BSD_ASPTE
ID BSD_ASPTE Reviewed; 130 AA.
AC P0C2P0; P78986; Q0CGS9;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Blasticidin-S deaminase;
DE EC=3.5.4.23;
GN Name=bsd;
OS Aspergillus terreus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=33178;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=S-712 / ATCC 28865;
RX PubMed=8159161; DOI=10.1007/bf00391004;
RA Kimura M., Kamakura T., Tao Q.Z., Kaneko I., Yamaguchi I.;
RT "Cloning of the blasticidin S deaminase gene (BSD) from Aspergillus terreus
RT and its use as a selectable marker for Schizosaccharomyces pombe and
RT Pyricularia oryzae.";
RL Mol. Gen. Genet. 242:121-129(1994).
RN [2]
RP CHARACTERIZATION, AND MUTAGENESIS OF GLU-56 AND CYS-91.
RX PubMed=10833262; DOI=10.1093/oxfordjournals.jbchem.a022711;
RA Kimura M., Sekido S., Isogai Y., Yamaguchi I.;
RT "Expression, purification, and characterization of blasticidin S deaminase
RT (BSD) from Aspergillus terreus: the role of catalytic zinc in enzyme
RT structure.";
RL J. Biochem. 127:955-963(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=10089374; DOI=10.1107/s0907444998011809;
RA Nakasako M., Kimura M., Yamaguchi I.;
RT "Crystallization and preliminary X-ray diffraction studies of blasticidin S
RT deaminase from Aspergillus terreus.";
RL Acta Crystallogr. D 55:547-548(1999).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE AND ZINC
RP IONS, AND SUBUNIT.
RX PubMed=17959604; DOI=10.1074/jbc.m704476200;
RA Kumasaka T., Yamamoto M., Furuichi M., Nakasako M., Teh A.H., Kimura M.,
RA Yamaguchi I., Ueki T.;
RT "Crystal structures of blasticidin S deaminase (BSD): implications for
RT dynamic properties of catalytic zinc.";
RL J. Biol. Chem. 282:37103-37111(2007).
CC -!- FUNCTION: Catalyzes the deamination of the cytosine moiety of the
CC antibiotics blasticidin S, cytomycin and acetylblasticidin S.
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;
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17959604}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000305}.
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DR EMBL; D83710; BAA12074.1; -; mRNA.
DR PIR; S41571; S41571.
DR PDB; 1WN5; X-ray; 1.80 A; A/B/C/D=1-130.
DR PDB; 1WN6; X-ray; 1.80 A; A/B=1-130.
DR PDB; 2Z3G; X-ray; 1.50 A; A/B/C/D=1-130.
DR PDB; 2Z3H; X-ray; 1.50 A; A/B/C/D=1-130.
DR PDB; 2Z3I; X-ray; 1.80 A; A/B/C/D=1-130.
DR PDB; 2Z3J; X-ray; 1.60 A; A/B/C/D=1-130.
DR PDBsum; 1WN5; -.
DR PDBsum; 1WN6; -.
DR PDBsum; 2Z3G; -.
DR PDBsum; 2Z3H; -.
DR PDBsum; 2Z3I; -.
DR PDBsum; 2Z3J; -.
DR AlphaFoldDB; P0C2P0; -.
DR SMR; P0C2P0; -.
DR DrugBank; DB04649; TETRAHEDRAL INTERMEDIATE OF BLASTICIDIN S.
DR VEuPathDB; FungiDB:ATEG_07113; -.
DR BRENDA; 3.5.4.23; 536.
DR EvolutionaryTrace; P0C2P0; -.
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 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Hydrolase; Metal-binding; Zinc.
FT CHAIN 1..130
FT /note="Blasticidin-S deaminase"
FT /id="PRO_0000171689"
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 BINDING 28
FT /ligand="substrate"
FT /ligand_note="ligand shared between two homotetrameric
FT partners"
FT /note="in other chain"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 82
FT /ligand="substrate"
FT /ligand_note="ligand shared between two homotetrameric
FT partners"
FT /note="in other chain"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 126
FT /ligand="substrate"
FT /ligand_note="ligand shared between two homotetrameric
FT partners"
FT BINDING 128
FT /ligand="substrate"
FT /ligand_note="ligand shared between two homotetrameric
FT partners"
FT /note="in other chain"
FT MUTAGEN 56
FT /note="E->D: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10833262"
FT MUTAGEN 56
FT /note="E->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10833262"
FT MUTAGEN 91
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10833262"
FT MUTAGEN 91
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10833262"
FT HELIX 5..20
FT /evidence="ECO:0007829|PDB:2Z3G"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:2Z3G"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:2Z3G"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:2Z3G"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:2Z3G"
FT HELIX 55..65
FT /evidence="ECO:0007829|PDB:2Z3G"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:2Z3G"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:2Z3G"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:2Z3G"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:2Z3G"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:2Z3G"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:2Z3G"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:2Z3G"
SQ SEQUENCE 130 AA; 13468 MW; 98D644B05110EE24 CRC64;
MPLSQEESTL IERATATINS IPISEDYSVA SAALSSDGRI FTGVNVYHFT GGPCAELVVL
GTAAAAAAGN LTCIVAIGNE NRGILSPCGR CRQVLLDLHP GIKAIVKDSD GQPTAVGIRE
LLPSGYVWEG
