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Conserved domains on  [gi|446461001|ref|WP_000538855|]
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MULTISPECIES: 3-hydroxybutyryl-CoA dehydrogenase [Bacillus]

Protein Classification

3-hydroxybutyryl-CoA dehydrogenase( domain architecture ID 11481671)

3-hydroxybutyryl-CoA dehydrogenase (BHBD) catalyzes the NAD-dependent oxidation of beta-hydroxybutyryl-CoA to acetoacetyl-CoA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05808 PRK05808
3-hydroxybutyryl-CoA dehydrogenase; Validated
 1-282 0e+00

3-hydroxybutyryl-CoA dehydrogenase; Validated


:

Pssm-ID: 180269 [Multi-domain]  Cd Length: 282  Bit Score: 533.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001   1 MGVQKIVVIGAGQMGSGIAQVCAMAGYDVKIQDLKQEQLDRGLAIITKNLVRQVEKGRMKEEEKEETLNRLTVTLDLDCV 80
Cdd:PRK05808   1 MGIQKIGVIGAGTMGNGIAQVCAVAGYDVVMVDISDAAVDRGLATITKSLDRLVKKGKMTEADKEAALARITGTTDLDDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001  81 KEADLVIEAAVEKMDIKKKIFANLDEIAPDHTILATNTSSLPITEIAAVTKRPEKVIGMHFMNPVPVMKLVEIIRGLATD 160
Cdd:PRK05808  81 KDADLVIEAATENMDLKKKIFAQLDEIAKPEAILATNTSSLSITELAAATKRPDKVIGMHFFNPVPVMKLVEIIRGLATS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001 161 DTVYETIEDITKKIGKVPVEVNDFPGFVSNRILLPMINEAIYTLYEGVATKEAIDEVMKLGMNHPMGPLTLADFIGLDTC 240
Cdd:PRK05808 161 DATHEAVEALAKKIGKTPVEVKNAPGFVVNRILIPMINEAIFVLAEGVATAEDIDEGMKLGCNHPIGPLALADLIGLDTC 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 446461001 241 LYIMEVLHEGLGDSKYRPCPLLRKYVNAGWLGRKTGRGFYVY 282
Cdd:PRK05808 241 LAIMEVLYEGFGDSKYRPCPLLRKMVAAGWLGRKTGRGFYDY 282
 
Name Accession Description Interval E-value
PRK05808 PRK05808
3-hydroxybutyryl-CoA dehydrogenase; Validated
 1-282 0e+00

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 180269 [Multi-domain]  Cd Length: 282  Bit Score: 533.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001   1 MGVQKIVVIGAGQMGSGIAQVCAMAGYDVKIQDLKQEQLDRGLAIITKNLVRQVEKGRMKEEEKEETLNRLTVTLDLDCV 80
Cdd:PRK05808   1 MGIQKIGVIGAGTMGNGIAQVCAVAGYDVVMVDISDAAVDRGLATITKSLDRLVKKGKMTEADKEAALARITGTTDLDDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001  81 KEADLVIEAAVEKMDIKKKIFANLDEIAPDHTILATNTSSLPITEIAAVTKRPEKVIGMHFMNPVPVMKLVEIIRGLATD 160
Cdd:PRK05808  81 KDADLVIEAATENMDLKKKIFAQLDEIAKPEAILATNTSSLSITELAAATKRPDKVIGMHFFNPVPVMKLVEIIRGLATS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001 161 DTVYETIEDITKKIGKVPVEVNDFPGFVSNRILLPMINEAIYTLYEGVATKEAIDEVMKLGMNHPMGPLTLADFIGLDTC 240
Cdd:PRK05808 161 DATHEAVEALAKKIGKTPVEVKNAPGFVVNRILIPMINEAIFVLAEGVATAEDIDEGMKLGCNHPIGPLALADLIGLDTC 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 446461001 241 LYIMEVLHEGLGDSKYRPCPLLRKYVNAGWLGRKTGRGFYVY 282
Cdd:PRK05808 241 LAIMEVLYEGFGDSKYRPCPLLRKMVAAGWLGRKTGRGFYDY 282
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 3-282 3.35e-172

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: 476.91  E-value: 3.35e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001   3 VQKIVVIGAGQMGSGIAQVCAMAGYDVKIQDLKQEQLDRGLAIITKNLVRQVEKGRMKEEEKEETLNRLTVTLDLDCVKE 82
Cdd:COG1250    2 IKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKLVKKGKLTEEEADAALARITPTTDLAALAD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001  83 ADLVIEAAVEKMDIKKKIFANLDEIAPDHTILATNTSSLPITEIAAVTKRPEKVIGMHFMNPVPVMKLVEIIRGLATDDT 162
Cdd:COG1250   82 ADLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIRGPATSDE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001 163 VYETIEDITKKIGKVPVEVNDFPGFVSNRILLPMINEAIYTLYEGVATKEAIDEVMKLGMNHPMGPLTLADFIGLDTCLY 242
Cdd:COG1250  162 TVATAVAFARRLGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPMGPFELADLVGLDTALA 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 446461001 243 IMEVLHEGLGDSKYRPCPLLRKYVNAGWLGRKTGRGFYVY 282
Cdd:COG1250  242 VLEVLYEALGDPRYRPPPLLKKLVEAGRLGRKTGRGFYDY 281
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
 5-183 2.69e-91

