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Conserved domains on  [gi|1780199935|ref|NP_005318|]
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hydroxyacyl-coenzyme A dehydrogenase, mitochondrial isoform 2 precursor [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 4.36e-137

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: 389.47  E-value: 4.36e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRK-VAKKKFAEnlkagdEFVEKTLSTIATSTD 105
Cdd:COG1250     2 IKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKlVKKGKLTE------EEADAALARITPTTD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 106 AASVVHStDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIK 185
Cdd:COG1250    76 LAALADA-DLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIR 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 186 TPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYV 265
Cdd:COG1250   155 GPATSDETVATAVAFARRLGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPMGPFELADLV 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1780199935 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 4.36e-137

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: 389.47  E-value: 4.36e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRK-VAKKKFAEnlkagdEFVEKTLSTIATSTD 105
Cdd:COG1250     2 IKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKlVKKGKLTE------EEADAALARITPTTD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 106 AASVVHStDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIK 185
Cdd:COG1250    76 LAALADA-DLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIR 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 186 TPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYV 265
Cdd:COG1250   155 GPATSDETVATAVAFARRLGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPMGPFELADLV 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1780199935 266 GLDTTKFIVDGWHEmDAENPLHQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:COG1250   235 GLDTALAVLEVLYE-ALGDPRYRPPPLLKKLVEAGRLGRKTGRGFYDY 281
PLN02545 PLN02545
3-hydroxybutyryl-CoA dehydrogenase
 27-313 1.20e-110

3-hydroxybutyryl-CoA dehydrogenase


Pssm-ID: 215300 [Multi-domain]  Cd Length: 295  Bit Score: 322.84  E-value: 1.20e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKfaenlKAGDEFVEKTLSTIATSTDA 106
Cdd:PLN02545    4 IKKVGVVGAGQMGSGIAQLAAAAGMDVWLLDSDPAALSRGLDSISSSLARLVKKG-----KMSQEEADATLGRIRCTTNL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 107 ASVvHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKT 186
Cdd:PLN02545   79 EEL-RDADFIIEAIVESEDLKKKLFSELDRICKPSAILASNTSSISITRLASATQRPQQVIGMHFMNPPPIMKLVEIIRG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 187 PMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYVG 266
Cdd:PLN02545  158 ADTSDEVFDATKALAERFGKTVVCSQDYPGFIVNRILMPMINEAFYALYTGVASKEDIDTGMKLGTNHPMGPLHLADFIG 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1780199935 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 3.15e-77

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


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 233.58  E-value: 3.15e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935  29 HVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKfaenlKAGDEFVEKTLSTIATSTDAAS 108
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKG-----RITEEEVDAALARISFTTDLAA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 109 VVHStDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKTPM 188
Cdd:pfam02737  76 AVDA-DLVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEK 154

                         170       180
                  ....*....|....*....|....*.
gi 1780199935 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 3.40e-52

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: 182.73  E-value: 3.40e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKFAENLKAgdefvEKTLSTIATSTDA 106
Cdd:TIGR02441 335 VKTLAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLNKKVKRKKITSLER-----DSILSNLTPTLDY 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 107 aSVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKT 186
Cdd:TIGR02441 410 -SGFKNADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEIITH 488

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 187 PMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERG-DASKEDidtAMKLGAGYPMGPFELLDYV 265
Cdd:TIGR02441 489 DGTSKDTLASAVAVGLKQGKVVIVVKDGPGFYTTRCLGPMLAEVIRLLQEGvDPKKLD---KLTTKFGFPVGAATLADEV 565

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1780199935 266 GLDTTKFIVDGWHEMDAENPLHQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:TIGR02441 566 GVDVAEHVAEDLGKAFGERFGGGSAELLSELVKAGFLGRKSGKGIFIY 613
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 28-120 3.33e-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: 41.57  E-value: 3.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935  28 KHVTVIGGGLMGAGIAQVAAATG-HTVVLVDqtedilakskkgIEESLRKVAKKKFAENLKAGDEfvEKTLSTIATSTDA 106
Cdd:cd08269   131 KTVAVIGAGFIGLLFLQLAAAAGaRRVIAID------------RRPARLALARELGATEVVTDDS--EAIVERVRELTGG 196

                          90
                  ....*....|....
gi 1780199935 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 4.36e-137

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: 389.47  E-value: 4.36e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRK-VAKKKFAEnlkagdEFVEKTLSTIATSTD 105
Cdd:COG1250     2 IKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKlVKKGKLTE------EEADAALARITPTTD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 106 AASVVHStDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIK 185
Cdd:COG1250    76 LAALADA-DLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIR 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 186 TPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYV 265
Cdd:COG1250   155 GPATSDETVATAVAFARRLGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPMGPFELADLV 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1780199935 266 GLDTTKFIVDGWHEmDAENPLHQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:COG1250   235 GLDTALAVLEVLYE-ALGDPRYRPPPLLKKLVEAGRLGRKTGRGFYDY 281
PLN02545 PLN02545
3-hydroxybutyryl-CoA dehydrogenase
 27-313 1.20e-110

3-hydroxybutyryl-CoA dehydrogenase


Pssm-ID: 215300 [Multi-domain]  Cd Length: 295  Bit Score: 322.84  E-value: 1.20e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKfaenlKAGDEFVEKTLSTIATSTDA 106
Cdd:PLN02545    4 IKKVGVVGAGQMGSGIAQLAAAAGMDVWLLDSDPAALSRGLDSISSSLARLVKKG-----KMSQEEADATLGRIRCTTNL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 107 ASVvHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKT 186
Cdd:PLN02545   79 EEL-RDADFIIEAIVESEDLKKKLFSELDRICKPSAILASNTSSISITRLASATQRPQQVIGMHFMNPPPIMKLVEIIRG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 187 PMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYVG 266
Cdd:PLN02545  158 ADTSDEVFDATKALAERFGKTVVCSQDYPGFIVNRILMPMINEAFYALYTGVASKEDIDTGMKLGTNHPMGPLHLADFIG 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1780199935 267 LDTTKFIVDGWHEMDAENPlHQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:PLN02545  238 LDTCLSIMKVLHEGLGDSK-YRPCPLLVQYVDAGRLGRKSGRGVYHY 283
PRK05808 PRK05808
3-hydroxybutyryl-CoA dehydrogenase; Validated
 27-313 1.25e-102

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 180269 [Multi-domain]  Cd Length: 282  Bit Score: 301.88  E-value: 1.25e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESL-RKVAKKKFAENLKagdefvEKTLSTIATSTD 105
Cdd:PRK05808    3 IQKIGVIGAGTMGNGIAQVCAVAGYDVVMVDISDAAVDRGLATITKSLdRLVKKGKMTEADK------EAALARITGTTD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 106 AASVvHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIK 185
Cdd:PRK05808   77 LDDL-KDADLVIEAATENMDLKKKIFAQLDEIAKPEAILATNTSSLSITELAAATKRPDKVIGMHFFNPVPVMKLVEIIR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 186 TPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYV 265
Cdd:PRK05808  156 GLATSDATHEAVEALAKKIGKTPVEVKNAPGFVVNRILIPMINEAIFVLAEGVATAEDIDEGMKLGCNHPIGPLALADLI 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1780199935 266 GLDTTKFIVDGWHEmDAENPLHQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:PRK05808  236 GLDTCLAIMEVLYE-GFGDSKYRPCPLLRKMVAAGWLGRKTGRGFYDY 282
PRK07819 PRK07819
3-hydroxybutyryl-CoA dehydrogenase; Validated
 30-313 6.46e-100

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181133 [Multi-domain]  Cd Length: 286  Bit Score: 295.36  E-value: 6.46e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935  30 VTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESL-RKVAKKKFAENLKagdefvEKTLSTIATSTDAAS 108
Cdd:PRK07819    8 VGVVGAGQMGAGIAEVCARAGVDVLVFETTEELATAGRNRIEKSLeRAVSRGKLTERER------DAALARLRFTTDLGD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 109 VVhSTDLVVEAIVENLKVKNELFKRLDKFAAE-HTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKTP 187
Cdd:PRK07819   82 FA-DRQLVIEAVVEDEAVKTEIFAELDKVVTDpDAVLASNTSSIPIMKLAAATKRPGRVLGLHFFNPVPVLPLVELVPTL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 188 MTSQKTFESLVDF-SKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYVG 266
Cdd:PRK07819  161 VTSEATVARAEEFaSDVLGKQVVRAQDRSGFVVNALLVPYLLSAIRMVESGFATAEDIDKAMVLGCAHPMGPLRLSDLVG 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1780199935 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 1780199935  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKfaenlKAGDEFVEKTLSTIATSTDA 106
Cdd:PRK08268    7 IATVAVIGAGAMGAGIAQVAAQAGHTVLLYDARAGAAAAARDGIAARLAKLVEKG-----KLTAEQADAALARLRPVEAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 107 ASVVhSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKT 186
Cdd:PRK08268   82 ADLA-DCDLVVEAIVERLDVKQALFAQLEAIVSPDCILATNTSSLSITAIAAALKHPERVAGLHFFNPVPLMKLVEVVSG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 187 PMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYVG 266
Cdd:PRK08268  161 LATDPAVADALYALARAWGKTPVRAKDTPGFIVNRAARPYYTEALRVLEEGVADPATIDAILREAAGFRMGPFELMDLIG 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1780199935 267 LD----TTKFIVDGWHemdaENPLHQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:PRK08268  241 LDvnhaVMESVYRQFY----QEPRFRPSLIQQELVAAGRLGRKSGQGFYRY 287
PRK07530 PRK07530
3-hydroxybutyryl-CoA dehydrogenase; Validated
 27-314 9.58e-93

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181018 [Multi-domain]  Cd Length: 292  Bit Score: 277.27  E-value: 9.58e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESL-RKVAKKKFAENLKAgdefveKTLSTIATSTD 105
Cdd:PRK07530    4 IKKVGVIGAGQMGNGIAHVCALAGYDVLLNDVSADRLEAGLATINGNLaRQVAKGKISEEARA------AALARISTATD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 106 AASVVhSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIK 185
Cdd:PRK07530   78 LEDLA-DCDLVIEAATEDETVKRKIFAQLCPVLKPEAILATNTSSISITRLASATDRPERFIGIHFMNPVPVMKLVELIR 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 186 TPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAI-RLYErGDASKEDIDTAMKLGAGYPMGPFELLDY 264
Cdd:PRK07530  157 GIATDEATFEAAKEFVTKLGKTITVAEDFPAFIVNRILLPMINEAIyTLYE-GVGSVEAIDTAMKLGANHPMGPLELADF 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1780199935 265 VGLDTTKFIVDGWHEMDAENPlHQPSPSLNKLVAENKFGKKTGEGFYKYK 314
Cdd:PRK07530  236 IGLDTCLSIMQVLHDGLADSK-YRPCPLLVKYVEAGWLGRKTGRGFYDYR 284
PRK06035 PRK06035
3-hydroxyacyl-CoA dehydrogenase; Validated
 27-305 4.36e-79

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 180361 [Multi-domain]  Cd Length: 291  Bit Score: 242.47  E-value: 4.36e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEES---LRKVAKK-KFAENLkagdefVEKTLSTIAT 102
Cdd:PRK06035    3 IKVIGVVGSGVMGQGIAQVFARTGYDVTIVDVSEEILKNAMELIESGpygLRNLVEKgKMSEDE------AKAIMARIRT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 103 STDAASVvHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVE 182
Cdd:PRK06035   77 STSYESL-SDADFIVEAVPEKLDLKRKVFAELERNVSPETIIASNTSGIMIAEIATALERKDRFIGMHWFNPAPVMKLIE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 183 VIKTPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELL 262
Cdd:PRK06035  156 VVRAALTSEETFNTTVELSKKIGKIPIEVADVPGFFTTRFIEGWLLEAIRSFEIGIATIKDIDEMCKLAFGFPMGPFELM 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1780199935 263 DYVGLDTTKFIVDGWHEmDAENPLHQPSPSLNKLVAENKFGKK 305
Cdd:PRK06035  236 DIIGIDTVYHIAEYLYE-ETGDPQFIPPNSLKQMVLNGYVGDK 277
PRK08293 PRK08293
3-hydroxyacyl-CoA dehydrogenase;
27-314 8.52e-79

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 181359 [Multi-domain]  Cd Length: 287  Bit Score: 241.38  E-value: 8.52e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEeslrKVAKKKFAENLKAGDEFVEKTLSTIATSTDA 106
Cdd:PRK08293    3 IKNVTVAGAGVLGSQIAFQTAFHGFDVTIYDISDEALEKAKERIA----KLADRYVRDLEATKEAPAEAALNRITLTTDL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 107 ASVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKT 186
Cdd:PRK08293   79 AEAVKDADLVIEAVPEDPEIKGDFYEELAKVAPEKTIFATNSSTLLPSQFAEATGRPEKFLALHFANEIWKNNTAEIMGH 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 187 PMTSQKTFESLVDFSKALGKHPVSC-KDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYV 265
Cdd:PRK08293  159 PGTDPEVFDTVVAFAKAIGMVPIVLkKEQPGYILNSLLVPFLSAALALWAKGVADPETIDKTWMIATGAPMGPFGILDIV 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1780199935 266 GLDTTKFIVDGWHEMDAENPLHQPSPSLNKLVAENKFGKKTGEGFYKYK 314
Cdd:PRK08293  239 GLDTAYNITSNWAEATDDENAKKAAALLKEYIDKGKLGVATGEGFYNYP 287
PRK09260 PRK09260
3-hydroxyacyl-CoA dehydrogenase;
27-313 2.02e-77

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 236434 [Multi-domain]  Cd Length: 288  Bit Score: 238.15  E-value: 2.02e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRK-VAKKKFAEnlkagdEFVEKTLSTIATSTD 105
Cdd:PRK09260    1 IEKLVVVGAGVMGRGIAYVFAVSGFQTTLVDIKQEQLESAQQEIASIFEQgVARGKLTE------AARQAALARLSYSLD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 106 AASVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIK 185
Cdd:PRK09260   75 LKAAVADADLVIEAVPEKLELKKAVFETADAHAPAECYIATNTSTMSPTEIASFTKRPERVIAMHFFNPVHKMKLVELIR 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 186 TPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYV 265
Cdd:PRK09260  155 GLETSDETVQVAKEVAEQMGKETVVVNEFPGFVTSRISALVGNEAFYMLQEGVATAEDIDKAIRLGLNFPMGPLELGDLV 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1780199935 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 3.15e-77

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


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 233.58  E-value: 3.15e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935  29 HVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKfaenlKAGDEFVEKTLSTIATSTDAAS 108
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKG-----RITEEEVDAALARISFTTDLAA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 109 VVHStDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKTPM 188
Cdd:pfam02737  76 AVDA-DLVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEK 154

                         170       180
                  ....*....|....*....|....*.
gi 1780199935 189 TSQKTFESLVDFSKALGKHPVSCKDT 214
Cdd:pfam02737 155 TSPETVATTVELAKKIGKTPVVVKDT 180
PRK06130 PRK06130
3-hydroxybutyryl-CoA dehydrogenase; Validated
 27-313 1.17e-72

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 235707 [Multi-domain]  Cd Length: 311  Bit Score: 226.58  E-value: 1.17e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEEslrkvakkkfAENLKAGDEFVEKTLSTIATSTDA 106
Cdd:PRK06130    4 IQNLAIIGAGTMGSGIAALFARKGLQVVLIDVMEGALERARGVIER----------ALGVYAPLGIASAGMGRIRMEAGL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 107 ASVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKT 186
Cdd:PRK06130   74 AAAVSGADLVIEAVPEKLELKRDVFARLDGLCDPDTIFATNTSGLPITAIAQAVTRPERFVGTHFFTPADVIPLVEVVRG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 187 PMTSQKTFESLVDFSKALGKHPVSC-KDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPM---GPFELL 262
Cdd:PRK06130  154 DKTSPQTVATTMALLRSIGKRPVLVkKDIPGFIANRIQHALAREAISLLEKGVASAEDIDEVVKWSLGIRLaltGPLEQR 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1780199935 263 DYVGLDTTKFIVDGWHEmDAENPLhQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:PRK06130  234 DMNGLDVHLAVASYLYQ-DLENRT-TPSPLLEEKVEAGELGAKSGQGFYAW 282
fadJ PRK11154
fatty acid oxidation complex subunit alpha FadJ;
27-314 5.04e-66

fatty acid oxidation complex subunit alpha FadJ;


Pssm-ID: 236864 [Multi-domain]  Cd Length: 708  Bit Score: 219.77  E-value: 5.04e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVdqtEDIlakSKKGIEESLR-------KVAKKKFaenLKAGDEfvEKTLST 99
Cdd:PRK11154  309 VNKVGVLGGGLMGGGIAYVTATKAGLPVRI---KDI---NPQGINHALKyswdlldKKVKRRH---LKPSER--DKQMAL 377

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 100 IATSTDAaSVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMK 179
Cdd:PRK11154  378 ISGTTDY-RGFKHADVVIEAVFEDLALKQQMVAEVEQNCAPHTIFASNTSSLPIGQIAAAAARPEQVIGLHYFSPVEKMP 456

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 180 LVEVIKTPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGdASKEDIDTAMkLGAGYPMGPF 259
Cdd:PRK11154  457 LVEVIPHAKTSAETIATTVALAKKQGKTPIVVRDGAGFYVNRILAPYINEAARLLLEG-EPIEHIDAAL-VKFGFPVGPI 534

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1780199935 260 ELLDYVGLDT-TKFIvdgwHEMDAE-NPLHQPSPSLNKLVAENKFGKKTGEGFYKYK 314
Cdd:PRK11154  535 TLLDEVGIDVgTKII----PILEAAlGERFSAPAAFDKLLNDDRKGRKNGRGFYLYG 587
fadB PRK11730
fatty acid oxidation complex subunit alpha FadB;
27-314 7.42e-62

fatty acid oxidation complex subunit alpha FadB;


Pssm-ID: 183293 [Multi-domain]  Cd Length: 715  Bit Score: 208.56  E-value: 7.42e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKskkGIEES---LRKVAKKKFAENLKAGdefveKTLSTIATS 103
Cdd:PRK11730  313 VKQAAVLGAGIMGGGIAYQSASKGVPVIMKDINQKALDL---GMTEAaklLNKQVERGKIDGAKMA-----GVLSSIRPT 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 104 TDAASVVHsTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEV 183
Cdd:PRK11730  385 LDYAGFER-VDVVVEAVVENPKVKAAVLAEVEQKVREDTILASNTSTISISLLAKALKRPENFCGMHFFNPVHRMPLVEV 463

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 184 IKTPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGdASKEDIDTAMKLGAGYPMGPFELLD 263
Cdd:PRK11730  464 IRGEKTSDETIATVVAYASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDG-ADFRQIDKVMEKQFGWPMGPAYLLD 542

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1780199935 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 3.40e-52

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: 182.73  E-value: 3.40e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKFAENLKAgdefvEKTLSTIATSTDA 106
Cdd:TIGR02441 335 VKTLAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLNKKVKRKKITSLER-----DSILSNLTPTLDY 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 107 aSVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKT 186
Cdd:TIGR02441 410 -SGFKNADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEIITH 488

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 187 PMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERG-DASKEDidtAMKLGAGYPMGPFELLDYV 265
Cdd:TIGR02441 489 DGTSKDTLASAVAVGLKQGKVVIVVKDGPGFYTTRCLGPMLAEVIRLLQEGvDPKKLD---KLTTKFGFPVGAATLADEV 565

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1780199935 266 GLDTTKFIVDGWHEMDAENPLHQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:TIGR02441 566 GVDVAEHVAEDLGKAFGERFGGGSAELLSELVKAGFLGRKSGKGIFIY 613
3HCDH pfam00725
3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda ...
 216-313 2.22e-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: 2.22e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 216 GFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYVGLDTTKFIVDGWHEmDAENPLHQPSPSLNK 295
Cdd:pfam00725   1 GFVVNRLLAPYLNEAIRLVEEGVATPEDIDAAMRLGLGLPMGPFELSDLVGLDVGYHILEVLAE-EFGDRAYRPPPLLEK 79

                          90
                  ....*....|....*...
gi 1780199935 296 LVAENKFGKKTGEGFYKY 313
Cdd:pfam00725  80 LVEAGRLGRKTGKGFYKY 97
PRK08269 PRK08269
3-hydroxybutyryl-CoA dehydrogenase; Validated
 38-313 9.17e-43

