BGAL1_ENTCL
ID BGAL1_ENTCL Reviewed; 1028 AA.
AC Q47077;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 90.
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};
OS Enterobacter cloacae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX NCBI_TaxID=550;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GAO;
RX PubMed=7765512; DOI=10.1271/bbb.58.1866;
RA Nagano H., Kawaguchi T., Omori M., Shoji Z., Arai M.;
RT "Molecular cloning and nucleotide sequence of the beta-galactosidase gene
RT from Enterobacter cloacae GAO.";
RL Biosci. Biotechnol. Biochem. 58:1866-1869(1994).
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}.
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DR EMBL; D42077; BAA07673.1; -; Genomic_DNA.
DR AlphaFoldDB; Q47077; -.
DR SMR; Q47077; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR PRIDE; Q47077; -.
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:0016052; P:carbohydrate catabolic process; IEA:UniProt.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 2.70.98.10; -; 1.
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 Pfam; PF02929; Bgal_small_N; 1.
DR Pfam; PF16353; DUF4981; 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 PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SUPFAM; SSF49303; SSF49303; 2.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF74650; SSF74650; 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; Sodium.
FT CHAIN 1..1028
FT /note="Beta-galactosidase"
FT /id="PRO_0000057661"
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 1003
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 1028 AA; 116678 MW; F4D61F55F9FEEAEC CRC64;
MSDTPSLTLS ALLARRDWEN PVVTQWNRLA AHAPLHSWRN EPSARDDAGS ARRQTLNGLW
RFSYFTAPEQ VPQAWVTEDC ADAVAMPVPS NWQMQGFDTP IYTNVTYPIP VNPPFVPQEN
PTGCYSLTFE VDDAWLQSGQ TRIIFDGVNS AFHLWCNGQW IGYSQDSRLP AEFDLSAALR
PGQNRLAVMV LRWCDGSYLE DQDMWRMSGI FRDVTLLHKP ETQIADYHVV TDLNAELDRA
VLKVDVTLAG AGFADGEVVF TLWRKGEKCA SVSRQPGSAI VDERGSWAER LTVTIPVETP
ALWSAETPEL YRLTMALLNP QGEVLEIEAC DVGFRRVEIS NGLLKLNGKP LLIRGVNRHE
HHSENGQVMD EATMRRDIET MKQHSFNAVR CSHYPNHPLW YQLCDRYGLY VVDEANIETH
GMVPMSRLAD DPRWLPAMSE RVTRMVQRDR NHPSIIIWSL GNESGHGANH DALYRWLKTT
DPTRPVQYEG GGANTAATDI VCPMYARVDR DQPFPAVPKW SIKKWIGMPD ETRPLILCEY
AHAMGNSFGG FAKYWQAFRS HPRLQGGFVW DWVDQALTKR DEDGNTFWAY GGDFGDKPND
RQFCLNGLVF PDRTPHPALY EAHGPQQFFT FTRVSTSPLV IEVQSGYLFR HTDNEVLNWT
VARDGDVLVA GEVTLAMVPE GTQRLEIALP ELNAGPGEVW LNVEVRQPRA TPWSPAAIAA
AGSSGRFRLR SLLLRQPRRR AAVLTQTDRI LEIAHRQQRW QFDRASGNLT QWWRNGVETL
LSPLTDNVSR APLDNDIGVS EATKIDPNAW VERWKAAGMY DLTPRVLHCE AEQHAGEVVV
TTQHVLEYRG KALFLSRKVW RIDEQGVLHG DIQVDMASDI PEPARIGLSV HLAETPENVR
WLGLGPHENY PDRKLAAQQG RWTLPLEAMH TPYIFPTENG LRCDTRELVV GMHQLNGHFH
FSVSRYSQQQ LRETTHHHLL REEPGCWLNL DAFHMGVGGD DSWSPSVSPE FILQTRQLRY
TFSWQQNP
