[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=4019459 [NCBI, ExPASy, EBI, Israel, Japan] Osumi T., Ishii N., Hijikata M., Kamijo K., Ozasa H., Furuta S., Miyazawa S., Kondo K., Inoue K., Kagamiyama H., Hashimoto T.; "Molecular cloning and nucleotide sequence of the cDNA for rat peroxisomal enoyl-CoA: hydratase-3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme."; J. Biol. Chem. 260:8905-8910(1985).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Liver; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24. PubMed=3036802 [NCBI, ExPASy, EBI, Israel, Japan] Ishii N., Hijikata M., Osumi T., Hashimoto T.; "Structural organization of the gene for rat enoyl-CoA hydratase:3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme."; J. Biol. Chem. 262:8144-8150(1987).
[4]	PROTEIN SEQUENCE OF 260-265; 294-302; 520-531 AND 710-719. PubMed=8856068 [NCBI, ExPASy, EBI, Israel, Japan] Dieuaide-Noubhani M., Novikov D., Baumgart E., Vanhooren J.C., Fransen M., Goethals M., Vandekerckhove J., Van Veldhoven P.P., Mannaerts G.P.; "Further characterization of the peroxisomal 3-hydroxyacyl-CoA dehydrogenases from rat liver. Relationship between the different dehydrogenases and evidence that fatty acids and the C27 bile acids di- and tri-hydroxycoprostanic acids are metabolized by separate multifunctional proteins."; Eur. J. Biochem. 240:660-666(1996).
[5]	FUNCTION AS AN ISOMERASE. PubMed=2303409 [NCBI, ExPASy, EBI, Israel, Japan] Palosaari P.M., Hiltunen J.K.; "Peroxisomal bifunctional protein from rat liver is a trifunctional enzyme possessing 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and delta 3, delta 2-enoyl-CoA isomerase activities."; J. Biol. Chem. 265:2446-2449(1990).
[6]	X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 260-722, AND SUBUNIT. DOI=10.1016/j.jmb.2005.10.085; PubMed=16330050 [NCBI, ExPASy, EBI, Israel, Japan] Taskinen J.P., Kiema T.R., Hiltunen J.K., Wierenga R.K.; "Structural studies of MFE-1: the 1.9 A crystal structure of the dehydrogenase part of rat peroxisomal MFE-1."; J. Mol. Biol. 355:734-746(2006).

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.
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

K03249; AAA41825.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC089777; AAH89777.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J02748; AAA41826.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A23575; DWRTEP.

NP_598290.1; -.

3D structure databases

PDB

1ZCJ; X-ray; 1.90 A; A=260-722.

[ExPASy / RCSB / EBI]

PDBsum

1ZCJ; -.

ModBase

P07896.

Organism-specific databases

RGD

621441; Ehhadh.

Gene expression databases

ArrayExpress

P07896; -.

GermOnline

ENSRNOG00000001770; Rattus norvegicus.

Ontologies

GO:0005777;	Cellular component: peroxisome (inferred from direct assay from HGNC).
GO:0003857;	Molecular function: 3-hydroxyacyl-CoA dehydrogenase activity (inferred from electronic annotation from EC).
GO:0050662;	Molecular function: coenzyme binding (inferred from electronic annotation from InterPro).
GO:0004165;	Molecular function: dodecenoyl-CoA delta-isomerase activity (inferred from electronic annotation from EC).
GO:0004300;	Molecular function: enoyl-CoA hydratase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.

Proteomics databases

PRIDE

P07896; -.

Genome annotation databases

Ensembl

ENSRNOG00000001770; Rattus norvegicus. [Contig view]

GeneID

171142; -.

KEGG

rno:171142; -.

NMPDR

fig|10116.3.peg.7563; -.

Phylogenomic databases

HOVERGEN

P07896; -.

Other

621936; -.

