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Information on EC 6.3.4.21 - nicotinate phosphoribosyltransferase and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WJW5

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EC Tree
     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.4 Other carbon-nitrogen ligases
                6.3.4.21 nicotinate phosphoribosyltransferase
IUBMB Comments
The enzyme, which is involved in pyridine nucleotide recycling, can form beta-nicotinate D-ribonucleotide and diphosphate from nicotinate and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) in the absence of ATP. However, when ATP is available the enzyme is phosphorylated resulting in a much lower Km for nicotinate. The phospho-enzyme is hydrolysed during the transferase reaction, regenerating the low affinity form. The presence of ATP shifts the products/substrates equilibrium from 0.67 to 1100 .
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Mycobacterium tuberculosis
UNIPROT: P9WJW5
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Word Map
The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The enzyme appears in selected viruses and cellular organisms
Synonyms
nicotinic acid phosphoribosyltransferase, nicotinate phosphoribosyltransferase, naprtase, naprt1, na phosphoribosyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
niacin ribonucleotidase
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nicotinate-nucleotide:pyrophosphate phospho-alpha-D-ribosyltransferase
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nicotinic acid mononucleotide glycohydrolase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentosyl group transfer
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PATHWAY SOURCE
PATHWAYS
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-, -, -
SYSTEMATIC NAME
IUBMB Comments
5-phospho-alpha-D-ribose 1-diphosphate:nicotinate ligase (ADP, diphosphate-forming)
The enzyme, which is involved in pyridine nucleotide recycling, can form beta-nicotinate D-ribonucleotide and diphosphate from nicotinate and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) in the absence of ATP. However, when ATP is available the enzyme is phosphorylated resulting in a much lower Km for nicotinate. The phospho-enzyme is hydrolysed during the transferase reaction, regenerating the low affinity form. The presence of ATP shifts the products/substrates equilibrium from 0.67 to 1100 [4].
CAS REGISTRY NUMBER
COMMENTARY hide
9030-26-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
show the reaction diagram
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Grubmeyer, C.T.; Gross, J.W.; Rajavel, M.
Energy coupling through molecular discrimination: nicotinate phosphoribosyltransferase
Methods Enzymol.
308
28-48
1999
Mycobacterium tuberculosis (P9WJW5), Mycobacterium tuberculosis H37Rv (P9WJW5), Saccharomyces cerevisiae, Saccharomyces cerevisiae (P39683), Salmonella enterica subsp. enterica serovar Typhimurium (P22253)
Manually annotated by BRENDA team