General rule information
[?]
Accession |
PRU01066 |
Dates |
24-SEP-2014 (Created) 22-NOV-2019 (Last updated, Version 6) |
Predictors |
PROSITE; PS50968; BIOTINYL_LIPOYL
|
Name |
Biotinyl/lipoyl domain |
Function |
Biotin and lipoic acid moieties are the covalently bound cofactors of several multicomponent enzyme complexes that catalyze key metabolic reactions. They are attached to a lysine residue, via an amide bond, by specific biotinyl and lipoyl protein ligases. |
Propagated annotation
[?]
case <Feature:PS50968:41-42=M-K> or <Feature:PS50968:42-43=K-M>
else case <Feature:PS50968:42=K>
Cofactor |
(R)-lipoate Note: Binds 1 lipoyl cofactor covalently. |
end case
case <Feature:PS50968:41-42=M-K> or <Feature:PS50968:42-43=K-M>
else case <Feature:PS50968:42=K>
end case
case <Feature:PS50968:41-42=M-K> or <Feature:PS50968:42-43=K-M>
From: PS50968 |
Key
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From
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To
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Description
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Tag
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Condition
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FTGroup
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DOMAIN
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from
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to
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Biotinyl-binding #
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MOD_RES
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42
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42
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N6-biotinyllysine
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K
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else
DOMAIN
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from
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to
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Lipoyl-binding #
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MOD_RES
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42
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42
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N6-lipoyllysine
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K
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end case
Additional information
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Size range |
57-96 amino acids |
Related rules |
None |
Repeats |
1-3 |
Topology |
Undefined |
Examples |
P0A6T9 (GCSH_ECOLI); P0ABD8 (BCCP_ECOLI): [Recover all] |
Scope |
Bacteria
Eukaryota
Archaea |
Comments |
None |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and
distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives
(CC BY-NC-ND 4.0) License, see
prosite_license.html.
UniProtKB rule member sequences
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