HADH

Functionⁱ

Plays an essential role in the mitochondrial beta-oxidation of short chain fatty acids. Exerts it highest activity toward 3-hydroxybutyryl-CoA.

Catalytic activityⁱ

(S)-3-hydroxyacyl-CoA + NAD⁺ = 3-oxoacyl-CoA + NADH.

Pathwayⁱ: fatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature key	Position(s)	Length	Description
Binding siteⁱ	57 – 57	1	NAD2 Publications Manual assertion based on experiment inⁱ Ref.10 "Biochemical characterization and crystal structure determination of human heart short chain L-3-hydroxyacyl-CoA dehydrogenase provide insights into catalytic mechanism." Barycki J.J., O'Brien L.K., Bratt J.M., Zhang R., Sanishvili R., Strauss A.W., Banaszak L.J. Biochemistry 38:5786-5798(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 13-314 IN COMPLEX WITH SUBSTRATE AND NAD. Ref.11 "Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase." Barycki J.J., O'Brien L.K., Strauss A.W., Banaszak L.J. J. Biol. Chem. 275:27186-27196(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 13-314 IN COMPLEX WITH SUBSTRATE AND NAD.
Binding siteⁱ	73 – 73	1	Coenzyme A
Binding siteⁱ	80 – 80	1	Coenzyme A
Binding siteⁱ	122 – 122	1	NAD2 Publications Manual assertion based on experiment inⁱ Ref.10 "Biochemical characterization and crystal structure determination of human heart short chain L-3-hydroxyacyl-CoA dehydrogenase provide insights into catalytic mechanism." Barycki J.J., O'Brien L.K., Bratt J.M., Zhang R., Sanishvili R., Strauss A.W., Banaszak L.J. Biochemistry 38:5786-5798(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 13-314 IN COMPLEX WITH SUBSTRATE AND NAD. Ref.11 "Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase." Barycki J.J., O'Brien L.K., Strauss A.W., Banaszak L.J. J. Biol. Chem. 275:27186-27196(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 13-314 IN COMPLEX WITH SUBSTRATE AND NAD.
Binding siteⁱ	127 – 127	1	NAD2 Publications Manual assertion based on experiment inⁱ Ref.10 "Biochemical characterization and crystal structure determination of human heart short chain L-3-hydroxyacyl-CoA dehydrogenase provide insights into catalytic mechanism." Barycki J.J., O'Brien L.K., Bratt J.M., Zhang R., Sanishvili R., Strauss A.W., Banaszak L.J. Biochemistry 38:5786-5798(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 13-314 IN COMPLEX WITH SUBSTRATE AND NAD. Ref.11 "Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase." Barycki J.J., O'Brien L.K., Strauss A.W., Banaszak L.J. J. Biol. Chem. 275:27186-27196(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 13-314 IN COMPLEX WITH SUBSTRATE AND NAD.
Binding siteⁱ	149 – 149	1	Coenzyme A
Binding siteⁱ	149 – 149	1	NAD2 Publications Manual assertion based on experiment inⁱ Ref.10 "Biochemical characterization and crystal structure determination of human heart short chain L-3-hydroxyacyl-CoA dehydrogenase provide insights into catalytic mechanism." Barycki J.J., O'Brien L.K., Bratt J.M., Zhang R., Sanishvili R., Strauss A.W., Banaszak L.J. Biochemistry 38:5786-5798(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 13-314 IN COMPLEX WITH SUBSTRATE AND NAD. Ref.11 "Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase." Barycki J.J., O'Brien L.K., Strauss A.W., Banaszak L.J. J. Biol. Chem. 275:27186-27196(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 13-314 IN COMPLEX WITH SUBSTRATE AND NAD.
Siteⁱ	170 – 170	1	Important for catalytic activityCurated
Binding siteⁱ	173 – 173	1	NAD2 Publications Manual assertion based on experiment inⁱ Ref.10 "Biochemical characterization and crystal structure determination of human heart short chain L-3-hydroxyacyl-CoA dehydrogenase provide insights into catalytic mechanism." Barycki J.J., O'Brien L.K., Bratt J.M., Zhang R., Sanishvili R., Strauss A.W., Banaszak L.J. Biochemistry 38:5786-5798(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 13-314 IN COMPLEX WITH SUBSTRATE AND NAD. Ref.11 "Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase." Barycki J.J., O'Brien L.K., Strauss A.W., Banaszak L.J. J. Biol. Chem. 275:27186-27196(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 13-314 IN COMPLEX WITH SUBSTRATE AND NAD.
Binding siteⁱ	305 – 305	1	NAD2 Publications Manual assertion based on experiment inⁱ Ref.10 "Biochemical characterization and crystal structure determination of human heart short chain L-3-hydroxyacyl-CoA dehydrogenase provide insights into catalytic mechanism." Barycki J.J., O'Brien L.K., Bratt J.M., Zhang R., Sanishvili R., Strauss A.W., Banaszak L.J. Biochemistry 38:5786-5798(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 13-314 IN COMPLEX WITH SUBSTRATE AND NAD. Ref.11 "Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase." Barycki J.J., O'Brien L.K., Strauss A.W., Banaszak L.J. J. Biol. Chem. 275:27186-27196(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 13-314 IN COMPLEX WITH SUBSTRATE AND NAD.

