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Q89ZI2 (OGA_BACTN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
O-GlcNAcase BT_4395
EC=3.2.1.169
Alternative name(s):
Beta-N-acetylhexosaminidase
Beta-hexosaminidase
GH84
Hexosaminidase B
N-acetyl-beta-glucosaminidase
Gene names
Ordered Locus Names:BT_4395
OrganismBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Taxonomic identifier226186 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides

Protein attributes

Sequence length737 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Biological function unknown. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins.

Catalytic activity

[Protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine + H2O = [protein]-L-serine + N-acetyl-D-glucosamine. Ref.2

[Protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine + H2O = [protein]-L-threonine + N-acetyl-D-glucosamine.

Enzyme regulation

Inhibited by 1,2-dideoxy-2'-methyl-alpha-D-glucopyranoso-[2,1-d]-delta 2'-thiazoline (NAG-thiazoline) and O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenyl-carbamate (PUGNAc). Not inhibited by Streptozotocin. Ref.2

Subunit structure

Homodimer. Ref.2

Miscellaneous

Metal-binding observed in X-ray crystal structures is artifactual.

Sequence similarities

Belongs to the glycosyl hydrolase 84 family.

Biophysicochemical properties

Kinetic parameters:

KM=0.30 mM for p-nitrophenyl-O-GlcNAc (pNP-O-GlcNAc) (at pH 7.4) Ref.2

KM=0.28 mM for p-nitrophenyl-O-GlcNAc (pNP-O-GlcNAc) (at pH 6.5) Ref.2

Vmax=3.2 µmol/min/mg enzyme (at pH 7.4) Ref.2

Vmax=19.9 µmol/min/mg enzyme (at pH 6.5) Ref.2

pH dependence:

Optimum pH is 6.0. Ref.2

Ontologies

Keywords
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionbeta-N-acetylhexosaminidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 737716O-GlcNAcase BT_4395
PRO_0000257984

Regions

Region148 – 433286Catalytic domain Ref.2
Region358 – 3658Substrate binding

Sites

Active site1871 Potential Ref.2
Active site2631 Ref.2
Active site2641Proton donor Probable Ref.2
Binding site1561Substrate; via carbonyl oxygen Ref.2
Binding site3031Substrate Ref.2
Binding site3931Substrate Ref.2

Experimental info

Mutagenesis1581Y → F: 99% decrease in activity for pNP-O-GlcNAc. Ref.2
Mutagenesis2631D → A: 99% decrease in activity for pNP-O-GlcNAc. Ref.2
Mutagenesis2631D → N: 99% decrease in activity for pNP-O-GlcNAc. Ref.2
Mutagenesis2641D → A: 99% decrease in activity for pNP-O-GlcNAc. Ref.2
Mutagenesis2641D → N: 99% decrease in activity for pNP-O-GlcNAc. Ref.2
Mutagenesis3031Y → F: 113% increase in activity for pNP-O-GlcNAc. Ref.2
Mutagenesis3931N → A: 95% decrease in activity for pNP-O-GlcNAc. Ref.2

Secondary structure

1 ..................................................................................................... 737
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q89ZI2 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 2DD4FC69C8C94378

FASTA73784,485
        10         20         30         40         50         60 
MKNNKIYLLG ACLLCAVTTF AQNVSLQPPP QQLIVQNKTI DLPAVYQLNG GEEANPHAVK 

        70         80         90        100        110        120 
VLKELLSGKQ SSKKGMLISI GEKGDKSVRK YSRQIPDHKE GYYLSVNEKE IVLAGNDERG 

       130        140        150        160        170        180 
TYYALQTFAQ LLKDGKLPEV EIKDYPSVRY RGVVEGFYGT PWSHQARLSQ LKFYGKNKMN 

       190        200        210        220        230        240 
TYIYGPKDDP YHSAPNWRLP YPDKEAAQLQ ELVAVANENE VDFVWAIHPG QDIKWNKEDR 

       250        260        270        280        290        300 
DLLLAKFEKM YQLGVRSFAV FFDDISGEGT NPQKQAELLN YIDEKFAQVK PDINQLVMCP 

