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Reviewed, UniProtKB/Swiss-Prot Q9DBM2 (ECHP_MOUSE)

Last modified February 9, 2010. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length718 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 718717Peroxisomal bifunctional enzyme
PRO_0000109248

Regions

Region2 – 280279Enoyl-CoA hydratase / isomerase
Region281 – 5672873-hydroxyacyl-CoA dehydrogenase
Motif716 – 7183Microbody targeting signal

Sites

Site1021Important for catalytic activity By similarity
Site1221Important for catalytic activity By similarity

Amino acid modifications

Modified residue2401N6-acetyllysine Ref.2
Modified residue3291N6-acetyllysine Ref.2
Modified residue5791N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9DBM2-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 8827B352265EC739

FASTA71878,243
        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 

« 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: 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.
IPIIPI00554834.
RefSeqNP_076226.2.
UniGeneMm.28100

3D structure databases

SMRQ9DBM2. Positions 7-701, 260-714.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9DBM2.

PTM databases

PhosphoSiteQ9DBM2.

Proteomic databases

PRIDEQ9DBM2.

Genome annotation databases

EnsemblENSMUST00000023559; ENSMUSP00000023559; ENSMUSG00000022853; Mus musculus. [Genome view]
GeneID74147.
KEGGmmu:74147.

Organism-specific databases

CTD74147.
MGIMGI:1277964. Ehhadh.

Phylogenomic databases

HOGENOMHBG691737.
HOVERGENQ9DBM2.
InParanoidQ9DBM2.
PhylomeDBQ9DBM2.

Enzyme and pathway databases

BRENDA1.1.1.35. 244.
4.2.1.17. 244.
5.3.3.8. 244.

Gene expression databases

ArrayExpressQ9DBM2.
BgeeQ9DBM2.
GenevestigatorQ9DBM2.
GermOnlineENSMUSG00000022853. Mus musculus.

Family and domain databases

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.
IPR013328. DH_multihelical.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
G3DSA:1.10.1040.10. Opine_DH. 2 hits.
PfamPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
PROSITEPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

Entry information

Entry nameECHP_MOUSE
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents