ID NUDT7_HUMAN Reviewed; 238 AA. AC P0C024; B4DLE5; H3BUB8; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 1. DT 27-MAR-2024, entry version 142. DE RecName: Full=Peroxisomal coenzyme A diphosphatase NUDT7 {ECO:0000305}; DE EC=3.6.1.-; DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 7; DE Short=Nudix motif 7; GN Name=NUDT7 {ECO:0000312|HGNC:HGNC:8054}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA Hong J.; RT "The transcript variant 2 encodes a short isoform for Homo sapiens nudix RT (nucleoside diphosphate linked moiety X)-type motif 7 (NUDT7)."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Tongue; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP TISSUE SPECIFICITY. RX PubMed=11415433; DOI=10.1042/0264-6021:3570033; RA Gasmi L., McLennan A.G.; RT "The mouse Nudt7 gene encodes a peroxisomal nudix hydrolase specific for RT coenzyme A and its derivatives."; RL Biochem. J. 357:33-38(2001). RN [6] {ECO:0007744|PDB:5T3P} RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 1-235. RA Srikannathasan V.; RT "Crystal structure of Human Peroxisomal coenzyme A diphosphatase NUDT7."; RL Submitted (AUG-2016) to the PDB data bank. RN [7] {ECO:0007744|PDB:5QGG, ECO:0007744|PDB:5QHH} RP X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 14-209. RA Krojer T., Talon R., Fairhead M., Diaz Saez L., Bradley A.R., Aimon A., RA Collins P., Brandao-Neto J., Douangamath A., Ruda G.F., Szommer T., RA Srikannathasan V., Elkins J., Spencer J., London N., Nelson A., RA Brennan P.E., Huber K., Bountra C., Arrowsmith C.H., Edwards A., RA von Delft F.; RT "PanDDA analysis group deposition of models with modelled events (e.g. RT bound ligands)."; RL Submitted (MAY-2018) to the PDB data bank. CC -!- FUNCTION: Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes CC fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'- CC bisphosphate (By similarity). Cleaves CoA, CoA esters and oxidized CoA CC with similar efficiencies (By similarity). Preferentially hydrolyzes CC medium-chain acyl-CoAs and bile acid-CoAs (By similarity). Has no CC activity toward NDP-sugars, CDP-alcohols, (deoxy)nucleoside 5'- CC triphosphates, nucleoside 5'-di or monophosphates, diadenosine CC polyphosphates, NAD, NADH, NADP, NADPH or thymidine-5'-monophospho-p- CC nitrophenyl ester (By similarity). May be required to eliminate CC oxidized CoA from peroxisomes, or regulate CoA and acyl-CoA levels in CC this organelle in response to metabolic demand (By similarity). Does CC not play a role in U8 snoRNA decapping activity (By similarity). Binds CC U8 snoRNA (By similarity). Exhibits decapping activity towards dpCoA- CC capped RNAs in vitro (By similarity). {ECO:0000250|UniProtKB:Q99P30}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + hexanoyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+) + CC hexanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:49980, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58343, CC ChEBI:CHEBI:62620, ChEBI:CHEBI:132012; CC Evidence={ECO:0000250|UniProtKB:Q99P30}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49981; CC Evidence={ECO:0000250|UniProtKB:Q99P30}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + octanoyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+) + CC S-octanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:50016, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57386, CC ChEBI:CHEBI:58343, ChEBI:CHEBI:132013; CC Evidence={ECO:0000250|UniProtKB:Q99P30}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50017; CC Evidence={ECO:0000250|UniProtKB:Q99P30}; CC -!