVT 149
Cdd:pfam01134  62 ----LMGKAADKTGIQFRMLNTSKGPAVralraqVDRdlySKEMTETLEN---HPNLTLIQGE-VTDLIPENGKVKGVVT 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 150 NNGEMIHSQSVIIAVG--GKSVPHTGSTgdgyewAEAAGHtitelfptevpvtsgepfIKQKTLQGLS--LRDVAVSVLN 225
Cdd:pfam01134 134 EDGEEYKAKAVVLATGtfLNGKIHIGLK------CYPAGR------------------LGELTSEGLSesLKELGFELGR 189

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 226 KKG--KPIITHK---MDMLFTHFG---------LSGPAILRcsQFV--VKELKKQPQVPIRIDLypdiNEETLFQKMYKE 289
Cdd:pfam01134 190 FKTgtPPRIDKDsidFSKLEEQPGdkpgppfsyLNCPMNKE--QYPcfLTYTNEATHEIIRDNL----HRSPMFEGCIEG 263

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 290 LKEAPKKTIKN-VLKPWMQERYLLFlLEKNGISPN----VSFS-ELPKDPFRQFVRDCKqftvlanGtlsLDKAFVTGGG 363
Cdd:pfam01134 264 IGPRYCPSIEDkPVRFADKPYHQVF-LEPEGLDTDeyylVGFStSLPEDVQKRVLRTIP-------G---LENAEIVRPG 332

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169125346 364 VSVKE--IDPKK----MASKKMEGLYFCGEIldihgyTG--GYniTSALVTGRLAGLNAGQYAR 419
Cdd:pfam01134 333 YAIEYdyIDPPQllptLETKKIPGLFFAGQI------NGteGY--EEAAAQGLLAGINAARKAL 388
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 1-169 6.42e-12

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


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 66.11  E-value: 6.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   1 MKQYDVIVIGGGPSGLMAAIAAGEQGAGVLLIDK---GNKLGRKLAISGGG-----RCNVTNRL-----PVEEIIKHIPG 67
Cdd:COG0654     1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVERappPRPDGRGIALSPRSlellrRLGLWDRLlargaPIRGIRVRDGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  68 NGRFLYSafsefnnediikffenlgIQLKEEDHGRMFPVTdkaQSVV-DALLNRLKQLRVTIRTNEKIKSVLyEDGQAAG 146
Cdd:COG0654    81 DGRVLAR------------------FDAAETGLPAGLVVP---RADLeRALLEAARALGVELRFGTEVTGLE-QDADGVT 138

                         170       180
                  ....*....|....*....|...
gi 1169125346 147 IVTNNGEMIHSQSVIIAVGGKSV 169
Cdd:COG0654   139 VTLADGRTLRADLVVGADGARSA 161
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 5-186 2.23e-11

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


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 64.94  E-value: 2.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   5 DVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGNKLGRKLaiSGGGRCNVTNRLpveeiIKHIPGNGRFlysaFSEFNNEdi 84
Cdd:pfam12831   1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGML--TSGLVGPDMGFY-----LNKEQVVGGI----AREFRQR-- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  85 ikffenlgiqLKEEDHGRMFPVTDKAQSVVD------ALLNRLKQLRVTIRTNEKIKSVLYEDGQAAGIVTNN---GEMI 155
Cdd:pfam12831  68 ----------LRARGGLPGPYGLRGGWVPFDpevakaVLDEMLAEAGVTVLLHTRVVGVVKEGGRITGVTVETkggRITI 137

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1169125346 156 HSQSVIIAvggksvphtgsTGDGyEWAEAAG 186
Cdd:pfam12831 138 RAKVFIDA-----------TGDG-DLAALAG 156
PRK08274 PRK08274
FAD-dependent tricarballylate dehydrogenase TcuA;
1-420 2.78e-11

FAD-dependent tricarballylate dehydrogenase TcuA;


Pssm-ID: 236214 [Multi-domain]  Cd Length: 466  Bit Score: 64.90  E-value: 2.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   1 MKQYDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGNK--LGRKLAISGGGRCN-------VTNRLPVEE----IIKHIPG 67
Cdd:PRK08274    2 ASMVDVLVIGGGNAALCAALAAREAGASVLLLEAAPRewRGGNSRHTRNLRCMhdapqdvLVGAYPEEEfwqdLLRVTGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  68 NG-----RFLYSAFSefnneDIIKFFENLGIQLKEEDHGRMFPVTDKAQ------SVVDALLNRLKQLRVTIRTNEKIKS 136
Cdd:PRK08274   82 RTdealaRLLIRESS-----DCRDWMRKHGVRFQPPLSGALHVARTNAFfwgggkALVNALYRSAERLGVEIRYDAPVTA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 137 VLYEDGQAAGIVTNNG----EMIHSQSVIIAVGG---------------------KSVPHtgSTGDGYEW-----AEAAG 186
Cdd:PRK08274  157 LELDDGRFVGARAGSAaggaERIRAKAVVLAAGGfesnrewlreawgqpadnflvRGTPY--NQGDLLKAlldagADRIG 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 187 HtitelfPTE---VPVTSGEPfikqKTLQGLSLRDVAVS---VLNKKGKPIITHKMDMLFTHFGLSGPAILRCSQ---FV 257
Cdd:PRK08274  235 D------PSQchaVAIDARAP----LYDGGICTRIDCVPlgiVVNRDGERFYDEGEDFWPKRYAIWGRLVAQQPGqiaYQ 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 258 VKELKKQPQVPIRidLYPDINEETLfqkmyKELKEA----PKKTIKNVlkpwmqERYllfllekngispNVSFSELPKDP 333
Cdd:PRK08274  305 IFDAKAIGRFMPP--VFPPIQADTL-----EELAEKlgldPAAFLRTV------AAF------------NAAVRPGPFDP 359

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 334 frqFVRDCKQFTVLA----NGTLSLDKA-FV----------TGGGVSVKEIDPKKMASKK-MEGLYFCGEIL--DI--HG 393
Cdd:PRK08274  360 ---TVLDDCGTEGLTppksHWARPIDTPpFYaypvrpgitfTYLGLKVDEDARVRFADGRpSPNLFAAGEMMagNVlgKG 436

