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Conserved domains on  [gi|500640697|ref|WP_011963142|]
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3-hydroxyacyl-CoA dehydrogenase [Flavobacterium psychrophilum]

Protein Classification

3-hydroxyacyl-CoA dehydrogenase family protein( domain architecture ID 11483238)

3-hydroxyacyl-CoA dehydrogenase family protein similar to Acinetobacter baylyi diketoreductase that catalyzes a two-step bioreduction on a dicarbonyl substrate

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK08293 PRK08293
3-hydroxyacyl-CoA dehydrogenase;
1-287 1.24e-178

3-hydroxyacyl-CoA dehydrogenase;


:

Pssm-ID: 181359 [Multi-domain]  Cd Length: 287  Bit Score: 494.07  E-value: 1.24e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697   1 MNYKNITVAGSGVLGYQIAFQAAFHNFNVTVYDINDEILAKAKLKFSSMSDAFKRDLHAS-EADLAVAFRNLKYSSNLAD 79
Cdd:PRK08293   1 MDIKNVTVAGAGVLGSQIAFQTAFHGFDVTIYDISDEALEKAKERIAKLADRYVRDLEATkEAPAEAALNRITLTTDLAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697  80 AVKDADLLIEAVPENPSIKIDFYKKLAQVAVAKTVFATNSSTLLPSQFAQVTGRPSQFLALHFANDIWRNNTAEIMGHTG 159
Cdd:PRK08293  81 AVKDADLVIEAVPEDPEIKGDFYEELAKVAPEKTIFATNSSTLLPSQFAEATGRPEKFLALHFANEIWKNNTAEIMGHPG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697 160 TNPEIFNDVVAFAKAIGMLALPLQKEQPGYILNSLLVPFLTAATSLLVKEVADPKTIDKTWMKATGAPIGPFAILDIVGI 239
Cdd:PRK08293 161 TDPEVFDTVVAFAKAIGMVPIVLKKEQPGYILNSLLVPFLSAALALWAKGVADPETIDKTWMIATGAPMGPFGILDIVGL 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 500640697 240 NTVYNINKMASEKSQDPFeIKTTAYLKEHFVDTNKLGVSTGEGFYTYP 287
Cdd:PRK08293 241 DTAYNITSNWAEATDDEN-AKKAAALLKEYIDKGKLGVATGEGFYNYP 287
 
Name Accession Description Interval E-value
PRK08293 PRK08293
3-hydroxyacyl-CoA dehydrogenase;
1-287 1.24e-178

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 181359 [Multi-domain]  Cd Length: 287  Bit Score: 494.07  E-value: 1.24e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697   1 MNYKNITVAGSGVLGYQIAFQAAFHNFNVTVYDINDEILAKAKLKFSSMSDAFKRDLHAS-EADLAVAFRNLKYSSNLAD 79
Cdd:PRK08293   1 MDIKNVTVAGAGVLGSQIAFQTAFHGFDVTIYDISDEALEKAKERIAKLADRYVRDLEATkEAPAEAALNRITLTTDLAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697  80 AVKDADLLIEAVPENPSIKIDFYKKLAQVAVAKTVFATNSSTLLPSQFAQVTGRPSQFLALHFANDIWRNNTAEIMGHTG 159
Cdd:PRK08293  81 AVKDADLVIEAVPEDPEIKGDFYEELAKVAPEKTIFATNSSTLLPSQFAEATGRPEKFLALHFANEIWKNNTAEIMGHPG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697 160 TNPEIFNDVVAFAKAIGMLALPLQKEQPGYILNSLLVPFLTAATSLLVKEVADPKTIDKTWMKATGAPIGPFAILDIVGI 239
Cdd:PRK08293 161 TDPEVFDTVVAFAKAIGMVPIVLKKEQPGYILNSLLVPFLSAALALWAKGVADPETIDKTWMIATGAPMGPFGILDIVGL 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 500640697 240 NTVYNINKMASEKSQDPFeIKTTAYLKEHFVDTNKLGVSTGEGFYTYP 287
Cdd:PRK08293 241 DTAYNITSNWAEATDDEN-AKKAAALLKEYIDKGKLGVATGEGFYNYP 287
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 4-286 5.46e-92

3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA dehydrogenase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440862 [Multi-domain]  Cd Length: 281  Bit Score: 274.30  E-value: 5.46e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697   4 KNITVAGSGVLGYQIAFQAAFHNFNVTVYDINDEILAKAKLKFSSMSDAFKRDLHASEADLAVAFRNLKYSSNLAdAVKD 83
Cdd:COG1250    3 KKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKLVKKGKLTEEEADAALARITPTTDLA-ALAD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697  84 ADLLIEAVPENPSIKIDFYKKLAQVAVAKTVFATNSSTLLPSQFAQVTGRPSQFLALHFANDIWRNNTAEIMGHTGTNPE 163
Cdd:COG1250   82 ADLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIRGPATSDE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697 164 IFNDVVAFAKAIGMLALPLqKEQPGYILNSLLVPFLTAATSLLVKEVADPKTIDKTWMKATGAPIGPFAILDIVGINTVY 243
Cdd:COG1250  162 TVATAVAFARRLGKTPVVV-KDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPMGPFELADLVGLDTAL 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 500640697 244 NINKMASEKSQDPFeIKTTAYLKEhFVDTNKLGVSTGEGFYTY 286
Cdd:COG1250  241 AVLEVLYEALGDPR-YRPPPLLKK-LVEAGRLGRKTGRGFYDY 281
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
 5-179 4.76e-49

3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda crystallin.


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 161.17  E-value: 4.76e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697    5 NITVAGSGVLGYQIAFQAAFHNFNVTVYDINDEILAKAKLKFSSMSDAFKRDLHASEADLAVAFRNLKYSSNLADAVkDA 84
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKGRITEEEVDAALARISFTTDLAAAV-DA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697   85 DLLIEAVPENPSIKIDFYKKLAQVAVAKTVFATNSSTLLPSQFAQVTGRPSQFLALHFANDIWRNNTAEIMGHTGTNPEI 164
Cdd:pfam02737  80 DLVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEKTSPET 159

                         170
                  ....*....|....*
gi 500640697  165 FNDVVAFAKAIGMLA 179
Cdd:pfam02737 160 VATTVELAKKIGKTP 174
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
 4-286 2.41e-21

fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of mitochondrial multifunctional fatty acid degradation enzyme complex. Subunit activities include: enoyl-CoA hydratase (EC 4.2.1.17) _ 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35). Some characterization in human (SP:P40939), pig (SP:Q29554), and rat (SP:Q64428). The beta subunit has activity: acetyl-CoA C-acyltransferase (EC 2.3.1.16).


Pssm-ID: 131494 [Multi-domain]  Cd Length: 737  Bit Score: 94.13  E-value: 2.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697    4 KNITVAGSGVLGYQIAFQAAFHNFNVTVYDINDEILAKAKLK-FSSMSDAFKRD-LHASEAD--LAVAFRNLKYSsnlad 79
Cdd:TIGR02441 336 KTLAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQvFKGLNKKVKRKkITSLERDsiLSNLTPTLDYS----- 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697   80 AVKDADLLIEAVPENPSIKIDFYKKLAQVAVAKTVFATNSSTLLPSQFAQVTGRPSQFLALHFANDIWRNNTAEIMGHTG 159
Cdd:TIGR02441 411 GFKNADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEIITHDG 490

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697  160 TNPEIFNDVVAFAKAIGMLALPLqKEQPGYILNSLLVPFLTAATSLLvKEVADPKTIDKtWMKATGAPIGPFAILDIVGI 239
Cdd:TIGR02441 491 TSKDTLASAVAVGLKQGKVVIVV-KDGPGFYTTRCLGPMLAEVIRLL-QEGVDPKKLDK-LTTKFGFPVGAATLADEVGV 567

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 500640697  240 NTVYNINKMASEKSQDPFEIKTTAYLKEhFVDTNKLGVSTGEGFYTY 286
Cdd:TIGR02441 568 DVAEHVAEDLGKAFGERFGGGSAELLSE-LVKAGFLGRKSGKGIFIY 613
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 5-91 2.52e-03

Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.


Pssm-ID: 240630 [Multi-domain]  Cd Length: 359  Bit Score: 38.93  E-value: 2.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697   5 NITVAGSGVLGYQIAFQAAFHNFNVTVYDINDEILAKaklkfssMSDAFKRDLHASEADlavafrnlkySSNLADAVKDA 84
Cdd:cd05305  170 KVVILGAGVVGENAARVALGLGAEVTVLDINLERLRY-------LDDIFGGRVTTLYSN----------PANLEEALKEA 232


                 ....*..
gi 500640697  85 DLLIEAV 91
Cdd:cd05305  233 DLVIGAV 239
 
Name Accession Description Interval E-value
PRK08293 PRK08293
3-hydroxyacyl-CoA dehydrogenase;
1-287 1.24e-178

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 181359 [Multi-domain]  Cd Length: 287  Bit Score: 494.07  E-value: 1.24e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697   1 MNYKNITVAGSGVLGYQIAFQAAFHNFNVTVYDINDEILAKAKLKFSSMSDAFKRDLHAS-EADLAVAFRNLKYSSNLAD 79
Cdd:PRK08293   1 MDIKNVTVAGAGVLGSQIAFQTAFHGFDVTIYDISDEALEKAKERIAKLADRYVRDLEATkEAPAEAALNRITLTTDLAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697  80 AVKDADLLIEAVPENPSIKIDFYKKLAQVAVAKTVFATNSSTLLPSQFAQVTGRPSQFLALHFANDIWRNNTAEIMGHTG 159
Cdd:PRK08293  81 AVKDADLVIEAVPEDPEIKGDFYEELAKVAPEKTIFATNSSTLLPSQFAEATGRPEKFLALHFANEIWKNNTAEIMGHPG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697 160 TNPEIFNDVVAFAKAIGMLALPLQKEQPGYILNSLLVPFLTAATSLLVKEVADPKTIDKTWMKATGAPIGPFAILDIVGI 239
Cdd:PRK08293 161 TDPEVFDTVVAFAKAIGMVPIVLKKEQPGYILNSLLVPFLSAALALWAKGVADPETIDKTWMIATGAPMGPFGILDIVGL 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 500640697 240 NTVYNINKMASEKSQDPFeIKTTAYLKEHFVDTNKLGVSTGEGFYTYP 287
Cdd:PRK08293 241 DTAYNITSNWAEATDDEN-AKKAAALLKEYIDKGKLGVATGEGFYNYP 287
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 4-286 5.46e-92