- CATALYTIC ACTIVITY: CC Reaction=butanoyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2 H(+) + CC S-butanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:49976, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57371, CC ChEBI:CHEBI:58343, ChEBI:CHEBI:132011; CC Evidence={ECO:0000250|UniProtKB:Q99P30}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49977; CC Evidence={ECO:0000250|UniProtKB:Q99P30}; CC -!- CATALYTIC ACTIVITY: CC Reaction=decanoyl-CoA + H2O = adenosine 3',5'-bisphosphate + decanoyl- CC 4'-phosphopantetheine + 2 H(+); Xref=Rhea:RHEA:50020, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58343, CC ChEBI:CHEBI:61430, ChEBI:CHEBI:132014; CC Evidence={ECO:0000250|UniProtKB:Q99P30}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50021; CC Evidence={ECO:0000250|UniProtKB:Q99P30}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dodecanoyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2 H(+) + CC S-dodecanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:50024, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57375, CC ChEBI:CHEBI:58343, ChEBI:CHEBI:132015; CC Evidence={ECO:0000250|UniProtKB:Q99P30}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50025; CC Evidence={ECO:0000250|UniProtKB:Q99P30}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + tetradecanoyl-CoA = adenosine 3',5'-bisphosphate + 2 CC H(+) + tetradecanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:50028, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57385, CC ChEBI:CHEBI:58343, ChEBI:CHEBI:132017; CC Evidence={ECO:0000250|UniProtKB:Q99P30}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50029; CC Evidence={ECO:0000250|UniProtKB:Q99P30}; CC -!- CATALYTIC ACTIVITY: CC Reaction=choloyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2 H(+) + S- CC choloyl-4'-phosphopantetheine; Xref=Rhea:RHEA:50036, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57373, CC ChEBI:CHEBI:58343, ChEBI:CHEBI:132020; CC Evidence={ECO:0000250|UniProtKB:Q99P30}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50037; CC Evidence={ECO:0000250|UniProtKB:Q99P30}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + CC H2O = 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-4'- CC phosphopantetheine + adenosine 3',5'-bisphosphate + 2 H(+); CC Xref=Rhea:RHEA:50040, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:58343, ChEBI:CHEBI:63001, ChEBI:CHEBI:132021; CC Evidence={ECO:0000250|UniProtKB:Q99P30}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50041; CC Evidence={ECO:0000250|UniProtKB:Q99P30}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2 H(+) + S- CC acetyl-4'-phosphopantetheine; Xref=Rhea:RHEA:64992, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:58343, ChEBI:CHEBI:156266; CC Evidence={ECO:0000250|UniProtKB:Q99P30}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64993; CC Evidence={ECO:0000250|UniProtKB:Q99P30}; CC -!- CATALYTIC ACTIVITY: CC Reaction=CoA + H2O = (R)-4'-phosphopantetheine + adenosine 3',5'- CC bisphosphate + 2 H(+); Xref=Rhea:RHEA:64988, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:58343, CC ChEBI:CHEBI:61723; Evidence={ECO:0000250|UniProtKB:Q99P30}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64989; CC Evidence={ECO:0000250|UniProtKB:Q99P30}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + propanoyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+) + CC propanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:67464, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57392, CC ChEBI:CHEBI:58343, ChEBI:CHEBI:172362; CC Evidence={ECO:0000250|UniProtKB:Q99P30}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67465; CC Evidence={ECO:0000250|UniProtKB:Q99P30}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + malonyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+) + CC