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

Keywords

3D-structure; Acetylation; Direct protein sequencing; Fatty acid metabolism; Isomerase; Lipid metabolism; Lyase; Multifunctional enzyme; NAD; Oxidoreductase; Peroxisome.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 722`	`721`	`Peroxisomal bifunctional enzyme.`	`PRO_0000109249`
`REGION`	`2 281`	`280`	`Enoyl-CoA hydratase / isomerase.`
`REGION`	`282 571`	`290`	`3-hydroxyacyl-CoA dehydrogenase.`
`MOTIF`	`720 722`	`3`	`Microbody targeting signal.`
`BINDING`	`100 100`		`Substrate; via amide nitrogen (By similarity).`
`SITE`	`123 123`	`1`	`Important for catalytic activity (By similarity).`
`MOD_RES`	`2 2`		`Blocked amino end (Ala).`
`MOD_RES`	`241 241`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`330 330`		`N6-acetyllysine (By similarity).`
`HELIX`	`262 272`	`11`
`HELIX`	`273 278`	`6`
`TURN`	`288 290`	`3`
`STRAND`	`298 302`	`5`
`HELIX`	`306 316`	`11`
`TURN`	`317 319`	`3`
`STRAND`	`321 325`	`5`
`HELIX`	`329 352`	`24`
`STRAND`	`362 366`	`5`
`HELIX`	`368 371`	`4`
`STRAND`	`375 379`	`5`
`HELIX`	`385 398`	`14`
`STRAND`	`404 407`	`4`
`STRAND`	`410 412`	`3`
`HELIX`	`414 418`	`5`
`HELIX`	`424 426`	`3`
`STRAND`	`427 432`	`6`
`TURN`	`436 438`	`3`
`STRAND`	`441 446`	`6`
`HELIX`	`452 464`	`13`
`STRAND`	`468 472`	`5`
`TURN`	`476 479`	`4`
`HELIX`	`480 496`	`17`
`HELIX`	`501 511`	`11`
`HELIX`	`517 524`	`8`
`HELIX`	`526 535`	`10`
`STRAND`	`538 541`	`4`
`HELIX`	`560 566`	`7`
`TURN`	`572 575`	`4`
`STRAND`	`576 583`	`8`
`STRAND`	`589 591`	`3`
`HELIX`	`593 605`	`13`
`HELIX`	`615 635`	`21`
`STRAND`	`638 640`	`3`
`HELIX`	`642 652`	`11`
`HELIX`	`657 659`	`3`
`HELIX`	`662 669`	`8`
`HELIX`	`671 684`	`14`
`HELIX`	`689 691`	`3`
`HELIX`	`695 702`	`8`
`HELIX`	`708 710`	`3`
`HELIX`	`711 715`	`5`

Sequence information

Length: 722 AA [This is the length of the unprocessed precursor]

Molecular weight: 78658 Da [This is the MW of the unprocessed precursor]

CRC64: 76ACC709C5F23E86 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAEYLRLPHS LAMIRLCNPP VNAVSPTVIR EVRNGLQKAG SDHTVKAIVI CGANGNFCAG 

        70         80         90        100        110        120 
ADIHGFSAFT PGLALGSLVD EIQRYQKPVL AAIQGVALGG GLELALGCHY RIANAKARVG 

       130        140        150        160        170        180 
LPEVTLGILP GARGTQLLPR VVGVPVALDL ITSGKYLSAD EALRLGILDA VVKSDPVEEA 

       190        200        210        220        230        240 
IKFAQKIIDK PIEPRRIFNK PVPSLPNMDS VFAEAIAKVR KQYPGVLAPE TCVRSIQASV 

       250        260        270        280        290        300 
KHPYEVGIKE EEKLFMYLRA SGQAKALQYA FFAEKSANKW STPSGASWKT ASAQPVSSVG 

       310        320        330        340        350        360 
VLGLGTMGRG IAISFARVGI SVVAVESDPK QLDAAKKIIT FTLEKEASRA HQNGQASAKP 

       370        380        390        400        410        420 
KLRFSSSTKE LSTVDLVVEA VFEDMNLKKK VFAELSALCK PGAFLCTNTS ALNVDDIASS 

       430        440        450        460        470        480 
TDRPQLVIGT HFFSPAHVMR LLEVIPSRYS SPTTIATVMS LSKKIGKIGV VVGNCYGFVG 

       490        500        510        520        530        540 
NRMLAPYYNQ GFFLLEEGSK PEDVDGVLEE FGFKMGPFRV SDLAGLDVGW KIRKGQGLTG 

       550        560        570        580        590        600 
PSLPPGTPVR KRGNSRYSPL GDMLCEAGRF GQKTGKGWYQ YDKPLGRIHK PDPWLSTFLS 

       610        620        630        640        650        660 
QYREVHHIEQ RTISKEEILE RCLYSLINEA FRILEEGMAA RPEHIDVIYL HGYGWPRHKG 

       670        680        690        700        710        720 
GPMFYAASVG LPTVLEKLQK YYRQNPDIPQ LEPSDYLRRL VAQGSPPLKE WQSLAGPHGS 


KL

P07896 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