ID A0A1R1EI94_9BACL Unreviewed; 1009 AA.
AC A0A1R1EI94;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=BK138_25110 {ECO:0000313|EMBL:OMF51546.1};
OS Paenibacillus rhizosphaerae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=297318 {ECO:0000313|EMBL:OMF51546.1, ECO:0000313|Proteomes:UP000187172};
RN [1] {ECO:0000313|EMBL:OMF51546.1, ECO:0000313|Proteomes:UP000187172}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R5-0378 {ECO:0000313|EMBL:OMF51546.1,
RC ECO:0000313|Proteomes:UP000187172};
RA Beno S.M.;
RT "Paenibacillus species isolates.";
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 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:OMF51546.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MRTP01000009; OMF51546.1; -; Genomic_DNA.
DR RefSeq; WP_076173547.1; NZ_MRTP01000009.1.
DR AlphaFoldDB; A0A1R1EI94; -.
DR STRING; 297318.BK138_25110; -.
DR Proteomes; UP000187172; 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:UP000187172}.
FT DOMAIN 730..1002
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1009 AA; 114779 MW; 2046CBBF56B95ACC CRC64;
MIKLDRVWED TSVLHIHREE PRSYYIPYGD AASARSGKRS RSPLFQTLNG AWKFRYHESV
QDVTDPFYED AFDASSWDEL VVPSCWQTEG YDQLHYTNVN YPIPVDPPYV PDANPAGLYV
REFTVREDWT GKQVYTMFEG VNSCFYLWIN GQFAGYSQGS RIPAEFNVSG LIRPGTNRIA
VMVLKWCDGT YLEDQDLWRF SGIFRDVYLL ARDEAHVRDV FIKQDISPDH SSAKLLCELE
TTGSLDALVL LQDAEGTTVA KGAVRADGRS VIALDIENPV LWNAEHPYLY ELFVQDGREV
LRFPVGFRRI DIVDSVFRIN GQAVKLKGVN RHDSHPDLGQ TVPLNHMIRD LKLMKRHNVN
TVRTSHYPND PRFLELCDRM GFYVVDEADL ECHGLAVSGD FHQLTRDPDW EKAFVDRAIR
LVERDKNHPC VIIWSMGNES GYGRNHIAMA EWTRERDESR LVHYEGASRR YHGDADTEAL
DIESEMYPTL EYVESYGQNP DHAKPLFLCE YSHAMGNGPG DLKEYWDLFY AYPNLMGGCV
WEWNDHGIRT QAPDGREYFG YGGDFGDHPN DGNFCIDGLV SPDRVPHAGL LELKQVIAPV
RMEAEDLSRG TLIITNLYDF SDLSHLTFDW SLERCGEIVE QGSLGTIQAG PQESVTVIIP
FQKAFPDGRC FLTLTASLCE STEWADRGEE IAFAQFEMAA EDSAVQPEQG WLTALRARPV
HVTEDGAQLI VTGMDFRHVF DRNLGTFVRI SKQGVDMLAA PLSFSIWRAP TDNDRNVQRQ
WKDAGYHRAG TKVYQVRVSE PQDDAIEMTV DFSLGGYMKH PVLHGQAVWR VDGSGEIALA
TSVKLREGLP FLPRFGLKAV MPAGTEEVEY FGLGPHASYV DKRQSVRVGK YLLRVDDMFE
PYIMPQENGS RYGTEWATVT SERGMGLAFH GNAPFSFNAS HYSPEDLEEA AHLHQLQLVK
RKETIVHLDY KMSGVGSNSC GPELLEKYRL DEREFEFSIR LRPVFKEDE
//
