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Blasticidin-S deaminase (EC 3.5.4.23)

 BSD_ASPTE               Reviewed;         130 AA.
P0C2P0; P78986; Q0CGS9;
03-APR-2007, integrated into UniProtKB/Swiss-Prot.
03-APR-2007, sequence version 1.
07-JUN-2017, entry version 53.
RecName: Full=Blasticidin-S deaminase;
EC=3.5.4.23;
Name=bsd;
Aspergillus terreus.
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
NCBI_TaxID=33178;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=S-712 / ATCC 28865;
PubMed=8159161; DOI=10.1007/BF00391004;
Kimura M., Kamakura T., Tao Q.Z., Kaneko I., Yamaguchi I.;
"Cloning of the blasticidin S deaminase gene (BSD) from Aspergillus
terreus and its use as a selectable marker for Schizosaccharomyces
pombe and Pyricularia oryzae.";
Mol. Gen. Genet. 242:121-129(1994).
[2]
CHARACTERIZATION, AND MUTAGENESIS OF GLU-56 AND CYS-91.
PubMed=10833262; DOI=10.1093/oxfordjournals.jbchem.a022711;
Kimura M., Sekido S., Isogai Y., Yamaguchi I.;
"Expression, purification, and characterization of blasticidin S
deaminase (BSD) from Aspergillus terreus: the role of catalytic zinc
in enzyme structure.";
J. Biochem. 127:955-963(2000).
[3]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=10089374; DOI=10.1107/S0907444998011809;
Nakasako M., Kimura M., Yamaguchi I.;
"Crystallization and preliminary X-ray diffraction studies of
blasticidin S deaminase from Aspergillus terreus.";
Acta Crystallogr. D 55:547-548(1999).
[4]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE AND
ZINC IONS, AND SUBUNIT.
PubMed=17959604; DOI=10.1074/jbc.M704476200;
Kumasaka T., Yamamoto M., Furuichi M., Nakasako M., Teh A.H.,
Kimura M., Yamaguchi I., Ueki T.;
"Crystal structures of blasticidin S deaminase (BSD): implications for
dynamic properties of catalytic zinc.";
J. Biol. Chem. 282:37103-37111(2007).
-!- FUNCTION: Catalyzes the deamination of the cytosine moiety of the
antibiotics blasticidin S, cytomycin and acetylblasticidin S.
-!- CATALYTIC ACTIVITY: Blasticidin S + H(2)O =
deaminohydroxyblasticidin S + NH(3).
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17959604}.
-!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
family. {ECO:0000305}.
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EMBL; D83710; BAA12074.1; -; mRNA.
PIR; S41571; S41571.
PDB; 1WN5; X-ray; 1.80 A; A/B/C/D=1-130.
PDB; 1WN6; X-ray; 1.80 A; A/B=1-130.
PDB; 2Z3G; X-ray; 1.50 A; A/B/C/D=1-130.
PDB; 2Z3H; X-ray; 1.50 A; A/B/C/D=1-130.
PDB; 2Z3I; X-ray; 1.80 A; A/B/C/D=1-130.
PDB; 2Z3J; X-ray; 1.60 A; A/B/C/D=1-130.
PDBsum; 1WN5; -.
PDBsum; 1WN6; -.
PDBsum; 2Z3G; -.
PDBsum; 2Z3H; -.
PDBsum; 2Z3I; -.
PDBsum; 2Z3J; -.
ProteinModelPortal; P0C2P0; -.
SMR; P0C2P0; -.
DrugBank; DB04649; TETRAHEDRAL INTERMEDIATE OF BLASTICIDIN S.
eggNOG; ENOG410JEFU; Eukaryota.
eggNOG; ENOG4111Y4T; LUCA.
HOGENOM; HOG000014707; -.
BRENDA; 3.5.4.23; 536.
EvolutionaryTrace; P0C2P0; -.
GO; GO:0047711; F:blasticidin-S deaminase activity; IEA:UniProtKB-EC.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
InterPro; IPR002125; CMP_dCMP_dom.
InterPro; IPR016193; Cytidine_deaminase-like.
Pfam; PF00383; dCMP_cyt_deam_1; 1.
SUPFAM; SSF53927; SSF53927; 1.
PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
1: Evidence at protein level;
3D-structure; Antibiotic resistance; Hydrolase; Metal-binding; Zinc.
CHAIN 1 130 Blasticidin-S deaminase.
/FTId=PRO_0000171689.
DOMAIN 1 129 CMP/dCMP-type deaminase.
{ECO:0000255|PROSITE-ProRule:PRU01083}.
ACT_SITE 56 56 Proton donor.
METAL 54 54 Zinc; catalytic.
METAL 88 88 Zinc; catalytic.
METAL 91 91 Zinc; catalytic.
BINDING 28 28 Substrate.
BINDING 82 82 Substrate.
BINDING 126 126 Substrate; shared with homotetrameric
partner.
BINDING 128 128 Substrate.
MUTAGEN 56 56 E->D: Loss of activity.
{ECO:0000269|PubMed:10833262}.
MUTAGEN 56 56 E->Q: Loss of activity.
{ECO:0000269|PubMed:10833262}.
MUTAGEN 91 91 C->A: Loss of activity.
{ECO:0000269|PubMed:10833262}.
MUTAGEN 91 91 C->S: Loss of activity.
{ECO:0000269|PubMed:10833262}.
HELIX 5 20 {ECO:0000244|PDB:2Z3G}.
STRAND 25 27 {ECO:0000244|PDB:2Z3G}.
STRAND 29 35 {ECO:0000244|PDB:2Z3G}.
STRAND 40 44 {ECO:0000244|PDB:2Z3G}.
TURN 49 51 {ECO:0000244|PDB:2Z3G}.
HELIX 55 65 {ECO:0000244|PDB:2Z3G}.
STRAND 71 78 {ECO:0000244|PDB:2Z3G}.
TURN 79 82 {ECO:0000244|PDB:2Z3G}.
STRAND 83 85 {ECO:0000244|PDB:2Z3G}.
HELIX 89 98 {ECO:0000244|PDB:2Z3G}.
STRAND 103 107 {ECO:0000244|PDB:2Z3G}.
STRAND 113 117 {ECO:0000244|PDB:2Z3G}.
HELIX 118 121 {ECO:0000244|PDB:2Z3G}.
SEQUENCE 130 AA; 13468 MW; 98D644B05110EE24 CRC64;
MPLSQEESTL IERATATINS IPISEDYSVA SAALSSDGRI FTGVNVYHFT GGPCAELVVL
GTAAAAAAGN LTCIVAIGNE NRGILSPCGR CRQVLLDLHP GIKAIVKDSD GQPTAVGIRE
LLPSGYVWEG


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