Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Putative 8-oxo-dGTP diphosphatase YtkD (8-oxo-dGTPase) (EC 3.6.1.55) (7,8-dihydro-8-oxoguanine-triphosphatase) (dGTP pyrophosphohydrolase)

 YTKD_BACSU              Reviewed;         158 AA.
O35013; Q795N9;
21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
05-DEC-2018, entry version 118.
RecName: Full=Putative 8-oxo-dGTP diphosphatase YtkD;
Short=8-oxo-dGTPase;
EC=3.6.1.55;
AltName: Full=7,8-dihydro-8-oxoguanine-triphosphatase;
AltName: Full=dGTP pyrophosphohydrolase;
Name=ytkD; Synonyms=mutTA; OrderedLocusNames=BSU30630;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
"Sequencing and functional annotation of the Bacillus subtilis genes
in the 200 kb rrnB-dnaB region.";
Microbiology 143:3431-3441(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[3]
FUNCTION, REGULATION, AND EXPRESSION.
PubMed=14761999; DOI=10.1128/JB.186.4.1050-1059.2004;
Ramirez M.I., Castellanos-Juarez F.X., Yasbin R.E., Pedraza-Reyes M.;
"The ytkD (mutTA) gene of Bacillus subtilis encodes a functional
antimutator 8-Oxo-(dGTP/GTP)ase and is under dual control of sigma A
and sigma F RNA polymerases.";
J. Bacteriol. 186:1050-1059(2004).
[4]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=15576788; DOI=10.1128/JB.186.24.8380-8384.2004;
Xu W., Jones C.R., Dunn C.A., Bessman M.J.;
"Gene ytkD of Bacillus subtilis encodes an atypical nucleoside
triphosphatase member of the Nudix hydrolase superfamily.";
J. Bacteriol. 186:8380-8384(2004).
[5]
DISRUPTION PHENOTYPE IN GROWING CELLS.
STRAIN=168 / PS832;
PubMed=16513759; DOI=10.1128/JB.188.6.2285-2289.2006;
Castellanos-Juarez F.X., Alvarez-Alvarez C., Yasbin R.E., Setlow B.,
Setlow P., Pedraza-Reyes M.;
"YtkD and MutT protect vegetative cells but not spores of Bacillus
subtilis from oxidative stress.";
J. Bacteriol. 188:2285-2289(2006).
[6]
DISRUPTION PHENOTYPE IN STATIONARY PHASE CELLS.
STRAIN=168 / YB955;
PubMed=19011023; DOI=10.1128/JB.01210-08;
Vidales L.E., Cardenas L.C., Robleto E., Yasbin R.E.,
Pedraza-Reyes M.;
"Defects in the error prevention oxidized guanine system potentiate
stationary-phase mutagenesis in Bacillus subtilis.";
J. Bacteriol. 191:506-513(2009).
-!- FUNCTION: Involved in the GO system responsible for removing an
oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine, 8-
oxo-dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted
opposite dA and dC residues of template DNA with almost equal
efficiency thus leading to A.T to G.C transversions (By
similarity). Functions, in conjunction with MutT, to protect
vegetatively growing cells from DNA-damaging agents such as
H(2)O(2) or t-BHP (t-butylhydroperoxide). The 2 proteins do not
however protect spores. According to PubMed:15576788,
phosphohydrolase that catalyzes the hydrolysis of all common
nucleoside triphosphates as well as of the mutagenic analog 8-oxo-
dGTP. The high catalytic efficiency on dGTP is in contrast to
results from PubMed:14761999. According to PubMed:14761999,
catalyzes the hydrolysis of 8-oxo-dGTP with a specific activity
413 times higher than that exhibited against dGTP. Preferentially
catalyzes the hydrolysis of 8-oxo-dGTP and 8-oxo-GTP. According to
PubMed:15576788, hydrolyzes nucleoside triphosphates in a stepwise
fashion through the diphosphate to the monophosphate, releasing
two molecules of inorganic orthophosphate. {ECO:0000250,
ECO:0000269|PubMed:14761999, ECO:0000269|PubMed:15576788}.
-!- CATALYTIC ACTIVITY:
Reaction=8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate + H(+);
Xref=Rhea:RHEA:31575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:33019, ChEBI:CHEBI:63224, ChEBI:CHEBI:77896;
EC=3.6.1.55;
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ACTIVITY REGULATION: Not induced by oxidative damage (following
treatment with paraquat or hydrogen peroxide). Not induced by
mitomycin C. Not induced by sigma-B general stress inducers such
as sodium chloride, ethanol or heat.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.16 mM for dGTP {ECO:0000269|PubMed:15576788};
KM=0.43 mM for 8-oxo-dGTP {ECO:0000269|PubMed:15576788};
KM=0.89 mM for dATP {ECO:0000269|PubMed:15576788};
Vmax=2.4 umol/min/mg enzyme with dGTP as substrate
{ECO:0000269|PubMed:15576788};
Vmax=3.1 umol/min/mg enzyme with 8-oxo-dGTP as substrate
{ECO:0000269|PubMed:15576788};
Vmax=4.7 umol/min/mg enzyme with dATP as substrate
{ECO:0000269|PubMed:15576788};
pH dependence:
Optimum pH is 8.5-9. {ECO:0000269|PubMed:15576788};
-!- DEVELOPMENTAL STAGE: Expressed during both vegetative growth and
early stage of sporulation.
-!- DISRUPTION PHENOTYPE: Growing cells lacking this gene have a 4-
fold increased spontaneous mutation frequency (a mild mutator
phenotype), as well as an increased sensitivity to DNA-damaging
agents such as H(2)O(2) or t-BHP. These phenotypes are increased
in a double ytkD/mutT disruption (PubMed:16513759). They are also
seen in stationary phase cells. Triple ytkD/mutM/mutY disrupted
strains show increased mutation rates during exponential and
stationary phase (PubMed:19011023). {ECO:0000269|PubMed:16513759,
ECO:0000269|PubMed:19011023}.
-!- MISCELLANEOUS: According to PubMed:14761999, can complement an
E.coli mutT mutant. According to PubMed:15576788, cannot
complement an E.coli mutT mutant.
-!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF008220; AAC00239.1; -; Genomic_DNA.
EMBL; AL009126; CAB15041.1; -; Genomic_DNA.
PIR; E69994; E69994.
RefSeq; NP_390941.1; NC_000964.3.
RefSeq; WP_003229087.1; NZ_JNCM01000036.1.
PDB; 4JZS; X-ray; 2.20 A; A/D=1-158.
PDB; 4JZT; X-ray; 2.90 A; A/D=1-158.
PDB; 4JZU; X-ray; 1.70 A; A/B=1-158.
PDB; 4JZV; X-ray; 2.20 A; A/B=1-158.
PDBsum; 4JZS; -.
PDBsum; 4JZT; -.
PDBsum; 4JZU; -.
PDBsum; 4JZV; -.
ProteinModelPortal; O35013; -.
SMR; O35013; -.
STRING; 224308.Bsubs1_010100016666; -.
PaxDb; O35013; -.
PRIDE; O35013; -.
EnsemblBacteria; CAB15041; CAB15041; BSU30630.
GeneID; 937072; -.
KEGG; bsu:BSU30630; -.
PATRIC; fig|224308.179.peg.3320; -.
eggNOG; COG0494; LUCA.
HOGENOM; HOG000027828; -.
InParanoid; O35013; -.
KO; K03574; -.
OMA; WVICRYG; -.
PhylomeDB; O35013; -.
BioCyc; BSUB:BSU30630-MONOMER; -.
BioCyc; MetaCyc:BSU30630-MONOMER; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
CDD; cd04665; Nudix_Hydrolase_8; 1.
InterPro; IPR020476; Nudix_hydrolase.
InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
InterPro; IPR020084; NUDIX_hydrolase_CS.
InterPro; IPR000086; NUDIX_hydrolase_dom.
InterPro; IPR014078; Nudix_YtkD.
Pfam; PF00293; NUDIX; 1.
PRINTS; PR00502; NUDIXFAMILY.
SUPFAM; SSF55811; SSF55811; 1.
TIGRFAMs; TIGR02705; nudix_YtkD; 1.
PROSITE; PS51462; NUDIX; 1.
PROSITE; PS00893; NUDIX_BOX; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Hydrolase; Magnesium; Metal-binding;
Reference proteome.
CHAIN 1 158 Putative 8-oxo-dGTP diphosphatase YtkD.
/FTId=PRO_0000057074.
DOMAIN 6 145 Nudix hydrolase. {ECO:0000255|PROSITE-
ProRule:PRU00794}.
MOTIF 53 74 Nudix box.
METAL 68 68 Magnesium. {ECO:0000250}.
METAL 72 72 Magnesium. {ECO:0000250}.
STRAND 2 5 {ECO:0000244|PDB:4JZU}.
STRAND 11 21 {ECO:0000244|PDB:4JZU}.
STRAND 26 34 {ECO:0000244|PDB:4JZU}.
STRAND 37 43 {ECO:0000244|PDB:4JZU}.
