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Protein

Beta-galactosidase

Gene

lacZ

Organism
Escherichia coli (strain K12)
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

<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

  • Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. EC:3.2.1.23

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the ‘Function’ 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 phenylethyl thio-beta-D-galactoside (PETG), isopropyl thio-beta-D-galactoside (IPTG), L-ribose, D-galactonolactone, lactose and 2-amino-D-galactose.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

The values for the enzymatic assays using manganese as cofactor are very close.
  1. KM=0.04 mM for p-nitrophenyl beta-D-galactoside6 Publications
  2. KM=0.12 mM for o-nitrophenyl beta-D-galactoside6 Publications
  3. KM=0.15 mM for 2,3-dinitrophenyl beta-D-galactopyranoside6 Publications
  4. KM=0.41 mM for 2,5-dinitrophenyl beta-D-galactopyranoside6 Publications
  5. KM=11.6 mM for p-nitrophenol-alpha-L-arabinopyranoside6 Publications
  6. KM=16.9 mM for p-nitrophenol-beta-D-fucopyranoside6 Publications
  7. KM=34 µM for p-nitrophenyl beta-D-galactoside (with magnesium as cofactor and 30 degrees Celsius)6 Publications
  8. KM=140 µM for o-nitrophenyl beta-D-galactoside (with magnesium as cofactor and 30 degrees Celsius)6 Publications
  9. KM=940 µM for allolactose (with magnesium as cofactor and 30 degrees Celsius)6 Publications
  10. KM=1350 µM for lactose (with magnesium as cofactor and 30 degrees Celsius)6 Publications
  1. Vmax=30.9 µmol/min/mg enzyme with lactose as substrate (with magnesium as cofactor and 30 degrees Celsius)6 Publications
  2. Vmax=49.7 µmol/min/mg enzyme with allolactose as substrate (with magnesium as cofactor and 30 degrees Celsius)6 Publications
  3. Vmax=59.7 µmol/min/mg enzyme with p-nitrophenyl beta-D-galactoside as substrate (with magnesium as cofactor and 30 degrees Celsius)6 Publications
  4. Vmax=360 µmol/min/mg enzyme with o-nitrophenyl beta-D-galactoside as substrate (with magnesium as cofactor and 30 degrees Celsius)6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei103Substrate1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi202Sodium1
Binding sitei202Substrate1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei358Transition state stabilizer1
Sitei392Transition state stabilizer1
Metal bindingi417Magnesium 11 Publication1
Metal bindingi419Magnesium 11 Publication1
<p>This subsection of the ‘Function’ 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 sitei462Proton donor1 Publication1
Metal bindingi462Magnesium 11 Publication1
Binding sitei462Substrate1
Active sitei538Nucleophile1 Publication1
Metal bindingi598Magnesium 21 Publication1
Metal bindingi602Sodium; via carbonyl oxygen1
Metal bindingi605Sodium1
Binding sitei605Substrate1
Binding sitei1000Substrate1
Sitei1000Important for ensuring that an appropriate proportion of lactose is converted to allolactose1

<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

  • alkali metal ion binding Source: EcoCyc
  • beta-galactosidase activity Source: EcoCyc
  • carbohydrate binding Source: InterPro
  • identical protein binding Source: IntAct
  • magnesium ion binding Source: EcoCyc

GO - Biological processi

  • lactose catabolic process Source: CACAO

<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
LigandMagnesium, Manganese, Metal-binding, Sodium

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:BETAGALACTOSID-MONOMER
MetaCyc:BETAGALACTOSID-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.2.1.23 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P00722

Protein family/group databases

Carbohydrate-Active enZymes

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CAZyi
GH2 Glycoside Hydrolase Family 2

<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:
Beta-galactosidase (EC:3.2.1.23)
Short name:
Beta-gal
Alternative name(s):
Lactase
<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
Name:lacZ
Ordered Locus Names:b0344, JW0335
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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
  • UP000000318 <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
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG10527 lacZ

