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Conserved domains on  [gi|491234295|ref|WP_005092523|]
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3-hydroxyacyl-CoA dehydrogenase family protein [Mycobacteroides abscessus]

Protein Classification

3-hydroxyacyl-CoA dehydrogenase family protein( domain architecture ID 11441205)

3-hydroxyacyl-CoA dehydrogenase (HCDH) family protein such as mitochondrial HCDH, which plays an essential role in the beta-oxidation of short chain fatty acids

CATH:  3.40.50.720|1.10.1040.10
EC:  1.1.1.-
Gene Ontology:  GO:0003857|GO:0006635|GO:0070403
PubMed:  3479790
SCOP:  4000107

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 ...
 12-285 2.94e-73

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: 226.15  E-value: 2.94e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  12 RPVAVLGAGTLGRRIALTFATRGGVVHLYDVSEESLQSAKEFLDQRIPELVKARSALGAQPAT----IEYYTDLpSAVKD 87
Cdd:COG1250    3 KKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKLVKKGKLTEEEADAalarITPTTDL-AALAD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  88 AWYVVESVPEVQALKIDMLGQLDEIAAPDAIIGTNSSSFMSSELIGKVKHPQRFLNTHYGQPPEA-PQAELVTDGHTNER 166
Cdd:COG1250   82 ADLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLmPLVEVIRGPATSDE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295 167 IFDI---LGAELPKhgfvTAVAHKESVGFIINRVWAAVKREALAVVAEGVSTPAEFDRIWVAS-GMsPIGVFRAIDRVGL 242
Cdd:COG1250  162 TVATavaFARRLGK----TPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGfGF-PMGPFELADLVGL 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 491234295 243 DVALDIEDNYIKHFPYIPTTSRDLLQQYVDEGKLGVKSGEGFY 285
Cdd:COG1250  237 DTALAVLEVLYEALGDPRYRPPPLLKKLVEAGRLGRKTGRGFY 279
 
Name Accession Description Interval E-value
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 12-285 2.94e-73

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: 226.15  E-value: 2.94e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  12 RPVAVLGAGTLGRRIALTFATRGGVVHLYDVSEESLQSAKEFLDQRIPELVKARSALGAQPAT----IEYYTDLpSAVKD 87
Cdd:COG1250    3 KKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKLVKKGKLTEEEADAalarITPTTDL-AALAD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  88 AWYVVESVPEVQALKIDMLGQLDEIAAPDAIIGTNSSSFMSSELIGKVKHPQRFLNTHYGQPPEA-PQAELVTDGHTNER 166
Cdd:COG1250   82 ADLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLmPLVEVIRGPATSDE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295 167 IFDI---LGAELPKhgfvTAVAHKESVGFIINRVWAAVKREALAVVAEGVSTPAEFDRIWVAS-GMsPIGVFRAIDRVGL 242
Cdd:COG1250  162 TVATavaFARRLGK----TPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGfGF-PMGPFELADLVGL 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 491234295 243 DVALDIEDNYIKHFPYIPTTSRDLLQQYVDEGKLGVKSGEGFY 285
Cdd:COG1250  237 DTALAVLEVLYEALGDPRYRPPPLLKKLVEAGRLGRKTGRGFY 279
PRK08293 PRK08293
3-hydroxyacyl-CoA dehydrogenase;
14-286 1.17e-54

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 181359 [Multi-domain]  Cd Length: 287  Bit Score: 178.98  E-value: 1.17e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  14 VAVLGAGTLGRRIALTFATRGGVVHLYDVSEESLQSAKEFLDQRIPELVKARSALGAQPAT-----IEYYTDLPSAVKDA 88
Cdd:PRK08293   6 VTVAGAGVLGSQIAFQTAFHGFDVTIYDISDEALEKAKERIAKLADRYVRDLEATKEAPAEaalnrITLTTDLAEAVKDA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  89 WYVVESVPEVQALKIDMLGQLDEIAAPDAIIGTNSSSFMSSELIGKVKHPQRFLNTHYGQPPEA-PQAELVtdGH--TNE 165
Cdd:PRK08293  86 DLVIEAVPEDPEIKGDFYEELAKVAPEKTIFATNSSTLLPSQFAEATGRPEKFLALHFANEIWKnNTAEIM--GHpgTDP 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295 166 RIFDILGAELPKHGFVTAVAHKESVGFIINRVWAAVKREALAVVAEGVSTPAEFDRIWVASGMSPIGVFRAIDRVGLDVA 245
Cdd:PRK08293 164 EVFDTVVAFAKAIGMVPIVLKKEQPGYILNSLLVPFLSAALALWAKGVADPETIDKTWMIATGAPMGPFGILDIVGLDTA 243

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 491234295 246 LDIEDNYikhfpyiPTTSRD--------LLQQYVDEGKLGVKSGEGFYH 286
Cdd:PRK08293 244 YNITSNW-------AEATDDenakkaaaLLKEYIDKGKLGVATGEGFYN 285
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
 14-173 1.51e-36

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


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 128.81  E-value: 1.51e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295   14 VAVLGAGTLGRRIALTFATRGGVVHLYDVSEESLQSAKEFLDQRIPELVKARSALGAQP----ATIEYYTDLPSAVkDAW 89
Cdd:pfam02737   2 VAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKGRITEEEVdaalARISFTTDLAAAV-DAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295   90 YVVESVPEVQALKIDMLGQLDEIAAPDAIIGTNSSSFMSSELIGKVKHPQRFLNTHYGQPPEA-PQAELVTDGHTNERIF 168
Cdd:pfam02737  81 LVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLmPLVEVVRGEKTSPETV 160


                  ....*
gi 491234295  169 DILGA 173
Cdd:pfam02737 161 ATTVE 165
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
 14-285 6.25e-24

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: 101.45  E-value: 6.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295   14 VAVLGAGTLGRRIALTFATRGGVVHLYDVSEESLQSAKEFLDQRIPELVKAR--------SALGAQPATIEYytdlpSAV 85
Cdd:TIGR02441 338 LAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLNKKVKRKkitslerdSILSNLTPTLDY-----SGF 412

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295   86 KDAWYVVESVPEVQALKIDMLGQLDEIAAPDAIIGTNSSSFMSSELIGKVKHPQRFLNTHYGQPPEAPQ-AELVT-DGHT 163
Cdd:TIGR02441 413 KNADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQlLEIIThDGTS 492

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  164 NERIFDILGAELpKHGFVTAVAhKESVGFIINRVWAAVKREALAVVAEGVStPAEFDRIWVASGMsPIGVFRAIDRVGLD 243
Cdd:TIGR02441 493 KDTLASAVAVGL-KQGKVVIVV-KDGPGFYTTRCLGPMLAEVIRLLQEGVD-PKKLDKLTTKFGF-PVGAATLADEVGVD 568

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 491234295  244 VALDIEDNYIKHF-PYIPTTSRDLLQQYVDEGKLGVKSGEGFY 285
Cdd:TIGR02441 569 VAEHVAEDLGKAFgERFGGGSAELLSELVKAGFLGRKSGKGIF 611
GH4_alpha_glucosidase_galactosidase cd05297
Glycoside Hydrolases Family 4; Alpha-glucosidases and alpha-galactosidases; Glucosidases ...
 14-95 5.98e-05

Glycoside Hydrolases Family 4; Alpha-glucosidases and alpha-galactosidases; Glucosidases cleave glycosidic bonds to release glucose from oligosaccharides. Alpha-glucosidases and alpha-galactosidases release alpha-D-glucose and alpha-D-galactose, respectively, via the hydrolysis of alpha-glycopyranoside bonds. Some bacteria simultaneously translocate and phosphorylate disaccharides via the phosphoenolpyruvate-dependent phosphotransferase system (PEP-PTS). After translocation, these phospho-disaccharides may be hydrolyzed by the GH4 glycoside hydrolases such as the alpha-glucosidases. Other organsisms (such as archaea and Thermotoga maritima) lack the PEP-PTS system, but have several enzymes normally associated with the PEP-PTS operon. Alpha-glucosidases and alpha-galactosidases are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133433 [Multi-domain]  Cd Length: 423  Bit Score: 44.09  E-value: 5.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  14 VAVLGAGTLG------RRIALTFATRGGVVHLYDVSEESLQSAKEFLDqripelvKARSALGAqPATIEYYTDLPSAVKD 87
Cdd:cd05297    3 IAFIGAGSVVftknlvGDLLKTPELSGSTIALMDIDEERLETVEILAK-------KIVEELGA-PLKIEATTDRREALDG 74


                 ....*...
gi 491234295  88 AWYVVESV 95
Cdd:cd05297   75 ADFVINTI 82
 
Name Accession Description Interval E-value
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 12-285 2.94e-73

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: 226.15  E-value: 2.94e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  12 RPVAVLGAGTLGRRIALTFATRGGVVHLYDVSEESLQSAKEFLDQRIPELVKARSALGAQPAT----IEYYTDLpSAVKD 87
Cdd:COG1250    3 KKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKLVKKGKLTEEEADAalarITPTTDL-AALAD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  88 AWYVVESVPEVQALKIDMLGQLDEIAAPDAIIGTNSSSFMSSELIGKVKHPQRFLNTHYGQPPEA-PQAELVTDGHTNER 166
Cdd:COG1250   82 ADLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLmPLVEVIRGPATSDE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295 167 IFDI---LGAELPKhgfvTAVAHKESVGFIINRVWAAVKREALAVVAEGVSTPAEFDRIWVAS-GMsPIGVFRAIDRVGL 242
Cdd:COG1250  162 TVATavaFARRLGK----TPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGfGF-PMGPFELADLVGL 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 491234295 243 DVALDIEDNYIKHFPYIPTTSRDLLQQYVDEGKLGVKSGEGFY 285
Cdd:COG1250  237 DTALAVLEVLYEALGDPRYRPPPLLKKLVEAGRLGRKTGRGFY 279
PRK08293 PRK08293
3-hydroxyacyl-CoA dehydrogenase;
14-286 1.17e-54

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 181359 [Multi-domain]  Cd Length: 287  Bit Score: 178.98  E-value: 1.17e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  14 VAVLGAGTLGRRIALTFATRGGVVHLYDVSEESLQSAKEFLDQRIPELVKARSALGAQPAT-----IEYYTDLPSAVKDA 88
Cdd:PRK08293   6 VTVAGAGVLGSQIAFQTAFHGFDVTIYDISDEALEKAKERIAKLADRYVRDLEATKEAPAEaalnrITLTTDLAEAVKDA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  89 WYVVESVPEVQALKIDMLGQLDEIAAPDAIIGTNSSSFMSSELIGKVKHPQRFLNTHYGQPPEA-PQAELVtdGH--TNE 165
Cdd:PRK08293  86 DLVIEAVPEDPEIKGDFYEELAKVAPEKTIFATNSSTLLPSQFAEATGRPEKFLALHFANEIWKnNTAEIM--GHpgTDP 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295 166 RIFDILGAELPKHGFVTAVAHKESVGFIINRVWAAVKREALAVVAEGVSTPAEFDRIWVASGMSPIGVFRAIDRVGLDVA 245
Cdd:PRK08293 164 EVFDTVVAFAKAIGMVPIVLKKEQPGYILNSLLVPFLSAALALWAKGVADPETIDKTWMIATGAPMGPFGILDIVGLDTA 243