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181340 [Multi-domain]  Cd Length: 314  Bit Score: 149.44  E-value: 9.17e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935  38 MGAGIAQVAAATGHTVVLVD-------QTEDILAKSKKGIEESLRKVAKKKFAENLKAgDEFVEKTlsTIATSTDAASVV 110
Cdd:PRK08269    1 MGQGIALAFAFAGHDVTLIDfkprdaaGWRALDAEARAEIERTLAALVALGRIDAAQA-DAVLARI--AVVARDGAADAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 111 HSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKTPMTS 190
Cdd:PRK08269   78 ADADLVFEAVPEVLDAKREALRWLGRHVDADAIIASTTSTFLVTDLQRHVAHPERFLNAHWLNPAYLMPLVEVSPSDATD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 191 QKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYP---MGPFELLDYVGL 267
Cdd:PRK08269  158 PAVVDRLAALLERIGKVPVVCGPSPGYIVPRIQALAMNEAARMVEEGVASAEDIDKAIRTGFGLRfavLGLLEFIDWGGC 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1780199935 268 DT----TKFIVDgwhEMDAENplHQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:PRK08269  238 DIlyyaSRYLAG---EIGPDR--FAPPAIVVRNMEEGRDGLRTGAGFYDY 282
PRK06129 PRK06129
3-hydroxyacyl-CoA dehydrogenase; Validated
 29-263 3.74e-41

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 235706 [Multi-domain]  Cd Length: 308  Bit Score: 145.19  E-value: 3.74e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935  29 HVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLrkvakKKFAENLKAGDEFVEKTLSTIATSTDAAS 108
Cdd:PRK06129    4 SVAIIGAGLIGRAWAIVFARAGHEVRLWDADPAAAAAAPAYIAGRL-----EDLAAFDLLDGEAPDAVLARIRVTDSLAD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 109 VVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKTPM 188
Cdd:PRK06129   79 AVADADYVQESAPENLELKRALFAELDALAPPHAILASSTSALLASAFTEHLAGRERCLVAHPINPPYLIPVVEVVPAPW 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1780199935 189 TSQKTFESLVDFSKALGKHPVSC-KDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYP---MGPFELLD 263
Cdd:PRK06129  159 TAPATLARAEALYRAAGQSPVRLrREIDGFVLNRLQGALLREAFRLVADGVASVDDIDAVIRDGLGLRwsfMGPFETID 237
PRK07066 PRK07066
L-carnitine dehydrogenase;
27-259 1.50e-21

L-carnitine dehydrogenase;


Pssm-ID: 168796 [Multi-domain]  Cd Length: 321  Bit Score: 92.98  E-value: 1.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEdilakskkGIEESLRK-VAKKKFA---ENLKAGDEfvEKTLSTIAT 102
Cdd:PRK07066    7 IKTFAAIGSGVIGSGWVARALAHGLDVVAWDPAP--------GAEAALRAnVANAWPAlerQGLAPGAS--PARLRFVAT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 103 stdAASVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVE 182
Cdd:PRK07066   77 ---IEACVADADFIQESAPEREALKLELHERISRAAKPDAIIASSTSGLLPTDFYARATHPERCVVGHPFNPVYLLPLVE 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 183 VIKTPMTSQKTFESLVDFSKALGKHPVSC-KDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYP---MGP 258
Cdd:PRK07066  154 VLGGERTAPEAVDAAMGIYRALGMRPLHVrKEVPGFIADRLLEALWREALHLVNEGVATTGEIDDAIRFGAGIRwsfMGT 233


                  .
gi 1780199935 259 F 259
Cdd:PRK07066  234 F 234
PRK07531 PRK07531
carnitine 3-dehydrogenase;
33-260 5.31e-15

carnitine 3-dehydrogenase;


Pssm-ID: 236044 [Multi-domain]  Cd Length: 495  Bit Score: 75.16  E-value: 5.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935  33 IGGGLMGAGIAQVAAATGHTVVLVD-------QTEDILAKSKKGIE----ESLRKVAKKKFAENLkagdefvektlstia 101
Cdd:PRK07531   10 IGGGVIGGGWAARFLLAGIDVAVFDphpeaerIIGEVLANAERAYAmltdAPLPPEGRLTFCASL--------------- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 102 tstdaASVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLV 181
Cdd:PRK07531   75 -----AEAVAGADWIQESVPERLDLKRRVLAEIDAAARPDALIGSSTSGFLPSDLQEGMTHPERLFVAHPYNPVYLLPLV 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 182 EVIKTPMTSQKTFESLVDFSKALGKHPVSC-KDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGY---PMG 257
Cdd:PRK07531  150 ELVGGGKTSPETIRRAKEILREIGMKPVHIaKEIDAFVGDRLLEALWREALWLVKDGIATTEEIDDVIRYSFGLrwaQMG 229


                  ...
gi 1780199935 258 PFE 260
Cdd:PRK07531  230 LFE 232
PRK08268 PRK08268
3-hydroxy-acyl-CoA dehydrogenase; Validated
 188-298 1.55e-10