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

<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>Mutagenesisi202D → E or N: Causes a significant decrease in binding affinity in the absence of monovalent cations or in the presence of potassium ions, but only a moderate decrease in the presence of sodium ions. 1 Publication1
Mutagenesisi202D → F: Obliterates all binding and catalysis. 1 Publication1
Mutagenesisi358H → D, F, L or N: Less stable to heat than wild-type. Causes significant destabilizations of the first transition state. 1 Publication1
Mutagenesisi392H → E, F or K: Essentially inactive unless very rapid purification. Causes very large destabilizations of the transition state. 1 Publication1
Mutagenesisi462E → H: Slowly inactivates galactosidase activity by reducing the binding of magnesium. It increases binding specificity. 1 Publication1
Mutagenesisi538E → Q: 10000-fold decrease in the beta-galactosidase activity. 1 Publication1
Mutagenesisi541H → E, F or N: Poorly reactive with galactosyl substrates. Less stable to heat than wild-type. 1 Publication1
Mutagenesisi602F → A: Decreases the stability of the loop 794-804. 1 Publication1
Mutagenesisi795G → A: It forces the apoenzyme to adopt the closed rather than the open conformation. Reduces the binding affinity. 1 Publication1
Mutagenesisi798E → A or L: The catalytic efficiency is not increased, when the sodium concentration increases. 1 Publication1
Mutagenesisi798E → D or Q: Small increase of the catalytic efficiency, when the sodium concentration increases. 1 Publication1
Mutagenesisi1000W → F, G, L or T: Decreases affinity for substrate. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4603

Drug and drug target database

More...
DrugBanki
DB01920 1-O-[O-Nitrophenyl]-Beta-D-Galactopyranose
DB02228 2-deoxy-2-fluoro-Beta-D-galactose
DB04382 2-Deoxy-Beta-D-Galactose
DB04155 2-Fluoro-2-Deoxy-Beta-D-Galactopyranosyl-Beta-D-Glucopyranose
DB02632 4-nitrophenyl-beta-D-galactoside
DB04116 Allolactose
DB01885 D-Galctopyranosyl-1-On
DB01862 Isopropyl beta-D-thiogalactopyranoside
DB04465 Lactose

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<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_00000576502 – 1024Beta-galactosidaseAdd BLAST1023

Proteomic databases

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

More...
PaxDbi
P00722

PRoteomics IDEntifications database

More...
PRIDEi
P00722

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By allolactose.1 Publication

<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

Homotetramer.4 Publications

<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
itself3EBI-369998,EBI-369998

