NUDT7_HUMAN
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 03-AUG-2022, entry version 134.
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}.
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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; P0C024; -.
DR PeptideAtlas; P0C024; -.
DR PRIDE; P0C024; -.
DR ProteomicsDB; 42887; -.
DR ProteomicsDB; 4528; -.
DR ProteomicsDB; 52288; -. [P0C024-1]
DR Antibodypedia; 48153; 28 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 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; CPNPAEV; -.
DR OrthoDB; 1253012at2759; -.
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 1078 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 167 other tissues.
DR ExpressionAtlas; P0C024; baseline and differential.
DR Genevisible; P0C024; HS.
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:0003986; F:acetyl-CoA hydrolase activity; IBA:GO_Central.
DR GO; GO:0010945; F:CoA pyrophosphatase 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 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; PTHR12992; 1.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS01293; NUDIX_COA; 1.
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
