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Protein

Peroxisomal bifunctional enzyme

Gene

Ehhadh

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

(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.

Enzyme regulationi

Enzyme activity enhanced by acetylation.By similarity

Pathwayi: fatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei99 – 991Substrate; via amide nitrogenBy similarity
Sitei102 – 1021Important for catalytic activityBy similarity
Sitei122 – 1221Important for catalytic activityBy similarity

GO - Molecular functioni

GO - Biological processi

  • acyl-CoA metabolic process Source: MGI
  • fatty acid beta-oxidation Source: MGI
  • internal protein amino acid acetylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase, Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiR-MMU-390918. Peroxisomal lipid metabolism.
UniPathwayiUPA00659.

Chemistry

SwissLipidsiSLP:000000402.
SLP:000000491.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisomal bifunctional enzyme
Short name:
PBE
Short name:
PBFE
Including the following 2 domains:
Enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase (EC:4.2.1.17, EC:5.3.3.8)
3-hydroxyacyl-CoA dehydrogenase (EC:1.1.1.35)
Gene namesi
Name:Ehhadh
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1277964. Ehhadh.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Ensembl
  • mitochondrion Source: MGI
  • peroxisome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 718718Peroxisomal bifunctional enzymePRO_0000109248Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei38 – 381N6-succinyllysineCombined sources
Modified residuei163 – 1631N6-acetyllysine; alternateBy similarity
Modified residuei163 – 1631N6-succinyllysine; alternateCombined sources
Modified residuei172 – 1721N6-acetyllysine; alternateCombined sources
Modified residuei172 – 1721N6-succinyllysine; alternateCombined sources
Modified residuei181 – 1811N6-succinyllysineCombined sources
Modified residuei189 – 1891N6-acetyllysine; alternateCombined sources
Modified residuei189 – 1891N6-succinyllysine; alternateCombined sources
Modified residuei217 – 2171N6-acetyllysine; alternateCombined sources
Modified residuei217 – 2171N6-succinyllysine; alternateCombined sources
Modified residuei240 – 2401N6-succinyllysineCombined sources
Modified residuei248 – 2481N6-acetyllysineCombined sources
Modified residuei252 – 2521N6-succinyllysineCombined sources
Modified residuei274 – 2741N6-acetyllysine; alternateCombined sources
Modified residuei274 – 2741N6-succinyllysine; alternateCombined sources
Modified residuei278 – 2781N6-succinyllysineCombined sources
Modified residuei288 – 2881N6-succinyllysineCombined sources
Modified residuei329 – 3291N6-succinyllysineCombined sources
Modified residuei344 – 3441N6-acetyllysineCombined sources
Modified residuei348 – 3481N6-acetyllysineCombined sources
Modified residuei355 – 3551N6-acetyllysineCombined sources
Modified residuei459 – 4591N6-acetyllysineCombined sources
Modified residuei527 – 5271N6-succinyllysineCombined sources
Modified residuei543 – 5431PhosphothreonineCombined sources
Modified residuei572 – 5721N6-succinyllysineCombined sources
Modified residuei579 – 5791N6-acetyllysine; alternateCombined sources
Modified residuei579 – 5791N6-succinyllysine; alternateCombined sources
Modified residuei586 – 5861N6-acetyllysine; alternateCombined sources
Modified residuei586 – 5861N6-succinyllysine; alternateCombined sources
Modified residuei705 – 7051N6-acetyllysine; alternateCombined sources
Modified residuei705 – 7051N6-succinyllysine; alternateCombined sources
Modified residuei717 – 7171N6-succinyllysineCombined sources

Post-translational modificationi

Acetylated, leading to enhanced enzyme activity. Acetylation is enhanced by up to 80% after treatment either with trichostin A (TCA) or with nicotinamide (NAM) with highest increase on Lys-344. Acetylation and enzyme activity increased by about 1.5% on addition of fatty acids (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9DBM2.
MaxQBiQ9DBM2.
PaxDbiQ9DBM2.
PeptideAtlasiQ9DBM2.
PRIDEiQ9DBM2.

PTM databases

iPTMnetiQ9DBM2.
PhosphoSiteiQ9DBM2.
SwissPalmiQ9DBM2.

Expressioni

Gene expression databases

BgeeiQ9DBM2.
GenevisibleiQ9DBM2. MM.

Interactioni

Subunit structurei

Monomer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ9DBM2. 5 interactions.
MINTiMINT-4121269.
STRINGi10090.ENSMUSP00000023559.

Structurei

3D structure databases

ProteinModelPortaliQ9DBM2.
SMRiQ9DBM2. Positions 1-714.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 280280Enoyl-CoA hydratase / isomeraseAdd
BLAST
Regioni281 – 5672873-hydroxyacyl-CoA dehydrogenaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi716 – 7183Microbody targeting signalBy similarity

Sequence similaritiesi

In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.Curated
In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.Curated

Phylogenomic databases

eggNOGiKOG1683. Eukaryota.
COG1250. LUCA.
GeneTreeiENSGT00720000108673.
HOGENOMiHOG000261347.
HOVERGENiHBG104990.
InParanoidiQ9DBM2.
KOiK07514.
OMAiKEINHEY.
OrthoDBiEOG725DH0.
TreeFamiTF316708.

Family and domain databases

Gene3Di1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH_1. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF51735. SSF51735. 1 hit.
SSF52096. SSF52096. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9DBM2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEYLRLPHS LAMIRLCNPP VNAISPTVIT EVRNGLQKAS LDHTVRAIVI
60 70 80 90 100
CGANDNFCAG ADIHGFKSPT GLTLGSLVDE IQRYQKPVVA AIQGVALGGG
110 120 130 140 150
LELALGCHYR IANAKARVGF PEVMLGILPG ARGTQLLPRV VGVPVALDLI
160 170 180 190 200
TSGRHISTDE ALKLGILDVV VKSDPVEEAI KFAQTVIGKP IEPRRILNKP
210 220 230 240 250
VPSLPNMDSV FAEAIAKVRK QYPGRLAPET CVRSVQASVK HPYEVAIKEE
260 270 280 290 300
AKLFMYLRGS GQARALQYAF FAEKSANKWS TPSGASWKTA SAQPVSSVGV
310 320 330 340 350
LGLGTMGRGI AISFARVGIP VVAVESDPKQ LDTAKKIITS TLEKEASKSG
360 370 380 390 400
QASAKPNLRF SSSTKELSSV DLVIEAVFED MNLKKKVFAE LSALCKPGAF
410 420 430 440 450
LCTNTSALDV DDIASSTDRP QLVIGTHFFS PAHIMRLLEV IPSRYSSPTT
460 470 480 490 500
IATVMSLSKR IGKIGVVVGN CYGFVGNRML APYYNQGYFL IEEGSKPEDV
510 520 530 540 550
DGVLEEFGFR MGPFRVSDLA GLDVGWKVRK GQGLTGPSLP PGTPTRKRGN
560 570 580 590 600
TRYSPIADML CEAGRFGQKT GKGWYQYDKP LGRIHKPDPW LSEFLSQYRE
610 620 630 640 650
THHIKQRSIS KEEILERCLY SLINEAFRIL EEGMAASPEH IDVIYLHGYG
660 670 680 690 700
WPRHVGGPMY YAASVGLPTV LEKLQKYYRQ NPDIPQLEPS DYLRRLVAQG
710
SPPLKEWQSL AGPHSSKL
Length:718
Mass (Da):78,301
Last modified:July 27, 2011 - v4
Checksum:iA405717EC7A3EBD9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti499 – 4991D → G in BAB23628 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004867 mRNA. Translation: BAB23628.1.
BC016899 mRNA. Translation: AAH16899.1.
CH466521 Genomic DNA. Translation: EDK97607.1.
CCDSiCCDS28063.1.
RefSeqiNP_076226.2. NM_023737.3.
UniGeneiMm.28100.

Genome annotation databases

EnsembliENSMUST00000023559; ENSMUSP00000023559; ENSMUSG00000022853.
GeneIDi74147.
KEGGimmu:74147.
UCSCiuc007yrm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004867 mRNA. Translation: BAB23628.1.
BC016899 mRNA. Translation: AAH16899.1.
CH466521 Genomic DNA. Translation: EDK97607.1.
CCDSiCCDS28063.1.
RefSeqiNP_076226.2. NM_023737.3.
UniGeneiMm.28100.

3D structure databases

ProteinModelPortaliQ9DBM2.
SMRiQ9DBM2. Positions 1-714.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9DBM2. 5 interactions.
MINTiMINT-4121269.
STRINGi10090.ENSMUSP00000023559.

Chemistry

SwissLipidsiSLP:000000402.
SLP:000000491.

PTM databases

iPTMnetiQ9DBM2.
PhosphoSiteiQ9DBM2.
SwissPalmiQ9DBM2.

Proteomic databases

EPDiQ9DBM2.
MaxQBiQ9DBM2.
PaxDbiQ9DBM2.
PeptideAtlasiQ9DBM2.
PRIDEiQ9DBM2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023559; ENSMUSP00000023559; ENSMUSG00000022853.
GeneIDi74147.
KEGGimmu:74147.
UCSCiuc007yrm.2. mouse.

Organism-specific databases

CTDi1962.
MGIiMGI:1277964. Ehhadh.

Phylogenomic databases

eggNOGiKOG1683. Eukaryota.
COG1250. LUCA.
GeneTreeiENSGT00720000108673.
HOGENOMiHOG000261347.
HOVERGENiHBG104990.
InParanoidiQ9DBM2.
KOiK07514.
OMAiKEINHEY.
OrthoDBiEOG725DH0.
TreeFamiTF316708.

Enzyme and pathway databases

UniPathwayiUPA00659.
ReactomeiR-MMU-390918. Peroxisomal lipid metabolism.

Miscellaneous databases

PROiQ9DBM2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DBM2.
GenevisibleiQ9DBM2. MM.

Family and domain databases

Gene3Di1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH_1. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF51735. SSF51735. 1 hit.
SSF52096. SSF52096. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Kidney.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-543, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Liver, Lung and Pancreas.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-38; LYS-163; LYS-172; LYS-181; LYS-189; LYS-217; LYS-240; LYS-252; LYS-274; LYS-278; LYS-288; LYS-329; LYS-527; LYS-572; LYS-579; LYS-586; LYS-705 AND LYS-717, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-172; LYS-189; LYS-217; LYS-248; LYS-274; LYS-344; LYS-348; LYS-355; LYS-459; LYS-579; LYS-586 AND LYS-705, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiECHP_MOUSE
AccessioniPrimary (citable) accession number: Q9DBM2
Secondary accession number(s): Q91W49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2001
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 143 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.