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-10081N

Protein interaction database and analysis system

More...
IntActi
P00722, 76 interactors

STRING: functional protein association networks

More...
STRINGi
316407.85674486

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P00722

<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

11024
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DP0X-ray1.70A/B/C/D10-1024[»]
1F4AX-ray2.80A/B/C/D4-1024[»]
1F4HX-ray2.80A/B/C/D4-1024[»]
1HN1X-ray3.00A/B/C/D10-1024[»]
1JYNX-ray1.80A/B/C/D10-1024[»]
1JYVX-ray1.75A/B/C/D10-1024[»]
1JYWX-ray1.55A/B/C/D10-1024[»]
1JYXX-ray1.75A/B/C/D10-1024[»]
1JZ2X-ray2.10A/B/C/D2-1024[»]
1JZ3X-ray1.75A/B/C/D10-1024[»]
1JZ4X-ray2.10A/B/C/D10-1024[»]
1JZ5X-ray1.80A/B/C/D10-1024[»]
1JZ6X-ray2.10A/B/C/D10-1024[»]
1JZ7X-ray1.50A/B/C/D10-1024[»]
1JZ8X-ray1.50A/B/C/D10-1024[»]
1PX3X-ray1.60A/B/C/D10-1024[»]
1PX4X-ray1.60A/B/C/D10-1024[»]
3CZJX-ray2.05A/B/C/D10-1024[»]
3DYMX-ray2.05A/B/C/D10-1024[»]
3DYOX-ray1.80A/B/C/D10-1024[»]
3DYPX-ray1.75A/B/C/D10-1024[»]
3E1FX-ray3.001/2/3/410-1024[»]
3I3BX-ray2.20A/B/C/D10-1024[»]
3I3DX-ray2.20A/B/C/D10-1024[»]
3I3EX-ray2.10A/B/C/D10-1024[»]
3IAPX-ray2.00A/B/C/D10-1024[»]
3IAQX-ray2.70A/B/C/D10-1024[»]
3J7Helectron microscopy3.20A/B/C/D1-1024[»]
3MUYX-ray2.501/2/3/410-1024[»]
3MUZX-ray1.901/2/3/410-1024[»]
3MV0X-ray2.201/2/3/410-1024[»]
3MV1X-ray2.201/2/3/410-1024[»]
3SEPX-ray2.05A/B/C/D10-1024[»]
3T08X-ray2.00A/B/C/D10-1024[»]
3T09X-ray1.75A/B/C/D10-1024[»]
3T0AX-ray1.90A/B/C/D10-1024[»]
3T0BX-ray2.40A/B/C/D10-1024[»]
3T0DX-ray1.93A/B/C/D10-1024[»]
3T2OX-ray1.85A/B/C/D10-1024[»]
3T2PX-ray2.60A/B/C/D10-1024[»]
3T2QX-ray2.40A/B/C/D10-1024[»]
3VD3X-ray2.80A/B/C/D10-1024[»]
3VD4X-ray2.00A/B/C/D10-1024[»]
3VD5X-ray2.70A/B/C/D10-1024[»]
3VD7X-ray2.87A/B/C/D10-1024[»]
3VD9X-ray2.05A/B/C/D10-1024[»]
3VDAX-ray2.50A/B/C/D10-1024[»]
3VDBX-ray2.05A/B/C/D10-1024[»]
3VDCX-ray2.55A/B/C/D10-1024[»]
4CKDelectron microscopy13.00A/B/C/D1-1024[»]
4DUVX-ray2.10A/B/C/D10-1024[»]
4DUWX-ray2.20A/B/C/D10-1024[»]
4DUXX-ray2.30A/B/C/D10-1024[»]
4TTGX-ray1.60A/B/C/D15-1024[»]
4V40X-ray2.50A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P2-1024[»]
4V41X-ray2.50A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P2-1024[»]
4V44X-ray2.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P2-1024[»]
4V45X-ray2.60A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P2-1024[»]
5A1Aelectron microscopy2.20A/B/C/D3-1024[»]
6CVMelectron microscopy1.90A/B/C/D3-1023[»]
6DRVelectron microscopy2.20A/B/C/D1-1024[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P00722

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

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SMRi
P00722

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P00722

<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>Regioni538 – 541Substrate binding4

<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 2 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105CNT Bacteria
COG3250 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000252443

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P00722

KEGG Orthology (KO)

More...
KOi
K01190

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P00722

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.120.260, 1 hit
2.60.40.10, 2 hits
2.70.98.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01687 Beta_gal, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR004199 B-gal_small/dom_5
IPR036156 Beta-gal/glucu_dom_sf
IPR011013 Gal_mutarotase_sf_dom
IPR008979 Galactose-bd-like_sf
IPR014718 GH-type_carb-bd
IPR006101 Glyco_hydro_2
IPR023232 Glyco_hydro_2_AS
IPR023933 Glyco_hydro_2_beta_Galsidase
IPR006103 Glyco_hydro_2_cat
IPR023230 Glyco_hydro_2_CS
IPR006102 Glyco_hydro_2_Ig-like
IPR006104 Glyco_hydro_2_N
IPR017853 Glycoside_hydrolase_SF
IPR013783 Ig-like_fold
IPR032312 LacZ_4

The PANTHER Classification System

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PANTHERi
PTHR10066:SF76 PTHR10066:SF76, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF02929 Bgal_small_N, 1 hit
PF16353 DUF4981, 1 hit
PF00703 Glyco_hydro_2, 1 hit
PF02836 Glyco_hydro_2_C, 1 hit
PF02837 Glyco_hydro_2_N, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00132 GLHYDRLASE2

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM01038 Bgal_small_N, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49303 SSF49303, 2 hits
SSF49785 SSF49785, 1 hit
SSF51445 SSF51445, 1 hit
SSF74650 SSF74650, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00719 GLYCOSYL_HYDROL_F2_1, 1 hit
PS00608 GLYCOSYL_HYDROL_F2_2, 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>.<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.

P00722-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTMITDSLAV VLQRRDWENP GVTQLNRLAA HPPFASWRNS EEARTDRPSQ
60 70 80 90 100
QLRSLNGEWR FAWFPAPEAV PESWLECDLP EADTVVVPSN WQMHGYDAPI
110 120 130 140 150
YTNVTYPITV NPPFVPTENP TGCYSLTFNV DESWLQEGQT RIIFDGVNSA
160 170 180 190 200
FHLWCNGRWV GYGQDSRLPS EFDLSAFLRA GENRLAVMVL RWSDGSYLED
210 220 230 240 250
QDMWRMSGIF RDVSLLHKPT TQISDFHVAT RFNDDFSRAV LEAEVQMCGE
260 270 280 290 300
LRDYLRVTVS LWQGETQVAS GTAPFGGEII DERGGYADRV TLRLNVENPK
310 320 330 340 350
LWSAEIPNLY RAVVELHTAD GTLIEAEACD VGFREVRIEN GLLLLNGKPL
360 370 380 390 400
LIRGVNRHEH HPLHGQVMDE QTMVQDILLM KQNNFNAVRC SHYPNHPLWY
410 420 430 440 450
TLCDRYGLYV VDEANIETHG MVPMNRLTDD PRWLPAMSER VTRMVQRDRN
460 470 480 490 500
HPSVIIWSLG NESGHGANHD ALYRWIKSVD PSRPVQYEGG GADTTATDII
510 520 530 540 550
CPMYARVDED QPFPAVPKWS IKKWLSLPGE TRPLILCEYA HAMGNSLGGF
560 570 580 590 600
AKYWQAFRQY PRLQGGFVWD WVDQSLIKYD ENGNPWSAYG GDFGDTPNDR
610 620 630 640 650
QFCMNGLVFA DRTPHPALTE AKHQQQFFQF RLSGQTIEVT SEYLFRHSDN
660 670 680 690 700
ELLHWMVALD GKPLASGEVP LDVAPQGKQL IELPELPQPE SAGQLWLTVR
710 720 730 740 750
VVQPNATAWS EAGHISAWQQ WRLAENLSVT LPAASHAIPH LTTSEMDFCI
760 770 780 790 800
ELGNKRWQFN RQSGFLSQMW IGDKKQLLTP LRDQFTRAPL DNDIGVSEAT
810 820 830 840 850
RIDPNAWVER WKAAGHYQAE AALLQCTADT LADAVLITTA HAWQHQGKTL
860 870 880 890 900
FISRKTYRID GSGQMAITVD VEVASDTPHP ARIGLNCQLA QVAERVNWLG
910 920 930 940 950
LGPQENYPDR LTAACFDRWD LPLSDMYTPY VFPSENGLRC GTRELNYGPH
960 970 980 990 1000
QWRGDFQFNI SRYSQQQLME TSHRHLLHAE EGTWLNIDGF HMGIGGDDSW
1010 1020
SPSVSAEFQL SAGRYHYQLV WCQK
Length:1,024
Mass (Da):116,483
Last modified:January 23, 2007 - v2
<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:i9D295EF4CEF90B08
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
J01636 Genomic DNA Translation: AAA24053.1
V00296 Genomic DNA Translation: CAA23573.1
U73857 Genomic DNA Translation: AAB18068.1
U00096 Genomic DNA Translation: AAC73447.1
AP009048 Genomic DNA Translation: BAE76126.1
V00295 Genomic DNA Translation: CAA23570.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A90981 GBEC

NCBI Reference Sequences

More...
RefSeqi
NP_414878.1, NC_000913.3
WP_000177906.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73447; AAC73447; b0344
BAE76126; BAE76126; BAE76126

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
945006

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0335
eco:b0344

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01636 Genomic DNA Translation: AAA24053.1
V00296 Genomic DNA Translation: CAA23573.1
U73857 Genomic DNA Translation: AAB18068.1
U00096 Genomic DNA Translation: AAC73447.1
AP009048 Genomic DNA Translation: BAE76126.1
V00295 Genomic DNA Translation: CAA23570.1
PIRiA90981 GBEC
RefSeqiNP_414878.1, NC_000913.3
WP_000177906.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DP0X-ray1.70A/B/C/D10-1024[»]
1F4AX-ray2.80A/B/C/D4-1024[»]
1F4HX-ray2.80A/B/C/D4-1024[»]
1HN1X-ray3.00A/B/C/D10-1024[»]
1JYNX-ray1.80A/B/C/D10-1024[»]
1JYVX-ray1.75A/B/C/D10-1024[»]
1JYWX-ray1.55A/B/C/D10-1024[»]
1JYXX-ray1.75A/B/C/D10-1024[»]
1JZ2X-ray2.10A/B/C/D2-1024[»]
1JZ3X-ray1.75A/B/C/D10-1024[»]
1JZ4X-ray2.10A/B/C/D10-1024[»]
1JZ5X-ray1.80A/B/C/D10-1024[»]
1JZ6X-ray2.10A/B/C/D10-1024[»]
1JZ7X-ray1.50A/B/C/D10-1024[»]
1JZ8X-ray1.50A/B/C/D10-1024[»]
1PX3X-ray1.60A/B/C/D10-1024[»]
1PX4X-ray1.60A/B/C/D10-1024[»]
3CZJX-ray2.05A/B/C/D10-1024[»]
3DYMX-ray2.05A/B/C/D10-1024[»]
3DYOX-ray1.80A/B/C/D10-1024[»]
3DYPX-ray1.75A/B/C/D10-1024[»]
3E1FX-ray3.001/2/3/410-1024[»]
3I3BX-ray2.20A/B/C/D10-1024[»]
3I3DX-ray2.20A/B/C/D10-1024[»]
3I3EX-ray2.10A/B/C/D10-1024[»]
3IAPX-ray2.00A/B/C/D10-1024[»]
3IAQX-ray2.70A/B/C/D10-1024[»]
3J7Helectron microscopy3.20A/B/C/D1-1024[»]
3MUYX-ray2.501/2/3/410-1024[»]
3MUZX-ray1.901/2/3/410-1024[»]
3MV0X-ray2.201/2/3/410-1024[»]
3MV1X-ray2.201/2/3/410-1024[»]
3SEPX-ray2.05A/B/C/D10-1024[»]
3T08X-ray2.00A/B/C/D10-1024[»]
3T09X-ray1.75A/B/C/D10-1024[»]
3T0AX-ray1.90A/B/C/D10-1024[»]
3T0BX-ray2.40A/B/C/D10-1024[»]
3T0DX-ray1.93A/B/C/D10-1024[»]
3T2OX-ray1.85A/B/C/D10-1024[»]
3T2PX-ray2.60A/B/C/D10-1024[»]
3T2QX-ray2.40A/B/C/D10-1024[»]
3VD3X-ray2.80A/B/C/D10-1024[»]
3VD4X-ray2.00A/B/C/D10-1024[»]
3VD5X-ray2.70A/B/C/D10-1024[»]
3VD7X-ray2.87A/B/C/D10-1024[»]
3VD9X-ray2.05A/B/C/D10-1024[»]
3VDAX-ray2.50A/B/C/D10-1024[»]
3VDBX-ray2.05A/B/C/D10-1024[»]
3VDCX-ray2.55A/B/C/D10-1024[»]
4CKDelectron microscopy13.00A/B/C/D1-1024[»]
4DUVX-ray2.10A/B/C/D10-1024[»]
4DUWX-ray2.20A/B/C/D10-1024[»]
4DUXX-ray2.30A/B/C/D10-1024[»]
4TTGX-ray1.60A/B/C/D15-1024[»]
4V40X-ray2.50A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P2-1024[»]
4V41X-ray2.50A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P2-1024[»]
4V44X-ray2.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P2-1024[»]
4V45X-ray2.60A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P2-1024[»]
5A1Aelectron microscopy2.20A/B/C/D3-1024[»]
6CVMelectron microscopy1.90A/B/C/D3-1023[»]
6DRVelectron microscopy2.20A/B/C/D1-1024[»]
ProteinModelPortaliP00722
SMRiP00722
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-10081N
IntActiP00722, 76 interactors
STRINGi316407.85674486

Chemistry databases

BindingDBiP00722
ChEMBLiCHEMBL4603
DrugBankiDB01920 1-O-[O-Nitrophenyl]-Beta-D-Galactopyranose
DB02228 2-deoxy-2-fluoro-Beta-D-galactose
DB04382 2-Deoxy-Beta-D-Galactose
DB04155 2-Fluoro-2-Deoxy-Beta-D-Galactopyranosyl-Beta-D-Glucopyranose
DB02632 4-nitrophenyl-beta-D-galactoside
DB04116 Allolactose
DB01885 D-Galctopyranosyl-1-On
DB01862 Isopropyl beta-D-thiogalactopyranoside
DB04465 Lactose

Protein family/group databases

CAZyiGH2 Glycoside Hydrolase Family 2

Proteomic databases

PaxDbiP00722
PRIDEiP00722

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73447; AAC73447; b0344
BAE76126; BAE76126; BAE76126
GeneIDi945006
KEGGiecj:JW0335
eco:b0344

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB0522
EcoGeneiEG10527 lacZ

Phylogenomic databases

eggNOGiENOG4105CNT Bacteria
COG3250 LUCA
HOGENOMiHOG000252443
InParanoidiP00722
KOiK01190
PhylomeDBiP00722

Enzyme and pathway databases

BioCyciEcoCyc:BETAGALACTOSID-MONOMER
MetaCyc:BETAGALACTOSID-MONOMER
BRENDAi3.2.1.23 2026
SABIO-RKiP00722

Miscellaneous databases

EvolutionaryTraceiP00722

Protein Ontology

More...
PROi
PR:P00722

Family and domain databases

Gene3Di2.60.120.260, 1 hit
2.60.40.10, 2 hits
2.70.98.10, 1 hit
HAMAPiMF_01687 Beta_gal, 1 hit
InterProiView protein in InterPro
IPR004199 B-gal_small/dom_5
IPR036156 Beta-gal/glucu_dom_sf
IPR011013 Gal_mutarotase_sf_dom
IPR008979 Galactose-bd-like_sf
IPR014718 GH-type_carb-bd
IPR006101 Glyco_hydro_2
IPR023232 Glyco_hydro_2_AS
IPR023933 Glyco_hydro_2_beta_Galsidase
IPR006103 Glyco_hydro_2_cat
IPR023230 Glyco_hydro_2_CS
IPR006102 Glyco_hydro_2_Ig-like
IPR006104 Glyco_hydro_2_N
IPR017853 Glycoside_hydrolase_SF
IPR013783 Ig-like_fold
IPR032312 LacZ_4
PANTHERiPTHR10066:SF76 PTHR10066:SF76, 1 hit
PfamiView protein in Pfam
PF02929 Bgal_small_N, 1 hit
PF16353 DUF4981, 1 hit
PF00703 Glyco_hydro_2, 1 hit
PF02836 Glyco_hydro_2_C, 1 hit
PF02837 Glyco_hydro_2_N, 1 hit
PRINTSiPR00132 GLHYDRLASE2
SMARTiView protein in SMART
SM01038 Bgal_small_N, 1 hit
SUPFAMiSSF49303 SSF49303, 2 hits
SSF49785 SSF49785, 1 hit
SSF51445 SSF51445, 1 hit
SSF74650 SSF74650, 1 hit
PROSITEiView protein in PROSITE
PS00719 GLYCOSYL_HYDROL_F2_1, 1 hit
PS00608 GLYCOSYL_HYDROL_F2_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiBGAL_ECOLI
<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: P00722
Secondary accession number(s): Q2MC80
<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: July 21, 1986
Last sequence update: January 23, 2007
Last modified: December 5, 2018
This is version 192 of the entry and version 2 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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