A0A0H3MPU9 · A0A0H3MPU9_MYCLB

Function

function

Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.

Catalytic activity

Pathway

Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site74-76L-glutamine (UniProtKB | ChEBI)
Active site106Nucleophile
Binding site138L-glutamine (UniProtKB | ChEBI)
Binding site166-167L-glutamine (UniProtKB | ChEBI)
Active site202
Active site202Charge relay system
Active site204
Active site204Charge relay system

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentglutaminase complex
Molecular Functionglutaminase activity
Molecular Functionpyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
Biological Processglutamine catabolic process
Biological Processpyridoxal phosphate biosynthetic process
Biological Processpyridoxine metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Pyridoxal 5'-phosphate synthase subunit PdxT
  • EC number
  • Alternative names
    • Pdx2
    • Pyridoxal 5'-phosphate synthase glutaminase subunit
      (EC:3.5.1.2
      ) . EC:3.5.1.2 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      pdxT
    • Ordered locus names
      MLBr00474

Organism names

Accessions

  • Primary accession
    A0A0H3MPU9

Proteomes

Subcellular Location

Interaction

Subunit

In the presence of PdxS, forms a dodecamer of heterodimers. Only shows activity in the heterodimer.

Family & Domains

Sequence similarities

Belongs to the glutaminase PdxT/SNO family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    223
  • Mass (Da)
    23,704
  • Last updated
    2015-09-16 v1
  • Checksum
    8EB675A7CB74E95B
MAAVMQEGLIRFPAGYPADSAVERVVSFPRVGVLALQGDTREHLTALREAGADSMPVRRRGELDEVDALVIPGGESTTISHLLLDCELLEPLRARLADGLPAYGACTGMILLASEILDAGVCGREALPLGAIDITVRRNAFGRQVDSFEGDIGFAGLVDPVRAVFIRAPWVERAGDGVQVLAQAAGHAVAVRQGSMLATAFHPEMTSDRRIHQLFVDIVNGIA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FM211192
EMBL· GenBank· DDBJ
CAR70567.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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