Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Binding sitei156Substrate; via carbonyl oxygen1 Publication1
Binding sitei187Substrate1 Publication1
Binding sitei263Substrate1 Publication1
Active sitei264Proton donor1 Publication1
Binding sitei303Substrate1 Publication1
Binding sitei365Substrate1 Publication1
Binding sitei393Substrate1 Publication1

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

BRENDAi3.2.1.169. 709.

Protein family/group databases

CAZyiGH84. Glycoside Hydrolase Family 84.

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)DescriptionActionsGraphical viewLength
Mutagenesisi158Y → F: 99% decrease in activity for pNP-O-GlcNAc. 1 Publication1
Mutagenesisi263D → A: 99% decrease in activity for pNP-O-GlcNAc. 1 Publication1
Mutagenesisi263D → N: 99% decrease in activity for pNP-O-GlcNAc. 1 Publication1
Mutagenesisi264D → A: 99% decrease in activity for pNP-O-GlcNAc. 1 Publication1
Mutagenesisi264D → N: 99% decrease in activity for pNP-O-GlcNAc. 1 Publication1
Mutagenesisi303Y → F: 113% increase in activity for pNP-O-GlcNAc. 1 Publication1
Mutagenesisi393N → A: 95% decrease in activity for pNP-O-GlcNAc. 1 Publication1

Chemistry databases

DrugBankiDB00428. Streptozocin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
ChainiPRO_000025798422 – 737O-GlcNAcase BT_4395Add BLAST716

Proteomic databases

PaxDbiQ89ZI2.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

DIPiDIP-29067N.
STRINGi226186.BT_4395.

Structurei

Secondary structure

1737
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi31 – 41Combined sources11
Beta strandi44 – 50Combined sources7
Turni51 – 53Combined sources3
Helixi56 – 66Combined sources11
Beta strandi69 – 71Combined sources3
Beta strandi73 – 82Combined sources10
Helixi86 – 91Combined sources6
Turni92 – 94Combined sources3
Beta strandi102 – 106Combined sources5
Beta strandi108 – 117Combined sources10
Helixi118 – 131Combined sources14
Beta strandi136 – 144Combined sources9
Beta strandi147 – 155Combined sources9
Beta strandi158 – 160Combined sources3
Helixi164 – 176Combined sources13
Beta strandi181 – 184Combined sources4
Turni190 – 192Combined sources3
Beta strandi193 – 195Combined sources3
Helixi196 – 198Combined sources3
Helixi203 – 218Combined sources16
Beta strandi222 – 227Combined sources6
Turni230 – 232Combined sources3
Helixi237 – 252Combined sources16
Beta strandi257 – 261Combined sources5
Helixi268 – 270Combined sources3
Helixi272 – 285Combined sources14
Turni286 – 289Combined sources4
Beta strandi290 – 292Combined sources3
Beta strandi296 – 299Combined sources4
Helixi305 – 307Combined sources3
Beta strandi310 – 312Combined sources3
Helixi314 – 321Combined sources8
Beta strandi326 – 330Combined sources5
Beta strandi333 – 336Combined sources4
Helixi341 – 351Combined sources11
Beta strandi355 – 359Combined sources5
Helixi384 – 386Combined sources3
Beta strandi387 – 392Combined sources6
Helixi399 – 401Combined sources3
Helixi402 – 413Combined sources12
Helixi415 – 417Combined sources3
Helixi420 – 431Combined sources12
Helixi433 – 435Combined sources3
Helixi436 – 444Combined sources9
Turni462 – 464Combined sources3
Helixi465 – 477Combined sources13
Helixi483 – 505Combined sources23
Helixi510 – 538Combined sources29
Helixi542 – 565Combined sources24
Beta strandi570 – 572Combined sources3
Turni579 – 581Combined sources3
Helixi582 – 601Combined sources20
Beta strandi613 – 615Combined sources3
Helixi623 – 625Combined sources3
Beta strandi628 – 631Combined sources4
Beta strandi634 – 637Combined sources4
Beta strandi644 – 646Combined sources3
Beta strandi653 – 667Combined sources15
Beta strandi680 – 688Combined sources9
Beta strandi690 – 692Combined sources3
Beta strandi697 – 699Combined sources3
Beta strandi702 – 704Combined sources3
Beta strandi709 – 714Combined sources6
Beta strandi719 – 721Combined sources3
Beta strandi723 – 725Combined sources3
Beta strandi730 – 734Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5FL0X-ray1.95A/B22-737[»]
5FL1X-ray1.95A/B22-737[»]
ProteinModelPortaliQ89ZI2.
SMRiQ89ZI2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ89ZI2.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni148 – 433Catalytic domain1 PublicationAdd BLAST286
Regioni358 – 360Substrate binding1 Publication3

Sequence similaritiesi

Belongs to the glycosyl hydrolase 84 family.Sequence analysis

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105CPE. Bacteria.
ENOG410XPBQ. LUCA.
HOGENOMiHOG000291220.
InParanoidiQ89ZI2.
KOiK01197.
OMAiCPTEYNK.
OrthoDBiPOG091H0IJT.

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
PDB 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[»]
5FL0X-ray1.95A/B22-737[»]
5FL1X-ray1.95A/B22-737[»]
ProteinModelPortaliQ89ZI2.
SMRiQ89ZI2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29067N.
STRINGi226186.BT_4395.

Chemistry databases

DrugBankiDB00428. Streptozocin.

Protein family/group databases

CAZyiGH84. Glycoside Hydrolase Family 84.

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.
OrthoDBiPOG091H0IJT.

Enzyme and pathway databases

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...

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: November 30, 2016
This is version 102 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.