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


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 268.25  E-value: 2.69e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001    5 KIVVIGAGQMGSGIAQVCAMAGYDVKIQDLKQEQLDRGLAIITKNLVRQVEKGRMKEEEKEETLNRLTVTLDLDCVKEAD 84
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKGRITEEEVDAALARISFTTDLAAAVDAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001   85 LVIEAAVEKMDIKKKIFANLDEIAPDHTILATNTSSLPITEIAAVTKRPEKVIGMHFMNPVPVMKLVEIIRGLATDDTVY 164
Cdd:pfam02737  81 LVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEKTSPETV 160

                         170
                  ....*....|....*....
gi 446461001  165 ETIEDITKKIGKVPVEVND 183
Cdd:pfam02737 161 ATTVELAKKIGKTPVVVKD 179
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
 3-283 3.57e-72

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: 235.50  E-value: 3.57e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001    3 VQKIVVIGAGQMGSGIAQVCAMAGYDVKIQDLKQEQLDRGLAIITKNLVRQVEKGRMKEEEKEETLNRLTVTLDLDCVKE 82
Cdd:TIGR02441 335 VKTLAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLNKKVKRKKITSLERDSILSNLTPTLDYSGFKN 414

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001   83 ADLVIEAAVEKMDIKKKIFANLDEIAPDHTILATNTSSLPITEIAAVTKRPEKVIGMHFMNPVPVMKLVEIIrglATDDT 162
Cdd:TIGR02441 415 ADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEII---THDGT 491

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001  163 VYETIEDITK---KIGKVPVEVNDFPGFVSNRILLPMINEAIYTLYEGVATKEAIDEVMKLGMnhPMGPLTLADFIGLDT 239
Cdd:TIGR02441 492 SKDTLASAVAvglKQGKVVIVVKDGPGFYTTRCLGPMLAEVIRLLQEGVDPKKLDKLTTKFGF--PVGAATLADEVGVDV 569

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 446461001  240 CLYIMEVLHEGLGDSKYRPCP-LLRKYVNAGWLGRKTGRGFYVYE 283
Cdd:TIGR02441 570 AEHVAEDLGKAFGERFGGGSAeLLSELVKAGFLGRKSGKGIFIYQ 614
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 4-90 8.77e-03

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 36.92  E-value: 8.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001   4 QKIVVIGAGQMGSGIAQVCAMAGYDVKIQDLKQEQLDRGLAIITKNLVrqvekgRMKEEEKEETLNRLTvtldldcVKEA 83
Cdd:cd05188  136 DTVLVLGAGGVGLLAAQLAKAAGARVIVTDRSDEKLELAKELGADHVI------DYKEEDLEEELRLTG-------GGGA 202


                 ....*..
gi 446461001  84 DLVIEAA 90
Cdd:cd05188  203 DVVIDAV 209
 
Name Accession Description Interval E-value
PRK05808 PRK05808
3-hydroxybutyryl-CoA dehydrogenase; Validated
 1-282 0e+00

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 180269 [Multi-domain]  Cd Length: 282  Bit Score: 533.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001   1 MGVQKIVVIGAGQMGSGIAQVCAMAGYDVKIQDLKQEQLDRGLAIITKNLVRQVEKGRMKEEEKEETLNRLTVTLDLDCV 80
Cdd:PRK05808   1 MGIQKIGVIGAGTMGNGIAQVCAVAGYDVVMVDISDAAVDRGLATITKSLDRLVKKGKMTEADKEAALARITGTTDLDDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001  81 KEADLVIEAAVEKMDIKKKIFANLDEIAPDHTILATNTSSLPITEIAAVTKRPEKVIGMHFMNPVPVMKLVEIIRGLATD 160
Cdd:PRK05808  81 KDADLVIEAATENMDLKKKIFAQLDEIAKPEAILATNTSSLSITELAAATKRPDKVIGMHFFNPVPVMKLVEIIRGLATS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001 161 DTVYETIEDITKKIGKVPVEVNDFPGFVSNRILLPMINEAIYTLYEGVATKEAIDEVMKLGMNHPMGPLTLADFIGLDTC 240
Cdd:PRK05808 161 DATHEAVEALAKKIGKTPVEVKNAPGFVVNRILIPMINEAIFVLAEGVATAEDIDEGMKLGCNHPIGPLALADLIGLDTC 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 446461001 241 LYIMEVLHEGLGDSKYRPCPLLRKYVNAGWLGRKTGRGFYVY 282
Cdd:PRK05808 241 LAIMEVLYEGFGDSKYRPCPLLRKMVAAGWLGRKTGRGFYDY 282
PRK07530 PRK07530
3-hydroxybutyryl-CoA dehydrogenase; Validated
 1-282 5.52e-174

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181018 [Multi-domain]  Cd Length: 292  Bit Score: 481.81  E-value: 5.52e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001   1 MGVQKIVVIGAGQMGSGIAQVCAMAGYDVKIQDLKQEQLDRGLAIITKNLVRQVEKGRMKEEEKEETLNRLTVTLDLDCV 80
Cdd:PRK07530   2 MAIKKVGVIGAGQMGNGIAHVCALAGYDVLLNDVSADRLEAGLATINGNLARQVAKGKISEEARAAALARISTATDLEDL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001  81 KEADLVIEAAVEKMDIKKKIFANLDEIAPDHTILATNTSSLPITEIAAVTKRPEKVIGMHFMNPVPVMKLVEIIRGLATD 160
Cdd:PRK07530  82 ADCDLVIEAATEDETVKRKIFAQLCPVLKPEAILATNTSSISITRLASATDRPERFIGIHFMNPVPVMKLVELIRGIATD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001 161 DTVYETIEDITKKIGKVPVEVNDFPGFVSNRILLPMINEAIYTLYEGVATKEAIDEVMKLGMNHPMGPLTLADFIGLDTC 240
Cdd:PRK07530 162 EATFEAAKEFVTKLGKTITVAEDFPAFIVNRILLPMINEAIYTLYEGVGSVEAIDTAMKLGANHPMGPLELADFIGLDTC 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 446461001 241 LYIMEVLHEGLGDSKYRPCPLLRKYVNAGWLGRKTGRGFYVY 282
Cdd:PRK07530 242 LSIMQVLHDGLADSKYRPCPLLVKYVEAGWLGRKTGRGFYDY 283
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 3-282 3.35e-172

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: 476.91  E-value: 3.35e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001   3 VQKIVVIGAGQMGSGIAQVCAMAGYDVKIQDLKQEQLDRGLAIITKNLVRQVEKGRMKEEEKEETLNRLTVTLDLDCVKE 82
Cdd:COG1250    2 IKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKLVKKGKLTEEEADAALARITPTTDLAALAD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001  83 ADLVIEAAVEKMDIKKKIFANLDEIAPDHTILATNTSSLPITEIAAVTKRPEKVIGMHFMNPVPVMKLVEIIRGLATDDT 162
Cdd:COG1250   82 ADLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIRGPATSDE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001 163 VYETIEDITKKIGKVPVEVNDFPGFVSNRILLPMINEAIYTLYEGVATKEAIDEVMKLGMNHPMGPLTLADFIGLDTCLY 242
Cdd:COG1250  162 TVATAVAFARRLGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPMGPFELADLVGLDTALA 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 446461001 243 IMEVLHEGLGDSKYRPCPLLRKYVNAGWLGRKTGRGFYVY 282
Cdd:COG1250  242 VLEVLYEALGDPRYRPPPLLKKLVEAGRLGRKTGRGFYDY 281
PLN02545 PLN02545
3-hydroxybutyryl-CoA dehydrogenase
 3-282 1.53e-153

3-hydroxybutyryl-CoA dehydrogenase


Pssm-ID: 215300 [Multi-domain]  Cd Length: 295  Bit Score: 430.31  E-value: 1.53e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001   3 VQKIVVIGAGQMGSGIAQVCAMAGYDVKIQDLKQEQLDRGLAIITKNLVRQVEKGRMKEEEKEETLNRLTVTLDLDCVKE 82
Cdd:PLN02545   4 IKKVGVVGAGQMGSGIAQLAAAAGMDVWLLDSDPAALSRGLDSISSSLARLVKKGKMSQEEADATLGRIRCTTNLEELRD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001  83 ADLVIEAAVEKMDIKKKIFANLDEIAPDHTILATNTSSLPITEIAAVTKRPEKVIGMHFMNPVPVMKLVEIIRGLATDDT 162
Cdd:PLN02545  84 ADFIIEAIVESEDLKKKLFSELDRICKPSAILASNTSSISITRLASATQRPQQVIGMHFMNPPPIMKLVEIIRGADTSDE 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001 163 VYETIEDITKKIGKVPVEVNDFPGFVSNRILLPMINEAIYTLYEGVATKEAIDEVMKLGMNHPMGPLTLADFIGLDTCLY 242
Cdd:PLN02545 164 VFDATKALAERFGKTVVCSQDYPGFIVNRILMPMINEAFYALYTGVASKEDIDTGMKLGTNHPMGPLHLADFIGLDTCLS 243

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 446461001 243 IMEVLHEGLGDSKYRPCPLLRKYVNAGWLGRKTGRGFYVY 282
Cdd:PLN02545 244 IMKVLHEGLGDSKYRPCPLLVQYVDAGRLGRKSGRGVYHY 283
PRK09260 PRK09260
3-hydroxyacyl-CoA dehydrogenase;
3-283 7.37e-120

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 236434 [Multi-domain]  Cd Length: 288  Bit Score: 344.85  E-value: 7.37e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001   3 VQKIVVIGAGQMGSGIAQVCAMAGYDVKIQDLKQEQLDRGLAIITKNLVRQVEKGRMKEEEKEETLNRLTVTLDL-DCVK 81
Cdd:PRK09260   1 IEKLVVVGAGVMGRGIAYVFAVSGFQTTLVDIKQEQLESAQQEIASIFEQGVARGKLTEAARQAALARLSYSLDLkAAVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001  82 EADLVIEAAVEKMDIKKKIFANLDEIAPDHTILATNTSSLPITEIAAVTKRPEKVIGMHFMNPVPVMKLVEIIRGLATDD 161
Cdd:PRK09260  81 DADLVIEAVPEKLELKKAVFETADAHAPAECYIATNTSTMSPTEIASFTKRPERVIAMHFFNPVHKMKLVELIRGLETSD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001 162 TVYETIEDITKKIGKVPVEVNDFPGFVSNRILLPMINEAIYTLYEGVATKEAIDEVMKLGMNHPMGPLTLADFIGLDTCL 241
Cdd:PRK09260 161 ETVQVAKEVAEQMGKETVVVNEFPGFVTSRISALVGNEAFYMLQEGVATAEDIDKAIRLGLNFPMGPLELGDLVGLDTRL 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 446461001 242 YIMEVLHEGLGDsKYRPCPLLRKYVNAGWLGRKTGRGFYVYE 283
Cdd:PRK09260 241 NNLKYLHETLGE-KYRPAPLLEKYVKAGRLGRKTGRGVYDYT 281
PRK07819 PRK07819
3-hydroxybutyryl-CoA dehydrogenase; Validated
 1-282 1.79e-115

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181133 [Multi-domain]  Cd Length: 286  Bit Score: 333.49  E-value: 1.79e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001   1 MGVQKIVVIGAGQMGSGIAQVCAMAGYDVKIQDLKQEQLDRGLAIITKNLVRQVEKGRMKEEEKEETLNRLTVTLDLDCV 80
Cdd:PRK07819   3 DAIQRVGVVGAGQMGAGIAEVCARAGVDVLVFETTEELATAGRNRIEKSLERAVSRGKLTERERDAALARLRFTTDLGDF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001  81 KEADLVIEAAVEKMDIKKKIFANLDEIAPD-HTILATNTSSLPITEIAAVTKRPEKVIGMHFMNPVPVMKLVEIIRGLAT 159
Cdd:PRK07819  83 ADRQLVIEAVVEDEAVKTEIFAELDKVVTDpDAVLASNTSSIPIMKLAAATKRPGRVLGLHFFNPVPVLPLVELVPTLVT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001 160 DDTVYETIED-ITKKIGKVPVEVNDFPGFVSNRILLPMINEAIYTLYEGVATKEAIDEVMKLGMNHPMGPLTLADFIGLD 238
Cdd:PRK07819 163 SEATVARAEEfASDVLGKQVVRAQDRSGFVVNALLVPYLLSAIRMVESGFATAEDIDKAMVLGCAHPMGPLRLSDLVGLD 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 446461001 239 TCLYIMEVLHEGLGDSKYRPCPLLRKYVNAGWLGRKTGRGFYVY 282
Cdd:PRK07819 243 TVKAIADSMYEEFKEPLYAPPPLLLRMVEAGLLGKKSGRGFYTY 286
PRK08268 PRK08268
3-hydroxy-acyl-CoA dehydrogenase; Validated
 3-283 3.63e-109

3-hydroxy-acyl-CoA dehydrogenase; Validated


Pssm-ID: 236211 [Multi-domain]  Cd Length: 507  Bit Score: 325.26  E-value: 3.63e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001   3 VQKIVVIGAGQMGSGIAQVCAMAGYDVKIQDLKQEQLDRGLAIITKNLVRQVEKGRMKEEEKEETLNRLTVTLDLDCVKE 82
Cdd:PRK08268   7 IATVAVIGAGAMGAGIAQVAAQAGHTVLLYDARAGAAAAARDGIAARLAKLVEKGKLTAEQADAALARLRPVEALADLAD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001  83 ADLVIEAAVEKMDIKKKIFANLDEIAPDHTILATNTSSLPITEIAAVTKRPEKVIGMHFMNPVPVMKLVEIIRGLATDDT 162
Cdd:PRK08268  87 CDLVVEAIVERLDVKQALFAQLEAIVSPDCILATNTSSLSITAIAAALKHPERVAGLHFFNPVPLMKLVEVVSGLATDPA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001 163 VYETIEDITKKIGKVPVEVNDFPGFVSNRILLPMINEAIYTLYEGVATKEAIDEVMKLGMNHPMGPLTLADFIGLDTCLY 242
Cdd:PRK08268 167 VADALYALARAWGKTPVRAKDTPGFIVNRAARPYYTEALRVLEEGVADPATIDAILREAAGFRMGPFELMDLIGLDVNHA 246

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 446461001 243 IME-VLHEGLGDSKYRPCPLLRKYVNAGWLGRKTGRGFYVYE 283
Cdd:PRK08268 247 VMEsVYRQFYQEPRFRPSLIQQELVAAGRLGRKSGQGFYRYA 288
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
 5-183 2.69e-91

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


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 268.25  E-value: 2.69e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001    5 KIVVIGAGQMGSGIAQVCAMAGYDVKIQDLKQEQLDRGLAIITKNLVRQVEKGRMKEEEKEETLNRLTVTLDLDCVKEAD 84
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKGRITEEEVDAALARISFTTDLAAAVDAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001   85 LVIEAAVEKMDIKKKIFANLDEIAPDHTILATNTSSLPITEIAAVTKRPEKVIGMHFMNPVPVMKLVEIIRGLATDDTVY 164
Cdd:pfam02737  81 LVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEKTSPETV 160

                         170
                  ....*....|....*....
gi 446461001  165 ETIEDITKKIGKVPVEVND 183
Cdd:pfam02737 161 ATTVELAKKIGKTPVVVKD 179
PRK06035 PRK06035
3-hydroxyacyl-CoA dehydrogenase; Validated
 1-274 5.61e-80

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 180361 [Multi-domain]  Cd Length: 291  Bit Score: 243.63  E-value: 5.61e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001   1 MGVQKIVVIGAGQMGSGIAQVCAMAGYDVKIQDLKQEQLDRGLAIITKN---LVRQVEKGRMKEEEKEETLNRLTVTLDL 77
Cdd:PRK06035   1 MDIKVIGVVGSGVMGQGIAQVFARTGYDVTIVDVSEEILKNAMELIESGpygLRNLVEKGKMSEDEAKAIMARIRTSTSY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001  78 DCVKEADLVIEAAVEKMDIKKKIFANLDEIAPDHTILATNTSSLPITEIAAVTKRPEKVIGMHFMNPVPVMKLVEIIRGL 157
Cdd:PRK06035  81 ESLSDADFIVEAVPEKLDLKRKVFAELERNVSPETIIASNTSGIMIAEIATALERKDRFIGMHWFNPAPVMKLIEVVRAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001 158 ATDDTVYETIEDITKKIGKVPVEVNDFPGFVSNRILLPMINEAIYTLYEGVATKEAIDEVMKLGMNHPMGPLTLADFIGL 237
Cdd:PRK06035 161 LTSEETFNTTVELSKKIGKIPIEVADVPGFFTTRFIEGWLLEAIRSFEIGIATIKDIDEMCKLAFGFPMGPFELMDIIGI 240

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 446461001 238 DTCLYIMEVLHEGLGDSKYRPCPLLRKYVNAGWLGRK 274
Cdd:PRK06035 241 DTVYHIAEYLYEETGDPQFIPPNSLKQMVLNGYVGDK 277
PRK08293 PRK08293
3-hydroxyacyl-CoA dehydrogenase;
1-282 6.84e-77

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 181359 [Multi-domain]  Cd Length: 287  Bit Score: 235.22  E-value: 6.84e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001   1 MGVQKIVVIGAGQMGSGIAQVCAMAGYDVKIQDLKQEQLDRGLAIITKNLVRQVEKGR-MKEEEKEETLNRLTVTLDLD- 78
Cdd:PRK08293   1 MDIKNVTVAGAGVLGSQIAFQTAFHGFDVTIYDISDEALEKAKERIAKLADRYVRDLEaTKEAPAEAALNRITLTTDLAe 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001  79 CVKEADLVIEAAVEKMDIKKKIFANLDEIAPDHTILATNTSSLPITEIAAVTKRPEKVIGMHFMNPVPVMKLVEIIRGLA 158
Cdd:PRK08293  81 AVKDADLVIEAVPEDPEIKGDFYEELAKVAPEKTIFATNSSTLLPSQFAEATGRPEKFLALHFANEIWKNNTAEIMGHPG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001 159 TDDTVYETIEDITKKIGKVPVEVN-DFPGFVSNRILLPMINEAIYTLYEGVATKEAIDEVMKLGMNHPMGPLTLADFIGL 237
Cdd:PRK08293 161 TDPEVFDTVVAFAKAIGMVPIVLKkEQPGYILNSLLVPFLSAALALWAKGVADPETIDKTWMIATGAPMGPFGILDIVGL 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 446461001 238 DTCLYIMEVLHEGLGDSKYRPCP-LLRKYVNAGWLGRKTGRGFYVY 282
Cdd:PRK08293 241 DTAYNITSNWAEATDDENAKKAAaLLKEYIDKGKLGVATGEGFYNY 286
fadB PRK11730
fatty acid oxidation complex subunit alpha FadB;
3-283 3.36e-75

fatty acid oxidation complex subunit alpha FadB;


Pssm-ID: 183293 [Multi-domain]  Cd Length: 715  Bit Score: 242.85  E-value: 3.36e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001   3 VQKIVVIGAGQMGSGIAQVCAMAGYDVKIQDLKQEQLDRGLAIITKNLVRQVEKGRMKEEEKEETLNRLTVTLDLDCVKE 82
Cdd:PRK11730 313 VKQAAVLGAGIMGGGIAYQSASKGVPVIMKDINQKALDLGMTEAAKLLNKQVERGKIDGAKMAGVLSSIRPTLDYAGFER 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001  83 ADLVIEAAVEKMDIKKKIFANLDEIAPDHTILATNTSSLPITEIAAVTKRPEKVIGMHFMNPVPVMKLVEIIRGLATDDT 162
Cdd:PRK11730 393 VDVVVEAVVENPKVKAAVLAEVEQKVREDTILASNTSTISISLLAKALKRPENFCGMHFFNPVHRMPLVEVIRGEKTSDE 472

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001 163 VYETIEDITKKIGKVPVEVNDFPGFVSNRILLPMINEAIYTLYEGvATKEAIDEVMKLGMNHPMGPLTLADFIGLDTCLY 242
Cdd:PRK11730 473 TIATVVAYASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDG-ADFRQIDKVMEKQFGWPMGPAYLLDVVGIDTAHH 551

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 446461001 243 IMEVLHEGLGDSKYRPCP-LLRKYVNAGWLGRKTGRGFYVYE 283
Cdd:PRK11730 552 AQAVMAEGFPDRMKKDYRdAIDVLFEAKRFGQKNGKGFYRYE 593
fadJ PRK11154
fatty acid oxidation complex subunit alpha FadJ;
3-283 4.68e-74

fatty acid oxidation complex subunit alpha FadJ;


Pssm-ID: 236864 [Multi-domain]  Cd Length: 708  Bit Score: 239.80  E-value: 4.68e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001   3 VQKIVVIGAGQMGSGIAQVCAM-AGYDVKIQDLKQEQLDRGLAIITKNLVRQVEKGRMKEEEKEETLNRLTVTLDLDCVK 81
Cdd:PRK11154 309 VNKVGVLGGGLMGGGIAYVTATkAGLPVRIKDINPQGINHALKYSWDLLDKKVKRRHLKPSERDKQMALISGTTDYRGFK 388

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001  82 EADLVIEAAVEKMDIKKKIFANLDEIAPDHTILATNTSSLPITEIAAVTKRPEKVIGMHFMNPVPVMKLVEIIRGLATDD 161
Cdd:PRK11154 389 HADVVIEAVFEDLALKQQMVAEVEQNCAPHTIFASNTSSLPIGQIAAAAARPEQVIGLHYFSPVEKMPLVEVIPHAKTSA 468

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001 162 TVYETIEDITKKIGKVPVEVNDFPGFVSNRILLPMINEAIYTLYEGVATkEAIDE-VMKLGMnhPMGPLTLADFIGLDTC 240
Cdd:PRK11154 469 ETIATTVALAKKQGKTPIVVRDGAGFYVNRILAPYINEAARLLLEGEPI-EHIDAaLVKFGF--PVGPITLLDEVGIDVG 545

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 446461001 241 LYIMEVLHEGLGDsKYRPCPLLRKYVNAGWLGRKTGRGFYVYE 283
Cdd:PRK11154 546 TKIIPILEAALGE-RFSAPAAFDKLLNDDRKGRKNGRGFYLYG 587
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
 3-283 3.57e-72

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: 235.50  E-value: 3.57e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001    3 VQKIVVIGAGQMGSGIAQVCAMAGYDVKIQDLKQEQLDRGLAIITKNLVRQVEKGRMKEEEKEETLNRLTVTLDLDCVKE 82
Cdd:TIGR02441 335 VKTLAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLNKKVKRKKITSLERDSILSNLTPTLDYSGFKN 414

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001   83 ADLVIEAAVEKMDIKKKIFANLDEIAPDHTILATNTSSLPITEIAAVTKRPEKVIGMHFMNPVPVMKLVEIIrglATDDT 162
Cdd:TIGR02441 415 ADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEII---THDGT 491

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001  163 VYETIEDITK---KIGKVPVEVNDFPGFVSNRILLPMINEAIYTLYEGVATKEAIDEVMKLGMnhPMGPLTLADFIGLDT 239
Cdd:TIGR02441 492 SKDTLASAVAvglKQGKVVIVVKDGPGFYTTRCLGPMLAEVIRLLQEGVDPKKLDKLTTKFGF--PVGAATLADEVGVDV 569

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 446461001  240 CLYIMEVLHEGLGDSKYRPCP-LLRKYVNAGWLGRKTGRGFYVYE 283
Cdd:TIGR02441 570 AEHVAEDLGKAFGERFGGGSAeLLSELVKAGFLGRKSGKGIFIYQ 614
PRK06130 PRK06130
3-hydroxybutyryl-CoA dehydrogenase; Validated
 3-283 5.37e-72

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 235707 [Multi-domain]  Cd Length: 311  Bit Score: 223.88  E-value: 5.37e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001   3 VQKIVVIGAGQMGSGIAQVCAMAGYDVKIQDLKQEQLDRGLAIItknlvrQVEKGRM-KEEEKEETLNRLTVTLDL-DCV 80
Cdd:PRK06130   4 IQNLAIIGAGTMGSGIAALFARKGLQVVLIDVMEGALERARGVI------ERALGVYaPLGIASAGMGRIRMEAGLaAAV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001  81 KEADLVIEAAVEKMDIKKKIFANLDEIAPDHTILATNTSSLPITEIAAVTKRPEKVIGMHFMNPVPVMKLVEIIRGLATD 160
Cdd:PRK06130  78 SGADLVIEAVPEKLELKRDVFARLDGLCDPDTIFATNTSGLPITAIAQAVTRPERFVGTHFFTPADVIPLVEVVRGDKTS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001 161 DTVYETIEDITKKIGKVPVEVN-DFPGFVSNRILLPMINEAIYTLYEGVATKEAIDEVMKLGMNHPM---GPLTLADFIG 236
Cdd:PRK06130 158 PQTVATTMALLRSIGKRPVLVKkDIPGFIANRIQHALAREAISLLEKGVASAEDIDEVVKWSLGIRLaltGPLEQRDMNG 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 446461001 237 LDTCLYIMEVLHEGLgDSKYRPCPLLRKYVNAGWLGRKTGRGFYVYE 283
Cdd:PRK06130 238 LDVHLAVASYLYQDL-ENRTTPSPLLEEKVEAGELGAKSGQGFYAWP 283
PRK08269 PRK08269
3-hydroxybutyryl-CoA dehydrogenase; Validated
 14-282 1.87e-51

