Summary: Biotin-requiring enzyme

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Wikipedia: Biotin attachment domain
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This is the Wikipedia entry entitled "Biotin attachment domain". More...

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Biotin attachment domain Edit Wikipedia article

Biotin-requiring enzyme

Identifiers

Symbol

Biotin_lipoyl

1lab / SCOPe / SUPFAM

TCDB

3.B.1

Available protein structures:
Pfam Â	structures / ECOD Â
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1dczA:55-122 1dd2A:55-122 1o78A:55-122 1k67B:81-155 2bdoA:81-155 1k69B:81-155 3bdoA:81-155 1bdo :81-155 1a6x :81-155 1y8pB:186-260 1y8nB:186-260 1fyc :186-260 1y8oB:186-260 1ghk :3-76 1ghj :3-76 1gjxA:4-76 1qjoA:207-278 1iyu :3-73 1iyv :3-73 1lac :3-76 1lab :3-76 1k8mA:65-138 1k8oA:65-138

Biotin/lipoyl attachment domain has a conserved lysine residue that binds biotin or lipoic acid. Biotin plays a catalytic role in some carboxyl transfer reactions and is covalently attached, via an amide bond, to a lysine residue in enzymes requiring this coenzyme^[1]. Lipoamide acyltransferases have an essential cofactor, lipoic acid, which is covalently bound via an amide linkage to a lysine group^[2]. The lipoic acid cofactor is found in a variety of proteins that include, H-protein of the glycine cleavage system (GCS), mammalian and yeast pyruvate dehydrogenases and fast migrating protein (FMP) (gene acoC) from Alcaligenes eutrophus.

Human proteins containing this domain

ACACA; ACACB; DBT; DLAT; DLST; DLSTP; MCCC1; PC; PCCA; PDHX;

References

^ Kumar GK, Shenoy BC, Wood HG, Samols D, Xie Y, Park VL, Beegen H (1992). "The importance of methionine residues for the catalysis of the biotin enzyme, transcarboxylase. Analysis by site-directed mutagenesis". J. Biol. Chem. 267 (26): 18407â€“18412. PMIDÂ 1526981.{{cite journal}}: CS1 maint: multiple names: authors list (link)
^ Guest JR, Russell GC (1991). "Sequence similarities within the family of dihydrolipoamide acyltransferases and discovery of a previously unidentified fungal enzyme". Biochim. Biophys. Acta. 1076 (2): 225â€“232. PMIDÂ 1825611.

This article incorporates text from the public domain Pfam and InterPro: IPR000089

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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.

Biotin-requiring enzyme Provide feedback

This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognise the Glycine cleavage system H proteins.

Internal database links

SCOOP:	Biotin_lipoyl_2 CusB_dom_1 DEC-1_N DUF2118 GCV_H HlyD_2 HlyD_3 HlyD_D23 NQRA Peptidase_M23 PTS_EIIA_1 RnfC_N
Similarity to PfamA using HHSearch:	GCV_H NQRA RnfC_N HlyD_3 Biotin_lipoyl_2 Biotin_lipoyl_2 HlyD_D23

External database links

HOMSTRAD:	biotin_lipoyl
PROSITE:	PDOC00167 PDOC00168
SCOP:	1lab
Transporter classification:	3.B.1

This tab holds annotation information from the InterPro database.

InterPro entry IPR000089

The biotin/lipoyl attachment domain has a conserved lysine residue that binds biotin or lipoic acid. The 80 residues surrounding the biotinyl-binding lysine residue display some sequence similarity to that around the lipoyl-binding lysine residue. Biotin plays a catalytic role in some carboxyl transfer reactions and is covalently attached, via an amide bond, to a lysine residue in enzymes requiring this coenzyme [ PUBMED:1526981 ]. E2 acyltransferases have an essential cofactor, lipoic acid, which is covalently bound via an amide linkage to a lysine group [ PUBMED:1825611 ]. The lipoic acid cofactor is found in a variety of proteins that include, H-protein of the glycine cleavage system (GCS), mammalian and yeast pyruvate dehydrogenases and branched-chain 2-oxo acid dehydrogenase complex (BCOADC).

The lipoyl domains of 2-oxo acid dehydrogenase multienzyme complexes and the biotinyl domains of biotin-dependent enzymes have been solved, which revealed that they have homologous structures consisting of a flattened 8-stranded -barrel with the target lysine positioned in comparable beta-turns. Additional important residues for specificity have been identified, such as the conserved methionine flanking the target lysine that is essential for the recognition of the biotinyl domain by the biotinyl protein ligase [ PUBMED:8950276 , PUBMED:8747466 ].

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 Hybrid (CL0105), which has the following description:

This superfamily contains proteins with a hybrid motif [1]. This motif is embedded in structurally diverse proteins.

The clan contains the following 26 members:

Apocytochr_F_C Biotin_carb_C Biotin_lipoyl Biotin_lipoyl_2 Complex1_51K CusB_dom_1 DUF2118 DUF2254 GARS_C GCV_H HlyD_2 HlyD_3 HlyD_D23 HlyD_D4 HMBD LAL_C2 NAPRTase_N NQRA OEP Peptidase_M23 PGM1_C PTS_EIIA_1 PurK_C PYNP_C QRPTase_N RnfC_N

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...

