ID BGAL_ERWT9 Reviewed; 1026 AA.
AC B2VHN8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Beta-galactosidase {ECO:0000255|HAMAP-Rule:MF_01687};
DE Short=Beta-gal {ECO:0000255|HAMAP-Rule:MF_01687};
DE EC=3.2.1.23 {ECO:0000255|HAMAP-Rule:MF_01687};
DE AltName: Full=Lactase {ECO:0000255|HAMAP-Rule:MF_01687};
GN Name=lacZ {ECO:0000255|HAMAP-Rule:MF_01687}; OrderedLocusNames=ETA_25680;
OS Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS 4357 / Et1/99).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=465817;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99;
RX PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA Geider K.;
RT "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT bacterium in the genus Erwinia.";
RL Environ. Microbiol. 10:2211-2222(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC in beta-D-galactosides.; EC=3.2.1.23; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01687};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01687};
CC Note=Binds 2 magnesium ions per monomer. {ECO:0000255|HAMAP-
CC Rule:MF_01687};
CC -!- COFACTOR:
CC Name=Na(+); Xref=ChEBI:CHEBI:29101;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01687};
CC Note=Binds 1 sodium ion per monomer. {ECO:0000255|HAMAP-Rule:MF_01687};
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01687}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_01687}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU468135; CAO97614.1; -; Genomic_DNA.
DR RefSeq; WP_012442279.1; NC_010694.1.
DR AlphaFoldDB; B2VHN8; -.
DR SMR; B2VHN8; -.
DR STRING; 465817.ETA_25680; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR KEGG; eta:ETA_25680; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_002346_1_1_6; -.
DR OrthoDB; 9758603at2; -.
DR Proteomes; UP000001726; Chromosome.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR HAMAP; MF_01687; Beta_gal; 1.
DR InterPro; IPR004199; B-gal_small/dom_5.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR023232; Glyco_hydro_2_AS.
DR InterPro; IPR023933; Glyco_hydro_2_beta_Galsidase.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR023230; Glyco_hydro_2_CS.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR032312; LacZ_4.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR Pfam; PF02929; Bgal_small_N; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR Pfam; PF16353; LacZ_4; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Glycosidase; Hydrolase; Magnesium; Metal-binding; Reference proteome;
KW Sodium.
FT CHAIN 1..1026
FT /note="Beta-galactosidase"
FT /id="PRO_0000366987"
FT ACT_SITE 463
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT ACT_SITE 539
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 203
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 418
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 420
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 463
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 539..542
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 599
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 603
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 606
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 606
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 1002
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT SITE 359
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT SITE 393
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
SQ SEQUENCE 1026 AA; 116920 MW; 63A6F9463A3FB870 CRC64;
MAKTDPLTLQ QLLAQRHWEN PALTQLNRLP AHTPLASWRN ADAARGDLAS PSQRLLDGEW
GFSYFDRPQA VPDAWINGDL PQVGRLSVPS NWQLSGYDAP IYTNVQYPIP TDPPRVPDDN
PTGCYSLTFH CQPAWLQSGQ TRIIFDGVNS AFYLWCNGEF IGYSQDSRLP AEFDLSQRLL
EGENRIAVMV LRWCDGSYLE DQDMWRMSGI FRSVSLLHKP HVRLDDIHID TRLSPEYRSA
QLRVLALCSL TDASAYQLKV TLWRDDTLIA QHQQPFGTPV VDERGRYLDR TRLSLQIDQP
LLWNAETPHL YRAVIALLDA DGTLIEAEAC DVGFRQVEVS GGLLKLNGKA LLIRGTNRHE
HHPDRGQVMD EPAMIADILL MKQHNFNAVR CSHYPNHPLW YRLCDRYGLY VVDEANIETH
GMQPMNRLAD DPSWFSAFSE RVTRMVQRDR NHACIIIWSL GNESGHGSTH DALYGWIKSD
DPSRPVQYEG GGADTAASDI ICPMYARVDR DQPFEAVPKW SIKKWIALPE ETRPLILCEY
AHAMGNSLGG FSRYWQAFRQ YPPLQGGFVW DWADQNLTRQ AADGSSWQAY GGDFGDMPND
RQFCMNGLVF ADRSPHPALF EAKRAQQFFQ FQLENTSPIT LGITSEYLFR HSDNERLCWR
IEHHGEQVAG GQITLNLPPE GTVSLMLGEL PSLAGELWLR VEVIQPAATA WSPANHRVAW
DGWQLPAALS LPKPDVPGEQ PRLHPQSQLI EVVQAGQRWQ FCRQSGELIQ WLQADKPQLL
SPLRDLFVRA PLDNDIGISE ANRIDPHAWA ERWQRAGYYR LESQLLRLQT DILNDGVQIR
SEQAWLADGE PRFLSRKCYR INRQGEMLLE VEVDIAAGLP EPARIGLHCQ LAEVAEEVCW
LGLGPHENYP DRRLAAEFSR WQLPLGALST PYVFPCENGL RGGTRELTFG HWHIRGDFHF
SLSRHSVEQL RKTSHRHLLR DEAGCWLTLD GFHMGVGGDD SWSPSVDEEF LLRARQYRYR
LILTRG
//