Regions

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Nucleotide bindingⁱ	34 – 39	6	NAD2 Publications Manual assertion based on experiment inⁱ Ref.10 "Biochemical characterization and crystal structure determination of human heart short chain L-3-hydroxyacyl-CoA dehydrogenase provide insights into catalytic mechanism." Barycki J.J., O'Brien L.K., Bratt J.M., Zhang R., Sanishvili R., Strauss A.W., Banaszak L.J. Biochemistry 38:5786-5798(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 13-314 IN COMPLEX WITH SUBSTRATE AND NAD. Ref.11 "Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase." Barycki J.J., O'Brien L.K., Strauss A.W., Banaszak L.J. J. Biol. Chem. 275:27186-27196(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 13-314 IN COMPLEX WITH SUBSTRATE AND NAD.

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS06563-MONOMER.
BRENDAⁱ	1.1.1.35. 2681.
Reactomeⁱ	R-HSA-77310. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA. R-HSA-77346. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA. R-HSA-77348. Beta oxidation of octanoyl-CoA to hexanoyl-CoA. R-HSA-77350. Beta oxidation of hexanoyl-CoA to butanoyl-CoA. R-HSA-77352. Beta oxidation of butanoyl-CoA to acetyl-CoA.
SABIO-RK	Q16836.
UniPathwayⁱ	UPA00659.

Chemistry

SwissLipidsⁱ	SLP:000001250.

SwissLipidsⁱ

SLP:000001250.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial (EC:1.1.1.35) Short name: HCDH Alternative name(s): Medium and short-chain L-3-hydroxyacyl-coenzyme A dehydrogenase Short-chain 3-hydroxyacyl-CoA dehydrogenase
Gene namesⁱ	Name:HADH Synonyms:HAD, HADHSC, SCHAD
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 4

Organism-specific databases

HGNCⁱ	HGNC:4799. HADH.

HGNCⁱ

HGNC:4799. HADH.

Subcellular locationⁱ

Mitochondrion matrix

GO - Cellular componentⁱ

cytoplasm Source: LIFEdb
mitochondrial inner membrane Source: Ensembl
mitochondrial matrix Source: Reactome
mitochondrion Source: HPA
nucleoplasm Source: HPA

Complete GO annotation...

Keywords - Cellular componentⁱ

Mitochondrion

Pathology & Biotechⁱ

Involvement in diseaseⁱ

3-alpha-hydroxyacyl-CoA dehydrogenase deficiency (HADH deficiency)1 Publication
Manual assertion based on experiment inⁱ
Ref.13
"Fulminant hepatic failure associated with mutations in the medium and short chain L-3-hydroxyacyl-CoA dehydrogenase gene."
O'Brien L.K., Rinaldo P., Sims H.F., Alonso E.M., Charrow J., Jones P.M., Bennett M.J., Barycki J.J., Banaszak L.J., Strauss A.W.
J. Inherit. Metab. Dis. 23 Suppl. 1:127-127(2000)
Cited for: VARIANTS HADH DEFICIENCY THR-40 AND GLU-57.

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA metabolic disorder with various clinical presentations including hypoglycemia, hepatoencephalopathy, myopathy or cardiomyopathy, and in some cases sudden death.

Familial hyperinsulinemic hypoglycemia 4 (HHF4)1 Publication
Manual assertion based on experiment inⁱ
Ref.14
"Hyperinsulinism in short-chain L-3-hydroxyacyl-CoA dehydrogenase deficiency reveals the importance of beta-oxidation in insulin secretion."
Clayton P.T., Eaton S., Aynsley-Green A., Edginton M., Hussain K., Krywawych S., Datta V., Malingre H.E.M., Berger R., van den Berg I.E.T.
J. Clin. Invest. 108:457-465(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HHF4 LEU-258, CHARACTERIZATION OF VARIANT HHF4 LEU-258.

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionMost common cause of persistent hypoglycemia in infancy. Unless early and aggressive intervention is undertaken, brain damage from recurrent episodes of hypoglycemia may occur. HHF4 should be easily recognizable by analysis of acylcarnitine species and that this disorder responds well to treatment with diazoxide. It provides the first 'experiment of nature' that links impaired fatty acid oxidation to hyperinsulinism and that provides support for the concept that a lipid signaling pathway is implicated in the control of insulin secretion.

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Natural variantⁱ	258 – 258	1	P → L in HHF4; loss of activity. 1 Publication Manual assertion based on experiment inⁱ Ref.14 "Hyperinsulinism in short-chain L-3-hydroxyacyl-CoA dehydrogenase deficiency reveals the importance of beta-oxidation in insulin secretion." Clayton P.T., Eaton S., Aynsley-Green A., Edginton M., Hussain K., Krywawych S., Datta V., Malingre H.E.M., Berger R., van den Berg I.E.T. J. Clin. Invest. 108:457-465(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HHF4 LEU-258, CHARACTERIZATION OF VARIANT HHF4 LEU-258. Corresponds to variant rs137853103 [ dbSNP \| Ensembl ].		VAR_024081

Keywords - Diseaseⁱ

Disease mutation

Organism-specific databases

MalaCardsⁱ	HADH.
MIMⁱ	231530. phenotype. 609975. phenotype.
Orphanetⁱ	71212. Hyperinsulinism due to short chain 3-hydroxylacyl-CoA dehydrogenase deficiency.
PharmGKBⁱ	PA29173.

Polymorphism and mutation databases

BioMutaⁱ	HADH.
DMDMⁱ	311033442.

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Transit peptideⁱ	1 – 12	12	Mitochondrion			Add BLAST
Chainⁱ	13 – 314	302	Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial		PRO_0000007406	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description
Modified residueⁱ	80 – 80	1	N6-succinyllysineBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q61425 (HCDH_MOUSE)
Modified residueⁱ	81 – 81	1	N6-acetyllysine; alternateBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q61425 (HCDH_MOUSE)
Modified residueⁱ	81 – 81	1	N6-succinyllysine; alternateBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q61425 (HCDH_MOUSE)
Modified residueⁱ	87 – 87	1	N6-acetyllysine; alternateBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q61425 (HCDH_MOUSE)
Modified residueⁱ	87 – 87	1	N6-succinyllysine; alternateBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q61425 (HCDH_MOUSE)
Modified residueⁱ	125 – 125	1	N6-acetyllysineBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q61425 (HCDH_MOUSE)
Modified residueⁱ	136 – 136	1	N6-acetyllysine; alternateBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q61425 (HCDH_MOUSE)
Modified residueⁱ	136 – 136	1	N6-succinyllysine; alternateBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q61425 (HCDH_MOUSE)
Modified residueⁱ	179 – 179	1	N6-acetyllysineBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q61425 (HCDH_MOUSE)
Modified residueⁱ	185 – 185	1	N6-acetyllysine; alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.6 "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-185; LYS-202; LYS-241 AND LYS-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	185 – 185	1	N6-succinyllysine; alternateBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q61425 (HCDH_MOUSE)
Modified residueⁱ	192 – 192	1	N6-acetyllysine; alternateBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q61425 (HCDH_MOUSE)
Modified residueⁱ	192 – 192	1	N6-succinyllysine; alternateBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q61425 (HCDH_MOUSE)
Modified residueⁱ	202 – 202	1	N6-acetyllysine; alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.6 "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-185; LYS-202; LYS-241 AND LYS-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	202 – 202	1	N6-succinyllysine; alternateBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q61425 (HCDH_MOUSE)
Modified residueⁱ	206 – 206	1	N6-succinyllysineBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q61425 (HCDH_MOUSE)
Modified residueⁱ	212 – 212	1	N6-acetyllysine; alternateBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q61425 (HCDH_MOUSE)
Modified residueⁱ	212 – 212	1	N6-succinyllysine; alternateBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q61425 (HCDH_MOUSE)
Modified residueⁱ	241 – 241	1	N6-acetyllysine; alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.6 "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-185; LYS-202; LYS-241 AND LYS-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	241 – 241	1	N6-succinyllysine; alternateBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q61425 (HCDH_MOUSE)
Modified residueⁱ	312 – 312	1	N6-acetyllysine; alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.6 "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-185; LYS-202; LYS-241 AND LYS-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	312 – 312	1	N6-succinyllysine; alternateBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q61425 (HCDH_MOUSE)

Post-translational modificationⁱ

Succinylation at Lys-81, adjacent to a coenzyme A binding site. Desuccinylated by SIRT5 (By similarity).By similarity

Keywords - PTMⁱ

Acetylation

Proteomic databases

EPDⁱ	Q16836.
MaxQBⁱ	Q16836.
PeptideAtlasⁱ	Q16836.
PRIDEⁱ	Q16836.
TopDownProteomicsⁱ	Q16836-1. [Q16836-1]

2D gel databases

REPRODUCTION-2DPAGE	IPI00298406.
UCD-2DPAGE	O00324. Q16836.

PTM databases

iPTMnetⁱ	Q16836.
PhosphoSiteⁱ	Q16836.

Expressionⁱ

Tissue specificityⁱ

Expressed in liver, kidney, pancreas, heart and skeletal muscle.

