ID A0A1I6U7X0_9BACI Unreviewed; 1047 AA.
AC A0A1I6U7X0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00013303, ECO:0000256|RuleBase:RU361154};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU361154};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230, ECO:0000256|RuleBase:RU361154};
GN ORFNames=SAMN04488145_10640 {ECO:0000313|EMBL:SFS97327.1};
OS Bacillus sp. 103mf.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1761751 {ECO:0000313|EMBL:SFS97327.1, ECO:0000313|Proteomes:UP000198993};
RN [1] {ECO:0000313|EMBL:SFS97327.1, ECO:0000313|Proteomes:UP000198993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=103MF {ECO:0000313|EMBL:SFS97327.1,
RC ECO:0000313|Proteomes:UP000198993};
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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DR EMBL; FPAF01000006; SFS97327.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6U7X0; -.
DR STRING; 1761751.SAMN04488145_10640; -.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000198993; Unassembled WGS sequence.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
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; IPR004199; B-gal_small/dom_5.
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; IPR023232; Glyco_hydro_2_AS.
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 InterPro; IPR032312; LacZ_4.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR Pfam; PF02929; Bgal_small_N; 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 Pfam; PF16353; LacZ_4; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
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.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154}.
FT DOMAIN 767..1039
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1047 AA; 120843 MW; 67AEEC199472C7E4 CRC64;
MLKILKKFNY APPKNGYPEW NNNPDIFQLN RLEPHATLMP YATVEEALKG NRKTSNYYYC
LNGDWKFSFS ENPEKRIRNF FENDYDDSTW KEIKVPAHWQ LQGYDYPHYT NLTYPWEGRE
DIKPPFAPTE YNPVGQYRTT FTVPKAWDGQ PVYISFQGVE SAFYVWVNGE LVGYSEDTFT
PADFDLTPYL IDGENKLAVE VYRWCDASWL EDQDFWRMSG IFRDVYLYSS PEVHINDFFV
VTELDENYEN ADVKIQAKVT NYFERNVGAV SFEAMLYDQD NHKVFDEPVT ADIVIDGKAE
VVLNVSKFVE NPLKWSAEHP NLYTLVLSLK DEKGHIIETE SCKVGFRKFE LKDGLMQING
KRIVFKGVNR HEFVAEKGRA DINYEDMLHD IKLMKKFNIN AVRTSHYPNH PVWYELCDEY
GLYVIDETNL ETHGTWEYGQ EEEGDTVPGS KPEWTENVLD RCNSMFQRDK NHPSIIIWSL
GNESFGGDNF IKMHQFFKEN DPTRLVHYEG VFHYRASEAA SDIESTMYVN VDGVEKYAQN
NPTKPYILCE YSHAMGNSCG NLFKYWDLFD KYPILQGAFI WDWKDQALKT KTADGIEYLA
YGGDFGETLH DGNFSGNGLI FADGTITPKI FEVKKCYQNV KIKAVDVKKG TVEIINQHLF
TNLKDYQLQW EIMKNGEVIE TGYEIVDIQP LSADVVQLPY QLPEERVTPD EYILTVSLRL
KGETLWAEKG HEIAFEQFII PVEKVEIKTI ENDYPEVKVV ESDTKLQVEG QDFAIVFSKE
SGSIESYSYK GHELLKSGFE PNFWRASTDN DIARGRGLAS RSATWREVGQ KRELQALTIE
RKANLVTIEA EFQLSTAAPS QCKIRYIILG NGIVEVKQDL CPGEKLPEIP EIGMMVIMDQ
AFENITWYGK GPHENYWDRE TGAKIAIHNG KVKDQYTPYL KPQECGNKVD VRWATITNNE
GIGLMVSGLP TVEVNALPYT PFELEEHDHP YKLPKSNKVA LRVNYKQMGV GGDDSWGQPT
HPEFTLYANR TYTYSFTFKG IEKNNIN
//
