ID A0A087DGU0_9BIFI Unreviewed; 1099 AA.
AC A0A087DGU0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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|ARBA:ARBA00032230, ECO:0000256|RuleBase:RU361154};
GN ORFNames=BSCA_0794 {ECO:0000313|EMBL:KFI94740.1};
OS Bifidobacterium scardovii.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=158787 {ECO:0000313|EMBL:KFI94740.1, ECO:0000313|Proteomes:UP000029033};
RN [1] {ECO:0000313|EMBL:KFI94740.1, ECO:0000313|Proteomes:UP000029033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21589 {ECO:0000313|EMBL:KFI94740.1,
RC ECO:0000313|Proteomes:UP000029033};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFI94740.1}.
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DR EMBL; JGZO01000006; KFI94740.1; -; Genomic_DNA.
DR RefSeq; WP_033517870.1; NZ_JGZO01000006.1.
DR AlphaFoldDB; A0A087DGU0; -.
DR STRING; 158787.BSCA_0794; -.
DR GeneID; 85166409; -.
DR eggNOG; COG3250; Bacteria.
DR Proteomes; UP000029033; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000029033}.
FT DOMAIN 824..1097
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
FT REGION 79..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..820
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1099 AA; 120421 MW; B6C2C6F9C3181D31 CRC64;
MSSSKLVATA ACMDWLTDPT VFAVNREPAH SDHRFYDHAP LPGETMGLRQ SLDGRWRVAV
TEAPRHAFPS FPTATAAAAG NAAPATAQTN ATSPTSPTTA NATPDFALPD YDDTAFSGVE
VPSMLEMAGL LTPKYVNQQY PWDGHADPKA PDIPDHGHVA VYRRDFAPSA TIQAALRAGR
RVTVTFHGAA TAIYVWLNGA FIGYAEDSFT PSEFDVTAAL REDGNILTVA CYEFASASWL
EDQDFWRLHG LFRSVEITAQ PAAHIEDLHV TADYDHVSGG GTLDVRAIVR DADRAGRAKV
SLADTDGSVL WCDDYDVASI VDTLDGSRFT DSTIGTAAIR FGTALASVLP WSAEDPRLYT
LTITLTSDSG EIIEVVPQRF GFRRFAIVDG IMTLNGKRIV FRGADRHEFD ARRGRAITEA
DMIADLTICK RNNINAIRAS HYPNQSRWYE LCDEYGIYLI DETNLETHGT WSSPGDVVMS
DTAVPGSDER WLGACVDRVA NMIGRDRNHP SVLIWSLGNE SYAGDVFRAM YRFAHTADPT
RPVHYEGMTW NRDYEDVTDI ETRMYAKPDE IERYLTDDPR KPYLSCEYMH AMGNSVGGLH
EYVALERYPH YQGGFIWDFI DQAIWQRIGD GTERLAYGGD FGDRPCDYEF SGNGLVFADR
TPTPKLQEVK RLYANVTITP NGHGVAIANG NLFRSTEGDL FTARMLVNGE PRWQADCRFA
VAAGETREFP IMFPDAAALA AGARGLGADG TIVEVTYEVS QRLAESTPWA PAGYEITFGQ
FTERVDGVAA APDPAARADS GESDAGPSSP SGSGSVTMGR WNIGVRTPDS EILLSRAHGG
IISFVRDGRE MVIRRPSITC FRPLIDNDRG NASGFDRAQW FGAGRYASVT GTRIERTDAG
VTAEYTYALA EPNRTAVTVR YAVDASSGRI RLTVNYPGGA QAPTLPAFGL EWMLPEQYAN
LRFYGLGPEE TYRDRLHGAR LGVFERTASE DCAAYLVPQE TGNHEGVRWA EVTDGDGHGM
RVSQAGDEPF AASLLPYSSL MLEEATHADE LPAVRHTFLR LLAAQMGVGG DDSWGAPVHE
AYQLPADRPY TLDVTLELI
//
