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Database: UniProt
Entry: A0A069D2D0_9BACE
LinkDB: A0A069D2D0_9BACE
Original site: A0A069D2D0_9BACE 
ID   A0A069D2D0_9BACE        Unreviewed;       465 AA.
AC   A0A069D2D0;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN   ORFNames=JCM15093_1648 {ECO:0000313|EMBL:GAK36480.1};
OS   Bacteroides graminisolvens DSM 19988 = JCM 15093.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1121097 {ECO:0000313|EMBL:GAK36480.1, ECO:0000313|Proteomes:UP000027601};
RN   [1] {ECO:0000313|EMBL:GAK36480.1, ECO:0000313|Proteomes:UP000027601}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 15093 {ECO:0000313|EMBL:GAK36480.1,
RC   ECO:0000313|Proteomes:UP000027601};
RX   PubMed=25736980;
RA   Inoue J., Oshima K., Suda W., Sakamoto M., Iino T., Noda S., Hongoh Y.,
RA   Hattori M., Ohkuma M.;
RT   "Distribution and evolution of nitrogen fixation genes in the phylum
RT   bacteroidetes.";
RL   Microbes Environ. 30:44-50(2015).
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|ARBA:ARBA00001412};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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:GAK36480.1}.
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DR   EMBL; BAJS01000007; GAK36480.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A069D2D0; -.
DR   eggNOG; COG3250; Bacteria.
DR   Proteomes; UP000027601; 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; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR006103; Glyco_hydro_2_cat.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR006104; Glyco_hydro_2_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR46323:SF2; LACTASE; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02836; Glyco_hydro_2_C; 1.
DR   Pfam; PF02837; Glyco_hydro_2_N; 1.
DR   PRINTS; PR00132; GLHYDRLASE2.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027601}.
FT   DOMAIN          67..233
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          236..347
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          349..439
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
SQ   SEQUENCE   465 AA;  52791 MW;  34B753F245755F3A CRC64;
     MNYLSKQFVG GLAALMLGTN LSAQTPDWEN PSVFAVNKEA PRATSLPYNN EQLAVNDVYE
     QSPYYLSLNG TWKFRWVKIP AERPVDFYME NYNTSDWDDI KVPGNWELQG YGIPIYTNVT
     YPHPKNPPFI PHNDNPVGSY KRSFDLPASW NGRRIYLHFE AGTSAMYIWV NGQKVGYSQV
     TKSPAEFDIT AYVKPGKNQV AVEVYRWSDG SYLEDQDFWR LSGIDRSVYL YSTDQVRIKD
     YFALADLDRS YKNGMLNVTV DLKNYKQQME SGVVHLSLLD QKGKSVVQLS KPVQVGAGEV
     TKVSFSRNVS SPALWSNETP VLYTVLLTLK DKSGRIIETT SCKTGFRKVE IKDAQLMLNG
     KPLLVRGVNL HEHNQYTGHY VDKETMLEDI RMMKRFNVNA VRMSHYPQSP LWYKLCDQYG
     LLICDEANIE THGMGAELQV GSTRAYIRLI FPNGTCSQGS CGTIG
//
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