ID   A0A1I6W037_9BACL        Unreviewed;       787 AA.
AC   A0A1I6W037;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:SFT19347.1};
GN   ORFNames=SAMN05428962_5026 {ECO:0000313|EMBL:SFT19347.1};
OS   Paenibacillus sp. BC26.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1881032 {ECO:0000313|EMBL:SFT19347.1, ECO:0000313|Proteomes:UP000199637};
RN   [1] {ECO:0000313|EMBL:SFT19347.1, ECO:0000313|Proteomes:UP000199637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BC26 {ECO:0000313|EMBL:SFT19347.1,
RC   ECO:0000313|Proteomes:UP000199637};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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DR   EMBL; FPAD01000004; SFT19347.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6W037; -.
DR   STRING; 1881032.SAMN05428962_5026; -.
DR   OrthoDB; 9762066at2; -.
DR   Proteomes; UP000199637; 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; 3.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR032311; DUF4982.
DR   InterPro; IPR048230; GalA-like.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR040605; Glyco_hydro2_dom5.
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   NCBIfam; NF041462; GalA; 1.
DR   PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR   Pfam; PF16355; DUF4982; 1.
DR   Pfam; PF18565; Glyco_hydro2_C5; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02836; Glyco_hydro_2_C; 2.
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}.
FT   DOMAIN          42..186
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          198..301
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          307..382
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
FT   DOMAIN          392..520
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
FT   DOMAIN          611..667
FT                   /note="DUF4982"
FT                   /evidence="ECO:0000259|Pfam:PF16355"
FT   DOMAIN          681..778
FT                   /note="Glycoside hydrolase family 2"
FT                   /evidence="ECO:0000259|Pfam:PF18565"
SQ   SEQUENCE   787 AA;  88076 MW;  352BBE5CA9E947F3 CRC64;
     MRRSKVDFDR DWLFYRGNID IPYAVKAGGA GSLTDCEKGE EGLWQQIAFT DKNSGVSVAP
     DEWETVNLPH DWLVEEEFSK DGPLERGYKK SGVGCYRKMF DIPAADEGKK IIIEFDGVMR
     HSSVWVNGHF VGTHPSGSVP FFYDITDIVR YGDEGRNVIF VKVDARDYEG WWYDGAGIYR
     HVWLTTTDRL HVGQWGTYVT TPAVSEATST VRIETTVNNE YRIAKDCELV IEIVDANGEV
     VASARSAATI PDGEIHTFVQ QVEVSDPLLW SLEAPNLYKA IAMVIENGTE TDRYETIFGI
     RTIEFTTDNG FFLNGKRTVI KGLCVHQDFA GVGVALPDSI IAYKLQLLQE MGANAYRSAH
     HPPTKELLEM CDRMGIMVID ENRRLDSSPE GIKNLKHMLY RDRNHPSIIA WSLENEEQLE
     GTVMGARILA TLVQVTKKLD PTRPTTAALN HGFNDGGYSD ELDIVGYNYG HKWGSFINDH
     AKHPERIIYG SEVSAYAVTR GIYEHDESKG YCSEYGTSWR ENEWLNSWTT SPEQSWGAVA
     ENPFLAGMFI WAGFDYRGEP SPFKWPNINS QYGTMDTCGF PKDNYYYYKS AWTDKPMIHL
     FPHWNWPGKE GQEIDVWAYS NLDTIELFLN GVSVGEQKRK PNGHVEWKVP YEPGKLLAVG
     RRDGEIVSEV TVETTGAAHH IRLMPHLSAV HANDTDAVAV RVAICDEQGR VVPTADNLVY
     FTVNGGGRII GVGNGDPISH EADKASKRRA FNGYCLLILQ AGTEVGALEL RAHSTGLLDG
     HAIISVG
//