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Protein
Submitted name:

Polysaccharide deacetylase

Gene

BC_0361

Organism
Bacillus cereus (strain ATCC 14579 / DSM 31)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi206 – 2061ZincCombined sources
Metal bindingi264 – 2641Zinc; via tele nitrogenCombined sources
Metal bindingi268 – 2681Zinc; via tele nitrogenCombined sources

GO - Molecular functioni

  1. hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds Source: InterPro
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Ligandi

Metal-bindingCombined sources, ZincCombined sources

Enzyme and pathway databases

BioCyciBCER226900:GJEU-363-MONOMER.

Names & Taxonomyi

Protein namesi
Submitted name:
Polysaccharide deacetylaseImported
Gene namesi
Ordered Locus Names:BC_0361Imported
OrganismiBacillus cereus (strain ATCC 14579 / DSM 31)Imported
Taxonomic identifieri226900 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000001417: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi226900.BC0361.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4HD5X-ray1.90A1-360[»]
ProteinModelPortaliQ81IM3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiCOG0726.
OMAiTEYMIVD.
OrthoDBiEOG6RRKJF.

Family and domain databases

Gene3Di3.20.20.370. 1 hit.
InterProiIPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR002509. Polysac_deacetylase.
[Graphical view]
PfamiPF01522. Polysacc_deac_1. 1 hit.
[Graphical view]
SUPFAMiSSF88713. SSF88713. 1 hit.
PROSITEiPS51677. NODB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q81IM3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKYAAIALC TSAILAGCNT SNVSQEPKKE KKVQEVAIQK EALQEQGKIS
60 70 80 90 100
YTPITHESTN TSIHITDLKD SLNEVQYKIW RTADGKERAK SFSSKEKEKQ
110 120 130 140 150
FTIPFDIKEF EGKRGEFQIE ATGMKEDGKT IPLTKSIITF EQKVPVLMYH
160 170 180 190 200
AIDDYHGQGI KDLFVSPANF EAQMKHLKDN GYTLLTFERW GDINKVNKPI
210 220 230 240 250
FVTFDDGMKN NMNAFRVLQK LKDDTFKPAA TEYMIVDNVD VEGALSTSEI
260 270 280 290 300
KEMVDSGIFS VQSHTATHAD LPKITNYEEE LKGSKEKLEK ITGKPVIAIA
310 320 330 340 350
YPFGHVDDKV VTETKKYYQF ATTTKPGQFI TKGEPDELLK MKRVRIHHTT
360
TVEQFASSIK
Length:360
Mass (Da):40,794
Last modified:June 1, 2003 - v1
Checksum:i4454545D5A0FC6EC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016877 Genomic DNA. Translation: AAP07401.1.
RefSeqiNP_830200.1. NC_004722.1.

Genome annotation databases

EnsemblBacteriaiAAP07401; AAP07401; BC_0361.
GeneIDi1202714.
KEGGibce:BC0361.
PATRICi32596350. VBIBacCer54481_0332.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016877 Genomic DNA. Translation: AAP07401.1.
RefSeqiNP_830200.1. NC_004722.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4HD5X-ray1.90A1-360[»]
ProteinModelPortaliQ81IM3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi226900.BC0361.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP07401; AAP07401; BC_0361.
GeneIDi1202714.
KEGGibce:BC0361.
PATRICi32596350. VBIBacCer54481_0332.

Phylogenomic databases

eggNOGiCOG0726.
OMAiTEYMIVD.
OrthoDBiEOG6RRKJF.

Enzyme and pathway databases

BioCyciBCER226900:GJEU-363-MONOMER.

Family and domain databases

Gene3Di3.20.20.370. 1 hit.
InterProiIPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR002509. Polysac_deacetylase.
[Graphical view]
PfamiPF01522. Polysacc_deac_1. 1 hit.
[Graphical view]
SUPFAMiSSF88713. SSF88713. 1 hit.
PROSITEiPS51677. NODB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 14579 / DSM 31Imported.
  2. "Structure determination through homology modelling and torsion-angle simulated annealing: application to a polysaccharide deacetylase from Bacillus cereus."
    Fadouloglou V.E., Kapanidou M., Agiomirgianaki A., Arnaouteli S., Bouriotis V., Glykos N.M., Kokkinidis M.
    Acta Crystallogr. D 69:276-283(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ZINC.

Entry informationi

Entry nameiQ81IM3_BACCR
AccessioniPrimary (citable) accession number: Q81IM3
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 2003
Last sequence update: June 1, 2003
Last modified: March 4, 2015
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

External Data

Dasty 3

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 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.