ID   C3R1C8_9BACE            Unreviewed;       949 AA.
AC   C3R1C8;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN   ORFNames=BSCG_04941 {ECO:0000313|EMBL:EEO58012.1};
OS   Bacteroides sp. 2_2_4.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=469590 {ECO:0000313|EMBL:EEO58012.1};
RN   [1] {ECO:0000313|EMBL:EEO58012.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2_2_4 {ECO:0000313|EMBL:EEO58012.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA   Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA   Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA   White J., Yandava C., Allen-Vercoe E., Strauss J., Ambrose C., Lander E.,
RA   Nusbaum C., Ilzarbe M., Galagan J., Birren B.;
RT   "The Genome Sequence of Bacteroides sp. strain 2_2_4.";
RL   Submitted (DEC-2008) 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; EQ973368; EEO58012.1; -; Genomic_DNA.
DR   AlphaFoldDB; C3R1C8; -.
DR   HOGENOM; CLU_009735_0_0_10; -.
DR   Proteomes; UP000003969; 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   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   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:EEO58012.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..949
FT                   /note="beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002931576"
FT   DOMAIN          32..159
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          195..307
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          312..467
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
SQ   SEQUENCE   949 AA;  107959 MW;  E5F32A958B820A0C CRC64;
     MKQLKLYVCC GLLAFSLMCK AQTTTGGDNI DLSGQWRLAL DYNNQGLQNE WYKYYSQWDS
     MSLPGTTDEA KKGRPESKRK YAYRGYAWYE KEVTIPENWK GKRVVFSIER AKGSMVWFDG
     QYIGCDSTYI CEQKFLLSNE AVPGKHKLTV RIYNGNDKKL LPPVSIGHQS NDGTATNWNG
     MLGKIQLCAY EDIWVDQVQL YPDIDTKTVK VKCVFDGVTD RQWEGTVRLC ANLWNAGSQK
     HTIPEKTFHV KGVSNTDTVR EFIYPMGQDV HLWSEWNPAL YKLTMSSELK SGEDVMADHR
     QLNFGMRKFA TNGKQFTING TPTFLRGKHD GQVFPHQGYA PMNVDEWVKI LRLLKDWGIN
     HIRCHTWCPP EACFTACDIV GIYMLPELPH WGSVGRKAKV VQGDVEQKLE VYDNTTTYLI
     GEGRRLLDQF GNHASFVMFE IGNELGGDRQ ELQKIITGFR AHDPRKLYAA GSNNFLTRPQ
     QQEGDDYWSS TLTGGKYGAG VYTDCEGYEV RASFPQSKFG HMNNYLRGTD YDFSAGNSHS
     TIPVIGHETG QYQMYPDTSE IHLYTGVTTL NNFVEYQKRL DKAGLGDLSH KYFKASGALA
     ALCYREEIES ALRTKDYGGF QLLDLQDFPG QGCALVGVLN AYFKPKGVIS QKEWHQFCSE
     VVPLLRYPEF TLTNNDTFEG RVQVANYSAK SLSKPVNWSI KDGQGNLIDK GSFGLKDIPQ
     GNVFDIATLR YSLDGINHAQ KLNITISIEG TEYENTYSIW VYPADAKIKE GKVQVFTSFN
     PKAQEALKKG KKVLILPTPE VLPTSVDGAF QSDFWNYNMF KKYGNVGTMG ILTDDEHPVF
     ADFPTEYHSN WQWFRLLRNG RPIDMASLPR EYRPMVQVID NFVLNRKLGV LFEAQVGKGK
     LMVCSMALQD NMKYPEGKQM YRSILNYMNS KQFNPKQILS VEQIKSIIH
//