There are various ways to view or download the sequence alignments that we store. We provide several sequence viewers and a plain-text Stockholm-format file for download.

Alignment types

We make a range of alignments for each Pfam-A family:

seed: the curated alignment from which the HMM for the family is built
full: the alignment generated by searching the sequence database using the HMM
RP15/RP35/RP55/RP75: Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
UniProt: alignment generated by searching the UniProtKB sequence database using the family HMM

Viewing

You can see the alignments as HTML or in three different sequence viewers:

jalview: a Java applet developed at the University of Dundee. You will need Java installed before running jalview
HTML: an HTML page showing the whole alignment.Please note: full Pfam alignments can be very large. These HTML views are extremely large and often cause problems for browsers. Please use either jalview or the Pfam viewer if you have trouble viewing the HTML version
PP/Heatmap: an HTML-based representation of the alignment, coloured according to the posterior-probability (PP) values from the HMM. As for the standard HTML view, heatmap alignments can also be very large and slow to render.

Reformatting

You can download (or view in your browser) a text representation of a Pfam alignment in various formats:

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You can also change the order in which sequences are listed in the alignment, change how insertions are represented, alter the characters that are used to represent gaps in sequences and, finally, choose whether to download the alignment or to view it in your browser directly.

Downloading

You may find that large alignments cause problems for the viewers and the reformatting tool, so we also provide all alignments in Stockholm format. You can download either the plain text alignment, or a gzipped version of it.

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 (66190)	Representative proteomes				UniProt (264909)
	Seed (38)	Full (66190)	RP15 (8590)	RP35 (29774)	RP55 (64370)	RP75 (108418)	UniProt (264909)
Jalview	View	View	View	View	View	View	View
HTML	View
PP/heatmap	₁

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

Key: available, not generated, — not available.

Format an alignment

	Seed (38)	Full (66190)	Representative proteomes				UniProt (264909)
	Seed (38)	Full (66190)	RP15 (8590)	RP35 (29774)	RP55 (64370)	RP75 (108418)	UniProt (264909)
Alignment:
Format:
Order:	Tree Alphabetical
Sequence:	Inserts lower case All upper case
Gaps:
Download/view:	Download View

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 (66190)	Representative proteomes				UniProt (264909)
	Seed (38)	Full (66190)	RP15 (8590)	RP35 (29774)	RP55 (64370)	RP75 (108418)	UniProt (264909)
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

Seed source:

Prosite

Previous IDs:

biotin_req_enzy; biotin_lipoyl;

Type:

Domain

Sequence Ontology:

SO:0000417

Author:

Finn RD

Number in seed:

38

Number in full:

66190

Average length of the domain:

71.5 aa

Average identity of full alignment:

28 %

Average coverage of the sequence by the domain:

12.78 %

HMM information

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	22.1	22.1
Trusted cut-off	22.1	22.1
Noise cut-off	22.0	22.0

Model length:

73

Family (HMM) version:

25

Download:

download the raw HMM for this family

Species distribution

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Colour assignments

Archea	Eukaryota
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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...

This chart is a modified "sunburst" visualisation of the species tree for this family. It shows each node in the tree as a separate arc, arranged radially with the superkingdoms at the centre and the species arrayed around the outermost ring.

How the sunburst is generated

The tree is built by considering the taxonomic lineage of each sequence that has a match to this family. For each node in the resulting tree, we draw an arc in the sunburst. The radius of the arc, its distance from the root node at the centre of the sunburst, shows the taxonomic level ("superkingdom", "kingdom", etc). The length of the arc represents either the number of sequences represented at a given level, or the number of species that are found beneath the node in the tree. The weighting scheme can be changed using the sunburst controls.

In order to reduce the complexity of the representation, we reduce the number of taxonomic levels that we show. We consider only the following eight major taxonomic levels:

superkingdom
kingdom
phylum
class
order
family
genus
species

Colouring and labels

Segments of the tree are coloured approximately according to their superkingdom. For example, archeal branches are coloured with shades of orange, eukaryotes in shades of purple, etc. The colour assignments are shown under the sunburst controls. Where space allows, the name of the taxonomic level will be written on the arc itself.

As you move your mouse across the sunburst, the current node will be highlighted. In the top section of the controls panel we show a summary of the lineage of the currently highlighed node. If you pause over an arc, a tooltip will be shown, giving the name of the taxonomic level in the title and a summary of the number of sequences and species below that node in the tree.

Anomalies in the taxonomy tree

There are some situations that the sunburst tree cannot easily handle and for which we have work-arounds in place.

Missing taxonomic levels

Some species in the taxonomic tree may not have one or more of the main eight levels that we display. For example, Bos taurus is not assigned an order in the NCBI taxonomic tree. In such cases we mark the omitted level with, for example, "No order", in both the tooltip and the lineage summary.

