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Database: UniProt
Entry: W4PA48_9BACE
LinkDB: W4PA48_9BACE
Original site: W4PA48_9BACE 
ID   W4PA48_9BACE            Unreviewed;       611 AA.
AC   W4PA48;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN   ORFNames=JCM6292_3064 {ECO:0000313|EMBL:GAE16610.1};
OS   Bacteroides pyogenes JCM 6292.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1235809 {ECO:0000313|EMBL:GAE16610.1, ECO:0000313|Proteomes:UP000018861};
RN   [1] {ECO:0000313|EMBL:GAE16610.1, ECO:0000313|Proteomes:UP000018861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 6292 {ECO:0000313|EMBL:GAE16610.1,
RC   ECO:0000313|Proteomes:UP000018861};
RA   Sakamoto M., Oshima K., Suda W., Kitamura K., Iida T., Hattori M.,
RA   Ohkuma M.;
RT   "Draft Genome Sequences of Three Strains of Bacteroides pyogenes Isolated
RT   from a Cat and Swine.";
RL   Genome Announc. 2:e01242-13(2014).
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, ECO:0000256|RuleBase:RU361154}.
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:GAE16610.1}.
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DR   EMBL; BAIQ01000038; GAE16610.1; -; Genomic_DNA.
DR   AlphaFoldDB; W4PA48; -.
DR   Proteomes; UP000018861; 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; IPR023230; Glyco_hydro_2_CS.
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; BETA-GALACTOSIDASE; 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.
DR   PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..611
FT                   /note="beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004845955"
FT   DOMAIN          65..234
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          239..336
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          338..555
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
SQ   SEQUENCE   611 AA;  69364 MW;  DB92D9B3346A2920 CRC64;
     MKKQLFSCCL AVLGLATTQA QTFNEWKDPE VNAVNRAAMH TNYFAYASAE EARTGIKEQS
     DNFMTLNGTW KFNWVRNADE RPTDFFRTGF DDRGWDNIKV PAVWELNGYG DPIYVNVGYA
     WRNQYKNNPP YVPTANNHVG SYRKEIELPA GWRGKEIFAH FGSVTSNMYL WVNGRYVGYS
     EDSKLEAEFN LTGYLKPGKN LIAFQVFRWC DGTYLEDQDF FRYSGVGRDC YLYAREKKHI
     RDIRVTPDLD EQYANGTLHV AIDMNGSGAV SLDLLDTQGQ RVAAAEVRGS GKLSTVLSVP
     NPEKWTAETP NLYKLVATLK SGNNPLEVIP VNVGFRKIEL KGSQILVNGQ PVLFKGANRH
     ELDPDGGYVV STERMVQDIQ VMKQLNINAV RTCHYPCDNR WYDLCDRYGI YVVAEANVES
     HGMGYGDKTL AKNPIYAKAH LERNQRNVQR GYNHPSIIFW SLGNEAGMGA NFEKCYTWAK
     KEDPTRAVQY EMARTSEFTD IYCPMYRDYE TCINYCEGDI DKPLIQCEYA HAMGNSEGGF
     KEYWDIIRKY PKYQADSSGI SSTNRAGGRI KTVWRYTVTE ATSTSTTLRT TTSATTDSSV
     PTACRIPMPM K
//
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