Summary: Acetyl-CoA hydrolase/transferase C-terminal domain
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Acetyl-CoA hydrolase/transferase C-terminal domain Provide feedback
This family contains several enzymes which take part in pathways involving acetyl-CoA. Acetyl-CoA hydrolase EC:18.104.22.168 (P32316) catalyses the formation of acetate from acetyl-CoA, CoA transferase (CAT1) EC:2.8.3.- (P38946) produces succinyl-CoA, and acetate-CoA transferase EC:22.214.171.124 (Q59323) utilises acyl-CoA and acetate to form acetyl-CoA.
Van Dyck L, Purnelle B, Skala J, Goffeau A; , Yeast 1992;8:769-776.: An 11.4 kb DNA segment on the left arm of yeast chromosome II carries the carboxypeptidase Y sorting gene PEP1, as well as ACH1, FUS3 and a putative ARS. PUBMED:1441754 EPMC:1441754
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|Similarity to PfamA using HHSearch:||CitF|
External database links
This tab holds annotation information from the InterPro database.
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This superfamily contains a variety of enzymes and non-enzymatic ligand binding domains.
The clan contains the following 11 members:5-FTHF_cyc-lig AcetylCoA_hyd_C AcetylCoA_hydro CitF CoA_trans DeoRC DUF162 Glucosamine_iso IF-2B Rib_5-P_isom_A Sugar-bind
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Number in seed:||251|
|Number in full:||2410|
|Average length of the domain:||149.60 aa|
|Average identity of full alignment:||42 %|
|Average coverage of the sequence by the domain:||31.00 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||1|
|Download:||download the raw HMM for this family|
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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 AcetylCoA_hyd_C domain has been found. There are 21 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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