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Protein

O-GlcNAcase BT_4395

Gene

BT_4395

Organism
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Can hydrolyze the glycosidic link of O-GlcNAcylated proteins. Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrates (in vitro).1 Publication

Catalytic activityi

[Protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine + H2O = [protein]-L-serine + N-acetyl-D-glucosamine.1 Publication
[Protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonine + H2O = [protein]-L-threonine + N-acetyl-D-glucosamine.1 Publication
Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.1 Publication

Enzyme regulationi

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.1 Publication

Kineticsi

  1. KM=0.30 mM for p-nitrophenyl-O-GlcNAc (pNP-O-GlcNAc) (at pH 7.4)1 Publication
  2. KM=0.28 mM for p-nitrophenyl-O-GlcNAc (pNP-O-GlcNAc) (at pH 6.5)1 Publication
  1. Vmax=3.2 µmol/min/mg enzyme (at pH 7.4)1 Publication
  2. Vmax=19.9 µmol/min/mg enzyme (at pH 6.5)1 Publication

pH dependencei

Optimum pH is 6.0.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei156 – 1561Substrate; via carbonyl oxygen1 Publication
Binding sitei187 – 1871Substrate1 Publication
Binding sitei263 – 2631Substrate1 Publication
Active sitei264 – 2641Proton donor1 Publication
Binding sitei303 – 3031Substrate1 Publication
Binding sitei365 – 3651Substrate1 Publication
Binding sitei393 – 3931Substrate1 Publication

GO - Molecular functioni

  • beta-N-acetylglucosaminidase activity Source: UniProtKB

GO - Biological processi

  • carbohydrate metabolic process Source: UniProtKB
  • protein deglycosylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciBTHE226186:GJXV-4475-MONOMER.
BRENDAi3.2.1.169. 709.

Names & Taxonomyi

Protein namesi
Recommended name:
O-GlcNAcase BT_4395 (EC:3.2.1.1691 Publication)
Alternative name(s):
Beta-N-acetylglucosaminidase (EC:3.2.1.521 Publication)
Beta-N-acetylhexosaminidase
Beta-hexosaminidase
Hexosaminidase B
N-acetyl-beta-glucosaminidase
Gene namesi
Ordered Locus Names:BT_4395
OrganismiBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Taxonomic identifieri226186 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides
Proteomesi
  • UP000001414 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi158 – 1581Y → F: 99% decrease in activity for pNP-O-GlcNAc. 1 Publication
Mutagenesisi263 – 2631D → A: 99% decrease in activity for pNP-O-GlcNAc. 1 Publication
Mutagenesisi263 – 2631D → N: 99% decrease in activity for pNP-O-GlcNAc. 1 Publication
Mutagenesisi264 – 2641D → A: 99% decrease in activity for pNP-O-GlcNAc. 1 Publication
Mutagenesisi264 – 2641D → N: 99% decrease in activity for pNP-O-GlcNAc. 1 Publication
Mutagenesisi303 – 3031Y → F: 113% increase in activity for pNP-O-GlcNAc. 1 Publication
Mutagenesisi393 – 3931N → A: 95% decrease in activity for pNP-O-GlcNAc. 1 Publication

Chemistry

DrugBankiDB00428. Streptozocin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 737716O-GlcNAcase BT_4395PRO_0000257984Add
BLAST

Proteomic databases

PaxDbiQ89ZI2.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

DIPiDIP-29067N.
STRINGi226186.BT_4395.

