ID A0A1I0Q4M7_9FLAO Unreviewed; 951 AA.
AC A0A1I0Q4M7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU361154};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU361154};
DE AltName: Full=Lactase {ECO:0000256|RuleBase:RU361154};
GN ORFNames=SAMN05421841_1654 {ECO:0000313|EMBL:SEW21858.1};
OS Chryseobacterium wanjuense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=356305 {ECO:0000313|EMBL:SEW21858.1, ECO:0000313|Proteomes:UP000199469};
RN [1] {ECO:0000313|EMBL:SEW21858.1, ECO:0000313|Proteomes:UP000199469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17724 {ECO:0000313|EMBL:SEW21858.1,
RC ECO:0000313|Proteomes:UP000199469};
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 ECO:0000256|RuleBase:RU361154};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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DR EMBL; FOIU01000001; SEW21858.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0Q4M7; -.
DR STRING; 356305.SAMN05421841_1654; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000199469; Unassembled WGS sequence.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 2.70.98.10; -; 1.
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; 2.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
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; 2.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154}.
FT DOMAIN 52..191
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 204..292
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 298..515
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
SQ SEQUENCE 951 AA; 108660 MW; 2C462F08E5ABF7F6 CRC64;
MNYSSKIFFL LCLCSQLLHS QSKEIQFLSG KDAEHTEAWD FWINGGRKSG NWSKIQVPSQ
WEQQGFGSYN YGRDYVTYGK NFKFNDEVGV YKHKFSVSNS WKGKSVNIVF EGSMTDTEVK
INGKPAGATH QGAFYEFKYD ISDKLIFGKE NILEVKVSKM SADKSVNNAE RLADYWVLGG
IFRPVYLEAT PRENISWTAI DAKADGTFRS NIHLKGIESS NNLKVELFDS NNTLVAESQV
NIEKGDTLKQ LQFSVKNPKL WTAETPNLYK AKFTLNKNKR RIYQTEEKFG FRTIEIRKDD
GIYINGTKIK MKGINRHVWW PETGRSVTEN IDLMDVQLIK EMNMNAVRCS HYPPNRSFLK
ICDSLGLYVL DELAGWQKKY STEIGKKLVR EMVTRDANHP SIIFWSNGNE GGHNFDLDAE
FAKYDLSNRP VIHAHHKPGN AFNGIDCNHY EDYYSTQKIL NGENIYMPTE FLHAQDDGGG
GTSLADYWEL HWNSKKGAGG FIWAFADEGL VRTDFNNQID VNAINAPDGV VGPHREKEGS
FYAIREIYSP VKIDLKTISN DFNGSIPVEN RYHFTNLNEC QFEWKLIQFK TPFSSESGFE
SIKTGKAESP NIKPTEKGNV NLNLPQNWKE SDALSLTAID PFGKEMYTWT WKIASNLEIS
KQFQKNLTKE FPVSVAENDS LFILKSDEKE FSIGKKDGLL KSVILDKKGK KMTFRNGPVF
MNGKVELSSI KSFAEGKNQF IEAYYKNGNK IIWKLNPDGI LELNYEYALS GDYPFAGVSF
DYPENYVINA KWLGKGPYHV WKNRTQGQTY NVWQNLKNST RTGFSSWIYP EFKGYFDDIS
WLQLDTAEGK ITIGTKEEKM FVRLFDFYGI YGAEGYPKLP TGNISFLDAI PPLGTVLAFN
INDKTESLGP ESELNHLNGT FKRTLYFYFG LPDLGDEKKQ FTMPEVNILT D
//