Gene expression databases

Bgeeⁱ	ENSG00000138796.
CleanExⁱ	HS_HADH.
ExpressionAtlasⁱ	Q16836. baseline and differential.
Genevisibleⁱ	Q16836. HS.

Organism-specific databases

HPAⁱ	HPA039588. HPA043888.

Interactionⁱ

Subunit structureⁱ

Homodimer.2 Publications

Protein-protein interaction databases

BioGridⁱ	109283. 23 interactions.
IntActⁱ	Q16836. 3 interactions.
MINTⁱ	MINT-5004681.

Structureⁱ

Secondary structure

314

Legend: HelixTurnBeta strand

Show more details

Feature key	Position(s)	Length	Description
Helixⁱ	1 – 11	11	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:3RQS
Helixⁱ	14 – 22	9	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:3RQS
Beta strandⁱ	29 – 33	5	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F0Y
Helixⁱ	37 – 48	12	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F0Y
Beta strandⁱ	52 – 56	5	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F0Y
Helixⁱ	60 – 79	20	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F0Y
Beta strandⁱ	82 – 84	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F0Y
Helixⁱ	86 – 98	13	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F0Y
Beta strandⁱ	100 – 104	5	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F0Y
Helixⁱ	106 – 109	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F0Y
Helixⁱ	110 – 112	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:3HAD
Beta strandⁱ	114 – 118	5	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F0Y
Helixⁱ	124 – 134	11	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F0Y
Turnⁱ	135 – 137	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F0Y
Beta strandⁱ	143 – 146	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F0Y
Beta strandⁱ	149 – 151	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F0Y
Helixⁱ	153 – 157	5	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F0Y
Helixⁱ	163 – 165	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F0Y
Beta strandⁱ	166 – 171	6	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F0Y
Turnⁱ	175 – 177	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F0Y
Beta strandⁱ	180 – 184	5	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F0Y
Helixⁱ	191 – 203	13	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F0Y
Beta strandⁱ	207 – 211	5	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F0Y
Turnⁱ	215 – 218	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F0Y
Helixⁱ	219 – 235	17	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F0Y
Helixⁱ	241 – 252	12	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F0Y
Helixⁱ	258 – 265	8	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F0Y
Helixⁱ	267 – 279	13	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F0Y
Turnⁱ	280 – 283	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F0Y
Helixⁱ	285 – 287	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F0Y
Helixⁱ	291 – 298	8	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F0Y
Turnⁱ	304 – 307	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F0Y
Beta strandⁱ	308 – 312	5	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F0Y

3D structure databases

Select the link destinations:
PDBeⁱ
RCSB PDBⁱ
PDBjⁱ

Links Updated

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F0Y	X-ray	1.80	A/B	13-314	[»]
1F12	X-ray	2.40	A/B	13-314	[»]
1F14	X-ray	2.30	A/B	13-314	[»]
1F17	X-ray	2.30	A/B	13-314	[»]
1IL0	X-ray	2.20	A/B	13-314	[»]
1LSJ	X-ray	2.50	A/B	13-314	[»]
1LSO	X-ray	2.60	A/B	13-314	[»]
1M75	X-ray	2.30	A/B	13-314	[»]
1M76	X-ray	2.15	A/B	13-314	[»]
2HDH	X-ray	2.20	A/B	24-314	[»]
3HAD	X-ray	2.00	A/B	13-314	[»]
3RQS	X-ray	2.00	A/B	1-314	[»]

ProteinModelPortalⁱ

Q16836.

SMRⁱ

Q16836. Positions 1-314.

ModBaseⁱ

Search...

MobiDBⁱ

Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q16836.

EvolutionaryTraceⁱ

Q16836.

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.Curated

Keywords - Domainⁱ

Transit peptide

Phylogenomic databases

GeneTreeⁱ	ENSGT00720000108673.
HOGENOMⁱ	HOG000141498.
HOVERGENⁱ	HBG000832.
InParanoidⁱ	Q16836.
KOⁱ	K00022.
PhylomeDBⁱ	Q16836.
TreeFamⁱ	TF300886.

Family and domain databases

Gene3Dⁱ	1.10.1040.10. 1 hit. 3.40.50.720. 1 hit.
InterProⁱ	IPR022694. 3-OHacyl-CoA_DH. IPR006180. 3-OHacyl-CoA_DH_CS. IPR006176. 3-OHacyl-CoA_DH_NAD-bd. IPR006108. 3HC_DH_C. IPR008927. 6-PGluconate_DH_C-like. IPR013328. 6PGD_dom_2. IPR016040. NAD(P)-bd_dom. [Graphical view]
Pfamⁱ	PF00725. 3HCDH. 1 hit. PF02737. 3HCDH_N. 1 hit. [Graphical view]
PIRSFⁱ	PIRSF000105. HCDH. 1 hit.
SUPFAMⁱ	SSF48179. SSF48179. 1 hit. SSF51735. SSF51735. 1 hit.
PROSITEⁱ	PS00067. 3HCDH. 1 hit. [Graphical view]

