ID A0A1Y5KBE5_9BACL Unreviewed; 1022 AA.
AC A0A1Y5KBE5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=B1748_16250 {ECO:0000313|EMBL:OUS75652.1};
OS Paenibacillus sp. MY03.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=302980 {ECO:0000313|EMBL:OUS75652.1, ECO:0000313|Proteomes:UP000195591};
RN [1] {ECO:0000313|EMBL:OUS75652.1, ECO:0000313|Proteomes:UP000195591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MY03 {ECO:0000313|EMBL:OUS75652.1,
RC ECO:0000313|Proteomes:UP000195591};
RA Liu H., Cheng Y., Gu J.Y., Han W.J.;
RT "Draft genome of a polysaccharide-degrading bacterium Paenibacillus sp.
RT MY03.";
RL Submitted (MAR-2017) 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:OUS75652.1}.
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DR EMBL; MXQD01000014; OUS75652.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5KBE5; -.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000195591; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000195591}.
FT DOMAIN 745..1015
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1022 AA; 116804 MW; F00B46ACFE4FC2F8 CRC64;
MLEINKYWED PRTLHINREK PRAYYIPHVD ADGAASRKRG RSPYYQTLNG AWKFRYYASV
EDVRDSFYEA DYDAGSWSSL LVPSCWQNNG YDGMHYSNLN YTIPCDPPFV PDDNPAGLYI
REFNLSPDWT EKEKYVVFEG VNACFYLWVN GRFVGYSQGS RVPAEFNISK HLVSGVNRMA
VMVLKFCDGT YLEDQDLWRY TGIFRDVYML ARDKAHIRDV FVRTTLLNGD REAQLNIELE
MAGGAVVQAV LRDPSGLEIA AAKGEIGQAG QLLMQVLDPQ LWSAEQPVLY ELLLSSGEEV
LRFSVGFRRV EIHEGVFQIN GVPVKLKGVN RHDSHPSLGQ TIPLQHMIQD LQVMKRHNIN
TIRASHYPND PRFLELCNEY GFYVVDEADL ECHGLAIADN WDNMAKGLGM QSYTDFHELS
NNPDWEEAFV DRAVRMVERD KNNPCVVFWS MGNESGYGPN HIAMAKWTRE RDSARPVHYE
GGASLYLGHP DTSVLDMESR MYASVPEIEA YAKDESKLKP LFLCEYSHAM GNGPGDLLDY
WKVIYAEPKL MGGCVWEWCD HGIERETEHG ETYYAYGGDF GEKPHDGNFC IDGLVAPDRT
PHTGLLELKQ VIAPVRMDAV ELEKGRLQIR NLYDFVDLSH LVFYWKVERE GVLLQQGELR
GLRTAPHTGE VVELPLQPKL FSLDAVSLTI SCCLEEENVW AERGHEIMFQ QFELTSSVGS
GASKLFENKA SHTSIQVLEV ERKLLITGFD FSHSFDLRKG MPDQLTRHGV ALLEQPLSFN
MWRAPLDNDR PLVTRWQYEG LEHAGMKVYR CDWEQRAEGE VVVTVEFSLG LYTRKPIVRG
SAQWLFDAQG AVTVKASAEV KKEIDFLPRF GLQLRMPAAM NTVEYVGYGP HESYVDKRQS
VRKGRYVQRV EEMGESYIMP QENGSRWGTD WALVSNELGM GLLLDGTEPF SLNASRYLPQ
DLTAAKHTYE LQQRKETIVQ LDYKMSGVGS HSCGPKLMDK YQLKEKQFDF QFTLRPVFKE
DE
//
