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Conserved domains on  [gi|311033442|sp|Q16836|]
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RecName: Full=Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial; Short=HCDH; AltName: Full=Medium and short-chain L-3-hydroxyacyl-coenzyme A dehydrogenase; AltName: Full=Short-chain 3-hydroxyacyl-CoA dehydrogenase; Flags: Precursor

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 311033442  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRK-VAKKKFAEnlkagdEFVEKTLSTIATSTD 105
Cdd:COG1250    2 IKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKlVKKGKLTE------EEADAALARITPTTD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 106 AASVVHStDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIK 185
Cdd:COG1250   76 LAALADA-DLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIR 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 186 TPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYV 265
Cdd:COG1250  155 GPATSDETVATAVAFARRLGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPMGPFELADLV 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 311033442 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 311033442  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRK-VAKKKFAEnlkagdEFVEKTLSTIATSTD 105
Cdd:COG1250    2 IKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKlVKKGKLTE------EEADAALARITPTTD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 106 AASVVHStDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIK 185
Cdd:COG1250   76 LAALADA-DLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIR 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 186 TPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYV 265
Cdd:COG1250  155 GPATSDETVATAVAFARRLGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPMGPFELADLV 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 311033442 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 311033442  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKfaenlKAGDEFVEKTLSTIATSTDA 106
Cdd:PLN02545   4 IKKVGVVGAGQMGSGIAQLAAAAGMDVWLLDSDPAALSRGLDSISSSLARLVKKG-----KMSQEEADATLGRIRCTTNL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 107 ASVvHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKT 186
Cdd:PLN02545  79 EEL-RDADFIIEAIVESEDLKKKLFSELDRICKPSAILASNTSSISITRLASATQRPQQVIGMHFMNPPPIMKLVEIIRG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 187 PMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYVG 266
Cdd:PLN02545 158 ADTSDEVFDATKALAERFGKTVVCSQDYPGFIVNRILMPMINEAFYALYTGVASKEDIDTGMKLGTNHPMGPLHLADFIG 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 311033442 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 311033442   29 HVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKfaenlKAGDEFVEKTLSTIATSTDAAS 108
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKG-----RITEEEVDAALARISFTTDLAA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442  109 VVHStDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKTPM 188
Cdd:pfam02737  76 AVDA-DLVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEK 154

                         170       180
                  ....*....|....*....|....*.
gi 311033442  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 311033442   27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKFAENLKAgdefvEKTLSTIATSTDA 106
Cdd:TIGR02441 335 VKTLAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLNKKVKRKKITSLER-----DSILSNLTPTLDY 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442  107 aSVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKT 186
Cdd:TIGR02441 410 -SGFKNADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEIITH 488

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442  187 PMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERG-DASKEDidtAMKLGAGYPMGPFELLDYV 265
Cdd:TIGR02441 489 DGTSKDTLASAVAVGLKQGKVVIVVKDGPGFYTTRCLGPMLAEVIRLLQEGvDPKKLD---KLTTKFGFPVGAATLADEV 565

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 311033442  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 311033442  28 KHVTVIGGGLMGAGIAQVAAATG-HTVVLVDqtedilakskkgIEESLRKVAKKKFAENLKAGDEfvEKTLSTIATSTDA 106
Cdd:cd08269  131 KTVAVIGAGFIGLLFLQLAAAAGaRRVIAID------------RRPARLALARELGATEVVTDDS--EAIVERVRELTGG 196

                         90
                 ....*....|....
gi 311033442 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 311033442  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRK-VAKKKFAEnlkagdEFVEKTLSTIATSTD 105
Cdd:COG1250    2 IKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKlVKKGKLTE------EEADAALARITPTTD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 106 AASVVHStDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIK 185
Cdd:COG1250   76 LAALADA-DLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIR 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 186 TPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYV 265
Cdd:COG1250  155 GPATSDETVATAVAFARRLGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPMGPFELADLV 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 311033442 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 311033442  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKfaenlKAGDEFVEKTLSTIATSTDA 106
Cdd:PLN02545   4 IKKVGVVGAGQMGSGIAQLAAAAGMDVWLLDSDPAALSRGLDSISSSLARLVKKG-----KMSQEEADATLGRIRCTTNL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 107 ASVvHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKT 186
Cdd:PLN02545  79 EEL-RDADFIIEAIVESEDLKKKLFSELDRICKPSAILASNTSSISITRLASATQRPQQVIGMHFMNPPPIMKLVEIIRG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 187 PMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYVG 266
Cdd:PLN02545 158 ADTSDEVFDATKALAERFGKTVVCSQDYPGFIVNRILMPMINEAFYALYTGVASKEDIDTGMKLGTNHPMGPLHLADFIG 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 311033442 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 311033442  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESL-RKVAKKKFAENLKagdefvEKTLSTIATSTD 105
Cdd:PRK05808   3 IQKIGVIGAGTMGNGIAQVCAVAGYDVVMVDISDAAVDRGLATITKSLdRLVKKGKMTEADK------EAALARITGTTD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 106 AASVvHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIK 185
Cdd:PRK05808  77 LDDL-KDADLVIEAATENMDLKKKIFAQLDEIAKPEAILATNTSSLSITELAAATKRPDKVIGMHFFNPVPVMKLVEIIR 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 186 TPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYV 265
Cdd:PRK05808 156 GLATSDATHEAVEALAKKIGKTPVEVKNAPGFVVNRILIPMINEAIFVLAEGVATAEDIDEGMKLGCNHPIGPLALADLI 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 311033442 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 311033442  30 VTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESL-RKVAKKKFAENLKagdefvEKTLSTIATSTDAAS 108
Cdd:PRK07819   8 VGVVGAGQMGAGIAEVCARAGVDVLVFETTEELATAGRNRIEKSLeRAVSRGKLTERER------DAALARLRFTTDLGD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 109 VVhSTDLVVEAIVENLKVKNELFKRLDKFAAE-HTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKTP 187
Cdd:PRK07819  82 FA-DRQLVIEAVVEDEAVKTEIFAELDKVVTDpDAVLASNTSSIPIMKLAAATKRPGRVLGLHFFNPVPVLPLVELVPTL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 188 MTSQKTFESLVDF-SKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYVG 266
Cdd:PRK07819 161 VTSEATVARAEEFaSDVLGKQVVRAQDRSGFVVNALLVPYLLSAIRMVESGFATAEDIDKAMVLGCAHPMGPLRLSDLVG 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 311033442 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 311033442  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKfaenlKAGDEFVEKTLSTIATSTDA 106
Cdd:PRK08268   7 IATVAVIGAGAMGAGIAQVAAQAGHTVLLYDARAGAAAAARDGIAARLAKLVEKG-----KLTAEQADAALARLRPVEAL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 107 ASVVhSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKT 186
Cdd:PRK08268  82 ADLA-DCDLVVEAIVERLDVKQALFAQLEAIVSPDCILATNTSSLSITAIAAALKHPERVAGLHFFNPVPLMKLVEVVSG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 187 PMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYVG 266
Cdd:PRK08268 161 LATDPAVADALYALARAWGKTPVRAKDTPGFIVNRAARPYYTEALRVLEEGVADPATIDAILREAAGFRMGPFELMDLIG 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 311033442 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 311033442  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESL-RKVAKKKFAENLKAgdefveKTLSTIATSTD 105
Cdd:PRK07530   4 IKKVGVIGAGQMGNGIAHVCALAGYDVLLNDVSADRLEAGLATINGNLaRQVAKGKISEEARA------AALARISTATD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 106 AASVVhSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIK 185
Cdd:PRK07530  78 LEDLA-DCDLVIEAATEDETVKRKIFAQLCPVLKPEAILATNTSSISITRLASATDRPERFIGIHFMNPVPVMKLVELIR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 186 TPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAI-RLYErGDASKEDIDTAMKLGAGYPMGPFELLDY 264
Cdd:PRK07530 157 GIATDEATFEAAKEFVTKLGKTITVAEDFPAFIVNRILLPMINEAIyTLYE-GVGSVEAIDTAMKLGANHPMGPLELADF 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 311033442 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 311033442  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEES---LRKVAKK-KFAENLkagdefVEKTLSTIAT 102
Cdd:PRK06035   3 IKVIGVVGSGVMGQGIAQVFARTGYDVTIVDVSEEILKNAMELIESGpygLRNLVEKgKMSEDE------AKAIMARIRT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 103 STDAASVvHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVE 182
Cdd:PRK06035  77 STSYESL-SDADFIVEAVPEKLDLKRKVFAELERNVSPETIIASNTSGIMIAEIATALERKDRFIGMHWFNPAPVMKLIE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 183 VIKTPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELL 262
Cdd:PRK06035 156 VVRAALTSEETFNTTVELSKKIGKIPIEVADVPGFFTTRFIEGWLLEAIRSFEIGIATIKDIDEMCKLAFGFPMGPFELM 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 311033442 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 311033442  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEeslrKVAKKKFAENLKAGDEFVEKTLSTIATSTDA 106
Cdd:PRK08293   3 IKNVTVAGAGVLGSQIAFQTAFHGFDVTIYDISDEALEKAKERIA----KLADRYVRDLEATKEAPAEAALNRITLTTDL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 107 ASVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKT 186
Cdd:PRK08293  79 AEAVKDADLVIEAVPEDPEIKGDFYEELAKVAPEKTIFATNSSTLLPSQFAEATGRPEKFLALHFANEIWKNNTAEIMGH 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 187 PMTSQKTFESLVDFSKALGKHPVSC-KDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYV 265
Cdd:PRK08293 159 PGTDPEVFDTVVAFAKAIGMVPIVLkKEQPGYILNSLLVPFLSAALALWAKGVADPETIDKTWMIATGAPMGPFGILDIV 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 311033442 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 311033442  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRK-VAKKKFAEnlkagdEFVEKTLSTIATSTD 105
Cdd:PRK09260   1 IEKLVVVGAGVMGRGIAYVFAVSGFQTTLVDIKQEQLESAQQEIASIFEQgVARGKLTE------AARQAALARLSYSLD 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 106 AASVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIK 185
Cdd:PRK09260  75 LKAAVADADLVIEAVPEKLELKKAVFETADAHAPAECYIATNTSTMSPTEIASFTKRPERVIAMHFFNPVHKMKLVELIR 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 186 TPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYV 265
Cdd:PRK09260 155 GLETSDETVQVAKEVAEQMGKETVVVNEFPGFVTSRISALVGNEAFYMLQEGVATAEDIDKAIRLGLNFPMGPLELGDLV 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 311033442 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 311033442   29 HVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKfaenlKAGDEFVEKTLSTIATSTDAAS 108
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKG-----RITEEEVDAALARISFTTDLAA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442  109 VVHStDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKTPM 188
Cdd:pfam02737  76 AVDA-DLVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEK 154

                         170       180
                  ....*....|....*....|....*.
gi 311033442  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 311033442  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEEslrkvakkkfAENLKAGDEFVEKTLSTIATSTDA 106
Cdd:PRK06130   4 IQNLAIIGAGTMGSGIAALFARKGLQVVLIDVMEGALERARGVIER----------ALGVYAPLGIASAGMGRIRMEAGL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 107 ASVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKT 186
Cdd:PRK06130  74 AAAVSGADLVIEAVPEKLELKRDVFARLDGLCDPDTIFATNTSGLPITAIAQAVTRPERFVGTHFFTPADVIPLVEVVRG 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 187 PMTSQKTFESLVDFSKALGKHPVSC-KDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPM---GPFELL 262
Cdd:PRK06130 154 DKTSPQTVATTMALLRSIGKRPVLVkKDIPGFIANRIQHALAREAISLLEKGVASAEDIDEVVKWSLGIRLaltGPLEQR 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 311033442 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 311033442  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVdqtEDIlakSKKGIEESLR-------KVAKKKFaenLKAGDEfvEKTLST 99
Cdd:PRK11154 309 VNKVGVLGGGLMGGGIAYVTATKAGLPVRI---KDI---NPQGINHALKyswdlldKKVKRRH---LKPSER--DKQMAL 377

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 100 IATSTDAaSVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMK 179
Cdd:PRK11154 378 ISGTTDY-RGFKHADVVIEAVFEDLALKQQMVAEVEQNCAPHTIFASNTSSLPIGQIAAAAARPEQVIGLHYFSPVEKMP 456

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 180 LVEVIKTPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGdASKEDIDTAMkLGAGYPMGPF 259
Cdd:PRK11154 457 LVEVIPHAKTSAETIATTVALAKKQGKTPIVVRDGAGFYVNRILAPYINEAARLLLEG-EPIEHIDAAL-VKFGFPVGPI 534

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 311033442 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 311033442  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKskkGIEES---LRKVAKKKFAENLKAGdefveKTLSTIATS 103
Cdd:PRK11730 313 VKQAAVLGAGIMGGGIAYQSASKGVPVIMKDINQKALDL---GMTEAaklLNKQVERGKIDGAKMA-----GVLSSIRPT 384

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 104 TDAASVVHsTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEV 183
Cdd:PRK11730 385 LDYAGFER-VDVVVEAVVENPKVKAAVLAEVEQKVREDTILASNTSTISISLLAKALKRPENFCGMHFFNPVHRMPLVEV 463

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 184 IKTPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGdASKEDIDTAMKLGAGYPMGPFELLD 263
Cdd:PRK11730 464 IRGEKTSDETIATVVAYASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDG-ADFRQIDKVMEKQFGWPMGPAYLLD 542

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 311033442 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 311033442   27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKFAENLKAgdefvEKTLSTIATSTDA 106
Cdd:TIGR02441 335 VKTLAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLNKKVKRKKITSLER-----DSILSNLTPTLDY 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442  107 aSVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKT 186
Cdd:TIGR02441 410 -SGFKNADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEIITH 488

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442  187 PMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERG-DASKEDidtAMKLGAGYPMGPFELLDYV 265
Cdd:TIGR02441 489 DGTSKDTLASAVAVGLKQGKVVIVVKDGPGFYTTRCLGPMLAEVIRLLQEGvDPKKLD---KLTTKFGFPVGAATLADEV 565

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 311033442  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 311033442  216 GFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYVGLDTTKFIVDGWHEmDAENPLHQPSPSLNK 295
Cdd:pfam00725   1 GFVVNRLLAPYLNEAIRLVEEGVATPEDIDAAMRLGLGLPMGPFELSDLVGLDVGYHILEVLAE-EFGDRAYRPPPLLEK 79

                          90
                  ....*....|....*...
gi 311033442  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 311033442  38 MGAGIAQVAAATGHTVVLVD-------QTEDILAKSKKGIEESLRKVAKKKFAENLKAgDEFVEKTlsTIATSTDAASVV 110
Cdd:PRK08269   1 MGQGIALAFAFAGHDVTLIDfkprdaaGWRALDAEARAEIERTLAALVALGRIDAAQA-DAVLARI--AVVARDGAADAL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 111 HSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKTPMTS 190
Cdd:PRK08269  78 ADADLVFEAVPEVLDAKREALRWLGRHVDADAIIASTTSTFLVTDLQRHVAHPERFLNAHWLNPAYLMPLVEVSPSDATD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 191 QKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYP---MGPFELLDYVGL 267
Cdd:PRK08269 158 PAVVDRLAALLERIGKVPVVCGPSPGYIVPRIQALAMNEAARMVEEGVASAEDIDKAIRTGFGLRfavLGLLEFIDWGGC 237

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 311033442 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 311033442  29 HVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLrkvakKKFAENLKAGDEFVEKTLSTIATSTDAAS 108
Cdd:PRK06129   4 SVAIIGAGLIGRAWAIVFARAGHEVRLWDADPAAAAAAPAYIAGRL-----EDLAAFDLLDGEAPDAVLARIRVTDSLAD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 109 VVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKTPM 188
Cdd:PRK06129  79 AVADADYVQESAPENLELKRALFAELDALAPPHAILASSTSALLASAFTEHLAGRERCLVAHPINPPYLIPVVEVVPAPW 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 311033442 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 311033442  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEdilakskkGIEESLRK-VAKKKFA---ENLKAGDEfvEKTLSTIAT 102
Cdd:PRK07066   7 IKTFAAIGSGVIGSGWVARALAHGLDVVAWDPAP--------GAEAALRAnVANAWPAlerQGLAPGAS--PARLRFVAT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 103 stdAASVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVE 182
Cdd:PRK07066  77 ---IEACVADADFIQESAPEREALKLELHERISRAAKPDAIIASSTSGLLPTDFYARATHPERCVVGHPFNPVYLLPLVE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 183 VIKTPMTSQKTFESLVDFSKALGKHPVSC-KDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYP---MGP 258
Cdd:PRK07066 154 VLGGERTAPEAVDAAMGIYRALGMRPLHVrKEVPGFIADRLLEALWREALHLVNEGVATTGEIDDAIRFGAGIRwsfMGT 233


                 .
gi 311033442 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 311033442  33 IGGGLMGAGIAQVAAATGHTVVLVD-------QTEDILAKSKKGIE----ESLRKVAKKKFAENLkagdefvektlstia 101
Cdd:PRK07531  10 IGGGVIGGGWAARFLLAGIDVAVFDphpeaerIIGEVLANAERAYAmltdAPLPPEGRLTFCASL--------------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 102 tstdaASVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLV 181
Cdd:PRK07531  75 -----AEAVAGADWIQESVPERLDLKRRVLAEIDAAARPDALIGSSTSGFLPSDLQEGMTHPERLFVAHPYNPVYLLPLV 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033442 182 EVIKTPMTSQKTFESLVDFSKALGKHPVSC-KDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGY---PMG 257
Cdd:PRK07531 150 ELVGGGKTSPETIRRAKEILREIGMKPVHIaKEIDAFVGDRLLEALWREALWLVKDGIATTEEIDDVIRYSFGLrwaQMG 229


                 ...
gi 311033442 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 311033442 188 MTSQKTFESLVD----FSKALGKhPVS-CKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELL 262
Cdd:PRK08268 384 MAAPATSPAARDaahaLFQQDGK-AVSvIRDSPGFVAQRTVAMIVNEAADIAQQGIASPADIDLAMRLGLNYPLGPLAWG 462

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 311033442 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 311033442   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 311033442  28 KHVTVIGGGLMGAGIAQVAAATG-HTVVLVDqtedilakskkgIEESLRKVAKKKFAENLKAGDEfvEKTLSTIATSTDA 106
Cdd:cd08269  131 KTVAVIGAGFIGLLFLQLAAAAGaRRVIAID------------RRPARLALARELGATEVVTDDS--EAIVERVRELTGG 196

                         90
                 ....*....|....
gi 311033442 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 311033442  28 KHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKskkgIEES------LRKVakkKFAENLKAgdefvektlstia 101
Cdd:COG0240    1 MKIAVLGAGSWGTALAKVLARNGHEVTLWGRDPEVAEE----INETrenpryLPGV---KLPENLRA------------- 60

                         90
                 ....*....|....*....
gi 311033442 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 311033442  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 311033442  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 311033442  28 KHVTVIGGGLMGAGIAQVAAATG--HTVVLVDQTEDILAKskkgieeslrkvakkkfAENLKAGDEFvektlstiatSTD 105
Cdd:COG0287    2 MRIAIIGLGLIGGSLALALKRAGlaHEVVGVDRSPETLER-----------------ALELGVIDRA----------ATD 54

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 311033442 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 311033442  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 311033442  28 KHVTVIGGGLMGAGIAQVAAATGHTVVLV----DQTEDILAKSK-----KGIeeslrkvakkKFAENLKAgdefvektls 98
Cdd:PRK00094   2 MKIAVLGAGSWGTALAIVLARNGHDVTLWardpEQAAEINADREnprylPGI----------KLPDNLRA---------- 61

                         90       100
                 ....*....|....*....|..
gi 311033442  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 311033442  27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKK-----FAENLKAgdefVEKTLSTIA 101
Cdd:COG0446  124 GKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGVLDPEMAALLEEELREHgvelrLGETVVA----IDGDDKVAV 199

                         90
                 ....*....|....*....
gi 311033442 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 311033442  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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