ID A0A139SNB7_9BACT Unreviewed; 1065 AA.
AC A0A139SNB7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=AXK11_04735 {ECO:0000313|EMBL:KXU35990.1};
OS Cephaloticoccus primus.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae;
OC Cephaloticoccus.
OX NCBI_TaxID=1548207 {ECO:0000313|EMBL:KXU35990.1, ECO:0000313|Proteomes:UP000070058};
RN [1] {ECO:0000313|Proteomes:UP000070058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAG34 {ECO:0000313|Proteomes:UP000070058};
RA Sanders J.G., Lin J.Y., Wertz J.T., Russell J.A., Moreau C.S., Powell S.;
RL Submitted (FEB-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:KXU35990.1}.
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DR EMBL; LSZQ01000040; KXU35990.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139SNB7; -.
DR STRING; 1548207.AXK11_04735; -.
DR Proteomes; UP000070058; 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 Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154}.
FT DOMAIN 769..1061
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1065 AA; 118882 MW; 71EB29B81E655B0C CRC64;
MSPETLSFNR LPARATLYPY ADAASAQRGD RTKSPWWQSL DGEWDFRYFE KPELVPEELL
KPANAIAAPA PAADTGWAKL PVPSNWTMHG YDRPQYTNVQ MPFATQPPEV PEANPTGLYR
RTFGVPRSWA GRRTILHVGA AESVLAVWVD GQPVGLAKDS RLPSEFDLTP YVRAGETHTL
TAVVIKWSDA SFIEDQDHWW MAGIHREVYL YSQAASYIED LFVRADLDES LRKGTLKIEG
RLGSAGEWGE PGHRLRVRLY DPAGKPLLRE PHEAAFPTGD SWNNPRKRLA IEIPVKAPRL
WSAESPARYT VVVSLVAPDG SEIEHTSVRT GFRRVEIKSR ELLINGQPVL IVGVNRHEHD
DRRGKAITRE GMLRDVLAMK QHNINAVRTS HYPNDVYWYE LCDEYGLYVW DEANVEAHGF
YHELSVDSRY APAFLDRAVR MIERDKNHPS IIAWSMGNES GYGPHHDAMA AWARRRDPGR
PVNNEGAINR DWSGGQVGTD IVSPMYASIE KITAWARAPK STDPRPLILC EYSHAMGNSN
GSLADYFDAF DAHHGLQGGF IWEWVDHALV KRAPDGREYW AYGGDFGDVP NDKNFVCDGL
VWPDRVPHPG LLEYKHLAQP VRVALKASVR GKSRFVIENR RWFTRLADLR GEWTLLVDGE
AMLAGSLPLF KTAPQAKEEF SIDTSALALP PGAEAHITFR FFTRKATPWC AAGHELAWEQ
HALPATSFAI ARRAEPRRAS AKPAAVRAVL PSRLDVAQTR TGWTISTTGG DAAGEVAFEV
NRDCGHLENL RRGKALLALR GPQLNLWRAA TDNDGLKLFE DAMWGAASDK ALARWLAAGY
DRLELTDTQT RVSTARGGAA ATITIRQRWL APGARRSLTH THRYRVAPSG ELSVENEFAI
DKALPELPRV GVSLVLPAAL EQLQWFGRGP WESYSDRKRS ALLGVWETSV TADYVPYILP
QEYGNKTDLR WLRLHDGKRS RGGGGAQLRV IGAPTFEASA SHFTAADLFA ARHTIDLVPR
PEVYLNIDYA QRGLGTASCG PDTLPQYLLP AGRYALRFSL SDRTD
//