3-hydroxy-acyl-CoA dehydrogenase; Validated


Pssm-ID: 236211 [Multi-domain]  Cd Length: 507  Bit Score: 61.79  E-value: 1.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935 188 MTSQKTFESLVD----FSKALGKhPVS-CKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELL 262
Cdd:PRK08268  384 MAAPATSPAARDaahaLFQQDGK-AVSvIRDSPGFVAQRTVAMIVNEAADIAQQGIASPADIDLAMRLGLNYPLGPLAWG 462

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1780199935 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 1780199935  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 3.33e-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: 41.57  E-value: 3.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935  28 KHVTVIGGGLMGAGIAQVAAATG-HTVVLVDqtedilakskkgIEESLRKVAKKKFAENLKAGDEfvEKTLSTIATSTDA 106
Cdd:cd08269   131 KTVAVIGAGFIGLLFLQLAAAAGaRRVIAID------------RRPARLALARELGATEVVTDDS--EAIVERVRELTGG 196

                          90
                  ....*....|....
gi 1780199935 107 ASVvhstDLVVEAI 120
Cdd:cd08269   197 AGA----DVVIEAV 206
GpsA COG0240
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
 28-120 9.57e-04

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: 40.40  E-value: 9.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935  28 KHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKskkgIEES------LRKVakkKFAENLKAgdefvektlstia 101
Cdd:COG0240     1 MKIAVLGAGSWGTALAKVLARNGHEVTLWGRDPEVAEE----INETrenpryLPGV---KLPENLRA------------- 60

                          90
                  ....*....|....*....
gi 1780199935 102 tSTDAASVVHSTDLVVEAI 120
Cdd:COG0240    61 -TSDLEEALAGADLVLLAV 78
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 23-65 1.10e-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: 1.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1780199935  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 1780199935  29 HVTVIGGGLMGAGIAQVAAATGHTVVLVDQ 58
Cdd:COG0665     4 DVVVIGGGIAGLSTAYHLARRGLDVTVLER 33
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 28-143 1.19e-03

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


Pssm-ID: 440056 [Multi-domain]  Cd Length: 278  Bit Score: 39.72  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935  28 KHVTVIGGGLMGAGIAQVAAATG--HTVVLVDQTEDILAKskkgieeslrkvakkkfAENLKAGDEFvektlstiatSTD 105
Cdd:COG0287     2 MRIAIIGLGLIGGSLALALKRAGlaHEVVGVDRSPETLER-----------------ALELGVIDRA----------ATD 54

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1780199935 106 AASVVHSTDLV-----VEAIVenlkvknELFKRLDKFAAEHTI 143
Cdd:COG0287    55 LEEAVADADLVvlavpVGATI-------EVLAELAPHLKPGAI 90
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 1780199935  32 VIGGGLMGAGIAQVAAATGHTVVLVDQ 58
Cdd:PRK13369   11 VIGGGINGAGIARDAAGRGLKVLLCEK 37
gpsA PRK00094
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;
28-120 3.53e-03

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


Pssm-ID: 234629 [Multi-domain]  Cd Length: 325  Bit Score: 38.51  E-value: 3.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935  28 KHVTVIGGGLMGAGIAQVAAATGHTVVLV----DQTEDILAKSK-----KGIeeslrkvakkKFAENLKAgdefvektls 98
Cdd:PRK00094    2 MKIAVLGAGSWGTALAIVLARNGHDVTLWardpEQAAEINADREnprylPGI----------KLPDNLRA---------- 61

                          90       100
                  ....*....|....*....|..
gi 1780199935  99 tiatSTDAASVVHSTDLVVEAI 120
Cdd:PRK00094   62 ----TTDLAEALADADLILVAV 79
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 27-120 4.43e-03

NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];


Pssm-ID: 440215 [Multi-domain]  Cd Length: 322  Bit Score: 38.25  E-value: 4.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780199935  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKK-----FAENLKAgdefVEKTLSTIA 101
Cdd:COG0446   124 GKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGVLDPEMAALLEEELREHgvelrLGETVVA----IDGDDKVAV 199

                          90
                  ....*....|....*....
gi 1780199935 102 TSTDAASVvhSTDLVVEAI 120
Cdd:COG0446   200 TLTDGEEI--PADLVVVAP 216
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 1780199935  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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