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Conserved domains on  [gi|1483511|emb|CAA65528|]
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3-hydroxyacyl-CoA dehydrogenase [Homo sapiens]

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 ...
 27-313 1.30e-136

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: 387.93  E-value: 1.30e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRK-VAKKKFAEnpkagdEFVEKTLSTIATSTD 105
Cdd:COG1250   2 IKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKlVKKGKLTE------EEADAALARITPTTD 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511  106 AASVVHStDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIK 185
Cdd:COG1250  76 LAALADA-DLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIR 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511  186 TPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYV 265
Cdd:COG1250 155 GPATSDETVATAVAFARRLGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPMGPFELADLV 234

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 1483511  266 GLDTTKFIVDGWHEmDAENPLHQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:COG1250 235 GLDTALAVLEVLYE-ALGDPRYRPPPLLKKLVEAGRLGRKTGRGFYDY 281
 
Name Accession Description Interval E-value
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 27-313 1.30e-136

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: 387.93  E-value: 1.30e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRK-VAKKKFAEnpkagdEFVEKTLSTIATSTD 105
Cdd:COG1250   2 IKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKlVKKGKLTE------EEADAALARITPTTD 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511  106 AASVVHStDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIK 185
Cdd:COG1250  76 LAALADA-DLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIR 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511  186 TPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYV 265
Cdd:COG1250 155 GPATSDETVATAVAFARRLGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPMGPFELADLV 234

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 1483511  266 GLDTTKFIVDGWHEmDAENPLHQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:COG1250 235 GLDTALAVLEVLYE-ALGDPRYRPPPLLKKLVEAGRLGRKTGRGFYDY 281
PLN02545 PLN02545
3-hydroxybutyryl-CoA dehydrogenase
 27-313 9.74e-111

3-hydroxybutyryl-CoA dehydrogenase


Pssm-ID: 215300 [Multi-domain]  Cd Length: 295  Bit Score: 323.22  E-value: 9.74e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511    27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKfaenpKAGDEFVEKTLSTIATSTDA 106
Cdd:PLN02545   4 IKKVGVVGAGQMGSGIAQLAAAAGMDVWLLDSDPAALSRGLDSISSSLARLVKKG-----KMSQEEADATLGRIRCTTNL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   107 ASVvHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKT 186
Cdd:PLN02545  79 EEL-RDADFIIEAIVESEDLKKKLFSELDRICKPSAILASNTSSISITRLASATQRPQQVIGMHFMNPPPIMKLVEIIRG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   187 PMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYVG 266
Cdd:PLN02545 158 ADTSDEVFDATKALAERFGKTVVCSQDYPGFIVNRILMPMINEAFYALYTGVASKEDIDTGMKLGTNHPMGPLHLADFIG 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 1483511   267 LDTTKFIVDGWHEMDAENPlHQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:PLN02545 238 LDTCLSIMKVLHEGLGDSK-YRPCPLLVQYVDAGRLGRKSGRGVYHY 283
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
 29-214 3.91e-77

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


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 233.20  E-value: 3.91e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511     29 HVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKfaenpKAGDEFVEKTLSTIATSTDAAS 108
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKG-----RITEEEVDAALARISFTTDLAA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511    109 VVHStDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKTPM 188
Cdd:pfam02737  76 AVDA-DLVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEK 154

                         170       180
                  ....*....|....*....|....*.
gi 1483511    189 TSQKTFESLVDFSKALGKHPVSCKDT 214
Cdd:pfam02737 155 TSPETVATTVELAKKIGKTPVVVKDT 180
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
 27-313 2.91e-51

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: 180.03  E-value: 2.91e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511     27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESL-RKVAKKKFAENPKagdefvEKTLSTIATSTD 105
Cdd:TIGR02441 335 VKTLAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLnKKVKRKKITSLER------DSILSNLTPTLD 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511    106 AaSVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIK 185
Cdd:TIGR02441 409 Y-SGFKNADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEIIT 487

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511    186 TPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERG-DASKEDidtAMKLGAGYPMGPFELLDY 264
Cdd:TIGR02441 488 HDGTSKDTLASAVAVGLKQGKVVIVVKDGPGFYTTRCLGPMLAEVIRLLQEGvDPKKLD---KLTTKFGFPVGAATLADE 564

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1483511    265 VGLDTTKFIVDGWHEMDAENPLHQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:TIGR02441 565 VGVDVAEHVAEDLGKAFGERFGGGSAELLSELVKAGFLGRKSGKGIFIY 613
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 28-120 1.86e-04

Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176230 [Multi-domain]  Cd Length: 312  Bit Score: 42.34  E-value: 1.86e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   28 KHVTVIGGGLMGAGIAQVAAATG-HTVVLVDqtedilakskkgIEESLRKVAKKKFAENPKAGDEfvEKTLSTIATSTDA 106
Cdd:cd08269 131 KTVAVIGAGFIGLLFLQLAAAAGaRRVIAID------------RRPARLALARELGATEVVTDDS--EAIVERVRELTGG 196

                        90
                ....*....|....
gi 1483511  107 ASVvhstDLVVEAI 120
Cdd:cd08269 197 AGA----DVVIEAV 206
 
Name Accession Description Interval E-value
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 27-313 1.30e-136

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: 387.93  E-value: 1.30e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRK-VAKKKFAEnpkagdEFVEKTLSTIATSTD 105
Cdd:COG1250   2 IKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKlVKKGKLTE------EEADAALARITPTTD 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511  106 AASVVHStDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIK 185
Cdd:COG1250  76 LAALADA-DLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIR 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511  186 TPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYV 265
Cdd:COG1250 155 GPATSDETVATAVAFARRLGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPMGPFELADLV 234

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 1483511  266 GLDTTKFIVDGWHEmDAENPLHQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:COG1250 235 GLDTALAVLEVLYE-ALGDPRYRPPPLLKKLVEAGRLGRKTGRGFYDY 281
PLN02545 PLN02545
3-hydroxybutyryl-CoA dehydrogenase
 27-313 9.74e-111

3-hydroxybutyryl-CoA dehydrogenase


Pssm-ID: 215300 [Multi-domain]  Cd Length: 295  Bit Score: 323.22  E-value: 9.74e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511    27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKfaenpKAGDEFVEKTLSTIATSTDA 106
Cdd:PLN02545   4 IKKVGVVGAGQMGSGIAQLAAAAGMDVWLLDSDPAALSRGLDSISSSLARLVKKG-----KMSQEEADATLGRIRCTTNL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   107 ASVvHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKT 186
Cdd:PLN02545  79 EEL-RDADFIIEAIVESEDLKKKLFSELDRICKPSAILASNTSSISITRLASATQRPQQVIGMHFMNPPPIMKLVEIIRG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   187 PMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYVG 266
Cdd:PLN02545 158 ADTSDEVFDATKALAERFGKTVVCSQDYPGFIVNRILMPMINEAFYALYTGVASKEDIDTGMKLGTNHPMGPLHLADFIG 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 1483511   267 LDTTKFIVDGWHEMDAENPlHQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:PLN02545 238 LDTCLSIMKVLHEGLGDSK-YRPCPLLVQYVDAGRLGRKSGRGVYHY 283
PRK05808 PRK05808
3-hydroxybutyryl-CoA dehydrogenase; Validated
 27-313 6.73e-103

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 180269 [Multi-domain]  Cd Length: 282  Bit Score: 302.65  E-value: 6.73e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511    27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESL-RKVAKKKFAENPKagdefvEKTLSTIATSTD 105
Cdd:PRK05808   3 IQKIGVIGAGTMGNGIAQVCAVAGYDVVMVDISDAAVDRGLATITKSLdRLVKKGKMTEADK------EAALARITGTTD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   106 AASVvHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIK 185
Cdd:PRK05808  77 LDDL-KDADLVIEAATENMDLKKKIFAQLDEIAKPEAILATNTSSLSITELAAATKRPDKVIGMHFFNPVPVMKLVEIIR 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   186 TPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYV 265
Cdd:PRK05808 156 GLATSDATHEAVEALAKKIGKTPVEVKNAPGFVVNRILIPMINEAIFVLAEGVATAEDIDEGMKLGCNHPIGPLALADLI 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 1483511   266 GLDTTKFIVDGWHEmDAENPLHQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:PRK05808 236 GLDTCLAIMEVLYE-GFGDSKYRPCPLLRKMVAAGWLGRKTGRGFYDY 282
PRK07819 PRK07819
3-hydroxybutyryl-CoA dehydrogenase; Validated
 30-313 4.41e-100

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181133 [Multi-domain]  Cd Length: 286  Bit Score: 295.74  E-value: 4.41e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511    30 VTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESL-RKVAKKKFAENPKagdefvEKTLSTIATSTDAAS 108
Cdd:PRK07819   8 VGVVGAGQMGAGIAEVCARAGVDVLVFETTEELATAGRNRIEKSLeRAVSRGKLTERER------DAALARLRFTTDLGD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   109 VVhSTDLVVEAIVENLKVKNELFKRLDKFAAE-HTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKTP 187
Cdd:PRK07819  82 FA-DRQLVIEAVVEDEAVKTEIFAELDKVVTDpDAVLASNTSSIPIMKLAAATKRPGRVLGLHFFNPVPVLPLVELVPTL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   188 MTSQKTFESLVDF-SKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYVG 266
Cdd:PRK07819 161 VTSEATVARAEEFaSDVLGKQVVRAQDRSGFVVNALLVPYLLSAIRMVESGFATAEDIDKAMVLGCAHPMGPLRLSDLVG 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 1483511   267 LDTTKFIVDGWHEMDAEnPLHQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:PRK07819 241 LDTVKAIADSMYEEFKE-PLYAPPPLLLRMVEAGLLGKKSGRGFYTY 286
PRK08268 PRK08268
3-hydroxy-acyl-CoA dehydrogenase; Validated
 27-313 6.05e-99

3-hydroxy-acyl-CoA dehydrogenase; Validated


Pssm-ID: 236211 [Multi-domain]  Cd Length: 507  Bit Score: 300.22  E-value: 6.05e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511    27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKfaenpKAGDEFVEKTLSTIATSTDA 106
Cdd:PRK08268   7 IATVAVIGAGAMGAGIAQVAAQAGHTVLLYDARAGAAAAARDGIAARLAKLVEKG-----KLTAEQADAALARLRPVEAL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   107 ASVVhSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKT 186
Cdd:PRK08268  82 ADLA-DCDLVVEAIVERLDVKQALFAQLEAIVSPDCILATNTSSLSITAIAAALKHPERVAGLHFFNPVPLMKLVEVVSG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   187 PMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYVG 266
Cdd:PRK08268 161 LATDPAVADALYALARAWGKTPVRAKDTPGFIVNRAARPYYTEALRVLEEGVADPATIDAILREAAGFRMGPFELMDLIG 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 1483511   267 LD----TTKFIVDGWHemdaENPLHQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:PRK08268 241 LDvnhaVMESVYRQFY----QEPRFRPSLIQQELVAAGRLGRKSGQGFYRY 287
PRK07530 PRK07530
3-hydroxybutyryl-CoA dehydrogenase; Validated
 27-314 1.50e-92

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181018 [Multi-domain]  Cd Length: 292  Bit Score: 276.89  E-value: 1.50e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511    27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESL-RKVAKKKFAENPKAgdefveKTLSTIATSTD 105
Cdd:PRK07530   4 IKKVGVIGAGQMGNGIAHVCALAGYDVLLNDVSADRLEAGLATINGNLaRQVAKGKISEEARA------AALARISTATD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   106 AASVVhSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIK 185
Cdd:PRK07530  78 LEDLA-DCDLVIEAATEDETVKRKIFAQLCPVLKPEAILATNTSSISITRLASATDRPERFIGIHFMNPVPVMKLVELIR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   186 TPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAI-RLYErGDASKEDIDTAMKLGAGYPMGPFELLDY 264
Cdd:PRK07530 157 GIATDEATFEAAKEFVTKLGKTITVAEDFPAFIVNRILLPMINEAIyTLYE-GVGSVEAIDTAMKLGANHPMGPLELADF 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 1483511   265 VGLDTTKFIVDGWHEMDAENPlHQPSPSLNKLVAENKFGKKTGEGFYKYK 314
Cdd:PRK07530 236 IGLDTCLSIMQVLHDGLADSK-YRPCPLLVKYVEAGWLGRKTGRGFYDYR 284
PRK08293 PRK08293
3-hydroxyacyl-CoA dehydrogenase;
27-314 1.86e-79

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 181359 [Multi-domain]  Cd Length: 287  Bit Score: 243.31  E-value: 1.86e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511    27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEeslrKVAKKKFAENPKAGDEFVEKTLSTIATSTDA 106
Cdd:PRK08293   3 IKNVTVAGAGVLGSQIAFQTAFHGFDVTIYDISDEALEKAKERIA----KLADRYVRDLEATKEAPAEAALNRITLTTDL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   107 ASVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKT 186
Cdd:PRK08293  79 AEAVKDADLVIEAVPEDPEIKGDFYEELAKVAPEKTIFATNSSTLLPSQFAEATGRPEKFLALHFANEIWKNNTAEIMGH 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   187 PMTSQKTFESLVDFSKALGKHPVSC-KDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYV 265
Cdd:PRK08293 159 PGTDPEVFDTVVAFAKAIGMVPIVLkKEQPGYILNSLLVPFLSAALALWAKGVADPETIDKTWMIATGAPMGPFGILDIV 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 1483511   266 GLDTTKFIVDGWHEMDAENPLHQPSPSLNKLVAENKFGKKTGEGFYKYK 314
Cdd:PRK08293 239 GLDTAYNITSNWAEATDDENAKKAAALLKEYIDKGKLGVATGEGFYNYP 287
PRK06035 PRK06035
3-hydroxyacyl-CoA dehydrogenase; Validated
 27-305 2.40e-79

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 180361 [Multi-domain]  Cd Length: 291  Bit Score: 243.24  E-value: 2.40e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511    27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEES---LRKVAKK-KFAENPkagdefVEKTLSTIAT 102
Cdd:PRK06035   3 IKVIGVVGSGVMGQGIAQVFARTGYDVTIVDVSEEILKNAMELIESGpygLRNLVEKgKMSEDE------AKAIMARIRT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   103 STDAASVvHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVE 182
Cdd:PRK06035  77 STSYESL-SDADFIVEAVPEKLDLKRKVFAELERNVSPETIIASNTSGIMIAEIATALERKDRFIGMHWFNPAPVMKLIE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   183 VIKTPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELL 262
Cdd:PRK06035 156 VVRAALTSEETFNTTVELSKKIGKIPIEVADVPGFFTTRFIEGWLLEAIRSFEIGIATIKDIDEMCKLAFGFPMGPFELM 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 1483511   263 DYVGLDTTKFIVDGWHEmDAENPLHQPSPSLNKLVAENKFGKK 305
Cdd:PRK06035 236 DIIGIDTVYHIAEYLYE-ETGDPQFIPPNSLKQMVLNGYVGDK 277
PRK09260 PRK09260
3-hydroxyacyl-CoA dehydrogenase;
27-313 1.37e-77

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 236434 [Multi-domain]  Cd Length: 288  Bit Score: 238.54  E-value: 1.37e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511    27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRK-VAKKKFAENPKAgdefveKTLSTIATSTD 105
Cdd:PRK09260   1 IEKLVVVGAGVMGRGIAYVFAVSGFQTTLVDIKQEQLESAQQEIASIFEQgVARGKLTEAARQ------AALARLSYSLD 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   106 AASVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIK 185
Cdd:PRK09260  75 LKAAVADADLVIEAVPEKLELKKAVFETADAHAPAECYIATNTSTMSPTEIASFTKRPERVIAMHFFNPVHKMKLVELIR 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   186 TPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYV 265
Cdd:PRK09260 155 GLETSDETVQVAKEVAEQMGKETVVVNEFPGFVTSRISALVGNEAFYMLQEGVATAEDIDKAIRLGLNFPMGPLELGDLV 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 1483511   266 GLDTTKFIVDGWHEMDAENplHQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:PRK09260 235 GLDTRLNNLKYLHETLGEK--YRPAPLLEKYVKAGRLGRKTGRGVYDY 280
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
 29-214 3.91e-77

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


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 233.20  E-value: 3.91e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511     29 HVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKfaenpKAGDEFVEKTLSTIATSTDAAS 108
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKG-----RITEEEVDAALARISFTTDLAA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511    109 VVHStDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKTPM 188
Cdd:pfam02737  76 AVDA-DLVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEK 154

                         170       180
                  ....*....|....*....|....*.
gi 1483511    189 TSQKTFESLVDFSKALGKHPVSCKDT 214
Cdd:pfam02737 155 TSPETVATTVELAKKIGKTPVVVKDT 180
PRK06130 PRK06130
3-hydroxybutyryl-CoA dehydrogenase; Validated
 27-313 2.22e-72

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 235707 [Multi-domain]  Cd Length: 311  Bit Score: 225.81  E-value: 2.22e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511    27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKkfaenpkagdEFVEKTLSTIATSTDA 106
Cdd:PRK06130   4 IQNLAIIGAGTMGSGIAALFARKGLQVVLIDVMEGALERARGVIERALGVYAPL----------GIASAGMGRIRMEAGL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   107 ASVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKT 186
Cdd:PRK06130  74 AAAVSGADLVIEAVPEKLELKRDVFARLDGLCDPDTIFATNTSGLPITAIAQAVTRPERFVGTHFFTPADVIPLVEVVRG 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   187 PMTSQKTFESLVDFSKALGKHPVSC-KDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPM---GPFELL 262
Cdd:PRK06130 154 DKTSPQTVATTMALLRSIGKRPVLVkKDIPGFIANRIQHALAREAISLLEKGVASAEDIDEVVKWSLGIRLaltGPLEQR 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 1483511   263 DYVGLDTTKFIVDGWHEmDAENPLhQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:PRK06130 234 DMNGLDVHLAVASYLYQ-DLENRT-TPSPLLEEKVEAGELGAKSGQGFYAW 282
fadJ PRK11154
fatty acid oxidation complex subunit alpha FadJ;
27-314 4.60e-65

fatty acid oxidation complex subunit alpha FadJ;


Pssm-ID: 236864 [Multi-domain]  Cd Length: 708  Bit Score: 217.07  E-value: 4.60e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511    27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVdqtEDIlakSKKGIEESLR-------KVAKKKFAenpKAGDEfvEKTLST 99
Cdd:PRK11154 309 VNKVGVLGGGLMGGGIAYVTATKAGLPVRI---KDI---NPQGINHALKyswdlldKKVKRRHL---KPSER--DKQMAL 377

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   100 IATSTDAaSVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMK 179
Cdd:PRK11154 378 ISGTTDY-RGFKHADVVIEAVFEDLALKQQMVAEVEQNCAPHTIFASNTSSLPIGQIAAAAARPEQVIGLHYFSPVEKMP 456

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   180 LVEVIKTPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGdASKEDIDTAMkLGAGYPMGPF 259
Cdd:PRK11154 457 LVEVIPHAKTSAETIATTVALAKKQGKTPIVVRDGAGFYVNRILAPYINEAARLLLEG-EPIEHIDAAL-VKFGFPVGPI 534

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 1483511   260 ELLDYVGLDT-TKFIvdgwHEMDAE-NPLHQPSPSLNKLVAENKFGKKTGEGFYKYK 314
Cdd:PRK11154 535 TLLDEVGIDVgTKII----PILEAAlGERFSAPAAFDKLLNDDRKGRKNGRGFYLYG 587
fadB PRK11730
fatty acid oxidation complex subunit alpha FadB;
27-314 8.36e-61

fatty acid oxidation complex subunit alpha FadB;


Pssm-ID: 183293 [Multi-domain]  Cd Length: 715  Bit Score: 205.87  E-value: 8.36e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511    27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKskkGIEES---LRKVAKKKFAENPKAGdefveKTLSTIATS 103
Cdd:PRK11730 313 VKQAAVLGAGIMGGGIAYQSASKGVPVIMKDINQKALDL---GMTEAaklLNKQVERGKIDGAKMA-----GVLSSIRPT 384

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   104 TDAASVVHsTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEV 183
Cdd:PRK11730 385 LDYAGFER-VDVVVEAVVENPKVKAAVLAEVEQKVREDTILASNTSTISISLLAKALKRPENFCGMHFFNPVHRMPLVEV 463

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   184 IKTPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGdASKEDIDTAMKLGAGYPMGPFELLD 263
Cdd:PRK11730 464 IRGEKTSDETIATVVAYASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDG-ADFRQIDKVMEKQFGWPMGPAYLLD 542

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 1483511   264 YVGLDT----TKFIVDGWHE-MDAENPlhqpsPSLNKLVAENKFGKKTGEGFYKYK 314
Cdd:PRK11730 543 VVGIDTahhaQAVMAEGFPDrMKKDYR-----DAIDVLFEAKRFGQKNGKGFYRYE 593
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
 27-313 2.91e-51

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: 180.03  E-value: 2.91e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511     27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESL-RKVAKKKFAENPKagdefvEKTLSTIATSTD 105
Cdd:TIGR02441 335 VKTLAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLnKKVKRKKITSLER------DSILSNLTPTLD 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511    106 AaSVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIK 185
Cdd:TIGR02441 409 Y-SGFKNADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEIIT 487

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511    186 TPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERG-DASKEDidtAMKLGAGYPMGPFELLDY 264
Cdd:TIGR02441 488 HDGTSKDTLASAVAVGLKQGKVVIVVKDGPGFYTTRCLGPMLAEVIRLLQEGvDPKKLD---KLTTKFGFPVGAATLADE 564

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1483511    265 VGLDTTKFIVDGWHEMDAENPLHQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:TIGR02441 565 VGVDVAEHVAEDLGKAFGERFGGGSAELLSELVKAGFLGRKSGKGIFIY 613
3HCDH pfam00725
3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda ...
 216-313 2.15e-44

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: 146.59  E-value: 2.15e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511    216 GFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYVGLDTTKFIVDGWHEmDAENPLHQPSPSLNK 295
Cdd:pfam00725   1 GFVVNRLLAPYLNEAIRLVEEGVATPEDIDAAMRLGLGLPMGPFELSDLVGLDVGYHILEVLAE-EFGDRAYRPPPLLEK 79

                          90
                  ....*....|....*...
gi 1483511    296 LVAENKFGKKTGEGFYKY 313
Cdd:pfam00725  80 LVEAGRLGRKTGKGFYKY 97
PRK08269 PRK08269
3-hydroxybutyryl-CoA dehydrogenase; Validated
 38-313 1.09e-42

