NUD11_ARATH
ID NUD11_ARATH Reviewed; 222 AA.
AC Q8LET2; B3H699; Q9FJ42;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Nudix hydrolase 11;
DE Short=AtNUDT11;
DE EC=3.6.1.-;
DE AltName: Full=Coenzyme A diphosphatase NUDT11;
GN Name=NUDT11; Synonyms=NUDX11; OrderedLocusNames=At5g45940;
GN ORFNames=K15I22.14;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION IN VITRO, AND TISSUE SPECIFICITY.
RX PubMed=15878881; DOI=10.1074/jbc.m503536200;
RA Ogawa T., Ueda Y., Yoshimura K., Shigeoka S.;
RT "Comprehensive analysis of cytosolic nudix hydrolases in Arabidopsis
RT thaliana.";
RL J. Biol. Chem. 280:25277-25283(2005).
RN [5]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18815383; DOI=10.1104/pp.108.128413;
RA Ogawa T., Yoshimura K., Miyake H., Ishikawa K., Ito D., Tanabe N.,
RA Shigeoka S.;
RT "Molecular characterization of organelle-type Nudix hydrolases in
RT Arabidopsis.";
RL Plant Physiol. 148:1412-1424(2008).
CC -!- FUNCTION: Coenzyme A diphosphatase which mediates the cleavage of CoA
CC into 3',5'-ADP from CoA and 4'-phosphopantetheine. Can use malonyl-CoA,
CC hexanoyl-CoA, lauroyl-CoA, myristoyl-CoA and palmitoyl-CoA as
CC substrates, but not isobutyryl-CoA or propionyl-CoA.
CC {ECO:0000269|PubMed:15878881}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=27.8 uM for CoA {ECO:0000269|PubMed:18815383};
CC Vmax=0.40 umol/min/mg enzyme with CoA as substrate
CC {ECO:0000269|PubMed:18815383};
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8LET2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8LET2-2; Sequence=VSP_037558, VSP_037559;
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems and leaves.
CC {ECO:0000269|PubMed:15878881}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. PCD1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AB016870; BAB09322.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95317.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95318.1; -; Genomic_DNA.
DR EMBL; AY085250; AAM62482.1; -; mRNA.
DR RefSeq; NP_001119380.1; NM_001125908.1. [Q8LET2-2]
DR RefSeq; NP_199406.1; NM_123962.3. [Q8LET2-1]
DR AlphaFoldDB; Q8LET2; -.
DR SMR; Q8LET2; -.
DR STRING; 3702.AT5G45940.1; -.
DR PaxDb; Q8LET2; -.
DR PRIDE; Q8LET2; -.
DR ProteomicsDB; 250583; -. [Q8LET2-1]
DR EnsemblPlants; AT5G45940.1; AT5G45940.1; AT5G45940. [Q8LET2-1]
DR EnsemblPlants; AT5G45940.2; AT5G45940.2; AT5G45940. [Q8LET2-2]
DR GeneID; 834634; -.
DR Gramene; AT5G45940.1; AT5G45940.1; AT5G45940. [Q8LET2-1]
DR Gramene; AT5G45940.2; AT5G45940.2; AT5G45940. [Q8LET2-2]
DR KEGG; ath:AT5G45940; -.
DR Araport; AT5G45940; -.
DR TAIR; locus:2152415; AT5G45940.
DR eggNOG; KOG3069; Eukaryota.
DR HOGENOM; CLU_040940_8_0_1; -.
DR InParanoid; Q8LET2; -.
DR OMA; WERPWDR; -.
DR OrthoDB; 1253012at2759; -.
DR PhylomeDB; Q8LET2; -.
DR BioCyc; ARA:AT5G45940-MON; -.
DR SABIO-RK; Q8LET2; -.
DR PRO; PR:Q8LET2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8LET2; baseline and differential.
DR Genevisible; Q8LET2; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003986; F:acetyl-CoA hydrolase activity; IBA:GO_Central.
DR GO; GO:0010945; F:CoA pyrophosphatase activity; IDA:TAIR.
DR GO; GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000210; F:NAD+ diphosphatase activity; IDA:TAIR.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IDA:TAIR.
DR GO; GO:0015938; P:coenzyme A catabolic process; IBA:GO_Central.
DR GO; GO:2001294; P:malonyl-CoA catabolic process; IDA:TAIR.
DR GO; GO:0006753; P:nucleoside phosphate metabolic process; IDA:TAIR.
DR CDD; cd03426; CoAse; 1.
DR InterPro; IPR045121; CoAse.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR PANTHER; PTHR12992; PTHR12992; 1.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Magnesium; Manganese; Membrane;
KW Metal-binding; Peroxisome; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..222
FT /note="Nudix hydrolase 11"
FT /id="PRO_0000057142"
FT TRANSMEM 186..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 31..175
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 73..96
FT /note="Nudix box"
FT BINDING 90
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT VAR_SEQ 155..163
FT /note="DRNRRAEER -> KQASRGTRA (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_037558"
FT VAR_SEQ 164..222
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_037559"
FT CONFLICT 48
FT /note="K -> I (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="E -> Q (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="T -> S (in Ref. 3; AAM62482)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="Q -> P (in Ref. 3; AAM62482)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="W -> L (in Ref. 3; AAM62482)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 222 AA; 25679 MW; C2BE6B88399D8440 CRC64;
MSSTTTDSTE LQNLIKLFQN CQTHPRQHFP AKSSAVLVCL YQEQREDKNE LRVILTKRST
TLSSHPGEVA LPGGKRDQED KDDIATALRE AREEIGLDPS LVTIISVLEP FVNKKGMSVA
PVIGFLHDKK AFKQLPNPAE VEEIFDVPLE MFLKDRNRRA EEREHEGERY LLQYFDYYSE
DKERSFIIWA LTAGILIRVA SIVYQRLPEF QERKPSFWNQ PN
