ID   A0A1M6NSX2_9FIRM        Unreviewed;      1005 AA.
AC   A0A1M6NSX2;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00013303};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE   AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230};
GN   ORFNames=SAMN02745136_01437 {ECO:0000313|EMBL:SHJ98807.1};
OS   Anaerocolumna jejuensis DSM 15929.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Anaerocolumna.
OX   NCBI_TaxID=1121322 {ECO:0000313|EMBL:SHJ98807.1, ECO:0000313|Proteomes:UP000184386};
RN   [1] {ECO:0000313|EMBL:SHJ98807.1, ECO:0000313|Proteomes:UP000184386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15929 {ECO:0000313|EMBL:SHJ98807.1,
RC   ECO:0000313|Proteomes:UP000184386};
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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DR   EMBL; FRAC01000008; SHJ98807.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M6NSX2; -.
DR   STRING; 1121322.SAMN02745136_01437; -.
DR   OrthoDB; 9762066at2; -.
DR   Proteomes; UP000184386; 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; 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.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184386}.
FT   DOMAIN          734..1003
FT                   /note="Beta galactosidase small chain/"
FT                   /evidence="ECO:0000259|SMART:SM01038"
SQ   SEQUENCE   1005 AA;  114238 MW;  3B477E35CDFA2945 CRC64;
     MLKSELKLPL YHEDTSVLHA GCEENRSYYI PFAPGERENS SRVELLNGEW DFRFYNNPFE
     LEDFTESGYL YKDYDTIPVP GCIQMYGYDR HQYTNINFPF PYDPPHVPLD NPTCVYHRSL
     PVEQMPEGQK YYLNFEGVDS CFYVYINSTL AGYSQVSHST SEFDITAYIK PGQNDITVVV
     LKWCDGSYLE DQDKFRMTGI FRDVYLISRP ADHIRDFFVK TQLKDNYTKA EIKVEFEFDG
     EAVPVVCTLT DASGKVVAED TVKDSQLFIP VEEPVLWNAE NPYLYTLAIA APDEVIYQKV
     GIRSVEVIKD IIHINGVKVK FKGVNRHDSD PVTGYTISRE QALKDLKLMK EANINAIRTS
     HYPNAPWFSG LCSEYGFYVV AESDLEAHGA TCFYGGGWET YGDLVQREMF AEAILDRNQR
     NVIRDKNNAS VIIWSMGNEA GYSKAFEDTG RWIKEYDSTR LLHYEGSTSQ TGGHTNDTSM
     LDIYSTMYAS IPSIEEYLAA NPKPYMLCEF VHAMGNGPGD MEDYFECIYS HERFAGGFVW
     EWCDHAIYRG ITVDGRKVFH YGGDSGEYPH DGNFCVDGMV SPDRIPHPAL AEYKNVIRPV
     RAAIVKKEEF TVELENKLDF TNLKDFLTIE AELLCNGERV AAYALGAVDL PPHGKTIIQL
     PVEKSLLEAQ SINAGITIKL NYIQSIELPF TSKGHKLGFD QLFIKESANP FVKAGGNGPK
     VTSITVEENA SKILVAGVDF KYCFDKLHGS FESLVIKNQN IIERPLEFNI WRAPMDNDRN
     IRSSWEMARY DRAFPRVYET WVSQEKGVTA IHCRLAITAI QIQHILDLNV TWFIGEDGTI
     TAEMEGKRNK ELPFLPRFGL RFFLPGEYDS VQYLGYGPGE SYVDKRRSAW FGRFDQKVSD
     MYVDYIKPQE NSSHYGCEEL KLSALTGKGI YITAQAPFSF QAGKYTQEEL ASKAHNYELE
     KADGTILCLD YKMSGTGSNS CGPALAEKYQ LNEEDISFKV TLQFS
//