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Conserved domains on  [gi|637168615|ref|WP_024426195|]
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MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Bacillus]

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: 584.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615    4 YDVIVIGGGPSGLMAAIASAEHGATVLLIDKGNKLGRKLAISGGGRCNVTN-RLPVEEIIKHIPGNGRFLYSAFSEFNNE 82
Cdd:pfam03486   1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLGRKILISGGGRCNVTNlSEEPDNFLSRYPGNPKFLKSALSRFTPW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   83 DIISFFENLGIELKEEDHGRMFPVSNKAQSVVDALLDRLRALNVTIRTNEKIKTVLYQDGQAAGIVTNNdEKISSKSVVI 162
Cdd:pfam03486  81 DFIAFFESLGVPLKEEDHGRLFPDSDKASDIVDALLNELKELGVKIRLRTRVLSVEKDDDGRFRVKTGG-EELEADSLVL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  163 AVGGKSVPHTGSTGDGYAWAEAAGHTITELFPTEVPVTSDERFIKEKVLQGLSLRSVAVSvlnkKGKPVVTHVMDMIFTH 242
Cdd:pfam03486 160 ATGGLSWPKTGSTGFGYPLAEQFGHTIIPLRPALVPFTIDEPFLFLKRLSGISLKNVVLS----NGKGGITFRGELLFTH 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  243 FGLSGPAVLRCSGFVVKELKKQPTVRLQIDLYPKLNDEELFQKLHRDLKDEPKKAIKNVLKSWMQERYLLFLLERNGIDP 322
Cdd:pfam03486 236 RGLSGPAILQLSSYWRRAILKKGGVTLSIDLLPDLDAEELAARLEKPRGAHPKKSLKNSLAGLLPKRLAEFLLEQAGIEP 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  323 QDTFSGLAKDKLRAFAHDCKHFIVHANGTLSLDKAFVTGGGVSVKEIEPKKMASKKMPGLYFCGEILDIHGYTGGYNITS 402
Cdd:pfam03486 316 DKKLAQLSKKELAALAQLLKAWTFTPNGTEGYRTAEVTAGGVDTKELSSKTMESKKVPGLFFAGEVLDVDGWTGGYNLQW 395

                         410
                  ....*....|.
gi 637168615  403 ALVTGRLAGMN 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: 584.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615    4 YDVIVIGGGPSGLMAAIASAEHGATVLLIDKGNKLGRKLAISGGGRCNVTN-RLPVEEIIKHIPGNGRFLYSAFSEFNNE 82
Cdd:pfam03486   1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLGRKILISGGGRCNVTNlSEEPDNFLSRYPGNPKFLKSALSRFTPW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   83 DIISFFENLGIELKEEDHGRMFPVSNKAQSVVDALLDRLRALNVTIRTNEKIKTVLYQDGQAAGIVTNNdEKISSKSVVI 162
Cdd:pfam03486  81 DFIAFFESLGVPLKEEDHGRLFPDSDKASDIVDALLNELKELGVKIRLRTRVLSVEKDDDGRFRVKTGG-EELEADSLVL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  163 AVGGKSVPHTGSTGDGYAWAEAAGHTITELFPTEVPVTSDERFIKEKVLQGLSLRSVAVSvlnkKGKPVVTHVMDMIFTH 242
Cdd:pfam03486 160 ATGGLSWPKTGSTGFGYPLAEQFGHTIIPLRPALVPFTIDEPFLFLKRLSGISLKNVVLS----NGKGGITFRGELLFTH 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  243 FGLSGPAVLRCSGFVVKELKKQPTVRLQIDLYPKLNDEELFQKLHRDLKDEPKKAIKNVLKSWMQERYLLFLLERNGIDP 322
Cdd:pfam03486 236 RGLSGPAILQLSSYWRRAILKKGGVTLSIDLLPDLDAEELAARLEKPRGAHPKKSLKNSLAGLLPKRLAEFLLEQAGIEP 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  323 QDTFSGLAKDKLRAFAHDCKHFIVHANGTLSLDKAFVTGGGVSVKEIEPKKMASKKMPGLYFCGEILDIHGYTGGYNITS 402
Cdd:pfam03486 316 DKKLAQLSKKELAALAQLLKAWTFTPNGTEGYRTAEVTAGGVDTKELSSKTMESKKVPGLFFAGEVLDVDGWTGGYNLQW 395

                         410
                  ....*....|.
gi 637168615  403 ALVTGRLAGMN 413
Cdd:pfam03486 396 AWSSGYAAGQG 406
YhiN COG2081
Predicted flavoprotein YhiN [General function prediction only];
7-415 0e+00

Predicted flavoprotein YhiN [General function prediction only];


Pssm-ID: 441684 [Multi-domain]  Cd Length: 402  Bit Score: 565.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   7 IVIGGGPSGLMAAIASAEHGATVLLIDKGNKLGRKLAISGGGRCNVTNRLPVEEIIKHIPGNGRFLYSAFSEFNNEDIIS 86
Cdd:COG2081    1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVGRKILISGGGRCNFTNSEPLPEFLNYYGGNPHFLKSALSRFTPEDLIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  87 FFENLGIELKEEDHGRMFPVSNKAQSVVDALLDRLRALNVTIRTNEKIKTVLYQDGqAAGIVTNNDEKISSKSVVIAVGG 166
Cdd:COG2081   81 FFEGLGIETKEESSGRVFPDSSKASDILRALLAELREAGVEIRLRTRVTGIEKEDG-GFGVETPDGETVRADAVVLATGG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615 167 KSVPHTGSTGDGYAWAEAAGHTITELFPTEVPVTSDERFIKEkvLQGLSLRSVAVSVlnkKGKPVVTHVMDMIFTHFGLS 246
Cdd:COG2081  160 LSYPKLGSTGDGYRLAEQFGHTITPLRPALVPLTLSEHFFKR--LAGLSLKNVALSV---GGKKIASFRGELLFTHRGLS 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615 247 GPAVLRCSGFVVKELKKqPTVRLQIDLYPKLNDEELFQKLHRDLKDEPKKAIKNVLKSWMQERYLLFLLERngIDPQDTF 326
Cdd:COG2081  235 GPAILQLSSYWRDALKK-GGATLTIDLLPDLDLEELDARLARPREKNGKKSLKNVLRGLLPKRLAALLLEL--ADPDKPL 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615 327 SGLAKDKLRAFAHDCKHFIVHANGTLSLDKAFVTGGGVSVKEIEPKKMASKKMPGLYFCGEILDIHGYTGGYNITSALVT 406
Cdd:COG2081  312 AQLSKKEREALAALLKAWPLTPTGTRGYDEAIVTAGGVDTKELDPKTMESKKVPGLYFAGEVLDVDGPTGGYNLQWAWSS 391


                 ....*....
gi 637168615 407 GRLAGMNAA 415
Cdd:COG2081  392 GYAAGQAAA 400
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: 525.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615    7 IVIGGGPSGLMAAIASAEHGATVLLIDKGNKLGRKLAISGGGRCNVTNRLPVEEIIKHIPGNGRFLYSAFSEFNNEDIIS 86
Cdd:TIGR00275   1 IIIGGGAAGLMAAITAARAGLSVLLLEKNKKIGKKLLISGGGRCNLTNSCPTPEFVAYYPRNGKFLRSALSRFSNKDLID 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   87 FFENLGIELKEEDHGRMFPVSNKAQSVVDALLDRLRALNVTIRTNEKIKTVlYQDGQAAGIVTNnDEKISSKSVVIAVGG 166
Cdd:TIGR00275  81 FFESLGLELKVEEDGRVFPCSDSAADVLDALLNELKELGVEILTNSKVKSI-EKEDGGFGVETS-GGEYEADKVIIATGG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  167 KSVPHTGSTGDGYAWAEAAGHTITELFPTEVPVTSDERFIKEkvLQGLSLRSVAVSVLNkkGKPVVTHVMDMIFTHFGLS 246
Cdd:TIGR00275 159 LSYPQLGSTGDGYEIAESLGHTIVPPVPALVPLTLDESFLKE--LSGISLDGVVLSLVN--GKKVLEEFGELLFTHFGLS 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  247 GPAVLRCSGFVVKELKKQPTVRLQIDLYPKLNDEELFQKLHRDLKDEPKKAIKNVLKSWMQERYLLFLLERNGIDPQDTF 326
Cdd:TIGR00275 235 GPAILDLSAFAARALLKHKGVELEIDLLPDLSEEELEQRLKRLRKSNPKKTVKNILKGLLPKRLAELLLEQLGIDPDLPA 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  327 SGLAKDKLRAFAHDCKHFIVHANGTLSLDKAFVTGGGVSVKEIEPKKMASKKMPGLYFCGEILDIHGYTGGYNITSALVT 406
Cdd:TIGR00275 315 AQLSKKEIKKLVQLLKNWPFTISGTRGFKEAEVTAGGVSLKEINPKTMESKLVPGLYFAGEVLDIDGDTGGYNLQWAWSS 394