3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA dehydrogenase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440862 [Multi-domain]  Cd Length: 281  Bit Score: 274.30  E-value: 5.46e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697   4 KNITVAGSGVLGYQIAFQAAFHNFNVTVYDINDEILAKAKLKFSSMSDAFKRDLHASEADLAVAFRNLKYSSNLAdAVKD 83
Cdd:COG1250    3 KKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKLVKKGKLTEEEADAALARITPTTDLA-ALAD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697  84 ADLLIEAVPENPSIKIDFYKKLAQVAVAKTVFATNSSTLLPSQFAQVTGRPSQFLALHFANDIWRNNTAEIMGHTGTNPE 163
Cdd:COG1250   82 ADLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIRGPATSDE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697 164 IFNDVVAFAKAIGMLALPLqKEQPGYILNSLLVPFLTAATSLLVKEVADPKTIDKTWMKATGAPIGPFAILDIVGINTVY 243
Cdd:COG1250  162 TVATAVAFARRLGKTPVVV-KDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPMGPFELADLVGLDTAL 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 500640697 244 NINKMASEKSQDPFeIKTTAYLKEhFVDTNKLGVSTGEGFYTY 286
Cdd:COG1250  241 AVLEVLYEALGDPR-YRPPPLLKK-LVEAGRLGRKTGRGFYDY 281
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
 5-179 4.76e-49

3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda crystallin.


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 161.17  E-value: 4.76e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697    5 NITVAGSGVLGYQIAFQAAFHNFNVTVYDINDEILAKAKLKFSSMSDAFKRDLHASEADLAVAFRNLKYSSNLADAVkDA 84
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKGRITEEEVDAALARISFTTDLAAAV-DA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697   85 DLLIEAVPENPSIKIDFYKKLAQVAVAKTVFATNSSTLLPSQFAQVTGRPSQFLALHFANDIWRNNTAEIMGHTGTNPEI 164
Cdd:pfam02737  80 DLVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEKTSPET 159

                         170
                  ....*....|....*
gi 500640697  165 FNDVVAFAKAIGMLA 179
Cdd:pfam02737 160 VATTVELAKKIGKTP 174
PRK09260 PRK09260
3-hydroxyacyl-CoA dehydrogenase;
4-288 8.41e-47

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 236434 [Multi-domain]  Cd Length: 288  Bit Score: 158.80  E-value: 8.41e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697   4 KNITVAGSGVLGYQIAFQAAFHNFNVTVYDINDEILAKAKLKFSSMSDAFKRDLHASEADLAVAFRNLKYSSNLADAVKD 83
Cdd:PRK09260   2 EKLVVVGAGVMGRGIAYVFAVSGFQTTLVDIKQEQLESAQQEIASIFEQGVARGKLTEAARQAALARLSYSLDLKAAVAD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697  84 ADLLIEAVPENPSIKIDFYKKLAQVAVAKTVFATNSSTLLPSQFAQVTGRPSQFLALHFANDIWRNNTAEIMGHTGTNPE 163
Cdd:PRK09260  82 ADLVIEAVPEKLELKKAVFETADAHAPAECYIATNTSTMSPTEIASFTKRPERVIAMHFFNPVHKMKLVELIRGLETSDE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697 164 IFNDVVAFAKAIGMLALPLQkEQPGYILNSLLVPFLTAATSLLVKEVADPKTIDKTWMKATGAPIGPFAILDIVGINTVY 243
Cdd:PRK09260 162 TVQVAKEVAEQMGKETVVVN-EFPGFVTSRISALVGNEAFYMLQEGVATAEDIDKAIRLGLNFPMGPLELGDLVGLDTRL 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 500640697 244 NINKMASEKSQDPFEiktTAYLKEHFVDTNKLGVSTGEGFYTYPN 288
Cdd:PRK09260 241 NNLKYLHETLGEKYR---PAPLLEKYVKAGRLGRKTGRGVYDYTN 282
PLN02545 PLN02545
3-hydroxybutyryl-CoA dehydrogenase
 4-286 1.36e-46

3-hydroxybutyryl-CoA dehydrogenase


Pssm-ID: 215300 [Multi-domain]  Cd Length: 295  Bit Score: 158.36  E-value: 1.36e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697   4 KNITVAGSGVLGYQIAFQAAFHNFNVTVYDINDEILAKAKLKFSSMSDAFKRDLHASEADLAVAFRNLKYSSNLADaVKD 83
Cdd:PLN02545   5 KKVGVVGAGQMGSGIAQLAAAAGMDVWLLDSDPAALSRGLDSISSSLARLVKKGKMSQEEADATLGRIRCTTNLEE-LRD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697  84 ADLLIEAVPENPSIKIDFYKKLAQVAVAKTVFATNSSTLLPSQFAQVTGRPSQFLALHFANDIWRNNTAEIMGHTGTNPE 163
Cdd:PLN02545  84 ADFIIEAIVESEDLKKKLFSELDRICKPSAILASNTSSISITRLASATQRPQQVIGMHFMNPPPIMKLVEIIRGADTSDE 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697 164 IFNDVVAFAKAIGMLALPLQkEQPGYILNSLLVPFLTAATSLLVKEVADPKTIDkTWMK-ATGAPIGPFAILDIVGINTV 242
Cdd:PLN02545 164 VFDATKALAERFGKTVVCSQ-DYPGFIVNRILMPMINEAFYALYTGVASKEDID-TGMKlGTNHPMGPLHLADFIGLDTC 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 500640697 243 YNINKMASEKSQDPfeikttAY----LKEHFVDTNKLGVSTGEGFYTY 286
Cdd:PLN02545 242 LSIMKVLHEGLGDS------KYrpcpLLVQYVDAGRLGRKSGRGVYHY 283
PRK06130 PRK06130
3-hydroxybutyryl-CoA dehydrogenase; Validated
 4-287 2.67e-43

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 235707 [Multi-domain]  Cd Length: 311  Bit Score: 150.31  E-value: 2.67e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697   4 KNITVAGSGVLGYQIAFQAAFHNFNVTVYDINDEILAKAKLKFSSmsdafKRDLHASEADLAVAFRNLKYSSNLADAVKD 83
Cdd:PRK06130   5 QNLAIIGAGTMGSGIAALFARKGLQVVLIDVMEGALERARGVIER-----ALGVYAPLGIASAGMGRIRMEAGLAAAVSG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697  84 ADLLIEAVPENPSIKIDFYKKLAQVAVAKTVFATNSSTLLPSQFAQVTGRPSQFLALHFANDIWRNNTAEIMGHTGTNPE 163
Cdd:PRK06130  80 ADLVIEAVPEKLELKRDVFARLDGLCDPDTIFATNTSGLPITAIAQAVTRPERFVGTHFFTPADVIPLVEVVRGDKTSPQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697 164 IFNDVVAFAKAIGMLALPLQKEQPGYILNSLLVPFLTAATSLLVKEVADPKTIDKTWMKATG---APIGPFAILDIVGIN 240
Cdd:PRK06130 160 TVATTMALLRSIGKRPVLVKKDIPGFIANRIQHALAREAISLLEKGVASAEDIDEVVKWSLGirlALTGPLEQRDMNGLD 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 500640697 241 TVYNInkmASEKSQDPFEIKTTAYLKEHFVDTNKLGVSTGEGFYTYP 287
Cdd:PRK06130 240 VHLAV---ASYLYQDLENRTTPSPLLEEKVEAGELGAKSGQGFYAWP 283
PRK05808 PRK05808
3-hydroxybutyryl-CoA dehydrogenase; Validated
 1-286 4.68e-41

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 180269 [Multi-domain]  Cd Length: 282  Bit Score: 143.57  E-value: 4.68e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697   1 MNYKNITVAGSGVLGYQIAFQAAFHNFNVTVYDINDEILAKAklkFSSMSDAFKRDLH---ASEADLAVAFRNLKYSSNL 77
Cdd:PRK05808   1 MGIQKIGVIGAGTMGNGIAQVCAVAGYDVVMVDISDAAVDRG---LATITKSLDRLVKkgkMTEADKEAALARITGTTDL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697  78 ADAvKDADLLIEAVPENPSIKIDFYKKLAQVAVAKTVFATNSSTLLPSQFAQVTGRPSQFLALHFANDIWRNNTAEIMGH 157
Cdd:PRK05808  78 DDL-KDADLVIEAATENMDLKKKIFAQLDEIAKPEAILATNTSSLSITELAAATKRPDKVIGMHFFNPVPVMKLVEIIRG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697 158 TGTNPEIFNDVVAFAKAIGMLALPLqKEQPGYILNSLLVPFLTAATSLLVKEVADPKTIDKTwMKAtGA--PIGPFAILD 235
Cdd:PRK05808 157 LATSDATHEAVEALAKKIGKTPVEV-KNAPGFVVNRILIPMINEAIFVLAEGVATAEDIDEG-MKL-GCnhPIGPLALAD 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 500640697 236 IVGINTVYNINKMASEKSQDPfEIKTTAYLKEhFVDTNKLGVSTGEGFYTY 286
Cdd:PRK05808 234 LIGLDTCLAIMEVLYEGFGDS-KYRPCPLLRK-MVAAGWLGRKTGRGFYDY 282
PRK06035 PRK06035
3-hydroxyacyl-CoA dehydrogenase; Validated
 1-256 4.10e-35

