A0A369P426 · A0A369P426_9ACTN
- ProteinMultifunctional fusion protein
- GenemurT
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids756 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
The lipid II isoglutaminyl synthase complex catalyzes the formation of alpha-D-isoglutamine in the cell wall lipid II stem peptide. The GatD subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia. The resulting ammonia molecule is channeled to the active site of MurT.
The lipid II isoglutaminyl synthase complex catalyzes the formation of alpha-D-isoglutamine in the cell wall lipid II stem peptide. The MurT subunit catalyzes the ATP-dependent amidation of D-glutamate residue of lipid II, converting it to an isoglutamine residue.
Catalytic activity
- beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + L-glutamine + ATP + H2O = beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-D-isoglutaminyl-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + L-glutamate + ADP + phosphate + H+
- beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + ATP = beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-O-P-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + ADP
- beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-O-P-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + NH4+ = beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-D-isoglutaminyl-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + phosphate + H+
Pathway
Cell wall biogenesis; peptidoglycan biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 205 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 208 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 227 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 230 | Zn2+ (UniProtKB | ChEBI) | |||
Active site | 358 | ||||
Active site | 601 | Nucleophile | |||
Binding site | 637 | substrate | |||
Active site | 703 | ||||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | acid-amino acid ligase activity | |
Molecular Function | ATP binding | |
Molecular Function | carbon-nitrogen ligase activity on lipid II | |
Molecular Function | glutaminase activity | |
Molecular Function | zinc ion binding | |
Biological Process | cell wall organization | |
Biological Process | cobalamin biosynthetic process | |
Biological Process | glutamine metabolic process | |
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 nameMultifunctional fusion protein
Including 2 domains:
- Recommended nameLipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit GatD
- EC number
- Alternative names
- Recommended nameLipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurT
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Coriobacteriia > Eggerthellales > Eggerthellaceae > Adlercreutzia
Accessions
- Primary accessionA0A369P426
Proteomes
Interaction
Subunit
Forms a heterodimer with GatD.
Forms a heterodimer with MurT.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 59-192 | Mur ligase central | |||
Domain | 322-436 | Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurT C-terminal | |||
Region | 465-505 | Disordered | |||
Domain | 513-710 | CobB/CobQ-like glutamine amidotransferase | |||
Sequence similarities
Belongs to the CobB/CobQ family. GatD subfamily.
Belongs to the MurCDEF family. MurT subfamily.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length756
- Mass (Da)80,647
- Last updated2018-11-07 v1
- ChecksumCF496B5E2C9CA5B3
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
PPUT01000005 EMBL· GenBank· DDBJ | RDC45995.1 EMBL· GenBank· DDBJ | Genomic DNA |