[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; DOI=10.1006/geno.1994.1013; PubMed=8188243 [NCBI, ExPASy, EBI, Israel, Japan] Hoefler G., Forstner M., McGuinness M.C., Hulla W., Hiden M., Krisper P., Kenner L., Ried T., Lengauer C., Zechner R., Moser H.W., Chen G.L.; "cDNA cloning of the human peroxisomal enoyl-CoA hydratase: 3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme and localization to chromosome 3q26.3-3q28: a free left Alu Arm is inserted in the 3' noncoding region."; Genomics 19:60-67(1994).
[2]	NUCLEOTIDE SEQUENCE [MRNA] OF 502-723. TISSUE=Liver; DOI=10.1016/0006-291X(91)91003-U; PubMed=1651711 [NCBI, ExPASy, EBI, Israel, Japan] Chen G.L., Balfe A., Erwa W., Hoefler G., Gaertner J., Aikawa J., Chen W.W.; "Import of human bifunctional enzyme into peroxisomes of human hepatoma cells in vitro."; Biochem. Biophys. Res. Commun. 178:1084-1091(1991).
[3]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan] Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; "Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).

Comments

CATALYTIC ACTIVITY: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H₂O.
CATALYTIC ACTIVITY: (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA.
CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD⁺ = 3-oxoacyl-CoA + NADH.
PATHWAY: Lipid metabolism; fatty acid beta-oxidation .
SUBUNIT: Monomer.
SUBCELLULAR LOCATION: Peroxisome.
TISSUE SPECIFICITY: Liver and kidney. Lower amounts seen in the brain.
DISEASE: Absent in patients suffering with peroxisomal disorders such as Zellweger syndrome, neonatal adrenoleukodystrophy and infantile Refsum disease.
SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.
SIMILARITY: In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L07077; AAA53289.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S50245; AAB19482.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A49613; A49613.

UniGene

Hs.429879

3D structure databases

HSSP

P14604; 1MJ3. [HSSP ENTRY / PDB]

Q08426; 262-717.

PTM databases

Q08426; -.

Organism-specific databases

HGNC:3247; EHHADH.

607037; gene. [NCBI / EBI]

Orphanet

50812; Zellweger-like syndrome, without peroxisomal anomalies.

PharmGKB

PA27682; -.

GeneCards

Q08426.

Gene expression databases

ArrayExpress

Q08426; -.

CleanEx

HS_EHHADH; -.

GermOnline

ENSG00000113790; Homo sapiens.

Ontologies

GO:0005777;	Cellular component: peroxisome (traceable author statement from ProtInc).
GO:0003857;	Molecular function: 3-hydroxyacyl-CoA dehydrogenase activity (traceable author statement from ProtInc).
GO:0004300;	Molecular function: enoyl-CoA hydratase activity (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR006180; 3-OHacyl-CoA_DHase_CS.
IPR006176; 3-OHacyl-CoA_DHase_NAD-bd.
IPR006108; 3HC_DHase_C.
IPR001753; Crotonase_core.
IPR013328; DHase_multihelical.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:1.10.1040.10; Opine_DH; 2.

Pfam

PF00725; 3HCDH; 1.
PF02737; 3HCDH_N; 1.
PF00378; ECH; 1.
Pfam graphical view of domain structure.

PROSITE

PS00067; 3HCDH; 1.
PS00166; ENOYL_COA_HYDRATASE; 1.

Genome annotation databases

Ensembl

ENSG00000113790; Homo sapiens. [Contig view]

Phylogenomic databases

HOGENOM

Q08426; -.

HOVERGEN

Q08426; -.

Other

DrugBank

DB00157; NADH.

SOURCE

EHHADH; Homo sapiens.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Fatty acid metabolism; Isomerase; Lipid metabolism; Lyase; Multifunctional enzyme; NAD; Oxidoreductase; Peroxisome; Phosphoprotein; Polymorphism.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 723`	`722`	`Peroxisomal bifunctional enzyme.`	`PRO_0000109247`
`REGION`	`2 282`	`281`	`Enoyl-CoA hydratase / isomerase.`
`REGION`	`283 572`	`290`	`3-hydroxyacyl-CoA dehydrogenase.`
`MOTIF`	`721 723`	`3`	`Microbody targeting signal.`
`BINDING`	`101 101`		`Substrate; via amide nitrogen (By similarity).`
`SITE`	`124 124`	`1`	`Important for catalytic activity (By similarity).`
`MOD_RES`	`359 359`		`Phosphoserine.`
`VARIANT`	`75 75`	`1`	`I -> T (in dbSNP:rs1062553 [NCBI]).`	`VAR_047132`
`VARIANT`	`274 274`	`1`	`A -> T (in dbSNP:rs2302819 [NCBI]).`	`VAR_047133 [3D]`
`VARIANT`	`606 606`	`1`	`P -> T (in dbSNP:rs1042438 [NCBI]).`	`VAR_047134 [3D]`
`VARIANT`	`685 685`	`1`	`Q -> K (in dbSNP:rs11919970 [NCBI]).`	`VAR_047135 [3D]`
`VARIANT`	`715 715`	`1`	`L -> S (in dbSNP:rs11927618 [NCBI]).`	`VAR_047136 [3D]`

Sequence information

Length: 723 AA [This is the length of the unprocessed precursor]

Molecular weight: 79340 Da [This is the MW of the unprocessed precursor]

CRC64: EF461DA96346DB65 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAEYTRLHNA LALIRLRNPP VNAISTTLLR DIKEGLQKAG RDHTIKAIVI CGAEGKFSAG 

        70         80         90        100        110        120 
ADIRGFSAPR TFGLILGHVV DEIQRNEKPV VAAIQGMAFG GGLELALGCH YRIAHADAQV 

       130        140        150        160        170        180 
GLPEVTLGLL PGARGTQLLP RLTGVPAALD LITSGRRILA DEALKLGILD KVVNSDPVEE 

       190        200        210        220        230        240 
AIRFAQRVSD QPLESRRLCN KPIQSLPNMD SIFSEALLKM RRQHPGCLAQ EACVRAVQAA 

       250        260        270        280        290        300 
VQYPYEVGIK KEEELFLYLL QSGQARALQY AFFAERKANK WSTPSGASWK TASARPVSSV 

       310        320        330        340        350        360 
GVVGLGTMGR GIVISFARAR IPVIGVDSDK NQLATANKMI TSVLEKEASK MQQSGHPWSG 

       370        380        390        400        410        420 
PKPRLTSSVK ELGGVDLVIE AVFEEMSLKK QVFAELSAVC KPEAFLCTNT SALDVDEIAS 

       430        440        450        460        470        480 
STDRPHLVIG THFFSPAHVM KLLEVIPSQY SSPTTIATVM NLSKKIKKIG VVVGNCFGFV 

       490        500        510        520        530        540 
GNRMLNPYYN QAYFLLEEGS KPEEVDQVLE EFGFKMGPFR VSDLAGLDVG WKSRKGQGLT 

       550        560        570        580        590        600 
GPTLLPGTPA RKRGNRRYCP IPDVLCELGR FGQKTGKGWY QYDKPLGRIH KPDPWLSTFL 

       610        620        630        640        650        660 
SRYRKPHHIE PRTISQDEIL ERCLYSLINE AFRILGEGIA ASPEHIDVVY LHGYGCARHK 

       670        680        690        700        710        720 
GGPMFYASTV GLPTVLEKLQ KYYRQNPDIP QLEPSDYLKK LASQGNPPLK EWQSLAGSPS 


SKL

Q08426 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools