ID A0A1M5DIU0_9BACE Unreviewed; 1027 AA.
AC A0A1M5DIU0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=SAMN05444349_12921 {ECO:0000313|EMBL:SHF66850.1};
OS Bacteroides faecichinchillae.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=871325 {ECO:0000313|EMBL:SHF66850.1, ECO:0000313|Proteomes:UP000184436};
RN [1] {ECO:0000313|EMBL:SHF66850.1, ECO:0000313|Proteomes:UP000184436}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26883 {ECO:0000313|EMBL:SHF66850.1,
RC ECO:0000313|Proteomes:UP000184436};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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DR EMBL; FQVD01000029; SHF66850.1; -; Genomic_DNA.
DR RefSeq; WP_073350174.1; NZ_SSTN01000036.1.
DR AlphaFoldDB; A0A1M5DIU0; -.
DR STRING; 871325.SAMN05444349_12921; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000184436; 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 Calcium {ECO:0000256|ARBA:ARBA00022837};
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:UP000184436}.
FT DOMAIN 750..1019
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1027 AA; 117495 MW; 09FFA04E22C18BC3 CRC64;
MNLKKRFFLI LLAGITIIPA TAQKLLLPEW QSQYAVGLNK VAPHTYVWPY VNASDIGKPG
EYEQSPYYMS LNGKWKFHWV KNPDNRPKKF YQPSYYTGGW ADINVPGNWE RQGYGTAIYV
NETYEFDDKM FHFKKNPPLV PFEENEVGSY RRTFNIPANW KGRRVVLCCE GVTSFYYIWV
NGKLLGYNQG SKTAAEWDIT DVLNEGENVI AMEVYRWSSG SYLECQDMWR LSGIERDVYL
YTTPKQYIAD YKVNASLDKD KYKDGVFGLE VTVEGPSTAS GSISYTLKDI SGKTVLQDDI
NIKAHSLSNF IVFDEKKIPE VRAWSAEYPN LYTLVLELKD AQGKVTELTG GEVGFRTSEI
KDGRFCINGV PVLVKGTNRH EHSQMGRTVS KELMEQDIKL MKQHNINLVR NSHYPTHPYW
YQLCNRYGLY MIDEANIESH GMGYGPASLA KDSTWLTAHM DRTQRMYERS KNHPAIVIWS
LGNEAGNGIN FERTYDWLKS VDQSRPVQYE RAELNYNTDI YCRMYRSVDE IKDYVTRKDI
TRPFILCEYL HAMGNSCGGL KEYWDVFENE PMAQGGNVWD WVDQSFREID KNGKWYWTYG
GDYGPEGVPS FGNFCCNGLV NADREPHPHL LEVKKIYQNI KAILLTPKNM KLRIKNWYDF
SNLNEYVLHW DVTTDQGEKL TEGTKVVDCE PHATIDIALG NVKLPDTVRE AYLNMSWTRK
EASPMINKTW EVAYDQFILP GNKSLVTYCP QKTGETAFVV DEKTGSLSSL TLDGKELLAT
PVTLSLFRPA TDNDNRDKNG AKLWRNAGLD NLTQKLVSLK EHTESTTAQV EILNVKGQKV
GQAEFVYILD KNGAVKVRTT FQPDTTIVKS MARLGLTFQM NDAFNDISYL GRGDNETYID
RNQSGRISIN RTTPERMFHY YVTPQSTGNR TDVRWAKLTD QSGEGLFFES NVPFQLSIIP
FSDILLEKAR HINELERDGM VTVHLDAKQA GVGTATCGPS VLPQYLVPLK KQSFEFTLCP
VKQALNK
//
