Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.7.7.1 - nicotinamide-nucleotide adenylyltransferase and Organism(s) Synechocystis sp. and UniProt Accession Q55928

for references in articles please use BRENDA:EC2.7.7.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Nicotinate nucleotide can also act as acceptor. See also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Synechocystis sp.
UNIPROT: Q55928
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Synechocystis sp.
The enzyme appears in selected viruses and cellular organisms
Synonyms
nmnat2, nmnat, nmnat1, nmnat3, nicotinamide mononucleotide adenylyltransferase, nmn adenylyltransferase, nicotinamide mononucleotide adenylyltransferase 1, nicotinamide mononucleotide adenylyltransferase 2, namnat, hnmnat-2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NMN adenylyltransferase/ADP-ribose pyrophosphatase
-
adenosine triphosphate-nicotinamide mononucleotide transadenylase
-
-
-
-
adenylyltransferase, nicotinamide mononucleotide
-
-
-
-
ATP:NMN adenylyltransferase
-
-
-
-
diphosphopyridine nucleotide pyrophosphorylase
-
-
-
-
NAD+ pyrophosphorylase
-
-
-
-
NadM-Nudix
-
-
nicotinamide adenine dinucleotide pyrophosphorylase
-
-
-
-
nicotinamide mononucleotide adenylyltransferase
-
-
-
-
nicotinamide/nicotinic acid mononucleotide adenylyltransferase
-
nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase
NMN adenylyltransferase
-
-
-
-
NMNAT
PNAT
-
-
-
-
pyridine nucleotide adenylyltransferase
-
-
-
-
additional information
the enzyme belongs to the (H/T)IGH motif containing nucleotidyltransferase superfamily, NadM family, bacterial NadM-Nudix subfamily
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + nicotinamide ribonucleotide = diphosphate + NAD+
show the reaction diagram
catalytic mechanism, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
-
-
nucleotidyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
ATP:nicotinamide-nucleotide adenylyltransferase
Nicotinate nucleotide can also act as acceptor. See also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-70-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + NMN
diphosphate + NAD+
show the reaction diagram
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
show the reaction diagram
-
-
-
-
r
ATP + nicotinic acid mononucleotide
diphosphate + nicotinic acid adenine dinucleotide
show the reaction diagram
-
-
-
-
r
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
ATP + NMN
diphosphate + NAD+
show the reaction diagram
the enzyme from Synechocystis sp. is primarily involved in NAD savage/recycling pathways
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
steady state kinetics
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
NMNAT appears to be a multifunctional protein that sits both at the core of central metabolism and at the crossroads of multiple cellular processes
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
syNadM-Nudix forms hexamer in both crystal and solution with two types of dimer interfaces, the dimer interface is formed primarily through ADPRase domain of each monomer, overview
oligomer
-
-
additional information
bacterial NadM-Nudix is a bifunctional enzyme containing a nicotinamide mononucleotide adenylyltransferase and an ADP-ribose diphosphatase domain, structures of the N-terminal NadM domain and ADPR domain, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the enzyme is complexed with the co-purified NAD and pyrophosphate in the NadM-domain active site, and with ADPR substrate in the Nudix-domain, X-ray diffraction structure determination and analysis at 2.6 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Huang, N.; Sorci, L.; Zhang, X.; Brautigam, C.A.; Li, X.; Raffaelli, N.; Magni, G.; Grishin, N.V.; Osterman, A.L.; Zhang, H.
Bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase: structure and function in bacterial NAD metabolism
Structure
16
196-209
2008
Francisella tularensis (Q5NHR1), Synechocystis sp. (Q55928)
Manually annotated by BRENDA team
Zhai, R.G.; Rizzi, M.; Garavaglia, S.
Nicotinamide/nicotinic acid mononucleotide adenylyltransferase, new insights into an ancient enzyme
Cell. Mol. Life Sci.
66
2805-2818
2009
Synechocystis sp., Bacillus anthracis, Escherichia coli, Haemophilus influenzae, Homo sapiens, Staphylococcus aureus, Pseudomonas aeruginosa, Methanothermobacter thermautotrophicus (O26253), Methanocaldococcus jannaschii (Q57961)
Manually annotated by BRENDA team