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161  structures 5366  species 0  interactions 20925  sequences 61  architectures

Family: CoA_trans (PF01144)

Summary: Coenzyme A transferase

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The Pfam group coordinates the annotation of Pfam families in Wikipedia, but we have not yet assigned a Wikipedia article to this family. If you think that a particular Wikipedia article provides good annotation, please let us know.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Coenzyme A transferase Provide feedback

No Pfam abstract.

Literature references

  1. Jacob U, Mack M, Clausen T, Huber R, Buckel W, Messerschmidt A; , Structure 1997;5:415-426.: Glutaconate CoA-transferase from Acidaminococcus fermentans: the crystal structure reveals homology with other CoA-transferases. PUBMED:9083111 EPMC:9083111


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR004165

CoA-transferases are found in organisms from all kingdoms of life. They catalyse reversible transfer reactions of coenzyme A groups from CoA-thioesters to free acids. There are at least three families of CoA-transferases, which differ in sequence and reaction mechanism:

  • Family I consists of CoA-transferases for 3-oxoacids ( EC , EC ), short-chain fatty acids ( EC , EC ) and glutaconate ( EC ). Most use succinyl-CoA or acetyl-CoA as CoA donors.
  • Family II consists of the homodimeric alpha-subunits of citrate lyase and citramalate lyase ( EC , EC ). These enzymes catalyse the transfer of acyl carrier protein (ACP) with a covalently bound CoA derivative, but can accept free CoA thioesters as well.
  • Family III consists of formyl-CoA:oxalate CoA-transferase [ PUBMED:15213226 ], succinyl-CoA:(R)-benzylsuccinate CoA-transferase [ PUBMED:11418570 ], (E)-cinnamoyl-CoA:(R)-phenyllactate CoA-transferase [ PUBMED:10849007 ], succinyl-CoA:mesaconate CoA-transferase [ PUBMED:28932214 ] and butyrobetainyl-CoA:(R)-carnitine CoA-transferase [ PUBMED:15823031 ]. These CoA-transferases occur in prokaryotes and eukaryotes, and catalyse CoA-transfer reactions in a highly substrate- and stereo-specific manner [ PUBMED:11749953 ].

Coenzyme A (CoA) transferases belong to an evolutionary conserved [ PUBMED:1624453 , PUBMED:9325289 ] family of enzymes catalyzing the reversible transfer of CoA from one carboxylic acid to another. They have been identified in many prokaryotes and in mammalian tissues. The bacterial enzymes are heterodimer of two subunits (A and B) of about 25 Kd each while eukaryotic SCOT consist of a single chain which is colinear with the two bacterial subunits.

This family consists of 3-oxoacid CoA-transferases and related CoA-transferases from family I.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan ISOCOT_Fold (CL0246), which has the following description:

This superfamily contains a variety of enzymes and non-enzymatic ligand binding domains.

The clan contains the following 12 members:

5-FTHF_cyc-lig AcetylCoA_hyd_C AcetylCoA_hydro CitF CoA_trans DeoRC Glucosamine_iso IF-2B LUD_dom Mal_decarbox_Al Rib_5-P_isom_A Sugar-bind

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

View options

We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(38)
Full
(20925)
Representative proteomes UniProt
(85641)
RP15
(2142)
RP35
(8678)
RP55
(20290)
RP75
(36068)
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PP/heatmap 1            

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(38)
Full
(20925)
Representative proteomes UniProt
(85641)
RP15
(2142)
RP35
(8678)
RP55
(20290)
RP75
(36068)
Alignment:
Format:
Order:
Sequence:
Gaps:
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Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(38)
Full
(20925)
Representative proteomes UniProt
(85641)
RP15
(2142)
RP35
(8678)
RP55
(20290)
RP75
(36068)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Prosite
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Finn RD , Bateman A , Griffiths-Jones SR
Number in seed: 38
Number in full: 20925
Average length of the domain: 206.70 aa
Average identity of full alignment: 27 %
Average coverage of the sequence by the domain: 79.75 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 23.0 23.0
Trusted cut-off 23.0 23.0
Noise cut-off 22.9 22.9
Model length: 217
Family (HMM) version: 26
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

Selections

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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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Structures

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 CoA_trans domain has been found. There are 161 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 sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A0R4IJ61 View 3D Structure Click here
A4I5L8 View 3D Structure Click here
A4I5L9 View 3D Structure Click here
A8KBV1 View 3D Structure Click here
B2GV06 View 3D Structure Click here
E9AHQ2 View 3D Structure Click here
O29069 View 3D Structure Click here
O34317 View 3D Structure Click here
O34466 View 3D Structure Click here
P0A101 View 3D Structure Click here
P0C7I7 View 3D Structure Click here
P0C7I8 View 3D Structure Click here
P23673 View 3D Structure Click here
P33752 View 3D Structure Click here
P37766 View 3D Structure Click here
P42315 View 3D Structure Click here
P42316 View 3D Structure Click here
P44874 View 3D Structure Click here
P44875 View 3D Structure Click here
P55809 View 3D Structure Click here
P56006 View 3D Structure Click here
P56007 View 3D Structure Click here
P76458 View 3D Structure Click here
P76459 View 3D Structure Click here
P9WPW1 View 3D Structure Click here
P9WPW3 View 3D Structure Click here
P9WPW5 View 3D Structure Click here
Q09450 View 3D Structure Click here
Q0S7P9 View 3D Structure Click here
Q29551 View 3D Structure Click here
Q2G1C6 View 3D Structure Click here
Q43973 View 3D Structure Click here
Q4D0L3 View 3D Structure Click here
Q4E2P8 View 3D Structure Click here
Q54JD9 View 3D Structure Click here
Q59091 View 3D Structure Click here
Q59111 View 3D Structure Click here
Q59112 View 3D Structure Click here
Q59Z19 View 3D Structure Click here
Q5XIJ9 View 3D Structure Click here