                  ....*.
gi 637168615  407 GRLAGM 412
Cdd:TIGR00275 395 GYLAGK 400
PRK08274 PRK08274
FAD-dependent tricarballylate dehydrogenase TcuA;
1-418 3.51e-12

FAD-dependent tricarballylate dehydrogenase TcuA;


Pssm-ID: 236214 [Multi-domain]  Cd Length: 466  Bit Score: 67.98  E-value: 3.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   1 MKHYDVIVIGGGPSGLMAAIASAEHGATVLLIDKGNK--LGRKLAISGGGRCN-------VTNRLPVEE----IIKHIPG 67
Cdd:PRK08274   2 ASMVDVLVIGGGNAALCAALAAREAGASVLLLEAAPRewRGGNSRHTRNLRCMhdapqdvLVGAYPEEEfwqdLLRVTGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  68 NG-----RFLYSAFSefnneDIISFFENLGIELKEEDHGRMFPVSNKAQ------SVVDALLDRLRALNVTIRTNEKIKT 136
Cdd:PRK08274  82 RTdealaRLLIRESS-----DCRDWMRKHGVRFQPPLSGALHVARTNAFfwgggkALVNALYRSAERLGVEIRYDAPVTA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615 137 VLYQDGQAAGIVTNND----EKISSKSVVIAVGG---------------------KSVPHtgSTGDGY-----AWAEAAG 186
Cdd:PRK08274 157 LELDDGRFVGARAGSAaggaERIRAKAVVLAAGGfesnrewlreawgqpadnflvRGTPY--NQGDLLkalldAGADRIG 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615 187 HtitelfPTE---VPVtsDERFIKEKVlqGLSLRSVAVS---VLNKKGKPVVTHVMDMIFTHFGLSGPAVLRCSG---FV 257
Cdd:PRK08274 235 D------PSQchaVAI--DARAPLYDG--GICTRIDCVPlgiVVNRDGERFYDEGEDFWPKRYAIWGRLVAQQPGqiaYQ 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615 258 VKELKKQPtvRLQIDLYPKLND---EELFQKLHRDlkdepkkaiknvlkswmQERYLLFLLERNGIDPQDTFSGLAKDkl 334
Cdd:PRK08274 305 IFDAKAIG--RFMPPVFPPIQAdtlEELAEKLGLD-----------------PAAFLRTVAAFNAAVRPGPFDPTVLD-- 363

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615 335 rafahDCKHFIVH---ANGTLSLDKA-FV----------TGGGVSVKEIEPKKMASKK-MPGLYFCGEIL--DI--HGYT 395
Cdd:PRK08274 364 -----DCGTEGLTppkSHWARPIDTPpFYaypvrpgitfTYLGLKVDEDARVRFADGRpSPNLFAAGEMMagNVlgKGYP 438

                        490       500
                 ....*....|....*....|...
gi 637168615 396 GGYNITSALVTGRLAGMNAALEA 418
Cdd:PRK08274 439 AGVGLTIGAVFGRIAGEEAARHA 461
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
 6-33 9.90e-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: 9.90e-03
                         10        20
                 ....*....|....*....|....*....
gi 637168615   6 VIVIGGGPSGLMAAIASAEHGA-TVLLID 33
Cdd:cd08284  171 VAVIGCGPVGLCAVLSAQVLGAaRVFAVD 199
 
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: 584.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615    4 YDVIVIGGGPSGLMAAIASAEHGATVLLIDKGNKLGRKLAISGGGRCNVTN-RLPVEEIIKHIPGNGRFLYSAFSEFNNE 82
Cdd:pfam03486   1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLGRKILISGGGRCNVTNlSEEPDNFLSRYPGNPKFLKSALSRFTPW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   83 DIISFFENLGIELKEEDHGRMFPVSNKAQSVVDALLDRLRALNVTIRTNEKIKTVLYQDGQAAGIVTNNdEKISSKSVVI 162
Cdd:pfam03486  81 DFIAFFESLGVPLKEEDHGRLFPDSDKASDIVDALLNELKELGVKIRLRTRVLSVEKDDDGRFRVKTGG-EELEADSLVL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  163 AVGGKSVPHTGSTGDGYAWAEAAGHTITELFPTEVPVTSDERFIKEKVLQGLSLRSVAVSvlnkKGKPVVTHVMDMIFTH 242
Cdd:pfam03486 160 ATGGLSWPKTGSTGFGYPLAEQFGHTIIPLRPALVPFTIDEPFLFLKRLSGISLKNVVLS----NGKGGITFRGELLFTH 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  243 FGLSGPAVLRCSGFVVKELKKQPTVRLQIDLYPKLNDEELFQKLHRDLKDEPKKAIKNVLKSWMQERYLLFLLERNGIDP 322
Cdd:pfam03486 236 RGLSGPAILQLSSYWRRAILKKGGVTLSIDLLPDLDAEELAARLEKPRGAHPKKSLKNSLAGLLPKRLAEFLLEQAGIEP 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  323 QDTFSGLAKDKLRAFAHDCKHFIVHANGTLSLDKAFVTGGGVSVKEIEPKKMASKKMPGLYFCGEILDIHGYTGGYNITS 402
Cdd:pfam03486 316 DKKLAQLSKKELAALAQLLKAWTFTPNGTEGYRTAEVTAGGVDTKELSSKTMESKKVPGLFFAGEVLDVDGWTGGYNLQW 395

                         410
                  ....*....|.
gi 637168615  403 ALVTGRLAGMN 413
Cdd:pfam03486 396 AWSSGYAAGQG 406
YhiN COG2081
Predicted flavoprotein YhiN [General function prediction only];
7-415 0e+00

Predicted flavoprotein YhiN [General function prediction only];


Pssm-ID: 441684 [Multi-domain]  Cd Length: 402  Bit Score: 565.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   7 IVIGGGPSGLMAAIASAEHGATVLLIDKGNKLGRKLAISGGGRCNVTNRLPVEEIIKHIPGNGRFLYSAFSEFNNEDIIS 86
Cdd:COG2081    1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVGRKILISGGGRCNFTNSEPLPEFLNYYGGNPHFLKSALSRFTPEDLIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  87 FFENLGIELKEEDHGRMFPVSNKAQSVVDALLDRLRALNVTIRTNEKIKTVLYQDGqAAGIVTNNDEKISSKSVVIAVGG 166
Cdd:COG2081   81 FFEGLGIETKEESSGRVFPDSSKASDILRALLAELREAGVEIRLRTRVTGIEKEDG-GFGVETPDGETVRADAVVLATGG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615 167 KSVPHTGSTGDGYAWAEAAGHTITELFPTEVPVTSDERFIKEkvLQGLSLRSVAVSVlnkKGKPVVTHVMDMIFTHFGLS 246
Cdd:COG2081  160 LSYPKLGSTGDGYRLAEQFGHTITPLRPALVPLTLSEHFFKR--LAGLSLKNVALSV---GGKKIASFRGELLFTHRGLS 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615 247 GPAVLRCSGFVVKELKKqPTVRLQIDLYPKLNDEELFQKLHRDLKDEPKKAIKNVLKSWMQERYLLFLLERngIDPQDTF 326
Cdd:COG2081  235 GPAILQLSSYWRDALKK-GGATLTIDLLPDLDLEELDARLARPREKNGKKSLKNVLRGLLPKRLAALLLEL--ADPDKPL 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615 327 SGLAKDKLRAFAHDCKHFIVHANGTLSLDKAFVTGGGVSVKEIEPKKMASKKMPGLYFCGEILDIHGYTGGYNITSALVT 406
Cdd:COG2081  312 AQLSKKEREALAALLKAWPLTPTGTRGYDEAIVTAGGVDTKELDPKTMESKKVPGLYFAGEVLDVDGPTGGYNLQWAWSS 391


                 ....*....
gi 637168615 407 GRLAGMNAA 415
Cdd:COG2081  392 GYAAGQAAA 400
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: 525.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615    7 IVIGGGPSGLMAAIASAEHGATVLLIDKGNKLGRKLAISGGGRCNVTNRLPVEEIIKHIPGNGRFLYSAFSEFNNEDIIS 86
Cdd:TIGR00275   1 IIIGGGAAGLMAAITAARAGLSVLLLEKNKKIGKKLLISGGGRCNLTNSCPTPEFVAYYPRNGKFLRSALSRFSNKDLID 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   87 FFENLGIELKEEDHGRMFPVSNKAQSVVDALLDRLRALNVTIRTNEKIKTVlYQDGQAAGIVTNnDEKISSKSVVIAVGG 166
Cdd:TIGR00275  81 FFESLGLELKVEEDGRVFPCSDSAADVLDALLNELKELGVEILTNSKVKSI-EKEDGGFGVETS-GGEYEADKVIIATGG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  167 KSVPHTGSTGDGYAWAEAAGHTITELFPTEVPVTSDERFIKEkvLQGLSLRSVAVSVLNkkGKPVVTHVMDMIFTHFGLS 246
Cdd:TIGR00275 159 LSYPQLGSTGDGYEIAESLGHTIVPPVPALVPLTLDESFLKE--LSGISLDGVVLSLVN--GKKVLEEFGELLFTHFGLS 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  247 GPAVLRCSGFVVKELKKQPTVRLQIDLYPKLNDEELFQKLHRDLKDEPKKAIKNVLKSWMQERYLLFLLERNGIDPQDTF 326
Cdd:TIGR00275 235 GPAILDLSAFAARALLKHKGVELEIDLLPDLSEEELEQRLKRLRKSNPKKTVKNILKGLLPKRLAELLLEQLGIDPDLPA 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  327 SGLAKDKLRAFAHDCKHFIVHANGTLSLDKAFVTGGGVSVKEIEPKKMASKKMPGLYFCGEILDIHGYTGGYNITSALVT 406
Cdd:TIGR00275 315 AQLSKKEIKKLVQLLKNWPFTISGTRGFKEAEVTAGGVSLKEINPKTMESKLVPGLYFAGEVLDIDGDTGGYNLQWAWSS 394


                  ....*.
gi 637168615  407 GRLAGM 412
Cdd:TIGR00275 395 GYLAGK 400
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 1-420 2.52e-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: 101.45  E-value: 2.52e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   1 MKHYDVIVIGGGPSGLMAAIASAEHGATVLLIDKGNKLGRKLAISGGGrCNVTN------------RLPVEEIIKhipgN 68
Cdd:COG1053    1 DHEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGGHTAAAQGG-INAAGtnvqkaagedspEEHFYDTVK----G 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  69 GRFLYS-----AFSEfNNEDIISFFENLGIELKEEDHGR------------MFPVSNKAQSVVDALLDRLRALNVTIRTN 131
Cdd:COG1053   76 GDGLADqdlveALAE-EAPEAIDWLEAQGVPFSRTPDGRlpqfgghsvgrtCYAGDGTGHALLATLYQAALRLGVEIFTE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615 132 EKIKTVLYQDGQAAGIVTNND----EKISSKSVVIAVGG------------------KSVPHTGSTGDGYAWAEAAG--- 186
Cdd:COG1053  155 TEVLDLIVDDGRVVGVVARDRtgeiVRIRAKAVVLATGGfgrnyemraeylpeaegaLSTNAPGNTGDGIAMALRAGaal 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615 187 --------HtitelfPTEVPVTSderfikekVLQGLSLRSVAVSVL-NKKGK---------PVVTH------------VM 236
Cdd:COG1053  235 admefvqfH------PTGLPGDG--------GLISEGARGKPGGILvNKEGErfmneyaprDVVSRaileeidepaylVL 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615 237 DmiFTHFGLsgPAVLRCSGFVVKElkkqPTVrlqidlypklndEELFQKLhrdlkDEPKKAIKNVLKSWMQeryllflLE 316
Cdd:COG1053  301 D--LRHRRR--LEEYLEAGYLVKA----DTI------------EELAAKL-----GIDAAELAATVARYNA-------AA 348

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615 317 RNGIDPQDTFSGLAKD------KLRAFAHdckhfivhanGTLsldkafvtgGGVSV--------KEIEPkkmaskkMPGL 382
Cdd:COG1053  349 KAGVDPRGTCLGPIKEgpfyaiPVRPGVH----------YTM---------GGLRVdadarvldADGTP-------IPGL 402

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|.
gi 637168615 383 YFCGEIL-DIHG--YTGGYNITSALVTGRLAGMNAALEAKE 420
Cdd:COG1053  403 YAAGEAAgSVHGanRLGGNSLGDALVFGRIAGRHAAEYAKA 443
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 5-198 1.77e-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: 80.79  E-value: 1.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615    5 DVIVIGGGPSGLMAAIASAEHGATVLLIDKGNKLGRKLAISGGGRC--NVTNRLPVEEIIKHIpgngRFLYSAFSEFNNE 82
Cdd:pfam00890   1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGATAWSSGGIDalGNPPQGGIDSPELHP----TDTLKGLDELADH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   83 DI-----------ISFFENLGIELKEEDHGR---------------MFPVSNK------AQSVVDALLDRLRALNVTIRT 130
Cdd:pfam00890  77 PYveafveaapeaVDWLEALGVPFSRTEDGHldlrplgglsatwrtPHDAADRrrglgtGHALLARLLEGLRKAGVDFQP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  131 NEKIKTVLYQDGQAAGIVTNNDEK------ISSKSVVIAVGGKSVPHT---------------GSTGDGYAWAEAAGHTI 189
Cdd:pfam00890 157 RTAADDLIVEDGRVTGAVVENRRNgrevriRAIAAVLLATGGFGRLAElllpaagyadttnppANTGDGLALALRAGAAL 236


                  ....*....
gi 637168615  190 TELFPTEVP 198
Cdd:pfam00890 237 TDDLMEFVQ 245
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 1-169 7.92e-15

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: 74.97  E-value: 7.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   1 MKHYDVIVIGGGPSGLMAAIASAEHGATVLLIDK---GNKLGRKLAISGGG-----RCNVTNRL-----PVEEIIKHIPG 67
Cdd:COG0654    1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVERappPRPDGRGIALSPRSlellrRLGLWDRLlargaPIRGIRVRDGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  68 NGRFLYSafsefnnediisffenlgIELKEEDHGRMFPVSNKAqsVVDALLDRLRALNVTIRTNEKIKTVLyQDGQAAGI 147
Cdd:COG0654   81 DGRVLAR------------------FDAAETGLPAGLVVPRAD--LERALLEAARALGVELRFGTEVTGLE-QDADGVTV 139

                        170       180
                 ....*....|....*....|..
gi 637168615 148 VTNNDEKISSKSVVIAVGGKSV 169
Cdd:COG0654  140 TLADGRTLRADLVVGADGARSA 161
PRK08274 PRK08274
FAD-dependent tricarballylate dehydrogenase TcuA;
1-418 3.51e-12

FAD-dependent tricarballylate dehydrogenase TcuA;


Pssm-ID: 236214 [Multi-domain]  Cd Length: 466  Bit Score: 67.98  E-value: 3.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   1 MKHYDVIVIGGGPSGLMAAIASAEHGATVLLIDKGNK--LGRKLAISGGGRCN-------VTNRLPVEE----IIKHIPG 67
Cdd:PRK08274   2 ASMVDVLVIGGGNAALCAALAAREAGASVLLLEAAPRewRGGNSRHTRNLRCMhdapqdvLVGAYPEEEfwqdLLRVTGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  68 NG-----RFLYSAFSefnneDIISFFENLGIELKEEDHGRMFPVSNKAQ------SVVDALLDRLRALNVTIRTNEKIKT 136
Cdd:PRK08274  82 RTdealaRLLIRESS-----DCRDWMRKHGVRFQPPLSGALHVARTNAFfwgggkALVNALYRSAERLGVEIRYDAPVTA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615 137 VLYQDGQAAGIVTNND----EKISSKSVVIAVGG---------------------KSVPHtgSTGDGY-----AWAEAAG 186
Cdd:PRK08274 157 LELDDGRFVGARAGSAaggaERIRAKAVVLAAGGfesnrewlreawgqpadnflvRGTPY--NQGDLLkalldAGADRIG 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615 187 HtitelfPTE---VPVtsDERFIKEKVlqGLSLRSVAVS---VLNKKGKPVVTHVMDMIFTHFGLSGPAVLRCSG---FV 257
Cdd:PRK08274 235 D------PSQchaVAI--DARAPLYDG--GICTRIDCVPlgiVVNRDGERFYDEGEDFWPKRYAIWGRLVAQQPGqiaYQ 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615 258 VKELKKQPtvRLQIDLYPKLND---EELFQKLHRDlkdepkkaiknvlkswmQERYLLFLLERNGIDPQDTFSGLAKDkl 334
Cdd:PRK08274 305 IFDAKAIG--RFMPPVFPPIQAdtlEELAEKLGLD-----------------PAAFLRTVAAFNAAVRPGPFDPTVLD-- 363

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615 335 rafahDCKHFIVH---ANGTLSLDKA-FV----------TGGGVSVKEIEPKKMASKK-MPGLYFCGEIL--DI--HGYT 395
Cdd:PRK08274 364 -----DCGTEGLTppkSHWARPIDTPpFYaypvrpgitfTYLGLKVDEDARVRFADGRpSPNLFAAGEMMagNVlgKGYP 438

                        490       500
                 ....*....|....*....|...
gi 637168615 396 GGYNITSALVTGRLAGMNAALEA 418
Cdd:PRK08274 439 AGVGLTIGAVFGRIAGEEAARHA 461
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 5-186 5.55e-12

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


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 66.86  E-value: 5.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615    5 DVIVIGGGPSGLMAAIASAEHGATVLLIDKGNKLGRKLaiSGGGRCNVTNRLpveeiIKHIPGNGRFlysaFSEFNNedi 84
Cdd:pfam12831   1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGML--TSGLVGPDMGFY-----LNKEQVVGGI----AREFRQ--- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   85 isffenlgiELKEEDHGRMFPVSNKAQSVVD------ALLDRLRALNVTIRTNEKIKTVLYQDGQAAGIVTNNDEK---I 155
Cdd:pfam12831  67 ---------RLRARGGLPGPYGLRGGWVPFDpevakaVLDEMLAEAGVTVLLHTRVVGVVKEGGRITGVTVETKGGritI 137

                         170       180       190
                  ....*....|....*....|....*....|.
gi 637168615  156 SSKSVVIAvggksvphtgsTGDGyAWAEAAG 186
Cdd:pfam12831 138 RAKVFIDA-----------TGDG-DLAALAG 156
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 1-198 9.21e-11

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: 63.18  E-value: 9.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   1 MKHYDVIVIGGGPSGLMAAIASAEHGATVLLIDKGNklgrklaisGGGRCnvTNRlpveeiikhipgnG-----RFLYSA 75
Cdd:COG1249    1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGR---------LGGTC--LNV-------------GcipskALLHAA 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  76 --FSEFNNediisfFENLGIELKEE--DHGRMFpvsNKAQSVVDAL----LDRLRALNVTIRtnekiktvlyqDGQA--A 145
Cdd:COG1249   57 evAHEARH------AAEFGISAGAPsvDWAALM---ARKDKVVDRLrggvEELLKKNGVDVI-----------RGRArfV 116

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 637168615 146 G---IVTNNDEKISSKSVVIAVGGKSV--PHTGSTGDGYawaeaagHTITELF-PTEVP 198
Cdd:COG1249  117 DphtVEVTGGETLTADHIVIATGSRPRvpPIPGLDEVRV-------LTSDEALeLEELP 168
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
4-165 4.81e-10

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 60.13  E-value: 4.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   4 YDVIVIGGGPSGLMAAIASAEHGATVLLIDKGNKlgrklaisgGGRCNVTnrlpveeiiKHIpgngrflysafsefnnED 83
Cdd:COG0492    1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEP---------GGQLATT---------KEI----------------EN 46

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  84 IISFFENL-GIELkeedhgrmfpvsnkaqsvVDALLDRLRALNVTIRTnEKIKTVlYQDGQAAGIVTNNDEKISSKSVVI 162
Cdd:COG0492   47 YPGFPEGIsGPEL------------------AERLREQAERFGAEILL-EEVTSV-DKDDGPFRVTTDDGTEYEAKAVII 106


                 ...
gi 637168615 163 AVG 165
Cdd:COG0492  107 ATG 109
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
11-163 5.72e-10

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 59.98  E-value: 5.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  11 GGPSGLMAAIASAEHGATVLLIDKGNKLGRKlaISGGGrcnvtnRLP--VEEIIkhIPGNGRFLYSAFSEFnnediisff 88
Cdd:COG0644    1 AGPAGSAAARRLARAGLSVLLLEKGSFPGDK--ICGGG------LLPraLEELE--PLGLDEPLERPVRGA--------- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  89 enlGIELKEEDHGRMFPVSNKAqSVVD------ALLDRLRALNVTIRTNEKIKTVLYQDGQAAgIVTNNDEKISSKSVVI 162
Cdd:COG0644   62 ---RFYSPGGKSVELPPGRGGG-YVVDrarfdrWLAEQAEEAGAEVRTGTRVTDVLRDDGRVV-VRTGDGEEIRADYVVD 136


                 .
gi 637168615 163 A 163
Cdd:COG0644  137 A 137
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 1-172 1.48e-09

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 59.86  E-value: 1.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   1 MKHYDVIVIGGGPSGLMAAIASAEHGATVLLIDKGNKLGRKLA-ISGGG------------------------------- 48
Cdd:COG1233    1 MMMYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRARtFERPGfrfdvgpsvltmpgvlerlfrelgledylel 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  49 -RCNVTNRLP----------------VEEIIKHIPGNG----RFLysAFSEFNNEDIISFF-----ENLGIELKEEDHGR 102
Cdd:COG1233   81 vPLDPAYRVPfpdgraldlprdlertAAELERLFPGDAeayrRFL--AELRRLYDALLEDLlyrplLSLRDLLRPLALAR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615 103 MFPVSNK-------------------------------------------------------AQSVVDALLDRLRALNVT 127
Cdd:COG1233  159 LLRLLLRslrdllrryfkdprlrallagqalylglspdrtpalyaliayleyaggvwypkggMGALADALARLAEELGGE 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 637168615 128 IRTNEKIKTVLYQDGQAAGIVTNNDEKISSKSVVIAVggkSVPHT 172
Cdd:COG1233  239 IRTGAEVERILVEGGRATGVRLADGEEIRADAVVSNA---DPAHT 280
GIDA pfam01134
Glucose inhibited division protein A;
5-175 1.84e-09

Glucose inhibited division protein A;


Pssm-ID: 250388 [Multi-domain]  Cd Length: 391  Bit Score: 59.10  E-value: 1.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615    5 DVIVIGGGPSGLMAAIASAEHGATVLLID-KGNKLGRkLAisgggrCNVTNRLP-----VEEIikhipgngRFLYSafse 78
Cdd:pfam01134   1 DVIVIGGGHAGCEAALAAARMGAKVLLIThNTDTIAE-LS------CNPSIGGIakghlVREI--------DALGG---- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   79 fnneDIISFFENLGIELKEEDHGRMFPV-SNKAQSVVD----ALLDRLRAL-NVTIRTNEkIKTVLYQDGQAAGIVTNND 152
Cdd:pfam01134  62 ----LMGKAADKTGIQFRMLNTSKGPAVrALRAQVDRDlyskEMTETLENHpNLTLIQGE-VTDLIPENGKVKGVVTEDG 136

                         170       180
                  ....*....|....*....|....*
gi 637168615  153 EKISSKSVVIAVG--GKSVPHTGST 175
Cdd:pfam01134 137 EEYKAKAVVLATGtfLNGKIHIGLK 161
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 4-169 1.98e-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: 58.48  E-value: 1.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615    4 YDVIVIGGGPSGLMAAIASAEHGATVLLIDKGnKLGRKLAISGG--GRCNVTNRLPVEEIIKhiPGNGRFLYSAFSEFNN 81
Cdd:TIGR02032   1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEKK-SFPRYKPCGGAlsPRALEELDLPGELIVN--LVRGARFFSPNGDSVE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   82 ediISFFENLGIELKEEDHGRMfpvsnkaqsvvdaLLDRLRALNVTIRTNEKIKTVLYQDGQAAGIVTNNDEKISSKSVV 161
Cdd:TIGR02032  78 ---IPIETELAYVIDRDAFDEQ-------------LAERAQEAGAELRLGTRVLDVEIHDDRVVVIVRGSEGTVTAKIVI 141


                  ....*...
gi 637168615  162 IAVGGKSV 169
Cdd:TIGR02032 142 GADGSRSI 149
NadB COG0029
Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the ...
 1-186 3.70e-09

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: 58.58  E-value: 3.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   1 MKHYDVIVIGGGPSGLMAAIASAEHGaTVLLIDKGnKLGR---KLA----------------------ISGGGRCNvtnr 55
Cdd:COG0029    2 RLKTDVLVIGSGIAGLSAALKLAERG-RVTLLTKG-ELGEsntRWAqggiaavldpgdspelhiadtlAAGAGLCD---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  56 lpvEEIIKHIPGNGRflysafsefnneDIISFFENLGIELKEEDHGR----MFPvsnkAQS--------------VVDAL 117
Cdd:COG0029   76 ---PEAVRVLVEEGP------------ERIRELIELGVPFDRDEDGElaltREG----GHSrrrilhagdatgreIERAL 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615 118 LDRLRAL-NVTIRTNEK-IKTVLYQDGQAAGIV-----TNNDEKISSKSVVIAVGG------KSVPHTGSTGDGYAWAEA 184
Cdd:COG0029  137 LEAVRAHpNITVLENHFaVDLITDADGRCVGAYvldekTGEVETIRAKAVVLATGGagqlyaYTTNPDVATGDGIAMAYR 216


                 ..
gi 637168615 185 AG 186
Cdd:COG0029  217 AG 218
PTZ00052 PTZ00052
thioredoxin reductase; Provisional
 4-210 5.41e-09

thioredoxin reductase; Provisional


Pssm-ID: 185416 [Multi-domain]  Cd Length: 499  Bit Score: 57.91  E-value: 5.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   4 YDVIVIGGGPSGLMAAIASAEHGATVLLID--KGNKLGRKLAIsgGGRCnvTNRLPVEEIIKHIPGNgrflysafsefnn 81
Cdd:PTZ00052   6 YDLVVIGGGSGGMAAAKEAAAHGKKVALFDyvKPSTQGTKWGL--GGTC--VNVGCVPKKLMHYAAN------------- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  82 edIISFFenlgiELKEEDHGRMFPVSNKAQSVVDALLDRLRALNVTIRTNEKIKTVLYQDGQAAGI--------VTNNDE 153
Cdd:PTZ00052  69 --IGSIF-----HHDSQMYGWKTSSSFNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKdehtvsygDNSQEE 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 637168615 154 KISSKSVVIAVGGKsvPHTGSTGDGyawaeaaghtitelfPTEVPVTSDERFIKEKV 210
Cdd:PTZ00052 142 TITAKYILIATGGR--PSIPEDVPG---------------AKEYSITSDDIFSLSKD 181
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 1-36 7.67e-09

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 57.49  E-value: 7.67e-09
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 637168615   1 MKHYDVIVIGGGPSGLMAAIASAEHGATVLLIDKGN 36
Cdd:PRK06292   1 MEKYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGP 36
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
1-39 9.38e-09

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


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 57.09  E-value: 9.38e-09
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 637168615   1 MKHYDVIVIGGGPSGLMAAIASAEHGATVLLIDKGNKLG 39
Cdd:PRK05249   3 MYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVG 41
PRK06481 PRK06481
flavocytochrome c;
4-229 1.30e-08

flavocytochrome c;


Pssm-ID: 180584 [Multi-domain]  Cd Length: 506  Bit Score: 56.77  E-value: 1.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   4 YDVIVIGGGPSGLMAAIASAEHGATVLLIDKGNKLGRKLAISGGGR------------CNVTNRLPVEEIIKHIPG-NGR 70
Cdd:PRK06481  62 YDIVIVGAGGAGMSAAIEAKDAGMNPVILEKMPVAGGNTMKASSGMnasetkfqkaqgIADSNDKFYEETLKGGGGtNDK 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  71 FLYSAFSEfNNEDIISFFENLGIEL---------KEEDHGRMFPVSNKAQSVVDALLDRLRALNVTIRTNEKIKTVLYQD 141
Cdd:PRK06481 142 ALLRYFVD-NSASAIDWLDSMGIKLdnltitggmSEKRTHRPHDGSAVGGYLVDGLLKNVQERKIPLFVNADVTKITEKD 220

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615 142 GQAAGIVT--NNDE--KISSKSVVIAVGG---------KSVP---------HTGSTGDGYAWAEAAGHTITELFPTEVPV 199
Cdd:PRK06481 221 GKVTGVKVkiNGKEtkTISSKAVVVTTGGfgankdmiaKYRPdlkgyvttnQEGSTGDGIKMIEKLGGTTVDMDQIQIHP 300

                        250       260       270
                 ....*....|....*....|....*....|
gi 637168615 200 TSDErfiKEKVLQGLSLRSVAVSVLNKKGK 229
Cdd:PRK06481 301 TVQQ---SKSYLIGEAVRGEGAILVNQKGK 327
PRK12839 PRK12839
FAD-dependent oxidoreductase;
4-47 2.86e-08

FAD-dependent oxidoreductase;


Pssm-ID: 237223 [Multi-domain]  Cd Length: 572  Bit Score: 55.61  E-value: 2.86e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 637168615   4 YDVIVIGGGPSGLMAAIASAEHGATVLLIDKGNKLGRKLAISGG 47
Cdd:PRK12839   9 YDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKASTCGGATAWSGG 52
PRK07494 PRK07494
UbiH/UbiF family hydroxylase;
1-33 4.89e-08

UbiH/UbiF family hydroxylase;


Pssm-ID: 181001 [Multi-domain]  Cd Length: 388  Bit Score: 54.52  E-value: 4.89e-08
                         10        20        30
                 ....*....|....*....|....*....|...
gi 637168615   1 MKHYDVIVIGGGPSGLMAAIASAEHGATVLLID 33
Cdd:PRK07494   5 KEHTDIAVIGGGPAGLAAAIALARAGASVALVA 37
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
2-166 6.37e-08

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 54.14  E-value: 6.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   2 KHYDVIVIGGGPSGLMAAIASAEHGATVLLIDKGnKLGRklAISG--GGRCNVTNRLPVEEiikhipgngrfLYSAFSEF 79
Cdd:COG0665    1 ATADVVVIGGGIAGLSTAYHLARRGLDVTVLERG-RPGS--GASGrnAGQLRPGLAALADR-----------ALVRLARE 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  80 NNEDIISFFENLGIELKEEDHGRMFPVSNKAQ------------------------------------------------ 111
Cdd:COG0665   67 ALDLWRELAAELGIDCDFRRTGVLYLARTEAElaalraeaealralglpvelldaaelrerepglgspdyagglydpddg 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615 112 -----SVVDALLDRLRALNVTIRTNEKIKTVLYQDGQAAGIVTNNDEkISSKSVVIAVGG 166
Cdd:COG0665  147 hvdpaKLVRALARAARAAGVRIREGTPVTGLEREGGRVTGVRTERGT-VRADAVVLAAGA 205
PRK05329 PRK05329
glycerol-3-phosphate dehydrogenase subunit GlpB;
2-35 9.19e-08

glycerol-3-phosphate dehydrogenase subunit GlpB;


Pssm-ID: 235412  Cd Length: 422  Bit Score: 53.70  E-value: 9.19e-08
                         10        20        30
                 ....*....|....*....|....*....|....
gi 637168615   2 KHYDVIVIGGGPSGLMAAIASAEHGATVLLIDKG 35
Cdd:PRK05329   1 MKFDVLVIGGGLAGLTAALAAAEAGKRVALVAKG 34
PRK06134 PRK06134
putative FAD-binding dehydrogenase; Reviewed
 4-192 1.12e-07

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 180419 [Multi-domain]  Cd Length: 581  Bit Score: 53.96  E-value: 1.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   4 YDVIVIGGGPSGLMAAIASAEHGATVLLIDKGNKLGRKLAISGGGRCNVTNRLPVEEIIKHIPGNGR-FLYSAFSEFNNE 82
Cdd:PRK06134  13 CDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGGTTAWSGGWMWIPRNPLARRAGIVEDIEQPRtYLRHELGARYDA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  83 DII-----------SFFEN---------------------------------------------LGIELKEED------- 99
Cdd:PRK06134  93 ARIdafleagphmvAFFERhtalrfadgnaipdyhgdtpgaatggrsliaapfdgrelgallerLRKPLRETSfmgmpim 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615 100 ----------------------------------HGRMFPVSNkAQSVVDALLDRLRALNVTIRTNEKIKTVLYQDGQAA 145
Cdd:PRK06134 173 agadlaaflnptrsfraflhvarrfarhlidlarHGRGMHLVN-GNALVARLLKSAEDLGVRIWESAPARELLREDGRVA 251

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 637168615 146 GIVTNNDEKI----SSKSVVIAVGG---------------------KSVPHTGSTGDGYAWAEAAGHTI-TEL 192
Cdd:PRK06134 252 GAVVETPGGLqeirARKGVVLAAGGfphdparraalfpraptghehLSLPPPGNSGDGLRLGESAGGVVaTDL 324
PRK13800 PRK13800
fumarate reductase/succinate dehydrogenase flavoprotein subunit;
5-190 1.55e-07

fumarate reductase/succinate dehydrogenase flavoprotein subunit;


Pssm-ID: 237512 [Multi-domain]  Cd Length: 897  Bit Score: 53.70  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   5 DVIVIGGGPSGLMAAIASAEHGATVLLIDKGN-KLGRKLAISGGGRCNVTnrLP--------VEEIIKHIPG--NGRFLY 73
Cdd:PRK13800  15 DVLVIGGGTAGTMAALTAAEHGANVLLLEKAHvRHSGALAMGMDGVNNAV--IPgkaepedyVAEITRANDGivNQRTVY 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  74 -SAFSEFNnedIISFFENLGIELKEEDHGR------------MFPVSnKAQSVVDALLD--RLRALNVTIRTNEKIKTV- 137
Cdd:PRK13800  93 qTATRGFA---MVQRLERYGVKFEKDEHGEyavrrvhrsgsyVLPMP-EGKDVKKALYRvlRQRSMRERIRIENRLMPVr 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 637168615 138 -LYQDGQ---AAGIVTNNDEKIS--SKSVVIAVG--GK-SVPHTG----------STGDGYAWAEAAGHTIT 190
Cdd:PRK13800 169 vLTEGGRavgAAALNTRTGEFVTvgAKAVILATGpcGRlGLPASGylygtyenptNAGDGYSMAYHAGAELS 240
TGR TIGR01438
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ...
 4-165 1.60e-07

thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member of the pyridine nucleotide disulfide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly, where SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily, Cys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-term arm of the protein is proposed to allow broad substrate specificity.


Pssm-ID: 273624 [Multi-domain]  Cd Length: 484  Bit Score: 53.32  E-value: 1.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615    4 YDVIVIGGGPSGLMAAIASAEHGATVLLID--KGNKLGRKLAIsgGGRCnvtnrLPVEEIIKHIPGNGRFLYSAFSEFNN 81
Cdd:TIGR01438   3 YDLIVIGGGSGGLAAAKEAAAYGAKVMLLDfvTPTPLGTRWGI--GGTC-----VNVGCIPKKLMHQAALLGQALKDSRN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   82 ediisfFENLGIELKEEDHGRMfpvsnkaqsvVDALLDRLRALNVTIRTNEKIKTVLYQDGQAAGI------VTNNDEK- 154
Cdd:TIGR01438  76 ------YGWKVEETVKHDWKRL----------VEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVdkhrikATNKKGKe 139

                         170
                  ....*....|...
gi 637168615  155 --ISSKSVVIAVG 165
Cdd:TIGR01438 140 kiYSAERFLIATG 152
PRK08275 PRK08275
putative oxidoreductase; Provisional
 4-186 1.95e-07

putative oxidoreductase; Provisional


Pssm-ID: 181346 [Multi-domain]  Cd Length: 554  Bit Score: 53.13  E-value: 1.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   4 YDVIVIGGGPSGLMAAIASAEH--GATVLLIDKGNkLGRKLAISGG--GRCNV------TNRLPVEEIIkhIPGNGRFLY 73
Cdd:PRK08275  10 TDILVIGGGTAGPMAAIKAKERnpALRVLLLEKAN-VKRSGAISMGmdGLNNAvipghaTPEQYTKEIT--IANDGIVDQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  74 SAFSEF--NNEDIISFFENLGIELKEEDHGR------------MFPVSNkAQSVVDALLDRLRALNVTIrTNEKIKTVLY 139
Cdd:PRK08275  87 KAVYAYaeHSFETIQQLDRWGVKFEKDETGDyavkkvhhmgsyVLPMPE-GHDIKKVLYRQLKRARVLI-TNRIMATRLL 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 637168615 140 --QDGQAAGIV-----TNNDEKISSKSVVIAVGGK---SVPHTG----------STGDGYAWAEAAG 186
Cdd:PRK08275 165 tdADGRVAGALgfdcrTGEFLVIRAKAVILCCGAAgrlGLPASGylfgtyenptNAGDGYAMAYHAG 231
YdhS COG4529
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
4-165 2.27e-07

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


Pssm-ID: 443597 [Multi-domain]  Cd Length: 466  Bit Score: 52.65  E-value: 2.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   4 YDVIVIGGGPSGLMAAIA---SAEHGATVLLIDKGNKLGRKLAISGGGRCNVTNrLPVEEIikhipgngrflySAFSEfN 80
Cdd:COG4529    6 KRIAIIGGGASGTALAIHllrRAPEPLRITLFEPRPELGRGVAYSTDSPEHLLN-VPAGRM------------SAFPD-D 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  81 NEDIISFFENLGIELKEEDHGRMFP--------VsnkaQSVVDALLDRLRALNVTIRTNEKIKTVLYQDGQAAgIVTNND 152
Cdd:COG4529   72 PDHFLRWLRENGARAAPAIDPDAFVprrlfgeyL----RERLAEALARAPAGVRLRHIRAEVVDLERDDGGYR-VTLADG 146

                        170
                 ....*....|...
gi 637168615 153 EKISSKSVVIAVG 165
Cdd:COG4529  147 ETLRADAVVLATG 159
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 5-166 2.85e-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: 52.01  E-value: 2.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615    5 DVIVIGGGPSGLMAAIASAEHGATVLLIDKGNKLGR-------KLaISGGGRCNVTNRLP---------VEEIIK----H 64
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGSgasgrnaGL-IHPGLRYLEPSELArlalealdlWEELEEelgiD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   65 IPGNGRFLYSAFSEFNNEDIISFFENL---GIE---LKEEDHGRMFPVSNK--------------AQSVVDALLDRLRAL 124
Cdd:pfam01266  80 CGFRRCGVLVLARDEEEEALEKLLAALrrlGVPaelLDAEELRELEPLLPGlrgglfypdgghvdPARLLRALARAAEAL 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 637168615  125 NVTIRTNEKIkTVLYQDGQAAGIVTNNdekiSSKSVVIAVGG 166
Cdd:pfam01266 160 GVRIIEGTEV-TGIEEEGGVWGVVTTG----EADAVVNAAGA 196
PRK12835 PRK12835
3-ketosteroid-delta-1-dehydrogenase; Reviewed
 3-48 6.41e-07

3-ketosteroid-delta-1-dehydrogenase; Reviewed


Pssm-ID: 237221 [Multi-domain]  Cd Length: 584  Bit Score: 51.35  E-value: 6.41e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 637168615   3 HYDVIVIGGGPSGLMAAIASAEHGATVLLIDKGNKLGRKLAISGGG 48
Cdd:PRK12835  11 EVDVLVVGSGGGGMTAALTAAARGLDTLVVEKSAHFGGSTALSGGG 56
GlpB COG3075
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
1-35 8.81e-07

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


Pssm-ID: 442309  Cd Length: 415  Bit Score: 50.95  E-value: 8.81e-07
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 637168615   1 MKhYDVIVIGGGPSGLMAAIASAEHGATVLLIDKG 35
Cdd:COG3075    1 MK-FDVVVIGGGLAGLTAAIRAAEAGLRVAIVSAG 34
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
 1-178 9.94e-07

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 50.69  E-value: 9.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   1 MKHYDVIVIGGGPSGLMAAIASAEHGATVLLID--KGNKLGRKLaisgGGRCnvTNRlpveeiiKHIPGNGrFLYSA--F 76
Cdd:PRK06327   2 SKQFDVVVIGAGPGGYVAAIRAAQLGLKVACIEawKNPKGKPAL----GGTC--LNV-------GCIPSKA-LLASSeeF 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  77 SEFNNEdiisfFENLGIELKEE--DHGRMfpVSNKaQSVVDALLDRLRALnvtIRTNeKIkTVLYQDGQAAGI------- 147
Cdd:PRK06327  68 ENAGHH-----FADHGIHVDGVkiDVAKM--IARK-DKVVKKMTGGIEGL---FKKN-KI-TVLKGRGSFVGKtdagyei 134

                        170       180       190
                 ....*....|....*....|....*....|...
gi 637168615 148 -VTNNDEK-ISSKSVVIAVGGKSVPHTGSTGDG 178
Cdd:PRK06327 135 kVTGEDETvITAKHVIIATGSEPRHLPGVPFDN 167
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 4-168 1.14e-06

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: 50.01  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615    4 YDVIVIGGGPSGLMAAIASAEHGATVLLIDKGNklgrklaisgggrcnvtnrlpveeiikHIPGNGRFLYSAFsefnned 83
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEG---------------------------TCPYGGCVLSKAL------- 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   84 iisffenlgieLKEEDHGRMFPVSNKAQSVVDALLDRLRAlNVTIRTNEKIKTVLYQDGQ--AAGIVTNNDEKISSKSVV 161
Cdd:pfam07992  47 -----------LGAAEAPEIASLWADLYKRKEEVVKKLNN-GIEVLLGTEVVSIDPGAKKvvLEELVDGDGETITYDRLV 114


