ID   A0A428WD26_9ACTN        Unreviewed;       602 AA.
AC   A0A428WD26;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=DMB66_56585 {ECO:0000313|EMBL:RSM40984.1};
OS   Actinoplanes sp. ATCC 53533.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=1288362 {ECO:0000313|EMBL:RSM40984.1, ECO:0000313|Proteomes:UP000287606};
RN   [1] {ECO:0000313|EMBL:RSM40984.1, ECO:0000313|Proteomes:UP000287606}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53533 {ECO:0000313|EMBL:RSM40984.1,
RC   ECO:0000313|Proteomes:UP000287606};
RA   Waglechner N., Wright G.D.;
RT   "Evolution of GPA BGCs.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|RuleBase:RU000675};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RSM40984.1}.
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DR   EMBL; QHHV01000341; RSM40984.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A428WD26; -.
DR   OrthoDB; 9813184at2; -.
DR   Proteomes; UP000287606; Unassembled WGS sequence.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR026283; B-gal_1-like.
DR   InterPro; IPR048912; BetaGal1-like_ABD1.
DR   InterPro; IPR048913; BetaGal_gal-bd.
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:SF165; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR   Pfam; PF21317; BetaGal_ABD_1; 1.
DR   Pfam; PF21467; BetaGal_gal-bd; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PIRSF; PIRSF006336; B-gal; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675};
KW   Reference proteome {ECO:0000313|Proteomes:UP000287606}.
FT   DOMAIN          23..334
FT                   /note="Glycoside hydrolase 35 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01301"
FT   DOMAIN          380..488
FT                   /note="Beta-galactosidase 1-like first all-beta"
FT                   /evidence="ECO:0000259|Pfam:PF21317"
FT   DOMAIN          515..569
FT                   /note="Beta-galactosidase galactose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21467"
FT   ACT_SITE        170
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT   ACT_SITE        246
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ   SEQUENCE   602 AA;  65142 MW;  9F68F91CC1342E43 CRC64;
     MPAPALAPAP APVSALTWHG RRFYRHGAPH RILSGALHYF RVHPELWRDR LRRVADLGLN
     TVDTYVAWNF HQHRADRAPR FDGWRDLEAF VGIAAEEGLD VIVRPGPYIC AEWSNGGLPS
     WLTARDVAIR TSDPAFTGPV ERWFDDLIPR IAALQAGAGG PVVAVQVENE YGSYGDDHAY
     LRWNRAALTA RGIDELLFTA DGPTELMLDG GTLPGTLTAA TLGSAPGAAR DLLARRRPGE
     PFVVAEYWNG WFDHWGERHH VRGVESTVRT LDGIIADGGS VSIYMAHGGT NFGLWAGANS
     RQGRLQPTVT SYDSDAPIAE DGALTAKFHA LRATLGARGP LRVPERMPVL PPTRVPLTHR
     ADLIDGLRAV PVPASSGPRP ATFEQLGLDA GLTLHTAYPR IPEGDHKLVL TDVRDRAVVF
     ADGIPIGVAD PDHPELGVRG TGAIVRLEIV VESLGRINYG PLLGQHKGLL GPVLVDRRIV
     HGWTSAPIAL PDWTPDDLRR ATAATPTATS SGFAVATLHV DTPADTFLAL PGSAHGLVWV
     NGFLLGRYWE IGPQVTLYCP APLLHAGDNT VTVLETDRLG PALELHDRPQ LGPTEEYVEE
     FA
//