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Conserved domains on  [gi|446408496|ref|WP_000486351|]
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MULTISPECIES: 3-hydroxyacyl-CoA dehydrogenase/enoyl-CoA hydratase family protein [Bacillus]

Protein Classification

3-hydroxyacyl-CoA dehydrogenase/enoyl-CoA hydratase family protein( domain architecture ID 12804111)

bifunctional 3-hydroxyacyl-CoA dehydrogenase/enoyl-CoA hydratase family protein may play a role in fatty acid metabolism

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 3-304 1.38e-101

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: 314.74  E-value: 1.38e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496   3 QIKKAAVLGSGVMGSGIAAHLANIGIPTLLLDIVPPALTKeeeakgltlehksVRNRFSNtALQKLLKQKP-APLTVKGN 81
Cdd:COG1250    1 EIKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALER-------------ARARIAK-LLDKLVKKGKlTEEEADAA 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  82 LALIEAgnlEDDLERLADVDWIIEVVVENLDIKKKLFERVDAVRKPGSIVSSNTSGISVEKMAEGRSDdfQKHFLGTHFF 161
Cdd:COG1250   67 LARITP---TTDLAALADADLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKR--PERFIGLHFF 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 162 NPPRYLKLLEVIPTKETDPQVLSFMKLFGEDvLGKGVVIAKDTPNFIGNRIGTYGLLVTLQEMIKRGYSIGEVDSVTGPL 241
Cdd:COG1250  142 NPVPLMPLVEVIRGPATSDETVATAVAFARR-LGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLG 220

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446408496 242 IGRPKsATFRTLDVVGLDTFVHVANNVYENVQEEErdvFKVPTFMHDMLDKKWLGSKTGQGFF 304
Cdd:COG1250  221 FGFPM-GPFELADLVGLDTALAVLEVLYEALGDPR---YRPPPLLKKLVEAGRLGRKTGRGFY 279
crotonase-like cd06558
Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse ...
 482-609 1.05e-19

Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse set of enzymes including enoyl-CoA hydratase, napthoate synthase, methylmalonyl-CoA decarboxylase, 3-hydoxybutyryl-CoA dehydratase, and dienoyl-CoA isomerase. Many of these play important roles in fatty acid metabolism. In addition to a conserved structural core and the formation of trimers (or dimers of trimers), a common feature in this superfamily is the stabilization of an enolate anion intermediate derived from an acyl-CoA substrate. This is accomplished by two conserved backbone NH groups in active sites that form an oxyanion hole.


:

Pssm-ID: 119339 [Multi-domain]  Cd Length: 195  Bit Score: 87.62  E-value: 1.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 482 LIDLGDGILCLEFHS--KSNAIGMDITQMINYAVDEVEKN--YKGLVIGNQSKNFCVGANLAMilMEAQDDNYFEIELVV 557
Cdd:cd06558    2 LVERDGGVATITLNRpeKRNALSLEMLDELAAALDEAEADpdVRVVVLTGAGKAFCAGADLKE--LAALSDAGEEARAFI 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446408496 558 KNFQDAMTKIKYSSKPVVAAPYGMTLGGGTEVCLPAASIQASSETYMGLVEV 609
Cdd:cd06558   80 RELQELLRALLRLPKPVIAAVNGAALGGGLELALACDIRIAAEDAKFGLPEV 131
3HCDH super family cl37630
3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda ...
 380-432 8.00e-03

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


The actual alignment was detected with superfamily member pfam00725:

Pssm-ID: 395588 [Multi-domain]  Cd Length: 97  Bit Score: 36.43  E-value: 8.00e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  380 DIVAIDQAMKWGFGWEQGPFEIWDAIG--VEKSIQK--MEENGVNVPA---WVKEMVEKG 432
Cdd:pfam00725  25 TPEDIDAAMRLGLGLPMGPFELSDLVGldVGYHILEvlAEEFGDRAYRpppLLEKLVEAG 84
 
Name Accession Description Interval E-value
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 3-304 1.38e-101

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: 314.74  E-value: 1.38e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496   3 QIKKAAVLGSGVMGSGIAAHLANIGIPTLLLDIVPPALTKeeeakgltlehksVRNRFSNtALQKLLKQKP-APLTVKGN 81
Cdd:COG1250    1 EIKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALER-------------ARARIAK-LLDKLVKKGKlTEEEADAA 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  82 LALIEAgnlEDDLERLADVDWIIEVVVENLDIKKKLFERVDAVRKPGSIVSSNTSGISVEKMAEGRSDdfQKHFLGTHFF 161
Cdd:COG1250   67 LARITP---TTDLAALADADLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKR--PERFIGLHFF 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 162 NPPRYLKLLEVIPTKETDPQVLSFMKLFGEDvLGKGVVIAKDTPNFIGNRIGTYGLLVTLQEMIKRGYSIGEVDSVTGPL 241
Cdd:COG1250  142 NPVPLMPLVEVIRGPATSDETVATAVAFARR-LGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLG 220

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446408496 242 IGRPKsATFRTLDVVGLDTFVHVANNVYENVQEEErdvFKVPTFMHDMLDKKWLGSKTGQGFF 304
Cdd:COG1250  221 FGFPM-GPFELADLVGLDTALAVLEVLYEALGDPR---YRPPPLLKKLVEAGRLGRKTGRGFY 279
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
 6-204 1.50e-51

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


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 177.73  E-value: 1.50e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496    6 KAAVLGSGVMGSGIAAHLANIGIPTLLLDIVPPALTKEEEAkgltlehksVRNRFSNTALQKLLKQkpapLTVKGNLALI 85
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALER---------IESSLERLVEKGRITE----EEVDAALARI 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496   86 eagNLEDDLERLADVDWIIEVVVENLDIKKKLFERVDAVRKPGSIVSSNTSGISVEKMAEGRSDDFQkhFLGTHFFNPPR 165
Cdd:pfam02737  68 ---SFTTDLAAAVDADLVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPER--FIGLHFFNPPP 142

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 446408496  166 YLKLLEVIPTKETDPQVLSFMKLFGEDvLGKGVVIAKDT 204
Cdd:pfam02737 143 LMPLVEVVRGEKTSPETVATTVELAKK-IGKTPVVVKDT 180
PRK06130 PRK06130
3-hydroxybutyryl-CoA dehydrogenase; Validated
 1-304 2.68e-44

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 235707 [Multi-domain]  Cd Length: 311  Bit Score: 162.25  E-value: 2.68e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496   1 MFQIKKAAVLGSGVMGSGIAAHLANIGIPTLLLDIVPPALTkeeeakgltlehksvrnrfsnTALQKLLKQkpapLTVKG 80
Cdd:PRK06130   1 MNPIQNLAIIGAGTMGSGIAALFARKGLQVVLIDVMEGALE---------------------RARGVIERA----LGVYA 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  81 NLALIEAG----NLEDDLER-LADVDWIIEVVVENLDIKKKLFERVDAVRKPGSIVSSNTSGISVEKMAEGRSddFQKHF 155
Cdd:PRK06130  56 PLGIASAGmgriRMEAGLAAaVSGADLVIEAVPEKLELKRDVFARLDGLCDPDTIFATNTSGLPITAIAQAVT--RPERF 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 156 LGTHFFNPPRYLKLLEVIPTKETDPQVLSFMKLFGEDVLGKGVVIAKDTPNFIGNRIgTYGLLVTLQEMIKRG------- 228
Cdd:PRK06130 134 VGTHFFTPADVIPLVEVVRGDKTSPQTVATTMALLRSIGKRPVLVKKDIPGFIANRI-QHALAREAISLLEKGvasaedi 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 229 -----YSIGEVDSVTGPLigrpksatfRTLDVVGLDTFVHVANNVYENVqEEERDVFKVPTfmhDMLDKKWLGSKTGQGF 303
Cdd:PRK06130 213 devvkWSLGIRLALTGPL---------EQRDMNGLDVHLAVASYLYQDL-ENRTTPSPLLE---EKVEAGELGAKSGQGF 279


                 .
gi 446408496 304 F 304
Cdd:PRK06130 280 Y 280
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
 4-416 6.29e-28

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: 120.33  E-value: 6.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496    4 IKKAAVLGSGVMGSGIAAHLANIGIPTLLLDIVPPALTKEEEAKGLTLEHKSVRNRFSNTALQKLLKQKPAPLTVKGnla 83
Cdd:TIGR02441 335 VKTLAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLNKKVKRKKITSLERDSILSNLTPTLDYSG--- 411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496   84 lieagnleddlerLADVDWIIEVVVENLDIKKKLFERVDAVRKPGSIVSSNTSGISVEKMAEGRSDdfQKHFLGTHFFNP 163
Cdd:TIGR02441 412 -------------FKNADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSR--PEKVIGMHYFSP 476

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  164 PRYLKLLEVIPTKETDPQVLSFMKLFGEDvLGKGVVIAKDTPNFIGNRI-GTygLLVTLQEMIKRGYSIGEVDSVTGPLi 242
Cdd:TIGR02441 477 VDKMQLLEIITHDGTSKDTLASAVAVGLK-QGKVVIVVKDGPGFYTTRClGP--MLAEVIRLLQEGVDPKKLDKLTTKF- 552

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  243 GRPKSATfrTL-DVVGLDTFVHVANNVYENVQeeERDVFKVPTFMHDMLDKKWLGSKTGQGFFLKQGKEilelnpetmey 321
Cdd:TIGR02441 553 GFPVGAA--TLaDEVGVDVAEHVAEDLGKAFG--ERFGGGSAELLSELVKAGFLGRKSGKGIFIYQEGK----------- 617

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  322 EARKKLKAASVELSKQEKGLANklKALVYAKDRAGELLWNIITPTLLYsakLHKEIADDIVAIDQAMKWGFGWEQ---GP 398
Cdd:TIGR02441 618 KGSKKVNSDADEILAQYKLPPK--AEVSSPEDIQIRLVSRFVNEAVLC---LEEGILASPSEGDIGAVFGLGFPPflgGP 692

                         410
                  ....*....|....*...
gi 446408496  399 FEIWDAIGVEKSIQKMEE 416
Cdd:TIGR02441 693 FRFVDLYGADKLVDKMEK 710
crotonase-like cd06558
Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse ...
 482-609 1.05e-19

Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse set of enzymes including enoyl-CoA hydratase, napthoate synthase, methylmalonyl-CoA decarboxylase, 3-hydoxybutyryl-CoA dehydratase, and dienoyl-CoA isomerase. Many of these play important roles in fatty acid metabolism. In addition to a conserved structural core and the formation of trimers (or dimers of trimers), a common feature in this superfamily is the stabilization of an enolate anion intermediate derived from an acyl-CoA substrate. This is accomplished by two conserved backbone NH groups in active sites that form an oxyanion hole.


Pssm-ID: 119339 [Multi-domain]  Cd Length: 195  Bit Score: 87.62  E-value: 1.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 482 LIDLGDGILCLEFHS--KSNAIGMDITQMINYAVDEVEKN--YKGLVIGNQSKNFCVGANLAMilMEAQDDNYFEIELVV 557
Cdd:cd06558    2 LVERDGGVATITLNRpeKRNALSLEMLDELAAALDEAEADpdVRVVVLTGAGKAFCAGADLKE--LAALSDAGEEARAFI 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446408496 558 KNFQDAMTKIKYSSKPVVAAPYGMTLGGGTEVCLPAASIQASSETYMGLVEV 609
Cdd:cd06558   80 RELQELLRALLRLPKPVIAAVNGAALGGGLELALACDIRIAAEDAKFGLPEV 131
CaiD COG1024
Enoyl-CoA hydratase/carnithine racemase [Lipid transport and metabolism]; Enoyl-CoA hydratase ...
 482-613 3.94e-19

Enoyl-CoA hydratase/carnithine racemase [Lipid transport and metabolism]; Enoyl-CoA hydratase/carnithine racemase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440647 [Multi-domain]  Cd Length: 249  Bit Score: 87.53  E-value: 3.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 482 LIDLGDGILCLEFHS--KSNAIGMDITQMINYAVDEVEKN--YKGLVIGNQSKNFCVGANLAMILMEAQDDnyfEIELVV 557
Cdd:COG1024    2 LVEREGGVATITLNRpeKLNALSLEMLAELAAALDEAEADpdVRVVVLTGAGKAFCAGADLKELAAAADPE---EARAFA 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446408496 558 KNFQDAMTKIKYSSKPVVAAPYGMTLGGGTEVCLPAASIQASSETYMGLVEVGVGL 613
Cdd:COG1024   79 RGLQRLFRALRRLPKPVIAAVNGAALGGGLELALACDLRIAAEDARFGLPEVRLGL 134
PRK08150 PRK08150
crotonase/enoyl-CoA hydratase family protein;
483-608 1.32e-05

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 181254  Cd Length: 255  Bit Score: 47.32  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 483 IDLGDGILCLEFH--SKSNAIGMDITQMINYAVDEVEKNYKGLVIGNQSKNFCVGANLAmilmEAQDDNYFEIELVVKNF 560
Cdd:PRK08150   6 YELDGGVATIGLNrpAKRNALNDGLIAALRAAFARLPEGVRAVVLHGEGDHFCAGLDLS----ELRERDAGEGMHHSRRW 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 446408496 561 QDAMTKIKYSSKPVVAAPYGMTLGGGTEVClPAASIQASSE-TYMGLVE 608
Cdd:PRK08150  82 HRVFDKIQYGRVPVIAALHGAVVGGGLELA-SAAHIRVADEsTYFALPE 129
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
 495-609 8.48e-05

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: 45.98  E-value: 8.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  495 HSKSNAIGMDITQMINYAVDEVEKN---YKGLVIGNQSKNFCVGANLAMILMEAQDDnyfEIELVVKNFQDAMTKIKYSS 571
Cdd:TIGR02441  32 NSKVNTLSKELFAEFKEVMNELWTNeaiKSAVLISGKPGSFVAGADIQMIAACKTAQ---EVTQLSQEGQEMFERIEKSQ 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 446408496  572 KPVVAAPYGMTLGGGTEVCLPAASIQAS--SETYMGLVEV 609
Cdd:TIGR02441 109 KPIVAAISGSCLGGGLELALACHYRIATkdRKTLLGLPEV 148
3HCDH pfam00725
3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda ...
 380-432 8.00e-03

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: 36.43  E-value: 8.00e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  380 DIVAIDQAMKWGFGWEQGPFEIWDAIG--VEKSIQK--MEENGVNVPA---WVKEMVEKG 432
Cdd:pfam00725  25 TPEDIDAAMRLGLGLPMGPFELSDLVGldVGYHILEvlAEEFGDRAYRpppLLEKLVEAG 84
 
Name Accession Description Interval E-value
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 3-304 1.38e-101

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: 314.74  E-value: 1.38e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496   3 QIKKAAVLGSGVMGSGIAAHLANIGIPTLLLDIVPPALTKeeeakgltlehksVRNRFSNtALQKLLKQKP-APLTVKGN 81
Cdd:COG1250    1 EIKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALER-------------ARARIAK-LLDKLVKKGKlTEEEADAA 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  82 LALIEAgnlEDDLERLADVDWIIEVVVENLDIKKKLFERVDAVRKPGSIVSSNTSGISVEKMAEGRSDdfQKHFLGTHFF 161
Cdd:COG1250   67 LARITP---TTDLAALADADLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKR--PERFIGLHFF 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 162 NPPRYLKLLEVIPTKETDPQVLSFMKLFGEDvLGKGVVIAKDTPNFIGNRIGTYGLLVTLQEMIKRGYSIGEVDSVTGPL 241
Cdd:COG1250  142 NPVPLMPLVEVIRGPATSDETVATAVAFARR-LGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLG 220

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446408496 242 IGRPKsATFRTLDVVGLDTFVHVANNVYENVQEEErdvFKVPTFMHDMLDKKWLGSKTGQGFF 304
Cdd:COG1250  221 FGFPM-GPFELADLVGLDTALAVLEVLYEALGDPR---YRPPPLLKKLVEAGRLGRKTGRGFY 279
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
 6-204 1.50e-51

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


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 177.73  E-value: 1.50e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496    6 KAAVLGSGVMGSGIAAHLANIGIPTLLLDIVPPALTKEEEAkgltlehksVRNRFSNTALQKLLKQkpapLTVKGNLALI 85
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALER---------IESSLERLVEKGRITE----EEVDAALARI 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496   86 eagNLEDDLERLADVDWIIEVVVENLDIKKKLFERVDAVRKPGSIVSSNTSGISVEKMAEGRSDDFQkhFLGTHFFNPPR 165
Cdd:pfam02737  68 ---SFTTDLAAAVDADLVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPER--FIGLHFFNPPP 142

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 446408496  166 YLKLLEVIPTKETDPQVLSFMKLFGEDvLGKGVVIAKDT 204
Cdd:pfam02737 143 LMPLVEVVRGEKTSPETVATTVELAKK-IGKTPVVVKDT 180
PRK06130 PRK06130
3-hydroxybutyryl-CoA dehydrogenase; Validated
 1-304 2.68e-44

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 235707 [Multi-domain]  Cd Length: 311  Bit Score: 162.25  E-value: 2.68e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496   1 MFQIKKAAVLGSGVMGSGIAAHLANIGIPTLLLDIVPPALTkeeeakgltlehksvrnrfsnTALQKLLKQkpapLTVKG 80
Cdd:PRK06130   1 MNPIQNLAIIGAGTMGSGIAALFARKGLQVVLIDVMEGALE---------------------RARGVIERA----LGVYA 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  81 NLALIEAG----NLEDDLER-LADVDWIIEVVVENLDIKKKLFERVDAVRKPGSIVSSNTSGISVEKMAEGRSddFQKHF 155
Cdd:PRK06130  56 PLGIASAGmgriRMEAGLAAaVSGADLVIEAVPEKLELKRDVFARLDGLCDPDTIFATNTSGLPITAIAQAVT--RPERF 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 156 LGTHFFNPPRYLKLLEVIPTKETDPQVLSFMKLFGEDVLGKGVVIAKDTPNFIGNRIgTYGLLVTLQEMIKRG------- 228
Cdd:PRK06130 134 VGTHFFTPADVIPLVEVVRGDKTSPQTVATTMALLRSIGKRPVLVKKDIPGFIANRI-QHALAREAISLLEKGvasaedi 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 229 -----YSIGEVDSVTGPLigrpksatfRTLDVVGLDTFVHVANNVYENVqEEERDVFKVPTfmhDMLDKKWLGSKTGQGF 303
Cdd:PRK06130 213 devvkWSLGIRLALTGPL---------EQRDMNGLDVHLAVASYLYQDL-ENRTTPSPLLE---EKVEAGELGAKSGQGF 279


                 .
gi 446408496 304 F 304
Cdd:PRK06130 280 Y 280
PLN02545 PLN02545
3-hydroxybutyryl-CoA dehydrogenase
 1-304 3.11e-43

3-hydroxybutyryl-CoA dehydrogenase


Pssm-ID: 215300 [Multi-domain]  Cd Length: 295  Bit Score: 158.74  E-value: 3.11e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496   1 MFQIKKAAVLGSGVMGSGIAAHLANIGIPTLLLDIVPPALTKEeeakgltlehksvRNRFSnTALQKLLKqkpapltvKG 80
Cdd:PLN02545   1 MAEIKKVGVVGAGQMGSGIAQLAAAAGMDVWLLDSDPAALSRG-------------LDSIS-SSLARLVK--------KG 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  81 NLALIEAGNLED------DLERLADVDWIIEVVVENLDIKKKLFERVDAVRKPGSIVSSNTSGISVEKMAEGRSDDFQkh 154
Cdd:PLN02545  59 KMSQEEADATLGrircttNLEELRDADFIIEAIVESEDLKKKLFSELDRICKPSAILASNTSSISITRLASATQRPQQ-- 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 155 FLGTHFFNPPRYLKLLEVIPTKETDPQVLSFMKLFGEDvLGKGVVIAKDTPNFIGNRI-------GTYGLL--VTLQEMI 225
Cdd:PLN02545 137 VIGMHFMNPPPIMKLVEIIRGADTSDEVFDATKALAER-FGKTVVCSQDYPGFIVNRIlmpmineAFYALYtgVASKEDI 215

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446408496 226 KRGYSIGeVDSVTGPLigrpksatfRTLDVVGLDTFVHVANNVYENVQEEErdvFKVPTFMHDMLDKKWLGSKTGQGFF 304
Cdd:PLN02545 216 DTGMKLG-TNHPMGPL---------HLADFIGLDTCLSIMKVLHEGLGDSK---YRPCPLLVQYVDAGRLGRKSGRGVY 281
PRK07819 PRK07819
3-hydroxybutyryl-CoA dehydrogenase; Validated
 4-304 5.73e-39