Sequences (3)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsⁱ produced by alternative splicing. Align Add to basket Added to basket

Isoform 1 (identifier: Q16836-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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        10         20         30         40         50
MAFVTRQFMR SVSSSSTASA SAKKIIVKHV TVIGGGLMGA GIAQVAAATG 
        60         70         80         90        100
HTVVLVDQTE DILAKSKKGI EESLRKVAKK KFAENLKAGD EFVEKTLSTI 
       110        120        130        140        150
ATSTDAASVV HSTDLVVEAI VENLKVKNEL FKRLDKFAAE HTIFASNTSS 
       160        170        180        190        200
LQITSIANAT TRQDRFAGLH FFNPVPVMKL VEVIKTPMTS QKTFESLVDF 
       210        220        230        240        250
SKALGKHPVS CKDTPGFIVN RLLVPYLMEA IRLYERGDAS KEDIDTAMKL 
       260        270        280        290        300
GAGYPMGPFE LLDYVGLDTT KFIVDGWHEM DAENPLHQPS PSLNKLVAEN 
       310 
KFGKKTGEGF YKYK

Length:314

Mass (Da):34,294

Last modified:November 2, 2010 - v3

Checksum:ⁱ0C6F7C01BBCE646A

GO

Isoform 2 (identifier: Q16836-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-1: M → MGRAGLEAPPPPCGVTGTPGARGLQGRVGPRPQSLAFRGCLPRASSLPGSPRCRRRCHTM
236-236: R → RDFQTCGDSNSGLGFSLK

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        10         20         30         40         50
MGRAGLEAPP PPCGVTGTPG ARGLQGRVGP RPQSLAFRGC LPRASSLPGS 
        60         70         80         90        100
PRCRRRCHTM AFVTRQFMRS VSSSSTASAS AKKIIVKHVT VIGGGLMGAG 
       110        120        130        140        150
IAQVAAATGH TVVLVDQTED ILAKSKKGIE ESLRKVAKKK FAENLKAGDE 
       160        170        180        190        200
FVEKTLSTIA TSTDAASVVH STDLVVEAIV ENLKVKNELF KRLDKFAAEH 
       210        220        230        240        250
TIFASNTSSL QITSIANATT RQDRFAGLHF FNPVPVMKLV EVIKTPMTSQ 
       260        270        280        290        300
KTFESLVDFS KALGKHPVSC KDTPGFIVNR LLVPYLMEAI RLYERDFQTC 
       310        320        330        340        350
GDSNSGLGFS LKGDASKEDI DTAMKLGAGY PMGPFELLDY VGLDTTKFIV 
       360        370        380        390
DGWHEMDAEN PLHQPSPSLN KLVAENKFGK KTGEGFYKYK

Show »

Length:390

Mass (Da):42,140

Checksum:ⁱ3C20D80AAC4EB142

GO

Isoform 3 (identifier: Q16836-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
236-236: R → RDFQTCGDSNSGLGFSLK

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        10         20         30         40         50
MAFVTRQFMR SVSSSSTASA SAKKIIVKHV TVIGGGLMGA GIAQVAAATG 
        60         70         80         90        100
HTVVLVDQTE DILAKSKKGI EESLRKVAKK KFAENLKAGD EFVEKTLSTI 
       110        120        130        140        150
ATSTDAASVV HSTDLVVEAI VENLKVKNEL FKRLDKFAAE HTIFASNTSS 
       160        170        180        190        200
LQITSIANAT TRQDRFAGLH FFNPVPVMKL VEVIKTPMTS QKTFESLVDF 
       210        220        230        240        250
SKALGKHPVS CKDTPGFIVN RLLVPYLMEA IRLYERDFQT CGDSNSGLGF 
       260        270        280        290        300
SLKGDASKED IDTAMKLGAG YPMGPFELLD YVGLDTTKFI VDGWHEMDAE 
       310        320        330 
NPLHQPSPSL NKLVAENKFG KKTGEGFYKY K

Note: No experimental confirmation available.