Structurei

Secondary structure

1
737
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi31 – 4111Combined sources
Beta strandi44 – 507Combined sources
Turni51 – 533Combined sources
Helixi56 – 6611Combined sources
Beta strandi69 – 713Combined sources
Beta strandi73 – 8210Combined sources
Helixi86 – 916Combined sources
Turni92 – 943Combined sources
Beta strandi102 – 1065Combined sources
Beta strandi108 – 11710Combined sources
Helixi118 – 13114Combined sources
Beta strandi136 – 1449Combined sources
Beta strandi147 – 1559Combined sources
Beta strandi158 – 1603Combined sources
Helixi164 – 17613Combined sources
Beta strandi181 – 1844Combined sources
Turni190 – 1923Combined sources
Beta strandi193 – 1953Combined sources
Helixi196 – 1983Combined sources
Helixi203 – 21816Combined sources
Beta strandi222 – 2276Combined sources
Turni230 – 2323Combined sources
Helixi237 – 25216Combined sources
Beta strandi257 – 2615Combined sources
Helixi268 – 2703Combined sources
Helixi272 – 28514Combined sources
Turni286 – 2894Combined sources
Beta strandi290 – 2923Combined sources
Beta strandi296 – 2994Combined sources
Helixi305 – 3073Combined sources
Beta strandi310 – 3123Combined sources
Helixi314 – 3218Combined sources
Beta strandi326 – 3305Combined sources
Beta strandi333 – 3364Combined sources
Helixi341 – 35111Combined sources
Beta strandi355 – 3595Combined sources
Helixi384 – 3863Combined sources
Beta strandi387 – 3926Combined sources
Helixi399 – 4013Combined sources
Helixi402 – 41312Combined sources
Helixi415 – 4173Combined sources
Helixi420 – 43112Combined sources
Helixi433 – 4353Combined sources
Helixi436 – 4449Combined sources
Turni462 – 4643Combined sources
Helixi465 – 47713Combined sources
Helixi483 – 50523Combined sources
Helixi510 – 53829Combined sources
Helixi542 – 56524Combined sources
Beta strandi570 – 5723Combined sources
Turni579 – 5813Combined sources
Helixi582 – 60120Combined sources
Beta strandi613 – 6153Combined sources
Beta strandi628 – 6314Combined sources
Beta strandi634 – 6374Combined sources
Beta strandi653 – 66715Combined sources
Beta strandi680 – 6889Combined sources
Beta strandi697 – 6993Combined sources
Beta strandi702 – 7043Combined sources
Beta strandi709 – 7146Combined sources
Beta strandi730 – 7345Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4AISX-ray2.00A/B1-737[»]
4AIUX-ray2.25A1-737[»]
4UR9X-ray2.20A/B22-737[»]
5ABEX-ray2.00A/B22-737[»]
5ABFX-ray2.10A/B22-737[»]
5ABGX-ray2.00A/B22-737[»]
5ABHX-ray1.95A/B22-737[»]
5FKYX-ray1.80A/B22-737[»]
ProteinModelPortaliQ89ZI2.
SMRiQ89ZI2. Positions 25-736.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ89ZI2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni148 – 433286Catalytic domain1 PublicationAdd
BLAST
Regioni358 – 3603Substrate binding1 Publication

Sequence similaritiesi

Belongs to the glycosyl hydrolase 84 family.Sequence analysis

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105CPE. Bacteria.
ENOG410XPBQ. LUCA.
HOGENOMiHOG000291220.
InParanoidiQ89ZI2.
KOiK01197.
OMAiCPTEYNK.
OrthoDBiEOG6BPDD0.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
3.30.379.10. 1 hit.
InterProiIPR011496. Beta-N-acetylglucosaminidase.
IPR029018. Chitobiase/Hex_dom_2-like.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR015882. HEX_bac_N.
[Graphical view]
PfamiPF02838. Glyco_hydro_20b. 1 hit.
PF07555. NAGidase. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF55545. SSF55545. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q89ZI2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNNKIYLLG ACLLCAVTTF AQNVSLQPPP QQLIVQNKTI DLPAVYQLNG
60 70 80 90 100
GEEANPHAVK VLKELLSGKQ SSKKGMLISI GEKGDKSVRK YSRQIPDHKE
110 120 130 140 150
GYYLSVNEKE IVLAGNDERG TYYALQTFAQ LLKDGKLPEV EIKDYPSVRY
160 170 180 190 200
RGVVEGFYGT PWSHQARLSQ LKFYGKNKMN TYIYGPKDDP YHSAPNWRLP
210 220 230 240 250
YPDKEAAQLQ ELVAVANENE VDFVWAIHPG QDIKWNKEDR DLLLAKFEKM
260 270 280 290 300
YQLGVRSFAV FFDDISGEGT NPQKQAELLN YIDEKFAQVK PDINQLVMCP
310 320 330 340 350
TEYNKSWSNP NGNYLTTLGD KLNPSIQIMW TGDRVISDIT RDGISWINER
360 370 380 390 400
IKRPAYIWWN FPVSDYVRDH LLLGPVYGND TTIAKEMSGF VTNPMEHAES
410 420 430 440 450
SKIAIYSVAS YAWNPAKYDT WQTWKDAIRT ILPSAAEELE CFAMHNSDLG
460 470 480 490 500
PNGHGYRREE SMDIQPAAER FLKAFKEGKN YDKADFETLQ YTFERMKESA
510 520 530 540 550
DILLMNTENK PLIVEITPWV HQFKLTAEMG EEVLKMVEGR NESYFLRKYN
560 570 580 590 600
HVKALQQQMF YIDQTSNQNP YQPGVKTATR VIKPLIDRTF ATVVKFFNQK
610 620 630 640 650
FNAHLDATTD YMPHKMISNV EQIKNLPLQV KANRVLISPA NEVVKWAAGN
660 670 680 690 700
SVEIELDAIY PGENIQINFG KDAPCTWGRL EISTDGKEWK TVDLKQKESR
710 720 730
LSAGLQKAPV KFVRFTNVSD EEQQVYLRQF VLTIEKK
Length:737
Mass (Da):84,485
Last modified:June 1, 2003 - v1
Checksum:i2DD4FC69C8C94378
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE015928 Genomic DNA. Translation: AAO79500.1.
RefSeqiNP_813306.1. NC_004663.1.
WP_011109237.1. NC_004663.1.

Genome annotation databases

EnsemblBacteriaiAAO79500; AAO79500; BT_4395.
GeneIDi1074035.
KEGGibth:BT_4395.
PATRICi21063856. VBIBacThe70966_4474.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE015928 Genomic DNA. Translation: AAO79500.1.
RefSeqiNP_813306.1. NC_004663.1.
WP_011109237.1. NC_004663.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4AISX-ray2.00A/B1-737[»]
4AIUX-ray2.25A1-737[»]
4UR9X-ray2.20A/B22-737[»]
5ABEX-ray2.00A/B22-737[»]
5ABFX-ray2.10A/B22-737[»]
5ABGX-ray2.00A/B22-737[»]
5ABHX-ray1.95A/B22-737[»]
5FKYX-ray1.80A/B22-737[»]
ProteinModelPortaliQ89ZI2.
SMRiQ89ZI2. Positions 25-736.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29067N.
STRINGi226186.BT_4395.

Chemistry

DrugBankiDB00428. Streptozocin.

Proteomic databases

PaxDbiQ89ZI2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAO79500; AAO79500; BT_4395.
GeneIDi1074035.
KEGGibth:BT_4395.
PATRICi21063856. VBIBacThe70966_4474.

Phylogenomic databases

eggNOGiENOG4105CPE. Bacteria.
ENOG410XPBQ. LUCA.
HOGENOMiHOG000291220.
InParanoidiQ89ZI2.
KOiK01197.
OMAiCPTEYNK.
OrthoDBiEOG6BPDD0.

Enzyme and pathway databases

BioCyciBTHE226186:GJXV-4475-MONOMER.
BRENDAi3.2.1.169. 709.

Miscellaneous databases

EvolutionaryTraceiQ89ZI2.
PROiQ89ZI2.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
3.30.379.10. 1 hit.
InterProiIPR011496. Beta-N-acetylglucosaminidase.
IPR029018. Chitobiase/Hex_dom_2-like.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR015882. HEX_bac_N.
[Graphical view]
PfamiPF02838. Glyco_hydro_20b. 1 hit.
PF07555. NAGidase. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF55545. SSF55545. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 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, FUNCTION, ACTIVE SITE.
    Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-54821 Publication.

Entry informationi

Entry nameiOGA_BACTN
AccessioniPrimary (citable) accession number: Q89ZI2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: June 1, 2003
Last modified: June 8, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.