Q9DBM2 (ECHP_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 114.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Peroxisomal bifunctional enzyme Short name=PBE Short name=PBFE | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) [Reference proteome] | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 718 AA. |
| Sequence status | Complete. |
| 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. |
| Enzyme regulation | Enzyme activity enhanced by acetylation By similarity. |
| Pathway | |
| 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. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 718 | 718 | Peroxisomal bifunctional enzyme | PRO_0000109248 | |||||
Regions | |||||||||
| Region | 1 – 280 | 280 | Enoyl-CoA hydratase / isomerase | ||||||
| Region | 281 – 567 | 287 | 3-hydroxyacyl-CoA dehydrogenase | ||||||
| Motif | 716 – 718 | 3 | Microbody targeting signal By similarity | ||||||
Sites | |||||||||
| Binding site | 99 | 1 | Substrate; via amide nitrogen By similarity | ||||||
| Site | 102 | 1 | Important for catalytic activity By similarity | ||||||
| Site | 122 | 1 | Important for catalytic activity By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 163 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 240 | 1 | N6-acetyllysine Ref.4 | ||||||
| Modified residue | 329 | 1 | N6-acetyllysine Ref.4 | ||||||
| Modified residue | 344 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 579 | 1 | N6-acetyllysine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 499 | 1 | D → G in BAB23628. Ref.1 | ||||||
Sequences
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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. 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] | "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] [Europe PMC] [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. BC016899 mRNA. Translation: AAH16899.1. CH466521 Genomic DNA. Translation: EDK97607.1. |
| IPI | IPI00554834. |
| RefSeq | NP_076226.2. NM_023737.3. |
| UniGene | Mm.28100. |
3D structure databases | |
| ProteinModelPortal | Q9DBM2. |
| SMR | Q9DBM2. Positions 1-714. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | Q9DBM2. |
Proteomic databases | |
| PaxDb | Q9DBM2. |
| PRIDE | Q9DBM2. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000023559; ENSMUSP00000023559; ENSMUSG00000022853. |
| GeneID | 74147. |
| KEGG | mmu:74147. |
Organism-specific databases | |
| CTD | 1962. |
| MGI | MGI:1277964. Ehhadh. |
Phylogenomic databases | |
| eggNOG | COG1250. |
| GeneTree | ENSGT00700000104363. |
| HOGENOM | HOG000261347. |
| HOVERGEN | HBG104990. |
| InParanoid | Q91W49. |
| KO | K07514. |
| OMA | NYEAQVK. |
| OrthoDB | EOG47PX5F. |
Enzyme and pathway databases | |
| UniPathway | UPA00659. |
Gene expression databases | |
| ArrayExpress | Q9DBM2. |
| Bgee | Q9DBM2. |
| Genevestigator | Q9DBM2. |
| GermOnline | ENSMUSG00000022853. Mus musculus. |
Family and domain databases | |
| Gene3D | 1.10.1040.10. 2 hits. 3.40.50.720. 1 hit. |
| 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. [Graphical view] |
| Pfam | PF00725. 3HCDH. 2 hits. PF02737. 3HCDH_N. 1 hit. PF00378. ECH. 1 hit. [Graphical view] |
| SUPFAM | SSF48179. 6DGDH_C_like. 2 hits. |
| PROSITE | PS00067. 3HCDH. 1 hit. PS00166. ENOYL_COA_HYDRATASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 339902. |
| SOURCE | Search... |
Entry information
| Entry name | ECHP_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q9DBM2 Secondary accession number(s): Q91W49 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
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 |

Clusters with