Show »

Length:331

Mass (Da):36,051

Checksum:ⁱ11B5646AD077A666

GO

Experimental Info

Feature key	Position(s)	Length	Description
Isoform 2 (identifier: Q16836-2)
Sequence conflictⁱ	41 – 41	1	L → P in AAB58153 (Ref. 2) Curated
Sequence conflictⁱ	56 – 56	1	R → H in AAB58153 (Ref. 2) Curated

Natural variant

Feature key	Position(s)	Length	Description	Feature identifier
Natural variantⁱ	40 – 40	1	A → T in HADH deficiency. 1 Publication Manual assertion based on experiment inⁱ Ref.13 "Fulminant hepatic failure associated with mutations in the medium and short chain L-3-hydroxyacyl-CoA dehydrogenase gene." O'Brien L.K., Rinaldo P., Sims H.F., Alonso E.M., Charrow J., Jones P.M., Bennett M.J., Barycki J.J., Banaszak L.J., Strauss A.W. J. Inherit. Metab. Dis. 23 Suppl. 1:127-127(2000) Cited for: VARIANTS HADH DEFICIENCY THR-40 AND GLU-57. Corresponds to variant rs137853101 [ dbSNP \| Ensembl ].	VAR_024079
Natural variantⁱ	57 – 57	1	D → E in HADH deficiency. 1 Publication Manual assertion based on experiment inⁱ Ref.13 "Fulminant hepatic failure associated with mutations in the medium and short chain L-3-hydroxyacyl-CoA dehydrogenase gene." O'Brien L.K., Rinaldo P., Sims H.F., Alonso E.M., Charrow J., Jones P.M., Bennett M.J., Barycki J.J., Banaszak L.J., Strauss A.W. J. Inherit. Metab. Dis. 23 Suppl. 1:127-127(2000) Cited for: VARIANTS HADH DEFICIENCY THR-40 AND GLU-57. Corresponds to variant rs137853102 [ dbSNP \| Ensembl ].	VAR_024080
Natural variantⁱ	86 – 86	1	L → P.4 Publications Manual assertion based on experiment inⁱ Ref.1 "Human short-chain L-3-hydroxyacyl-CoA dehydrogenase: cloning and characterization of the coding sequence." Vredendaal P.J.C.M., van den Berg I.E.T., Malingre H.E.M., Stroobants A.K., Oldeweghuis D.E.M., Berger R. Biochem. Biophys. Res. Commun. 223:718-723(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS PRO-86 AND HIS-152. Ref.2 "Cloning of a L-3-hydroxyacyl CoA dehydrogenase that binds to GLUT4 glucose transporter cytoplasmic C-terminus: possible crosstalk between glucose transport and fatty acid metabolism." Shi Y., Samuel S.J., Lee W., Yu C.H., Zhang W., Lachaal M., Jung C.Y. Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 7-314 (ISOFORM 1), VARIANT PRO-86. Ref.3 "Human short chain L-3-hydroxyacyl-CoA dehydrogenase." O'Brien L.K., Sims H.F., Strauss A.W. Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PRO-86. Ref.5 "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT PRO-86. Corresponds to variant rs4956145 [ dbSNP \| Ensembl ].	VAR_026764
Natural variantⁱ	152 – 152	1	Q → H.1 Publication Manual assertion based on experiment inⁱ Ref.1 "Human short-chain L-3-hydroxyacyl-CoA dehydrogenase: cloning and characterization of the coding sequence." Vredendaal P.J.C.M., van den Berg I.E.T., Malingre H.E.M., Stroobants A.K., Oldeweghuis D.E.M., Berger R. Biochem. Biophys. Res. Commun. 223:718-723(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS PRO-86 AND HIS-152. Corresponds to variant rs1051519 [ dbSNP \| Ensembl ].	VAR_055701
Natural variantⁱ	258 – 258	1	P → L in HHF4; loss of activity. 1 Publication Manual assertion based on experiment inⁱ Ref.14 "Hyperinsulinism in short-chain L-3-hydroxyacyl-CoA dehydrogenase deficiency reveals the importance of beta-oxidation in insulin secretion." Clayton P.T., Eaton S., Aynsley-Green A., Edginton M., Hussain K., Krywawych S., Datta V., Malingre H.E.M., Berger R., van den Berg I.E.T. J. Clin. Invest. 108:457-465(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HHF4 LEU-258, CHARACTERIZATION OF VARIANT HHF4 LEU-258. Corresponds to variant rs137853103 [ dbSNP \| Ensembl ].	VAR_024081

Alternative sequence

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Alternative sequenceⁱ	1 – 1	1	M → MGRAGLEAPPPPCGVTGTPG ARGLQGRVGPRPQSLAFRGC LPRASSLPGSPRCRRRCHTM in isoform 2. 1 Publication Manual assertion based on opinion inⁱ Ref.2 "Cloning of a L-3-hydroxyacyl CoA dehydrogenase that binds to GLUT4 glucose transporter cytoplasmic C-terminus: possible crosstalk between glucose transport and fatty acid metabolism." Shi Y., Samuel S.J., Lee W., Yu C.H., Zhang W., Lachaal M., Jung C.Y. Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 7-314 (ISOFORM 1), VARIANT PRO-86.		VSP_016551
Alternative sequenceⁱ	236 – 236	1	R → RDFQTCGDSNSGLGFSLK in isoform 2 and isoform 3. 1 Publication Manual assertion based on opinion inⁱ Ref.2 "Cloning of a L-3-hydroxyacyl CoA dehydrogenase that binds to GLUT4 glucose transporter cytoplasmic C-terminus: possible crosstalk between glucose transport and fatty acid metabolism." Shi Y., Samuel S.J., Lee W., Yu C.H., Zhang W., Lachaal M., Jung C.Y. Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 7-314 (ISOFORM 1), VARIANT PRO-86.		VSP_016552

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X96752 mRNA. Translation: CAA65528.1. AF001902 mRNA. Translation: AAB54008.1. AF001903 mRNA. Translation: AAB54009.1. AF001904 Genomic DNA. Translation: AAB58153.1. AF095703 Genomic DNA. Translation: AAD13581.1. AC114733 Genomic DNA. Translation: AAY41050.1. AC118062 Genomic DNA. No translation available. BC000306 mRNA. Translation: AAH00306.1.
CCDSⁱ	CCDS3678.1. [Q16836-1] CCDS54790.1. [Q16836-3]
PIRⁱ	JC4879.
RefSeqⁱ	NP_001171634.2. NM_001184705.2. NP_005318.3. NM_005327.4.
UniGeneⁱ	Hs.438289.

Genome annotation databases

Ensemblⁱ	ENST00000309522; ENSP00000312288; ENSG00000138796. [Q16836-1] ENST00000603302; ENSP00000474560; ENSG00000138796. [Q16836-3]
GeneIDⁱ	3033.
KEGGⁱ	hsa:3033.
UCSCⁱ	uc003hyq.4. human. [Q16836-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X96752 mRNA. Translation: CAA65528.1. AF001902 mRNA. Translation: AAB54008.1. AF001903 mRNA. Translation: AAB54009.1. AF001904 Genomic DNA. Translation: AAB58153.1. AF095703 Genomic DNA. Translation: AAD13581.1. AC114733 Genomic DNA. Translation: AAY41050.1. AC118062 Genomic DNA. No translation available. BC000306 mRNA. Translation: AAH00306.1.
CCDSⁱ	CCDS3678.1. [Q16836-1] CCDS54790.1. [Q16836-3]
PIRⁱ	JC4879.
RefSeqⁱ	NP_001171634.2. NM_001184705.2. NP_005318.3. NM_005327.4.
UniGeneⁱ	Hs.438289.

3D structure databases

Select the link destinations:
PDBeⁱ
RCSB PDBⁱ
PDBjⁱ

Links Updated

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F0Y	X-ray	1.80	A/B	13-314	[»]
1F12	X-ray	2.40	A/B	13-314	[»]
1F14	X-ray	2.30	A/B	13-314	[»]
1F17	X-ray	2.30	A/B	13-314	[»]
1IL0	X-ray	2.20	A/B	13-314	[»]
1LSJ	X-ray	2.50	A/B	13-314	[»]
1LSO	X-ray	2.60	A/B	13-314	[»]
1M75	X-ray	2.30	A/B	13-314	[»]
1M76	X-ray	2.15	A/B	13-314	[»]
2HDH	X-ray	2.20	A/B	24-314	[»]
3HAD	X-ray	2.00	A/B	13-314	[»]
3RQS	X-ray	2.00	A/B	1-314	[»]

ProteinModelPortalⁱ

Q16836.

SMRⁱ

Q16836. Positions 1-314.

ModBaseⁱ

Search...

MobiDBⁱ

Search...

Protein-protein interaction databases

BioGridⁱ	109283. 23 interactions.
IntActⁱ	Q16836. 3 interactions.
MINTⁱ	MINT-5004681.

Chemistry

SwissLipidsⁱ	SLP:000001250.

SwissLipidsⁱ

SLP:000001250.

PTM databases

iPTMnetⁱ	Q16836.
PhosphoSiteⁱ	Q16836.

Polymorphism and mutation databases

BioMutaⁱ	HADH.
DMDMⁱ	311033442.

2D gel databases

REPRODUCTION-2DPAGE	IPI00298406.
UCD-2DPAGE	O00324. Q16836.

Proteomic databases

EPDⁱ	Q16836.
MaxQBⁱ	Q16836.
PeptideAtlasⁱ	Q16836.
PRIDEⁱ	Q16836.
TopDownProteomicsⁱ	Q16836-1. [Q16836-1]

Protocols and materials databases

DNASUⁱ	3033.
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000309522; ENSP00000312288; ENSG00000138796. [Q16836-1] ENST00000603302; ENSP00000474560; ENSG00000138796. [Q16836-3]
GeneIDⁱ	3033.
KEGGⁱ	hsa:3033.
UCSCⁱ	uc003hyq.4. human. [Q16836-1]

Organism-specific databases

CTDⁱ	3033.
GeneCardsⁱ	HADH.
GeneReviewsⁱ	HADH.
HGNCⁱ	HGNC:4799. HADH.
HPAⁱ	HPA039588. HPA043888.
MalaCardsⁱ	HADH.
MIMⁱ	231530. phenotype. 601609. gene. 609975. phenotype.
neXtProtⁱ	NX_Q16836.
Orphanetⁱ	71212. Hyperinsulinism due to short chain 3-hydroxylacyl-CoA dehydrogenase deficiency.
PharmGKBⁱ	PA29173.
GenAtlasⁱ	Search...

