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InterPro: IPR010071 Amino acid adenylation

Protein matchesHelp
UniProtKB
Matches:
4247 proteins
AccessionHelp IPR010071 AA_adenyl_domain
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR000873 AMP-dependent synthetase/ligase
Found in IPR010072 D-alanine-activating enzyme
IPR014397 L-aminoadipate-semialdehyde dehydrogenase, large subunit
Contains IPR020459 AMP-binding
IPR020845 AMP-binding, conserved site
GO Term annotationHelp
Function GO:0016874 ligase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This entry represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalysed is aa + ATP to aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called 'A-domains' in that context (for a review, see [1]). A-domains are almost invariably followed by 'T-domains' (thiolation domains, IPR006163) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a 'C-domain' (condensation domain, IPR001242) which catalyses the ligation of two amino acid thiol-esters from neighbouring modules. This domain is a subset of the AMP-binding domain, which also hits substrate--CoA ligases and luciferases.

Structural linksHelp
SCOP: e.23.1.1

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR010071 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O30409 Tyrocidine synthetase 3

O43103 Ferrichrome siderophore peptide synthetase

P07702 L-aminoadipate-semialdehyde dehydrogenase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR001242 Condensation domain
IPR013120 Male sterility, NAD-binding
IPR020845 AMP-binding, conserved site
IPR016040 NAD(P)-binding domain
IPR010080 Thioester reductase
IPR014397 L-aminoadipate-semialdehyde dehydrogenase, large subunit
IPR009081 Acyl carrier protein-like
IPR006162 Phosphopantetheine attachment site
IPR001031 Thioesterase
IPR006163 Phosphopantetheine-binding
IPR010071 Amino acid adenylation
IPR000873 AMP-dependent synthetase/ligase
IPR020806 Polyketide synthase, phosphopantetheine-binding
PDB Chain
ModBase
CATH Domain
SWISS-MODEL
SCOP Domain

PublicationsHelp
1. Konz D, Marahiel MA.
How do peptide synthetases generate structural diversity?
Chem. Biol. 6 R39-48 1999 [PubMed: 10021423]
http://dx.doi.org/10.1016/S1074-5521(99)80002-7

Additional ReadingHelp
Conti E, Stachelhaus T, Marahiel MA, Brick P.
Structural basis for the activation of phenylalanine in the non-ribosomal biosynthesis of gramicidin S.
EMBO J. 16 1997 4174-83 [PubMed: 9250661]
http://dx.doi.org/10.1093/emboj/16.14.4174
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InterPro 23.1