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Information on EC 3.6.1.13 - ADP-ribose diphosphatase

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EC Tree
     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.1 In phosphorus-containing anhydrides
                3.6.1.13 ADP-ribose diphosphatase
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UNIPROT: Q5SHB0 not found.
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The enzyme appears in viruses and cellular organisms
Synonyms
nudt5, nudt9, adp-ribose pyrophosphatase, adprase, atnudt7, adpribase-mn, atnudx7, adp-ribose hydrolase, nudt5 protein, adpr pyrophosphatase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
adenosine diphosphoribose pyrophosphatase
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ADP-ribose diphosphatase
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ADP-ribose phosphohydrolase
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ADP-ribose pyrophosphatase
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ADPR-PPase
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ADPRibase
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ADPribose pyrophosphatase
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pyrophosphatase, adenosine diphosphoribose
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphorous acid anhydride hydrolysis
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
ADP-D-ribose ribophosphohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
9024-83-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme displays both nicotinamide mononucleotide deamidase and ADP-ribose diphosphatase activities
UniProt
Manually annotated by BRENDA team
enzyme displays both nicotinamide mononucleotide deamidase and ADP-ribose diphosphatase activities
UniProt
Manually annotated by BRENDA team
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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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 2.16 A resolution. The crystal structure shows an unusual asymmetric dimer, with three domains for each chain. The C-terminal domain harbors the nicotinamide mononucleotide deamidase activity. The N-terminal domain belongs to the COG1058 family and is associated with the ADP-ribose diphosphatase activity. The mechanism for the ADP-ribose diphosphatase reaction involves a rotation of the COG1058 domain dimer as part of the reaction cycle
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 DSM 579 (Q5SHB0)
Manually annotated by BRENDA team