                  ....*..
gi 637168615  162 IAVGGKS 168
Cdd:pfam07992 115 IATGARP 121
PRK09126 PRK09126
FAD-dependent hydroxylase;
1-163 1.59e-06

FAD-dependent hydroxylase;


Pssm-ID: 236385 [Multi-domain]  Cd Length: 392  Bit Score: 49.94  E-value: 1.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   1 MKHYDVIVIGGGPSGLMAAIASAEHGATVLLIDKG--NKL------GRKLAISGGGR-----CNVTNRLPVEEI--IKHI 65
Cdd:PRK09126   1 MMHSDIVVVGAGPAGLSFARSLAGSGLKVTLIERQplAALadpafdGREIALTHASReilqrLGAWDRIPEDEIspLRDA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615  66 P-GNGRFLYSAFSEFNNEDIisffENLGielkeedhgrmFPVSNkaQSVVDALLDRLRAL-NVTIRTNEKIKTVlYQDGQ 143
Cdd:PRK09126  81 KvLNGRSPFALTFDARGRGA----DALG-----------YLVPN--HLIRRAAYEAVSQQdGIELLTGTRVTAV-RTDDD 142

                        170       180
                 ....*....|....*....|
gi 637168615 144 AAGIVTNNDEKISSKSVVIA 163
Cdd:PRK09126 143 GAQVTLANGRRLTARLLVAA 162
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 3-39 3.13e-06

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: 49.18  E-value: 3.13e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 637168615    3 HYDVIVIGGGPSGLMAAIASAEHGATVLLIDKgNKLG 39
Cdd:TIGR01350   1 AYDVIVIGGGPGGYVAAIRAAQLGLKVALVEK-EYLG 36
PRK08132 PRK08132
FAD-dependent oxidoreductase; Provisional
 3-145 4.96e-06

FAD-dependent oxidoreductase; Provisional


Pssm-ID: 236158 [Multi-domain]  Cd Length: 547  Bit Score: 48.71  E-value: 4.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   3 HYDVIVIGGGPSGLMAAIASAEHGATVLLIDKGNKLgrklaiSGGGR--C------NVTNRLPVEEII--KHIPGN-GRf 71
Cdd:PRK08132  23 RHPVVVVGAGPVGLALAIDLAQQGVPVVLLDDDDTL------STGSRaiCfakrslEIFDRLGCGERMvdKGVSWNvGK- 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 637168615  72 lysafSEFNNEDIISFfeNLgieLKEEDHgRMFPVSNKAQSVVDA-LLDRLRAL-NVTIRTNEKIKTVLYQDGQAA 145
Cdd:PRK08132  96 -----VFLRDEEVYRF--DL---LPEPGH-RRPAFINLQQYYVEGyLVERAQALpNIDLRWKNKVTGLEQHDDGVT 160
PRK12844 PRK12844
3-ketosteroid-delta-1-dehydrogenase; Reviewed
 4-48 5.33e-06

3-ketosteroid-delta-1-dehydrogenase; Reviewed


Pssm-ID: 183787 [Multi-domain]  Cd Length: 557  Bit Score: 48.60  E-value: 5.33e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 637168615   4 YDVIVIGGGPSGLMAAIASAEHGATVLLIDKGNKLGRKLAISGGG 48
Cdd:PRK12844   7 YDVVVVGSGGGGMCAALAAADSGLEPLIVEKQDKVGGSTAMSGGV 51
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 3-39 7.04e-06

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 48.22  E-value: 7.04e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 637168615   3 HYDVIVIGGGPSGLMAAIASAEHGATVLLIDKGnKLG 39
Cdd:PRK06416   4 EYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKE-KLG 39
PRK07843 PRK07843
3-oxosteroid 1-dehydrogenase;
4-48 7.38e-06

3-oxosteroid 1-dehydrogenase;


Pssm-ID: 236111 [Multi-domain]  Cd Length: 557  Bit Score: 48.11  E-value: 7.38e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 637168615   4 YDVIVIGGGPSGLMAAIASAEHGATVLLIDKGNKLGRKLAISGGG 48
Cdd:PRK07843   8 YDVVVVGSGAAGMVAALTAAHRGLSTVVVEKAPHYGGSTARSGGG 52
PRK07121 PRK07121
FAD-binding protein;
4-47 1.04e-05

FAD-binding protein;


Pssm-ID: 180854 [Multi-domain]  Cd Length: 492  Bit Score: 47.57  E-value: 1.04e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 637168615   4 YDVIVIGGGPSGLMAAIASAEHGATVLLIDKGNKLGRKLAISGG 47
Cdd:PRK07121  21 ADVVVVGFGAAGACAAIEAAAAGARVLVLERAAGAGGATALSGG 64
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
8-39 1.05e-05

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 42.90  E-value: 1.05e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 637168615    8 VIGGGPSGLMAAIASAEHGATVLLIDKGNKLG 39
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLG 32
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 1-39 1.16e-05

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: 47.16  E-value: 1.16e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 637168615   1 MKHYDVIVIGGGPSGLMAAIASAEHGATVLLIDKGNKLG 39
Cdd:COG2072    4 TEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVG 42
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
5-43 1.61e-05

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 47.16  E-value: 1.61e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 637168615   5 DVIVIGGGPSGLMAAIASAEHGATVLLIDKGNKLGRKLA 43
Cdd:COG1148  142 RALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAA 180
MnmG COG0445
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ...
 2-32 2.99e-05

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: 46.15  E-value: 2.99e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 637168615   2 KHYDVIVIGGGPSGLMAAIASAEHGATVLLI 32
Cdd:COG0445    5 KEYDVIVVGGGHAGCEAALAAARMGAKTLLL 35
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 3-39 3.03e-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: 45.98  E-value: 3.03e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 637168615   3 HYDVIVIGGGPSGLMAAIASAEHGATVLLIDKGNKLG 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 3.89e-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: 45.39  E-value: 3.89e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 637168615    4 YDVIVIGGGPSGLMAAIASAEHGATVLLIDK 34
Cdd:pfam01494   2 TDVLIVGGGPAGLMLALLLARAGVRVVLVER 32
PRK12842 PRK12842
putative succinate dehydrogenase; Reviewed
 4-47 5.58e-05

putative succinate dehydrogenase; Reviewed


Pssm-ID: 237224 [Multi-domain]  Cd Length: 574  Bit Score: 45.45  E-value: 5.58e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 637168615   4 YDVIVIGGGPSGLMAAIASAEHGATVLLIDKGNKLGRKLAISGG 47
Cdd:PRK12842  10 CDVLVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGGTTAFSGG 53
PRK12843 PRK12843
FAD-dependent oxidoreductase;
4-48 9.40e-05

FAD-dependent oxidoreductase;


Pssm-ID: 237225 [Multi-domain]  Cd Length: 578  Bit Score: 44.73  E-value: 9.40e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 637168615   4 YDVIVIGGGPSGLMAAIASAEHGATVLLIDKGNKLGRKLAISGGG 48
Cdd:PRK12843  17 FDVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGTTATSAGT 61
PRK06370 PRK06370
FAD-containing oxidoreductase;
1-35 1.09e-04

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 44.42  E-value: 1.09e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 637168615   1 MKHYDVIVIGGGPSGLMAAIASAEHGATVLLIDKG 35
Cdd:PRK06370   3 AQRYDAIVIGAGQAGPPLAARAAGLGMKVALIERG 37
COG3573 COG3573
Predicted oxidoreductase [General function prediction only];
3-33 1.17e-04

Predicted oxidoreductase [General function prediction only];


Pssm-ID: 442794 [Multi-domain]  Cd Length: 551  Bit Score: 44.40  E-value: 1.17e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 637168615   3 HYDVIVIGGGPSGLMAAIASAEHGATVLLID 33
Cdd:COG3573    5 DADVIVVGAGLAGLVAAAELADAGRRVLLLD 35
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
 6-39 1.99e-04

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 44.00  E-value: 1.99e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 637168615    6 VIVIGGGPSGLMAAIASAEHGATVLLIDKGNKLG 39
Cdd:PTZ00306  412 VIVVGGGLAGCSAAIEAASCGAQVILLEKEAKLG 445
PRK06116 PRK06116
glutathione reductase; Validated
 1-39 3.11e-04

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 42.84  E-value: 3.11e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 637168615   1 MKHYDVIVIGGGPSGLMAAIASAEHGATVLLIDkGNKLG 39
Cdd:PRK06116   2 TKDYDLIVIGGGSGGIASANRAAMYGAKVALIE-AKRLG 39
glycerol3P_GlpB TIGR03378
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are ...
 4-35 3.51e-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: 42.70  E-value: 3.51e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 637168615    4 YDVIVIGGGPSGLMAAIASAEHGATVLLIDKG 35
Cdd:TIGR03378   1 FDVIIIGGGLAGLSCALRLAEAGKKCAIIAAG 32
sdhA PRK07803
succinate dehydrogenase flavoprotein subunit; Reviewed
 3-34 3.84e-04

succinate dehydrogenase flavoprotein subunit; Reviewed


Pssm-ID: 236101 [Multi-domain]  Cd Length: 626  Bit Score: 42.72  E-value: 3.84e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 637168615   3 HYDVIVIGGGPSGLMAAIASAEHGATVLLIDK 34
Cdd:PRK07803   8 SYDVVVIGAGGAGLRAAIEARERGLRVAVVCK 39
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
1-57 6.41e-04

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 41.83  E-value: 6.41e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 637168615   1 MKHYDVIVIGGGPSGLMAAIASAEHGATVLLIDKGNKLgrklaisgGGRCnVTNRLP 57
Cdd:COG1231    5 ARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRV--------GGRV-WTLRFG 52
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
1-40 7.88e-04

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


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 41.28  E-value: 7.88e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 637168615   1 MKHYDVIVIGGGPSGLmaAIA---SAEHGATVLLIDKGNKLGR 40
Cdd:COG0579    2 MEMYDVVIIGAGIVGL--ALArelSRYEDLKVLVLEKEDDVAQ 42
sdhA PRK08641
succinate dehydrogenase flavoprotein subunit; Reviewed
 1-32 8.53e-04

succinate dehydrogenase flavoprotein subunit; Reviewed


Pssm-ID: 236319 [Multi-domain]  Cd Length: 589  Bit Score: 41.50  E-value: 8.53e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 637168615   1 MKHYDVIVIGGGPSGLMAAIASAEHGATVLLI 32
Cdd:PRK08641   1 MAKGKVIVVGGGLAGLMATIKAAEAGVHVDLF 32
carotene-cycl TIGR01790
lycopene cyclase family protein; This family includes lycopene beta and epsilion cyclases ...
 5-186 8.79e-04

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


Pssm-ID: 130850 [Multi-domain]  Cd Length: 388  Bit Score: 41.26  E-value: 8.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615    5 DVIVIGGGPSGLMAAIASAEHGATVLLIDKGNKlgrklaisgggrcnvtnrlpveeiikhIPGNGRflYSAF-SEFNNED 83
Cdd:TIGR01790   1 DLAVIGGGPAGLAIALELARPGLRVQLIEPHPP---------------------------IPGNHT--YGVWdDDLSDLG 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637168615   84 IISFFENL---GIELKEEDHGRMFpvsNKAQsvvdALLDRLRALNVTIRTNEKiKTVLYQDGQAAGIV----------TN 150
Cdd:TIGR01790  52 LADCVEHVwpdVYEYRFPKQPRKL---GTAY----GSVDSTRLHEELLQKCPE-GGVLWLERKAIHAEadgvalstvyCA 123

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 637168615  151 NDEKISSKSVVIAVGGKSVPHTGSTGDGYAWAEAAG 186
Cdd:TIGR01790 124 GGQRIQARLVIDARGFGPLVQYVRFPLNVGFQVAYG 159
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
3-34 1.26e-03

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


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 41.05  E-value: 1.26e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 637168615   3 HYDVIVIGGGPSGLMAAIASAEHGATVLLIDK 34
Cdd:PRK06183  10 DTDVVIVGAGPVGLTLANLLGQYGVRVLVLER 41
PRK10015 PRK10015
oxidoreductase; Provisional
 4-67 1.44e-03

oxidoreductase; Provisional


Pssm-ID: 182194 [Multi-domain]  Cd Length: 429  Bit Score: 40.73  E-value: 1.44e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 637168615   4 YDVIVIGGGPSGLMAAIASAEHGATVLLIDKGNKLGRKlAISGGgrcnvtnRLPVEEIIKHIPG 67
Cdd:PRK10015   6 FDAIVVGAGVAGSVAALVMARAGLDVLVIERGDSAGCK-NMTGG-------RLYAHTLEAIIPG 61
BetA COG2303
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General ...
 1-35 1.49e-03

Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General function prediction only]; Choline dehydrogenase or related flavoprotein is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 441878 [Multi-domain]  Cd Length: 531  Bit Score: 40.58  E-value: 1.49e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 637168615   1 MKHYDVIVIGGGPSG-LMAAIASAEHGATVLLIDKG 35
Cdd:COG2303    2 LEEYDYVIVGAGSAGcVLANRLSEDAGLRVLLLEAG 37
PRK07845 PRK07845
flavoprotein disulfide reductase; Reviewed
 6-33 2.07e-03

flavoprotein disulfide reductase; Reviewed


Pssm-ID: 236112 [Multi-domain]  Cd Length: 466  Bit Score: 40.23  E-value: 2.07e-03
                         10        20
                 ....*....|....*....|....*...
gi 637168615   6 VIVIGGGPSGLMAAIASAEHGATVLLID 33
Cdd:PRK07845   4 IVIIGGGPGGYEAALVAAQLGADVTVIE 31
PRK07804 PRK07804
L-aspartate oxidase; Provisional
 3-35 3.67e-03

L-aspartate oxidase; Provisional


Pssm-ID: 236102 [Multi-domain]  Cd Length: 541  Bit Score: 39.57  E-value: 3.67e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 637168615   3 HYDVIVIGGGPSGLMAAIASAEHGATVLLIDKG 35
Cdd:PRK07804  16 AADVVVVGSGVAGLTAALAARRAGRRVLVVTKA 48
PRK05329 PRK05329
glycerol-3-phosphate dehydrogenase subunit GlpB;
115-166 4.25e-03

glycerol-3-phosphate dehydrogenase subunit GlpB;


Pssm-ID: 235412  Cd Length: 422  Bit Score: 39.06  E-value: 4.25e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 637168615 115 DALLDRLRALNVTIRTNEKIKTVLYQDGQAAGIVTNN--DEKISSKSVVIAVGG 166
Cdd:PRK05329 263 NALRRAFERLGGRIMPGDEVLGAEFEGGRVTAVWTRNhgDIPLRARHFVLATGS 316
PRK12834 PRK12834
putative FAD-binding dehydrogenase; Reviewed
 1-36 4.49e-03

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 183782 [Multi-domain]  Cd Length: 549  Bit Score: 39.11  E-value: 4.49e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 637168615   1 MKHYDVIVIGGGPSGLMAAIASAEHGATVLLIDKGN 36
Cdd:PRK12834   2 AMDADVIVVGAGLAGLVAAAELADAGKRVLLLDQEN 37
TrmFO COG1206
Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and ...
 374-422 5.80e-03

Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and biogenesis]; Folate-dependent tRNA-U54 methylase TrmFO/GidA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440819  Cd Length: 436  Bit Score: 38.89  E-value: 5.80e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 637168615 374 MASKKMPGLYFCGEIldihgyTG--GYnITSAlVTGRLAGMNAALEAKERD 422
Cdd:COG1206  325 LQLKARPNLFFAGQI------TGveGY-VESA-ASGLLAGINAARLLLGKE 367
PRK06126 PRK06126
hypothetical protein; Provisional
 5-35 7.06e-03

hypothetical protein; Provisional


Pssm-ID: 235704 [Multi-domain]  Cd Length: 545  Bit Score: 38.44  E-value: 7.06e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 637168615   5 DVIVIGGGPSGLMAAIASAEHGATVLLIDKG 35
Cdd:PRK06126   9 PVLIVGGGPVGLALALDLGRRGVDSILVERK 39
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
 374-422 8.32e-03

tRNA (uracil-5-)-methyltransferase Gid; Reviewed


Pssm-ID: 235416  Cd Length: 436  Bit Score: 38.20  E-value: 8.32e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 637168615 374 MASKKMPGLYFCGEIldihgyTG--GYnITSAlVTGRLAGMNAALEAKERD 422
Cdd:PRK05335 325 LQLKKRPNLFFAGQI------TGveGY-VESA-ASGLLAGINAARLALGKE 367
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 6-39 8.98e-03

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 38.32  E-value: 8.98e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 637168615   6 VIVIGGGPSGLMAAIASAEHGATVLLIDKGNKLG 39
Cdd:PRK12771 140 VAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLG 173
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
 6-33 9.90e-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: 9.90e-03
                         10        20
                 ....*....|....*....|....*....
gi 637168615   6 VIVIGGGPSGLMAAIASAEHGA-TVLLID 33
Cdd:cd08284  171 VAVIGCGPVGLCAVLSAQVLGAaRVFAVD 199
 
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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