UniProt Accession

 ECHP_MOUSE; Q9DBM2; Q91W49 

Genbank Protein ID

 AK004867; BC016899; CH466521 

Genbank Nucleotide ID

 BAB23628.1; AAH16899.1; EDK97607.1 

Protein Name

 Peroxisomal bifunctional enzyme 

Protein Synonyms/Alias

 PBE; PBFE; Enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase; 3-hydroxyacyl-CoA dehydrogenase 

Gene Name

 Ehhadh 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
38	EVRNGLQKASLDHTV	acetylation	[1, 2, 3]
38	EVRNGLQKASLDHTV	succinylation	[2]
38	EVRNGLQKASLDHTV	ubiquitination	[4]
163	ISTDEALKLGILDVV	acetylation	[2, 5]
163	ISTDEALKLGILDVV	succinylation	[2]
163	ISTDEALKLGILDVV	ubiquitination	[4]
172	GILDVVVKSDPVEEA	acetylation	[2, 5, 6]
172	GILDVVVKSDPVEEA	succinylation	[2]
172	GILDVVVKSDPVEEA	ubiquitination	[4]
181	DPVEEAIKFAQTVIG	acetylation	[2, 5]
181	DPVEEAIKFAQTVIG	succinylation	[2]
189	FAQTVIGKPIEPRRI	acetylation	[1, 2, 3, 5, 6, 7]
189	FAQTVIGKPIEPRRI	succinylation	[2]
189	FAQTVIGKPIEPRRI	ubiquitination	[4]
217	VFAEAIAKVRKQYPG	acetylation	[2, 3, 5]
217	VFAEAIAKVRKQYPG	succinylation	[2]
240	RSVQASVKHPYEVAI	acetylation	[1, 2, 8]
240	RSVQASVKHPYEVAI	succinylation	[2]
248	HPYEVAIKEEAKLFM	acetylation	[1, 3, 5, 7]
248	HPYEVAIKEEAKLFM	ubiquitination	[4]
252	VAIKEEAKLFMYLRG	acetylation	[1, 2, 3]
252	VAIKEEAKLFMYLRG	succinylation	[2]
274	QYAFFAEKSANKWST	acetylation	[1, 2, 3, 5, 6, 7, 9]
274	QYAFFAEKSANKWST	succinylation	[2]
274	QYAFFAEKSANKWST	ubiquitination	[4]
278	FAEKSANKWSTPSGA	acetylation	[1, 2, 3, 5, 6]
278	FAEKSANKWSTPSGA	succinylation	[2]
278	FAEKSANKWSTPSGA	ubiquitination	[4]
288	TPSGASWKTASAQPV	acetylation	[2]
288	TPSGASWKTASAQPV	succinylation	[2]
329	VAVESDPKQLDTAKK	acetylation	[1, 2, 3, 6, 8]
329	VAVESDPKQLDTAKK	succinylation	[2]
329	VAVESDPKQLDTAKK	ubiquitination	[4]
335	PKQLDTAKKIITSTL	acetylation	[1, 3, 5]
336	KQLDTAKKIITSTLE	acetylation	[1, 5]
336	KQLDTAKKIITSTLE	ubiquitination	[4]
344	IITSTLEKEASKSGQ	acetylation	[1, 3, 5, 6, 7]
344	IITSTLEKEASKSGQ	ubiquitination	[4]
348	TLEKEASKSGQASAK	acetylation	[1, 2, 3, 5]
348	TLEKEASKSGQASAK	succinylation	[2]
348	TLEKEASKSGQASAK	ubiquitination	[4]
355	KSGQASAKPNLRFSS	acetylation	[1, 3, 5]
386	EDMNLKKKVFAELSA	acetylation	[2]
386	EDMNLKKKVFAELSA	succinylation	[2]
459	ATVMSLSKRIGKIGV	acetylation	[1, 3, 5]
459	ATVMSLSKRIGKIGV	ubiquitination	[4]
463	SLSKRIGKIGVVVGN	ubiquitination	[4]
527	AGLDVGWKVRKGQGL	acetylation	[1, 2, 3, 5]
527	AGLDVGWKVRKGQGL	succinylation	[2]
527	AGLDVGWKVRKGQGL	ubiquitination	[4]
569	EAGRFGQKTGKGWYQ	acetylation	[3]
572	RFGQKTGKGWYQYDK	acetylation	[2]
572	RFGQKTGKGWYQYDK	succinylation	[2]
572	RFGQKTGKGWYQYDK	ubiquitination	[4]
579	KGWYQYDKPLGRIHK	acetylation	[1, 2, 3, 5, 6, 7, 10]
579	KGWYQYDKPLGRIHK	succinylation	[2]
579	KGWYQYDKPLGRIHK	ubiquitination	[4]
586	KPLGRIHKPDPWLSE	acetylation	[1, 2, 3, 5]
586	KPLGRIHKPDPWLSE	succinylation	[2]
605	YRETHHIKQRSISKE	acetylation	[1, 3]
611	IKQRSISKEEILERC	acetylation	[1, 2, 3]
611	IKQRSISKEEILERC	succinylation	[2]
673	GLPTVLEKLQKYYRQ	acetylation	[3]
676	TVLEKLQKYYRQNPD	acetylation	[1]
705	AQGSPPLKEWQSLAG	acetylation	[2, 3, 5]
705	AQGSPPLKEWQSLAG	succinylation	[2]
717	LAGPHSSKL******	acetylation	[2]
717	LAGPHSSKL******	succinylation	[2]