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181133 [Multi-domain]  Cd Length: 286  Bit Score: 146.28  E-value: 5.73e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496   4 IKKAAVLGSGVMGSGIAAHLANIGIPTLLLDIVPPALTKEEEAKGLTLEHKSVRNRFSNTALQKLLkqkpAPLTVKGnla 83
Cdd:PRK07819   5 IQRVGVVGAGQMGAGIAEVCARAGVDVLVFETTEELATAGRNRIEKSLERAVSRGKLTERERDAAL----ARLRFTT--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  84 lieagnledDLERLADVDWIIEVVVENLDIKKKLFERVDA-VRKPGSIVSSNTSGISVEK--MAEGRSDdfqkHFLGTHF 160
Cdd:PRK07819  78 ---------DLGDFADRQLVIEAVVEDEAVKTEIFAELDKvVTDPDAVLASNTSSIPIMKlaAATKRPG----RVLGLHF 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 161 FNPPRYLKLLEVIPTKETDPQVLSFMKLFGEDVLGKGVVIAKDTPNFIGNrigtyGLLV--TLQ--EMIKRGYSIGE-VD 235
Cdd:PRK07819 145 FNPVPVLPLVELVPTLVTSEATVARAEEFASDVLGKQVVRAQDRSGFVVN-----ALLVpyLLSaiRMVESGFATAEdID 219

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446408496 236 SVT--------GPLigrpksatfRTLDVVGLDTFVHVANNVYENVQEEerdVFKVPTFMHDMLDKKWLGSKTGQGFF 304
Cdd:PRK07819 220 KAMvlgcahpmGPL---------RLSDLVGLDTVKAIADSMYEEFKEP---LYAPPPLLLRMVEAGLLGKKSGRGFY 284
PRK08268 PRK08268
3-hydroxy-acyl-CoA dehydrogenase; Validated
 1-304 9.67e-37

3-hydroxy-acyl-CoA dehydrogenase; Validated


Pssm-ID: 236211 [Multi-domain]  Cd Length: 507  Bit Score: 145.37  E-value: 9.67e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496   1 MFQIKKAAVLGSGVMGSGIAAHLANIGIPTLLLDIVPPALTKEEEAKGLTLEHKSVRNRFSNTALQKLLKQkpapltvkg 80
Cdd:PRK08268   4 LPSIATVAVIGAGAMGAGIAQVAAQAGHTVLLYDARAGAAAAARDGIAARLAKLVEKGKLTAEQADAALAR--------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  81 nlaLIEAGNLEDdlerLADVDWIIEVVVENLDIKKKLFERVDAVRKPGSIVSSNTSGISVEKMAEGrsddfQKH---FLG 157
Cdd:PRK08268  75 ---LRPVEALAD----LADCDLVVEAIVERLDVKQALFAQLEAIVSPDCILATNTSSLSITAIAAA-----LKHperVAG 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 158 THFFNPPRYLKLLEVIPTKETDPQVLSFMKLFGEDvLGKGVVIAKDTPNFIGNRIG----TYGLLVtLQEmikRGYSIGE 233
Cdd:PRK08268 143 LHFFNPVPLMKLVEVVSGLATDPAVADALYALARA-WGKTPVRAKDTPGFIVNRAArpyyTEALRV-LEE---GVADPAT 217

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446408496 234 VDSV--------TGPligrpksatFRTLDVVGLDTFVHVANNVYENVQEEERdvFKVPTFMHDMLDKKWLGSKTGQGFF 304
Cdd:PRK08268 218 IDAIlreaagfrMGP---------FELMDLIGLDVNHAVMESVYRQFYQEPR--FRPSLIQQELVAAGRLGRKSGQGFY 285
PRK05808 PRK05808
3-hydroxybutyryl-CoA dehydrogenase; Validated
 4-304 5.73e-35

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 180269 [Multi-domain]  Cd Length: 282  Bit Score: 134.71  E-value: 5.73e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496   4 IKKAAVLGSGVMGSGIAAHLANIGIPTLLLDIVPPALtkeeeAKGLTLEHKSvrnrfsntaLQKLLK-------QKPAPL 76
Cdd:PRK05808   3 IQKIGVIGAGTMGNGIAQVCAVAGYDVVMVDISDAAV-----DRGLATITKS---------LDRLVKkgkmteaDKEAAL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  77 T-VKGNLalieagnledDLERLADVDWIIEVVVENLDIKKKLFERVDAVRKPGSIVSSNTSGISVEKMAEG--RSDdfqk 153
Cdd:PRK05808  69 ArITGTT----------DLDDLKDADLVIEAATENMDLKKKIFAQLDEIAKPEAILATNTSSLSITELAAAtkRPD---- 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 154 HFLGTHFFNPPRYLKLLEVIPTKETDPQVLSFMKLFGEDvLGKGVVIAKDTPNFIGNRI---------GTYGLLVTLQEM 224
Cdd:PRK05808 135 KVIGMHFFNPVPVMKLVEIIRGLATSDATHEAVEALAKK-IGKTPVEVKNAPGFVVNRIlipmineaiFVLAEGVATAED 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 225 IKRGYSIGeVDSVTGPLigrpksatfrTL-DVVGLDTFVHVANNVYEnvqEEERDVFKVPTFMHDMLDKKWLGSKTGQGF 303
Cdd:PRK05808 214 IDEGMKLG-CNHPIGPL----------ALaDLIGLDTCLAIMEVLYE---GFGDSKYRPCPLLRKMVAAGWLGRKTGRGF 279


                 .
gi 446408496 304 F 304
Cdd:PRK05808 280 Y 280
PRK07530 PRK07530
3-hydroxybutyryl-CoA dehydrogenase; Validated
 1-304 1.37e-34

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181018 [Multi-domain]  Cd Length: 292  Bit Score: 133.59  E-value: 1.37e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496   1 MFQIKKAAVLGSGVMGSGIAAHLANIGIPTLLLDIVPPALTKeeeakGLTLEHKsvrnrfsNTALQkLLKQKPAPLTVKG 80
Cdd:PRK07530   1 MMAIKKVGVIGAGQMGNGIAHVCALAGYDVLLNDVSADRLEA-----GLATING-------NLARQ-VAKGKISEEARAA 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  81 NLALIEAGnleDDLERLADVDWIIEVVVENLDIKKKLFERVDAVRKPGSIVSSNTSGISVEKMAEgrSDDFQKHFLGTHF 160
Cdd:PRK07530  68 ALARISTA---TDLEDLADCDLVIEAATEDETVKRKIFAQLCPVLKPEAILATNTSSISITRLAS--ATDRPERFIGIHF 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 161 FNPPRYLKLLEVIPTKETDPQVLSFMKLFGEDvLGKGVVIAKDTPNFIGNRIgtygLLVTLQEMIKRGYS-IGEVDSV-- 237
Cdd:PRK07530 143 MNPVPVMKLVELIRGIATDEATFEAAKEFVTK-LGKTITVAEDFPAFIVNRI----LLPMINEAIYTLYEgVGSVEAIdt 217

