A0A0G0USN4 · A0A0G0USN4_9BACT

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis.
Purine metabolism; purine nucleoside salvage.

Features

Showing features for binding site, site.

TypeIDPosition(s)Description
Binding site19phosphate (UniProtKB | ChEBI)
Binding site61-62phosphate (UniProtKB | ChEBI)
Binding site94-95phosphate (UniProtKB | ChEBI)
Site173Important for substrate specificity
Binding site191substrate
Binding site192phosphate (UniProtKB | ChEBI)
Binding site215-217substrate
Site228Important for substrate specificity
Binding site402-408ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular FunctionS-methyl-5-thioadenosine phosphorylase activity
Molecular FunctionUDP-N-acetylmuramate-L-alanine ligase activity
Biological Processcell division
Biological Processcell wall organization
Biological Processpeptidoglycan biosynthetic process
Biological Processpurine ribonucleoside salvage
Biological Processregulation of cell shape

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Multifunctional fusion protein

Including 2 domains:

  • Recommended name
    UDP-N-acetylmuramate--L-alanine ligase
  • EC number
  • Alternative names
    • UDP-N-acetylmuramoyl-L-alanine synthetase
  • Recommended name
    Purine nucleoside phosphorylase
  • EC number
  • Short names
    PNP

Gene names

    • Name
      murC
    • ORF names
      UU43_C0002G0042

Organism names

Accessions

  • Primary accession
    A0A0G0USN4

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homohexamer. Dimer of a homotrimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain12-250Nucleoside phosphorylase
Domain294-396Mur ligase N-terminal catalytic
Domain400-591Mur ligase central
Domain613-759Mur ligase C-terminal

Sequence similarities

Belongs to the MurCDEF family.
Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    771
  • Mass (Da)
    86,035
  • Last updated
    2015-07-22 v1
  • Checksum
    0B4D3664D4676934
MNNNLINMNKIKIAIIGGSGLDDPGILKNAKKVNLATPFGATAAPLICGQIDGVDMVVLARHGINHTFMPTKVPYRANIWALKEIGCTHIIATTACGSLQEKIKPRDLIFLDQFIDFTKHRNLTFFEDKVVHTAMADPFCPDLREILIKTAEELKFAHHKQGTIITIEGPRFSTRAESRFFKQMGADVINMSTVPEVILAREVGICYGSVAMATDYDAWRKDEKAVTWGMVMQVMKDNTNNVVKLLLNIIPKIALELADEECENCGYIRSEKITNCKPPPNRFYIYMDLNKIKKIYLIGIKGVGMTMLAQYLVGQNIDVSGSDGPEKYMTDAVLKKCGIKIIEKFDAKNIPHDADLIIYSTAYNAETNVEVAVALAGKIKIMTYAQALGETFNQKYGIAVVGSHGKTTTTAWLGYVMKMSGLGPSVMAGAPVPQFDGCSISGQADYLVIEADEYQNKLQYYQPKAVLLNNIDYDHPDFFPTATDYENTYIEFIKKIPAKGFLVANFDDSLIRKIAQVNCRGKVITYAIDETADYVAFDLKANNGKQYFKVKLEVEDELDEEETRVEELGGFSIQLAGRHNILNALAVIATAIELNIELFKIRKYLAEFTGTARRMQALGEFRGATVIDDYAHHPTEIKATVSAVRQKYGSRKLMVAFQPHTFSRTKALFNDFVKSFAQVDELIILDIYGSAREKPGGAHSRDLAEKIRIRNQESLRRQGFGGQAGIRQTVKYISTLAECERYLRDRVERNDVVVLMGAGDIFRVGENLVKG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LCAP01000002
EMBL· GenBank· DDBJ
KKR91733.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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