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Q9DBM2 (ECHP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxisomal bifunctional enzyme

Short name=PBE
Short name=PBFE

Including the following 2 domains:

  1. Enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase
    EC=4.2.1.17
    EC=5.3.3.8
  2. 3-hydroxyacyl-CoA dehydrogenase
    EC=1.1.1.35
Gene names
Name:Ehhadh
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length718 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Enzyme regulation

Enzyme activity enhanced by acetylation By similarity.

Pathway

Lipid metabolism; fatty acid beta-oxidation.

Subunit structure

Monomer By similarity.

Subcellular location

Peroxisome By similarity.

Post-translational modification

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.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 718718Peroxisomal bifunctional enzyme
PRO_0000109248

Regions

Region1 – 280280Enoyl-CoA hydratase / isomerase
Region281 – 5672873-hydroxyacyl-CoA dehydrogenase
Motif716 – 7183Microbody targeting signal By similarity

Sites

Binding site991Substrate; via amide nitrogen By similarity
Site1021Important for catalytic activity By similarity
Site1221Important for catalytic activity By similarity

Amino acid modifications

Modified residue381N6-succinyllysine Ref.4
Modified residue1631N6-acetyllysine; alternate By similarity
Modified residue1631N6-succinyllysine; alternate Ref.4
Modified residue1721N6-acetyllysine; alternate Ref.5
Modified residue1721N6-succinyllysine; alternate Ref.4
Modified residue1811N6-succinyllysine Ref.4
Modified residue1891N6-acetyllysine; alternate Ref.5
Modified residue1891N6-succinyllysine; alternate Ref.4
Modified residue2171N6-acetyllysine; alternate Ref.5
Modified residue2171N6-succinyllysine; alternate Ref.4
Modified residue2401N6-succinyllysine Ref.4
Modified residue2481N6-acetyllysine Ref.5
Modified residue2521N6-succinyllysine Ref.4
Modified residue2741N6-acetyllysine; alternate Ref.5
Modified residue2741N6-succinyllysine; alternate Ref.4
Modified residue2781N6-succinyllysine Ref.4
Modified residue2881N6-succinyllysine Ref.4
Modified residue3291N6-succinyllysine Ref.4
Modified residue3441N6-acetyllysine Ref.5
Modified residue3481N6-acetyllysine Ref.5
Modified residue3551N6-acetyllysine Ref.5
Modified residue4591N6-acetyllysine Ref.5
Modified residue5271N6-succinyllysine Ref.4
Modified residue5721N6-succinyllysine Ref.4
Modified residue5791N6-acetyllysine; alternate Ref.5
Modified residue5791N6-succinyllysine; alternate Ref.4
Modified residue5861N6-acetyllysine; alternate Ref.5
Modified residue5861N6-succinyllysine; alternate Ref.4
Modified residue7051N6-acetyllysine; alternate Ref.5
Modified residue7051N6-succinyllysine; alternate Ref.4
Modified residue7171N6-succinyllysine Ref.4

Experimental info

Sequence conflict4991D → G in BAB23628. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9DBM2 [UniParc].

Last modified July 27, 2011. Version 4.
Checksum: A405717EC7A3EBD9

FASTA71878,301
        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 IEEGSKPEDV 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 

« Hide

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. expand/collapse author list , 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]"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.
[5]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK004867 mRNA. Translation: BAB23628.1.
BC016899 mRNA. Translation: AAH16899.1.
CH466521 Genomic DNA. Translation: EDK97607.1.
RefSeqNP_076226.2. NM_023737.3.
UniGeneMm.28100.

3D structure databases

ProteinModelPortalQ9DBM2.
SMRQ9DBM2. Positions 1-714.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9DBM2. 5 interactions.
MINTMINT-4121269.

PTM databases

PhosphoSiteQ9DBM2.

Proteomic databases

PaxDbQ9DBM2.
PRIDEQ9DBM2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023559; ENSMUSP00000023559; ENSMUSG00000022853.
GeneID74147.
KEGGmmu:74147.
UCSCuc007yrm.2. mouse.

Organism-specific databases

CTD1962.
MGIMGI:1277964. Ehhadh.

Phylogenomic databases

eggNOGCOG1250.
GeneTreeENSGT00720000108673.
HOGENOMHOG000261347.
HOVERGENHBG104990.
InParanoidQ91W49.
KOK07514.
OMAKGWYQYD.
OrthoDBEOG725DH0.
TreeFamTF316708.

Enzyme and pathway databases

UniPathwayUPA00659.

Gene expression databases

BgeeQ9DBM2.
GenevestigatorQ9DBM2.

Family and domain databases

Gene3D1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
InterProIPR006180. 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.
[Graphical view]
PfamPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMSSF48179. SSF48179. 2 hits.
PROSITEPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio339902.
PROQ9DBM2.
SOURCESearch...

Entry information

Entry nameECHP_MOUSE
AccessionPrimary (citable) accession number: Q9DBM2
Secondary accession number(s): Q91W49
Entry history
Integrated into UniProtKB/Swiss-Prot: October 24, 2001
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 123 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot