A0A1H5SQN7 · A0A1H5SQN7_9CLOT
- ProteinD-alanine--D-alanine ligase
- Geneddl
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids393 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Cell wall formation.
Catalytic activity
- ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H+ + phosphate
Cofactor
Protein has several cofactor binding sites:
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Binds 2 magnesium or manganese ions per subunit.
Pathway
Cell wall biogenesis; peptidoglycan biosynthesis.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 16 | |||||
Sequence: E | ||||||
Binding site | 145 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 190-192 | ATP (UniProtKB | ChEBI) | ||||
Sequence: FVK | ||||||
Active site | 198 | |||||
Sequence: S | ||||||
Binding site | 198-199 | ATP (UniProtKB | ChEBI) | ||||
Sequence: SS | ||||||
Binding site | 228-236 | ATP (UniProtKB | ChEBI) | ||||
Sequence: EEAVNNPME | ||||||
Binding site | 317 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 330-331 | ATP (UniProtKB | ChEBI) | ||||
Sequence: NE | ||||||
Binding site | 331 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 331 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 333 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Active site | 340 | |||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | D-alanine-D-alanine ligase activity | |
Molecular Function | metal ion binding | |
Biological Process | cell wall organization | |
Biological Process | peptidoglycan biosynthetic process | |
Biological Process | regulation of cell shape |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameD-alanine--D-alanine ligase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Eubacteriales > Clostridiaceae > Caloramator
Accessions
- Primary accessionA0A1H5SQN7
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 149-360 | ATP-grasp | ||||
Sequence: KDIFKANGIPIVNYTWFLRKDYINDSEKVLKHIEEKLKYPMFVKPANLGSSIGISKAKNREELINAIEIAINYDRKVIVEEAVNNPMEINCSVIGFDNDYQASVLEQPVSWQEFLSFEDKYLRGNKNSGMKSAERRIPAPIEDAKASEIKELAIKVFKCLDCSGISRIDFLVEKDTMKIYVNEINTMPGSISFYLWEPTGIKFKDLIDKLIG |
Sequence similarities
Belongs to the D-alanine--D-alanine ligase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length393
- Mass (Da)44,628
- Last updated2017-01-18 v1
- Checksum7BDC940301E4A9CB
Keywords
- Technical term