DUT_MYCTU
ID DUT_MYCTU Reviewed; 154 AA.
AC P9WNS5; L0TAD4; O07199; P0A552;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase {ECO:0000255|HAMAP-Rule:MF_00116};
DE Short=dUTPase {ECO:0000255|HAMAP-Rule:MF_00116, ECO:0000303|PubMed:15276840};
DE EC=3.6.1.23 {ECO:0000255|HAMAP-Rule:MF_00116, ECO:0000305|PubMed:15276840};
DE AltName: Full=dUTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00116};
GN Name=dut; OrderedLocusNames=Rv2697c; ORFNames=MTCY05A6.18c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
RA Sawaya M.R., Chan S., Segelke B.W., Lekin T., Heike K., Cho U.S.,
RA Naranjo C., Perry L.J., Yeates T.O., Eisenberg D.;
RT "Crystal structure of dUTPase from Mycobacterium tuberculosis.";
RL Submitted (SEP-2002) to the PDB data bank.
RN [4] {ECO:0007744|PDB:1MQ7, ECO:0007744|PDB:1SIX, ECO:0007744|PDB:1SJN, ECO:0007744|PDB:1SLH, ECO:0007744|PDB:1SM8, ECO:0007744|PDB:1SMC, ECO:0007744|PDB:1SNF}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH MAGNESIUM ION AND
RP SUBSTRATE ANALOG, COFACTOR, AND SUBUNIT.
RX PubMed=15276840; DOI=10.1016/j.jmb.2004.06.028;
RA Chan S., Segelke B., Lekin T., Krupka H., Cho U.S., Kim M.-Y., So M.,
RA Kim C.-Y., Naranjo C.M., Rogers Y.C., Park M.S., Waldo G.S., Pashkov I.,
RA Cascio D., Perry J.L., Sawaya M.R.;
RT "Crystal structure of the Mycobacterium tuberculosis dUTPase: insights into
RT the catalytic mechanism.";
RL J. Mol. Biol. 341:503-517(2004).
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_00116}.
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_00116,
CC ECO:0000305|PubMed:15276840};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00116,
CC ECO:0000269|PubMed:15276840};
CC -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP
CC route): step 2/2. {ECO:0000255|HAMAP-Rule:MF_00116}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00116,
CC ECO:0000269|PubMed:15276840}.
CC -!- MISCELLANEOUS: Each trimer binds three substrate molecules. The ligands
CC are bound between subunits, and for each substrate molecule, residues
CC from adjacent subunits contribute to the binding interactions.
CC {ECO:0000269|PubMed:15276840}.
CC -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000255|HAMAP-
CC Rule:MF_00116, ECO:0000305}.
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DR EMBL; AL123456; CCP45495.1; -; Genomic_DNA.
DR PIR; D70530; D70530.
DR RefSeq; NP_217213.1; NC_000962.3.
DR RefSeq; WP_003413930.1; NZ_NVQJ01000017.1.
DR PDB; 1MQ7; X-ray; 1.95 A; A=1-154.
DR PDB; 1SIX; X-ray; 1.30 A; A=1-154.
DR PDB; 1SJN; X-ray; 1.80 A; A/B/C=1-154.
DR PDB; 1SLH; X-ray; 3.00 A; A/B/C=1-154.
DR PDB; 1SM8; X-ray; 2.90 A; A/B/C=1-154.
DR PDB; 1SMC; X-ray; 2.10 A; A/B/C=1-154.
DR PDB; 1SNF; X-ray; 1.85 A; A/B/C=1-154.
DR PDB; 2PY4; X-ray; 1.49 A; A=1-154.
DR PDB; 3H6D; X-ray; 1.80 A; A=1-154.
DR PDB; 3HZA; X-ray; 1.20 A; A=1-154.
DR PDB; 3I93; X-ray; 1.80 A; A=1-138.
DR PDB; 3LOJ; X-ray; 1.25 A; A=1-154.
DR PDB; 4GCY; X-ray; 1.50 A; A=1-154.
