ID   A0A081NXI5_9BACL        Unreviewed;       591 AA.
AC   A0A081NXI5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=ET33_17475 {ECO:0000313|EMBL:KEQ23158.1};
OS   Paenibacillus tyrfis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1501230 {ECO:0000313|EMBL:KEQ23158.1, ECO:0000313|Proteomes:UP000028123};
RN   [1] {ECO:0000313|EMBL:KEQ23158.1, ECO:0000313|Proteomes:UP000028123}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSt1 {ECO:0000313|EMBL:KEQ23158.1,
RC   ECO:0000313|Proteomes:UP000028123};
RA   Aw Y.K., Ong K.S., Gan H.M., Lee S.M.;
RT   "Draft genome sequence of Paenibacillus sp. MSt1.";
RL   Submitted (JUN-2014) 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:KEQ23158.1}.
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DR   EMBL; JNVM01000024; KEQ23158.1; -; Genomic_DNA.
DR   RefSeq; WP_036689166.1; NZ_JNVM01000024.1.
DR   AlphaFoldDB; A0A081NXI5; -.
DR   eggNOG; COG1874; Bacteria.
DR   OrthoDB; 9813184at2; -.
DR   Proteomes; UP000028123; 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:SF199; 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:UP000028123}.
FT   DOMAIN          10..326
FT                   /note="Glycoside hydrolase 35 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01301"
FT   DOMAIN          371..482
FT                   /note="Beta-galactosidase 1-like first all-beta"
FT                   /evidence="ECO:0000259|Pfam:PF21317"
FT   DOMAIN          501..560
FT                   /note="Beta-galactosidase galactose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21467"
FT   ACT_SITE        158
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT   ACT_SITE        234
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ   SEQUENCE   591 AA;  67234 MW;  B6E57EC5650C995F CRC64;
     MATFDVQNGQ FCLDGEPIRL VSGAIHYFRV VPEYWRDRLL KLKACGFNTV ETYIPWNLHE
     PKPGQFRFDG LADVVRFVEI AGEVGLHVIV RPSPYICAEW EFGGLPAWLL ADPGMRVRCM
     HRPYLDRVDA YYDVLLPLFK PLLCTNGGPI IAMQIENEYG SYGNDRAYLV YLKDAMLQRG
     MDVLLFTSDG PEHFMLQGGM IPGVLETVNF GSRAEEAFEM LRKYQPDGPI MCMEYWNGWF
     DHWGEDHHTR DAKDVADVFD DMLRLGASVN FYMFHGGTNF GYMSGANCPQ RDHYEPTITS
     YDYDVPLNES GEPTDKFYAV RETLSRYMEL PPLELPQPIP KAAYGSVPVR EAASLFGQLD
     SLSEAVRHTC PEPMEAVGQN DGFILYETFI SGPREERELV LQDCRDRALV YVNDEFLGVI
     ERWDPSQKVS FAVPEGGATL RILVENMGRI NYGPFMLDRK GITEGIRHGN QFLFGWNIYP
     LPLEDVAPVS FDGKEAEPGY PGFYRAVLPI EGQPADTFLR LDGWNKGTVY VNGFHLGRYW
     KRGPQQTLYI PAPLLREGEN EIVVFELHGT EKRELTFTDR PELGPVSQVT L
//