ID   BSR_BACCE               Reviewed;         140 AA.
AC   P33967;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Blasticidin-S deaminase;
DE            EC=3.5.4.23;
GN   Name=bsr;
OS   Bacillus cereus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-46, AND FUNCTION.
RC   STRAIN=K55-S1;
RX   PubMed=1368770; DOI=10.1271/bbb1961.55.3155;
RA   Kobayashi K., Kamakura T., Tanaka T., Yamaguchi I., Endo T.;
RT   "Nucleotide sequence of the bsr gene and N-terminal amino acid sequence of
RT   blasticidin S deaminase from blasticidin S resistant Escherichia coli
RT   TK121.";
RL   Agric. Biol. Chem. 55:3155-3157(1991).
CC   -!- FUNCTION: Catalyzes the deamination of the cytosine moiety of the
CC       antibiotics blasticidin S, cytomycin and acetylblasticidin S.
CC       {ECO:0000269|PubMed:1368770}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=blasticidin S + H(+) + H2O = deaminohydroxyblasticidin S +
CC         NH4(+); Xref=Rhea:RHEA:10148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:57289, ChEBI:CHEBI:57697; EC=3.5.4.23;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. {ECO:0000305}.
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DR   EMBL; S81409; AAC60404.1; -; Genomic_DNA.
DR   PIR; JS0609; JS0609.
DR   AlphaFoldDB; P33967; -.
DR   SMR; P33967; -.
DR   GO; GO:0047711; F:blasticidin-S deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR   InterPro; IPR002125; CMP_dCMP_dom.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR   SUPFAM; SSF53927; SSF53927; 1.
DR   PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR   PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE   1: Evidence at protein level;
KW   Antibiotic resistance; Direct protein sequencing; Hydrolase; Metal-binding;
KW   Zinc.
FT   CHAIN           1..140
FT                   /note="Blasticidin-S deaminase"
FT                   /id="PRO_0000171690"
FT   DOMAIN          8..140
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT   ACT_SITE        61
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         59
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   140 AA;  15573 MW;  603DD6CC9F1C8F59 CRC64;
     MKTFNISQQD LELVEVATEK ITMLYEDNKH HVGAAIRTKT GEIISAVHIE AYIGRVTVCA
     EAIAIGSAVS NGQKDFDTIV AVRHPYSDEV DRSIRVVSPC GMCRELISDY APDCFVLIEM
     NGKLVKTTIE ELIPLKYTRN