ID D6ZTL3_BIFLJ Unreviewed; 1023 AA.
AC D6ZTL3;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
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 OrderedLocusNames=BLJ_0749 {ECO:0000313|EMBL:ADH00219.1};
OS Bifidobacterium longum subsp. longum (strain JDM301).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=759350 {ECO:0000313|EMBL:ADH00219.1, ECO:0000313|Proteomes:UP000006740};
RN [1] {ECO:0000313|EMBL:ADH00219.1, ECO:0000313|Proteomes:UP000006740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JDM301 {ECO:0000313|EMBL:ADH00219.1,
RC ECO:0000313|Proteomes:UP000006740};
RX PubMed=20525832; DOI=10.1128/JB.00538-10;
RA Wei Y.X., Zhang Z.Y., Liu C., Zhu Y.Z., Zhu Y.Q., Zheng H., Zhao G.P.,
RA Wang S., Guo X.K.;
RT "Complete genome sequence of Bifidobacterium longum JDM301.";
RL J. Bacteriol. 192:4076-4077(2010).
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; CP002010; ADH00219.1; -; Genomic_DNA.
DR RefSeq; WP_013140536.1; NC_014169.1.
DR AlphaFoldDB; D6ZTL3; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR KEGG; bll:BLJ_0749; -.
DR HOGENOM; CLU_002346_0_2_11; -.
DR Proteomes; UP000006740; Chromosome.
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 747..1021
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1023 AA; 114519 MW; 4A0778BA524BDB92 CRC64;
MTDVTHVDRA SQAWLTDPTV FEVNRTPAHS SHKWYARDPQ SGQWSDLKQS LDGEWRVEVV
QAADINLEEE PATAESFDDS SFERIQVPGH LQTAGLMNHK YVNVQYPWDG HENPLEPNIP
ENNHVALYRR KFTVSAPVAN AKQAGGSVSI VFHGMATAIY VWVNGAFVGY GEDGFTPNEF
DITGLLHDGE NVVAVACYEY SSASWLEDQD FWRLHGLFRS VELAARPHVH IENTQIEADW
DPEAGTASLD AALTVLNAAD AATVRATLKD ADGNTVWQTT GDAKAQTALS SGPLQGIAPW
SAESPTLYEL DVDVIDQSGD VIECTSQKVG FRRFRIEDGI LTINGKRIVF KGADRHEFDA
ERGRAITEQD MIDDVVFCKR HNINSIRTSH YPNQERWYEL CDEYGIYLID ETNLEAHGSW
SLPGDVLTED TIVPGSKREW EGACVDRVNS MMRRDYNHPS VLIWSLGNES YVGDVFRAMY
KHVHDIDPNR PVHYEGVTHN RDYDDVTDIE TRMYSHADEI EKYLKDDPKK PYLSCEYMHA
MGNSVGNMDE YTALERYPKY QGGFIWDFID QAIYATQPDG TRSLRYGGDF GDRPSDYEFS
GDGLLFADRK PSPKAQEVKQ LYSNVHIDVT KDSVSVKNDN LFTATGDYVF VLSVLADGKP
VWQSTRRFDV PAGETRTFDV AWPVAAYRAD ARELVLQVSQ RLAKATDWAE SGYELAFGQT
VVPADATATP DTKPADGTIT VGRWNAGVRG AGREVLLSRT QGGMVSYTFA GNEFVLRRPA
ITTFRPLTDN DRGAGHGFER VQWLGAGRYA RCVDNVLEQI DDSTLKGTYT YELATAQRTK
VTVSYTAHTD GRVNLHVEYP GEQGDLPTIP AFGIEWTLPV QYTNLRFFGT GPEETYLDRK
HAKLGVWSTN AFADHAPYLM PQETGNHEDV RWAEITDDHG HGMRVSRADG AAPFAVSLLP
YSSFMLEEAQ HQDELPKPKH MFLRVLAAQM GVGGDDSWMS PVHSQYHIPA DKPISLDVDL
ELI
//
