Summary: Biotin carboxylase C-terminal domain
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This is the Wikipedia entry entitled "Biotin carboxylase". More...
Biotin carboxylase Edit Wikipedia article
| biotin carboxylase | |||||||
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| Identifiers | |||||||
| EC number | 6.3.4.14 | ||||||
| CAS number | 9075-71-2 | ||||||
| Databases | |||||||
| IntEnz | IntEnz view | ||||||
| BRENDA | BRENDA entry | ||||||
| ExPASy | NiceZyme view | ||||||
| KEGG | KEGG entry | ||||||
| MetaCyc | metabolic pathway | ||||||
| PRIAM | profile | ||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||
| Gene Ontology | AmiGO / EGO | ||||||
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| crystal structure of biotin carboxylase domain of acetyl-coenzyme a carboxylase from saccharomyces cerevisiae in complex with soraphen a | |||||||||
| Identifiers | |||||||||
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| Symbol | Biotin_carb_C | ||||||||
| Pfam | PF02785 | ||||||||
| InterPro | IPR005482 | ||||||||
| SCOP | 1dv1 | ||||||||
| SUPERFAMILY | 1dv1 | ||||||||
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In enzymology, a biotin carboxylase (EC 6.3.4.14) is an enzyme that catalyzes the chemical reaction
- ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
The 3 substrates of this enzyme are ATP, biotin-carboxyl-carrier protein, and CO2, whereas its 3 products are ADP, phosphate, and carboxybiotin-carboxyl-carrier protein.
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of this enzyme class is biotin-carboxyl-carrier-protein:carbon-dioxide ligase (ADP-forming). This enzyme is also called biotin carboxylase (component of acetyl CoA carboxylase). This enzyme participates in fatty acid biosynthesis.
A C-terminal conserved domain within this enzyme contains most of the active site residues.[1]
[edit] Structural studies
As of late 2007[update], 5 structures have been solved for this class of enzymes, with PDB accession codes 1BNC, 1DV1, 1DV2, 2GPS, and 2GPW.
[edit] References
- ^ Waldrop, G. L.; Rayment, I.; Holden, H. M. (1994). "Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase". Biochemistry 33 (34): 10249–10256. doi:10.1021/bi00200a004. PMID 7915138.
[edit] Further reading
- Dimroth P, Guchhait RB, Stoll E, Lane MD (1970). "Enzymatic carboxylation of biotin: molecular and catalytic properties of a component enzyme of acetyl CoA carboxylase". Proc. Natl. Acad. Sci. U.S.A. 67 (3): 1353–60. doi:10.1073/pnas.67.3.1353. PMC 283359. PMID 4922289. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=283359.
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Biotin carboxylase C-terminal domain Provide feedback
Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference [1] are in this C-terminal domain.
Literature references
-
Waldrop GL, Rayment I, Holden HM; , Biochemistry 1994;33:10249-10256.: Three-dimensional structure of the biotin carboxylase subunit. of acetyl-CoA carboxylase. PUBMED:7915138 EPMC:7915138
External database links
| PANDIT: | PF02785 |
| Pseudofam: | PF02785 |
| SCOP: | 1dv1 |
| SYSTERS: | Biotin_carb_C |
This tab holds annotation information from the InterPro database.
InterPro entry IPR005482
Acetyl-CoA carboxylase is found in all animals, plants, and bacteria and catalyzes the first committed step in fatty acid synthesis. It is a multicomponent enzyme containing a biotin carboxylase activity, a biotin carboxyl carrier protein, and a carboxyltransferase functionality. The "B-domain" extends from the main body of the subunit where it folds into two alpha-helical regions and three strands of beta-sheet. Following the excursion into the B-domain, the polypeptide chain folds back into the body of the protein where it forms an eight-stranded antiparallel beta-sheet. In addition to this major secondary structural element, the C-terminal domain also contains a smaller three-stranded antiparallel beta-sheet and seven alpha-helices [PUBMED:7915138].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Molecular function | ligase activity (GO:0016874) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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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 using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
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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 (109) |
Full (10242) |
Representative proteomes | NCBI (8078) |
Meta (3751) |
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| RP15 (942) |
RP35 (1879) |
RP55 (2586) |
RP75 (3077) |
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| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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not generated,
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Format an alignment
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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 (109) |
Full (10242) |
Representative proteomes | NCBI (8078) |
Meta (3751) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (942) |
RP35 (1879) |
RP55 (2586) |
RP75 (3077) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
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
| Seed source: | ref [1] |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Griffiths-Jones SR |
| Number in seed: | 109 |
| Number in full: | 10242 |
| Average length of the domain: | 106.20 aa |
| Average identity of full alignment: | 38 % |
| Average coverage of the sequence by the domain: | 14.54 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 107 | ||||||||||||
| Family (HMM) version: | 14 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Interactions
There are 5 interactions for this family. More...
Biotin_lipoyl Biotin_carb_C PYC_OADA CPSase_L_chain CPSase_L_D2Structures
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 Biotin_carb_C domain has been found. There are 113 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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ADP + phosphate + carboxybiotin-carboxyl-carrier protein
Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence