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Information on EC 3.5.1.42 - nicotinamide-nucleotide amidase

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EC Tree
IUBMB Comments
Also acts more slowly on beta-nicotinamide D-ribonucleoside.
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This record set is specific for:
UNIPROT: Q5SHB0
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Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
nmn deamidase, nicotinamide mononucleotide deamidase, atcina, oipncc, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nicotinamide mononucleotide amidohydrolase
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nicotinamide mononucleotide deamidase
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nicotinamide mononucleotide deaminase
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nicotinamide nucleoside amidase
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NMN deaminase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
beta-nicotinamide D-ribonucleotide + H2O = beta-nicotinate D-ribonucleotide + NH3
show the reaction diagram
catalytic mechanism, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic acid amide
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
nicotinamide-D-ribonucleotide amidohydrolase
Also acts more slowly on beta-nicotinamide D-ribonucleoside.
CAS REGISTRY NUMBER
COMMENTARY hide
37355-58-1
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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
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
show the reaction diagram
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?
additional information
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
show the reaction diagram
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?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene cinA
UniProt
Manually annotated by BRENDA team
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
gene cinA
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme's N-terminal domain belongs to the COG1058 family and is associated with the ADP-ribose pyrophosphatase activity
metabolism
the enzyme is associated with natural competence and is proposed to have a function as an enzyme participating in the pyridine nucleotide cycle, which recycles products formed by non-redox uses of NAD+
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q5SHB0_THET8
Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
394
0
42915
TrEMBL
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
an unusual asymmetric dimer, with three domains for each chain, the C-terminal domain harbors the nicotinamide mononucleotide deamidase activity. The asymmetry in the CinA dimer arises from two alternative orientations of the N-terminal COG1058 domains, only one of which forms a contact with the KH-type domain from the other chain, effectively closing the active site into, we propose, a catalytically competent state
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant detagged enzyme free or in complex with nicotinate mononucleotide, or AMP/Mg2+, or ATP/Mg2+, or ribose-ADP/Mg2+, sitting drop vapor diffusion, mixing of 200 nl of protein with 200 nl of well solution containing 0.2 M Na2SO4, 0.1 M Bis-Tris propane, pH 6.5, and 20% w/v, PEG 3350 at 20°C, rodlike crystals, 5-7 days, X-ray diffraction structure determination and analysis at 1.98-2.46 A resolution, molecular replacement and modeling
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli strain T7 by nickel affinity chromatgraphy, cleavage of the tag by thrombin, anion exchange chromatography, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene cinA, recombinant expression of His6-tagged enzyme with a thrombin cleavage site at the N terminus in Escherichia coli strain T7
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Karuppiah, V.; Thistlethwaite, A.; Dajani, R.; Warwicker, J.; Derrick, J.P.
Structure and mechanism of the bifunctional CinA enzyme from Thermus thermophilus
J. Biol. Chem.
289
33187-33197
2014
Thermus thermophilus (Q5SHB0), Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q5SHB0)
Manually annotated by BRENDA team