ID A0A1S9CAT2_9FIRM Unreviewed; 1011 AA.
AC A0A1S9CAT2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=ATN31_04755 {ECO:0000313|EMBL:OON93938.1};
OS Epulopiscium sp. AS2M-Bin001.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Candidatus Epulonipiscium.
OX NCBI_TaxID=1764958 {ECO:0000313|EMBL:OON93938.1, ECO:0000313|Proteomes:UP000190284};
RN [1] {ECO:0000313|EMBL:OON93938.1, ECO:0000313|Proteomes:UP000190284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS2M-Bin001 {ECO:0000313|EMBL:OON93938.1};
RA Seilhamer J.J.;
RL Submitted (AUG-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 -!- 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:OON93938.1}.
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DR EMBL; LNZM01000127; OON93938.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S9CAT2; -.
DR STRING; 1764958.ATN31_04755; -.
DR Proteomes; UP000190284; 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:UP000190284}.
FT DOMAIN 738..1007
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1011 AA; 117246 MW; F659F67734184169 CRC64;
MTFSRDWICD PEIFSVNRLK AHTYFQSYIP KKNGSDVTEM EMSLRGMWYF KYYENLEDLG
VPRASVDISC KSWGQIKVPS HIQLQGFDRP HYVNRMYPWD GVEEISHPNV PKYFNPVGVY
VKYFKLNKDW NLDDRTVISF LGVESGFALW LNGKFIGYSE DTFTTSEFDI TDFIKEGENK
LYMEVYKFTT GSWMEDQDFW RFSGIFRDVY LYRTAKTYIE DFNIKATPKN PLESNIGDLA
INLSVVGEGD FKIFAGIYEK EHLLSTYELK KVAAGQYAVE VVMNNIKLWS SEAPNMYEVL
FALKSDKDKL IQVVPYKFGF REIKIIDKII YINGKRIVFN GVNRHEFSHV NGRAVTYDEM
LWDVIQMKRH NINAVRTSHY PNHPVFYDLC DEYGIYVLDE VNLEAHGTWK YNIKEFQENA
LPGNNVLWTA AVVDRTASMY ERDKNHPSVI IWSLGNESYA GENFREMKKY ITDRDSRPVH
YEGTCHAPGF KDVSDIESHM YTTNVDAYFE KEYDKPFILC EYAHAMGNSC GALHKYIDLT
KKYPSYQGGF IWDYIDQSIL TKDRYGNEYL AYGGDFGDRP NDENFCVNGL IFGDRKLSPK
MENVKHCYQY IEITPNKTEV NIKNNYLFTD LKNFEFRASI AVDGEVIESE RLEVELKPGE
EKVFQLPFIQ PILIGEILIT VEATLKESTK WEKAGYEVAF GQFIYKENID AVNSDEDNED
KIKKSHELRI ENSEINIGVY GQGFSYMFAR KKAEFTSMRI GNQEMLTHTP RPNFWRASTD
NDRGNGMDYN CAIWQVAGKN ARVRQVTFTN EGDHVKIQYT YGLAAVETIC YVSYLIYEDG
SIRVEYEYKG KEGLPKIPEV GMIWGFIPEL RNISWYGYGK EDNYADTINR AKIGVYRTTV
LENVQPYVIP QETGNKSGVR WMTITDDQGV GIKISDKNLL EISALPYTPI QLEEANHHYK
LPAVYDTFVR VNHRQMGVGG DNSWGAPVHE EYTIASNEDI KYSYKIEICL P
//
