Reviewed, UniProtKB/Swiss-Prot P07896 (ECHP_RAT)

Names and origin

Protein names

Recommended name:
    Peroxisomal bifunctional enzyme
      Short name=PBE
      Short name=PBFE
Including the following 2 domains:
    1- Recommended name:
            Enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase
              EC=4.2.1.17
              EC=5.3.3.8
    2- Recommended name:
            3-hydroxyacyl-CoA dehydrogenase
              EC=1.1.1.35

Gene names

Name:

Ehhadh

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	722 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O. (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA. (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.
Pathway	Lipid metabolism; fatty acid beta-oxidation.
Subunit structure	Monomer. Ref.6
Subcellular location	Peroxisome.
Sequence similarities	In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Peroxisome
Ligand	NAD
Molecular function	Isomerase Lyase Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing Multifunctional enzyme
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	peroxisome Inferred from direct assay. Source: HGNC
Molecular function	3-hydroxyacyl-CoA dehydrogenase activity Ref.1 Inferred from direct assay. Source: RGD coenzyme binding Inferred from electronic annotation. Source: InterPro dodecenoyl-CoA delta-isomerase activity Inferred from electronic annotation. Source: EC enoyl-CoA hydratase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 722

721

Peroxisomal bifunctional enzyme

PRO_0000109249

Regions

Region

2 – 281

280

Enoyl-CoA hydratase / isomerase

Region

282 – 571

290

3-hydroxyacyl-CoA dehydrogenase

Motif

720 – 722

3

Microbody targeting signal

Sites

Binding site

100

1

Substrate; via amide nitrogen By similarity

Site

123

1

Important for catalytic activity By similarity

Amino acid modifications

Modified residue

2

1

Blocked amino end (Ala)

Modified residue

241

1

N6-acetyllysine By similarity

Modified residue

330

1

N6-acetyllysine By similarity

Modified residue

583

1

N6-acetyllysine By similarity

Secondary structure

1

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722

Helix Strand Turn

Details...

Helix

262 – 272

11

Helix

273 – 278

6

Turn

288 – 290

3

Beta strand

298 – 302

5

Helix

306 – 316

11

Turn

317 – 319

3

Beta strand

321 – 325

5

Helix

329 – 352

24

Beta strand

362 – 366

5

Helix

368 – 371

4

Beta strand

375 – 379

5

Helix

385 – 398

14

Beta strand

404 – 407

4

Beta strand

410 – 412

3

Helix

414 – 418

5

Helix

424 – 426

3

Beta strand

427 – 432

6

Turn

436 – 438

3

Beta strand

441 – 446

6

Helix

452 – 464

13

Beta strand

468 – 472

5

Turn

476 – 479

4

Helix

480 – 496

17

Helix

501 – 511

11

Helix

517 – 524

8

Helix

526 – 535

10

Beta strand

538 – 541

4

Helix

560 – 566

7

Turn

572 – 575

4

Beta strand

576 – 583

8

Beta strand

589 – 591

3

Helix

593 – 605

13

Helix

615 – 635

21

Beta 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

Sequences

	Sequence		Length	Mass (Da)
	P07896-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 76ACC709C5F23E86	FASTA	722	78,658
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and nucleotide sequence of the cDNA for rat peroxisomal enoyl-CoA: hydratase-3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme." Osumi T., Ishii N., Hijikata M., Kamijo K., Ozasa H., Furuta S., Miyazawa S., Kondo K., Inoue K., Kagamiyama H., Hashimoto T. J. Biol. Chem. 260:8905-8910(1985) [PubMed: 4019459] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
[3]	"Structural organization of the gene for rat enoyl-CoA hydratase:3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme." Ishii N., Hijikata M., Osumi T., Hashimoto T. J. Biol. Chem. 262:8144-8150(1987) [PubMed: 3036802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
[4]	"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." Dieuaide-Noubhani M., Novikov D., Baumgart E., Vanhooren J.C., Fransen M., Goethals M., Vandekerckhove J., Van Veldhoven P.P., Mannaerts G.P. Eur. J. Biochem. 240:660-666(1996) [PubMed: 8856068] [Abstract] Cited for: PROTEIN SEQUENCE OF 260-265; 294-302; 520-531 AND 710-719.
[5]	"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." Palosaari P.M., Hiltunen J.K. J. Biol. Chem. 265:2446-2449(1990) [PubMed: 2303409] [Abstract] Cited for: FUNCTION AS AN ISOMERASE.
[6]	"Structural studies of MFE-1: the 1.9 A crystal structure of the dehydrogenase part of rat peroxisomal MFE-1." Taskinen J.P., Kiema T.R., Hiltunen J.K., Wierenga R.K. J. Mol. Biol. 355:734-746(2006) [PubMed: 16330050] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 260-722, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

K03249 mRNA. Translation: AAA41825.1.
BC089777 mRNA. Translation: AAH89777.1.
J02748 Genomic DNA. Translation: AAA41826.1.

IPI

IPI00232011.

PIR

DWRTEP. A23575.

RefSeq

NP_598290.1.

UniGene

Rn.3671

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZCJ	X-ray	1.90	A	260-722	[»]

SMR

P07896. Positions 7-705.

ModBase

Search...

Protein-protein interaction databases

STRING

P07896.

PTM databases

PhosphoSite

P07896.

Proteomic databases

PRIDE

P07896.

Genome annotation databases

Ensembl

ENSRNOT00000002410; ENSRNOP00000002410; ENSRNOG00000001770; Rattus norvegicus. [Genome view]

GeneID

171142.

KEGG

rno:171142.

NMPDR

fig|10116.3.peg.7563.

UCSC

NM_133606. rat.

Organism-specific databases

CTD

171142.

RGD

621441. Ehhadh.

Phylogenomic databases

eggNOG

roNOG09760.

HOVERGEN

P07896.

InParanoid

P07896.

OMA

PYYNQTY.

OrthoDB

EOG93JFQ9.

PhylomeDB

P07896.

Enzyme and pathway databases

BRENDA

1.1.1.35. 248.
4.2.1.17. 248.
5.3.3.8. 248.

Gene expression databases

ArrayExpress

P07896.

Genevestigator

P07896.

GermOnline

ENSRNOG00000001770. Rattus norvegicus.

Family and domain databases

InterPro

IPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR001753. Crotonase_core.
IPR013328. DH_multihelical.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Gene3D

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

Pfam

PF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]

PROSITE

PS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

621936.

Entry information

Entry name

ECHP_RAT

Accession

Primary (citable) accession number: P07896
Secondary accession number(s): Q5EBD2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	January 23, 2007
Last modified:	January 19, 2010
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)