EHHADH
entrez
1962
canonical
uniprot
Q08426
canonical
ensembl
ENSG00000113790
resolver
ensp
ENSP00000231887
resolver
ensp
ENSP00000387746
resolver
genesymbol
EHHADH
resolver
genesymbol_syn
ECHD
resolver
hgnc
HGNC:3247
resolver
uniprot
A8K6Y3
resolver
uniprot
B4DWG3
resolver
uniprot
D3DNU0
resolver
uniprot
Q58EZ5
resolver
uniprot_entry
ECHP_HUMAN
resolver
uniprot_sec
A8K6Y3
resolver
uniprot_sec
B4DWG3
resolver
uniprot_sec
D3DNU0
resolver
uniprot_sec
Q58EZ5
resolver
activity_regulation
ACTIVITY REGULATION: Enzyme activity enhanced by acetylation. {ECO:0000269|PubMed:20167786}.
uniprot
proteins
amino_acid_sequence
MAEYTRLHNALALIRLRNPPVNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIRGFSAPRTFGLTLGHVVDEIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSDPVEEAIRFAQRVSDQPLESRRLCNKPIQSLPNMDSIFSEALLKMRRQHPGCLAQEACVRAVQAAVQYPYEVGIKKEEELFLYLLQSGQARALQYAFFAERKANKWSTPSGASWKTASARPVSSVGVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMITSVLEKEASKMQQSGHPWSGPKPRLTSSVKELGGVDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQYSSPTTIATVMNLSKKIKKIGVVVGNCFGFVGNRMLNPYYNQAYFLLEEGSKPEEVDQVLEEFGFKMGPFRVSDLAGLDVGWKSRKGQGLTGPTLLPGTPARKRGNRRYCPIPDVLCELGRFGQKTGKGWYQYDKPLGRIHKPDPWLSKFLSRYRKTHHIEPRTISQDEILERCLYSLINEAFRILGEGIAASPEHIDVVYLHGYGWPRHKGGPMFYASTVGLPTVLEKLQKYYRQNPDIPQLEPSDYLKKLASQGNPPLKEWQSLAGSPSSKL
uniprot
proteins
disease_involvement
DISEASE: Fanconi renotubular syndrome 3 (FRTS3) [MIM:615605]: A form of Fanconi renotubular syndrome, a disease due to a generalized dysfunction of the proximal kidney tubule resulting in decreased solute and water reabsorption. Patients have polydipsia and polyuria with phosphaturia, glycosuria and aminoaciduria. They may develop hypophosphatemic rickets or osteomalacia, acidosis and a tendency toward dehydration. Some eventually develop renal insufficiency. FRTS3 inheritance is autosomal dominant. {ECO:0000269|PubMed:24401050}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
1.1.1.35
uniprot
proteins
ec_number
4.2.1.17
uniprot
proteins
ec_number
5.3.3.8
uniprot
proteins
function
FUNCTION: Peroxisomal trifunctional enzyme possessing 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and delta 3, delta 2-enoyl-CoA isomerase activities. Catalyzes two of the four reactions of the long chain fatty acids peroxisomal beta-oxidation pathway (By similarity). Can also use branched-chain fatty acids such as 2-methyl-2E-butenoyl-CoA as a substrate, which is hydrated into (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA (By similarity). Optimal isomerase for 2,5 double bonds into 3,5 form isomerization in a range of enoyl-CoA species (Probable). Also able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species (By similarity). With HSD17B4, catalyzes the hydration of trans-2-enoyl-CoA and the dehydrogenation of 3-hydroxyacyl-CoA, but with opposite chiral specificity (PubMed:15060085). Regulates the amount of medium-chain dicarboxylic fatty acids which are essential regulators of all fatty acid oxidation pathways (By similarity). Also involved in the degradation of long-chain dicarboxylic acids through peroxisomal beta-oxidation (PubMed:15060085). {ECO:0000250|UniProtKB:P07896, ECO:0000250|UniProtKB:Q9DBM2, ECO:0000269|PubMed:15060085, ECO:0000305|PubMed:15060085}.
uniprot
proteins
mass_dalton
79495
uniprot
proteins
mutagenesis
MUTAGEN 165; /note="K->Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-171; Q-346 and Q-584."; /evidence="ECO:0000269|PubMed:20167786"; MUTAGEN 171; /note="K->Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-346 and Q-584."; /evidence="ECO:0000269|PubMed:20167786"; MUTAGEN 346; /note="K->Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-584."; /evidence="ECO:0000269|PubMed:20167786"; MUTAGEN 584; /note="K->Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-346."; /evidence="ECO:0000269|PubMed:20167786
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000269|PubMed:15060085}.
uniprot
proteins
post_translational_modification
PTM: Acetylated, leading to enhanced enzyme activity. Acetylation is enhanced by up to 80% after treatment either with trichostin A (TSA) or with nicotinamide (NAM) with highest increase on Lys-346. Acetylation and enzyme activity increased by about 1.5% on addition of fatty acids. {ECO:0000269|PubMed:20167786}.
uniprot
proteins
protein_family
Enoyl-CoA hydratase/isomerase family; 3-hydroxyacyl-CoA dehydrogenase family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15060085
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1651711
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
20167786
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24401050
uniprot
proteins
pubmed
3469675
uniprot
proteins
pubmed
8188243
uniprot
proteins
sequence_length
723
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}.
uniprot
proteins