Unmapped species names

The tree is built by looking at each sequence in the full alignment for the family. We take the name of the species given by UniProt and try to map that to the full taxonomic tree from NCBI. In some cases, the name chosen by UniProt does not map to any node in the NCBI tree, perhaps because the chosen name is listed as a synonym or a misspelling in the NCBI taxonomy.

So that these nodes are not simply omitted from the sunburst tree, we group them together in a separate branch (or segment of the sunburst tree). Since we cannot determine the lineage for these unmapped species, we show all levels between the superkingdom and the species as "uncategorised".

Sub-species

Since we reduce the species tree to only the eight main taxonomic levels, sequences that are mapped to the sub-species level in the tree would not normally be shown. Rather than leave out these species, we map them instead to their parent species. So, for example, for sequences belonging to one of the Vibrio cholerae sub-species in the NCBI taxonomy, we show them instead as belonging to the species Vibrio cholerae.

Too many species/sequences

For large species trees, you may see blank regions in the outer layers of the sunburst. These occur when there are large numbers of arcs to be drawn in a small space. If an arc is less than approximately one pixel wide, it will not be drawn and the space will be left blank. You may still be able to get some information about the species in that region by moving your mouse across the area, but since each arc will be very small, it will be difficult to accurately locate a particular species.

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The tree shows the occurrence of this domain across different species. More...

Species trees

We show the species tree in one of two ways. For smaller trees we try to show an interactive representation, which allows you to select specific nodes in the tree and view them as an alignment or as a set of Pfam domain graphics.

Unfortunately we have found that there are problems viewing the interactive tree when the it becomes larger than a certain limit. Furthermore, we have found that Internet Explorer can become unresponsive when viewing some trees, regardless of their size. We therefore show a text representation of the species tree when the size is above a certain limit or if you are using Internet Explorer to view the site.

If you are using IE you can still load the interactive tree by clicking the "Generate interactive tree" button, but please be aware of the potential problems that the interactive species tree can cause.

Interactive tree

For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.

We also count the number of unique sequences on which each domain is found, which is shown in green. Note that a domain may appear multiple times on the same sequence, leading to the difference between these two numbers.

Finally, we group sequences from the same organism according to the NCBI code that is assigned by UniProt, allowing us to count the number of distinct sequences on which the domain is found. This value is shown in the pink boxes.

We use the NCBI species tree to group organisms according to their taxonomy and this forms the structure of the displayed tree. Note that in some cases the trees are too large (have too many nodes) to allow us to build an interactive tree, but in most cases you can still view the tree in a plain text, non-interactive representation. Those species which are represented in the seed alignment for this domain are highlighted.

You can use the tree controls to manipulate how the interactive tree is displayed:

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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 Biotin_lipoyl domain has been found. There are 147 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.

Loading structure mapping...

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
A0A044QWC9	View 3D Structure	Click here
A0A044RKQ4	View 3D Structure	Click here
A0A044UN15	View 3D Structure	Click here
A0A077YXC6	View 3D Structure	Click here
A0A077YY51	View 3D Structure	Click here
A0A077Z0H4	View 3D Structure	Click here
A0A077Z0S4	View 3D Structure	Click here
A0A077Z2U7	View 3D Structure	Click here
A0A077ZBT2	View 3D Structure	Click here
A0A077ZCA7	View 3D Structure	Click here
A0A077ZLQ4	View 3D Structure	Click here
A0A0A2V2S3	View 3D Structure	Click here
A0A0D2DEU4	View 3D Structure	Click here
A0A0D2DZB4	View 3D Structure	Click here
A0A0D2F234	View 3D Structure	Click here
A0A0D2G879	View 3D Structure	Click here
A0A0D2G9V4	View 3D Structure	Click here
A0A0D2GDK4	View 3D Structure	Click here
A0A0D2GGC2	View 3D Structure	Click here
A0A0D2GGQ9	View 3D Structure	Click here
A0A0D2GNL4	View 3D Structure	Click here
A0A0D2GQ46	View 3D Structure	Click here
A0A0D2GSQ9	View 3D Structure	Click here
A0A0D2GSY8	View 3D Structure	Click here
A0A0D2GW69	View 3D Structure	Click here
A0A0D2H2S1	View 3D Structure	Click here
A0A0H3GLJ0	View 3D Structure	Click here
A0A0H3GNC0	View 3D Structure	Click here
A0A0H3GRI1	View 3D Structure	Click here
A0A0H3GSC6	View 3D Structure	Click here
A0A0H3H3Q3	View 3D Structure	Click here
A0A0K0DSJ4	View 3D Structure	Click here
A0A0K0DX55	View 3D Structure	Click here
A0A0K0EJZ9	View 3D Structure	Click here
A0A0K0EKD4	View 3D Structure	Click here
A0A0K0ENC3	View 3D Structure	Click here
A0A0K0ENX5	View 3D Structure	Click here
A0A0K0ER14	View 3D Structure	Click here
A0A0N4U0I9	View 3D Structure	Click here
A0A0N4U4U7	View 3D Structure	Click here

Showing 40 matches

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Family: Biotin_lipoyl (PF00364)

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