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 180361 [Multi-domain]  Cd Length: 291  Bit Score: 128.45  E-value: 4.10e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697   1 MNYKNITVAGSGVLGYQIAFQAAFHNFNVTVYDINDEILAKAKLKFSSMSDAFKRDLHA---SEADLAVAFRNLKYSSNL 77
Cdd:PRK06035   1 MDIKVIGVVGSGVMGQGIAQVFARTGYDVTIVDVSEEILKNAMELIESGPYGLRNLVEKgkmSEDEAKAIMARIRTSTSY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697  78 aDAVKDADLLIEAVPENPSIKIDFYKKLAQVAVAKTVFATNSSTLLPSQFAQVTGRPSQFLALHFANDIWRNNTAEIMGH 157
Cdd:PRK06035  81 -ESLSDADFIVEAVPEKLDLKRKVFAELERNVSPETIIASNTSGIMIAEIATALERKDRFIGMHWFNPAPVMKLIEVVRA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697 158 TGTNPEIFNDVVAFAKAIGMLALPLqKEQPGYILNSLLVPFLTAATSLLVKEVADPKTIDKTWMKATGAPIGPFAILDIV 237
Cdd:PRK06035 160 ALTSEETFNTTVELSKKIGKIPIEV-ADVPGFFTTRFIEGWLLEAIRSFEIGIATIKDIDEMCKLAFGFPMGPFELMDII 238

                        250
                 ....*....|....*....
gi 500640697 238 GINTVYNINKMASEKSQDP 256
Cdd:PRK06035 239 GIDTVYHIAEYLYEETGDP 257
PRK07819 PRK07819
3-hydroxybutyryl-CoA dehydrogenase; Validated
 8-286 5.58e-35

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181133 [Multi-domain]  Cd Length: 286  Bit Score: 127.80  E-value: 5.58e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697   8 VAGSGVLGYQIAFQAAFHNFNVTVYDINDEILAKAKLK-FSSMSDAFKRD-LHASEADLAVAfrNLKYSSNLADaVKDAD 85
Cdd:PRK07819  10 VVGAGQMGAGIAEVCARAGVDVLVFETTEELATAGRNRiEKSLERAVSRGkLTERERDAALA--RLRFTTDLGD-FADRQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697  86 LLIEAVPENPSIKIDFYKKLAQVAVAK-TVFATNSSTLLPSQFAQVTGRPSQFLALHFANDIWRNNTAEIMGHTGTNPEI 164
Cdd:PRK07819  87 LVIEAVVEDEAVKTEIFAELDKVVTDPdAVLASNTSSIPIMKLAAATKRPGRVLGLHFFNPVPVLPLVELVPTLVTSEAT 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697 165 FNDVVAFAKAIgmlalpLQKE------QPGYILNSLLVPFLTAATSLLVKEVADPKTIDKTWMKATGAPIGPFAILDIVG 238
Cdd:PRK07819 167 VARAEEFASDV------LGKQvvraqdRSGFVVNALLVPYLLSAIRMVESGFATAEDIDKAMVLGCAHPMGPLRLSDLVG 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 500640697 239 INTVyninKMASEKSQDpfEIKTTAY----LKEHFVDTNKLGVSTGEGFYTY 286
Cdd:PRK07819 241 LDTV----KAIADSMYE--EFKEPLYapppLLLRMVEAGLLGKKSGRGFYTY 286
PRK07530 PRK07530
3-hydroxybutyryl-CoA dehydrogenase; Validated
 1-286 1.05e-31

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181018 [Multi-domain]  Cd Length: 292  Bit Score: 119.34  E-value: 1.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697   1 MNYKNITVAGSGVLGYQIAFQAAFHNFNVTVYDINDEILAKAklkFSSMSDAFKRDLHA---SEADLAVAFRNLKYSSNL 77
Cdd:PRK07530   2 MAIKKVGVIGAGQMGNGIAHVCALAGYDVLLNDVSADRLEAG---LATINGNLARQVAKgkiSEEARAAALARISTATDL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697  78 ADaVKDADLLIEAVPENPSIKIDFYKKLAQVAVAKTVFATNSSTLLPSQFAQVTGRPSQFLALHFANDIWRNNTAEIMGH 157
Cdd:PRK07530  79 ED-LADCDLVIEAATEDETVKRKIFAQLCPVLKPEAILATNTSSISITRLASATDRPERFIGIHFMNPVPVMKLVELIRG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697 158 TGTNPEIFNDVVAFAKAIGMLAlPLQKEQPGYILNSLLVPFLTAATSLLVKEVADPKTIDkTWMKaTGA--PIGPFAILD 235
Cdd:PRK07530 158 IATDEATFEAAKEFVTKLGKTI-TVAEDFPAFIVNRILLPMINEAIYTLYEGVGSVEAID-TAMK-LGAnhPMGPLELAD 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 500640697 236 IVGINTVYNINKMASEKSQD------PFEIKttaylkehFVDTNKLGVSTGEGFYTY 286
Cdd:PRK07530 235 FIGLDTCLSIMQVLHDGLADskyrpcPLLVK--------YVEAGWLGRKTGRGFYDY 283
PRK08268 PRK08268
3-hydroxy-acyl-CoA dehydrogenase; Validated
 1-288 4.05e-25

3-hydroxy-acyl-CoA dehydrogenase; Validated


Pssm-ID: 236211 [Multi-domain]  Cd Length: 507  Bit Score: 104.54  E-value: 4.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697   1 MNYKNITVA--GSGVLGYQIAFQAAFHNFNVTVYDINDEILAKAKLKFSSMSD--AFKRDLHASEADLAVAfrNLKYSSN 76
Cdd:PRK08268   3 ALPSIATVAviGAGAMGAGIAQVAAQAGHTVLLYDARAGAAAAARDGIAARLAklVEKGKLTAEQADAALA--RLRPVEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697  77 LADaVKDADLLIEAVPENPSIKIDFYKKLAQVAVAKTVFATNSSTLLPSQFAQVTGRPSQFLALHFANDIWRNNTAEIMG 156
Cdd:PRK08268  81 LAD-LADCDLVVEAIVERLDVKQALFAQLEAIVSPDCILATNTSSLSITAIAAALKHPERVAGLHFFNPVPLMKLVEVVS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697 157 HTGTNPEIFNDVVAFAKAIGmlALPLQ-KEQPGYILNSLLVPFLTAATSLLVKEVADPKTIDKTWMKATGAPIGPFAILD 235
Cdd:PRK08268 160 GLATDPAVADALYALARAWG--KTPVRaKDTPGFIVNRAARPYYTEALRVLEEGVADPATIDAILREAAGFRMGPFELMD 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500640697 236 IVGI-------NTVYNinkmasEKSQDP-FeikTTAYLKEHFVDTNKLGVSTGEGFYTYPN 288
Cdd:PRK08268 238 LIGLdvnhavmESVYR------QFYQEPrF---RPSLIQQELVAAGRLGRKSGQGFYRYAD 289
fadB PRK11730
fatty acid oxidation complex subunit alpha FadB;
8-286 2.26e-24

fatty acid oxidation complex subunit alpha FadB;


Pssm-ID: 183293 [Multi-domain]  Cd Length: 715  Bit Score: 103.02  E-value: 2.26e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697   8 VAGSGVLGYQIAFQAAFHNFNVTVYDINDEILAkaklkfSSMSDAFKRdLHA-------SEADLAVAFRNLKYSSNLADa 80
Cdd:PRK11730 318 VLGAGIMGGGIAYQSASKGVPVIMKDINQKALD------LGMTEAAKL-LNKqvergkiDGAKMAGVLSSIRPTLDYAG- 389

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697  81 VKDADLLIEAVPENPSIKIDFYKKLAQVAVAKTVFATNSSTLLPSQFAQVTGRPSQFLALHFANDIWRNNTAEIMGHTGT 160
Cdd:PRK11730 390 FERVDVVVEAVVENPKVKAAVLAEVEQKVREDTILASNTSTISISLLAKALKRPENFCGMHFFNPVHRMPLVEVIRGEKT 469

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697 161 NPEIFNDVVAFAKAIGMLALPLQkEQPGYILNSLLVPFLtAATSLLVKEVADPKTIDKTWMKATGAPIGPFAILDIVGIN 240
Cdd:PRK11730 470 SDETIATVVAYASKMGKTPIVVN-DCPGFFVNRVLFPYF-AGFSQLLRDGADFRQIDKVMEKQFGWPMGPAYLLDVVGID 547

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 500640697 241 T-VYNINKMAS---EKSQDPFeikTTAYlkEHFVDTNKLGVSTGEGFYTY 286
Cdd:PRK11730 548 TaHHAQAVMAEgfpDRMKKDY---RDAI--DVLFEAKRFGQKNGKGFYRY 592
fadJ PRK11154
fatty acid oxidation complex subunit alpha FadJ;
4-294 5.50e-24

fatty acid oxidation complex subunit alpha FadJ;


Pssm-ID: 236864 [Multi-domain]  Cd Length: 708  Bit Score: 101.90  E-value: 5.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697   4 KNITVAGSGVLGYQIAF-QAAFHNFNVTVYDINDEILAKAkLKFSSmsDAF-----KRDLHASEAD--LAVAFRNLKYSS 75
Cdd:PRK11154 310 NKVGVLGGGLMGGGIAYvTATKAGLPVRIKDINPQGINHA-LKYSW--DLLdkkvkRRHLKPSERDkqMALISGTTDYRG 386

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697  76 nladaVKDADLLIEAVPENPSIKIDFYKKLAQVAVAKTVFATNSSTLLPSQFAQVTGRPSQFLALHFANDIWRNNTAEIM 155
Cdd:PRK11154 387 -----FKHADVVIEAVFEDLALKQQMVAEVEQNCAPHTIFASNTSSLPIGQIAAAAARPEQVIGLHYFSPVEKMPLVEVI 461

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697 156 GHTGTNPEIFNDVVAFAKAIGMLALpLQKEQPGYILNSLLVPFLTAATSLLVkEVADPKTIDKTWMKaTGAPIGPFAILD 235
Cdd:PRK11154 462 PHAKTSAETIATTVALAKKQGKTPI-VVRDGAGFYVNRILAPYINEAARLLL-EGEPIEHIDAALVK-FGFPVGPITLLD 538

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500640697 236 IVGINTVYNINKMASE------KSQDPFEIkttaylkehFVDTNKLGVSTGEGFYTYPNPAYKEK 294
Cdd:PRK11154 539 EVGIDVGTKIIPILEAalgerfSAPAAFDK---------LLNDDRKGRKNGRGFYLYGQKGKKSK 594
3HCDH pfam00725
3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda ...
 188-286 1.20e-21

3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda crystallin. Some proteins include two copies of this domain.


Pssm-ID: 395588 [Multi-domain]  Cd Length: 97  Bit Score: 86.89  E-value: 1.20e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697  188 GYILNSLLVPFLTAATSLLVKEVADPKTIDKTWMKATGAPIGPFAILDIVGINTVYNINK-MASEKSQDPFEIkttAYLK 266
Cdd:pfam00725   1 GFVVNRLLAPYLNEAIRLVEEGVATPEDIDAAMRLGLGLPMGPFELSDLVGLDVGYHILEvLAEEFGDRAYRP---PPLL 77

                          90       100
                  ....*....|....*....|
gi 500640697  267 EHFVDTNKLGVSTGEGFYTY 286
Cdd:pfam00725  78 EKLVEAGRLGRKTGKGFYKY 97
PRK06129 PRK06129
3-hydroxyacyl-CoA dehydrogenase; Validated
 5-236 1.33e-21

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 235706 [Multi-domain]  Cd Length: 308  Bit Score: 92.41  E-value: 1.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697   5 NITVAGSGVLGYQIAFQAAFHNFNVTVYDINDEILAKAKLKFSSMSDAFKR-DLHASEADLAVAFRnLKYSSNLADAVKD 83
Cdd:PRK06129   4 SVAIIGAGLIGRAWAIVFARAGHEVRLWDADPAAAAAAPAYIAGRLEDLAAfDLLDGEAPDAVLAR-IRVTDSLADAVAD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697  84 ADLLIEAVPENPSIKIDFYKKLAQVAVAKTVFATNSSTLLPSQFAQ-VTGRpSQFLALHFANDIWRNNTAEIMGHTGTNP 162
Cdd:PRK06129  83 ADYVQESAPENLELKRALFAELDALAPPHAILASSTSALLASAFTEhLAGR-ERCLVAHPINPPYLIPVVEVVPAPWTAP 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500640697 163 EIFNDVVAFAKAIGMLALPLQKEQPGYILNSLLVPFLTAATSLLVKEVADPKTIDKTWMKATG---APIGPFAILDI 236
Cdd:PRK06129 162 ATLARAEALYRAAGQSPVRLRREIDGFVLNRLQGALLREAFRLVADGVASVDDIDAVIRDGLGlrwSFMGPFETIDL 238
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
 4-286 2.41e-21

fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of mitochondrial multifunctional fatty acid degradation enzyme complex. Subunit activities include: enoyl-CoA hydratase (EC 4.2.1.17) _ 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35). Some characterization in human (SP:P40939), pig (SP:Q29554), and rat (SP:Q64428). The beta subunit has activity: acetyl-CoA C-acyltransferase (EC 2.3.1.16).


Pssm-ID: 131494 [Multi-domain]  Cd Length: 737  Bit Score: 94.13  E-value: 2.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697    4 KNITVAGSGVLGYQIAFQAAFHNFNVTVYDINDEILAKAKLK-FSSMSDAFKRD-LHASEAD--LAVAFRNLKYSsnlad 79
Cdd:TIGR02441 336 KTLAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQvFKGLNKKVKRKkITSLERDsiLSNLTPTLDYS----- 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697   80 AVKDADLLIEAVPENPSIKIDFYKKLAQVAVAKTVFATNSSTLLPSQFAQVTGRPSQFLALHFANDIWRNNTAEIMGHTG 159
Cdd:TIGR02441 411 GFKNADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEIITHDG 490

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697  160 TNPEIFNDVVAFAKAIGMLALPLqKEQPGYILNSLLVPFLTAATSLLvKEVADPKTIDKtWMKATGAPIGPFAILDIVGI 239
Cdd:TIGR02441 491 TSKDTLASAVAVGLKQGKVVIVV-KDGPGFYTTRCLGPMLAEVIRLL-QEGVDPKKLDK-LTTKFGFPVGAATLADEVGV 567

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 500640697  240 NTVYNINKMASEKSQDPFEIKTTAYLKEhFVDTNKLGVSTGEGFYTY 286
Cdd:TIGR02441 568 DVAEHVAEDLGKAFGERFGGGSAELLSE-LVKAGFLGRKSGKGIFIY 613
PRK07066 PRK07066
L-carnitine dehydrogenase;
4-217 4.16e-18

L-carnitine dehydrogenase;


Pssm-ID: 168796 [Multi-domain]  Cd Length: 321  Bit Score: 82.96  E-value: 4.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697   4 KNITVAGSGVLGYQIAFQAAFHNFNVTVYDINDEILAKAKLKFSSMSDAFKRDLHASEADLAvafrNLKYSSNLADAVKD 83
Cdd:PRK07066   8 KTFAAIGSGVIGSGWVARALAHGLDVVAWDPAPGAEAALRANVANAWPALERQGLAPGASPA----RLRFVATIEACVAD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697  84 ADLLIEAVPENPSIKIDFYKKLAQVAVAKTVFATNSSTLLPSQFAQVTGRPSQFLALHFANDIWRNNTAEIMGHTGTNPE 163
Cdd:PRK07066  84 ADFIQESAPEREALKLELHERISRAAKPDAIIASSTSGLLPTDFYARATHPERCVVGHPFNPVYLLPLVEVLGGERTAPE 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 500640697 164 IFNDVVAFAKAIGMLALPLQKEQPGYILNSLLVPFLTAATSLLVKEVADPKTID 217
Cdd:PRK07066 164 AVDAAMGIYRALGMRPLHVRKEVPGFIADRLLEALWREALHLVNEGVATTGEID 217
PRK08269 PRK08269
3-hydroxybutyryl-CoA dehydrogenase; Validated
 14-298 7.33e-18

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181340 [Multi-domain]  Cd Length: 314  Bit Score: 82.03  E-value: 7.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697  14 LGYQIAFQAAFHNFNVTVYDIND-------EILAKAKLKFSSMSDAFKR--DLHASEADLAVAFRNLKYSSNLADAVKDA 84
Cdd:PRK08269   1 MGQGIALAFAFAGHDVTLIDFKPrdaagwrALDAEARAEIERTLAALVAlgRIDAAQADAVLARIAVVARDGAADALADA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697  85 DLLIEAVPENPSIKIDFYKKLAQVAVAKTVFATNSSTLLPSQFAQVTGRPSQFLALHFANDIWRNNTAEIMGHTGTNPEI 164
Cdd:PRK08269  81 DLVFEAVPEVLDAKREALRWLGRHVDADAIIASTTSTFLVTDLQRHVAHPERFLNAHWLNPAYLMPLVEVSPSDATDPAV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697 165 FNDVVAFAKAIGmlALPLQ-KEQPGYIlnsllVPFLTA-----ATSLLVKEVADPKTIDktwmKATGAPIGP-FAILDIV 237
Cdd:PRK08269 161 VDRLAALLERIG--KVPVVcGPSPGYI-----VPRIQAlamneAARMVEEGVASAEDID----KAIRTGFGLrFAVLGLL 229

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500640697 238 ------GINTVYNINK-MASEKSQDPFeikTTAYLKEHFVDTNKLGVSTGEGFYTYPN---PAYKEK---DFLR 298
Cdd:PRK08269 230 efidwgGCDILYYASRyLAGEIGPDRF---APPAIVVRNMEEGRDGLRTGAGFYDYAGvdvPAYRRQrlgEFAR 300
PRK07531 PRK07531
carnitine 3-dehydrogenase;
10-217 6.88e-13

carnitine 3-dehydrogenase;


Pssm-ID: 236044 [Multi-domain]  Cd Length: 495  Bit Score: 68.61  E-value: 6.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697  10 GSGVLGYQIAFQAAFHNFNVTVYD-------INDEILAKAKLKFSSMSDAfkrdlhaseadlAVAFR-NLKYSSNLADAV 81
Cdd:PRK07531  11 GGGVIGGGWAARFLLAGIDVAVFDphpeaerIIGEVLANAERAYAMLTDA------------PLPPEgRLTFCASLAEAV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697  82 KDADLLIEAVPENPSIKIDFYKKLAQVAVAKTVFATNSSTLLPSQFAQVTGRPSQFLALHFANDIWRNNTAEIMGHTGTN 161
Cdd:PRK07531  79 AGADWIQESVPERLDLKRRVLAEIDAAARPDALIGSSTSGFLPSDLQEGMTHPERLFVAHPYNPVYLLPLVELVGGGKTS 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 500640697 162 PEIFNDVVAFAKAIGMLALPLQKEQPGYILNSLLVPFLTAATSLLVKEVADPKTID 217
Cdd:PRK07531 159 PETIRRAKEILREIGMKPVHIAKEIDAFVGDRLLEALWREALWLVKDGIATTEEID 214
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 4-177 1.05e-03

Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440056 [Multi-domain]  Cd Length: 278  Bit Score: 39.72  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697   4 KNITVAGSGVLG--YQIAFQAAFHNFNVTVYDINDEILAKAKlkfssmsdafkrdlhaseaDLAVAFRnlkYSSNLADAV 81
Cdd:COG0287    2 MRIAIIGLGLIGgsLALALKRAGLAHEVVGVDRSPETLERAL-------------------ELGVIDR---AATDLEEAV 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697  82 KDADLLIEAVPenPSIKIDFYKKLAQVAVAKTVFATNSST--LLPSQFAQVTGRPSQFLALH-------------FAnDI 146
Cdd:COG0287   60 ADADLVVLAVP--VGATIEVLAELAPHLKPGAIVTDVGSVkgAVVEAAEALLPDGVRFVGGHpmagteksgpeaaDA-DL 136

                        170       180       190
                 ....*....|....*....|....*....|.
gi 500640697 147 WRNNTAEIMGHTGTNPEIFNDVVAFAKAIGM 177
Cdd:COG0287  137 FEGAPYILTPTEGTDPEALERVEELWEALGA 167
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 5-91 2.52e-03

Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.


Pssm-ID: 240630 [Multi-domain]  Cd Length: 359  Bit Score: 38.93  E-value: 2.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500640697   5 NITVAGSGVLGYQIAFQAAFHNFNVTVYDINDEILAKaklkfssMSDAFKRDLHASEADlavafrnlkySSNLADAVKDA 84
Cdd:cd05305  170 KVVILGAGVVGENAARVALGLGAEVTVLDINLERLRY-------LDDIFGGRVTTLYSN----------PANLEEALKEA 232


                 ....*..
gi 500640697  85 DLLIEAV 91
Cdd:cd05305  233 DLVIGAV 239
 
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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