ID A0A0Q9U317_9BACL Unreviewed; 1036 AA.
AC A0A0Q9U317;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=ASG93_21355 {ECO:0000313|EMBL:KRF42244.1};
OS Paenibacillus sp. Soil787.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736411 {ECO:0000313|EMBL:KRF42244.1, ECO:0000313|Proteomes:UP000051948};
RN [1] {ECO:0000313|EMBL:KRF42244.1, ECO:0000313|Proteomes:UP000051948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil787 {ECO:0000313|EMBL:KRF42244.1,
RC ECO:0000313|Proteomes:UP000051948};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRF42244.1, ECO:0000313|Proteomes:UP000051948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil787 {ECO:0000313|EMBL:KRF42244.1,
RC ECO:0000313|Proteomes:UP000051948};
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:KRF42244.1}.
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; LMSP01000003; KRF42244.1; -; Genomic_DNA.
DR RefSeq; WP_056830149.1; NZ_LMSP01000003.1.
DR AlphaFoldDB; A0A0Q9U317; -.
DR STRING; 1736411.ASG93_21355; -.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000051948; 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..1033
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1036 AA; 118009 MW; 1ED7A0FDA70236E3 CRC64;
MFKKLDYQPP ANGYPEWNNN PDIFMLNRMD ARATFTPYDT FEEAVRNDPS ASRRILSLNG
MWKFHWAGNP EGRPTDFERE GYDVSGWDEI PVPSQWQFHG YDYPQYTNVH YPWSNQEDLK
PPFAPTKYNP VGSYVRTFSV PEDWAGSPVY LHFRGVESAF YVWLNGDLVG YSEDTFTPAE
FDLTPYLQPG ENKLAVEVYR WCDASWLEDQ DFWRLSGIFR EVLLISPPPE HIYDFRVRTE
LDESYDDAEL EVQVKLLRYA GLGGGELQVD GVLLDACGQP VTGSAFRSSV RVEDGSFATT
QLRASVANPH KWSAEHPNLY TLVLSLRGKD GTLLQAVSCK VGFRKFEIQD NVMLLNGKRI
VFKGTNRHEF SCETGRALSL EDMVKDVRLM KAYNINAVRT SHYPNHPAWY DLCDEFGLYV
IDETNLESHG TWRFYNEEDI VPASKPEWKD NVVDRARSMM ERDKNHPSIL MWSLGNEASC
GENFRHMYRF LKENDPTRLV QYEGVFLNRQ FEDVSDVESQ MYTFPVDVER YALKQPKKPF
ILCEYSHAMG NSNGNLFKYT QLFDKYPVLQ GGFIWDWVDQ AIRTRTPDGT EYLAYGGDFG
ESPHDGNGCG NGLLFADRKV SPKLEEVKAC YQNVGFSGWN PVTGGLTVTN KFLFTRLDEF
EWVWQLLLGG RPVGEAMRGS FAVEPLTTSD IVLRLPEFPS EPEDAELLLE VSLRLKKTEL
WAEAGHEVAW AQLPVHMIPA GRKPTPATGA GMPELTESSG QWLVRGSAFE AAFDTATGTI
VSYRFDGAEL LQMGPEPTFW RAMTDNDRGS NLPNRSEVWR EAGQELTLRR LTRRPSAGAW
EITAEFTLET TAISFCTVRY TVFEDGMVAV EETLAPGENL PELPAIGMML VMDAGYDRIE
WYGRGPHENH WDRAVGAKLG VFTGRAMEEF MPYLKPQECG NKTGVRWIKV HNEAGQGMLF
TAENEMEASV LPYTPTELEE SDHAYKLPPA DKTVVRILHK QMGVGGDESW SAKTHPEFTL
YANRIYSYRY TMSGVR
//
