ID A0A2A7MEQ8_9CLOT Unreviewed; 993 AA.
AC A0A2A7MEQ8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00013303, 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=CQ394_15040 {ECO:0000313|EMBL:PEG30146.1};
OS Clostridium neonatale.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=137838 {ECO:0000313|EMBL:PEG30146.1, ECO:0000313|Proteomes:UP000220840};
RN [1] {ECO:0000313|EMBL:PEG30146.1, ECO:0000313|Proteomes:UP000220840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LCDC99A005 {ECO:0000313|EMBL:PEG30146.1,
RC ECO:0000313|Proteomes:UP000220840};
RA Bernard K., Burdz T., Wiebe D., Balcewich B., Alfa M., Bernier A.-M.;
RT "Effective Description of Clostridium neonatale sp. nov. linked to
RT necrotizing enterocolitis in neonates and a clarification of species
RT assignable to the genus Clostridium (Prazmowski 1880) emend. Lawson and
RT Rainey 2016.";
RL Submitted (OCT-2017) 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:PEG30146.1}.
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DR EMBL; PDCJ01000002; PEG30146.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A7MEQ8; -.
DR STRING; 137838.GCA_001458595_01242; -.
DR Proteomes; UP000220840; 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; IPR023232; Glyco_hydro_2_AS.
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.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000220840}.
FT DOMAIN 717..986
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 993 AA; 116745 MW; A4DAF876F3A28EBC CRC64;
MLPRRSYYIP FENCDEALKC KDRNNQIRFN SLNGNWSFRY FNSLDEVELE YKDELFNNIN
VPSVWQMEGY DYNQYTNVKY PIPFNPPFVP KDNPCGLYIK EFNLENFCDK RDYHLNFEGV
DSCFYIWIND YFVGYSQISH SISEFDITKY LSSGINVIKV LVLKWCDGTY FEDQDKFRMS
GIFRDVYILE RANQRINDYS IKTNVDLVKN IGYIYIDILD TKNKPDIKYY LFNDNNDMIL
SGNIIDDKIM LKIEDVQLWN PEDPKLYTLL METKAEVIKE KIGVRVINIE DKVLKINSIP
VKLKGVNHHD SHPKKGYVMS REDMLLDLKL MKESNINSIR TAHYPKSPIF YELCDEYGFL
VMSEADIETH GVVELYGLGY LENYNMIADD PIYEKVIIDR IESSIIPFKN RPSIFMWSLG
NESGYGYNFE KGLKCARKLD PTRLLHYEGA YYADKNRKND FTELDVISRM YPSIDEIQEY
FDKGIDKPLI LCEYAHAMGN GPGGLKEYDD LIQANEEFAG AYVWEWCDHS IYNGSNKDGK
SIYAYGGDFG EYPNDGNFCV DGLVYPDRRK HIGLLEYQNI NRPIRVIEID TVNNKVKLKN
MLDFRDVNDI VQITYKLFSD GDMICKKEIK LDTLKPKEEK WYDLSIQDLP KTIVTILFEY
TVKLDILLYK KGFVLGYDQI IWPNNIEKLK SFKQLINIDE KEKFKINYID NIENNIQITN
GDFKYIYDKR IGMFTLIEKG NKKFINHPLN FTIWRPPTDN DRKIKNDWIE AGFDKLDVRV
NEVTIEEDIN SLAIISRLSL TPIYRQKVLD ILVEWRIFSN GLINCRIKAY KKLDKPFLPR
FGVEIKLDKS YEDLSYFGLG PYENYQDKHY SSYLGRFDSK VSEMHEDYIR PQENGSRSCC
KELCIKNDNS KIYVLSENKD FSFNASHFSK EELTDKTHNY ELEESNATFL IIDYKQSGIG
SNSCGPVLEE KYQLNESEID FSFYLKFSEN NNN
//