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Protein

Blasticidin-S deaminase

Gene

bsd

Organism
Aspergillus terreus
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the deamination of the cytosine moiety of the antibiotics blasticidin S, cytomycin and acetylblasticidin S.

Catalytic activityi

Blasticidin S + H2O = deaminohydroxyblasticidin S + NH3.

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei28 – 281Substrate
Metal bindingi54 – 541Zinc; catalytic
Active sitei56 – 561Proton donor
Binding sitei82 – 821Substrate
Metal bindingi88 – 881Zinc; catalytic
Metal bindingi91 – 911Zinc; catalytic
Binding sitei126 – 1261Substrate; shared with homotetrameric partner
Binding sitei128 – 1281Substrate

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antibiotic resistance

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.4.23. 536.

Names & Taxonomyi

Protein namesi
Recommended name:
Blasticidin-S deaminase (EC:3.5.4.23)
Gene namesi
Name:bsd
OrganismiAspergillus terreus
Taxonomic identifieri33178 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi56 – 561E → D: Loss of activity. 1 Publication
Mutagenesisi56 – 561E → Q: Loss of activity. 1 Publication
Mutagenesisi91 – 911C → A: Loss of activity. 1 Publication
Mutagenesisi91 – 911C → S: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 130130Blasticidin-S deaminasePRO_0000171689Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

1
130
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 2016Combined sources
Beta strandi25 – 273Combined sources
Beta strandi29 – 357Combined sources
Beta strandi40 – 445Combined sources
Turni49 – 513Combined sources
Helixi55 – 6511Combined sources
Beta strandi71 – 788Combined sources
Turni79 – 824Combined sources
Beta strandi83 – 853Combined sources
Helixi89 – 9810Combined sources
Beta strandi103 – 1075Combined sources
Beta strandi113 – 1175Combined sources
Helixi118 – 1214Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WN5X-ray1.80A/B/C/D1-130[»]
1WN6X-ray1.80A/B1-130[»]
2Z3GX-ray1.50A/B/C/D1-130[»]
2Z3HX-ray1.50A/B/C/D1-130[»]
2Z3IX-ray1.80A/B/C/D1-130[»]
2Z3JX-ray1.60A/B/C/D1-130[»]
ProteinModelPortaliP0C2P0.
SMRiP0C2P0. Positions 2-128.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C2P0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 129129CMP/dCMP-type deaminasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 CMP/dCMP-type deaminase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410JEFU. Eukaryota.
ENOG4111Y4T. LUCA.
HOGENOMiHOG000014707.

Family and domain databases

InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
[Graphical view]
PfamiPF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]
SUPFAMiSSF53927. SSF53927. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES_1. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0C2P0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLSQEESTL IERATATINS IPISEDYSVA SAALSSDGRI FTGVNVYHFT
60 70 80 90 100
GGPCAELVVL GTAAAAAAGN LTCIVAIGNE NRGILSPCGR CRQVLLDLHP
110 120 130
GIKAIVKDSD GQPTAVGIRE LLPSGYVWEG
Length:130
Mass (Da):13,468
Last modified:April 3, 2007 - v1
Checksum:i98D644B05110EE24
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D83710 mRNA. Translation: BAA12074.1.
PIRiS41571.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D83710 mRNA. Translation: BAA12074.1.
PIRiS41571.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WN5X-ray1.80A/B/C/D1-130[»]
1WN6X-ray1.80A/B1-130[»]
2Z3GX-ray1.50A/B/C/D1-130[»]
2Z3HX-ray1.50A/B/C/D1-130[»]
2Z3IX-ray1.80A/B/C/D1-130[»]
2Z3JX-ray1.60A/B/C/D1-130[»]
ProteinModelPortaliP0C2P0.
SMRiP0C2P0. Positions 2-128.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410JEFU. Eukaryota.
ENOG4111Y4T. LUCA.
HOGENOMiHOG000014707.

Enzyme and pathway databases

BRENDAi3.5.4.23. 536.

Miscellaneous databases

EvolutionaryTraceiP0C2P0.

Family and domain databases

InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
[Graphical view]
PfamiPF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]
SUPFAMiSSF53927. SSF53927. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES_1. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning of the blasticidin S deaminase gene (BSD) from Aspergillus terreus and its use as a selectable marker for Schizosaccharomyces pombe and Pyricularia oryzae."
    Kimura M., Kamakura T., Tao Q.Z., Kaneko I., Yamaguchi I.
    Mol. Gen. Genet. 242:121-129(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: S-712 / ATCC 28865.
  2. "Expression, purification, and characterization of blasticidin S deaminase (BSD) from Aspergillus terreus: the role of catalytic zinc in enzyme structure."
    Kimura M., Sekido S., Isogai Y., Yamaguchi I.
    J. Biochem. 127:955-963(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, MUTAGENESIS OF GLU-56 AND CYS-91.
  3. "Crystallization and preliminary X-ray diffraction studies of blasticidin S deaminase from Aspergillus terreus."
    Nakasako M., Kimura M., Yamaguchi I.
    Acta Crystallogr. D 55:547-548(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  4. "Crystal structures of blasticidin S deaminase (BSD): implications for dynamic properties of catalytic zinc."
    Kumasaka T., Yamamoto M., Furuichi M., Nakasako M., Teh A.H., Kimura M., Yamaguchi I., Ueki T.
    J. Biol. Chem. 282:37103-37111(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE AND ZINC IONS, SUBUNIT.

Entry informationi

Entry nameiBSD_ASPTE
AccessioniPrimary (citable) accession number: P0C2P0
Secondary accession number(s): P78986, Q0CGS9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: April 3, 2007
Last modified: November 11, 2015
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.