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446408496 238 ---------TGPLigrpksatfRTLDVVGLDTFVHVANNVYENVQEEErdvFKVPTFMHDMLDKKWLGSKTGQGFF 304
Cdd:PRK07530 218 amklganhpMGPL---------ELADFIGLDTCLSIMQVLHDGLADSK---YRPCPLLVKYVEAGWLGRKTGRGFY 281
PRK06035 PRK06035
3-hydroxyacyl-CoA dehydrogenase; Validated
 3-298 1.65e-29

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 180361 [Multi-domain]  Cd Length: 291  Bit Score: 119.21  E-value: 1.65e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496   3 QIKKAAVLGSGVMGSGIAAHLANIGIPTLLLDIVPPALTKEEEAKGltlehksvRNRFsntALQKLLKQ-KPAPLTVKGN 81
Cdd:PRK06035   2 DIKVIGVVGSGVMGQGIAQVFARTGYDVTIVDVSEEILKNAMELIE--------SGPY---GLRNLVEKgKMSEDEAKAI 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  82 LALIEAGNledDLERLADVDWIIEVVVENLDIKKKLFERVDAVRKPGSIVSSNTSGISVEKMAEGRSddFQKHFLGTHFF 161
Cdd:PRK06035  71 MARIRTST---SYESLSDADFIVEAVPEKLDLKRKVFAELERNVSPETIIASNTSGIMIAEIATALE--RKDRFIGMHWF 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 162 NPPRYLKLLEVIPTKETDPQVLSFMKLFGEDVlGKGVVIAKDTPNFIGNRIGTYGLLVTLQEMIKRGYSIGEVDSVTGPL 241
Cdd:PRK06035 146 NPAPVMKLIEVVRAALTSEETFNTTVELSKKI-GKIPIEVADVPGFFTTRFIEGWLLEAIRSFEIGIATIKDIDEMCKLA 224

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446408496 242 IGRPKsATFRTLDVVGLDTFVHVANNVYENVQEEErdvFKVPTFMHDMLDKKWLGSK 298
Cdd:PRK06035 225 FGFPM-GPFELMDIIGIDTVYHIAEYLYEETGDPQ---FIPPNSLKQMVLNGYVGDK 277
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
 4-416 6.29e-28

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: 120.33  E-value: 6.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496    4 IKKAAVLGSGVMGSGIAAHLANIGIPTLLLDIVPPALTKEEEAKGLTLEHKSVRNRFSNTALQKLLKQKPAPLTVKGnla 83
Cdd:TIGR02441 335 VKTLAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLNKKVKRKKITSLERDSILSNLTPTLDYSG--- 411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496   84 lieagnleddlerLADVDWIIEVVVENLDIKKKLFERVDAVRKPGSIVSSNTSGISVEKMAEGRSDdfQKHFLGTHFFNP 163
Cdd:TIGR02441 412 -------------FKNADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSR--PEKVIGMHYFSP 476

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  164 PRYLKLLEVIPTKETDPQVLSFMKLFGEDvLGKGVVIAKDTPNFIGNRI-GTygLLVTLQEMIKRGYSIGEVDSVTGPLi 242
Cdd:TIGR02441 477 VDKMQLLEIITHDGTSKDTLASAVAVGLK-QGKVVIVVKDGPGFYTTRClGP--MLAEVIRLLQEGVDPKKLDKLTTKF- 552

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  243 GRPKSATfrTL-DVVGLDTFVHVANNVYENVQeeERDVFKVPTFMHDMLDKKWLGSKTGQGFFLKQGKEilelnpetmey 321
Cdd:TIGR02441 553 GFPVGAA--TLaDEVGVDVAEHVAEDLGKAFG--ERFGGGSAELLSELVKAGFLGRKSGKGIFIYQEGK----------- 617

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  322 EARKKLKAASVELSKQEKGLANklKALVYAKDRAGELLWNIITPTLLYsakLHKEIADDIVAIDQAMKWGFGWEQ---GP 398
Cdd:TIGR02441 618 KGSKKVNSDADEILAQYKLPPK--AEVSSPEDIQIRLVSRFVNEAVLC---LEEGILASPSEGDIGAVFGLGFPPflgGP 692

                         410
                  ....*....|....*...
gi 446408496  399 FEIWDAIGVEKSIQKMEE 416
Cdd:TIGR02441 693 FRFVDLYGADKLVDKMEK 710
fadB PRK11730
fatty acid oxidation complex subunit alpha FadB;
4-338 3.67e-27

fatty acid oxidation complex subunit alpha FadB;


Pssm-ID: 183293 [Multi-domain]  Cd Length: 715  Bit Score: 118.04  E-value: 3.67e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496   4 IKKAAVLGSGVMGSGIAAHLANIGIPTLLLDIVPPALTKE-EEAKGLtlehksvrnrfsntaLQKLLKQ-KPAPLTVKGN 81
Cdd:PRK11730 313 VKQAAVLGAGIMGGGIAYQSASKGVPVIMKDINQKALDLGmTEAAKL---------------LNKQVERgKIDGAKMAGV 377

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  82 LALIEAGNLEDDLErlaDVDWIIEVVVENLDIKKKLFERVDAVRKPGSIVSSNTSGISVEKMAEG--RSDDfqkhFLGTH 159
Cdd:PRK11730 378 LSSIRPTLDYAGFE---RVDVVVEAVVENPKVKAAVLAEVEQKVREDTILASNTSTISISLLAKAlkRPEN----FCGMH 450

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 160 FFNPPRYLKLLEVIPTKETDPQVL-------SFMklfgedvlGKGVVIAKDTPNFIGNRI-----GTYGLLVtlqemiKR 227
Cdd:PRK11730 451 FFNPVHRMPLVEVIRGEKTSDETIatvvayaSKM--------GKTPIVVNDCPGFFVNRVlfpyfAGFSQLL------RD 516

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 228 GYSIGEVDSVTGPLIGRPKSATFrTLDVVGLDTFVHVANNVYEN----VQEEERDVFKVptfmhdMLDKKWLGSKTGQGF 303
Cdd:PRK11730 517 GADFRQIDKVMEKQFGWPMGPAY-LLDVVGIDTAHHAQAVMAEGfpdrMKKDYRDAIDV------LFEAKRFGQKNGKGF 589

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 446408496 304 FL----KQGKEILELNPETmeYEARKKLKAASVELSKQE 338
Cdd:PRK11730 590 YRyeedKKGKPKKEVDPAV--YELLAPVVQPKREFSDEE 626
PRK08293 PRK08293
3-hydroxyacyl-CoA dehydrogenase;
3-304 6.02e-27

