Y1184_DEIRA
ID Y1184_DEIRA Reviewed; 194 AA.
AC Q9RV46;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Nudix hydrolase DR_1184 {ECO:0000303|PubMed:12837785};
DE EC=3.6.1.- {ECO:0000250|UniProtKB:Q99P30};
DE AltName: Full=Coenzyme A pyrophosphatase {ECO:0000303|PubMed:12837785};
DE AltName: Full=DR-CoAse {ECO:0000303|PubMed:12837785};
DE AltName: Full=MutT/nudix family protein {ECO:0000312|EMBL:AAF10752.1};
GN OrderedLocusNames=DR_1184 {ECO:0000312|EMBL:AAF10752.1};
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230 {ECO:0000312|EMBL:AAF10752.1, ECO:0000312|Proteomes:UP000002524};
RN [1] {ECO:0000312|EMBL:AAF10752.1, ECO:0000312|Proteomes:UP000002524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422 {ECO:0000312|Proteomes:UP000002524};
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [2] {ECO:0007744|PDB:1NQY, ECO:0007744|PDB:1NQZ}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) AND IN COMPLEX WITH MAGNESIUM,
RP COFACTOR, AND SUBUNIT.
RX PubMed=12837785; DOI=10.1128/jb.185.14.4110-4118.2003;
RA Kang L.W., Gabelli S.B., Bianchet M.A., Xu W.L., Bessman M.J., Amzel L.M.;
RT "Structure of a coenzyme A pyrophosphatase from Deinococcus radiodurans: a
RT member of the Nudix family.";
RL J. Bacteriol. 185:4110-4118(2003).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12837785};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q99P30};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12837785}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. PCD1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AE000513; AAF10752.1; -; Genomic_DNA.
DR PIR; G75427; G75427.
DR RefSeq; NP_294908.1; NC_001263.1.
DR RefSeq; WP_010887827.1; NZ_CP015081.1.
DR PDB; 1NQY; X-ray; 2.09 A; A=1-194.
DR PDB; 1NQZ; X-ray; 1.70 A; A=1-194.
DR PDBsum; 1NQY; -.
DR PDBsum; 1NQZ; -.
DR SMR; Q9RV46; -.
DR STRING; 243230.DR_1184; -.
DR EnsemblBacteria; AAF10752; AAF10752; DR_1184.
DR KEGG; dra:DR_1184; -.
DR PATRIC; fig|243230.17.peg.1383; -.
DR eggNOG; COG0494; Bacteria.
DR HOGENOM; CLU_040940_5_2_0; -.
DR InParanoid; Q9RV46; -.
DR OMA; IWGLTAK; -.
DR OrthoDB; 1623169at2; -.
DR EvolutionaryTrace; Q9RV46; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0010945; F:CoA pyrophosphatase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0015938; P:coenzyme A 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 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 3D-structure; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..194
FT /note="Nudix hydrolase DR_1184"
FT /id="PRO_0000455514"
FT DOMAIN 33..181
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 71..92
FT /note="Nudix box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:12837785,
FT ECO:0007744|PDB:1NQZ"
FT BINDING 90
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q99P30"
SQ SEQUENCE 194 AA; 21250 MW; 8EEE41BC46530C05 CRC64;
MTAPHDPLDD IQADPWALWL SGRTRTALEL PHYRRAAVLV ALTREADPRV LLTVRSSELP
THKGQIAFPG GSLDAGETPT QAALREAQEE VALDPAAVTL LGELDDVFTP VGFHVTPVLG
RIAPEALDTL RVTPEVAQII TPTLAELRAV PLVRERRTLP DGTEVPLYRY PWRGLDIWGM
TARVLHDLLE QGPG