Reference

 [1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [3] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [4] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [5] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [6] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [7] Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice.
 Fritz KS, Galligan JJ, Hirschey MD, Verdin E, Petersen DR.
 J Proteome Res. 2012 Mar 2;11(3):1633-43. [PMID: 22309199]
 [8] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [9] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
 [10] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379] 

Functional Description

  

Sequence Annotation

 REGION 1 280 Enoyl-CoA hydratase / isomerase.
 REGION 281 567 3-hydroxyacyl-CoA dehydrogenase.
 MOTIF 716 718 Microbody targeting signal (By
 BINDING 99 99 Substrate; via amide nitrogen (By
 MOD_RES 163 163 N6-acetyllysine (By similarity).
 MOD_RES 240 240 N6-acetyllysine.
 MOD_RES 329 329 N6-acetyllysine.
 MOD_RES 344 344 N6-acetyllysine (By similarity).
 MOD_RES 579 579 N6-acetyllysine (By similarity).  

Keyword

 Acetylation; Complete proteome; Fatty acid metabolism; Isomerase; Lipid metabolism; Lyase; Multifunctional enzyme; NAD; Oxidoreductase; Peroxisome; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 718 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; IEA:Compara.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0005777; C:peroxisome; TAS:MGI.
 GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; TAS:MGI.
 GO:0050662; F:coenzyme binding; IEA:InterPro.
 GO:0004165; F:dodecenoyl-CoA delta-isomerase activity; IEA:EC.
 GO:0004300; F:enoyl-CoA hydratase activity; IEA:EC.
 GO:0006637; P:acyl-CoA metabolic process; TAS:MGI.
 GO:0006635; P:fatty acid beta-oxidation; IMP:MGI.
 GO:0006475; P:internal protein amino acid acetylation; ISS:UniProtKB. 

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_superfam.
 IPR013328; DH_multihelical.
 IPR018376; Enoyl-CoA_hyd/isom_CS.
 IPR016040; NAD(P)-bd_dom. 

Pfam

 PF00725; 3HCDH
 PF02737; 3HCDH_N
 PF00378; ECH 

SMART

  

PROSITE

 PS00067; 3HCDH
 PS00166; ENOYL_COA_HYDRATASE 

PRINTS