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
//