TURN 44 46 {ECO:0000244|PDB:4JZU}.
STRAND 47 49 {ECO:0000244|PDB:4JZU}.
STRAND 52 54 {ECO:0000244|PDB:4JZU}.
STRAND 57 59 {ECO:0000244|PDB:4JZV}.
HELIX 61 73 {ECO:0000244|PDB:4JZU}.
STRAND 75 89 {ECO:0000244|PDB:4JZU}.
STRAND 94 107 {ECO:0000244|PDB:4JZU}.
STRAND 114 124 {ECO:0000244|PDB:4JZU}.
HELIX 129 131 {ECO:0000244|PDB:4JZU}.
HELIX 137 139 {ECO:0000244|PDB:4JZU}.
STRAND 140 142 {ECO:0000244|PDB:4JZT}.
HELIX 143 154 {ECO:0000244|PDB:4JZU}.
SEQUENCE 158 AA; 18512 MW; F4AC08535F32CBD0 CRC64;
MYEFKDYYQN TVQLSFDDQP FSDSPKHVWV ICRFGGKWLL TEHEDRGYEF PGGKVEPMEC
AEEAALREVK EETGARVKSL KYLGQYKVLG KEKVIVKNIY FADIEKLEKQ ADYFETKGPV
LFHELPENLS RNKKFSFIMK DSVLPISLKK LKESGWIE


Related products :

Catalog number Product name Quantity
EIAAB28209 8-oxo-dGTPase NUDT15,mMTH2,Mouse,Mth2,Mus musculus,MutT homolog 2,Nucleoside diphosphate-linked moiety X motif 15,Nudix motif 15,Nudt15,Probable 7,8-dihydro-8-oxoguanine triphosphatase NUDT15
EIAAB28210 8-oxo-dGTPase NUDT15,Homo sapiens,Human,MTH2,MTH2,MutT homolog 2,Nucleoside diphosphate-linked moiety X motif 15,Nudix motif 15,NUDT15,Probable 7,8-dihydro-8-oxoguanine triphosphatase NUDT15
EH2255 7,8-dihydro-8-oxoguanine triphosphatase Elisa Kit 96T
CSB-EL016154RA Rat 7,8-dihydro-8-oxoguanine triphosphatase(NUDT1) ELISA kit 96T
CSB-EL016154HU Human 7,8-dihydro-8-oxoguanine triphosphatase(NUDT1) ELISA kit 96T
CSB-EL016154RA Rat 7,8-dihydro-8-oxoguanine triphosphatase(NUDT1) ELISA kit SpeciesRat 96T
CSB-EL016154MO Mouse 7,8-dihydro-8-oxoguanine triphosphatase(NUDT1) ELISA kit 96T
CSB-EL016154MO Mouse 7,8-dihydro-8-oxoguanine triphosphatase(NUDT1) ELISA kit SpeciesMouse 96T
CSB-EL016154HU Human 7,8-dihydro-8-oxoguanine triphosphatase(NUDT1) ELISA kit SpeciesHuman 96T
G0934 Probable 7, 8-dihydro-8-oxoguanine triphosphatase NUDT15 (NUDT15), Human, ELISA Kit 96T
CSB-EL016160HU Human Probable 7,8-dihydro-8-oxoguanine triphosphatase NUDT15(NUDT15) ELISA kit 96T
CSB-EL016160MO Mouse Probable 7,8-dihydro-8-oxoguanine triphosphatase NUDT15(NUDT15) ELISA kit 96T
G0935 Probable 7, 8-dihydro-8-oxoguanine triphosphatase NUDT15 (NUDT15), Mouse, ELISA Kit 96T
CSB-EL016160MO Mouse Probable 7,8-dihydro-8-oxoguanine triphosphatase NUDT15(NUDT15) ELISA kit SpeciesMouse 96T
CSB-EL016160HU Human Probable 7,8-dihydro-8-oxoguanine triphosphatase NUDT15(NUDT15) ELISA kit SpeciesHuman 96T
NUD15_MOUSE ELISA Kit FOR Probable 7,8-dihydro-8-oxoguanine triphosphatase NUDT15; organism: Mouse; gene name: Nudt15 96T
YT016 dGTP 1
K6011102-400 dGTP 400 µl (100 mM)
DG1000 dGTP 100 mM, 1 ml
YT016 dGTP 100 mM, 100 ml
D108 dGTP (100 mM) 40 ml
DG0100 100 mM dGTP 1 ml
509-043 dGTP, 100mM 1ml
2013G dGTP 1ml/vial
509-043 dGTP, 100mM 1ml


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur