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Entry version 121 (11 Dec 2019)
Sequence version 1 (01 Jun 2003)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

Miscellaneous

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei156Substrate; via carbonyl oxygen1 Publication1
Binding sitei187Substrate1 Publication1
Binding sitei263Substrate1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei264Proton donor1 Publication1
Binding sitei303Substrate1 Publication1
Binding sitei365Substrate1 Publication1
Binding sitei393Substrate1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionGlycosidase, Hydrolase

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
BTHE:G13PU-9377-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.2.1.169 709

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GH84 Glycoside Hydrolase Family 84

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
O-GlcNAcase BT_4395 (EC:3.2.1.1691 Publication)
Alternative name(s):
Beta-N-acetylglucosaminidase
Beta-N-acetylhexosaminidase
Beta-hexosaminidase
Hexosaminidase B
N-acetyl-beta-glucosaminidase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Ordered Locus Names:BT_4395
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri226186 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001414 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

Drug and drug target database

More...
DrugBanki
DB08255 (3AR,5R,6S,7R,7AR)-5-(HYDROXYMETHYL)-2-PROPYL-5,6,7,7A-TETRAHYDRO-3AH-PYRANO[3,2-D][1,3]THIAZOLE-6,7-DIOL
DB07432 [[(3R,4R,5S,6R)-3-(butanoylamino)-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-ylidene]amino] N-phenylcarbamate
DB00428 Streptozocin

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 21Sequence analysisAdd BLAST21
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000025798422 – 737O-GlcNAcase BT_4395Add BLAST716

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q89ZI2

PRoteomics IDEntifications database

More...
PRIDEi
Q89ZI2

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-15576571,EBI-15576571

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-29067N

STRING: functional protein association networks

More...
STRINGi
226186.BT_4395

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1737
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q89ZI2

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q89ZI2

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni148 – 433Catalytic domain1 PublicationAdd BLAST286
Regioni358 – 360Substrate binding1 Publication3

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the glycosyl hydrolase 84 family.Sequence analysis

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105CPE Bacteria
ENOG410XPBQ LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000291220

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q89ZI2

KEGG Orthology (KO)

More...
KOi
K01197

Identification of Orthologs from Complete Genome Data

More...
OMAi
CPTEYNK

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.1180, 1 hit
3.30.379.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011496 Beta-N-acetylglucosaminidase
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF
IPR029018 Hex-like_dom2
IPR015882 HEX_bac_N

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02838 Glyco_hydro_20b, 1 hit
PF07555 NAGidase, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51445 SSF51445, 1 hit
SSF55545 SSF55545, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i2DD4FC69C8C94378
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AE015928 Genomic DNA Translation: AAO79500.1

NCBI Reference Sequences

More...
RefSeqi
NP_813306.1, NC_004663.1
WP_011109237.1, NC_004663.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAO79500; AAO79500; BT_4395

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1074035

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bth:BT_4395

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|226186.12.peg.4474

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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[»]
5MI4X-ray1.80A23-737[»]
5MI5X-ray2.15A23-737[»]
5MI6X-ray2.00A23-737[»]
5MI7X-ray2.10A23-737[»]
SMRiQ89ZI2
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-29067N
STRINGi226186.BT_4395

Chemistry databases

DrugBankiDB08255 (3AR,5R,6S,7R,7AR)-5-(HYDROXYMETHYL)-2-PROPYL-5,6,7,7A-TETRAHYDRO-3AH-PYRANO[3,2-D][1,3]THIAZOLE-6,7-DIOL
DB07432 [[(3R,4R,5S,6R)-3-(butanoylamino)-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-ylidene]amino] N-phenylcarbamate
DB00428 Streptozocin

Protein family/group databases

CAZyiGH84 Glycoside Hydrolase Family 84

Proteomic databases

PaxDbiQ89ZI2
PRIDEiQ89ZI2

Genome annotation databases

EnsemblBacteriaiAAO79500; AAO79500; BT_4395
GeneIDi1074035
KEGGibth:BT_4395
PATRICifig|226186.12.peg.4474

Phylogenomic databases

eggNOGiENOG4105CPE Bacteria
ENOG410XPBQ LUCA
HOGENOMiHOG000291220
InParanoidiQ89ZI2
KOiK01197
OMAiCPTEYNK

Enzyme and pathway databases

BioCyciBTHE:G13PU-9377-MONOMER
BRENDAi3.2.1.169 709

Miscellaneous databases

EvolutionaryTraceiQ89ZI2

Protein Ontology

More...
PROi
PR:Q89ZI2

Family and domain databases

Gene3Di2.60.40.1180, 1 hit
3.30.379.10, 1 hit
InterProiView protein in InterPro
IPR011496 Beta-N-acetylglucosaminidase
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF
IPR029018 Hex-like_dom2
IPR015882 HEX_bac_N
PfamiView protein in Pfam
PF02838 Glyco_hydro_20b, 1 hit
PF07555 NAGidase, 1 hit
SUPFAMiSSF51445 SSF51445, 1 hit
SSF55545 SSF55545, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiOGA_BACTN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q89ZI2
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: June 1, 2003
Last modified: December 11, 2019
This is version 121 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

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