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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)DescriptionActionsGraphical viewLength
Binding sitei28Substrate1
Metal bindingi54Zinc; catalytic1
Active sitei56Proton donor1
Binding sitei82Substrate1
Metal bindingi88Zinc; catalytic1
Metal bindingi91Zinc; catalytic1
Binding sitei126Substrate; shared with homotetrameric partner1
Binding sitei128Substrate1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processAntibiotic resistance
LigandMetal-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)DescriptionActionsGraphical viewLength
Mutagenesisi56E → D: Loss of activity. 1 Publication1
Mutagenesisi56E → Q: Loss of activity. 1 Publication1
Mutagenesisi91C → A: Loss of activity. 1 Publication1
Mutagenesisi91C → S: Loss of activity. 1 Publication1

Chemistry databases

DrugBankiDB04649. TETRAHEDRAL INTERMEDIATE OF BLASTICIDIN S.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001716891 – 130Blasticidin-S deaminaseAdd BLAST130

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

1130
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 20Combined sources16
Beta strandi25 – 27Combined sources3
Beta strandi29 – 35Combined sources7
Beta strandi40 – 44Combined sources5
Turni49 – 51Combined sources3
Helixi55 – 65Combined sources11
Beta strandi71 – 78Combined sources8
Turni79 – 82Combined sources4
Beta strandi83 – 85Combined sources3
Helixi89 – 98Combined sources10
Beta strandi103 – 107Combined sources5
Beta strandi113 – 117Combined sources5
Helixi118 – 121Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C2P0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 129CMP/dCMP-type deaminasePROSITE-ProRule annotationAdd BLAST129

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410JEFU. Eukaryota.
ENOG4111Y4T. LUCA.
HOGENOMiHOG000014707.

Family and domain databases

InterProiView protein in InterPro
IPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_dom.
IPR016193. Cytidine_deaminase-like.
PfamiView protein in Pfam
PF00383. dCMP_cyt_deam_1. 1 hit.
SUPFAMiSSF53927. SSF53927. 1 hit.
PROSITEiView protein in PROSITE
PS00903. CYT_DCMP_DEAMINASES_1. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 1 hit.

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

DrugBankiDB04649. TETRAHEDRAL INTERMEDIATE OF BLASTICIDIN S.

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

InterProiView protein in InterPro
IPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_dom.
IPR016193. Cytidine_deaminase-like.
PfamiView protein in Pfam
PF00383. dCMP_cyt_deam_1. 1 hit.
SUPFAMiSSF53927. SSF53927. 1 hit.
PROSITEiView protein in PROSITE
PS00903. CYT_DCMP_DEAMINASES_1. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiBSD_ASPTE
AccessioniPrimary (citable) accession number: P0C2P0
Secondary accession number(s): P78986, Q0CGS9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: April 3, 2007
Last modified: June 7, 2017
This is version 53 of the entry and version 1 of the sequence. See 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.