ID   BGAL_ARTSB              Reviewed;        1015 AA.
AC   Q59140;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Beta-galactosidase;
DE            Short=Beta-gal;
DE            EC=3.2.1.23;
DE   AltName: Full=Lactase;
GN   Name=lacZ;
OS   Arthrobacter sp. (strain B7).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=86041;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-5, AND
RP   CHARACTERIZATION.
RX   PubMed=7811090; DOI=10.1128/aem.60.12.4544-4552.1994;
RA   Trimbur D.E., Gutshall K.R., Prema P., Brenchley J.E.;
RT   "Characterization of a psychrotrophic Arthrobacter gene and its cold-active
RT   beta-galactosidase.";
RL   Appl. Environ. Microbiol. 60:4544-4552(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;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.2.;
CC       Temperature dependence:
CC         Optimum temperature is 30 degrees Celsius with o-nitrophenyl-beta-D-
CC         galactopyranoside (ONPG) as substrate. Has high specific activity at
CC         low temperatures.;
CC   -!- INDUCTION: By growth on lactose.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000305}.
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DR   EMBL; U12334; AAA69907.1; -; Genomic_DNA.
DR   PIR; I39697; I39697.
DR   AlphaFoldDB; Q59140; -.
DR   SMR; Q59140; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   PRIDE; Q59140; -.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR   Gene3D; 2.60.40.10; -; 2.
DR   Gene3D; 2.70.98.10; -; 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; IPR006103; Glyco_hydro_2_cat.
DR   InterPro; IPR023230; Glyco_hydro_2_CS.
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; 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   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase; Magnesium; Manganese.
FT   CHAIN           1..1015
FT                   /note="Beta-galactosidase"
FT                   /id="PRO_0000057657"
FT   ACT_SITE        434
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        513
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1015 AA;  110903 MW;  7846E36D62F76302 CRC64;
     MSSSYITDQG PGSGLRVPAR SWLNSDAPSL SLNGDWRFRL LPTAPGTPGA GSVLATGETV
     EAVASESFDD SSWDTLAVPS HWVLAEDGKY GRPIYTNVQY PFPIDPPFVP DANPTGDYRR
     TFDVPDSWFE STTAALTLRF DGVESRYKVW VNGVEIGVGS GSRLAQEFDV SEALRPGKNL
     LVVRVHQWSA ASYLEDQDQW WLPGIFRDVK LQARPVGGLT DVWLRTDWSG SGTITPEITA
     DPAAFPVTLR VPELGLEVIW DSPADVAPVS IDAVEPWSAE VPRLYDASVS SAAESISLRL
     GFRTVKIVGD QFLVNGRKVI FHGVNRHETN ADRGRVFDEA SAREDLALMK RFNVNAIRTS
     HYPPHPRFLD LADELGFWVI LECDLETHGF HALKWVGNPS DDPAWRDALV DRMERTVERD
     KNHASIVMWS LGNESGTGAN LAAMAAWTHA RDLSRPVHYE GDYTGAYTDV YSRMYSSIPE
     TDSIGRNDSH ALLLGCNAIE SARQRTRPFI LCEYVHAMGN GPGAIDQYED LVDKYPRLHG
     GFVWEWRDHG IRTRTADGTE FFAYGGDFDE VIHDGNFVMD GMILSDSTPT PGLFEYKQIV
     SPIRLALTLN AEGNAGLTVA NLRHTSDASD VVLRWRVEHN GTRVDAGELT TDGANGPLQA
     GDSLTLTLPT IVAAAEGETW LSVEAVLREA TAWAPAGHPL SETQLDLSPA QPPLRVPRPA
     SPIAGAAPVE LGPATFDAGS LVTLAGLPVA GPRLELWRAP TDNDKGQGFG AYGPEDPWIN
     SGRGVPAPSS AVVWQQAGLD RLTRRVEDVA ALPQGLRVRS RYAAANSEHD VAVEENWQLS
     GDELWLRIDI APSAGWDLVF PRIGVRLDLP SEVDGASWFG AGPRESYPDS LHSAVVGTHG
     GSLEELNVNY ARPQETGHHS DVRWVELSRD GAPWLRIEAD PDALGRRPGF SLAKNTAQEV
     ALAPHPHELP ESQHSYLYLD AAQHGLGSRA CGPDVWPDFA LRPEARTLVL RIRAA