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 181359 [Multi-domain]  Cd Length: 287  Bit Score: 111.57  E-value: 6.02e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496   3 QIKKAAVLGSGVMGSGIAAHLANIGIPTLLLDIVPPALtkeEEAKGLTlehKSVRNRFSNTAlqKLLKQKPApltvKGNL 82
Cdd:PRK08293   2 DIKNVTVAGAGVLGSQIAFQTAFHGFDVTIYDISDEAL---EKAKERI---AKLADRYVRDL--EATKEAPA----EAAL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  83 ALIEagnLEDDLERLA-DVDWIIEVVVENLDIKKKLFERVDAVRKPGSIVSSNTSGISVEKMAE--GRSDdfqkHFLGTH 159
Cdd:PRK08293  70 NRIT---LTTDLAEAVkDADLVIEAVPEDPEIKGDFYEELAKVAPEKTIFATNSSTLLPSQFAEatGRPE----KFLALH 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 160 FFNPPRYLKLLEVIPTKETDPQVLSFMKLFGEDVLGKGVVIAKDTPNFIGNrigtyGLLVTL----QEMIKRGY-SIGEV 234
Cdd:PRK08293 143 FANEIWKNNTAEIMGHPGTDPEVFDTVVAFAKAIGMVPIVLKKEQPGYILN-----SLLVPFlsaaLALWAKGVaDPETI 217

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446408496 235 DS----VTGPLIGrPksatFRTLDVVGLDTFVHVANNVYENVQEEerDVFKVPTFMHDMLDKKWLGSKTGQGFF 304
Cdd:PRK08293 218 DKtwmiATGAPMG-P----FGILDIVGLDTAYNITSNWAEATDDE--NAKKAAALLKEYIDKGKLGVATGEGFY 284
PRK09260 PRK09260
3-hydroxyacyl-CoA dehydrogenase;
4-304 1.19e-26

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 236434 [Multi-domain]  Cd Length: 288  Bit Score: 110.65  E-value: 1.19e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496   4 IKKAAVLGSGVMGSGIAAHLANIGIPTLLLDIVPPALTKEEEAKGLTLEHKSVRNRFSNTALQKLLKQKPAPLTVKgnla 83
Cdd:PRK09260   1 IEKLVVVGAGVMGRGIAYVFAVSGFQTTLVDIKQEQLESAQQEIASIFEQGVARGKLTEAARQAALARLSYSLDLK---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  84 lieagnleddlERLADVDWIIEVVVENLDIKKKLFERVDAVRKPGSIVSSNTSGISVEKMAEGRSDDFQkhFLGTHFFNP 163
Cdd:PRK09260  77 -----------AAVADADLVIEAVPEKLELKKAVFETADAHAPAECYIATNTSTMSPTEIASFTKRPER--VIAMHFFNP 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 164 PRYLKLLEVIPTKETDPQVLSFMKLFGEDvLGKGVVIAKDTPNFIGNRI----GTYGLLVtLQEMIKrgySIGEVDSVTG 239
Cdd:PRK09260 144 VHKMKLVELIRGLETSDETVQVAKEVAEQ-MGKETVVVNEFPGFVTSRIsalvGNEAFYM-LQEGVA---TAEDIDKAIR 218

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446408496 240 PLIGRPKsATFRTLDVVGLDTFVHVANNVYENVQEEerdvFKVPTFMHDMLDKKWLGSKTGQGFF 304
Cdd:PRK09260 219 LGLNFPM-GPLELGDLVGLDTRLNNLKYLHETLGEK----YRPAPLLEKYVKAGRLGRKTGRGVY 278
fadJ PRK11154
fatty acid oxidation complex subunit alpha FadJ;
4-311 8.65e-23

fatty acid oxidation complex subunit alpha FadJ;


Pssm-ID: 236864 [Multi-domain]  Cd Length: 708  Bit Score: 103.82  E-value: 8.65e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496   4 IKKAAVLGSGVMGSGIA-AHLANIGIPTLLLDIvppaltkeeeakgltlEHKSVRN--RFSNTALQKLLKQK---PAPLT 77
Cdd:PRK11154 309 VNKVGVLGGGLMGGGIAyVTATKAGLPVRIKDI----------------NPQGINHalKYSWDLLDKKVKRRhlkPSERD 372

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  78 VKgnLALIEAGNledDLERLADVDWIIEVVVENLDIKKKLFERVDAVRKPGSIVSSNTSGISVEKMAEGRSDDFQkhFLG 157
Cdd:PRK11154 373 KQ--MALISGTT---DYRGFKHADVVIEAVFEDLALKQQMVAEVEQNCAPHTIFASNTSSLPIGQIAAAAARPEQ--VIG 445

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 158 THFFNPPRYLKLLEVIPTKETDPQVLSFMKLFGEDvLGKGVVIAKDTPNFIGNRIgtygLLVTLQE---MIKRGYSIGEV 234
Cdd:PRK11154 446 LHYFSPVEKMPLVEVIPHAKTSAETIATTVALAKK-QGKTPIVVRDGAGFYVNRI----LAPYINEaarLLLEGEPIEHI 520

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 235 DSV-------TGPLigrpksatfRTLDVVGLDtfvhVANNVYENVQEEERDVFKVPTFMHDMLDKKWLGSKTGQGFFL-- 305
Cdd:PRK11154 521 DAAlvkfgfpVGPI---------TLLDEVGID----VGTKIIPILEAALGERFSAPAAFDKLLNDDRKGRKNGRGFYLyg 587

                        330
                 ....*....|
gi 446408496 306 ----KQGKEI 311
Cdd:PRK11154 588 qkgkKSKKQV 597
crotonase-like cd06558
Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse ...
 482-609 1.05e-19

Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse set of enzymes including enoyl-CoA hydratase, napthoate synthase, methylmalonyl-CoA decarboxylase, 3-hydoxybutyryl-CoA dehydratase, and dienoyl-CoA isomerase. Many of these play important roles in fatty acid metabolism. In addition to a conserved structural core and the formation of trimers (or dimers of trimers), a common feature in this superfamily is the stabilization of an enolate anion intermediate derived from an acyl-CoA substrate. This is accomplished by two conserved backbone NH groups in active sites that form an oxyanion hole.


Pssm-ID: 119339 [Multi-domain]  Cd Length: 195  Bit Score: 87.62  E-value: 1.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 482 LIDLGDGILCLEFHS--KSNAIGMDITQMINYAVDEVEKN--YKGLVIGNQSKNFCVGANLAMilMEAQDDNYFEIELVV 557
Cdd:cd06558    2 LVERDGGVATITLNRpeKRNALSLEMLDELAAALDEAEADpdVRVVVLTGAGKAFCAGADLKE--LAALSDAGEEARAFI 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446408496 558 KNFQDAMTKIKYSSKPVVAAPYGMTLGGGTEVCLPAASIQASSETYMGLVEV 609
Cdd:cd06558   80 RELQELLRALLRLPKPVIAAVNGAALGGGLELALACDIRIAAEDAKFGLPEV 131
CaiD COG1024
Enoyl-CoA hydratase/carnithine racemase [Lipid transport and metabolism]; Enoyl-CoA hydratase ...
 482-613 3.94e-19

Enoyl-CoA hydratase/carnithine racemase [Lipid transport and metabolism]; Enoyl-CoA hydratase/carnithine racemase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440647 [Multi-domain]  Cd Length: 249  Bit Score: 87.53  E-value: 3.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 482 LIDLGDGILCLEFHS--KSNAIGMDITQMINYAVDEVEKN--YKGLVIGNQSKNFCVGANLAMILMEAQDDnyfEIELVV 557
Cdd:COG1024    2 LVEREGGVATITLNRpeKLNALSLEMLAELAAALDEAEADpdVRVVVLTGAGKAFCAGADLKELAAAADPE---EARAFA 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446408496 558 KNFQDAMTKIKYSSKPVVAAPYGMTLGGGTEVCLPAASIQASSETYMGLVEVGVGL 613
Cdd:COG1024   79 RGLQRLFRALRRLPKPVIAAVNGAALGGGLELALACDLRIAAEDARFGLPEVRLGL 134
PRK07531 PRK07531
carnitine 3-dehydrogenase;
1-212 1.62e-17

carnitine 3-dehydrogenase;


Pssm-ID: 236044 [Multi-domain]  Cd Length: 495  Bit Score: 86.33  E-value: 1.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496   1 MFQIKKAAVLGSGVMGSGIAAHLANIGIPTLLLDIVPPALTKEEEAkgltlehksVRNrfSNTALQKLLKqkpAPLTVKG 80
Cdd:PRK07531   1 MTMIMKAACIGGGVIGGGWAARFLLAGIDVAVFDPHPEAERIIGEV---------LAN--AERAYAMLTD---APLPPEG 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  81 NLALieAGNLEddlERLADVDWIIEVVVENLDIKKKLFERVDAVRKPGSIVSSNTSGISVEKMAEGrsddfQKH---FLG 157
Cdd:PRK07531  67 RLTF--CASLA---EAVAGADWIQESVPERLDLKRRVLAEIDAAARPDALIGSSTSGFLPSDLQEG-----MTHperLFV 136

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446408496 158 THFFNPPRYLKLLEVIPTKETDPQVLSFMKLFGEDVLGKGVVIAKDTPNFIGNRI 212
Cdd:PRK07531 137 AHPYNPVYLLPLVELVGGGKTSPETIRRAKEILREIGMKPVHIAKEIDAFVGDRL 191
PRK06129 PRK06129
3-hydroxyacyl-CoA dehydrogenase; Validated
 6-241 5.74e-17

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 235706 [Multi-domain]  Cd Length: 308  Bit Score: 82.40  E-value: 5.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496   6 KAAVLGSGVMGSGIAAHLANIGIPTLLLDIVPPALtkeEEAKGLtlehksVRNRFSNTALQKLLKQKPaPLTVkgnLALI 85
Cdd:PRK06129   4 SVAIIGAGLIGRAWAIVFARAGHEVRLWDADPAAA---AAAPAY------IAGRLEDLAAFDLLDGEA-PDAV---LARI 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  86 E-AGNLEDdleRLADVDWIIEVVVENLDIKKKLFERVDAVRKPGSIVSSNTSGISVEKMAEGRSDdfQKHFLGTHFFNPP 164
Cdd:PRK06129  71 RvTDSLAD---AVADADYVQESAPENLELKRALFAELDALAPPHAILASSTSALLASAFTEHLAG--RERCLVAHPINPP 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 165 RYLKLLEVIPTKETDPQVLSFMKLFGEDVLGKGVVIAKDTPNFIGNRIgtYGLLvtLQEM---IKRGY-SIGEVD----- 235
Cdd:PRK06129 146 YLIPVVEVVPAPWTAPATLARAEALYRAAGQSPVRLRREIDGFVLNRL--QGAL--LREAfrlVADGVaSVDDIDavird 221

                        250
                 ....*....|..
gi 446408496 236 ------SVTGPL 241
Cdd:PRK06129 222 glglrwSFMGPF 233
PRK08269 PRK08269
3-hydroxybutyryl-CoA dehydrogenase; Validated
 15-212 1.56e-14

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181340 [Multi-domain]  Cd Length: 314  Bit Score: 75.48  E-value: 1.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  15 MGSGIAAHLANIGIPTLLLDIvppaltKEEEAKGltlehksvRNRFSNTALQKLLkqkpAPLTVKGNLALIEAGNLEDDL 94
Cdd:PRK08269   1 MGQGIALAFAFAGHDVTLIDF------KPRDAAG--------WRALDAEARAEIE----RTLAALVALGRIDAAQADAVL 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  95 ER------------LADVDWIIEVVVENLDIKKKLFERVDAVRKPGSIVSSNTSGISVekmaegrsDDFQKH------FL 156
Cdd:PRK08269  63 ARiavvardgaadaLADADLVFEAVPEVLDAKREALRWLGRHVDADAIIASTTSTFLV--------TDLQRHvahperFL 134

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446408496 157 GTHFFNPPRYLKLLEVIPTKETDPQVLSFMKLFGEDVlGKGVVIAKDTPNFIGNRI 212
Cdd:PRK08269 135 NAHWLNPAYLMPLVEVSPSDATDPAVVDRLAALLERI-GKVPVVCGPSPGYIVPRI 189
PRK07066 PRK07066
L-carnitine dehydrogenase;
3-212 5.16e-14

L-carnitine dehydrogenase;


Pssm-ID: 168796 [Multi-domain]  Cd Length: 321  Bit Score: 73.72  E-value: 5.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496   3 QIKKAAVLGSGVMGSG-IAAHLANiGIPTLLLDIVPPAltkeeeakgltleHKSVRNRFSNtALQKLLKQKPAPLTVKGN 81
Cdd:PRK07066   6 DIKTFAAIGSGVIGSGwVARALAH-GLDVVAWDPAPGA-------------EAALRANVAN-AWPALERQGLAPGASPAR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  82 L---ALIEagnleddlERLADVDWIIEVVVENLDIKKKLFERVDAVRKPGSIVSSNTSGISVEKMAEgRSDDFQKHFLGt 158
Cdd:PRK07066  71 LrfvATIE--------ACVADADFIQESAPEREALKLELHERISRAAKPDAIIASSTSGLLPTDFYA-RATHPERCVVG- 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446408496 159 HFFNPPRYLKLLEVIPTKETDPQVLSFMKLFGEDVLGKGVVIAKDTPNFIGNRI 212
Cdd:PRK07066 141 HPFNPVYLLPLVEVLGGERTAPEAVDAAMGIYRALGMRPLHVRKEVPGFIADRL 194
3HCDH pfam00725
3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda ...
 207-304 3.20e-08

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: 51.83  E-value: 3.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  207 FIGNRIGtYGLLVTLQEMIKRGY-SIGEVDSVTGPLIGRPkSATFRTLDVVGLDTFVHVANNVYENVQEeerDVFKVPTF 285
Cdd:pfam00725   2 FVVNRLL-APYLNEAIRLVEEGVaTPEDIDAAMRLGLGLP-MGPFELSDLVGLDVGYHILEVLAEEFGD---RAYRPPPL 76

                          90
                  ....*....|....*....
gi 446408496  286 MHDMLDKKWLGSKTGQGFF 304
Cdd:pfam00725  77 LEKLVEAGRLGRKTGKGFY 95
PRK08150 PRK08150
crotonase/enoyl-CoA hydratase family protein;
483-608 1.32e-05

