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Conserved domains on  [gi|6435806|pdb|3HDH|C]
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Chain C, PROTEIN (L-3-HYDROXYACYL COA DEHYDROGENASE)

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 ...
 15-301 1.26e-138

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: 392.55  E-value: 1.26e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C       15 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRK-VAKKKFAEnpkagdEFVEKTLSSISTSTD 93
Cdd:COG1250   2 IKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKlVKKGKLTE------EEADAALARITPTTD 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C       94 AASVVHStDLVVEAIVENLKVKSELFKRLDKFAAEHTIFASNTSSLQITSLANATTRQDRFAGLHFFNPVPLMKLVEVVK 173
Cdd:COG1250  76 LAALADA-DLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIR 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C      174 TPMTSQKTLESLVDFSKTLGKHPVSCKDTPGFIVNRLLVPYLIEAVRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYV 253
Cdd:COG1250 155 GPATSDETVATAVAFARRLGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPMGPFELADLV 234

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
3HDH_C      254 GLDTTKFIIDGWHEmDSQNPLFQPSPAMNKLVAENKFGKKTGEGFYKY 301
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 ...
 15-301 1.26e-138

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: 392.55  E-value: 1.26e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C       15 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRK-VAKKKFAEnpkagdEFVEKTLSSISTSTD 93
Cdd:COG1250   2 IKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKlVKKGKLTE------EEADAALARITPTTD 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C       94 AASVVHStDLVVEAIVENLKVKSELFKRLDKFAAEHTIFASNTSSLQITSLANATTRQDRFAGLHFFNPVPLMKLVEVVK 173
Cdd:COG1250  76 LAALADA-DLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIR 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C      174 TPMTSQKTLESLVDFSKTLGKHPVSCKDTPGFIVNRLLVPYLIEAVRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYV 253
Cdd:COG1250 155 GPATSDETVATAVAFARRLGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPMGPFELADLV 234

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
3HDH_C      254 GLDTTKFIIDGWHEmDSQNPLFQPSPAMNKLVAENKFGKKTGEGFYKY 301
Cdd:COG1250 235 GLDTALAVLEVLYE-ALGDPRYRPPPLLKKLVEAGRLGRKTGRGFYDY 281
PLN02545 PLN02545
3-hydroxybutyryl-CoA dehydrogenase
 15-301 6.13e-108

3-hydroxybutyryl-CoA dehydrogenase


Pssm-ID: 215300 [Multi-domain]  Cd Length: 295  Bit Score: 315.52  E-value: 6.13e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        15 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKfaenpKAGDEFVEKTLSSISTSTDA 94
Cdd:PLN02545   4 IKKVGVVGAGQMGSGIAQLAAAAGMDVWLLDSDPAALSRGLDSISSSLARLVKKG-----KMSQEEADATLGRIRCTTNL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        95 ASVvHSTDLVVEAIVENLKVKSELFKRLDKFAAEHTIFASNTSSLQITSLANATTRQDRFAGLHFFNPVPLMKLVEVVKT 174
Cdd:PLN02545  79 EEL-RDADFIIEAIVESEDLKKKLFSELDRICKPSAILASNTSSISITRLASATQRPQQVIGMHFMNPPPIMKLVEIIRG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C       175 PMTSQKTLESLVDFSKTLGKHPVSCKDTPGFIVNRLLVPYLIEAVRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYVG 254
Cdd:PLN02545 158 ADTSDEVFDATKALAERFGKTVVCSQDYPGFIVNRILMPMINEAFYALYTGVASKEDIDTGMKLGTNHPMGPLHLADFIG 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
3HDH_C       255 LDTTKFIIDGWHEmDSQNPLFQPSPAMNKLVAENKFGKKTGEGFYKY 301
Cdd:PLN02545 238 LDTCLSIMKVLHE-GLGDSKYRPCPLLVQYVDAGRLGRKSGRGVYHY 283
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
 17-202 2.22e-78

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


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 235.90  E-value: 2.22e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C         17 HVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKfaenpKAGDEFVEKTLSSISTSTDAAS 96
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKG-----RITEEEVDAALARISFTTDLAA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C         97 VVHStDLVVEAIVENLKVKSELFKRLDKFAAEHTIFASNTSSLQITSLANATTRQDRFAGLHFFNPVPLMKLVEVVKTPM 176
Cdd:pfam02737  76 AVDA-DLVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEK 154

                         170       180
                  ....*....|....*....|....*.
3HDH_C        177 TSQKTLESLVDFSKTLGKHPVSCKDT 202
Cdd:pfam02737 155 TSPETVATTVELAKKIGKTPVVVKDT 180
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
 15-301 1.37e-49

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: 175.03  E-value: 1.37e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C         15 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESL-RKVAKKKFAENPKagdefvEKTLSSISTSTD 93
Cdd:TIGR02441 335 VKTLAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLnKKVKRKKITSLER------DSILSNLTPTLD 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C         94 AaSVVHSTDLVVEAIVENLKVKSELFKRLDKFAAEHTIFASNTSSLQITSLANATTRQDRFAGLHFFNPVPLMKLVEVVK 173
Cdd:TIGR02441 409 Y-SGFKNADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEIIT 487

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        174 TPMTSQKTLESLVDFSKTLGKHPVSCKDTPGFIVNRLLVPYLIEAVRLYERG-DASKEDidtAMKLGAGYPMGPFELLDY 252
Cdd:TIGR02441 488 HDGTSKDTLASAVAVGLKQGKVVIVVKDGPGFYTTRCLGPMLAEVIRLLQEGvDPKKLD---KLTTKFGFPVGAATLADE 564

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
3HDH_C        253 VGLDTTKfiidgwHEMDSQNPLFQP-----SPA-MNKLVAENKFGKKTGEGFYKY 301
Cdd:TIGR02441 565 VGVDVAE------HVAEDLGKAFGErfgggSAElLSELVKAGFLGRKSGKGIFIY 613
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 16-108 4.74e-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: 41.19  E-value: 4.74e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C       16 KHVTVIGGGLMGAGIAQVAAATG-HTVVLVDqtedilakskkgIEESLRKVAKKKFAENPKAGDEfvEKTLSSISTSTDA 94
Cdd:cd08269 131 KTVAVIGAGFIGLLFLQLAAAAGaRRVIAID------------RRPARLALARELGATEVVTDDS--EAIVERVRELTGG 196

                        90
                ....*....|....
3HDH_C       95 ASVvhstDLVVEAI 108
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 ...
 15-301 1.26e-138

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: 392.55  E-value: 1.26e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C       15 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRK-VAKKKFAEnpkagdEFVEKTLSSISTSTD 93
Cdd:COG1250   2 IKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKlVKKGKLTE------EEADAALARITPTTD 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C       94 AASVVHStDLVVEAIVENLKVKSELFKRLDKFAAEHTIFASNTSSLQITSLANATTRQDRFAGLHFFNPVPLMKLVEVVK 173
Cdd:COG1250  76 LAALADA-DLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIR 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C      174 TPMTSQKTLESLVDFSKTLGKHPVSCKDTPGFIVNRLLVPYLIEAVRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYV 253
Cdd:COG1250 155 GPATSDETVATAVAFARRLGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPMGPFELADLV 234

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
3HDH_C      254 GLDTTKFIIDGWHEmDSQNPLFQPSPAMNKLVAENKFGKKTGEGFYKY 301
Cdd:COG1250 235 GLDTALAVLEVLYE-ALGDPRYRPPPLLKKLVEAGRLGRKTGRGFYDY 281
PLN02545 PLN02545
3-hydroxybutyryl-CoA dehydrogenase
 15-301 6.13e-108

3-hydroxybutyryl-CoA dehydrogenase


Pssm-ID: 215300 [Multi-domain]  Cd Length: 295  Bit Score: 315.52  E-value: 6.13e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        15 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKfaenpKAGDEFVEKTLSSISTSTDA 94
Cdd:PLN02545   4 IKKVGVVGAGQMGSGIAQLAAAAGMDVWLLDSDPAALSRGLDSISSSLARLVKKG-----KMSQEEADATLGRIRCTTNL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        95 ASVvHSTDLVVEAIVENLKVKSELFKRLDKFAAEHTIFASNTSSLQITSLANATTRQDRFAGLHFFNPVPLMKLVEVVKT 174
Cdd:PLN02545  79 EEL-RDADFIIEAIVESEDLKKKLFSELDRICKPSAILASNTSSISITRLASATQRPQQVIGMHFMNPPPIMKLVEIIRG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C       175 PMTSQKTLESLVDFSKTLGKHPVSCKDTPGFIVNRLLVPYLIEAVRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYVG 254
Cdd:PLN02545 158 ADTSDEVFDATKALAERFGKTVVCSQDYPGFIVNRILMPMINEAFYALYTGVASKEDIDTGMKLGTNHPMGPLHLADFIG 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
3HDH_C       255 LDTTKFIIDGWHEmDSQNPLFQPSPAMNKLVAENKFGKKTGEGFYKY 301
Cdd:PLN02545 238 LDTCLSIMKVLHE-GLGDSKYRPCPLLVQYVDAGRLGRKSGRGVYHY 283
PRK08268 PRK08268
3-hydroxy-acyl-CoA dehydrogenase; Validated
 14-301 4.12e-102

3-hydroxy-acyl-CoA dehydrogenase; Validated


Pssm-ID: 236211 [Multi-domain]  Cd Length: 507  Bit Score: 307.93  E-value: 4.12e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        14 LVKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKfaenpKAGDEFVEKTLSSISTSTD 93
Cdd:PRK08268   6 SIATVAVIGAGAMGAGIAQVAAQAGHTVLLYDARAGAAAAARDGIAARLAKLVEKG-----KLTAEQADAALARLRPVEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        94 AASVVhSTDLVVEAIVENLKVKSELFKRLDKFAAEHTIFASNTSSLQITSLANATTRQDRFAGLHFFNPVPLMKLVEVVK 173
Cdd:PRK08268  81 LADLA-DCDLVVEAIVERLDVKQALFAQLEAIVSPDCILATNTSSLSITAIAAALKHPERVAGLHFFNPVPLMKLVEVVS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C       174 TPMTSQKTLESLVDFSKTLGKHPVSCKDTPGFIVNRLLVPYLIEAVRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYV 253
Cdd:PRK08268 160 GLATDPAVADALYALARAWGKTPVRAKDTPGFIVNRAARPYYTEALRVLEEGVADPATIDAILREAAGFRMGPFELMDLI 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
3HDH_C       254 GLDTTkfiidgwHE-MDS------QNPLFQPSPAMNKLVAENKFGKKTGEGFYKY 301
Cdd:PRK08268 240 GLDVN-------HAvMESvyrqfyQEPRFRPSLIQQELVAAGRLGRKSGQGFYRY 287
PRK05808 PRK05808
3-hydroxybutyryl-CoA dehydrogenase; Validated
 15-301 7.50e-101

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 180269 [Multi-domain]  Cd Length: 282  Bit Score: 296.87  E-value: 7.50e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        15 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESL-RKVAKKKFAENPKagdefvEKTLSSISTSTD 93
Cdd:PRK05808   3 IQKIGVIGAGTMGNGIAQVCAVAGYDVVMVDISDAAVDRGLATITKSLdRLVKKGKMTEADK------EAALARITGTTD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        94 AASVvHSTDLVVEAIVENLKVKSELFKRLDKFAAEHTIFASNTSSLQITSLANATTRQDRFAGLHFFNPVPLMKLVEVVK 173
Cdd:PRK05808  77 LDDL-KDADLVIEAATENMDLKKKIFAQLDEIAKPEAILATNTSSLSITELAAATKRPDKVIGMHFFNPVPVMKLVEIIR 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C       174 TPMTSQKTLESLVDFSKTLGKHPVSCKDTPGFIVNRLLVPYLIEAVRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYV 253
Cdd:PRK05808 156 GLATSDATHEAVEALAKKIGKTPVEVKNAPGFVVNRILIPMINEAIFVLAEGVATAEDIDEGMKLGCNHPIGPLALADLI 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
3HDH_C       254 GLDTTKFIIDGWHEmDSQNPLFQPSPAMNKLVAENKFGKKTGEGFYKY 301
Cdd:PRK05808 236 GLDTCLAIMEVLYE-GFGDSKYRPCPLLRKMVAAGWLGRKTGRGFYDY 282
PRK07819 PRK07819
3-hydroxybutyryl-CoA dehydrogenase; Validated
 18-301 5.21e-100

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181133 [Multi-domain]  Cd Length: 286  Bit Score: 294.97  E-value: 5.21e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        18 VTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESL-RKVAKKKFAENPKagdefvEKTLSSISTSTDAAS 96
Cdd:PRK07819   8 VGVVGAGQMGAGIAEVCARAGVDVLVFETTEELATAGRNRIEKSLeRAVSRGKLTERER------DAALARLRFTTDLGD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        97 VVhSTDLVVEAIVENLKVKSELFKRLDKFAAE-HTIFASNTSSLQITSLANATTRQDRFAGLHFFNPVPLMKLVEVVKTP 175
Cdd:PRK07819  82 FA-DRQLVIEAVVEDEAVKTEIFAELDKVVTDpDAVLASNTSSIPIMKLAAATKRPGRVLGLHFFNPVPVLPLVELVPTL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C       176 MTSQKTLESLVDF-SKTLGKHPVSCKDTPGFIVNRLLVPYLIEAVRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYVG 254
Cdd:PRK07819 161 VTSEATVARAEEFaSDVLGKQVVRAQDRSGFVVNALLVPYLLSAIRMVESGFATAEDIDKAMVLGCAHPMGPLRLSDLVG 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
3HDH_C       255 LDTTKFIIDGWHEmDSQNPLFQPSPAMNKLVAENKFGKKTGEGFYKY 301
Cdd:PRK07819 241 LDTVKAIADSMYE-EFKEPLYAPPPLLLRMVEAGLLGKKSGRGFYTY 286
PRK07530 PRK07530
3-hydroxybutyryl-CoA dehydrogenase; Validated
 15-302 1.76e-92

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181018 [Multi-domain]  Cd Length: 292  Bit Score: 276.12  E-value: 1.76e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        15 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESL-RKVAKKKFAENPKAgdefveKTLSSISTSTD 93
Cdd:PRK07530   4 IKKVGVIGAGQMGNGIAHVCALAGYDVLLNDVSADRLEAGLATINGNLaRQVAKGKISEEARA------AALARISTATD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        94 AASVVhSTDLVVEAIVENLKVKSELFKRLDKFAAEHTIFASNTSSLQITSLANATTRQDRFAGLHFFNPVPLMKLVEVVK 173
Cdd:PRK07530  78 LEDLA-DCDLVIEAATEDETVKRKIFAQLCPVLKPEAILATNTSSISITRLASATDRPERFIGIHFMNPVPVMKLVELIR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C       174 TPMTSQKTLESLVDFSKTLGKHPVSCKDTPGFIVNRLLVPYLIEAV-RLYErGDASKEDIDTAMKLGAGYPMGPFELLDY 252
Cdd:PRK07530 157 GIATDEATFEAAKEFVTKLGKTITVAEDFPAFIVNRILLPMINEAIyTLYE-GVGSVEAIDTAMKLGANHPMGPLELADF 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
3HDH_C       253 VGLDTTKFIIDGWHE--MDSQnplFQPSPAMNKLVAENKFGKKTGEGFYKYK 302
Cdd:PRK07530 236 IGLDTCLSIMQVLHDglADSK---YRPCPLLVKYVEAGWLGRKTGRGFYDYR 284
PRK06035 PRK06035
3-hydroxyacyl-CoA dehydrogenase; Validated
 15-293 8.47e-79

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 180361 [Multi-domain]  Cd Length: 291  Bit Score: 241.32  E-value: 8.47e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        15 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEES---LRKVAKK-KFAENPkagdefVEKTLSSIST 90
Cdd:PRK06035   3 IKVIGVVGSGVMGQGIAQVFARTGYDVTIVDVSEEILKNAMELIESGpygLRNLVEKgKMSEDE------AKAIMARIRT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        91 STDAASVvHSTDLVVEAIVENLKVKSELFKRLDKFAAEHTIFASNTSSLQITSLANATTRQDRFAGLHFFNPVPLMKLVE 170
Cdd:PRK06035  77 STSYESL-SDADFIVEAVPEKLDLKRKVFAELERNVSPETIIASNTSGIMIAEIATALERKDRFIGMHWFNPAPVMKLIE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C       171 VVKTPMTSQKTLESLVDFSKTLGKHPVSCKDTPGFIVNRLLVPYLIEAVRLYERGDASKEDIDTAMKLGAGYPMGPFELL 250
Cdd:PRK06035 156 VVRAALTSEETFNTTVELSKKIGKIPIEVADVPGFFTTRFIEGWLLEAIRSFEIGIATIKDIDEMCKLAFGFPMGPFELM 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
3HDH_C       251 DYVGLDTTKFIIDGWHEmDSQNPLFQPSPAMNKLVAENKFGKK 293
Cdd:PRK06035 236 DIIGIDTVYHIAEYLYE-ETGDPQFIPPNSLKQMVLNGYVGDK 277
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
 17-202 2.22e-78

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


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 235.90  E-value: 2.22e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C         17 HVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKfaenpKAGDEFVEKTLSSISTSTDAAS 96
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKG-----RITEEEVDAALARISFTTDLAA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C         97 VVHStDLVVEAIVENLKVKSELFKRLDKFAAEHTIFASNTSSLQITSLANATTRQDRFAGLHFFNPVPLMKLVEVVKTPM 176
Cdd:pfam02737  76 AVDA-DLVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEK 154

                         170       180
                  ....*....|....*....|....*.
3HDH_C        177 TSQKTLESLVDFSKTLGKHPVSCKDT 202
Cdd:pfam02737 155 TSPETVATTVELAKKIGKTPVVVKDT 180
PRK09260 PRK09260
3-hydroxyacyl-CoA dehydrogenase;
15-301 3.01e-78

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 236434 [Multi-domain]  Cd Length: 288  Bit Score: 239.69  E-value: 3.01e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        15 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRK-VAKKKFAENPKAgdefveKTLSSISTSTD 93
Cdd:PRK09260   1 IEKLVVVGAGVMGRGIAYVFAVSGFQTTLVDIKQEQLESAQQEIASIFEQgVARGKLTEAARQ------AALARLSYSLD 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        94 AASVVHSTDLVVEAIVENLKVKSELFKRLDKFAAEHTIFASNTSSLQITSLANATTRQDRFAGLHFFNPVPLMKLVEVVK 173
Cdd:PRK09260  75 LKAAVADADLVIEAVPEKLELKKAVFETADAHAPAECYIATNTSTMSPTEIASFTKRPERVIAMHFFNPVHKMKLVELIR 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C       174 TPMTSQKTLESLVDFSKTLGKHPVSCKDTPGFIVNRLLVPYLIEAVRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYV 253
Cdd:PRK09260 155 GLETSDETVQVAKEVAEQMGKETVVVNEFPGFVTSRISALVGNEAFYMLQEGVATAEDIDKAIRLGLNFPMGPLELGDLV 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
3HDH_C       254 GLDTTKFIIDGWHEMDSQNplFQPSPAMNKLVAENKFGKKTGEGFYKY 301
Cdd:PRK09260 235 GLDTRLNNLKYLHETLGEK--YRPAPLLEKYVKAGRLGRKTGRGVYDY 280
PRK08293 PRK08293
3-hydroxyacyl-CoA dehydrogenase;
15-302 1.62e-77

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 181359 [Multi-domain]  Cd Length: 287  Bit Score: 237.92  E-value: 1.62e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        15 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEeslrKVAKKKFAENPKAGDEFVEKTLSSISTSTDA 94
Cdd:PRK08293   3 IKNVTVAGAGVLGSQIAFQTAFHGFDVTIYDISDEALEKAKERIA----KLADRYVRDLEATKEAPAEAALNRITLTTDL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        95 ASVVHSTDLVVEAIVENLKVKSELFKRLDKFAAEHTIFASNTSSLQITSLANATTRQDRFAGLHFFNPVPLMKLVEVVKT 174
Cdd:PRK08293  79 AEAVKDADLVIEAVPEDPEIKGDFYEELAKVAPEKTIFATNSSTLLPSQFAEATGRPEKFLALHFANEIWKNNTAEIMGH 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C       175 PMTSQKTLESLVDFSKTLGKHPVSC-KDTPGFIVNRLLVPYLIEAVRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYV 253
Cdd:PRK08293 159 PGTDPEVFDTVVAFAKAIGMVPIVLkKEQPGYILNSLLVPFLSAALALWAKGVADPETIDKTWMIATGAPMGPFGILDIV 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
3HDH_C       254 GLDTTKFIIDGWHEMDSQNPLFQPSPAMNKLVAENKFGKKTGEGFYKYK 302
Cdd:PRK08293 239 GLDTAYNITSNWAEATDDENAKKAAALLKEYIDKGKLGVATGEGFYNYP 287
PRK06130 PRK06130
3-hydroxybutyryl-CoA dehydrogenase; Validated
 15-301 1.08e-70

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 235707 [Multi-domain]  Cd Length: 311  Bit Score: 221.18  E-value: 1.08e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        15 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKkfaenpkagdEFVEKTLSSISTSTDA 94
Cdd:PRK06130   4 IQNLAIIGAGTMGSGIAALFARKGLQVVLIDVMEGALERARGVIERALGVYAPL----------GIASAGMGRIRMEAGL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        95 ASVVHSTDLVVEAIVENLKVKSELFKRLDKFAAEHTIFASNTSSLQITSLANATTRQDRFAGLHFFNPVPLMKLVEVVKT 174
Cdd:PRK06130  74 AAAVSGADLVIEAVPEKLELKRDVFARLDGLCDPDTIFATNTSGLPITAIAQAVTRPERFVGTHFFTPADVIPLVEVVRG 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C       175 PMTSQKTLESLVDFSKTLGKHPVSC-KDTPGFIVNRLLVPYLIEAVRLYERGDASKEDIDTAMKLGAGYPM---GPFELL 250
Cdd:PRK06130 154 DKTSPQTVATTMALLRSIGKRPVLVkKDIPGFIANRIQHALAREAISLLEKGVASAEDIDEVVKWSLGIRLaltGPLEQR 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
3HDH_C       251 DYVGLDTTKFIIDGWHEmDSQNPLfQPSPAMNKLVAENKFGKKTGEGFYKY 301
Cdd:PRK06130 234 DMNGLDVHLAVASYLYQ-DLENRT-TPSPLLEEKVEAGELGAKSGQGFYAW 282
fadJ PRK11154
fatty acid oxidation complex subunit alpha FadJ;
15-302 4.59e-65

fatty acid oxidation complex subunit alpha FadJ;


Pssm-ID: 236864 [Multi-domain]  Cd Length: 708  Bit Score: 216.69  E-value: 4.59e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        15 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVdqtEDIlakSKKGIEESLR-------KVAKKKFAenpKAGDEfvEKTLSS 87
Cdd:PRK11154 309 VNKVGVLGGGLMGGGIAYVTATKAGLPVRI---KDI---NPQGINHALKyswdlldKKVKRRHL---KPSER--DKQMAL 377

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        88 ISTSTDAaSVVHSTDLVVEAIVENLKVKSELFKRLDKFAAEHTIFASNTSSLQITSLANATTRQDRFAGLHFFNPVPLMK 167
Cdd:PRK11154 378 ISGTTDY-RGFKHADVVIEAVFEDLALKQQMVAEVEQNCAPHTIFASNTSSLPIGQIAAAAARPEQVIGLHYFSPVEKMP 456

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C       168 LVEVVKTPMTSQKTLESLVDFSKTLGKHPVSCKDTPGFIVNRLLVPYLIEAVRLYERGdASKEDIDTAMkLGAGYPMGPF 247
Cdd:PRK11154 457 LVEVIPHAKTSAETIATTVALAKKQGKTPIVVRDGAGFYVNRILAPYINEAARLLLEG-EPIEHIDAAL-VKFGFPVGPI 534

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
3HDH_C       248 ELLDYVGLDTTKFIIdgwHEMDSQ-NPLFQPSPAMNKLVAENKFGKKTGEGFYKYK 302
Cdd:PRK11154 535 TLLDEVGIDVGTKII---PILEAAlGERFSAPAAFDKLLNDDRKGRKNGRGFYLYG 587
fadB PRK11730
fatty acid oxidation complex subunit alpha FadB;
15-302 1.18e-63

fatty acid oxidation complex subunit alpha FadB;


Pssm-ID: 183293 [Multi-domain]  Cd Length: 715  Bit Score: 212.80  E-value: 1.18e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        15 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKskkGIEES---LRKVAKKKFAENPKAGdefveKTLSSISTS 91
Cdd:PRK11730 313 VKQAAVLGAGIMGGGIAYQSASKGVPVIMKDINQKALDL---GMTEAaklLNKQVERGKIDGAKMA-----GVLSSIRPT 384

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        92 TDAASVVHsTDLVVEAIVENLKVKSELFKRLDKFAAEHTIFASNTSSLQITSLANATTRQDRFAGLHFFNPVPLMKLVEV 171
Cdd:PRK11730 385 LDYAGFER-VDVVVEAVVENPKVKAAVLAEVEQKVREDTILASNTSTISISLLAKALKRPENFCGMHFFNPVHRMPLVEV 463

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C       172 VKTPMTSQKTLESLVDFSKTLGKHPVSCKDTPGFIVNRLLVPYLIEAVRLYERGdASKEDIDTAMKLGAGYPMGPFELLD 251
Cdd:PRK11730 464 IRGEKTSDETIATVVAYASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDG-ADFRQIDKVMEKQFGWPMGPAYLLD 542

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
3HDH_C       252 YVGLDT----TKFIIDGWHE-MDSQNPlfqpsPAMNKLVAENKFGKKTGEGFYKYK 302
Cdd:PRK11730 543 VVGIDTahhaQAVMAEGFPDrMKKDYR-----DAIDVLFEAKRFGQKNGKGFYRYE 593
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
 15-301 1.37e-49

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: 175.03  E-value: 1.37e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C         15 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESL-RKVAKKKFAENPKagdefvEKTLSSISTSTD 93
Cdd:TIGR02441 335 VKTLAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLnKKVKRKKITSLER------DSILSNLTPTLD 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C         94 AaSVVHSTDLVVEAIVENLKVKSELFKRLDKFAAEHTIFASNTSSLQITSLANATTRQDRFAGLHFFNPVPLMKLVEVVK 173
Cdd:TIGR02441 409 Y-SGFKNADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEIIT 487

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        174 TPMTSQKTLESLVDFSKTLGKHPVSCKDTPGFIVNRLLVPYLIEAVRLYERG-DASKEDidtAMKLGAGYPMGPFELLDY 252
Cdd:TIGR02441 488 HDGTSKDTLASAVAVGLKQGKVVIVVKDGPGFYTTRCLGPMLAEVIRLLQEGvDPKKLD---KLTTKFGFPVGAATLADE 564

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
3HDH_C        253 VGLDTTKfiidgwHEMDSQNPLFQP-----SPA-MNKLVAENKFGKKTGEGFYKY 301
Cdd:TIGR02441 565 VGVDVAE------HVAEDLGKAFGErfgggSAElLSELVKAGFLGRKSGKGIFIY 613
3HCDH pfam00725
3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda ...
 204-301 6.56e-46

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: 150.06  E-value: 6.56e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        204 GFIVNRLLVPYLIEAVRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYVGLDTTKFIIDGWHEmDSQNPLFQPSPAMNK 283
Cdd:pfam00725   1 GFVVNRLLAPYLNEAIRLVEEGVATPEDIDAAMRLGLGLPMGPFELSDLVGLDVGYHILEVLAE-EFGDRAYRPPPLLEK 79

                          90
                  ....*....|....*...
3HDH_C        284 LVAENKFGKKTGEGFYKY 301
Cdd:pfam00725  80 LVEAGRLGRKTGKGFYKY 97
PRK08269 PRK08269
3-hydroxybutyryl-CoA dehydrogenase; Validated
 26-301 1.34e-45

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181340 [Multi-domain]  Cd Length: 314  Bit Score: 156.37  E-value: 1.34e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        26 MGAGIAQVAAATGHTVVLVD-------QTEDILAKSKKGIEESLRKVAKKKFAENPKAgDEFVEKTlsSISTSTDAASVV 98
Cdd:PRK08269   1 MGQGIALAFAFAGHDVTLIDfkprdaaGWRALDAEARAEIERTLAALVALGRIDAAQA-DAVLARI--AVVARDGAADAL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        99 HSTDLVVEAIVENLKVKSELFKRLDKFAAEHTIFASNTSSLQITSLANATTRQDRFAGLHFFNPVPLMKLVEVVKTPMTS 178
Cdd:PRK08269  78 ADADLVFEAVPEVLDAKREALRWLGRHVDADAIIASTTSTFLVTDLQRHVAHPERFLNAHWLNPAYLMPLVEVSPSDATD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C       179 QKTLESLVDFSKTLGKHPVSCKDTPGFIVNRLLVPYLIEAVRLYERGDASKEDIDTAMKLGAGYP---MGPFELLDYVGL 255
Cdd:PRK08269 158 PAVVDRLAALLERIGKVPVVCGPSPGYIVPRIQALAMNEAARMVEEGVASAEDIDKAIRTGFGLRfavLGLLEFIDWGGC 237

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
3HDH_C       256 DT----TKFIIDgwhEMDSQNplFQPSPAMNKLVAENKFGKKTGEGFYKY 301
Cdd:PRK08269 238 DIlyyaSRYLAG---EIGPDR--FAPPAIVVRNMEEGRDGLRTGAGFYDY 282
PRK06129 PRK06129
3-hydroxyacyl-CoA dehydrogenase; Validated
 17-251 8.89e-43

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 235706 [Multi-domain]  Cd Length: 308  Bit Score: 149.04  E-value: 8.89e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        17 HVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLrkvakKKFAENPKAGDEFVEKTLSSISTSTDAAS 96
Cdd:PRK06129   4 SVAIIGAGLIGRAWAIVFARAGHEVRLWDADPAAAAAAPAYIAGRL-----EDLAAFDLLDGEAPDAVLARIRVTDSLAD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        97 VVHSTDLVVEAIVENLKVKSELFKRLDKFAAEHTIFASNTSSLQITSLANATTRQDRFAGLHFFNPVPLMKLVEVVKTPM 176
Cdd:PRK06129  79 AVADADYVQESAPENLELKRALFAELDALAPPHAILASSTSALLASAFTEHLAGRERCLVAHPINPPYLIPVVEVVPAPW 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
3HDH_C       177 TSQKTLESLVDFSKTLGKHPVSC-KDTPGFIVNRLLVPYLIEAVRLYERGDASKEDIDTAMKLGAGYP---MGPFELLD 251
Cdd:PRK06129 159 TAPATLARAEALYRAAGQSPVRLrREIDGFVLNRLQGALLREAFRLVADGVASVDDIDAVIRDGLGLRwsfMGPFETID 237
PRK07066 PRK07066
L-carnitine dehydrogenase;
15-247 7.75e-23

L-carnitine dehydrogenase;


Pssm-ID: 168796 [Multi-domain]  Cd Length: 321  Bit Score: 96.06  E-value: 7.75e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        15 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKFAenPKAGDEfvekTLSSISTstdA 94
Cdd:PRK07066   7 IKTFAAIGSGVIGSGWVARALAHGLDVVAWDPAPGAEAALRANVANAWPALERQGLA--PGASPA----RLRFVAT---I 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        95 ASVVHSTDLVVEAIVENLKVKSELFKRLDKFAAEHTIFASNTSSLQITSLANATTRQDRFAGLHFFNPVPLMKLVEVVKT 174
Cdd:PRK07066  78 EACVADADFIQESAPEREALKLELHERISRAAKPDAIIASSTSGLLPTDFYARATHPERCVVGHPFNPVYLLPLVEVLGG 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
3HDH_C       175 PMTSQKTLESLVDFSKTLGKHPVSC-KDTPGFIVNRLLVPYLIEAVRLYERGDASKEDIDTAMKLGAGYP---MGPF 247
Cdd:PRK07066 158 ERTAPEAVDAAMGIYRALGMRPLHVrKEVPGFIADRLLEALWREALHLVNEGVATTGEIDDAIRFGAGIRwsfMGTF 234
PRK07531 PRK07531
carnitine 3-dehydrogenase;
21-248 1.76e-17

carnitine 3-dehydrogenase;


