ID   BSD_ASPTN               Reviewed;         130 AA.
AC   P0C2P1; P78986; Q0CGS9;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Blasticidin-S deaminase;
DE            EC=3.5.4.23;
GN   Name=bsd; ORFNames=ATEG_07113;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the deamination of the cytosine moiety of the
CC       antibiotics blasticidin S, cytomycin and acetylblasticidin S.
CC       {ECO:0000250}.
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   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. {ECO:0000305}.
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DR   EMBL; CH476603; EAU32497.1; -; Genomic_DNA.
DR   RefSeq; XP_001209799.1; XM_001209799.1.
DR   AlphaFoldDB; P0C2P1; -.
DR   SMR; P0C2P1; -.
DR   EnsemblFungi; EAU32497; EAU32497; ATEG_07113.
DR   GeneID; 4318849; -.
DR   VEuPathDB; FungiDB:ATEG_07113; -.
DR   eggNOG; ENOG502ST2E; Eukaryota.
DR   HOGENOM; CLU_097262_4_1_1; -.
DR   OMA; RYRNDWQ; -.
DR   OrthoDB; 1400471at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
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:0006139; P:nucleobase-containing compound metabolic process; IEA:UniProt.
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   3: Inferred from homology;
KW   Antibiotic resistance; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..130
FT                   /note="Blasticidin-S deaminase"
FT                   /id="PRO_0000283714"
FT   DOMAIN          1..129
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT   ACT_SITE        56
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         28
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between two homotetrameric
FT                   partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         82
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between two homotetrameric
FT                   partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         91
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between two homotetrameric
FT                   partners"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   130 AA;  13455 MW;  9D77B27B0110EE24 CRC64;
     MPLSQEESTL IERATATINS IPISEDYSVA SAALSSDGRI FTGVNVYHFT GGPCAELVVL
     GTAAAAAAGN LTCIVAIGNE NRGILSPCGR CRQVLLDLHP GIKAVVKDSD GQPTAVGIRE
     LLPSGYMNRA