ID Q8G3I4_BIFLO Unreviewed; 200 AA.
AC Q8G3I4;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN OrderedLocusNames=BL1775 {ECO:0000313|EMBL:AAN25558.1};
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=206672 {ECO:0000313|EMBL:AAN25558.1, ECO:0000313|Proteomes:UP000000439};
RN [1] {ECO:0000313|EMBL:AAN25558.1, ECO:0000313|Proteomes:UP000000439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705 {ECO:0000313|Proteomes:UP000000439};
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA Zwahlen M.C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014295; AAN25558.1; -; Genomic_DNA.
DR RefSeq; NP_696922.1; NC_004307.2.
DR AlphaFoldDB; Q8G3I4; -.
DR STRING; 206672.BL1775; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR EnsemblBacteria; AAN25558; AAN25558; BL1775.
DR KEGG; blo:BL1775; -.
DR PATRIC; fig|206672.9.peg.1829; -.
DR HOGENOM; CLU_075527_1_0_11; -.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000000439; 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 Gene3D; 2.70.98.10; -; 1.
DR InterPro; IPR004199; B-gal_small/dom_5.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR014718; GH-type_carb-bd.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR Pfam; PF02929; Bgal_small_N; 1.
DR SMART; SM01038; Bgal_small_N; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000000439}.
FT DOMAIN 2..198
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 200 AA; 22118 MW; 57B72B323718C534 CRC64;
MPVGGIRHTL AEPGETQVAV RYEVDAASGR VHLTARYAGA TDAPTLPAFG LEWTLPKQYE
NLRFYGLAPE ETYHDRLHGG KLGIFERTAA EDNAPYLVPQ ETGNHEDLRW AEVLDAQGHG
MRISQAGSEH FAASLLPYSS LMLEEATHQN ELPPVRHTFL RLLAAQMGVG GDDSWGAPVH
EQYQLPADRA YTLDVNLELF
//
