DUT_METTH
ID DUT_METTH Reviewed; 150 AA.
AC O27642;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 113.
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=MTH_1605;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
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; AE000666; AAB86078.1; -; Genomic_DNA.
DR PIR; D69081; D69081.
DR AlphaFoldDB; O27642; -.
DR SMR; O27642; -.
DR STRING; 187420.MTH_1605; -.
DR EnsemblBacteria; AAB86078; AAB86078; MTH_1605.
DR KEGG; mth:MTH_1605; -.
DR PATRIC; fig|187420.15.peg.1569; -.
DR HOGENOM; CLU_103451_2_0_2; -.
DR OMA; EYNGSYQ; -.
DR UniPathway; UPA00610; UER00666.
DR Proteomes; UP000005223; 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..150
FT /note="Probable deoxyuridine 5'-triphosphate
FT nucleotidohydrolase"
FT /id="PRO_0000153641"
SQ SEQUENCE 150 AA; 16997 MW; AFA09D55FB371648 CRC64;
MMIGEQLLKK LFPDFEELVQ PAGIDLRVDK VYRQMGPGSL IDDEKNLPPL EMLEPPIYRL
EPGKAYLASV DRMIEIPEGY AMLYLPRSTL LRSFVSVQTA VGDPGFRGTL QFLLHNHGEY
EYTLKRGERI VQAVVFPVEG SGKYSGSYQE
