ID W4D7T3_9BACL Unreviewed; 1037 AA.
AC W4D7T3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=C173_24887 {ECO:0000313|EMBL:ETT63591.1};
OS Paenibacillus sp. FSL R7-277.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1227352 {ECO:0000313|EMBL:ETT63591.1, ECO:0000313|Proteomes:UP000019051};
RN [1] {ECO:0000313|EMBL:ETT63591.1, ECO:0000313|Proteomes:UP000019051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R7-277 {ECO:0000313|EMBL:ETT63591.1,
RC ECO:0000313|Proteomes:UP000019051};
RX PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT "Genomic comparison of sporeforming bacilli isolated from milk.";
RL BMC Genomics 15:26-26(2014).
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:ETT63591.1}.
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DR EMBL; ASPX01000080; ETT63591.1; -; Genomic_DNA.
DR RefSeq; WP_036729785.1; NZ_ASPX01000080.1.
DR AlphaFoldDB; W4D7T3; -.
DR PATRIC; fig|1227352.4.peg.4991; -.
DR eggNOG; COG3250; Bacteria.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000019051; 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}.
FT DOMAIN 763..1035
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1037 AA; 116639 MW; DF784F67F30D9B63 CRC64;
MRNKLSYQQP ANGYPEWNNN PEIFQLNRID AHASMMSFPA AADALQGDKA SSSRYQTLNG
TWKFAFAETP DARIKDFYKA GYDAAGWADI AVPSHWQFQG YDYPQYTNVR YPWEVSEPDL
KPPFAPTVYN PVGSYIRSFS VPQDWDGQPV FLSFQGVESA FYVWVNGELA GYSEDTFTPS
EFDITAYLLP GENKLAVEVY RWCDASWLED QDFWRLSGIF RDVYLYTAPP VRVADFFVRT
ELDKSFTDAE LQVDLTLENY YNRVIGAHTV EVQLYDSKQQ PVWAAPVSSG FAFEQEGTQL
LKLSAAVKNP LKWSAEKPNL YTLLISVKDD QGQLLEALSC KTGFRTFEIR DGLMKINGKR
IVFKGTNRHE FSCDTGRALS KEDMITDIKL MKLHNINAVR TSHYPNQPVW YELCDEYGLY
VIDETNLETH GSWQYGQKEL HEGNVPGSRP EWRANVIDRC NSMMQRDKNH TSVIIWSLGN
ESFGGDNFLA MYDHLKQADP TRPVHYEGTY HYRPSDAASD IESTMYIKPD EVVEYALSNP
KKPYILCEYS HAMGNSCGGL HLYTELFDKY DSIQGGFIWD WVDQAIRTTT PEGVSYLAYG
GDFGEKPHDG NFSGNGLLFA DRSVTPKLYE VKKCYQNITI TALDLKSGSF EARNNFLFTD
LADYQLRWTL ALNGVAAQEG QLPLSAAPGE AVSFTVPLDS ALLESDKEAV LTVSFVQEDA
TAWSEAAHEV AWEQFVLTPY IPSRNPELSG GTLQVKEQDG FVNFEGNGFA LAFETATGAL
VSLKSSGKEV LHAPVRPNFW RAVTDNDLGN KHPERCVIWK EASYERQLAR FSCRVEGGLG
FVTADYLLGT QPQSTLRVHY EIRTDGSVEI VQELNPGSST LPEIPEFGMV FELDSSLDTI
LWYGRGPHEN YWDRKAGAPL GLYTGKVSEQ FTNYLRPQEC GNKTDVRYAS VTAGSEGHGL
SVEGAVPLEV NALPWSPAEL EASDHGYKLP ASDKTVLRVN YKQMGVGGDD SWGAPTHEQF
TLPANRPYTF KFKLSLL
//