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 491234295 246 LDIEDNYikhfpyiPTTSRD--------LLQQYVDEGKLGVKSGEGFYH 286
Cdd:PRK08293 244 YNITSNW-------AEATDDenakkaaaLLKEYIDKGKLGVATGEGFYN 285
PRK06130 PRK06130
3-hydroxybutyryl-CoA dehydrogenase; Validated
 12-290 2.34e-42

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 235707 [Multi-domain]  Cd Length: 311  Bit Score: 147.61  E-value: 2.34e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  12 RPVAVLGAGTLGRRIALTFATRGGVVHLYDVSEESLQSAKEFLDQRIPELVKARSALGAQpATIEYYTDLPSAVKDAWYV 91
Cdd:PRK06130   5 QNLAIIGAGTMGSGIAALFARKGLQVVLIDVMEGALERARGVIERALGVYAPLGIASAGM-GRIRMEAGLAAAVSGADLV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  92 VESVPEVQALKIDMLGQLDEIAAPDAIIGTNSSSFMSSELIGKVKHPQRFLNTHYGQPPEA-PQAELVTDGHTNERIFDI 170
Cdd:PRK06130  84 IEAVPEKLELKRDVFARLDGLCDPDTIFATNTSGLPITAIAQAVTRPERFVGTHFFTPADViPLVEVVRGDKTSPQTVAT 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295 171 LGAELPKHGFVTAVAHKESVGFIINRVWAAVKREALAVVAEGVSTPAEFDRI--W-VASGMSPIGVFRAIDRVGLDVALD 247
Cdd:PRK06130 164 TMALLRSIGKRPVLVKKDIPGFIANRIQHALAREAISLLEKGVASAEDIDEVvkWsLGIRLALTGPLEQRDMNGLDVHLA 243

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 491234295 248 IEDnYIKHFPYIPTTSRDLLQQYVDEGKLGVKSGEGFYHDCPE 290
Cdd:PRK06130 244 VAS-YLYQDLENRTTPSPLLEEKVEAGELGAKSGQGFYAWPPE 285
PRK05808 PRK05808
3-hydroxybutyryl-CoA dehydrogenase; Validated
 14-285 8.46e-41

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 180269 [Multi-domain]  Cd Length: 282  Bit Score: 142.79  E-value: 8.46e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  14 VAVLGAGTLGRRIALTFATRGGVVHLYDVSEESLQSAKEFLDQRIPELVKARSALGAQPAT----IEYYTDLpSAVKDAW 89
Cdd:PRK05808   6 IGVIGAGTMGNGIAQVCAVAGYDVVMVDISDAAVDRGLATITKSLDRLVKKGKMTEADKEAalarITGTTDL-DDLKDAD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  90 YVVESVPEVQALKIDMLGQLDEIAAPDAIIGTNSSSFMSSELIGKVKHPQRFLNTHYGQPpeAPQAELV-------TDGH 162
Cdd:PRK05808  85 LVIEAATENMDLKKKIFAQLDEIAKPEAILATNTSSLSITELAAATKRPDKVIGMHFFNP--VPVMKLVeiirglaTSDA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295 163 TNERIFDiLGAELPKhgfvTAVAHKESVGFIINRVWAAVKREALAVVAEGVSTPAEFDriwvaSGMS-----PIGVFRAI 237
Cdd:PRK05808 163 THEAVEA-LAKKIGK----TPVEVKNAPGFVVNRILIPMINEAIFVLAEGVATAEDID-----EGMKlgcnhPIGPLALA 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 491234295 238 DRVGLDVALDIEDNYIKHF---PYIPTTsrdLLQQYVDEGKLGVKSGEGFY 285
Cdd:PRK05808 233 DLIGLDTCLAIMEVLYEGFgdsKYRPCP---LLRKMVAAGWLGRKTGRGFY 280
PLN02545 PLN02545
3-hydroxybutyryl-CoA dehydrogenase
 14-286 1.07e-38

3-hydroxybutyryl-CoA dehydrogenase


Pssm-ID: 215300 [Multi-domain]  Cd Length: 295  Bit Score: 137.55  E-value: 1.07e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  14 VAVLGAGTLGRRIALTFATRGGVVHLYDVSEESLQSAKEFLDQRIPELVKARSALGAQP----ATIEYYTDLpSAVKDAW 89
Cdd:PLN02545   7 VGVVGAGQMGSGIAQLAAAAGMDVWLLDSDPAALSRGLDSISSSLARLVKKGKMSQEEAdatlGRIRCTTNL-EELRDAD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  90 YVVESVPEVQALKIDMLGQLDEIAAPDAIIGTNSSSFMSSELIGKVKHPQRFLNTHYGQPPE-APQAELVTDGHTNERIF 168
Cdd:PLN02545  86 FIIEAIVESEDLKKKLFSELDRICKPSAILASNTSSISITRLASATQRPQQVIGMHFMNPPPiMKLVEIIRGADTSDEVF 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295 169 DILGAELPKHGfVTAVAHKESVGFIINRVWAAVKREALAVVAEGVSTPAEFDRiwvasGMS-----PIGVFRAIDRVGLD 243
Cdd:PLN02545 166 DATKALAERFG-KTVVCSQDYPGFIVNRILMPMINEAFYALYTGVASKEDIDT-----GMKlgtnhPMGPLHLADFIGLD 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 491234295 244 VALDIEDNYIKHF---PYIPTTsrdLLQQYVDEGKLGVKSGEGFYH 286
Cdd:PLN02545 240 TCLSIMKVLHEGLgdsKYRPCP---LLVQYVDAGRLGRKSGRGVYH 282
PRK06129 PRK06129
3-hydroxyacyl-CoA dehydrogenase; Validated
 12-238 2.85e-38

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 235706 [Multi-domain]  Cd Length: 308  Bit Score: 137.10  E-value: 2.85e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  12 RPVAVLGAGTLGRRIALTFATRGGVVHLYDVSEESLQSAKEFLDQRIPELVKARSALGAQPAT----IEYYTDLPSAVKD 87
Cdd:PRK06129   3 GSVAIIGAGLIGRAWAIVFARAGHEVRLWDADPAAAAAAPAYIAGRLEDLAAFDLLDGEAPDAvlarIRVTDSLADAVAD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  88 AWYVVESVPEVQALKIDMLGQLDEIAAPDAIIGTNSSSFMSSELIGKVKHPQRFLNTHYGQPPE-APQAELV----TDGH 162
Cdd:PRK06129  83 ADYVQESAPENLELKRALFAELDALAPPHAILASSTSALLASAFTEHLAGRERCLVAHPINPPYlIPVVEVVpapwTAPA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295 163 TNERIFDILGAElpkhGFVTAVAHKESVGFIINRVWAAVKREALAVVAEGVSTPAEFDRIwVASGM----SPIGVFRAID 238
Cdd:PRK06129 163 TLARAEALYRAA----GQSPVRLRREIDGFVLNRLQGALLREAFRLVADGVASVDDIDAV-IRDGLglrwSFMGPFETID 237
PRK09260 PRK09260
3-hydroxyacyl-CoA dehydrogenase;
14-285 4.15e-37

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 236434 [Multi-domain]  Cd Length: 288  Bit Score: 133.38  E-value: 4.15e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  14 VAVLGAGTLGRRIALTFATRGGVVHLYDVSEESLQSAKefldQRIPELVKARSALG--------AQPATIEYYTDLPSAV 85
Cdd:PRK09260   4 LVVVGAGVMGRGIAYVFAVSGFQTTLVDIKQEQLESAQ----QEIASIFEQGVARGklteaarqAALARLSYSLDLKAAV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  86 KDAWYVVESVPEVQALKIDMLGQLDEIAAPDAIIGTNSSSFMSSELIGKVKHPQRFLNTHYGQP-PEAPQAELVTDGHTN 164
Cdd:PRK09260  80 ADADLVIEAVPEKLELKKAVFETADAHAPAECYIATNTSTMSPTEIASFTKRPERVIAMHFFNPvHKMKLVELIRGLETS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295 165 ERIFDILGAELPKHGfVTAVAHKESVGFIINRVWAAVKREALAVVAEGVSTPAEFDRIWVASGMSPIGVFRAIDRVGLDV 244
Cdd:PRK09260 160 DETVQVAKEVAEQMG-KETVVVNEFPGFVTSRISALVGNEAFYMLQEGVATAEDIDKAIRLGLNFPMGPLELGDLVGLDT 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 491234295 245 ALDIednyikhFPYIPTTSRD------LLQQYVDEGKLGVKSGEGFY 285
Cdd:PRK09260 239 RLNN-------LKYLHETLGEkyrpapLLEKYVKAGRLGRKTGRGVY 278
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
 14-173 1.51e-36

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


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 128.81  E-value: 1.51e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295   14 VAVLGAGTLGRRIALTFATRGGVVHLYDVSEESLQSAKEFLDQRIPELVKARSALGAQP----ATIEYYTDLPSAVkDAW 89
Cdd:pfam02737   2 VAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKGRITEEEVdaalARISFTTDLAAAV-DAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295   90 YVVESVPEVQALKIDMLGQLDEIAAPDAIIGTNSSSFMSSELIGKVKHPQRFLNTHYGQPPEA-PQAELVTDGHTNERIF 168
Cdd:pfam02737  81 LVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLmPLVEVVRGEKTSPETV 160


                  ....*
gi 491234295  169 DILGA 173
Cdd:pfam02737 161 ATTVE 165
PRK08268 PRK08268
3-hydroxy-acyl-CoA dehydrogenase; Validated
 7-285 2.81e-32

3-hydroxy-acyl-CoA dehydrogenase; Validated


Pssm-ID: 236211 [Multi-domain]  Cd Length: 507  Bit Score: 124.57  E-value: 2.81e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295   7 ADIDNRPVAVLGAGTLGRRIALTFATRGGVVHLYDVSEESLQSAKEFLDQRIPELVK-------ARSALGA--QPAtiey 77
Cdd:PRK08268   3 ALPSIATVAVIGAGAMGAGIAQVAAQAGHTVLLYDARAGAAAAARDGIAARLAKLVEkgkltaeQADAALArlRPV---- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  78 yTDLpSAVKDAWYVVESVPEVQALKIDMLGQLDEIAAPDAIIGTNSSSFMSSELIGKVKHPQRFLNTHYGQPpeAPQAEL 157
Cdd:PRK08268  79 -EAL-ADLADCDLVVEAIVERLDVKQALFAQLEAIVSPDCILATNTSSLSITAIAAALKHPERVAGLHFFNP--VPLMKL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295 158 V-------TDGHTNERIFDiLGAELPKhgfvTAVAHKESVGFIINRVWAAVKREALAVVAEGVSTPAEFDRIWVASGMSP 230
Cdd:PRK08268 155 VevvsglaTDPAVADALYA-LARAWGK----TPVRAKDTPGFIVNRAARPYYTEALRVLEEGVADPATIDAILREAAGFR 229

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 491234295 231 IGVFRAIDRVGLDVAL----DIEDNYIKHFPYIPTTsrdLLQQYVDEGKLGVKSGEGFY 285
Cdd:PRK08268 230 MGPFELMDLIGLDVNHavmeSVYRQFYQEPRFRPSL---IQQELVAAGRLGRKSGQGFY 285
PRK07819 PRK07819
3-hydroxybutyryl-CoA dehydrogenase; Validated
 14-286 1.59e-27

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181133 [Multi-domain]  Cd Length: 286  Bit Score: 107.76  E-value: 1.59e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  14 VAVLGAGTLGRRIALTFATRGGVVHLYDVSEESLQSAKEFLDQRIPELVKA----RSALGAQPATIEYYTDLpSAVKDAW 89
Cdd:PRK07819   8 VGVVGAGQMGAGIAEVCARAGVDVLVFETTEELATAGRNRIEKSLERAVSRgkltERERDAALARLRFTTDL-GDFADRQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  90 YVVESVPEVQALKIDMLGQLDEI-AAPDAIIGTNSSSFMSSELIGKVKHPQRFLNTHYGQP-PEAPQAELVTDGHTNERI 167
Cdd:PRK07819  87 LVIEAVVEDEAVKTEIFAELDKVvTDPDAVLASNTSSIPIMKLAAATKRPGRVLGLHFFNPvPVLPLVELVPTLVTSEAT 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295 168 FDIlgAElpkhGFVTAVAHKESV------GFIINRVWAAVKREALAVVAEGVSTPAEFDRIWVASGMSPIGVFRAIDRVG 241
Cdd:PRK07819 167 VAR--AE----EFASDVLGKQVVraqdrsGFVVNALLVPYLLSAIRMVESGFATAEDIDKAMVLGCAHPMGPLRLSDLVG 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 491234295 242 LDVALDIEDNYIKHFP---YIPTTsrdLLQQYVDEGKLGVKSGEGFYH 286
Cdd:PRK07819 241 LDTVKAIADSMYEEFKeplYAPPP---LLLRMVEAGLLGKKSGRGFYT 285
PRK08269 PRK08269
3-hydroxybutyryl-CoA dehydrogenase; Validated
 22-285 8.76e-26

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181340 [Multi-domain]  Cd Length: 314  Bit Score: 103.98  E-value: 8.76e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  22 LGRRIALTFATRGGVVHLYDVSEESLQSAKEFLDQRIPELVK---ARSALG------AQP--ATIEYYT--DLPSAVKDA 88
Cdd:PRK08269   1 MGQGIALAFAFAGHDVTLIDFKPRDAAGWRALDAEARAEIERtlaALVALGridaaqADAvlARIAVVArdGAADALADA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  89 WYVVESVPEVQALKIDMLGQLDEIAAPDAIIGTNSSSFMSSELIGKVKHPQRFLNTHYGQPPE-APQAELVTDGHTNERI 167
Cdd:PRK08269  81 DLVFEAVPEVLDAKREALRWLGRHVDADAIIASTTSTFLVTDLQRHVAHPERFLNAHWLNPAYlMPLVEVSPSDATDPAV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295 168 FDILGAELPKHGFVTAVAhKESVGFIINRVWAAVKREALAVVAEGVSTPAEFD---RIWVASGMSPIGVFRAIDRVGLDV 244
Cdd:PRK08269 161 VDRLAALLERIGKVPVVC-GPSPGYIVPRIQALAMNEAARMVEEGVASAEDIDkaiRTGFGLRFAVLGLLEFIDWGGCDI 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 491234295 245 aLDIEDNY----IKHFPYIPTtsrDLLQQYVDEGKLGVKSGEGFY 285
Cdd:PRK08269 240 -LYYASRYlageIGPDRFAPP---AIVVRNMEEGRDGLRTGAGFY 280
PRK07530 PRK07530
3-hydroxybutyryl-CoA dehydrogenase; Validated
 12-292 1.88e-24

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181018 [Multi-domain]  Cd Length: 292  Bit Score: 99.70  E-value: 1.88e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  12 RPVAVLGAGTLGRRIALTFATRGGVVHLYDVSEESLQSAKEFLDQRIPELVK----ARSALGAQPATIEYYTDLpSAVKD 87
Cdd:PRK07530   5 KKVGVIGAGQMGNGIAHVCALAGYDVLLNDVSADRLEAGLATINGNLARQVAkgkiSEEARAAALARISTATDL-EDLAD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  88 AWYVVESVPEVQALKIDMLGQLDEIAAPDAIIGTNSSSFMSSELIGKVKHPQRFLNTHYGQP-PEAPQAELVTDGHTNER 166
Cdd:PRK07530  84 CDLVIEAATEDETVKRKIFAQLCPVLKPEAILATNTSSISITRLASATDRPERFIGIHFMNPvPVMKLVELIRGIATDEA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295 167 IFDILGAELPKHGFVTAVAhKESVGFIINRVWAAVKREALAVVAEGVSTPAEFDRIWVASGMSPIGVFRAIDRVGLDVAL 246
Cdd:PRK07530 164 TFEAAKEFVTKLGKTITVA-EDFPAFIVNRILLPMINEAIYTLYEGVGSVEAIDTAMKLGANHPMGPLELADFIGLDTCL 242

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 491234295 247 DIEDnyIKHFPYIPTTSR--DLLQQYVDEGKLGVKSGEGFY---HDCPEPS 292
Cdd:PRK07530 243 SIMQ--VLHDGLADSKYRpcPLLVKYVEAGWLGRKTGRGFYdyrGEVPVPT 291
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
 14-285 6.25e-24

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: 101.45  E-value: 6.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295   14 VAVLGAGTLGRRIALTFATRGGVVHLYDVSEESLQSAKEFLDQRIPELVKAR--------SALGAQPATIEYytdlpSAV 85
Cdd:TIGR02441 338 LAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLNKKVKRKkitslerdSILSNLTPTLDY-----SGF 412

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295   86 KDAWYVVESVPEVQALKIDMLGQLDEIAAPDAIIGTNSSSFMSSELIGKVKHPQRFLNTHYGQPPEAPQ-AELVT-DGHT 163
Cdd:TIGR02441 413 KNADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQlLEIIThDGTS 492

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  164 NERIFDILGAELpKHGFVTAVAhKESVGFIINRVWAAVKREALAVVAEGVStPAEFDRIWVASGMsPIGVFRAIDRVGLD 243
Cdd:TIGR02441 493 KDTLASAVAVGL-KQGKVVIVV-KDGPGFYTTRCLGPMLAEVIRLLQEGVD-PKKLDKLTTKFGF-PVGAATLADEVGVD 568

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 491234295  244 VALDIEDNYIKHF-PYIPTTSRDLLQQYVDEGKLGVKSGEGFY 285
Cdd:TIGR02441 569 VAEHVAEDLGKAFgERFGGGSAELLSELVKAGFLGRKSGKGIF 611
PRK06035 PRK06035
3-hydroxyacyl-CoA dehydrogenase; Validated
 10-279 2.54e-23

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 180361 [Multi-domain]  Cd Length: 291  Bit Score: 96.87  E-value: 2.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  10 DNRPVAVLGAGTLGRRIALTFATRGGVVHLYDVSEESLQSAKEFLDQR---IPELVK----ARSALGAQPATIEYYTDLp 82
Cdd:PRK06035   2 DIKVIGVVGSGVMGQGIAQVFARTGYDVTIVDVSEEILKNAMELIESGpygLRNLVEkgkmSEDEAKAIMARIRTSTSY- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  83 SAVKDAWYVVESVPEVQALKIDMLGQLDEIAAPDAIIGTNSSSFMSSELIGKVKHPQRFLNTHYGQP-PEAPQAELVTDG 161
Cdd:PRK06035  81 ESLSDADFIVEAVPEKLDLKRKVFAELERNVSPETIIASNTSGIMIAEIATALERKDRFIGMHWFNPaPVMKLIEVVRAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295 162 HTNERIFDILgAELPKHGFVTAVAHKESVGFIINRVWAAVKREALAVVAEGVSTPAEFDRIWVASGMSPIGVFRAIDRVG 241
Cdd:PRK06035 161 LTSEETFNTT-VELSKKIGKIPIEVADVPGFFTTRFIEGWLLEAIRSFEIGIATIKDIDEMCKLAFGFPMGPFELMDIIG 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 491234295 242 LDVALDIED---NYIKHFPYIPTTSrdlLQQYVDEGKLGVK 279
Cdd:PRK06035 240 IDTVYHIAEylyEETGDPQFIPPNS---LKQMVLNGYVGDK 277
PRK07066 PRK07066
L-carnitine dehydrogenase;
10-220 1.05e-20

L-carnitine dehydrogenase;


Pssm-ID: 168796 [Multi-domain]  Cd Length: 321  Bit Score: 89.89  E-value: 1.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  10 DNRPVAVLGAGTLGRRIALTFATRGGVVHLYDVSEESLQSAKEFLDQRIPELVKARSALGAQPATIEYYTDLPSAVKDAW 89
Cdd:PRK07066   6 DIKTFAAIGSGVIGSGWVARALAHGLDVVAWDPAPGAEAALRANVANAWPALERQGLAPGASPARLRFVATIEACVADAD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  90 YVVESVPEVQALKIDMLGQLDEIAAPDAIIGTNSSSFMSSELIGKVKHPQRFLNTHYGQP----------------PEAP 153
Cdd:PRK07066  86 FIQESAPEREALKLELHERISRAAKPDAIIASSTSGLLPTDFYARATHPERCVVGHPFNPvyllplvevlggertaPEAV 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491234295 154 QAELvtdghtneRIFDILGAElPKHgfvtavAHKESVGFIINRVWAAVKREALAVVAEGVSTPAEFD 220
Cdd:PRK07066 166 DAAM--------GIYRALGMR-PLH------VRKEVPGFIADRLLEALWREALHLVNEGVATTGEID 217
PRK07531 PRK07531
carnitine 3-dehydrogenase;
15-222 1.47e-20

carnitine 3-dehydrogenase;


Pssm-ID: 236044 [Multi-domain]  Cd Length: 495  Bit Score: 91.34  E-value: 1.47e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  15 AVLGAGTLGRRIALTFATRGGVVHLYDVSEESLQSAKEFLDQripelvkARSALGA-------QPATIEYYTDLPSAVKD 87
Cdd:PRK07531   8 ACIGGGVIGGGWAARFLLAGIDVAVFDPHPEAERIIGEVLAN-------AERAYAMltdaplpPEGRLTFCASLAEAVAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  88 AWYVVESVPEVQALKIDMLGQLDEIAAPDAIIGTNSSSFMSSELIGKVKHPQRFLNTHYGQPPE-APQAELVTDGHTN-- 164
Cdd:PRK07531  81 ADWIQESVPERLDLKRRVLAEIDAAARPDALIGSSTSGFLPSDLQEGMTHPERLFVAHPYNPVYlLPLVELVGGGKTSpe 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295 165 --ERIFDILgAELPKHGFVTAvahKESVGFIINRVWAAVKREALAVVAEGVSTPAEFDRI 222
Cdd:PRK07531 161 tiRRAKEIL-REIGMKPVHIA---KEIDAFVGDRLLEALWREALWLVKDGIATTEEIDDV 216
3HCDH pfam00725
3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda ...
 191-285 1.14e-19

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: 81.88  E-value: 1.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  191 GFIINRVWAAVKREALAVVAEGVSTPAEFDRIWVAS-GMsPIGVFRAIDRVGLDVALDIEDNYIKHFPYIPTTSRDLLQQ 269
Cdd:pfam00725   1 GFVVNRLLAPYLNEAIRLVEEGVATPEDIDAAMRLGlGL-PMGPFELSDLVGLDVGYHILEVLAEEFGDRAYRPPPLLEK 79

                          90
                  ....*....|....*.
gi 491234295  270 YVDEGKLGVKSGEGFY 285
Cdd:pfam00725  80 LVEAGRLGRKTGKGFY 95
fadJ PRK11154
fatty acid oxidation complex subunit alpha FadJ;
7-285 2.93e-19

fatty acid oxidation complex subunit alpha FadJ;


Pssm-ID: 236864 [Multi-domain]  Cd Length: 708  Bit Score: 87.64  E-value: 2.93e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295   7 ADIDNRP---VAVLGAGTLGRRIALTFATRGGV-VHLYDVSEESLQSAKEFLDQRIPELVKAR----SALGAQPATIEYY 78
Cdd:PRK11154 302 SDAKPRPvnkVGVLGGGLMGGGIAYVTATKAGLpVRIKDINPQGINHALKYSWDLLDKKVKRRhlkpSERDKQMALISGT 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  79 TDLpSAVKDAWYVVESVPEVQALKIDMLGQLDEIAAPDAIIGTNSSSFMSSELIGKVKHPQRFLNTHYGQPPEA-PQAEL 157
Cdd:PRK11154 382 TDY-RGFKHADVVIEAVFEDLALKQQMVAEVEQNCAPHTIFASNTSSLPIGQIAAAAARPEQVIGLHYFSPVEKmPLVEV 460

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295 158 VTDGHTNERIFDILGAELPKHGfVTAVAHKESVGFIINRVWAAVKREALAVVAEGVSTpAEFDRIWVASGMsPIGVFRAI 237
Cdd:PRK11154 461 IPHAKTSAETIATTVALAKKQG-KTPIVVRDGAGFYVNRILAPYINEAARLLLEGEPI-EHIDAALVKFGF-PVGPITLL 537

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 491234295 238 DRVGLDVALDI----EDNYIKHFpyiptTSRDLLQQYVDEGKLGVKSGEGFY 285
Cdd:PRK11154 538 DEVGIDVGTKIipilEAALGERF-----SAPAAFDKLLNDDRKGRKNGRGFY 584
fadB PRK11730
fatty acid oxidation complex subunit alpha FadB;
14-285 8.29e-13

fatty acid oxidation complex subunit alpha FadB;


Pssm-ID: 183293 [Multi-domain]  Cd Length: 715  Bit Score: 68.35  E-value: 8.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  14 VAVLGAGTLGRRIALTFATRGGVVHLYDVSEESLQS----AKEFLDQRI------PElvKARSALGAQPATIEYytdlpS 83
Cdd:PRK11730 316 AAVLGAGIMGGGIAYQSASKGVPVIMKDINQKALDLgmteAAKLLNKQVergkidGA--KMAGVLSSIRPTLDY-----A 388

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  84 AVKDAWYVVESVPEVQALKIDMLGQLDEIAAPDAIIGTNSSSFMSSELIGKVKHPQRFLNTHYGQP-PEAPQAELVTDGH 162
Cdd:PRK11730 389 GFERVDVVVEAVVENPKVKAAVLAEVEQKVREDTILASNTSTISISLLAKALKRPENFCGMHFFNPvHRMPLVEVIRGEK 468

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295 163 TNERIFDILGAELPKHGfVTAVAHKESVGFIINRVWAAVKREALAVVAEGvstpAEFDRI---------WvasgmsPIGV 233
Cdd:PRK11730 469 TSDETIATVVAYASKMG-KTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDG----ADFRQIdkvmekqfgW------PMGP 537

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 491234295 234 FRAIDRVGLDVALDIEDNYIKHFP-YIPTTSRDLLQQYVDEGKLGVKSGEGFY 285
Cdd:PRK11730 538 AYLLDVVGIDTAHHAQAVMAEGFPdRMKKDYRDAIDVLFEAKRFGQKNGKGFY 590
gpsA PRK00094
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;
14-119 4.26e-06

NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;


Pssm-ID: 234629 [Multi-domain]  Cd Length: 325  Bit Score: 47.37  E-value: 4.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  14 VAVLGAGTLGRRIALTFATRGGVVHLYDVSEESlqsAKEFLDQRIPELVKARSALgaqPATIEYYTDLPSAVKDAWYVVE 93
Cdd:PRK00094   4 IAVLGAGSWGTALAIVLARNGHDVTLWARDPEQ---AAEINADRENPRYLPGIKL---PDNLRATTDLAEALADADLILV 77

                         90       100
                 ....*....|....*....|....*.
gi 491234295  94 SVPeVQALKiDMLGQLDEIAAPDAII 119
Cdd:PRK00094  78 AVP-SQALR-EVLKQLKPLLPPDAPI 101
GpsA COG0240
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
 14-119 8.04e-06

Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate dehydrogenase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440010 [Multi-domain]  Cd Length: 327  Bit Score: 46.57  E-value: 8.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  14 VAVLGAGTLGRRIALTFATRGGVVHLYDVSEE---SLQSAKE---FL-DQRIPELVKArsalgaqpatieyYTDLPSAVK 86
Cdd:COG0240    3 IAVLGAGSWGTALAKVLARNGHEVTLWGRDPEvaeEINETREnprYLpGVKLPENLRA-------------TSDLEEALA 69

                         90       100       110
                 ....*....|....*....|....*....|...
gi 491234295  87 DAWYVVESVPeVQALKiDMLGQLDEIAAPDAII 119
Cdd:COG0240   70 GADLVLLAVP-SQALR-EVLEQLAPLLPPGAPV 100
NAD_Gly3P_dh_N pfam01210
NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent ...
 13-119 3.03e-05

NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent glycerol-3-phosphate dehydrogenase (GPDH) catalyzes the interconversion of dihydroxyacetone phosphate and L-glycerol-3-phosphate. This family represents the N-terminal NAD-binding domain.


Pssm-ID: 395967 [Multi-domain]  Cd Length: 158  Bit Score: 43.33  E-value: 3.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295   13 PVAVLGAGTLGRRIALTFATRGGVVHLYDVSEESLQSAKEfldqripELVKARSALGAQ-PATIEYYTDLPSAVKDAWYV 91
Cdd:pfam01210   1 KIAVLGAGSWGTALAKVLADNGHEVRLWGRDEELIEEINT-------THENVRYLPGIKlPENLKATTDLAEALKGADII 73

                          90       100
                  ....*....|....*....|....*...
gi 491234295   92 VESVPeVQALKiDMLGQLDEIAAPDAII 119
Cdd:pfam01210  74 VIVVP-SQALR-EVLKQLKGLLKPDAIL 99
GH4_alpha_glucosidase_galactosidase cd05297
Glycoside Hydrolases Family 4; Alpha-glucosidases and alpha-galactosidases; Glucosidases ...
 14-95 5.98e-05

Glycoside Hydrolases Family 4; Alpha-glucosidases and alpha-galactosidases; Glucosidases cleave glycosidic bonds to release glucose from oligosaccharides. Alpha-glucosidases and alpha-galactosidases release alpha-D-glucose and alpha-D-galactose, respectively, via the hydrolysis of alpha-glycopyranoside bonds. Some bacteria simultaneously translocate and phosphorylate disaccharides via the phosphoenolpyruvate-dependent phosphotransferase system (PEP-PTS). After translocation, these phospho-disaccharides may be hydrolyzed by the GH4 glycoside hydrolases such as the alpha-glucosidases. Other organsisms (such as archaea and Thermotoga maritima) lack the PEP-PTS system, but have several enzymes normally associated with the PEP-PTS operon. Alpha-glucosidases and alpha-galactosidases are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133433 [Multi-domain]  Cd Length: 423  Bit Score: 44.09  E-value: 5.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  14 VAVLGAGTLG------RRIALTFATRGGVVHLYDVSEESLQSAKEFLDqripelvKARSALGAqPATIEYYTDLPSAVKD 87
Cdd:cd05297    3 IAFIGAGSVVftknlvGDLLKTPELSGSTIALMDIDEERLETVEILAK-------KIVEELGA-PLKIEATTDRREALDG 74


                 ....*...
gi 491234295  88 AWYVVESV 95
Cdd:cd05297   75 ADFVINTI 82
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 12-119 8.12e-04

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: 40.11  E-value: 8.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  12 RPVAVLGAGTLGRRIALTFATRGGV--VHLYDVSEESLQSAKEfldqripelvkarsaLGaqpATIEYYTDLPSAVKDAW 89
Cdd:COG0287    2 MRIAIIGLGLIGGSLALALKRAGLAheVVGVDRSPETLERALE---------------LG---VIDRAATDLEEAVADAD 63

                         90       100       110
                 ....*....|....*....|....*....|
gi 491234295  90 YVVESVPeVQALkIDMLGQLDEIAAPDAII 119
Cdd:COG0287   64 LVVLAVP-VGAT-IEVLAELAPHLKPGAIV 91
PRK15076 PRK15076
alpha-galactosidase; Provisional
 14-92 6.96e-03

alpha-galactosidase; Provisional


Pssm-ID: 185035 [Multi-domain]  Cd Length: 431  Bit Score: 37.51  E-value: 6.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491234295  14 VAVLGAGTLG------RRIALTFATRGGVVHLYDVSEESLQSAKEFLDqripelvKARSALGAqPATIEYYTDLPSAVKD 87
Cdd:PRK15076   4 ITFIGAGSTVftknllGDILSVPALRDAEIALMDIDPERLEESEIVAR-------KLAESLGA-SAKITATTDRREALQG 75


                 ....*
gi 491234295  88 AWYVV 92
Cdd:PRK15076  76 ADYVI 80
 
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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