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 181254  Cd Length: 255  Bit Score: 47.32  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 483 IDLGDGILCLEFH--SKSNAIGMDITQMINYAVDEVEKNYKGLVIGNQSKNFCVGANLAmilmEAQDDNYFEIELVVKNF 560
Cdd:PRK08150   6 YELDGGVATIGLNrpAKRNALNDGLIAALRAAFARLPEGVRAVVLHGEGDHFCAGLDLS----ELRERDAGEGMHHSRRW 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 446408496 561 QDAMTKIKYSSKPVVAAPYGMTLGGGTEVClPAASIQASSE-TYMGLVE 608
Cdd:PRK08150  82 HRVFDKIQYGRVPVIAALHGAVVGGGLELA-SAAHIRVADEsTYFALPE 129
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
 495-609 8.48e-05

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: 45.98  E-value: 8.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  495 HSKSNAIGMDITQMINYAVDEVEKN---YKGLVIGNQSKNFCVGANLAMILMEAQDDnyfEIELVVKNFQDAMTKIKYSS 571
Cdd:TIGR02441  32 NSKVNTLSKELFAEFKEVMNELWTNeaiKSAVLISGKPGSFVAGADIQMIAACKTAQ---EVTQLSQEGQEMFERIEKSQ 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 446408496  572 KPVVAAPYGMTLGGGTEVCLPAASIQAS--SETYMGLVEV 609
Cdd:TIGR02441 109 KPIVAAISGSCLGGGLELALACHYRIATkdRKTLLGLPEV 148
PRK06142 PRK06142
crotonase/enoyl-CoA hydratase family protein;
483-609 1.13e-04

crotonase/enoyl-CoA hydratase family protein;


Pssm-ID: 235714  Cd Length: 272  Bit Score: 44.58  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 483 IDLGDGI--LCLEFHSKSNAIGMDITQMINYAVDEVEKN--YKGLVIGNQSKNFCVGANLAM-------ILMEAQDDNYF 551
Cdd:PRK06142  10 VELADHVaqVTLNRPGKGNAMNPAFWSELPEIFRWLDADpeVRAVVLSGSGKHFSYGIDLPAmagvfgqLGKDGLARPRT 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446408496 552 EIELVVKNFQDAMTKIKYSSKPVVAAPYGMTLGGGTEVCLpAASIQ-ASSETYMGLVEV 609
Cdd:PRK06142  90 DLRREILRLQAAINAVADCRKPVIAAVQGWCIGGGVDLIS-ACDMRyASADAKFSVREV 147
PRK07658 PRK07658
enoyl-CoA hydratase; Provisional
 487-608 2.11e-04

enoyl-CoA hydratase; Provisional


Pssm-ID: 181070 [Multi-domain]  Cd Length: 257  Bit Score: 43.85  E-value: 2.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 487 DGILCLEFHSK-SNAIGMDITQMINYAVDEVEKN--YKGLVIGNQSKNFCVGANLAMILMEAQDDNYfeiELVVKNFQDA 563
Cdd:PRK07658  10 DHVAVITLNHPpANALSSQVLHELSELLDQVEKDdnVRVVVIHGEGRFFSAGADIKEFTSVTEAEQA---TELAQLGQVT 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446408496 564 MTKIKYSSKPVVAAPYGMTLGGGTEVCLpAASIQ-ASSETYMGLVE 608
Cdd:PRK07658  87 FERVEKFSKPVIAAIHGAALGGGLELAM-SCHIRfATESAKLGLPE 131
PLN02664 PLN02664
enoyl-CoA hydratase/delta3,5-delta2,4-dienoyl-CoA isomerase
 473-601 2.64e-03

enoyl-CoA hydratase/delta3,5-delta2,4-dienoyl-CoA isomerase


Pssm-ID: 178269 [Multi-domain]  Cd Length: 275  Bit Score: 40.66  E-value: 2.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 473 VLKKNSGASLIDLGdgilcLEFHSKSNAIGMDITQMINYAVDEVEKNYKGLVI--GNQSKNFCVGANLAMILMEAQDDNY 550
Cdd:PLN02664   9 IIQKSPNSSVFHLN-----LNRPSQRNALSLDFFTEFPKALSSLDQNPNVSVIilSGAGDHFCSGIDLKTLNSISEQSSS 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446408496 551 FE-------IELVVKNFQDAMTKIKYSSKPVVAAPYGMTLGGGTEVcLPAASIQASSE 601
Cdd:PLN02664  84 GDrgrsgerLRRKIKFLQDAITAIEQCRKPVIAAIHGACIGGGVDI-VTACDIRYCSE 140
PRK05809 PRK05809
short-chain-enoyl-CoA hydratase;
499-609 3.05e-03

short-chain-enoyl-CoA hydratase;


Pssm-ID: 180270 [Multi-domain]  Cd Length: 260  Bit Score: 40.12  E-value: 3.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 499 NAIGMDITQMINYAVDEVEKN---YKGLVIGNQSKNFCVGANLAmilmEAQDDNYFEIELVVKNFQDAMTKIKYSSKPVV 575
Cdd:PRK05809  26 NALNSETLKELDTVLDDIENDdnvYAVILTGAGEKAFVAGADIS----EMKDLNEEEGRKFGLLGNKVFRKLENLDKPVI 101

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446408496 576 AAPYGMTLGGGTEVCLPAASIQASSETYMGLVEV 609
Cdd:PRK05809 102 AAINGFALGGGCELSMACDIRIASEKAKFGQPEV 135
PRK06688 PRK06688
enoyl-CoA hydratase; Provisional
 482-609 6.52e-03

enoyl-CoA hydratase; Provisional


Pssm-ID: 235852 [Multi-domain]  Cd Length: 259  Bit Score: 39.08  E-value: 6.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496 482 LIDLGDGILCLEFH--SKSNAIGMDITQMINYAVDEVEKN--YKGLVIGNQSKNFCVGANLAMILMEAQDDnyfeiELVV 557
Cdd:PRK06688   8 LVELEDGVLTITINrpDKKNALTAAMYQALADALEAAATDpaVRVVVLTGAGRAFSAGGDIKDFPKAPPKP-----PDEL 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446408496 558 KNFQDAMTKIKYSSKPVVAAPYGMTLGGGTEVCLPAASIQASSETYMGLVEV 609
Cdd:PRK06688  83 APVNRFLRAIAALPKPVVAAVNGPAVGVGVSLALACDLVYASESAKFSLPFA 134
3HCDH pfam00725
3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda ...
 380-432 8.00e-03

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: 36.43  E-value: 8.00e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446408496  380 DIVAIDQAMKWGFGWEQGPFEIWDAIG--VEKSIQK--MEENGVNVPA---WVKEMVEKG 432
Cdd:pfam00725  25 TPEDIDAAMRLGLGLPMGPFELSDLVGldVGYHILEvlAEEFGDRAYRpppLLEKLVEAG 84
 
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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