P22253 · PNCB_SALTY

Function

function

Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP.

Catalytic activity

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
1.5 μMnicotinate in the presence of ATP
0.3 mMnicotinate in the absence of ATP
22 μM5-phospho-alpha-D-ribose 1-diphosphate in the presence of ATP
4.5 mM5-phospho-alpha-D-ribose 1-diphosphate in the absence of ATP

Pathway

Cofactor biosynthesis; NAD+ biosynthesis; nicotinate D-ribonucleotide from nicotinate: step 1/1.

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionnicotinate phosphoribosyltransferase activity
Biological Processbioluminescence
Biological ProcessNAD salvage

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Nicotinate phosphoribosyltransferase
  • EC number
  • Short names
    NAPRTase

Gene names

    • Name
      pncB
    • Ordered locus names
      STM1004

Organism names

Accessions

  • Primary accession
    P22253

Proteomes

Subcellular Location

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis220Loss of ATP hydrolysis and autophosphorylation.

PTM/Processing

Features

Showing features for initiator methionine, chain, modified residue.

Type
IDPosition(s)Description
Initiator methionine1Removed
ChainPRO_00002058462-400Nicotinate phosphoribosyltransferase
Modified residue220Phosphohistidine; by autocatalysis

Post-translational modification

Transiently phosphorylated on a His residue during the reaction cycle (PubMed:9521740).
Phosphorylation strongly increases the affinity for substrates and increases the rate of nicotinate D-ribonucleotide production. Dephosphorylation regenerates the low-affinity form of the enzyme, leading to product release (PubMed:7503993, PubMed:9521740, PubMed:9521741).

Keywords

Proteomic databases

PTM databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the NAPRTase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    400
  • Mass (Da)
    45,661
  • Last updated
    2007-01-23 v2
  • Checksum
    BA76FF5EF0D02F3A
MTQFASPVLHSLLDTDAYKLHMQQAVFHHYYDVQVAAEFRCRGDDLLGIYADAIREQVDAMQHLRLLEDEFQWLSGLPFFKPDYLNWLREFRYNPAQVCVTNDNGKLNIRLTGPWREVIMWEVPLLAVISELVHHYRSPNAGVDQALDALESKLVDFTALTANLDMSRFHLMDFGTRRRFSREVQQAIVKRLQQESWFVGTSNYDLARRLALTPMGTQAHEWFQAHQQISPDLATSQRAALAAWLNEYPDQLGIALTDCITMDAFLRDFGIEFASRYQGLRHDSGDPVAWGEKAIAHYEKLGIDPLTKTLVFSDNLDLPKAVELYRHFASRVQLSFGIGTRLTCDIPQVKPLNIVIKLVECNGKPVAKLSDSPGKTICHDKAFVRALRKAFDLPQVRKAS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M55986
EMBL· GenBank· DDBJ
AAA27190.1
EMBL· GenBank· DDBJ
Genomic DNA
AE006468
EMBL· GenBank· DDBJ
AAL19938.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help