DR PDB; 5ECT; X-ray; 1.30 A; A=1-142.
DR PDB; 5EDD; X-ray; 1.97 A; A=1-154.
DR PDBsum; 1MQ7; -.
DR PDBsum; 1SIX; -.
DR PDBsum; 1SJN; -.
DR PDBsum; 1SLH; -.
DR PDBsum; 1SM8; -.
DR PDBsum; 1SMC; -.
DR PDBsum; 1SNF; -.
DR PDBsum; 2PY4; -.
DR PDBsum; 3H6D; -.
DR PDBsum; 3HZA; -.
DR PDBsum; 3I93; -.
DR PDBsum; 3LOJ; -.
DR PDBsum; 4GCY; -.
DR PDBsum; 5ECT; -.
DR PDBsum; 5EDD; -.
DR AlphaFoldDB; P9WNS5; -.
DR SMR; P9WNS5; -.
DR STRING; 83332.Rv2697c; -.
DR DrugBank; DB01965; 2'-Deoxyuridine 5'-alpha,beta-imido-triphosphate.
DR DrugBank; DB03800; Deoxyuridine monophosphate.
DR DrugBank; DB03413; Deoxyuridine-5'-Diphosphate.
DR DrugBank; DB02333; Deoxyuridine-5'-Triphosphate.
DR PaxDb; P9WNS5; -.
DR GeneID; 45426685; -.
DR GeneID; 887290; -.
DR KEGG; mtu:Rv2697c; -.
DR TubercuList; Rv2697c; -.
DR eggNOG; COG0756; Bacteria.
DR OMA; YAAFVHP; -.
DR PhylomeDB; P9WNS5; -.
DR BRENDA; 3.6.1.23; 3445.
DR UniPathway; UPA00610; UER00666.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0004170; F:dUTP diphosphatase activity; IDA:MTBBASE.
DR GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
DR GO; GO:0006226; P:dUMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0046081; P:dUTP catabolic process; IBA:GO_Central.
DR GO; GO:0046080; P:dUTP metabolic process; IDA:MTBBASE.
DR CDD; cd07557; trimeric_dUTPase; 1.
DR Gene3D; 2.70.40.10; -; 1.
DR HAMAP; MF_00116; dUTPase_bact; 1.
DR InterPro; IPR008181; dUTPase.
DR InterPro; IPR029054; dUTPase-like.
DR InterPro; IPR036157; dUTPase-like_sf.
DR InterPro; IPR033704; dUTPase_trimeric.
DR PANTHER; PTHR11241; PTHR11241; 1.
DR Pfam; PF00692; dUTPase; 1.
DR SUPFAM; SSF51283; SSF51283; 1.
DR TIGRFAMs; TIGR00576; dut; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW Reference proteome.
FT CHAIN 1..154
FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT /id="PRO_0000182884"
FT BINDING 64..66
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116,
FT ECO:0000269|PubMed:15276840"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116,
FT ECO:0000269|PubMed:15276840"
FT BINDING 81..83
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116,
FT ECO:0000269|PubMed:15276840"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15276840"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:3HZA"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:3HZA"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:3HZA"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:3HZA"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:3HZA"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:3HZA"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:3HZA"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:3HZA"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:3HZA"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:3HZA"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:3HZA"
FT STRAND 110..118
FT /evidence="ECO:0007829|PDB:3HZA"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:1SJN"
FT TURN 130..134
FT /evidence="ECO:0007829|PDB:3HZA"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:1SIX"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:3HZA"
SQ SEQUENCE 154 AA; 15803 MW; 836D5E6420EF455B CRC64;
MSTTLAIVRL DPGLPLPSRA HDGDAGVDLY SAEDVELAPG RRALVRTGVA VAVPFGMVGL
VHPRSGLATR VGLSIVNSPG TIDAGYRGEI KVALINLDPA APIVVHRGDR IAQLLVQRVE
LVELVEVSSF DEAGLASTSR GDGGHGSSGG HASL
