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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.7.7.18 - nicotinate-nucleotide adenylyltransferase and Organism(s) Pseudomonas aeruginosa and UniProt Accession Q9HX21

for references in articles please use BRENDA:EC2.7.7.18
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Pseudomonas aeruginosa
UNIPROT: Q9HX21 not found.
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: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
nicotinate mononucleotide adenylyltransferase, nicotinic acid mononucleotide adenylyltransferase, pfnmnat, namn at, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nicotinic acid mononucleotide adenylyltransferase
-
adenylyltransferase, nicotinate mononucleotide
-
-
-
-
deamido-NAD+ pyrophosphorylase
-
-
-
-
deamidonicotinamide adenine dinucleotide pyrophosphorylase
-
-
-
-
NaMN AT
-
-
-
-
NaMN-ATase
-
-
-
-
nicotinamide/nicotinic acid mononucleotide adenylyltransferase
-
-
nicotinic acid mononucleotide adenylyltransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:nicotinate-ribonucleotide adenylyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9026-98-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
show the reaction diagram
-
-
-
-
r
ATP + nicotinic acid mononucleotide
nicotinic acid adenine dinucleotide + diphosphate
show the reaction diagram
-
-
-
-
r
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of NaMN-bound form at 1.7 A, ATP-bound form at 2.0 A, apo-form at 2.0 A. The substrate-unbound and substrate-complexed structures are all in the fully open conformation. There is little conformational change upon binding each of the substrates. A conformational change is necessary to bring the two substrates closer together for initiating the catalysis. The authors suggest that such a conformational change likely occurs only after both substrates are simultaneously bound in the active site
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yoon, H.J.; Kim, H.L.; Mikami, B.; Suh, S.W.
Crystal structure of nicotinic acid mononucleotide adenylyltransferase from Pseudomonas aeruginosa in its Apo and substrate-complexed forms reveals a fully open conformation
J. Mol. Biol.
351
258-265
2005
Pseudomonas aeruginosa (Q9HX21), Pseudomonas aeruginosa
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
Bacillus anthracis, Escherichia coli, Homo sapiens, Pseudomonas aeruginosa
Manually annotated by BRENDA team