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181340 [Multi-domain]  Cd Length: 314  Bit Score: 171.01  E-value: 1.87e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001  14 MGSGIAQVCAMAGYDVKIQDLKQ------EQLD-RGLAIITKNLVRQVEKGRMKEEEKEETLNRLT-VTLD--LDCVKEA 83
Cdd:PRK08269   1 MGQGIALAFAFAGHDVTLIDFKPrdaagwRALDaEARAEIERTLAALVALGRIDAAQADAVLARIAvVARDgaADALADA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001  84 DLVIEAAVEKMDIKKKIFANLDEIAPDHTILATNTSSLPITEIAAVTKRPEKVIGMHFMNPVPVMKLVEIIRGLATDDTV 163
Cdd:PRK08269  81 DLVFEAVPEVLDAKREALRWLGRHVDADAIIASTTSTFLVTDLQRHVAHPERFLNAHWLNPAYLMPLVEVSPSDATDPAV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001 164 YETIEDITKKIGKVPVEVNDFPGFVSNRILLPMINEAIYTLYEGVATKEAIDEVMKLGMNHPMGPLTLADFI---GLDTC 240
Cdd:PRK08269 161 VDRLAALLERIGKVPVVCGPSPGYIVPRIQALAMNEAARMVEEGVASAEDIDKAIRTGFGLRFAVLGLLEFIdwgGCDIL 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 446461001 241 LYIMEVLHEGLGDSKYRPCPLLRKYVNAGWLGRKTGRGFYVY 282
Cdd:PRK08269 241 YYASRYLAGEIGPDRFAPPAIVVRNMEEGRDGLRTGAGFYDY 282
3HCDH pfam00725
3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda ...
 186-282 2.40e-48

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: 155.84  E-value: 2.40e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001  186 GFVSNRILLPMINEAIYTLYEGVATKEAIDEVMKLGMNHPMGPLTLADFIGLDTCLYIMEVLHEGLGDSKYRPCPLLRKY 265
Cdd:pfam00725   1 GFVVNRLLAPYLNEAIRLVEEGVATPEDIDAAMRLGLGLPMGPFELSDLVGLDVGYHILEVLAEEFGDRAYRPPPLLEKL 80

                          90
                  ....*....|....*..
gi 446461001  266 VNAGWLGRKTGRGFYVY 282
Cdd:pfam00725  81 VEAGRLGRKTGKGFYKY 97
PRK06129 PRK06129
3-hydroxyacyl-CoA dehydrogenase; Validated
 5-233 9.60e-40

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 235706 [Multi-domain]  Cd Length: 308  Bit Score: 140.56  E-value: 9.60e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001   5 KIVVIGAGQMGSGIAQVCAMAGYDVKIQDLKQEQLDRGLAIITKNLVRQVEKGRMKEEEKEETLNRLTVTLDL-DCVKEA 83
Cdd:PRK06129   4 SVAIIGAGLIGRAWAIVFARAGHEVRLWDADPAAAAAAPAYIAGRLEDLAAFDLLDGEAPDAVLARIRVTDSLaDAVADA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001  84 DLVIEAAVEKMDIKKKIFANLDEIAPDHTILATNTSSLPITEIAAVTKRPEKVIGMHFMNPVPVMKLVEIIRGLATDDTV 163
Cdd:PRK06129  84 DYVQESAPENLELKRALFAELDALAPPHAILASSTSALLASAFTEHLAGRERCLVAHPINPPYLIPVVEVVPAPWTAPAT 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446461001 164 YETIEDITKKIGKVPVEVN-DFPGFVSNRILLPMINEAIYTLYEGVATKEAIDEVMKLGMN---HPMGPLTLAD 233
Cdd:PRK06129 164 LARAEALYRAAGQSPVRLRrEIDGFVLNRLQGALLREAFRLVADGVASVDDIDAVIRDGLGlrwSFMGPFETID 237
PRK07531 PRK07531
carnitine 3-dehydrogenase;
2-221 1.68e-24

carnitine 3-dehydrogenase;


Pssm-ID: 236044 [Multi-domain]  Cd Length: 495  Bit Score: 102.12  E-value: 1.68e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001   2 GVQKIVVIGAGQMGSGIAQVCAMAGYDVKIQDLKQEQlDRGLAIITKNLVRQVEKGRMKEEEKEetlNRLTVTLDL-DCV 80
Cdd:PRK07531   3 MIMKAACIGGGVIGGGWAARFLLAGIDVAVFDPHPEA-ERIIGEVLANAERAYAMLTDAPLPPE---GRLTFCASLaEAV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001  81 KEADLVIEAAVEKMDIKKKIFANLDEIAPDHTILATNTSSLPITEIAAVTKRPEKVIGMHFMNPVPVMKLVEIIRGLATD 160
Cdd:PRK07531  79 AGADWIQESVPERLDLKRRVLAEIDAAARPDALIGSSTSGFLPSDLQEGMTHPERLFVAHPYNPVYLLPLVELVGGGKTS 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446461001 161 DTVYETIEDITKKIGKVPVEV-NDFPGFVSNRILLPMINEAIYTLYEGVATKEAIDEVMKLG 221
Cdd:PRK07531 159 PETIRRAKEILREIGMKPVHIaKEIDAFVGDRLLEALWREALWLVKDGIATTEEIDDVIRYS 220
PRK07066 PRK07066
L-carnitine dehydrogenase;
3-221 5.41e-22

L-carnitine dehydrogenase;


Pssm-ID: 168796 [Multi-domain]  Cd Length: 321  Bit Score: 93.36  E-value: 5.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001   3 VQKIVVIGAGQMGSG-IAQVCAmAGYDVKIQDLK---QEQLDRGLAiitkNLVRQVEKGRMKEEEKEETLnRLTVTLDlD 78
Cdd:PRK07066   7 IKTFAAIGSGVIGSGwVARALA-HGLDVVAWDPApgaEAALRANVA----NAWPALERQGLAPGASPARL-RFVATIE-A 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001  79 CVKEADLVIEAAVEKMDIKKKIFANLDEIAPDHTILATNTSSLPITEIAAVTKRPEKVIGMHFMNPVPVMKLVEIIRGLA 158
Cdd:PRK07066  80 CVADADFIQESAPEREALKLELHERISRAAKPDAIIASSTSGLLPTDFYARATHPERCVVGHPFNPVYLLPLVEVLGGER 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446461001 159 TDDTVYETIEDITKKIGKVPVEV-NDFPGFVSNRILLPMINEAIYTLYEGVATKEAIDEVMKLG 221
Cdd:PRK07066 160 TAPEAVDAAMGIYRALGMRPLHVrKEVPGFIADRLLEALWREALHLVNEGVATTGEIDDAIRFG 223
PRK08268 PRK08268
3-hydroxy-acyl-CoA dehydrogenase; Validated
 177-269 1.03e-21

3-hydroxy-acyl-CoA dehydrogenase; Validated


Pssm-ID: 236211 [Multi-domain]  Cd Length: 507  Bit Score: 94.14  E-value: 1.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001 177 VPVEV-NDFPGFVSNRILLPMINEAIYTLYEGVATKEAIDEVMKLGMNHPMGPLTLADFIGLDTCLYIMEVLHEGLGDSK 255
Cdd:PRK08268 406 KAVSViRDSPGFVAQRTVAMIVNEAADIAQQGIASPADIDLAMRLGLNYPLGPLAWGDRLGAARILRVLENLQALYGDPR 485

                         90
                 ....*....|....
gi 446461001 256 YRPCPLLRKYVNAG 269
Cdd:PRK08268 486 YRPSPWLRRRAALG 499
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 5-94 1.67e-03

Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 441497 [Multi-domain]  Cd Length: 305  Bit Score: 39.45  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001   5 KIVVIGAGQMGSGIAQVCAMAGYDVKIqdlkqeqLDRG--LAIITKNLVrqvekgRMKEEEKEETLNRLTVTLDLDCVKE 82
Cdd:COG1893    2 KIAILGAGAIGGLLGARLARAGHDVTL-------VARGahAEALRENGL------RLESPDGDRTTVPVPAVTDPEELGP 68

                         90       100
                 ....*....|....*....|
gi 446461001  83 ADLVI--------EAAVEKM 94
Cdd:COG1893   69 ADLVLvavkaydlEAAAEAL 88
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
6-31 4.08e-03

Predicted dinucleotide-binding enzyme [General function prediction only];


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 37.46  E-value: 4.08e-03
                         10        20
                 ....*....|....*....|....*.
gi 446461001   6 IVVIGAGQMGSGIAQVCAMAGYDVKI 31
Cdd:COG2085    1 IGIIGTGNIGSALARRLAAAGHEVVI 26
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 4-140 5.95e-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: 37.41  E-value: 5.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001   4 QKIVVIGAGQMGSGIAQVCAMAGYDVKI--QDLKQEQLDRGLAIitkNLVRqvekgrmkeeekeetlnRLTVTLDlDCVK 81
Cdd:COG0287    2 MRIAIIGLGLIGGSLALALKRAGLAHEVvgVDRSPETLERALEL---GVID-----------------RAATDLE-EAVA 60

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446461001  82 EADLVIEAA-VEKMdikKKIFANLDEIAPDHTILaTNTSS---LPITEIAAVTKRPEKVIGMH 140
Cdd:COG0287   61 DADLVVLAVpVGAT---IEVLAELAPHLKPGAIV-TDVGSvkgAVVEAAEALLPDGVRFVGGH 119
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 4-90 8.77e-03

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 36.92  E-value: 8.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446461001   4 QKIVVIGAGQMGSGIAQVCAMAGYDVKIQDLKQEQLDRGLAIITKNLVrqvekgRMKEEEKEETLNRLTvtldldcVKEA 83
Cdd:cd05188  136 DTVLVLGAGGVGLLAAQLAKAAGARVIVTDRSDEKLELAKELGADHVI------DYKEEDLEEELRLTG-------GGGA 202


                 ....*..
gi 446461001  84 DLVIEAA 90
Cdd:cd05188  203 DVVIDAV 209
 
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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