Phylogenomic databases

GeneTreeⁱ	ENSGT00720000108673.
HOGENOMⁱ	HOG000141498.
HOVERGENⁱ	HBG000832.
InParanoidⁱ	Q16836.
KOⁱ	K00022.
PhylomeDBⁱ	Q16836.
TreeFamⁱ	TF300886.

Enzyme and pathway databases

UniPathwayⁱ	UPA00659.
BioCycⁱ	MetaCyc:HS06563-MONOMER.
BRENDAⁱ	1.1.1.35. 2681.
Reactomeⁱ	R-HSA-77310. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA. R-HSA-77346. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA. R-HSA-77348. Beta oxidation of octanoyl-CoA to hexanoyl-CoA. R-HSA-77350. Beta oxidation of hexanoyl-CoA to butanoyl-CoA. R-HSA-77352. Beta oxidation of butanoyl-CoA to acetyl-CoA.
SABIO-RK	Q16836.

Miscellaneous databases

ChiTaRSⁱ	HADH. human.
EvolutionaryTraceⁱ	Q16836.
GeneWikiⁱ	Hydroxyacyl-Coenzyme_A_dehydrogenase.
GenomeRNAiⁱ	3033.
PROⁱ	Q16836.
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000138796.
CleanExⁱ	HS_HADH.
ExpressionAtlasⁱ	Q16836. baseline and differential.
Genevisibleⁱ	Q16836. HS.

Family and domain databases

Gene3Dⁱ	1.10.1040.10. 1 hit. 3.40.50.720. 1 hit.
InterProⁱ	IPR022694. 3-OHacyl-CoA_DH. IPR006180. 3-OHacyl-CoA_DH_CS. IPR006176. 3-OHacyl-CoA_DH_NAD-bd. IPR006108. 3HC_DH_C. IPR008927. 6-PGluconate_DH_C-like. IPR013328. 6PGD_dom_2. IPR016040. NAD(P)-bd_dom. [Graphical view]
Pfamⁱ	PF00725. 3HCDH. 1 hit. PF02737. 3HCDH_N. 1 hit. [Graphical view]
PIRSFⁱ	PIRSF000105. HCDH. 1 hit.
SUPFAMⁱ	SSF48179. SSF48179. 1 hit. SSF51735. SSF51735. 1 hit.
PROSITEⁱ	PS00067. 3HCDH. 1 hit. [Graphical view]
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ

HCDH_HUMAN

Accessionⁱ

Primary (citable) accession number: Q16836
Secondary accession number(s): J3KQ17

Q4W5B4

Entry historyⁱ

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 2, 2010
Last modified:	September 7, 2016
This is version 183 of the entry and version 3 of the sequence. [Complete history]

Entry statusⁱ

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

Human chromosome 4
Human chromosome 4: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PATHWAY comments
Index of metabolic and biosynthesis pathways
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families

Similar proteinsⁱ

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:

100%	UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%	UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%	UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

UniProtKB

UniParc

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UniRef

Proteomes

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Supporting data

UniProtKB - Q16836 (HCDH_HUMAN)

UniProt

Q16836 - HCDH_HUMAN

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Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial

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<p>Provides any useful information about the protein, mostly biological knowledge.</p><p><a href='../manual/function_section' target='_top'>More...</a></p>Functioni

<p>Describes the metabolic pathway(s) associated with a protein.</p><p><a href='../manual/pathway' target='_top'>More...</a></p>Pathwayi: fatty acid beta-oxidation

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

Chemistry

<p>Provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.</p><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>Provides information on the location and the topology of the mature protein in the cell.</p><p><a href='../manual/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>Provides information on the disease(s) and phenotype(s) associated with a protein.</p><p><a href='../manual/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Organism-specific databases

Polymorphism and mutation databases

<p>Describes post-translational modifications (PTMs) and/or processing events.</p><p><a href='../manual/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

2D gel databases

PTM databases

<p>Provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.</p><p><a href='../manual/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>Provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.</p><p><a href='../manual/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>Provides information on the tertiary and secondary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>Provides information on sequence similarities with other proteins and the domain(s) present in a protein.</p><p><a href='../manual/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>Displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequences (3)i

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

<p>Is used to point to information related to entries and found in data collections other than UniProtKB.</p><p><a href='../manual/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry

PTM databases

Polymorphism and mutation databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>Contains any relevant information that doesn’t fit in any other defined sections</p><p><a href='../manual/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

Pathwayⁱ: fatty acid beta-oxidation

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequences (3)ⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