                         490       500
                  ....*....|....*....|....*..
gi 1169125346 394 YTGGYNITSALVTGRLAGLNAGQYARS 420
Cdd:PRK08274  437 YPAGVGLTIGAVFGRIAGEEAARHAQH 463
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
4-165 3.95e-10

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 60.52  E-value: 3.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   4 YDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGNKlgrklaisgGGRCNVTNRlpveeiIKHIPGngrflysafsefnned 83
Cdd:COG0492     1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEP---------GGQLATTKE------IENYPG---------------- 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  84 iikffenlgiqlkeedhgrmFPVTDKAQSVVDALLNRLKQLRVTIRTnEKIKSVlYEDGQAAGIVTNNGEMIHSQSVIIA 163
Cdd:COG0492    50 --------------------FPEGISGPELAERLREQAERFGAEILL-EEVTSV-DKDDGPFRVTTDDGTEYEAKAVIIA 107


                  ..
gi 1169125346 164 VG 165
Cdd:COG0492   108 TG 109
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 4-169 1.00e-09

geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273936 [Multi-domain]  Cd Length: 295  Bit Score: 59.25  E-value: 1.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   4 YDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGnKLGRKLAISGG--GRCNVTNRLPVEEIIKhiPGNGRFLYSAFSEFNN 81
Cdd:TIGR02032   1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEKK-SFPRYKPCGGAlsPRALEELDLPGELIVN--LVRGARFFSPNGDSVE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  82 ediIKFFENLGIQLKEEDHGRMfpVTDKAQSVvdallnrlkqlRVTIRTNEKIKSVLYEDGQAAGIVTNNGEMIHSQSVI 161
Cdd:TIGR02032  78 ---IPIETELAYVIDRDAFDEQ--LAERAQEA-----------GAELRLGTRVLDVEIHDDRVVVIVRGSEGTVTAKIVI 141


                  ....*...
gi 1169125346 162 IAVGGKSV 169
Cdd:TIGR02032 142 GADGSRSI 149
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
11-163 3.20e-09

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 57.67  E-value: 3.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  11 GGPSGLMAAIAAGEQGAGVLLIDKGNKLGRKlaISGGGRC----NVTNRLPVEEIIKHiPGNGRFLYSAfsefnNEDIIK 86
Cdd:COG0644     1 AGPAGSAAARRLARAGLSVLLLEKGSFPGDK--ICGGGLLpralEELEPLGLDEPLER-PVRGARFYSP-----GGKSVE 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169125346  87 FFEnlgiqlkEEDHGRMFpvtDKAQsVVDALLNRLKQLRVTIRTNEKIKSVLYEDGQAAgIVTNNGEMIHSQSVIIA 163
Cdd:COG0644    73 LPP-------GRGGGYVV---DRAR-FDRWLAEQAEEAGAEVRTGTRVTDVLRDDGRVV-VRTGDGEEIRADYVVDA 137
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 1-198 3.83e-09

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: 58.17  E-value: 3.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   1 MKQYDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGNklgrklaisGGGRCnvTNRlpveeiikhipgnG-----RFLYSA 75
Cdd:COG1249     1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGR---------LGGTC--LNV-------------GcipskALLHAA 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  76 --FSEFNNediikfFENLGIQLKEE--DHGRMFpvtDKAQSVVDAL----LNRLKQLRVTIRTNE-KIKSvlyeDGQaag 146
Cdd:COG1249    57 evAHEARH------AAEFGISAGAPsvDWAALM---ARKDKVVDRLrggvEELLKKNGVDVIRGRaRFVD----PHT--- 120

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1169125346 147 IVTNNGEMIHSQSVIIAVGGKSV--PHTGSTGDGYewaeaagHTITELF-PTEVP 198
Cdd:COG1249   121 VEVTGGETLTADHIVIATGSRPRvpPIPGLDEVRV-------LTSDEALeLEELP 168
PRK08275 PRK08275
putative oxidoreductase; Provisional
 4-186 4.00e-09

putative oxidoreductase; Provisional


Pssm-ID: 181346 [Multi-domain]  Cd Length: 554  Bit Score: 58.53  E-value: 4.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   4 YDVIVIGGGPSGLMAAIAAGEQ--GAGVLLIDKGNkLGRKLAISGG--GRCNV------TNRLPVEEIIkhIPGNGRFLY 73
Cdd:PRK08275   10 TDILVIGGGTAGPMAAIKAKERnpALRVLLLEKAN-VKRSGAISMGmdGLNNAvipghaTPEQYTKEIT--IANDGIVDQ 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  74 SAFSEF--NNEDIIKFFENLGIQ----------LKEEDH-GRMFPVTDKAQSVVDALLNRLKQLRVTIrTNEKIKSVLY- 139
Cdd:PRK08275   87 KAVYAYaeHSFETIQQLDRWGVKfekdetgdyaVKKVHHmGSYVLPMPEGHDIKKVLYRQLKRARVLI-TNRIMATRLLt 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169125346 140 -EDGQAAGIV---TNNGEM--IHSQSVIIAVGGK---SVPHTG----------STGDGYEWAEAAG 186
Cdd:PRK08275  166 dADGRVAGALgfdCRTGEFlvIRAKAVILCCGAAgrlGLPASGylfgtyenptNAGDGYAMAYHAG 231
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 1-172 5.77e-09

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 57.94  E-value: 5.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   1 MKQYDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGNKLGRKLA-ISGGG------------------------------- 48
Cdd:COG1233     1 MMMYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRARtFERPGfrfdvgpsvltmpgvlerlfrelgledylel 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  49 -RCNVTNRLP----------------VEEIIKHIPGNGR-------------------FLYSAF---------------- 76
Cdd:COG1233    81 vPLDPAYRVPfpdgraldlprdlertAAELERLFPGDAEayrrflaelrrlydalledLLYRPLlslrdllrplalarll 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  77 ------------SEFNNEDIIKFFENLG----------------IQLKEEDHGRMFPVtDKAQSVVDALLNRLKQLRVTI 128
Cdd:COG1233   161 rlllrslrdllrRYFKDPRLRALLAGQAlylglspdrtpalyalIAYLEYAGGVWYPK-GGMGALADALARLAEELGGEI 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1169125346 129 RTNEKIKSVLYEDGQAAGIVTNNGEMIHSQSVIIAVggkSVPHT 172
Cdd:COG1233   240 RTGAEVERILVEGGRATGVRLADGEEIRADAVVSNA---DPAHT 280
PRK13800 PRK13800
fumarate reductase/succinate dehydrogenase flavoprotein subunit;
5-190 1.55e-08

fumarate reductase/succinate dehydrogenase flavoprotein subunit;


Pssm-ID: 237512 [Multi-domain]  Cd Length: 897  Bit Score: 56.78  E-value: 1.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   5 DVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGN-KLGRKLAISGGGRCNVTnrLP--------VEEIIKHIPG--NGRFLY 73
Cdd:PRK13800   15 DVLVIGGGTAGTMAALTAAEHGANVLLLEKAHvRHSGALAMGMDGVNNAV--IPgkaepedyVAEITRANDGivNQRTVY 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  74 -SAFSEFNnedIIKFFENLGIQLKEEDHGR------------MFPVTDkAQSVVDALLNRLKQ--LRVTIRTNEKIKSV- 137
Cdd:PRK13800   93 qTATRGFA---MVQRLERYGVKFEKDEHGEyavrrvhrsgsyVLPMPE-GKDVKKALYRVLRQrsMRERIRIENRLMPVr 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169125346 138 -LYEDGQ---AAGIVTNNGEM--IHSQSVIIAVG--GK-SVPHTG----------STGDGYEWAEAAGHTIT 190
Cdd:PRK13800  169 vLTEGGRavgAAALNTRTGEFvtVGAKAVILATGpcGRlGLPASGylygtyenptNAGDGYSMAYHAGAELS 240
PRK12839 PRK12839
FAD-dependent oxidoreductase;
3-47 4.12e-08

FAD-dependent oxidoreductase;


Pssm-ID: 237223 [Multi-domain]  Cd Length: 572  Bit Score: 55.22  E-value: 4.12e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1169125346   3 QYDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGNKLGRKLAISGG 47
Cdd:PRK12839    8 TYDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKASTCGGATAWSGG 52
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 1-36 4.87e-08

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 54.80  E-value: 4.87e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1169125346   1 MKQYDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGN 36
Cdd:PRK06292    1 MEKYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGP 36
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
1-39 9.43e-08

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


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 54.01  E-value: 9.43e-08
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1169125346   1 MKQYDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGNKLG 39
Cdd:PRK05249    3 MYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVG 41
PRK05329 PRK05329
glycerol-3-phosphate dehydrogenase subunit GlpB;
1-35 1.24e-07

glycerol-3-phosphate dehydrogenase subunit GlpB;


Pssm-ID: 235412  Cd Length: 422  Bit Score: 53.32  E-value: 1.24e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1169125346   1 MKqYDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKG 35
Cdd:PRK05329    1 MK-FDVLVIGGGLAGLTAALAAAEAGKRVALVAKG 34
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
 1-178 2.16e-07

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 53.01  E-value: 2.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   1 MKQYDVIVIGGGPSGLMAAIAAGEQGAGVLLID--KGNKLGRKLaisgGGRCnvTNR--LPVEEIIkhipgngrflysAF 76
Cdd:PRK06327    2 SKQFDVVVIGAGPGGYVAAIRAAQLGLKVACIEawKNPKGKPAL----GGTC--LNVgcIPSKALL------------AS 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  77 SEfNNEDIIKFFENLGIQLKEE--DHGRMFPVTDKaqsVVDALLNRLKQLrvtIRTNeKIkSVLYEDGQAAG-------- 146
Cdd:PRK06327   64 SE-EFENAGHHFADHGIHVDGVkiDVAKMIARKDK---VVKKMTGGIEGL---FKKN-KI-TVLKGRGSFVGktdagyei 134

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1169125346 147 -IVTNNGEMIHSQSVIIAVGGKSVPHTGSTGDG 178
Cdd:PRK06327  135 kVTGEDETVITAKHVIIATGSEPRHLPGVPFDN 167
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
2-166 2.19e-07

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 52.60  E-value: 2.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   2 KQYDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGnKLGRklAISG--GGRCNVTNRLPVEEiikhipgngrfLYSAFSEF 79
Cdd:COG0665     1 ATADVVVIGGGIAGLSTAYHLARRGLDVTVLERG-RPGS--GASGrnAGQLRPGLAALADR-----------ALVRLARE 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  80 NNEDIIKFFENLGIQLKEEDHGRMFPVTDKAQ------------------------------------------------ 111
Cdd:COG0665    67 ALDLWRELAAELGIDCDFRRTGVLYLARTEAElaalraeaealralglpvelldaaelrerepglgspdyagglydpddg 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 112 -----SVVDALLNRLKQLRVTIRTNEKIKSVLYEDGQAAGIVTNNGEmIHSQSVIIAVGG 166
Cdd:COG0665   147 hvdpaKLVRALARAARAAGVRIREGTPVTGLEREGGRVTGVRTERGT-VRADAVVLAAGA 205
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 5-166 2.23e-07

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


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 52.40  E-value: 2.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   5 DVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGNKLGR-------KLaISGGGRCNVTNRLP---------VEEIIK----H 64
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGSgasgrnaGL-IHPGLRYLEPSELArlalealdlWEELEEelgiD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  65 IPGNGRFLYSAFSEFNNEDIIKFFENL---GIQ---LKEEDHGRMFPVTDK--------------AQSVVDALLNRLKQL 124
Cdd:pfam01266  80 CGFRRCGVLVLARDEEEEALEKLLAALrrlGVPaelLDAEELRELEPLLPGlrgglfypdgghvdPARLLRALARAAEAL 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1169125346 125 RVTIRTNEKIKSVLyEDGQAAGIVTNNgemiHSQSVIIAVGG 166
Cdd:pfam01266 160 GVRIIEGTEVTGIE-EEGGVWGVVTTG----EADAVVNAAGA 196
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 1-172 3.45e-07

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: 52.17  E-value: 3.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   1 MKQYDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGNKLGrklaisG--------GGRCNVTNrlpveeiikhipgngrFL 72
Cdd:COG2072     4 TEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVG------GtwrdnrypGLRLDTPS----------------HL 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  73 YSaFSefnnediikFFENlgiqlkeEDHGRMFP----VTDKAQSVVDALlnrlkQLRVTIRTNEKIKSVLYEDGQAAGIV 148
Cdd:COG2072    62 YS-LP---------FFPN-------WSDDPDFPtgdeILAYLEAYADKF-----GLRRPIRFGTEVTSARWDEADGRWTV 119

                         170       180
                  ....*....|....*....|....*
gi 1169125346 149 -TNNGEMIHSQSVIIAVGGKSVPHT 172
Cdd:COG2072   120 tTDDGETLTARFVVVATGPLSRPKI 144
PRK07494 PRK07494
UbiH/UbiF family hydroxylase;
1-33 5.25e-07

UbiH/UbiF family hydroxylase;


Pssm-ID: 181001 [Multi-domain]  Cd Length: 388  Bit Score: 51.44  E-value: 5.25e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1169125346   1 MKQYDVIVIGGGPSGLMAAIAAGEQGAGVLLID 33
Cdd:PRK07494    5 KEHTDIAVIGGGPAGLAAAIALARAGASVALVA 37
NadB COG0029
Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the ...
 1-186 1.02e-06

Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 439800 [Multi-domain]  Cd Length: 521  Bit Score: 50.88  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   1 MKQYDVIVIGGGPSGLMAAIAAGEQGAgVLLIDKGnKLGR---KLA----------------------ISGGGRCNvtnr 55
Cdd:COG0029     2 RLKTDVLVIGSGIAGLSAALKLAERGR-VTLLTKG-ELGEsntRWAqggiaavldpgdspelhiadtlAAGAGLCD---- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  56 lpvEEIIKHIPGNGRflysafsefnneDIIKFFENLGIQLKEEDHG-------------RMFPVTDKA-QSVVDALLNRL 121
Cdd:COG0029    76 ---PEAVRVLVEEGP------------ERIRELIELGVPFDRDEDGelaltregghsrrRILHAGDATgREIERALLEAV 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169125346 122 KQL-RVTIRTNEKIKSVL-YEDGQAAGIV-----TNNGEMIHSQSVIIAVGG------KSVPHTGSTGDGYEWAEAAG 186
Cdd:COG0029   141 RAHpNITVLENHFAVDLItDADGRCVGAYvldekTGEVETIRAKAVVLATGGagqlyaYTTNPDVATGDGIAMAYRAG 218
PRK12835 PRK12835
3-ketosteroid-delta-1-dehydrogenase; Reviewed
 4-48 1.05e-06

3-ketosteroid-delta-1-dehydrogenase; Reviewed


Pssm-ID: 237221 [Multi-domain]  Cd Length: 584  Bit Score: 50.96  E-value: 1.05e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1169125346   4 YDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGNKLGRKLAISGGG 48
Cdd:PRK12835   12 VDVLVVGSGGGGMTAALTAAARGLDTLVVEKSAHFGGSTALSGGG 56
YdhS COG4529
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
4-165 1.12e-06

Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];


Pssm-ID: 443597 [Multi-domain]  Cd Length: 466  Bit Score: 50.72  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   4 YDVIVIGGGPSGLMAAIA---AGEQGAGVLLIDKGNKLGRKLAISGGGRCNVTNrLPVEEIikhipgngrflySAFSEfN 80
Cdd:COG4529     6 KRIAIIGGGASGTALAIHllrRAPEPLRITLFEPRPELGRGVAYSTDSPEHLLN-VPAGRM------------SAFPD-D 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  81 NEDIIKFFENLGIQLKEEDHGRMFP--------VtdkaQSVVDALLNRLKQLRVTIRTNEKIKSVLYEDGQAAgIVTNNG 152
Cdd:COG4529    72 PDHFLRWLRENGARAAPAIDPDAFVprrlfgeyL----RERLAEALARAPAGVRLRHIRAEVVDLERDDGGYR-VTLADG 146

                         170
                  ....*....|...
gi 1169125346 153 EMIHSQSVIIAVG 165
Cdd:COG4529   147 ETLRADAVVLATG 159
GlpB COG3075
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
1-35 1.75e-06

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


Pssm-ID: 442309  Cd Length: 415  Bit Score: 49.79  E-value: 1.75e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1169125346   1 MKqYDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKG 35
Cdd:COG3075     1 MK-FDVVVIGGGLAGLTAAIRAAEAGLRVAIVSAG 34
PRK07121 PRK07121
FAD-binding protein;
4-47 4.15e-06

FAD-binding protein;


Pssm-ID: 180854 [Multi-domain]  Cd Length: 492  Bit Score: 48.73  E-value: 4.15e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1169125346   4 YDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGNKLGRKLAISGG 47
Cdd:PRK07121   21 ADVVVVGFGAAGACAAIEAAAAGARVLVLERAAGAGGATALSGG 64
PRK06134 PRK06134
putative FAD-binding dehydrogenase; Reviewed
 4-192 4.53e-06

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 180419 [Multi-domain]  Cd Length: 581  Bit Score: 48.95  E-value: 4.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   4 YDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGNKLGRKLAISGGGRCNVTNRLPVEEIIKHIPGNGR-FLYSAFSEFNNE 82
Cdd:PRK06134   13 CDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGGTTAWSGGWMWIPRNPLARRAGIVEDIEQPRtYLRHELGARYDA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  83 DIIKFFENLG---IQLKEED--------------HGRMFPVTDKAQSV---------VDALLNRLK-------------- 122
Cdd:PRK06134   93 ARIDAFLEAGphmVAFFERHtalrfadgnaipdyHGDTPGAATGGRSLiaapfdgreLGALLERLRkplretsfmgmpim 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 123 --------------------------------------------------------QLRVTIRTNEKIKSVLYEDGQAAG 146
Cdd:PRK06134  173 agadlaaflnptrsfraflhvarrfarhlidlarhgrgmhlvngnalvarllksaeDLGVRIWESAPARELLREDGRVAG 252

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169125346 147 IVTNNGE---MIHSQ-SVIIAVGG---------------------KSVPHTGSTGDGYEWAEAAGHTI-TEL 192
Cdd:PRK06134  253 AVVETPGglqEIRARkGVVLAAGGfphdparraalfpraptghehLSLPPPGNSGDGLRLGESAGGVVaTDL 324
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
5-43 4.99e-06

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 48.70  E-value: 4.99e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1169125346   5 DVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGNKLGRKLA 43
Cdd:COG1148   142 RALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAA 180
PRK07843 PRK07843
3-oxosteroid 1-dehydrogenase;
3-48 5.76e-06

3-oxosteroid 1-dehydrogenase;


Pssm-ID: 236111 [Multi-domain]  Cd Length: 557  Bit Score: 48.49  E-value: 5.76e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1169125346   3 QYDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGNKLGRKLAISGGG 48
Cdd:PRK07843    7 EYDVVVVGSGAAGMVAALTAAHRGLSTVVVEKAPHYGGSTARSGGG 52
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
 6-229 7.90e-06

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 48.24  E-value: 7.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346    6 VIVIGGGPSGLMAAIAAGEQGAGVLLIDKGNKLG--RKLAISG----GGRCNVTNrlpveeiikHIPGNGRF-------- 71
Cdd:PTZ00306   412 VIVVGGGLAGCSAAIEAASCGAQVILLEKEAKLGgnSAKATSGingwGTRAQAKQ---------DVLDGGKFferdthls 482

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   72 ---------LYSAFSeFNNEDIIKFFENLGI------QLKEEDHGRMFPVTDKA------------QSVVDALLNRLkQL 124
Cdd:PTZ00306   483 gkgghcdpgLVKTLS-VKSADAISWLSSLGVpltvlsQLGGASRKRCHRAPDKKdgtpvpigftimRTLEDHIRTKL-SG 560

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  125 RVTIRTNEKIKSVLYE-----DG----QAAGIVTNNGEMIHSQS-------VIIAVGGKSVPHTG--------------- 173
Cdd:PTZ00306   561 RVTIMTETTVTSLLSEssarpDGvreiRVTGVRYKQASDASGQVmdlladaVILATGGFSNDHTPnsllreyapqlsgfp 640

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169125346  174 ------STGDGYEWAEAAGHTI-----TELFPTEVpVTSGEPFIKQKTLQGLSLRDVAVSVLNKKGK 229
Cdd:PTZ00306   641 ttngpwATGDGVKLARKLGATLvdmdkVQLHPTGL-IDPKDPSNRTKYLGPEALRGSGGVLLNKNGE 706
PRK12842 PRK12842
putative succinate dehydrogenase; Reviewed
 4-203 1.47e-05

putative succinate dehydrogenase; Reviewed


Pssm-ID: 237224 [Multi-domain]  Cd Length: 574  Bit Score: 46.99  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   4 YDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGNKLGRKLAISGG----------GRCNVTN-RLPVEEIIKHIPGNG--- 69
Cdd:PRK12842   10 CDVLVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGGTTAFSGGvlwipgnphaREAGVADsREAARTYLKHETGAFfda 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  70 -----------------------RFLYSAFSE---------------------------------------------FN- 80
Cdd:PRK12842   90 aaveafldngpemvefferetevKFVPTLYPDyhpdapggvdigrsilaapydirglgkdmarlrpplktitfigmmFNs 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  81 -NEDIIKFF-------------ENLGIQLKEED-HGRMFPVTDkAQSVVDALLNRLKQLRVTIRTNEKIKSVLYEDGQAA 145
Cdd:PRK12842  170 sNADLKHFFnatrsltsfiyvaKRLATHLKDLAlYRRGTQVTS-GNALAARLAKSALDLGIPILTGTPARELLTEGGRVV 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 146 GIVTNNG----EMIHSQSVIIAVGG---------KSVPH------------TGSTGDGYEWAEAAGHTITELFP------ 194
Cdd:PRK12842  249 GARVIDAggerRITARRGVVLACGGfshdlariaRAYPHlarggehlspvpAGNTGDGIRLAEAVGGAVDIRFPdaaawm 328

                         330
                  ....*....|.
gi 1169125346 195 --TEVPVTSGE 203
Cdd:PRK12842  329 pvSKVPLGGGR 339
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 4-39 2.29e-05

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: 46.48  E-value: 2.29e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1169125346   4 YDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKgNKLG 39
Cdd:TIGR01350   2 YDVIVIGGGPGGYVAAIRAAQLGLKVALVEK-EYLG 36
PRK12844 PRK12844
3-ketosteroid-delta-1-dehydrogenase; Reviewed
 4-48 2.40e-05

3-ketosteroid-delta-1-dehydrogenase; Reviewed


Pssm-ID: 183787 [Multi-domain]  Cd Length: 557  Bit Score: 46.29  E-value: 2.40e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1169125346   4 YDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGNKLGRKLAISGGG 48
Cdd:PRK12844    7 YDVVVVGSGGGGMCAALAAADSGLEPLIVEKQDKVGGSTAMSGGV 51
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 3-39 4.56e-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: 45.59  E-value: 4.56e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1169125346   3 QYDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGNKLG 39
Cdd:COG1232     1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVG 37
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 4-34 5.11e-05

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


Pssm-ID: 396193 [Multi-domain]  Cd Length: 348  Bit Score: 45.01  E-value: 5.11e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1169125346   4 YDVIVIGGGPSGLMAAIAAGEQGAGVLLIDK 34
Cdd:pfam01494   2 TDVLIVGGGPAGLMLALLLARAGVRVVLVER 32
sdhA PRK07803
succinate dehydrogenase flavoprotein subunit; Reviewed
 3-34 5.24e-05

succinate dehydrogenase flavoprotein subunit; Reviewed


Pssm-ID: 236101 [Multi-domain]  Cd Length: 626  Bit Score: 45.41  E-value: 5.24e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1169125346   3 QYDVIVIGGGPSGLMAAIAAGEQGAGVLLIDK 34
Cdd:PRK07803    8 SYDVVVIGAGGAGLRAAIEARERGLRVAVVCK 39
PTZ00052 PTZ00052
thioredoxin reductase; Provisional
 4-172 7.21e-05

thioredoxin reductase; Provisional


Pssm-ID: 185416 [Multi-domain]  Cd Length: 499  Bit Score: 44.81  E-value: 7.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   4 YDVIVIGGGPSGLMAAIAAGEQGAGVLLID--KGNKLGRKLAIsgGGRCnvTNRLPVEEIIKHipgngrflYSAfsefnn 81
Cdd:PTZ00052    6 YDLVVIGGGSGGMAAAKEAAAHGKKVALFDyvKPSTQGTKWGL--GGTC--VNVGCVPKKLMH--------YAA------ 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  82 ediikffeNLGIQLKEEDHGRMFPVTDKAQ--SVVDALLNRLKQLRVTIRTNEKIKSVLY-------EDGQAAGIVTNNG 152
Cdd:PTZ00052   68 --------NIGSIFHHDSQMYGWKTSSSFNwgKLVTTVQNHIRSLNFSYRTGLRSSKVEYinglaklKDEHTVSYGDNSQ 139

                         170       180
                  ....*....|....*....|..
gi 1169125346 153 EM-IHSQSVIIAVGGK-SVPHT 172
Cdd:PTZ00052  140 EEtITAKYILIATGGRpSIPED 161
TGR TIGR01438
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ...
 4-52 7.21e-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: 44.84  E-value: 7.21e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169125346   4 YDVIVIGGGPSGLMAAIAAGEQGAGVLLID--KGNKLGRKLAIsgGGRC-NV 52
Cdd:TIGR01438   3 YDLIVIGGGSGGLAAAKEAAAYGAKVMLLDfvTPTPLGTRWGI--GGTCvNV 52
PRK10157 PRK10157
putative oxidoreductase FixC; Provisional
 4-169 9.28e-05

putative oxidoreductase FixC; Provisional


Pssm-ID: 182273 [Multi-domain]  Cd Length: 428  Bit Score: 44.52  E-value: 9.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   4 YDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGNKLGRKlaisgggrcNVT-NRLPVEEIIKHIPGngrFLYSAFSE-FNN 81
Cdd:PRK10157    6 FDAIIVGAGLAGSVAALVLAREGAQVLVIERGNSAGAK---------NVTgGRLYAHSLEHIIPG---FADSAPVErLIT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  82 EDIIKFFENLGIQLKEEDHGRMFPVTDKAQSVV----DA-LLNRLKQLRVTIRTNEKIKSVLYEDGQAAGiVTNNGEMIH 156
Cdd:PRK10157   74 HEKLAFMTEKSAMTMDYCNGDETSPSQRSYSVLrskfDAwLMEQAEEAGAQLITGIRVDNLVQRDGKVVG-VEADGDVIE 152

                         170
                  ....*....|...
gi 1169125346 157 SQSVIIAVGGKSV 169
Cdd:PRK10157  153 AKTVILADGVNSI 165
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
8-39 1.32e-04

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 39.82  E-value: 1.32e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1169125346   8 VIGGGPSGLMAAIAAGEQGAGVLLIDKGNKLG 39
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLG 32
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 3-39 1.39e-04

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 43.98  E-value: 1.39e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1169125346   3 QYDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGnKLG 39
Cdd:PRK06416    4 EYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKE-KLG 39
PRK12843 PRK12843
FAD-dependent oxidoreductase;
4-48 1.40e-04

FAD-dependent oxidoreductase;


Pssm-ID: 237225 [Multi-domain]  Cd Length: 578  Bit Score: 43.96  E-value: 1.40e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1169125346   4 YDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGNKLGRKLAISGGG 48
Cdd:PRK12843   17 FDVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGTTATSAGT 61
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 4-36 2.36e-04

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: 42.69  E-value: 2.36e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1169125346   4 YDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGN 36
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEG 33
sdhA PRK08641
succinate dehydrogenase flavoprotein subunit; Reviewed
 1-32 3.99e-04

succinate dehydrogenase flavoprotein subunit; Reviewed


Pssm-ID: 236319 [Multi-domain]  Cd Length: 589  Bit Score: 42.65  E-value: 3.99e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1169125346   1 MKQYDVIVIGGGPSGLMAAIAAGEQGAGVLLI 32
Cdd:PRK08641    1 MAKGKVIVVGGGLAGLMATIKAAEAGVHVDLF 32
sdhA PRK05945
succinate dehydrogenase/fumarate reductase flavoprotein subunit;
1-186 4.15e-04

succinate dehydrogenase/fumarate reductase flavoprotein subunit;


Pssm-ID: 180319 [Multi-domain]  Cd Length: 575  Bit Score: 42.41  E-value: 4.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   1 MKQYDVIVIGGGPSGLMAA--IAAGEQGAGVLLIDKGNKL-GRKLAISGGGRCNVTNRLPVEEIIKH----IPGNGrFL- 72
Cdd:PRK05945    1 MLEHDVVIVGGGLAGCRAAleIKRLDPSLDVAVVAKTHPIrSHSVAAQGGIAASLKNVDPEDSWEAHafdtVKGSD-YLa 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  73 -YSAFSEFNNE--DIIKFFENLGIQLKE-ED------------HGRMFPVTDK-AQSVVDALLNRLKQLRVTIRTNEKIK 135
Cdd:PRK05945   80 dQDAVAILTQEapDVIIDLEHLGVLFSRlPDgriaqrafgghsHNRTCYAADKtGHAILHELVNNLRRYGVTIYDEWYVM 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169125346 136 SVLYEDGQAAGIV-----TNNGEMIHSQSVIIAVGGKS-VPHT-----GSTGDGYEWAEAAG 186
Cdd:PRK05945  160 RLILEDNQAKGVVmyhiaDGRLEVVRAKAVMFATGGYGrVFNTtsndyASTGDGLAMTAIAG 221
PRK08132 PRK08132
FAD-dependent oxidoreductase; Provisional
 6-39 5.34e-04

FAD-dependent oxidoreductase; Provisional


Pssm-ID: 236158 [Multi-domain]  Cd Length: 547  Bit Score: 42.16  E-value: 5.34e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1169125346   6 VIVIGGGPSGLMAAIAAGEQGAGVLLIDKGNKLG 39
Cdd:PRK08132   26 VVVVGAGPVGLALAIDLAQQGVPVVLLDDDDTLS 59
PRK06370 PRK06370
FAD-containing oxidoreductase;
1-35 5.77e-04

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 42.11  E-value: 5.77e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1169125346   1 MKQYDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKG 35
Cdd:PRK06370    3 AQRYDAIVIGAGQAGPPLAARAAGLGMKVALIERG 37
COG3573 COG3573
Predicted oxidoreductase [General function prediction only];
3-33 8.12e-04

Predicted oxidoreductase [General function prediction only];


Pssm-ID: 442794 [Multi-domain]  Cd Length: 551  Bit Score: 41.70  E-value: 8.12e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1169125346   3 QYDVIVIGGGPSGLMAAIAAGEQGAGVLLID 33
Cdd:COG3573     5 DADVIVVGAGLAGLVAAAELADAGRRVLLLD 35
glycerol3P_GlpB TIGR03378
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are ...
 4-35 8.49e-04

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


Pssm-ID: 213807  Cd Length: 419  Bit Score: 41.54  E-value: 8.49e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1169125346   4 YDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKG 35
Cdd:TIGR03378   1 FDVIIIGGGLAGLSCALRLAEAGKKCAIIAAG 32
PRK06753 PRK06753
hypothetical protein; Provisional
 6-179 1.84e-03

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 40.06  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   6 VIVIGGGPSGLMAAIAAGEQGAGVLLIDKGNKL---GRKLAISGggrcNVTNRLPVEEIIKHIPGNGRFLysafSEFN-- 80
Cdd:PRK06753    3 IAIIGAGIGGLTAAALLQEQGHEVKVFEKNESVkevGAGIGIGD----NVIKKLGNHDLAKGIKNAGQIL----STMNll 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  81 -------NEDIIKFFE-NLGIQlkeedhgrmfpvtdkAQSVVDALLNRLKQlrVTIRTNEKIKSVlYEDGQAAGIVTNNG 152
Cdd:PRK06753   75 ddkgtllNKVKLKSNTlNVTLH---------------RQTLIDIIKSYVKE--DAIFTGKEVTKI-ENETDKVTIHFADG 136

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1169125346 153 EMIHSQSVIIAVGGKSV------PHTGSTGDGY 179
Cdd:PRK06753  137 ESEAFDLCIGADGIHSKvrqsvnADSKVRYQGY 169
MnmG COG0445
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ...
 2-32 1.86e-03

tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440214 [Multi-domain]  Cd Length: 626  Bit Score: 40.37  E-value: 1.86e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1169125346   2 KQYDVIVIGGGPSGLMAAIAAGEQGAGVLLI 32
Cdd:COG0445     5 KEYDVIVVGGGHAGCEAALAAARMGAKTLLL 35
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
3-34 1.93e-03

bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 40.28  E-value: 1.93e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1169125346   3 QYDVIVIGGGPSGLMAAIAAGEQGAGVLLIDK 34
Cdd:PRK06183   10 DTDVVIVGAGPVGLTLANLLGQYGVRVLVLER 41
PRK07804 PRK07804
L-aspartate oxidase; Provisional
 5-35 2.08e-03

L-aspartate oxidase; Provisional


Pssm-ID: 236102 [Multi-domain]  Cd Length: 541  Bit Score: 40.34  E-value: 2.08e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1169125346   5 DVIVIGGGPSGLMAAIAAGEQGAGVLLIDKG 35
Cdd:PRK07804   18 DVVVVGSGVAGLTAALAARRAGRRVLVVTKA 48
PRK10015 PRK10015
oxidoreductase; Provisional
 3-67 2.58e-03

oxidoreductase; Provisional


Pssm-ID: 182194 [Multi-domain]  Cd Length: 429  Bit Score: 39.96  E-value: 2.58e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169125346   3 QYDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGNKLGRKlAISGGgrcnvtnRLPVEEIIKHIPG 67
Cdd:PRK10015    5 KFDAIVVGAGVAGSVAALVMARAGLDVLVIERGDSAGCK-NMTGG-------RLYAHTLEAIIPG 61
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
1-57 2.61e-03

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 39.90  E-value: 2.61e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169125346   1 MKQYDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGNKLgrklaisgGGRCnVTNRLP 57
Cdd:COG1231     5 ARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRV--------GGRV-WTLRFG 52
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 102-186 2.67e-03

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: 39.41  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346 102 RMFPVTDKAqsVVDALLNRLKQLRVTIRTNEKIKSVLYEDGqaAGIVTNNGEMIHSQSVIIAVGgkSVPHTgstgdgyEW 181
Cdd:COG0446   158 RLLGVLDPE--MAALLEEELREHGVELRLGETVVAIDGDDK--VAVTLTDGEEIPADLVVVAPG--VRPNT-------EL 224


                  ....*
gi 1169125346 182 AEAAG 186
Cdd:COG0446   225 AKDAG 229
PRK12845 PRK12845
3-ketosteroid-delta-1-dehydrogenase; Reviewed
 5-47 3.54e-03

3-ketosteroid-delta-1-dehydrogenase; Reviewed


Pssm-ID: 237226 [Multi-domain]  Cd Length: 564  Bit Score: 39.75  E-value: 3.54e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1169125346   5 DVIVIGGGpSGLMAAIAAGEQGAGVLLIDKGNKLGRKLAISGG 47
Cdd:PRK12845   18 DLLVVGSG-TGMAAALAAHELGLSVLIVEKSSYVGGSTARSGG 59
PFDH_like cd08282
Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde ...
 6-67 5.10e-03

Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. Unlike typical FDH, Pseudomonas putida aldehyde-dismutating FDH (PFDH) is glutathione-independent. PFDH converts 2 molecules of aldehydes to corresponding carboxylic acid and alcohol. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like the zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. Unlike ADH, where NAD(P)(H) acts as a cofactor, NADH in FDH is a tightly bound redox cofactor (similar to nicotinamide proteins). The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176242 [Multi-domain]  Cd Length: 375  Bit Score: 38.73  E-value: 5.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169125346   6 VIVIGGGPSGLMAAIAAGEQGAG-VLLIDKgNKLGRKLAISGGgrC---NVTNRLPVEEIIKHIPG 67
Cdd:cd08282   180 VAVFGAGPVGLMAAYSAILRGASrVYVVDH-VPERLDLAESIG--AipiDFSDGDPVEQILGLEPG 242
PRK08849 PRK08849
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
 1-33 6.09e-03

2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional


Pssm-ID: 181564 [Multi-domain]  Cd Length: 384  Bit Score: 38.60  E-value: 6.09e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1169125346   1 MKQYDVIVIGGGPSGLMAAIAAGEQGAGVLLID 33
Cdd:PRK08849    1 MNKYDIAVVGGGMVGAATALGFAKQGRSVAVIE 33
PRK06126 PRK06126
hypothetical protein; Provisional
 5-35 6.52e-03

hypothetical protein; Provisional


Pssm-ID: 235704 [Multi-domain]  Cd Length: 545  Bit Score: 38.82  E-value: 6.52e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1169125346   5 DVIVIGGGPSGLMAAIAAGEQGAGVLLIDKG 35
Cdd:PRK06126    9 PVLIVGGGPVGLALALDLGRRGVDSILVERK 39
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 6-169 8.43e-03

ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 37.67  E-value: 8.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   6 VIVIGGGPSGLMAAIAAGEQGAGV----LLIDKGNKLGRKLAISGggrcnvTNRLPVEEIIK-----HIpgngrflysAF 76
Cdd:COG0614     3 IVSLSPSATELLLALGAGDRLVGVsdwgYCDYPELELKDLPVVGG------TGEPNLEAILAlkpdlVL---------AS 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  77 SEFNNEDIIKFFENLGI-----------QLKE--EDHGRMFPVTDKAQSVVDALLNRLKQLRVTIRTNEKIKSVLYEDGQ 143
Cdd:COG0614    68 SSGNDEEDYEQLEKIGIpvvvldprsleDLYEsiRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWS 147

                         170       180
                  ....*....|....*....|....*.
gi 1169125346 144 AAGIVTNNGEMIHSQsVIIAVGGKSV 169
Cdd:COG0614   148 GDPLYTAGGGSFIGE-LLELAGGRNV 172
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 6-69 8.75e-03

NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol dehydrogenases and other sugar dehydrogenases of the medium-chain dehydrogenase/reductase family (MDR), which includes zinc-dependent alcohol dehydrogenase and related proteins. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Related proteins include threonine dehydrogenase, formaldehyde dehydrogenase, and butanediol dehydrogenase. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Horse liver alcohol dehydrogenase is a dimeric enzyme and each subunit has two domains. The NAD binding domain is in a Rossmann fold and the catalytic domain contains a zinc ion to which substrates bind. There is a cleft between the domains that closes upon formation of the ternary complex.


Pssm-ID: 176198 [Multi-domain]  Cd Length: 343  Bit Score: 37.98  E-value: 8.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169125346   6 VIVIGGGPSGLMAAIAAGEQGAG-VLLIDKGnklGRKLAIS---GGGRCNVTNRLPVEEIIKHIPGNG 69
Cdd:cd08236   163 VVVIGAGTIGLLAIQWLKILGAKrVIAVDID---DEKLAVArelGADDTINPKEEDVEKVRELTEGRG 227
PRK09126 PRK09126
FAD-dependent hydroxylase;
1-34 8.82e-03

FAD-dependent hydroxylase;


Pssm-ID: 236385 [Multi-domain]  Cd Length: 392  Bit Score: 38.00  E-value: 8.82e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1169125346   1 MKQYDVIVIGGGPSGLMAAIAAGEQGAGVLLIDK 34
Cdd:PRK09126    1 MMHSDIVVVGAGPAGLSFARSLAGSGLKVTLIER 34
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
 6-33 9.13e-03

Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; Glutathione-dependent formaldehyde dehydrogenases (FDHs) are members of the zinc-dependent/medium chain alcohol dehydrogenase family. Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD to formate and NADH. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. These tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176244 [Multi-domain]  Cd Length: 344  Bit Score: 38.01  E-value: 9.13e-03
                          10        20
                  ....*....|....*....|....*....
gi 1169125346   6 VIVIGGGPSGLMAAIAAGEQGAG-VLLID 33
Cdd:cd08284   171 VAVIGCGPVGLCAVLSAQVLGAArVFAVD 199
PRK08401 PRK08401
L-aspartate oxidase; Provisional
 6-168 9.57e-03

L-aspartate oxidase; Provisional


Pssm-ID: 236259 [Multi-domain]  Cd Length: 466  Bit Score: 38.24  E-value: 9.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346   6 VIVIGGGPSGLMAAIAAGEQGAGVLLIDKG-NKLGRKLAISGGGrcnvtnrLPVEE---IIKHIPGN---GRFLysafse 78
Cdd:PRK08401    4 VGIVGGGLAGLTAAISLAKKGFDVTIIGPGiKKSNSYLAQAGIA-------FPILEgdsIRAHVLDTiraGKYI------ 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169125346  79 fNNEDII-----------KFFENLGIQL--KEEDHGRMFP--VTDKAQS---VVDALLNRLKQLRVTIrTNEKIKSVLYE 140
Cdd:PRK08401   71 -NDEEVVwnvisksseayDFLTSLGLEFegNELEGGHSFPrvFTIKNETgkhIIKILYKHARELGVNF-IRGFAEELAIK 148

                         170       180
                  ....*....|....*....|....*...
gi 1169125346 141 DGQAAGIVTnNGEMIHSQSVIIAVGGKS 168
Cdd:PRK08401  149 NGKAYGVFL-DGELLKFDATVIATGGFS 175
PRK12834 PRK12834
putative FAD-binding dehydrogenase; Reviewed
 1-36 9.79e-03

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 183782 [Multi-domain]  Cd Length: 549  Bit Score: 37.96  E-value: 9.79e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1169125346   1 MKQYDVIVIGGGPSGLMAAIAAGEQGAGVLLIDKGN 36
Cdd:PRK12834    2 AMDADVIVVGAGLAGLVAAAELADAGKRVLLLDQEN 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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