       310        320        330        340        350        360 
TEYNKSWSNP NGNYLTTLGD KLNPSIQIMW TGDRVISDIT RDGISWINER IKRPAYIWWN 

       370        380        390        400        410        420 
FPVSDYVRDH LLLGPVYGND TTIAKEMSGF VTNPMEHAES SKIAIYSVAS YAWNPAKYDT 

       430        440        450        460        470        480 
WQTWKDAIRT ILPSAAEELE CFAMHNSDLG PNGHGYRREE SMDIQPAAER FLKAFKEGKN 

       490        500        510        520        530        540 
YDKADFETLQ YTFERMKESA DILLMNTENK PLIVEITPWV HQFKLTAEMG EEVLKMVEGR 

       550        560        570        580        590        600 
NESYFLRKYN HVKALQQQMF YIDQTSNQNP YQPGVKTATR VIKPLIDRTF ATVVKFFNQK 

       610        620        630        640        650        660 
FNAHLDATTD YMPHKMISNV EQIKNLPLQV KANRVLISPA NEVVKWAAGN SVEIELDAIY 

       670        680        690        700        710        720 
PGENIQINFG KDAPCTWGRL EISTDGKEWK TVDLKQKESR LSAGLQKAPV KFVRFTNVSD 

       730 
EEQQVYLRQF VLTIEKK

« Hide

References

« Hide 'large scale' references
[1]"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
Science 299:2074-2076(2003) [PubMed: 12663928] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.
[2]"Structure and mechanism of a bacterial beta-glucosaminidase having O-GlcNAcase activity."
Dennis R.J., Taylor E.J., Macauley M.S., Stubbs K.A., Turkenburg J.P., Hart S.J., Black G.N., Vocadlo D.J., Davies G.J.
Nat. Struct. Mol. Biol. 13:365-371(2006) [PubMed: 16565725] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 22-737 IN COMPLEX WITH SUBSTRATE ANALOG, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-158; ASP-263; ASP-264; TYR-303 AND ASN-393.
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE015928 Genomic DNA. Translation: AAO79500.1.
RefSeqNP_813306.1. NC_004663.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CHNX-ray1.95A/B22-737[»]
2CHOX-ray1.85A/B22-737[»]
2J47X-ray1.98A22-737[»]
2J4GX-ray2.25A/B23-737[»]
2JIWX-ray1.95A/B23-737[»]
2VVNX-ray1.85A/B1-737[»]
2VVSX-ray2.24A1-737[»]
2W4XX-ray2.42A22-737[»]
2W66X-ray2.27A/B22-737[»]
2W67X-ray2.25A/B22-737[»]
2WCAX-ray2.30A22-737[»]
2WZHX-ray2.20A1-737[»]
2WZIX-ray1.90A/B1-737[»]
2X0HX-ray2.21A/B1-737[»]
2XJ7X-ray2.00A/B22-737[»]
2XM1X-ray2.00A/B22-737[»]
2XM2X-ray1.95A/B22-737[»]
ProteinModelPortalQ89ZI2.
SMRQ89ZI2. Positions 25-736.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29067N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1074035.
GenomeReviewsGene locus BT_4395 in contig AE015928_GR.
KEGGbth:BT_4395.
NMPDRfig|226186.1.peg.4393.
PATRIC21063856. VBIBacThe70966_4474.

Phylogenomic databases

HOGENOMHBG346283.
OMAISGEGTN.
ProtClustDBCLSK823930.

Enzyme and pathway databases

BioCycBTHE226186:BT_4395-MONOMER.

Family and domain databases

InterProIPR015882. Acetylhexosaminidase_sua/b.
IPR011496. Beta-N-acetylglucosaminidase.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
KOK01197.
PfamPF02838. Glyco_hydro_20b. 1 hit.
PF07555. NAGidase. 1 hit.
[Graphical view]
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
ProtoNetSearch...

Entry information

Entry nameOGA_BACTN
AccessionPrimary (citable) accession number: Q89ZI2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents