A0A0G0USN4 · A0A0G0USN4_9BACT
- ProteinMultifunctional fusion protein
- GenemurC
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids771 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Cell wall formation.
Purine nucleoside phosphorylase involved in purine salvage.
Miscellaneous
Although this enzyme belongs to the family of MTA phosphorylases based on sequence homology, it lacks several conserved amino acids in the substrate binding pocket that confer specificity towards MTA.
Catalytic activity
- ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H+ + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
Pathway
Cell wall biogenesis; peptidoglycan biosynthesis.
Purine metabolism; purine nucleoside salvage.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 19 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 61-62 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: RH | ||||||
Binding site | 94-95 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: TA | ||||||
Site | 173 | Important for substrate specificity | ||||
Sequence: S | ||||||
Binding site | 191 | substrate | ||||
Sequence: M | ||||||
Binding site | 192 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 215-217 | substrate | ||||
Sequence: DYD | ||||||
Site | 228 | Important for substrate specificity | ||||
Sequence: W | ||||||
Binding site | 402-408 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GSHGKTT |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | S-methyl-5-thioadenosine phosphorylase activity | |
Molecular Function | UDP-N-acetylmuramate-L-alanine ligase activity | |
Biological Process | cell division | |
Biological Process | cell wall organization | |
Biological Process | peptidoglycan biosynthetic process | |
Biological Process | purine ribonucleoside salvage | |
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 nameUDP-N-acetylmuramate--L-alanine ligase
- EC number
- Alternative names
- Recommended namePurine nucleoside phosphorylase
- EC number
- Short namesPNP
Gene names
Organism names
- Taxonomic lineageBacteria > Candidatus Falkowbacteria
Accessions
- Primary accessionA0A0G0USN4
Proteomes
Subcellular Location
Interaction
Subunit
Homohexamer. Dimer of a homotrimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 12-250 | Nucleoside phosphorylase | ||||
Sequence: KIAIIGGSGLDDPGILKNAKKVNLATPFGATAAPLICGQIDGVDMVVLARHGINHTFMPTKVPYRANIWALKEIGCTHIIATTACGSLQEKIKPRDLIFLDQFIDFTKHRNLTFFEDKVVHTAMADPFCPDLREILIKTAEELKFAHHKQGTIITIEGPRFSTRAESRFFKQMGADVINMSTVPEVILAREVGICYGSVAMATDYDAWRKDEKAVTWGMVMQVMKDNTNNVVKLLLNII | ||||||
Domain | 294-396 | Mur ligase N-terminal catalytic | ||||
Sequence: KIYLIGIKGVGMTMLAQYLVGQNIDVSGSDGPEKYMTDAVLKKCGIKIIEKFDAKNIPHDADLIIYSTAYNAETNVEVAVALAGKIKIMTYAQALGETFNQKY | ||||||
Domain | 400-591 | Mur ligase central | ||||
Sequence: VVGSHGKTTTTAWLGYVMKMSGLGPSVMAGAPVPQFDGCSISGQADYLVIEADEYQNKLQYYQPKAVLLNNIDYDHPDFFPTATDYENTYIEFIKKIPAKGFLVANFDDSLIRKIAQVNCRGKVITYAIDETADYVAFDLKANNGKQYFKVKLEVEDELDEEETRVEELGGFSIQLAGRHNILNALAVIATA | ||||||
Domain | 613-759 | Mur ligase C-terminal | ||||
Sequence: RRMQALGEFRGATVIDDYAHHPTEIKATVSAVRQKYGSRKLMVAFQPHTFSRTKALFNDFVKSFAQVDELIILDIYGSAREKPGGAHSRDLAEKIRIRNQESLRRQGFGGQAGIRQTVKYISTLAECERYLRDRVERNDVVVLMGAG |
Sequence similarities
Belongs to the MurCDEF family.
Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length771
- Mass (Da)86,035
- Last updated2015-07-22 v1
- Checksum0B4D3664D4676934
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LCAP01000002 EMBL· GenBank· DDBJ | KKR91733.1 EMBL· GenBank· DDBJ | Genomic DNA |