malonyl-4'-phosphopantetheine; Xref=Rhea:RHEA:67468, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57384, CC ChEBI:CHEBI:58343, ChEBI:CHEBI:172363; CC Evidence={ECO:0000250|UniProtKB:Q99P30}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67469; CC Evidence={ECO:0000250|UniProtKB:Q99P30}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + succinyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+) + CC succinyl-4'-phosphopantetheine; Xref=Rhea:RHEA:67472, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57292, CC ChEBI:CHEBI:58343, ChEBI:CHEBI:172364; CC Evidence={ECO:0000250|UniProtKB:Q99P30}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67473; CC Evidence={ECO:0000250|UniProtKB:Q99P30}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end CoA-ribonucleoside in mRNA + H2O = (R)-4'- CC phosphopantetheine + a 5'-end phospho-adenosine-phospho- CC ribonucleoside in mRNA + 2 H(+); Xref=Rhea:RHEA:67592, Rhea:RHEA- CC COMP:15719, Rhea:RHEA-COMP:17276, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:61723, ChEBI:CHEBI:144051, CC ChEBI:CHEBI:172371; Evidence={ECO:0000250|UniProtKB:Q99P30}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67593; CC Evidence={ECO:0000250|UniProtKB:Q99P30}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000250|UniProtKB:Q99P30}; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:Q99P30}; CC -!- ACTIVITY REGULATION: Inhibited by fluoride. CC {ECO:0000250|UniProtKB:Q99P30}. CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q99P30}. CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:Q99P30}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P0C024-1; Sequence=Displayed; CC Name=2; CC IsoId=P0C024-2; Sequence=VSP_047605; CC Name=3; CC IsoId=P0C024-3; Sequence=VSP_053820, VSP_053821; CC -!- TISSUE SPECIFICITY: Expressed in liver, kidney, pancreas, pituitary, CC small intestine, spleen, heart and placenta. Weakly expressed in brain. CC {ECO:0000269|PubMed:11415433}. CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. PCD1 subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; EU981826; ACH71652.1; -; mRNA. DR EMBL; AK296963; BAG59507.1; -; mRNA. DR EMBL; AC092134; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC092724; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471114; EAW95595.1; -; Genomic_DNA. DR CCDS; CCDS42195.1; -. [P0C024-1] DR CCDS; CCDS58479.1; -. [P0C024-3] DR CCDS; CCDS58480.1; -. [P0C024-2] DR RefSeq; NP_001099133.1; NM_001105663.2. [P0C024-1] DR RefSeq; NP_001230586.1; NM_001243657.1. [P0C024-3] DR RefSeq; NP_001230589.1; NM_001243660.1. DR RefSeq; NP_001230590.1; NM_001243661.1. [P0C024-2] DR PDB; 5QGG; X-ray; 1.91 A; A=14-209. DR PDB; 5QGH; X-ray; 1.82 A; A=14-209. DR PDB; 5QGI; X-ray; 1.95 A; A=14-209. DR PDB; 5QGJ; X-ray; 1.95 A; A=14-209. DR PDB; 5QGK; X-ray; 1.81 A; A=14-209. DR PDB; 5QGL; X-ray; 2.27 A; A=14-209. DR PDB; 5QGM; X-ray; 1.96 A; A=14-209. DR PDB; 5QGN; X-ray; 1.95 A; A=14-209. DR PDB; 5QGO; X-ray; 1.82 A; A=14-209. DR PDB; 5QGP; X-ray; 2.09 A; A=14-209. DR PDB; 5QGQ; X-ray; 1.95 A; A=14-209. DR PDB; 5QGR; X-ray; 1.96 A; A=14-209. DR PDB; 5QGS; X-ray; 1.55 A; A=14-209. DR PDB; 5QGT; X-ray; 1.97 A; A=14-209. DR PDB; 5QGU; X-ray; 1.71 A; A=14-209. DR PDB; 5QGV; X-ray; 1.59 A; A=14-209. DR PDB; 5QGW; X-ray; 1.94 A; A=14-209. DR PDB; 5QGX; X-ray; 1.61 A; A=14-209. DR PDB; 5QGY; X-ray; 1.72 A; A=14-209. DR PDB; 5QGZ; X-ray; 1.65 A; A=14-209. DR PDB; 5QH0; X-ray; 1.57 A; A=14-209. DR PDB; 5QH1; X-ray; 1.65 A; A=14-209. DR PDB; 5QH2; X-ray; 1.74 A; A=14-209. DR PDB; 5QH3; X-ray; 1.65 A; A=14-209. DR PDB; 5QH4; X-ray; 1.67 A; A=14-209. DR PDB; 5QH5; X-ray; 1.85 A; A=14-209. DR PDB; 5QH6; X-ray; 2.00 A; A=14-209. DR PDB; 5QH7; X-ray; 1.74 A; A=14-209. DR PDB; 5QH8; X-ray; 1.75 A; A=14-209. DR PDB; 5QH9; X-ray; 1.72 A; A=14-209. DR PDB; 5QHA; X-ray; 1.57 A; A=14-209. DR PDB; 5QHB; X-ray; 1.57 A; A=14-209. DR PDB; 5QHC; X-ray; 2.21 A; A=14-209. DR PDB; 5QHE; X-ray; 1.74 A; A=14-209. DR PDB; 5QHF; X-ray; 1.67 A; A=14-209. DR PDB; 5QHG; X-ray; 1.92 A; A=14-209. DR PDB; 5QHH; X-ray; 1.52 A; A=14-209. DR PDB; 5T3P; X-ray; 2.03 A; A/B/C=1-235. DR PDBsum; 5QGG; -. DR PDBsum; 5QGH; -. DR PDBsum; 5QGI; -. DR PDBsum; 5QGJ; -. DR PDBsum; 5QGK; -. DR PDBsum; 5QGL; -. DR PDBsum; 5QGM; -. DR PDBsum; 5QGN; -. DR PDBsum; 5QGO; -. DR PDBsum; 5QGP; -. DR PDBsum; 5QGQ; -. DR PDBsum; 5QGR; -. DR PDBsum; 5QGS; -. DR PDBsum; 5QGT; -. DR PDBsum; 5QGU; -. DR PDBsum; 5QGV; -. DR PDBsum; 5QGW; -. DR PDBsum; 5QGX; -. DR PDBsum; 5QGY; -. DR PDBsum; 5QGZ; -. DR PDBsum; 5QH0; -. DR PDBsum; 5QH1; -. DR PDBsum; 5QH2; -. DR PDBsum; 5QH3; -. DR PDBsum; 5QH4; -. DR PDBsum; 5QH5; -. DR PDBsum; 5QH6; -. DR PDBsum; 5QH7; -. DR PDBsum; 5QH8; -. DR PDBsum; 5QH9; -. DR PDBsum; 5QHA; -. DR PDBsum; 5QHB; -. DR PDBsum; 5QHC; -. DR PDBsum; 5QHE; -. DR PDBsum; 5QHF; -. DR PDBsum; 5QHG; -. DR PDBsum; 5QHH; -. DR PDBsum; 5T3P; -. DR AlphaFoldDB; P0C024; -. DR SMR; P0C024; -. DR BioGRID; 129708; 2. DR IntAct; P0C024; 1. DR STRING; 9606.ENSP00000268533; -. DR GuidetoPHARMACOLOGY; 3085; -. DR iPTMnet; P0C024; -. DR PhosphoSitePlus; P0C024; -. DR BioMuta; NUDT7; -. DR DMDM; 68565858; -. DR EPD; P0C024; -. DR jPOST; P0C024; -. DR MassIVE; P0C024; -. DR MaxQB; P0C024; -. DR PaxDb; 9606-ENSP00000268533; -. DR PeptideAtlas; P0C024; -. DR ProteomicsDB; 42887; -. DR ProteomicsDB; 4528; -. DR ProteomicsDB; 52288; -. [P0C024-1] DR Antibodypedia; 48153; 29 antibodies from 11 providers. DR DNASU; 283927; -. DR Ensembl; ENST00000268533.9; ENSP00000268533.5; ENSG00000140876.11. [P0C024-1] DR Ensembl; ENST00000437314.3; ENSP00000387707.3; ENSG00000140876.11. [P0C024-2] DR Ensembl; ENST00000564085.5; ENSP00000457566.1; ENSG00000140876.11. [P0C024-3] DR GeneID; 283927; -. DR KEGG; hsa:283927; -. DR MANE-Select; ENST00000268533.9; ENSP00000268533.5; NM_001105663.3; NP_001099133.1. DR UCSC; uc010chd.4; human. [P0C024-1] DR AGR; HGNC:8054; -. DR CTD; 283927; -. DR DisGeNET; 283927; -. DR GeneCards; NUDT7; -. DR HGNC; HGNC:8054; NUDT7. DR HPA; ENSG00000140876; Tissue enhanced (liver). DR MIM; 609231; gene. DR neXtProt; NX_P0C024; -. DR OpenTargets; ENSG00000140876; -. DR PharmGKB; PA31840; -. DR VEuPathDB; HostDB:ENSG00000140876; -. DR eggNOG; KOG3069; Eukaryota. DR GeneTree; ENSGT00940000159631; -. DR HOGENOM; CLU_040940_6_0_1; -. DR InParanoid; P0C024; -. DR OMA; VGAKYSH; -. DR OrthoDB; 399667at2759; -. DR PhylomeDB; P0C024; -. DR TreeFam; TF106350; -. DR PathwayCommons; P0C024; -. DR Reactome; R-HSA-390918; Peroxisomal lipid metabolism. DR Reactome; R-HSA-9033241; Peroxisomal protein import. DR SignaLink; P0C024; -. DR BioGRID-ORCS; 283927; 16 hits in 1156 CRISPR screens. DR ChiTaRS; NUDT7; human. DR GenomeRNAi; 283927; -. DR Pharos; P0C024; Tdark. DR PRO; PR:P0C024; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; P0C024; Protein. DR Bgee; ENSG00000140876; Expressed in left ventricle myocardium and 168 other cell types or tissues. DR ExpressionAtlas; P0C024; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome. DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB. DR GO; GO:0010945; F:coenzyme A diphosphatase activity; ISS:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB. DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro. DR GO; GO:0030515; F:snoRNA binding; ISS:UniProtKB. DR GO; GO:0046356; P:acetyl-CoA catabolic process; ISS:UniProtKB. DR GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl. DR GO; GO:0044580; P:butyryl-CoA catabolic process; ISS:UniProtKB. DR GO; GO:0015938; P:coenzyme A catabolic process; ISS:UniProtKB. DR GO; GO:2001294; P:malonyl-CoA catabolic process; ISS:UniProtKB. DR GO; GO:0036114; P:medium-chain fatty-acyl-CoA catabolic process; ISS:UniProtKB. DR GO; GO:0009132; P:nucleoside diphosphate metabolic process; IEA:InterPro. DR GO; GO:1902859; P:propionyl-CoA catabolic process; ISS:UniProtKB. DR GO; GO:1902858; P:propionyl-CoA metabolic process; ISS:UniProtKB. DR GO; GO:1901289; P:succinyl-CoA catabolic process; ISS:UniProtKB. DR CDD; cd03426; CoAse; 1. DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1. DR InterPro; IPR045121; CoAse. DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR000059; NUDIX_hydrolase_NudL_CS. DR PANTHER; PTHR12992; NUDIX HYDROLASE; 1. DR PANTHER; PTHR12992:SF24; PEROXISOMAL COENZYME A DIPHOSPHATASE NUDT7; 1. DR Pfam; PF00293; NUDIX; 1. DR SUPFAM; SSF55811; Nudix; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS01293; NUDIX_COA; 1. DR Genevisible; P0C024; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Hydrolase; Magnesium; Manganese; KW Metal-binding; Peroxisome; Reference proteome; RNA-binding. FT CHAIN 1..238 FT /note="Peroxisomal coenzyme A diphosphatase NUDT7" FT /id="PRO_0000057140" FT DOMAIN 37..172 FT /note="Nudix hydrolase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794" FT MOTIF 77..98 FT /note="Nudix box" FT MOTIF 236..238 FT /note="Microbody targeting signal" FT /evidence="ECO:0000250" FT BINDING 92 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q99P30" FT BINDING 96 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q99P30" FT SITE 66 FT /note="Important for coenzyme A binding" FT /evidence="ECO:0000250|UniProtKB:Q99P30" FT MOD_RES 20 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99P30" FT VAR_SEQ 64..116 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1" FT /id="VSP_047605" FT VAR_SEQ 117..170 FT /note="TDTLITPFVGLIDHNFQAQPNPAEVKDVFLVPLAYFLHPQVHDQHYVTRLGH FT RF -> RWGSRYVDEAGLELLASSDPPTSASQSAGITDRYIDNSICGFNRPQLPGPAES FT C (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_053820" FT VAR_SEQ 171..238 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_053821" FT VARIANT 100 FT /note="R -> H (in dbSNP:rs308925)" FT /id="VAR_050415" FT VARIANT 181 FT /note="E -> G (in dbSNP:rs16946429)" FT /id="VAR_050416" FT HELIX 15..24 FT /evidence="ECO:0007829|PDB:5QHH" FT TURN 29..34 FT /evidence="ECO:0007829|PDB:5QHH" FT STRAND 35..49 FT /evidence="ECO:0007829|PDB:5QHH" FT STRAND 52..60 FT /evidence="ECO:0007829|PDB:5QHH" FT STRAND 65..67 FT /evidence="ECO:0007829|PDB:5QHH" FT STRAND 74..77 FT /evidence="ECO:0007829|PDB:5QHH" FT HELIX 85..97 FT /evidence="ECO:0007829|PDB:5QHH" FT HELIX 101..103 FT /evidence="ECO:0007829|PDB:5QHH" FT STRAND 104..109 FT /evidence="ECO:0007829|PDB:5QHH" FT STRAND 113..115 FT /evidence="ECO:0007829|PDB:5QHH" FT TURN 116..118 FT /evidence="ECO:0007829|PDB:5QHH" FT STRAND 119..128 FT /evidence="ECO:0007829|PDB:5QHH" FT TURN 138..140 FT /evidence="ECO:0007829|PDB:5QHH" FT STRAND 141..148 FT /evidence="ECO:0007829|PDB:5QHH" FT HELIX 149..153 FT /evidence="ECO:0007829|PDB:5QHH" FT STRAND 156..159 FT /evidence="ECO:0007829|PDB:5QHH" FT STRAND 173..178 FT /evidence="ECO:0007829|PDB:5QHH" FT TURN 180..182 FT /evidence="ECO:0007829|PDB:5QHH" FT STRAND 185..188 FT /evidence="ECO:0007829|PDB:5QHH" FT HELIX 190..204 FT /evidence="ECO:0007829|PDB:5QHH" FT HELIX 219..228 FT /evidence="ECO:0007829|PDB:5T3P" SQ SEQUENCE 238 AA; 26942 MW; 6F5BE439D609DC88 CRC64; MSRLGLPEEP VRNSLLDDAK ARLRKYDIGG KYSHLPYNKY SVLLPLVAKE GKLHLLFTVR SEKLRRAPGE VCFPGGKRDP TDMDDAATAL REAQEEVGLR PHQVEVVCCL VPCLIDTDTL ITPFVGLIDH NFQAQPNPAE VKDVFLVPLA YFLHPQVHDQ HYVTRLGHRF INHIFEYTNP EDGVTYQIKG MTANLAVLVA FIILEKKPTF EVQFNLNDVL ASSEELFLKV HKKATSRL //