CPLM-019993

Genbank Nucleotide ID

Peroxisomal coenzyme A diphosphatase NUDT7

Protein Synonyms/Alias

Nucleoside diphosphate-linked moiety X motif 7; Nudix motif 7

Mus musculus (Mouse)

Position	Peptide	Type	References
20	NNLIDDAKARLRKSD	acetylation	[1]
20	NNLIDDAKARLRKSD	succinylation	[1]
20	NNLIDDAKARLRKSD	ubiquitination	[2]
65	TVRSDKLKREPGEVC	acetylation	[3]
65	TVRSDKLKREPGEVC	ubiquitination	[2]
77	EVCFPGGKRDPVDTD	acetylation	[1, 3, 4]
77	EVCFPGGKRDPVDTD	succinylation	[1]
178	IMHCFEYKDPETGVN	acetylation	[1]
178	IMHCFEYKDPETGVN	succinylation	[1]

[1] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
[2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
[3] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
[4] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
J Biol Chem. 2013 Jul 17;. [PMID: 23864654]

Functional Description

Coenzyme A diphosphatase which mediates the cleavage of CoA, CoA esters and oxidized CoA with similar efficiencies, yielding 3',5'-ADP and the corresponding 4'-phosphopantetheine derivative as products. CoA into 3',5'-ADP and 4'- phosphopantetheine. Has no activity toward NDP-sugars, CDP- alcohols, (deoxy)nucleoside 5'-triphosphates, nucleoside 5'-di or monophosphates, diadenosine polyphosphates, NAD, NADH, NADP, NADPH or thymidine-5'-monophospho-p-nitrophenyl ester. May be required to eliminate oxidized CoA from peroxisomes, or regulate CoA and acyl-CoA levels in this organelle in response to metabolic demand. Does not play a role in U8 snoRNA decapping activity. Binds U8 snoRNA.

DOMAIN 37 169 Nudix hydrolase.
MOTIF 77 98 Nudix box.
MOTIF 234 236 Microbody targeting signal (Probable).
METAL 92 92 Magnesium or manganese (By similarity).
METAL 96 96 Magnesium or manganese (By similarity).

Alternative splicing; Complete proteome; Hydrolase; Magnesium; Manganese; Metal-binding; Peroxisome; Reference proteome; RNA-binding.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005777; C:peroxisome; IDA:UniProtKB.
GO:0003986; F:acetyl-CoA hydrolase activity; IDA:MGI.
GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO:0030145; F:manganese ion binding; IEA:InterPro.
GO:0030515; F:snoRNA binding; IDA:UniProtKB.
GO:0046356; P:acetyl-CoA catabolic process; IDA:MGI.
GO:0050873; P:brown fat cell differentiation; IDA:MGI.
GO:0015938; P:coenzyme A catabolic process; IDA:MGI.
GO:0009132; P:nucleoside diphosphate metabolic process; IEA:InterPro.

IPR000086; NUDIX_hydrolase_dom.
IPR015797; NUDIX_hydrolase_dom-like.
IPR000059; NUDIX_hydrolase_NudL_CS.

PS51462; NUDIX
PS00893; NUDIX_BOX
PS01293; NUDIX_COA