ID C9KJA8_9FIRM Unreviewed; 348 AA.
AC C9KJA8;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=dUTP diphosphatase {ECO:0000256|ARBA:ARBA00012379};
DE EC=3.6.1.23 {ECO:0000256|ARBA:ARBA00012379};
GN Name=dut {ECO:0000313|EMBL:EEX69974.1};
GN ORFNames=MITSMUL_03105 {ECO:0000313|EMBL:EEX69974.1};
OS Mitsuokella multacida DSM 20544.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Mitsuokella.
OX NCBI_TaxID=500635 {ECO:0000313|EMBL:EEX69974.1, ECO:0000313|Proteomes:UP000003671};
RN [1] {ECO:0000313|EMBL:EEX69974.1, ECO:0000313|Proteomes:UP000003671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20544 {ECO:0000313|EMBL:EEX69974.1,
RC ECO:0000313|Proteomes:UP000003671};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000878};
CC -!- SIMILARITY: Belongs to the dUTPase family.
CC {ECO:0000256|ARBA:ARBA00006581}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEX69974.1}.
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DR EMBL; ABWK02000001; EEX69974.1; -; Genomic_DNA.
DR AlphaFoldDB; C9KJA8; -.
DR STRING; 500635.MITSMUL_03105; -.
DR PATRIC; fig|500635.8.peg.89; -.
DR eggNOG; COG0756; Bacteria.
DR HOGENOM; CLU_796492_0_0_9; -.
DR Proteomes; UP000003671; Unassembled WGS sequence.
DR GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0006226; P:dUMP biosynthetic process; IEA:InterPro.
DR GO; GO:0046081; P:dUTP catabolic process; IEA:InterPro.
DR CDD; cd07557; trimeric_dUTPase; 1.
DR Gene3D; 2.70.40.10; -; 1.
DR InterPro; IPR008181; dUTPase.
DR InterPro; IPR029054; dUTPase-like.
DR InterPro; IPR036157; dUTPase-like_sf.
DR InterPro; IPR033704; dUTPase_trimeric.
DR PANTHER; PTHR11241; DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE; 1.
DR PANTHER; PTHR11241:SF0; DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE; 1.
DR Pfam; PF00692; dUTPase; 1.
DR SUPFAM; SSF51283; dUTPase-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EEX69974.1};
KW Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080}.
FT DOMAIN 230..347
FT /note="dUTPase-like"
FT /evidence="ECO:0000259|Pfam:PF00692"
SQ SEQUENCE 348 AA; 39744 MW; 5C1C38513E222040 CRC64;
MNIKDHLEGN KYGKLTVIER DKNKGGSHWI CKCDCGNITS VVGTDLKLGK TKSCGCLGRE
IHREKSTKHG FSKTKLYRIW KGMKSRCYSK GHNSYKYYGG KGIKVCKQWE HDFVAFRTWS
LNNGYKEGLS IDRIDSNKDY GPDNCRWVTP LVQSNNTSRN HIITYHGESK TMAEWADEVG
IKYSTLRGRI NTSKWPIEKA LFAPLQRQEE AVIKVKYRDS LCQLEQNGSW IDLRASQDYS
YKKGDFIMID LGVCIKLPER HEAHLLPRSS TFKRYGLIMT NSMGIIDSAY SGNDDWWAMP
CLAVRDGEIH KGDRVAQFRI AKEQPVMYAE SVDHLDDVSR GGFGSTGR
//
