ID   A0A0U4CAJ2_9BACT        Unreviewed;       618 AA.
AC   A0A0U4CAJ2;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=AUC43_09025 {ECO:0000313|EMBL:ALW85225.1};
OS   Hymenobacter sedentarius.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=1411621 {ECO:0000313|EMBL:ALW85225.1, ECO:0000313|Proteomes:UP000059542};
RN   [1] {ECO:0000313|EMBL:ALW85225.1, ECO:0000313|Proteomes:UP000059542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG5B {ECO:0000313|EMBL:ALW85225.1,
RC   ECO:0000313|Proteomes:UP000059542};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) 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|RuleBase:RU000675};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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DR   EMBL; CP013909; ALW85225.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0U4CAJ2; -.
DR   STRING; 1411621.AUC43_09025; -.
DR   KEGG; hyg:AUC43_09025; -.
DR   OrthoDB; 703126at2; -.
DR   Proteomes; UP000059542; Chromosome.
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; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR026283; B-gal_1-like.
DR   InterPro; IPR048912; BetaGal1-like_ABD1.
DR   InterPro; IPR048913; BetaGal_gal-bd.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR019801; Glyco_hydro_35_CS.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR23421:SF165; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR   Pfam; PF21317; BetaGal_ABD_1; 1.
DR   Pfam; PF21467; BetaGal_gal-bd; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PIRSF; PIRSF006336; B-gal; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675};
KW   Reference proteome {ECO:0000313|Proteomes:UP000059542};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..618
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006847711"
FT   DOMAIN          40..356
FT                   /note="Glycoside hydrolase 35 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01301"
FT   DOMAIN          400..510
FT                   /note="Beta-galactosidase 1-like first all-beta"
FT                   /evidence="ECO:0000259|Pfam:PF21317"
FT   DOMAIN          536..590
FT                   /note="Beta-galactosidase galactose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21467"
FT   ACT_SITE        188
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT   ACT_SITE        263
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ   SEQUENCE   618 AA;  68764 MW;  0AA1C8125295BBC7 CRC64;
     MDFSLRKRFR HFLLLSILSA CCLVAQAQAP RHTFALGAES FLLDGQPFQM ISGELHYPRI
     PREAWRSRLK MAKAMGLNTI GTYVFWNAHE PQPGQYDFKG NNDVAAFVRM AQEEGLWVVL
     RPSPYVCAEW EFGGYPYWLQ NVPGLKVRSQ EPQYVAAYRR YIQAVGQQLA PLQVNHGGPV
     LMVQVENEYG SYGSDKQYLA LNQQLFQQAG FDGLLYTCDP ANDVAAGHLP GLLPAVNGLD
     QPREVKALVR ANHNGQGPYF IAEWYPAWFD WWGAPHHTVP AEKYTARLDS VLKAGLSINL
     YMFHGGSTRG FMNGANYKGG TTRYEPQVSS YDYDAPLDEA GNATPKFLAF RQVIAKYRPA
     GQPLPPVPAA RPAAALPTLQ LTRVASLLSR LPAPVVSSTP LTFEGLRQAY GFVLYRATVR
     GGRTQLLKIT ELRDYAVVLV NGQRVGTLDR RLNQDSLRLA LPKGPVQLDI LVENMGRINF
     GKYLLENTKG ITQNVRLDGR EVKDWRMYRL PFDTAPVVAQ GTAPTSAATA APVLRSATFT
     LATPADTYLD MRAWGKGCVW VNGHHLGRYW AIGPQQTLYV PAEWLKKGAN DITVLELLKP
     QQATLPSLAH PILSELQP
//