DUT_METJA
ID DUT_METJA Reviewed; 156 AA.
AC Q58502;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase {ECO:0000305};
DE Short=dUTPase {ECO:0000255|HAMAP-Rule:MF_00635};
DE EC=3.6.1.23 {ECO:0000255|HAMAP-Rule:MF_00635, ECO:0000269|PubMed:12538648, ECO:0000269|PubMed:12670946};
DE AltName: Full=MjDUT;
DE AltName: Full=dUTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00635};
GN Name=dut {ECO:0000255|HAMAP-Rule:MF_00635}; OrderedLocusNames=MJ1102;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP PROTEIN SEQUENCE OF 2-10, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND PATHWAY.
RX PubMed=12670946; DOI=10.1074/jbc.m213010200;
RA Bjoernberg O., Neuhard J., Nyman P.O.;
RT "A bifunctional dCTP deaminase-dUTP nucleotidohydrolase from the
RT hyperthermophilic archaeon Methanocaldococcus jannaschii.";
RL J. Biol. Chem. 278:20667-20672(2003).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP SUBUNIT.
RX PubMed=12538648; DOI=10.1074/jbc.m212460200;
RA Li H., Xu H., Graham D.E., White R.H.;
RT "The Methanococcus jannaschii dCTP deaminase is a bifunctional deaminase
RT and diphosphatase.";
RL J. Biol. Chem. 278:11100-11106(2003).
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 ECO:0000269|PubMed:12538648, ECO:0000269|PubMed:12670946}.
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 ECO:0000269|PubMed:12538648, ECO:0000269|PubMed:12670946};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.4 uM for dUTP {ECO:0000269|PubMed:12670946};
CC KM=103 uM for dUTP {ECO:0000269|PubMed:12538648};
CC Note=kcat is 4.6 sec(-1). {ECO:0000269|PubMed:12538648};
CC -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP
CC route): step 2/2. {ECO:0000255|HAMAP-Rule:MF_00635,
CC ECO:0000269|PubMed:12538648, ECO:0000269|PubMed:12670946}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:12538648}.
CC -!- SIMILARITY: Belongs to the dCTP deaminase family. Archaeal dUTPase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00635, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB99105.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L77117; AAB99105.1; ALT_INIT; Genomic_DNA.
DR PIR; E64437; E64437.
DR RefSeq; WP_064496724.1; NC_000909.1.
DR AlphaFoldDB; Q58502; -.
DR SMR; Q58502; -.
DR STRING; 243232.MJ_1102; -.
DR EnsemblBacteria; AAB99105; AAB99105; MJ_1102.
DR GeneID; 1451999; -.
DR KEGG; mja:MJ_1102; -.
DR eggNOG; arCOG04048; Archaea.
DR HOGENOM; CLU_103451_2_0_2; -.
DR InParanoid; Q58502; -.
DR OMA; WDAGYEG; -.
DR OrthoDB; 94658at2157; -.
DR PhylomeDB; Q58502; -.
DR SABIO-RK; Q58502; -.
DR UniPathway; UPA00610; UER00666.
DR Proteomes; UP000000805; 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 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Nucleotide metabolism;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12670946"
FT CHAIN 2..156
FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT /id="PRO_0000153638"
SQ SEQUENCE 156 AA; 18070 MW; AF6E28A4CF91FF3D CRC64;
MIIGANTSKN FFDNLEEEQI QQCGIDLRVW KIFKIEGEGV IDFSNEKRKL PNYIEIFNSE
KDEHIKLDRG VYIVKVADYI KIPENVAGFA YPRSSLLRMG ATLYSAVHDP GYEGRPEYLM
QVFNPITIYK YARIAQIVFV ECRDVKGVYE GIYKGR
