ID W2VDT0_9BIFI Unreviewed; 1036 AA.
AC W2VDT0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=HMPREF1494_1202 {ECO:0000313|EMBL:ETO95782.1};
OS Bifidobacterium sp. MSTE12.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1161409 {ECO:0000313|EMBL:ETO95782.1, ECO:0000313|Proteomes:UP000018909};
RN [1] {ECO:0000313|EMBL:ETO95782.1, ECO:0000313|Proteomes:UP000018909}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSTE12 {ECO:0000313|EMBL:ETO95782.1,
RC ECO:0000313|Proteomes:UP000018909};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (DEC-2013) 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:ETO95782.1}.
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DR EMBL; AZYA01000037; ETO95782.1; -; Genomic_DNA.
DR RefSeq; WP_034522366.1; NZ_AZYA01000037.1.
DR AlphaFoldDB; W2VDT0; -.
DR PATRIC; fig|1161409.3.peg.1887; -.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000018909; 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; 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.
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 762..1034
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
FT REGION 417..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1036 AA; 116324 MW; C30E3889CD56E00F CRC64;
MSHIFSSTEA QESWLTDPTV FAVNRLPAHS SHHCYDHKPL AGEPTGLKQR LDGQWQVKVV
DMSEAGFPSD FAQTQCTESG FSSIEVPSNL ETKGLLKPQY VNVQYPWDGH EDPQQPNIPQ
HNHVALYRRE FTPSASVTRA IRENRQITLT FHAASTAIYV WLNGTFIGYA EDSFTPSEFD
VTDAIQEGHN TLAVACFEFS SAAWLEDQDF WRLHGLYRSV ELTAIPAAHV RDWKIDPDFD
ATTGDATLAF VASISNADAA SKAVATLYGT DGTIAWQSEQ LPVNEMITTE AVIANIKPWS
AEEPNLYTLD LTLYGADGTV IEVSRERIGF RHFAIENGVM KLNGKRIMFK GVNRHEFDAR
RGRAVNEEDM LYDITFFKQH NINAVRTSHY PNQERWYELC DEYGIYMIDE TNIETHGSWT
APSDPVTPDT NVPGSKSEWQ EACVDRIESM MRRDYNHPAV VIWSLGNESY AGTVFKAMSD
FAHANDPLRP VHYEGVFWNR QFDDISDMES RMYAKPAEIA EYLEANPKKP YISCEYMHAM
GNSVGGMHLY TELERYEQYQ GGFIWDYIDQ ALFQRLPDGT ERLTYGGDWD DRPNDYEFSG
DGIIFADRTA SPKAQEVKQL YANVNIKPDA HGVTIRNENL FVSTADYVFT ARMLVNGEER
WQADYRFDVA AGASERFDIA FPAASDLMAS RCDEELPNGS IEVTYEVDQR LAEATAWAPA
GFELTFGQHV QVFNDAADTD AAAVTDGHTH DVTVTDGRWN AGVKAGGREA LLSKAQGGLV
SFTRDGHEML SRKPSLLTFR PLTDNDRGNA SGFDRAQWFA AGRYAKTVGT EIVRDGNTIV
GTYTYELAIT QRTKVTARYE LLEDGRIHLT LTYPGGIEAA SLPAFGMEWM LPVEYSNLRF
YGLGPAETYR DRLHGAKLGV FESTAEADNA PYLVPQETGN HEGLRWIEVT DRHGHGMRVS
QAGDEHFAAS LLPYSTLMLE EATHQEELPT PRHMFLRLLA AQMGVGGDDS WGAPVHERFQ
LPADRPLTLD VMLELF
//