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181340 [Multi-domain]  Cd Length: 314  Bit Score: 149.44  E-value: 1.09e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511    38 MGAGIAQVAAATGHTVVLVD-------QTEDILAKSKKGIEESLRKVAKKKFAENPKAgDEFVEKTlsTIATSTDAASVV 110
Cdd:PRK08269   1 MGQGIALAFAFAGHDVTLIDfkprdaaGWRALDAEARAEIERTLAALVALGRIDAAQA-DAVLARI--AVVARDGAADAL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   111 HSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKTPMTS 190
Cdd:PRK08269  78 ADADLVFEAVPEVLDAKREALRWLGRHVDADAIIASTTSTFLVTDLQRHVAHPERFLNAHWLNPAYLMPLVEVSPSDATD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   191 QKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYP---MGPFELLDYVGL 267
Cdd:PRK08269 158 PAVVDRLAALLERIGKVPVVCGPSPGYIVPRIQALAMNEAARMVEEGVASAEDIDKAIRTGFGLRfavLGLLEFIDWGGC 237

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 1483511   268 DT----TKFIVDgwhEMDAENplHQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:PRK08269 238 DIlyyaSRYLAG---EIGPDR--FAPPAIVVRNMEEGRDGLRTGAGFYDY 282
PRK06129 PRK06129
3-hydroxyacyl-CoA dehydrogenase; Validated
 29-263 3.02e-41

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 235706 [Multi-domain]  Cd Length: 308  Bit Score: 145.19  E-value: 3.02e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511    29 HVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLrkvakKKFAENPKAGDEFVEKTLSTIATSTDAAS 108
Cdd:PRK06129   4 SVAIIGAGLIGRAWAIVFARAGHEVRLWDADPAAAAAAPAYIAGRL-----EDLAAFDLLDGEAPDAVLARIRVTDSLAD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   109 VVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKTPM 188
Cdd:PRK06129  79 AVADADYVQESAPENLELKRALFAELDALAPPHAILASSTSALLASAFTEHLAGRERCLVAHPINPPYLIPVVEVVPAPW 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1483511   189 TSQKTFESLVDFSKALGKHPVSC-KDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYP---MGPFELLD 263
Cdd:PRK06129 159 TAPATLARAEALYRAAGQSPVRLrREIDGFVLNRLQGALLREAFRLVADGVASVDDIDAVIRDGLGLRwsfMGPFETID 237
PRK07066 PRK07066
L-carnitine dehydrogenase;
27-259 9.97e-22

L-carnitine dehydrogenase;


Pssm-ID: 168796 [Multi-domain]  Cd Length: 321  Bit Score: 93.36  E-value: 9.97e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511    27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKFAenPKAGDEfvekTLSTIATstdA 106
Cdd:PRK07066   7 IKTFAAIGSGVIGSGWVARALAHGLDVVAWDPAPGAEAALRANVANAWPALERQGLA--PGASPA----RLRFVAT---I 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   107 ASVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKT 186
Cdd:PRK07066  78 EACVADADFIQESAPEREALKLELHERISRAAKPDAIIASSTSGLLPTDFYARATHPERCVVGHPFNPVYLLPLVEVLGG 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1483511   187 PMTSQKTFESLVDFSKALGKHPVSC-KDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYP---MGPF 259
Cdd:PRK07066 158 ERTAPEAVDAAMGIYRALGMRPLHVrKEVPGFIADRLLEALWREALHLVNEGVATTGEIDDAIRFGAGIRwsfMGTF 234
PRK07531 PRK07531
carnitine 3-dehydrogenase;
33-260 2.58e-15

carnitine 3-dehydrogenase;


Pssm-ID: 236044 [Multi-domain]  Cd Length: 495  Bit Score: 75.93  E-value: 2.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511    33 IGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKFAENPKAGdefvekTLSTIATSTDAasvVHS 112
Cdd:PRK07531  10 IGGGVIGGGWAARFLLAGIDVAVFDPHPEAERIIGEVLANAERAYAMLTDAPLPPEG------RLTFCASLAEA---VAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   113 TDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKTPMTSQK 192
Cdd:PRK07531  81 ADWIQESVPERLDLKRRVLAEIDAAARPDALIGSSTSGFLPSDLQEGMTHPERLFVAHPYNPVYLLPLVELVGGGKTSPE 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1483511   193 TFESLVDFSKALGKHPVSC-KDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGY---PMGPFE 260
Cdd:PRK07531 161 TIRRAKEILREIGMKPVHIaKEIDAFVGDRLLEALWREALWLVKDGIATTEEIDDVIRYSFGLrwaQMGLFE 232
PRK08268 PRK08268
3-hydroxy-acyl-CoA dehydrogenase; Validated
 188-298 1.50e-10

