Reviewed, UniProtKB/Swiss-Prot Q9DBM2 (ECHP_MOUSE)

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

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	718 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 By similarity.
Subcellular location	Peroxisome By similarity.
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	Multifunctional enzyme
Gene Ontology (GO)
Biological process	acyl-CoA metabolic process Traceable author statement. Source: MGI fatty acid beta-oxidation Inferred from mutant phenotype. Source: MGI oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from direct assay. Source: MGI peroxisome Traceable author statement. Source: MGI
Molecular function	3-hydroxyacyl-CoA dehydrogenase activity Traceable author statement. Source: MGI 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 By similarity
	Chain	2 – 718	717	Peroxisomal bifunctional enzyme		PRO_0000109248
Regions
	Region	2 – 280	279	Enoyl-CoA hydratase / isomerase
	Region	281 – 567	287	3-hydroxyacyl-CoA dehydrogenase
	Motif	716 – 718	3	Microbody targeting signal
Sites
	Site	102	1	Important for catalytic activity By similarity
	Site	122	1	Important for catalytic activity By similarity
Amino acid modifications
	Modified residue	240	1	N6-acetyllysine Ref.2
	Modified residue	329	1	N6-acetyllysine Ref.2
	Modified residue	579	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9DBM2-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 8827B352265EC739	FASTA	718	78,243
	10 20 30 40 50 60 MAEYLRLPHS LAMIRLCNPP VNAISPTVIT EVRNGLQKAS LDHTVRAIVI CGANDNFCAG 70 80 90 100 110 120 ADIHGFKSPT GLTLGSLVDE IQRYQKPVVA AIQGVALGGG LELALGCHYR IANAKARVGF 130 140 150 160 170 180 PEVMLGILPG ARGTQLLPRV VGVPVALDLI TSGRHISTDE ALKLGILDVV VKSDPVEEAI 190 200 210 220 230 240 KFAQTVIGKP IEPRRILNKP VPSLPNMDSV FAEAIAKVRK QYPGRLAPET CVRSVQASVK 250 260 270 280 290 300 HPYEVAIKEE AKLFMYLRGS GQARALQYAF FAEKSANKWS TPSGASWKTA SAQPVSSVGV 310 320 330 340 350 360 LGLGTMGRGI AISFARVGIP VVAVESDPKQ LDTAKKIITS TLEKEASKSG QASAKPNLRF 370 380 390 400 410 420 SSSTKELSSV DLVIEAVFED MNLKKKVFAE LSALCKPGAF LCTNTSALDV DDIASSTDRP 430 440 450 460 470 480 QLVIGTHFFS PAHIMRLLEV IPSRYSSPTT IATVMSLSKR IGKIGVVVGN CYGFVGNRML 490 500 510 520 530 540 APYYNQGYFL IEEGSKPEGV DGVLEEFGFR MGPFRVSDLA GLDVGWKVRK GQGLTGPSLP 550 560 570 580 590 600 PGTPTRKRGN TRYSPIADML CEAGRFGQKT GKGWYQYDKP LGRIHKPDPW LSEFLSQYRE 610 620 630 640 650 660 THHIKQRSIS KEEILERCLY SLINEAFRIL EEGMAASPEH IDVIYLHGYG WPRHVGGPMY 670 680 690 700 710 YAASVGLPTV LEKLQKYYRQ NPDIPQLEPS DYLRRLVAQG SPPLKEWQSL AGPHSSKL

References

[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Liver.
[2]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-240 AND LYS-329, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK004867 mRNA. Translation: BAB23628.1.
IPI	IPI00554834.
RefSeq	NP_076226.2.
UniGene	Mm.28100
3D structure databases
SMR	Q9DBM2. Positions 7-701, 260-714.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9DBM2.
PTM databases
PhosphoSite	Q9DBM2.
Proteomic databases
PRIDE	Q9DBM2.
Genome annotation databases
Ensembl	ENSMUST00000023559; ENSMUSP00000023559; ENSMUSG00000022853; Mus musculus. [Genome view]
GeneID	74147.
KEGG	mmu:74147.
Organism-specific databases
CTD	74147.
MGI	MGI:1277964. Ehhadh.
Phylogenomic databases
HOGENOM	HBG691737.
HOVERGEN	Q9DBM2.
InParanoid	Q9DBM2.
PhylomeDB	Q9DBM2.
Enzyme and pathway databases
BRENDA	1.1.1.35. 244. 4.2.1.17. 244. 5.3.3.8. 244.
Gene expression databases
ArrayExpress	Q9DBM2.
Bgee	Q9DBM2.
Genevestigator	Q9DBM2.
GermOnline	ENSMUSG00000022853. Mus musculus.
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
SOURCE	Search...

Entry information

Entry name

ECHP_MOUSE

Accession

Primary (citable) accession number: Q9DBM2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 24, 2001
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 86 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)