Summary: 3-hydroxyacyl-CoA dehydrogenase, C-terminal domain
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3-hydroxyacyl-CoA dehydrogenase, C-terminal domain Provide feedback
This family also includes lambda crystallin. Some proteins include two copies of this domain.
Birktoft JJ, Holden HM, Hamlin R, Xuong NH, Banaszak LJ; , Proc Natl Acad Sci U S A 1987;84:8262-8266.: Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary chain tracing at 2.8-A resolution. PUBMED:3479790 EPMC:3479790
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This tab holds annotation information from the InterPro database.
InterPro entry IPR006108
3-hydroxyacyl-CoA dehydrogenase (EC) (HCDH) [PUBMED:3479790] is an enzyme involved in fatty acid metabolism, it catalyzes the reduction of 3-hydroxyacyl-CoA to 3-oxoacyl-CoA. Most eukaryotic cells have 2 fatty-acid beta-oxidation systems, one located in mitochondria and the other in peroxisomes. In peroxisomes 3-hydroxyacyl-CoA dehydrogenase forms, with enoyl-CoA hydratase (ECH) and 3,2-trans-enoyl-CoA isomerase (ECI) a multifunctional enzyme where the N-terminal domain bears the hydratase/isomerase activities and the C-terminal domain the dehydrogenase activity. There are two mitochondrial enzymes: one which is monofunctional and the other which is, like its peroxisomal counterpart, multifunctional.
In Escherichia coli (gene fadB) and Pseudomonas fragi (gene faoA) HCDH is part of a multifunctional enzyme which also contains an ECH/ECI domain as well as a 3-hydroxybutyryl-CoA epimerase domain [PUBMED:2204034].
There are two major region of similarities in the sequences of proteins of the HCDH family, the first one located in the N-terminal, corresponds to the NAD-binding site, the second one is located in the centre of the sequence. This represents the C-terminal domain which is also found in lambda crystallin. Some proteins include two copies of this domain.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||3-hydroxyacyl-CoA dehydrogenase activity (GO:0003857)|
|oxidoreductase activity (GO:0016491)|
|Biological process||fatty acid metabolic process (GO:0006631)|
|oxidation-reduction process (GO:0055114)|
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Curation and family details
|Seed source:||Pfam-B_743 (release 2.1)|
|Author:||Bateman A, Griffiths-Jones SR|
|Number in seed:||69|
|Number in full:||48537|
|Average length of the domain:||94.70 aa|
|Average identity of full alignment:||27 %|
|Average coverage of the sequence by the domain:||22.71 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||18|
|Download:||download the raw HMM for this family|
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There are 5 interactions for this family. More...
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the 3HCDH domain has been found. There are 104 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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