ID A0A1M6IE59_9BACE Unreviewed; 1071 AA.
AC A0A1M6IE59;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN05444350_12269 {ECO:0000313|EMBL:SHJ32735.1};
OS Bacteroides stercorirosoris.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=871324 {ECO:0000313|EMBL:SHJ32735.1, ECO:0000313|Proteomes:UP000184192};
RN [1] {ECO:0000313|EMBL:SHJ32735.1, ECO:0000313|Proteomes:UP000184192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26884 {ECO:0000313|EMBL:SHJ32735.1,
RC ECO:0000313|Proteomes:UP000184192};
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; FQZN01000022; SHJ32735.1; -; Genomic_DNA.
DR RefSeq; WP_025833125.1; NZ_FQZN01000022.1.
DR AlphaFoldDB; A0A1M6IE59; -.
DR eggNOG; COG3250; Bacteria.
DR Proteomes; UP000184192; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1071
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009918375"
FT DOMAIN 766..1056
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1071 AA; 123361 MW; 3E8653F3FE03D4A8 CRC64;
MKRLTFITCL ALLPLALPAQ EGRYEQLTNP KLTHINKMSP RSTFTSYISE EDAIVNDRTN
GTYRLSLNGK WKFNYVENFA DRPTDFMNAR TDVSRWPDIN VPGNWELQGF GTPIYVNQPY
EFCSKGYEPY WDKPNPPYVP KEWNPTGTYC REFTVGNDWE GKEIFMSADG VRGAAFYYIN
GKFVGMSKDS KTPARFNVTA MVKRGKNIIA IQVHRFSDAN YLECQDFWRI SGIERDIYLY
ATPKIYIADF KAETPLDPYY KDGILKLKVK LANESDIKSP YVVSYRLLDN EDQQVTQSST
RVEGDQTEVE FTKKTLRGVK QWTAETPNLY TLVISLKRTN GEVIEATSCK VGFRTVEIKD
KQLLVNGVPI LVKGVNVHEH NEYTGHYVPE ELMLKDFELW KKYNVNTVRT CHYPQQERFY
ELCDQYGIYV IDEANIESHG MGYDLHVGGT LGNNPLFMNA HLDRTMNMYE RDKNHPCVIT
WSLGNEAGNG LNFYVTYNTL KMLDNRPIQY ERAGLEWNTD IYCPMYSSPQ SIEKYAQNKE
MTRPLILCEY AHAMGNSLGN FQDYWDIIEK YPILQGGCIW DWVDQGFAAK TSDGRKYWTY
GGDYGENGTP SDGNFCINGV VYPDRSVKPQ TIEMGKVYQN IKFIKFDPQT STVQIRNDFS
FTDLNKYDFH YIVRDHGKEI YKGKMDNINA APGKTATSPF LQGIPKEKNT VGDVRIEFYA
TVRKAEPFLP VGTVIAREQT YVHPFFKKEV AYQAPAKMEE VFSQVVFSGD GFKAAFDKQS
GLLVSYVYNK QEYIYDGQGP RPFFWRAPTD NDYGAKLPVR LKAWREASYQ TLKAESFNVS
KEGGNSIVKV AYRFPQTDAR WEITYKVYAN GIIKVNNRFV AEGTETPMIP RVGLRMQLSE
TLTNLTYYGR GPEENYRDRR TSQFIGEYTT PIKDLYEPYI RPQENEHRTD IYWCALTNKQ
KGGLLFIADR TFELNASNYP LGSLDSGETI DNGAPRTANT NHRHLTDPQP EKMVDMFIDY
RMMGVGGDNS WGAMAHEPYL IRPGVENAIE YGFSIVPFDK KTDYKNLIYQ Y
//
