Reviewed,
UniProtKB/Swiss-Prot Q08426 (ECHP_HUMAN)
Last modified
February 9, 2010.
Version 107.
History...
Clusters with 100%,
90%,
50% identity |
Documents (6) |
Third-party data |
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Names and origin
| Protein names | Recommended 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 |
| ||||
| Organism | Homo sapiens (Human) [Complete proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 723 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| 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. |
| Pathway | |
| Subunit structure | Monomer. |
| Subcellular location | |
| Tissue specificity | Liver and kidney. Lower amounts seen in the brain. |
| 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
| Keywords | |
|---|---|
| Biological process | Fatty acid metabolism Lipid metabolism |
| Cellular component | Peroxisome |
| Coding sequence diversity | Polymorphism |
| Ligand | NAD |
| Molecular function | Isomerase Lyase Oxidoreductase |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | peroxisome Ref.1 Traceable author statement. Source: ProtInc |
| Molecular function | 3-hydroxyacyl-CoA dehydrogenase activity Ref.1 Traceable author statement. Source: ProtInc coenzyme bindingInferred from electronic annotation. Source: InterPro dodecenoyl-CoA delta-isomerase activityInferred from electronic annotation. Source: EC enoyl-CoA hydratase activity Ref.1Traceable author statement. Source: ProtInc |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 723 | 722 | Peroxisomal bifunctional enzyme | PRO_0000109247 | |||||
Regions | |||||||||
| Region | 2 – 282 | 281 | Enoyl-CoA hydratase / isomerase | ||||||
| Region | 283 – 572 | 290 | 3-hydroxyacyl-CoA dehydrogenase | ||||||
| Motif | 721 – 723 | 3 | Microbody targeting signal | ||||||
Sites | |||||||||
| Binding site | 101 | 1 | Substrate; via amide nitrogen By similarity | ||||||
| Site | 124 | 1 | Important for catalytic activity By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 359 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 584 | 1 | N6-acetyllysine Ref.10 | ||||||
Natural variations | |||||||||
| Natural variant | 40 | 1 | V → G: dbSNP rs1062551. Ref.1 | VAR_054329 | |||||
| Natural variant | 41 | 1 | I → R: dbSNP rs1062552. Ref.1 | VAR_054330 | |||||
| Natural variant | 75 | 1 | T → I: dbSNP rs1062553. Ref.1 | VAR_047132 | |||||
| Natural variant | 274 | 1 | A → T: dbSNP rs2302819. Ref.3 | VAR_047133 | |||||
| Natural variant | 325 | 1 | A → G: dbSNP rs1062555. Ref.1 | VAR_054331 | |||||
| Natural variant | 598 | 1 | K → T: dbSNP rs1042437. Ref.1 Ref.7 | VAR_054332 | |||||
| Natural variant | 606 | 1 | T → P: dbSNP rs1042438. Ref.1 Ref.7 | VAR_047134 | |||||
| Natural variant | 685 | 1 | Q → K: dbSNP rs11919970. | VAR_047135 | |||||
| Natural variant | 715 | 1 | L → S: dbSNP rs11927618. | VAR_047136 | |||||
Experimental info | |||||||||
| Sequence conflict | 117 | 1 | E → D in AAA53289. Ref.1 | ||||||
| Sequence conflict | 656 – 657 | 2 | WP → CA in AAA53289. Ref.1 | ||||||
| Sequence conflict | 656 – 657 | 2 | WP → CA in AAB19482. Ref.7 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "cDNA cloning of the human peroxisomal enoyl-CoA hydratase: 3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme and localization to chromosome 3q26.3-3q28: a free left Alu Arm is inserted in the 3' noncoding region." Hoefler G., Forstner M., McGuinness M.C., Hulla W., Hiden M., Krisper P., Kenner L., Ried T., Lengauer C., Zechner R., Moser H.W., Chen G.L. Genomics 19:60-67(1994) [PubMed: 8188243] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS GLY-40; ARG-41; ILE-75; GLY-325; THR-598 AND PRO-606. Tissue: Liver. |
| [2] | "Structural organization of gene for human peroxisomal enoyl-CoA hydratase/L-3-hydroxyacyl-CoA dehydrogenase: L-bifunctional enzyme (L-PBE)." Cherkaoui-Malki M., Surapureddi S., Yeldandi A.V., Rao S.M., Zhu Y., Reddy J.K. Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | "Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-274. Tissue: Placenta. |
| [4] | Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney. |
| [5] | Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [6] | "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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Uterus. |
| [7] | "Import of human bifunctional enzyme into peroxisomes of human hepatoma cells in vitro." Chen G.L., Balfe A., Erwa W., Hoefler G., Gaertner J., Aikawa J., Chen W.W. Biochem. Biophys. Res. Commun. 178:1084-1091(1991) [PubMed: 1651711] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 502-723, VARIANTS THR-598 AND PRO-606. Tissue: Liver. |
| [8] | "Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, MASS SPECTROMETRY. |
| [9] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [10] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-584, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L07077 mRNA. Translation: AAA53289.1. AJ427345 AJ427351 Genomic DNA. Translation: CAD22483.1. AK291798 mRNA. Translation: BAF84487.1. AK223460 mRNA. Translation: BAD97180.1. CH471052 Genomic DNA. Translation: EAW78229.1. BC038948 mRNA. Translation: AAH38948.1. BC110460 mRNA. Translation: AAI10461.1. S50245 mRNA. Translation: AAB19482.1. |
| IPI | IPI00216164. |
| PIR | A49613. |
| RefSeq | NP_001159887.1. NP_001957.2. |
| UniGene | Hs.429879 |
3D structure databases | |
| SMR | Q08426. Positions 262-717. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q08426. 1 interaction. |
| STRING | Q08426. |
PTM databases | |
| PhosphoSite | Q08426. |
Proteomic databases | |
| PRIDE | Q08426. |
Genome annotation databases | |
| Ensembl | ENST00000231887; ENSP00000231887; ENSG00000113790; Homo sapiens. [Genome view] |
| GeneID | 1962. |
Organism-specific databases | |
| CTD | 1962. |
| GeneCards | GC03M186391. |
| HGNC | HGNC:3247. EHHADH. |
| MIM | 607037. gene. |
| Orphanet | 50812. Zellweger-like syndrome, without peroxisomal anomalies. |
| PharmGKB | PA27682. |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOGENOM | HBG691737. |
| HOVERGEN | Q08426. |
| InParanoid | Q08426. |
| OMA | PYYNQTY. |
| OrthoDB | EOG93JFQ9. |
| PhylomeDB | Q08426. |
Enzyme and pathway databases | |
| BRENDA | 1.1.1.35. 247. 4.2.1.17. 247. 5.3.3.8. 247. |
| Reactome | REACT_602. Metabolism of lipids and lipoproteins. |
Gene expression databases | |
| ArrayExpress | Q08426. |
| Bgee | Q08426. |
| CleanEx | HS_EHHADH. |
| Genevestigator | Q08426. |
| GermOnline | ENSG00000113790. Homo sapiens. |
Family and domain databases | |
| 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. IPR013328. DH_multihelical. IPR018376. Enoyl-CoA_hyd/isom_CS. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 2 hits. |
| Pfam | PF00725. 3HCDH. 2 hits. PF02737. 3HCDH_N. 1 hit. PF00378. ECH. 1 hit. [Graphical view] |
| PROSITE | PS00067. 3HCDH. 1 hit. PS00166. ENOYL_COA_HYDRATASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| DrugBank | DB00157. NADH. |
| SOURCE | Search... |
Entry information
| Entry name | ECHP_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q08426 Secondary accession number(s): A8K6Y3, Q58EZ5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Human chromosome 3 Human chromosome 3: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


