ID A0A1P8F7C6_9CHLR Unreviewed; 612 AA.
AC A0A1P8F7C6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=dTTP/UTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_00528};
DE Short=dTTPase/UTPase {ECO:0000256|HAMAP-Rule:MF_00528};
DE EC=3.6.1.9 {ECO:0000256|HAMAP-Rule:MF_00528};
DE AltName: Full=Nucleoside triphosphate pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_00528};
DE AltName: Full=Nucleotide pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_00528};
DE Short=Nucleotide PPase {ECO:0000256|HAMAP-Rule:MF_00528};
GN Name=rumA {ECO:0000313|EMBL:APV44379.1};
GN ORFNames=Dform_01044 {ECO:0000313|EMBL:APV44379.1};
OS Dehalogenimonas formicexedens.
OC Bacteria; Chloroflexota; Dehalococcoidia; Dehalogenimonas.
OX NCBI_TaxID=1839801 {ECO:0000313|EMBL:APV44379.1, ECO:0000313|Proteomes:UP000185934};
RN [1] {ECO:0000313|Proteomes:UP000185934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSZ-14 {ECO:0000313|Proteomes:UP000185934};
RA Key T.A., Bowman K.S., Lee I., Chun J., Albuquerque L., da Costa M.S.,
RA Rainey F.A., Moe W.M.;
RT "Dehalogenimonas formicexedens sp. nov., a chlorinated alkane respiring
RT bacterium isolated from contaminated groundwater.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP
CC and UTP. May have a dual role in cell division arrest and in preventing
CC the incorporation of modified nucleotides into cellular nucleic acids.
CC {ECO:0000256|HAMAP-Rule:MF_00528}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + UTP = diphosphate + H(+) + UMP; Xref=Rhea:RHEA:29395,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:46398, ChEBI:CHEBI:57865; EC=3.6.1.9;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00528};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dTTP + H2O = diphosphate + dTMP + H(+); Xref=Rhea:RHEA:28534,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37568, ChEBI:CHEBI:63528; EC=3.6.1.9;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00528};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00528};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00528}.
CC -!- SIMILARITY: Belongs to the Maf family. YhdE subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00528}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA M5U methyltransferase family. {ECO:0000256|PROSITE-
CC ProRule:PRU01024}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00528}.
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DR EMBL; CP018258; APV44379.1; -; Genomic_DNA.
DR RefSeq; WP_076004066.1; NZ_CP018258.1.
DR AlphaFoldDB; A0A1P8F7C6; -.
DR STRING; 1839801.Dform_01044; -.
DR KEGG; dfo:Dform_01044; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000185934; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0036218; F:dTTP diphosphatase activity; IEA:RHEA.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0036221; F:UTP diphosphatase activity; IEA:RHEA.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0034470; P:ncRNA processing; IEA:UniProt.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009451; P:RNA modification; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd00555; Maf; 1.
DR Gene3D; 2.40.50.1070; -; 1.
DR Gene3D; 3.90.950.10; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR HAMAP; MF_00528; Maf; 1.
DR InterPro; IPR029001; ITPase-like_fam.
DR InterPro; IPR003697; Maf-like.
DR InterPro; IPR030390; MeTrfase_TrmA_AS.
DR InterPro; IPR030391; MeTrfase_TrmA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002792; TRAM_dom.
DR InterPro; IPR010280; U5_MeTrfase_fam.
DR NCBIfam; TIGR00172; maf; 1.
DR PANTHER; PTHR11061; RNA M5U METHYLTRANSFERASE; 1.
DR PANTHER; PTHR11061:SF30; TRNA (URACIL(54)-C(5))-METHYLTRANSFERASE; 1.
DR Pfam; PF02545; Maf; 1.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR SUPFAM; SSF52972; ITPase-like; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR PROSITE; PS50926; TRAM; 1.
DR PROSITE; PS01230; TRMA_1; 1.
DR PROSITE; PS01231; TRMA_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00528};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00528};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01024}; Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_00528};
KW Reference proteome {ECO:0000313|Proteomes:UP000185934};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01024};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01024}.
FT DOMAIN 1..59
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT ACT_SITE 349
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 349
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT ACT_SITE 470
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00528"
FT BINDING 229
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 258
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 279
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 322
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT SITE 413
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00528"
FT SITE 471
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00528"
FT SITE 555
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00528"
SQ SEQUENCE 612 AA; 67216 MW; D2780A75030D9D2B CRC64;
MNETSALIIV RLTGLGEFGE TVAEYEGRTI NIFGGIPGET VEARVIRNTP GAADAIVTKA
IVASVHRREP VCPRFGECSG CQWQHVEYSH QLELKRGLVK RALESEGLDG SLVREVVPSP
SEFGYRNHAR LSIRRRLNSF GFINRVTHQF VAVDRCPIMA EGVNSLLAAL NGRCGETTQF
SIRYGINTDE YLIQPQFKNP EVTVITGQVH YHEIMAGRKF RISSPSFFQV NTPQAERLAE
IIRQRLTLNG DETIIDAYAG VGTFSVMLAP YANKVIAIEE SGAAIKDARI NVREIPNVEL
IEARTETVLP HLGRLADATI IDPSRVGCHP AALKTLNFYP SKKLVYVSCN PETMARDLRV
LAHGPYEIQD VTPVDLFPQT YHVESVALLR FDPEKENAFI EKQRIVLAST SPRRSEILAS
MGLKFEIVAS NFDETPAEGL SPEEQAASHA RAKAVAVAAG RSSGTVISAD TVVVLGEEML
GKPASSAEAV EMLKQLRDKT HRVVTAVAVT DAATKETFAD FRSTQVTIRN LTDLEIEDYV
KSGSPLDKAG AYGIQDKLFQ PVARIKGCYL NVVGLPVCLM LDLLLKIGVH PKISTNWRPP
GDCADCHKWQ CG
//