Pssm-ID: 236044 [Multi-domain]  Cd Length: 495  Bit Score: 82.48  E-value: 1.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C        21 IGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKFAENPKAGdefvektlsSISTSTDAASVVHS 100
Cdd:PRK07531  10 IGGGVIGGGWAARFLLAGIDVAVFDPHPEAERIIGEVLANAERAYAMLTDAPLPPEG---------RLTFCASLAEAVAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C       101 TDLVVEAIVENLKVKSELFKRLDKFAAEHTIFASNTSSLQITSLANATTRQDRFAGLHFFNPVPLMKLVEVVKTPMTSQK 180
Cdd:PRK07531  81 ADWIQESVPERLDLKRRVLAEIDAAARPDALIGSSTSGFLPSDLQEGMTHPERLFVAHPYNPVYLLPLVELVGGGKTSPE 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
3HDH_C       181 TLESLVDFSKTLGKHPVSC-KDTPGFIVNRLLVPYLIEAVRLYERGDASKEDIDTAMKLGAGY---PMGPFE 248
Cdd:PRK07531 161 TIRRAKEILREIGMKPVHIaKEIDAFVGDRLLEALWREALWLVKDGIATTEEIDDVIRYSFGLrwaQMGLFE 232
PRK08268 PRK08268
3-hydroxy-acyl-CoA dehydrogenase; Validated
 201-286 2.05e-09

3-hydroxy-acyl-CoA dehydrogenase; Validated


Pssm-ID: 236211 [Multi-domain]  Cd Length: 507  Bit Score: 57.93  E-value: 2.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C       201 DTPGFIVNRLlVPYLI-EAVRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYVGLDTTKFIIDGWHEMDSQnPLFQPSP 279
Cdd:PRK08268 413 DSPGFVAQRT-VAMIVnEAADIAQQGIASPADIDLAMRLGLNYPLGPLAWGDRLGAARILRVLENLQALYGD-PRYRPSP 490


                 ....*..
3HDH_C       280 AMNKLVA 286
Cdd:PRK08268 491 WLRRRAA 497
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 17-50 6.73e-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: 6.73e-05
                          10        20        30
                  ....*....|....*....|....*....|....
3HDH_C         17 HVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDI 50
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDP 34
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 11-53 4.06e-04

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: 41.21  E-value: 4.06e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
3HDH_C       11 KKILVKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAK 53
Cdd:COG0569  91 IKKLKMHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVER 133
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 16-108 4.74e-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: 41.19  E-value: 4.74e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C       16 KHVTVIGGGLMGAGIAQVAAATG-HTVVLVDqtedilakskkgIEESLRKVAKKKFAENPKAGDEfvEKTLSSISTSTDA 94
Cdd:cd08269 131 KTVAVIGAGFIGLLFLQLAAAAGaRRVIAID------------RRPARLALARELGATEVVTDDS--EAIVERVRELTGG 196

                        90
                ....*....|....
3HDH_C       95 ASVvhstDLVVEAI 108
Cdd:cd08269 197 AGA----DVVIEAV 206
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
17-46 1.03e-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: 1.03e-03
                        10        20        30
                ....*....|....*....|....*....|
3HDH_C       17 HVTVIGGGLMGAGIAQVAAATGHTVVLVDQ 46
Cdd:COG0665   4 DVVVIGGGIAGLSTAYHLARRGLDVTVLER 33
PRK13369 PRK13369
glycerol-3-phosphate dehydrogenase; Provisional
 20-46 1.34e-03

glycerol-3-phosphate dehydrogenase; Provisional


Pssm-ID: 237365 [Multi-domain]  Cd Length: 502  Bit Score: 39.95  E-value: 1.34e-03
                         10        20
                 ....*....|....*....|....*..
3HDH_C        20 VIGGGLMGAGIAQVAAATGHTVVLVDQ 46
Cdd:PRK13369  11 VIGGGINGAGIARDAAGRGLKVLLCEK 37
GpsA COG0240
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
 16-108 2.78e-03

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


Pssm-ID: 440010 [Multi-domain]  Cd Length: 327  Bit Score: 38.86  E-value: 2.78e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HDH_C       16 KHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKskkgIEESlRkvakkkfaENPK--AGDEFVEktlsSISTSTD 93
Cdd:COG0240   1 MKIAVLGAGSWGTALAKVLARNGHEVTLWGRDPEVAEE----INET-R--------ENPRylPGVKLPE----NLRATSD 63

                        90
                ....*....|....*
3HDH_C       94 AASVVHSTDLVVEAI 108
Cdd:COG0240  64 LEEALAGADLVLLAV 78
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
18-43 7.63e-03

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


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 37.07  E-value: 7.63e-03
                        10        20
                ....*....|....*....|....*.
3HDH_C       18 VTVIGGGLMGAGIAQVAAATGHTVVL 43
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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