ID   BGAL_BIFBI              Reviewed;         689 AA.
AC   D4QFE7;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Beta-galactosidase BbgII;
DE            Short=Beta-gal {ECO:0000250|UniProtKB:P19668};
DE            EC=3.2.1.23;
GN   Name=bbgII {ECO:0000312|EMBL:BAI94826.1};
OS   Bifidobacterium bifidum.
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=1681;
RN   [1] {ECO:0000312|EMBL:BAI94826.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 20082 / JCM 1254 / KCTC 3440 {ECO:0000312|EMBL:BAI94826.1};
RX   PubMed=20581010; DOI=10.1093/glycob/cwq101;
RA   Miwa M., Horimoto T., Kiyohara M., Katayama T., Kitaoka M., Ashida H.,
RA   Yamamoto K.;
RT   "Cooperation of beta-galactosidase and beta-N-acetylhexosaminidase from
RT   bifidobacteria in assimilation of human milk oligosaccharides with type 2
RT   structure.";
RL   Glycobiology 20:1402-1409(2010).
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:0000250|UniProtKB:P19668};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family. {ECO:0000255}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB542712; BAI94826.1; -; Genomic_DNA.
DR   RefSeq; WP_047270929.1; NZ_QDJA01000004.1.
DR   AlphaFoldDB; D4QFE7; -.
DR   SMR; D4QFE7; -.
DR   STRING; 1681.RY70_1493; -.
DR   GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006012; P:galactose metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR013739; Beta_galactosidase_C.
DR   InterPro; IPR013738; Beta_galactosidase_Trimer.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR003476; Glyco_hydro_42.
DR   InterPro; IPR013529; Glyco_hydro_42_N.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR36447; PTHR36447; 1.
DR   Pfam; PF02449; Glyco_hydro_42; 1.
DR   Pfam; PF08533; Glyco_hydro_42C; 1.
DR   Pfam; PF08532; Glyco_hydro_42M; 1.
DR   PIRSF; PIRSF001084; B-galactosidase; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase.
FT   CHAIN           1..689
FT                   /note="Beta-galactosidase BbgII"
FT                   /id="PRO_0000407684"
FT   ACT_SITE        161
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   ACT_SITE        320
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   BINDING         160
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   BINDING         328
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   BINDING         368..371
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
SQ   SEQUENCE   689 AA;  77217 MW;  886064A1622193CC CRC64;
     MSKRRKHSWP QPLKGAESRL WYGGDYNPDQ WPEEVWDDDI RLMKKAGVNL VSVGIFSWAK
     IEPEEGKYDF DWLDRAIDKL GKAGIAVDLA SATASPPMWL TQAHPEVLWK DERGDTVWPG
     AREHWRPTSP VFREYALNLC RRMAEHYKGN PYVVAWHVSN EYGCHNRFDY SDDAMRAFQK
     WCKKRYKTID AVNEAWGTAF WAQHMNDFSE IIPPRYIGDG NFMNPGKLLD YKRFSSDALK
     ELYIAERDVL ESITPGLPLT TNFMVSAGGS MLDYDDWGAE VDFVSNDHYF TPGEAHFDEV
     AYAASLMDGI SRKEPWFQME HSTSAVNWRP INYRAEPGSV VRDSLAQVAM GADAICYFQW
     RQSKAGAEKW HSSMVPHAGE DSQIFRDVCE LGADLGRLSD EGLMGTKTVK SKVAVVFDYE
     SQWATEYTAN PTQQVDHWTE PLDWFRALAD NGITADVVPV RSDWDSYEIA VLPCVYLLSE
     ETSRRVREFV ANGGKLFVTY YTGLSDENDH IWLGGYPGSI RDVVGVRVEE FAPMGNDMPG
     ALDHLDLDNG TVAHDFADVI TSTADTSTVL ASYKAERWTG MNEVPAIVAN GYGDGRTVYV
     GCRLGRQGLA KSLPAMLGSM GLSDLAGDGR VLRVERADAA AANHFEFVFN RTHEPVTVDV
     EGEAIAASLA HVDDGRATID PTGVVVLRR