DUT_METAC
ID DUT_METAC Reviewed; 171 AA.
AC Q8TGX9;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Probable deoxyuridine 5'-triphosphate nucleotidohydrolase {ECO:0000255|HAMAP-Rule:MF_00635};
DE Short=dUTPase {ECO:0000255|HAMAP-Rule:MF_00635};
DE EC=3.6.1.23 {ECO:0000255|HAMAP-Rule:MF_00635};
DE AltName: Full=dUTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00635};
GN Name=dut {ECO:0000255|HAMAP-Rule:MF_00635}; OrderedLocusNames=MA_0440;
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
CC -!- FUNCTION: This enzyme is involved in nucleotide metabolism: it produces
CC dUMP, the immediate precursor of thymidine nucleotides and it decreases
CC the intracellular concentration of dUTP so that uracil cannot be
CC incorporated into DNA. {ECO:0000255|HAMAP-Rule:MF_00635}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00635};
CC -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP
CC route): step 2/2. {ECO:0000255|HAMAP-Rule:MF_00635}.
CC -!- SIMILARITY: Belongs to the dCTP deaminase family. Archaeal dUTPase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00635}.
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DR EMBL; AE010299; AAM03887.1; -; Genomic_DNA.
DR RefSeq; WP_011020492.1; NC_003552.1.
DR AlphaFoldDB; Q8TGX9; -.
DR SMR; Q8TGX9; -.
DR STRING; 188937.MA_0440; -.
DR EnsemblBacteria; AAM03887; AAM03887; MA_0440.
DR GeneID; 1472332; -.
DR KEGG; mac:MA_0440; -.
DR HOGENOM; CLU_103451_2_0_2; -.
DR InParanoid; Q8TGX9; -.
DR OMA; WDAGYEG; -.
DR OrthoDB; 94658at2157; -.
DR PhylomeDB; Q8TGX9; -.
DR UniPathway; UPA00610; UER00666.
DR Proteomes; UP000002487; Chromosome.
DR GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006226; P:dUMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07557; trimeric_dUTPase; 1.
DR Gene3D; 2.70.40.10; -; 1.
DR HAMAP; MF_00635; dUTPase_arch; 1.
DR InterPro; IPR029054; dUTPase-like.
DR InterPro; IPR036157; dUTPase-like_sf.
DR InterPro; IPR023537; dUTPase_archaeal.
DR InterPro; IPR033704; dUTPase_trimeric.
DR Pfam; PF00692; dUTPase; 1.
DR SUPFAM; SSF51283; SSF51283; 1.
PE 3: Inferred from homology;
KW Hydrolase; Nucleotide metabolism; Reference proteome.
FT CHAIN 1..171
FT /note="Probable deoxyuridine 5'-triphosphate
FT nucleotidohydrolase"
FT /id="PRO_0000153637"
SQ SEQUENCE 171 AA; 19259 MW; 645B29D302AE49E8 CRC64;
MTLLSSNELR KLIQATPHLL ENAVDIETQI QPNGLELTLK EIKTIEGVGA VDFDNSERKV
PDAKPLEFED DDWIHLPKGI YKVIFNEIVN IPMNLAAIAK PRSSLIRCGA TLETAVWDAG
YRGRSESMLV VYNSAGFRLK KNARIMQLLF YTLNSEVEEG YSGVYQNENT K