ID   BGAL_XANMN              Reviewed;         598 AA.
AC   P48982;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Beta-galactosidase;
DE            Short=Lactase;
DE            EC=3.2.1.23;
DE   Flags: Precursor;
GN   Name=bga;
OS   Xanthomonas manihotis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=43353;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 22-38, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=7AS1;
RX   PubMed=8563148; DOI=10.1093/glycob/5.6.603;
RA   Taron C.H., Benner J.S., Hornstra L.J., Guthrie E.P.;
RT   "A novel beta-galactosidase gene isolated from the bacterium Xanthomonas
RT   manihotis exhibits strong homology to several eukaryotic beta-
RT   galactosidases.";
RL   Glycobiology 5:603-610(1995).
CC   -!- FUNCTION: Preferentially hydrolyzes beta(1->3) galactosyl linkages over
CC       beta(1->4) linkages.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 4.5. {ECO:0000269|PubMed:8563148};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
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DR   EMBL; L35444; AAC41485.1; -; Genomic_DNA.
DR   PIR; A57249; A57249.
DR   AlphaFoldDB; P48982; -.
DR   SMR; P48982; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR026283; B-gal_1-like.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR019801; Glyco_hydro_35_CS.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR23421; PTHR23421; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PIRSF; PIRSF006336; B-gal; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:8563148"
FT   CHAIN           22..598
FT                   /note="Beta-galactosidase"
FT                   /id="PRO_0000012198"
FT   ACT_SITE        184
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        260
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   598 AA;  66086 MW;  DB4C3F05E01435BF CRC64;
     MLRTTLAPLV LALALALPAA AATPESWPTF GTQGTQFVRD GKPYQLLSGA IHFQRIPRAY
     WKDRLQKARA LGLNTVETYV FWNLVEPQQG QFDFSGNNDV AAFVKEAAAQ GLNVILRPGP
     YACAEWEAGG YPAWLFGKGN IRVRSRDPRF LAASQAYLDA LAKQVQPLLN HNGGPIIAVQ
     VENEYGSYAD DHAYMADNRA MYVKAGFDKA LLFTSDGADM LANGTLPDTL AVVNFAPGEA
     KSAFDKLIKF RPDQPRMVGE YWAGWFDHWG KPHAATDARQ QAEEFEWILR QGHSANLYMF
     IGGTSFGFMN GANFQNNPSD HYAPQTTSYD YDAILDEAGH PTPKFALMRD AIARVTGVQP
     PALPAPITTT TLPATPLRES ASLWDNLPTP IAIDTPQPME QFGQDYGYIL YRTTITGPRK
     GPLYLGDVRD VARVYVDQRP VGSVERRLQQ VSLEVEIPAG QHTLDVLVEN SGRINYGTRM
     ADGRAGLVDP VLLDSQQLTG WQAFPLPMRT PDSIRGWTGK AVQGPAFHRG TLRIGTPTDT
     YLDMRAFGKG FAWANGVNLG RHWNIGPQTA LYLRPSSARV TTRWWSSTWT MLHPSVRG