ID   A0A1I1TGQ2_9BACT        Unreviewed;       958 AA.
AC   A0A1I1TGQ2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN   ORFNames=SAMN05518672_102409 {ECO:0000313|EMBL:SFD55593.1};
OS   Chitinophaga sp. CF118.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=1884367 {ECO:0000313|EMBL:SFD55593.1, ECO:0000313|Proteomes:UP000199596};
RN   [1] {ECO:0000313|EMBL:SFD55593.1, ECO:0000313|Proteomes:UP000199596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF118 {ECO:0000313|EMBL:SFD55593.1,
RC   ECO:0000313|Proteomes:UP000199596};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; FOMK01000002; SFD55593.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1TGQ2; -.
DR   STRING; 1884367.SAMN05518672_102409; -.
DR   OrthoDB; 9814867at2; -.
DR   Proteomes; UP000199596; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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; 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; 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   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, ECO:0000313|EMBL:SFD55593.1}.
FT   DOMAIN          21..199
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          218..327
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          333..483
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
SQ   SEQUENCE   958 AA;  108603 MW;  0C34167A84253F82 CRC64;
     MKKILLLILL SVKCYAGDTL SLKGIWRFKE DPADVGITEK WYVQKLTGSI RLPGSMTENG
     KGEDVTLNMH WTGSIYDSSW YFNPEMAKYR QPGNLKFPFW LTPLKYYVGA AWYQQDVTIP
     ASWQKRHISL TLERPHWETT VWIDDKPAGL QNSLSTAHVY DLSALLTPGK HTISVRIDNR
     IKKINVGQDS HSITDHTQGN WNGMTGRLQL TAGAPVWLED VQVYPDVAHQ LARVSIRVRK
     PSQQMLSGKI ILKAHSFNSA ITQEVVPLQT TFKISGLDDS SRIEISYPMG PHIQLWDEFD
     PALYQLTVTV VPDEGMKDEI QVQFGMREFK ADGKRFTING RPVFLRGTVE NCVFPLTGYP
     PMDEKEWLRI FRIAKSFGLN HMRFHSWCPP EAAFSAADKA GFYLQPEGPS WANHGTSLGD
     GLPVDQYIYD ETNRMTTSYG NHASFCMLAY GNEPRGGKQA AYLGKFVNYW KAKDSRRLYT
     GASVGMSWPW VPESEFIVKS GPRGLRWSQL PGTAFDYYDK IREQKVPYIT HEMGQYCVFP
     DFKEIKEYTG VFRARNFELF KENLTDHHMG DQANDFLMAS GKLQVLCYKA EIEATLRTPG
     LAGFQLLSLN DYPGQGTALV GILNPFWEEK GYVTAPEFRR FCSPTVLLAK LDRMVYQNSE
     ILNVPLVVTH FGNAPLQHAK PVWRIKDNHG VIIAEGELPV KDIPLGDNIE LGNIRFPLSA
     VSKATALQLE VSLDKSDIIN SWPLWVYPST LPAADTTGIY VCDTLDALAQ QKLQAGGKVL
     LLAAGKVQQG KEVIQSFTPV FWNTSWFKMR PPHTLGFLCD PSHPVFNAFP TEYHSNYQWW
     ELVNNAQVMD LTAFSSSFKP LLQNIDTWFL NRRLAMLIEA RVGKGRLMIT SLDLSRDPEH
     RFVAKQLRYS LLHYMQSDAF KPSGVVSLAT IQALFTAQPV KQINMYTKDS PDELKPKK
//