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Q06GJ0 (Q06GJ0_OSTFU) Unreviewed, UniProtKB/TrEMBL

Last modified December 11, 2013. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length594 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. PIRNR PIRNR001093

Sequence similarities

Belongs to the glycosyl hydrolase 20 family. PIRNR PIRNR001093

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site3681Proton donor By similarity PIRSR PIRSR001093-1
Binding site1321N-acetyl-D-glucosamine PDB 3VTR
Binding site1641N-acetyl-D-glucosamine PDB 3VTR
Binding site3751N-acetyl-D-glucosamine PDB 3VTR
Binding site3911N-acetyl-D-glucosamine; via carbonyl oxygen PDB 3VTR

Sequences

Sequence LengthMass (Da)Tools
Q06GJ0 [UniParc].

Last modified October 31, 2006. Version 1.
Checksum: 87E8DE2ADE107ED9

FASTA59467,964
        10         20         30         40         50         60 
MWSRRIPLFI FGVLVLILSV AAEDVVWRWS CDNGKCVKLK NDPRSSEPAL SLEACKMFCN 

        70         80         90        100        110        120 
EYGLLWPRPT GEADLGNFLS KINLNSIEVK ILKKGATDDL MEAAAKRFKE QVSLAIPRGS 

       130        140        150        160        170        180 
TPKLTGKAVD VYLVNENPNE KAFSLEMDES YGLRVSPSGA DRVNATITAN SFFGMRHGLE 

       190        200        210        220        230        240 
TLSQLFVFDD IRDHLLMVRD VNISDKPVYP YRGILLDTAR NYYSIESIKR TIEAMAAVKL 

       250        260        270        280        290        300 
NTFHWHITDS QSFPFVTTKR PNLYKFGALS PQKVYTKAAI REVVRFGLER GVRVLPEFDA 

       310        320        330        340        350        360 
PAHVGEGWQD TDLTVCFKAE PWKSYCVEPP CGQLNPTKDE LYQYLEDIYS DMAEVFDTTD 

       370        380        390        400        410        420 
IFHMGGDEVS EACWNSSDSI QNFMMQNRWD LDKESFLKLW NYFQQKAQDK AYKAFGKKLP 

       430        440        450        460        470        480 
LILWTSTLTN YKHIDDYLNK DDYIIQVWTT GVDPQIKGLL EKGYRLIMSN YDALYFDCGY 

       490        500        510        520        530        540 
GAWVGAGNNW CSPYIGWQKV YDNSPAVIAL EHRDQVLGGE AALWSEQSDT STLDGRLWPR 

       550        560        570        580        590 
AAALAERLWA EPATSWQDAE YRMLHIRERL VRMGIQAESL QPEWCYQNEG YCYS 

« Hide

References

[1]"A novel beta-N-acetyl-D-hexosaminidase from the insect Ostrinia furnacalis (Guenee)."
Yang Q., Liu T., Liu F., Qu M., Qian X.
FEBS J. 275:5690-5702(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[2]"Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 complexed with NGT."
Zhang H., Liu T., Liu F., Shen X., Yang Q.
Submitted (SEP-2010) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 23-594.
[3]"Active-pocket size differentiating insectile from bacterial chitinolytic ?-N-acetyl-D-hexosaminidases."
Liu T., Zhang H., Liu F., Chen L., Shen X., Yang Q.
Biochem. J. 438:467-474(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 23-594.
[4]"Structural determinants of an insect beta-N-Acetyl-D-hexosaminidase specialized as a chitinolytic enzyme."
Liu T., Zhang H., Liu F., Wu Q., Shen X., Yang Q.
J. Biol. Chem. 286:4049-4058(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 23-594.
[5]"Structural insights into cellulolytic and chitinolytic enzymes revealing crucial residues of insect ?-N-acetyl-D-hexosaminidase."
Liu T., Zhou Y., Chen L., Chen W., Liu L., Shen X., Zhang W., Zhang J., Yang Q.
PLoS ONE 7:e52225-e52225(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 23-594 IN COMPLEX WITH N-ACETYL-D-GLUCOSAMINE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ887769 mRNA. Translation: ABI81756.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3NSMX-ray2.10A23-594[»]
3NSNX-ray2.10A23-594[»]
3OZOX-ray2.00A23-594[»]
3OZPX-ray2.00A23-594[»]
3S6TX-ray2.30A20-594[»]
3VTRX-ray2.50A23-594[»]
ProteinModelPortalQ06GJ0.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH20. Glycoside Hydrolase Family 20.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR025705. Beta_hexosaminidase_sua/sub.
IPR015883. Glyco_hydro_20_cat-core.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00728. Glyco_hydro_20. 1 hit.
[Graphical view]
PIRSFPIRSF001093. B-hxosamndse_ab_euk_. 1 hit.
PRINTSPR00738. GLHYDRLASE20.
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ06GJ0.

Entry information

Entry nameQ06GJ0_OSTFU
AccessionPrimary (citable) accession number: Q06GJ0
Entry history
Integrated into UniProtKB/TrEMBL: October 31, 2006
Last sequence update: October 31, 2006
Last modified: December 11, 2013
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)