ID A0A0Q9LC94_9BACL Unreviewed; 1010 AA.
AC A0A0Q9LC94;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=ASG81_09720 {ECO:0000313|EMBL:KRE47138.1};
OS Paenibacillus sp. Soil522.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736388 {ECO:0000313|EMBL:KRE47138.1, ECO:0000313|Proteomes:UP000051180};
RN [1] {ECO:0000313|Proteomes:UP000051180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil522 {ECO:0000313|Proteomes:UP000051180};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE47138.1, ECO:0000313|Proteomes:UP000051180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil522 {ECO:0000313|EMBL:KRE47138.1,
RC ECO:0000313|Proteomes:UP000051180};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRE47138.1}.
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DR EMBL; LMRV01000033; KRE47138.1; -; Genomic_DNA.
DR RefSeq; WP_056632575.1; NZ_LMRV01000033.1.
DR AlphaFoldDB; A0A0Q9LC94; -.
DR STRING; 1736388.ASG81_09720; -.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000051180; 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 736..1008
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1010 AA; 114262 MW; FE891D6758AD70F7 CRC64;
MNRIKPNISW LADVSIFAVN RLPAHSDHRY YESLEEAEAS APMALRHDLN GSWKFSYSVK
PADRPERFHQ ADYDCDSWRD IEVPGHIQLQ GYGKPQYVNT MYPWDGHNDI RPPAIPEDHN
PVGSYVKYFK VPDNMQGKPV YVSFQGVESA FFLWLNGEFV GYSEDSFTPA EFDLTPYLRE
GENKLAVEVY QRSTGSWLED QDFWRFSGIF RDVYLYTVPS VHVRDLFVHA ELDKAYSNGS
LRADLKLAGQ LPSSVKLELK DAEGQTIAAA ASEPSGSDTL SLSVDAGKVK PWSAEKPYLY
TLYITVYDQA GKLVEAVPQM VGFRKFEMIN KIMHLNGKRI VFKGVNRHEF NSRRGRAITK
EDMLWDISTL KRNNLNAVRT SHYPNQSYWY ELCDIYGIYV IDEMNLETHG SWQKMGAVEP
SWNIPANKPE WQPIVMDRAI SMVERDKNHP SILIWSVGNE AYAGEVLLNV SNYFRETDPS
RLVHYEGVFH NRKYNDTSDM ESRMYAKPAD IEEYLNDNPQ KPYISCEYMH AMGNSVGGMH
KYTELEQKYA MYQGGFIWDY IDQVIVKKDR YGKEFLAYGG DFGDRATDYN FCTNGIVYAD
RKESPKMQEV KFLYQNIKLI PDRQGLKVIN ENLFEGTDVY DLVIVLHYEG KEIFRSSTDI
DVAAQSEAYM PLALPAADEP GEYALHVSLH LKEGNLWAAS GYEISFGQYV YQIEGRAASA
KPDGTLRVVE GDVNIGVHGR DFSVMFSKQA GTLISLNYAG REMIAIPPAP LFWRATTDND
KGFSLGFDSG AWFAASLTRK CVGVELEEQA GSATVTFRYK LSISPDLLVT VAYTVLADGS
LNVKSRYGGA EGLPKLPIFA LSFKVPADYC HLDWYAMGPE ENYIDRAFGA RLGVFKNNAA
DNVSAYVVPQ ESGNRTGVRR VSITDDHDRG IRITAPAAQP VECNISPYTA FELESAYHHY
ELPSVHYTVV TVAGRQMGVG GDDSWGAPVH DEYLIQAGQE LSFEFIIHRL
//
