53DR_BACSU
ID 53DR_BACSU Reviewed; 172 AA.
AC P68522; O31895; O64153;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=5'(3')-deoxyribonucleotidase {ECO:0000305|PubMed:25848029};
DE EC=3.1.3.- {ECO:0000305|PubMed:25848029};
DE AltName: Full=Putative SPbeta prophage-derived 5'(3')-deoxyribonucleotidase;
GN Name=yorS; OrderedLocusNames=BSU20270;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP FUNCTION, AND COFACTOR.
RX PubMed=25848029; DOI=10.1073/pnas.1423570112;
RA Huang H., Pandya C., Liu C., Al-Obaidi N.F., Wang M., Zheng L.,
RA Toews Keating S., Aono M., Love J.D., Evans B., Seidel R.D.,
RA Hillerich B.S., Garforth S.J., Almo S.C., Mariano P.S., Dunaway-Mariano D.,
RA Allen K.N., Farelli J.D.;
RT "Panoramic view of a superfamily of phosphatases through substrate
RT profiling.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E1974-E1983(2015).
CC -!- FUNCTION: Dephosphorylates nucleoside monophosphates such as the 5' and
CC 2'(3')-phosphates of deoxyribonucleotides in vitro. Also catalyzes the
CC dephosphorylation of coenzyme A (CoA), pyridoxal-5'-phosphate (PLP),
CC riboflavine-5-phosphate (FMN) and nicotinamide adenine dinucleotide
CC phosphate (NADP) in vitro. {ECO:0000269|PubMed:25848029}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:25848029};
CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family.
CC {ECO:0000305}.
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DR EMBL; AL009126; CAB13919.1; -; Genomic_DNA.
DR PIR; T12904; T12904.
DR RefSeq; NP_389909.1; NC_000964.3.
DR RefSeq; WP_004399368.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P68522; -.
DR SMR; P68522; -.
DR STRING; 224308.BSU20270; -.
DR PaxDb; P68522; -.
DR PRIDE; P68522; -.
DR DNASU; 939520; -.
DR EnsemblBacteria; CAB13919; CAB13919; BSU_20270.
DR GeneID; 939520; -.
DR KEGG; bsu:BSU20270; -.
DR PATRIC; fig|224308.179.peg.2217; -.
DR eggNOG; COG4502; Bacteria.
DR InParanoid; P68522; -.
DR OMA; FNAKFRW; -.
DR BioCyc; BSUB:BSU20270-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0008253; F:5'-nucleotidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009223; P:pyrimidine deoxyribonucleotide catabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR010708; 5'(3')-deoxyribonucleotidase.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR Pfam; PF06941; NT5C; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..172
FT /note="5'(3')-deoxyribonucleotidase"
FT /id="PRO_0000164373"
FT ACT_SITE 8
FT /note="Nucleophile"
FT /evidence="ECO:0000305"
FT ACT_SITE 10
FT /note="Proton donor"
FT /evidence="ECO:0000305"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8CTG7"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8CTG7"
FT BINDING 132
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8CTG7"
SQ SEQUENCE 172 AA; 20417 MW; CA89B7BA30226EE8 CRC64;
MKKVIAIDMD QVLADLLSDW VAYINTYDDP FLKEKDILCW DIKKYTNTNN NVYRHLDYDL
FRNLNVIEGS QRVTKELMKK YEVYVVTTAT NHPDSLKAKL EWLTEYFPFI PHSNVVLCGN
KNIIKADIMI DDGIHNLESF EGMKILFDAP HNRNENRFIR VMNWEEIERK LL