3-hydroxy-acyl-CoA dehydrogenase; Validated


Pssm-ID: 236211 [Multi-domain]  Cd Length: 507  Bit Score: 61.79  E-value: 1.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   188 MTSQKTFESLVD----FSKALGKhPVS-CKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELL 262
Cdd:PRK08268 384 MAAPATSPAARDaahaLFQQDGK-AVSvIRDSPGFVAQRTVAMIVNEAADIAQQGIASPADIDLAMRLGLNYPLGPLAWG 462

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 1483511   263 DYVGLDTTKFIVDGWHEMDAEnPLHQPSPSLNKLVA 298
Cdd:PRK08268 463 DRLGAARILRVLENLQALYGD-PRYRPSPWLRRRAA 497
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 29-62 7.26e-05

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 43.93  E-value: 7.26e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1483511     29 HVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDI 62
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDP 34
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 28-120 1.86e-04

Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176230 [Multi-domain]  Cd Length: 312  Bit Score: 42.34  E-value: 1.86e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   28 KHVTVIGGGLMGAGIAQVAAATG-HTVVLVDqtedilakskkgIEESLRKVAKKKFAENPKAGDEfvEKTLSTIATSTDA 106
Cdd:cd08269 131 KTVAVIGAGFIGLLFLQLAAAAGaRRVIAID------------RRPARLALARELGATEVVTDDS--EAIVERVRELTGG 196

                        90
                ....*....|....
gi 1483511  107 ASVvhstDLVVEAI 120
Cdd:cd08269 197 AGA----DVVIEAV 206
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 23-65 1.07e-03

Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 40.05  E-value: 1.07e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 1483511   23 KKIIVKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAK 65
Cdd:COG0569  91 IKKLKMHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVER 133
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
29-58 1.10e-03

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 40.27  E-value: 1.10e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 1483511   29 HVTVIGGGLMGAGIAQVAAATGHTVVLVDQ 58
Cdd:COG0665   4 DVVVIGGGIAGLSTAYHLARRGLDVTVLER 33
PRK13369 PRK13369
glycerol-3-phosphate dehydrogenase; Provisional
 32-58 1.44e-03

glycerol-3-phosphate dehydrogenase; Provisional


Pssm-ID: 237365 [Multi-domain]  Cd Length: 502  Bit Score: 39.95  E-value: 1.44e-03
                         10        20
                 ....*....|....*....|....*..
gi 1483511    32 VIGGGLMGAGIAQVAAATGHTVVLVDQ 58
Cdd:PRK13369  11 VIGGGINGAGIARDAAGRGLKVLLCEK 37
GpsA COG0240
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
 28-120 8.15e-03

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: 37.32  E-value: 8.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511   28 KHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKskkgIEESlRkvakkkfaENPK--AGDEFVEktlsTIATSTD 105
Cdd:COG0240   1 MKIAVLGAGSWGTALAKVLARNGHEVTLWGRDPEVAEE----INET-R--------ENPRylPGVKLPE----NLRATSD 63

                        90
                ....*....|....*
gi 1483511  106 AASVVHSTDLVVEAI 120
Cdd:COG0240  64 LEEALAGADLVLLAV 78
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
30-55 9.54e-03

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


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 36.69  E-value: 9.54e-03
                        10        20
                ....*....|....*....|....*.
gi 1483511   30 VTVIGGGLMGAGIAQVAAATGHTVVL 55
Cdd:COG2085   1 IGIIGTGNIGSALARRLAAAGHEVVI 26
 
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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