ID A0A1Y5KC96_9BACL Unreviewed; 1113 AA.
AC A0A1Y5KC96;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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_22190 {ECO:0000313|EMBL:OUS73627.1};
OS Paenibacillus sp. MY03.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=302980 {ECO:0000313|EMBL:OUS73627.1, ECO:0000313|Proteomes:UP000195591};
RN [1] {ECO:0000313|EMBL:OUS73627.1, ECO:0000313|Proteomes:UP000195591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MY03 {ECO:0000313|EMBL:OUS73627.1,
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:OUS73627.1}.
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DR EMBL; MXQD01000032; OUS73627.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5KC96; -.
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; 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:UP000195591}.
FT DOMAIN 815..1091
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
FT REGION 776..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1113 AA; 123531 MW; 0F00C4F1E9C60FC8 CRC64;
MVRRRETMKR TRREAASLPD YENLNVLQRG TERPRAAAVP FADERSALEN DGLASPYYRC
LSGDWKFHYA ESPVEAPAGF HEPSYSCEDW ATLPVPSNWQ LHGYGVPLYS SSKYPFPVDP
PHIPKRNPTG CYVTTFSLGD EWLERCLVLA FDGVDAAFHL WVNGEEAGFG QGSHNRMEFD
ITSLVRKGEN KLAVRVYQWS TGSYLEDQDK WRLSGIFRDV HLLSVSGTHL FDAKLVTRLR
DSYREGALEV AVTIRNRSQG RAARSEETCS IEAKLLSPAM AAIASAAIAA AGPDPGEETV
ICAELPVAAP ELWSAEWPAL YTLLLTLKNG QGEATEVQRF SVGFRDVQVK DGKVLVNGNP
IIIRGVNRNE FHPDLGHVTT MEDMIRDIAL MKQHNINTVR CSHYPNDERW LDLCDRYGLY
VIDEADLETH GCVFLGEISR WINNPDEKTA FESTLAEDPA WREAFLDRMA RLVERDKNHP
SVIVWSIGNE SGYGVNHDAM AAWTRAADPT RPIHYERAGE SPVVDIVSSM YPSVDMLIAE
GEKEDTRPYL MVEFGHAMGN ALGNQQEYWD AVYRYPRLCG GLIWEWSDLA IRRKMDDGSL
RYAYGGDFGD EPHSGHFCID GLLFPDRSSK PALAEFKKAI EPVVVRPVEP ETGILRIINR
YDSVTLEHLL PRWRVYRNGD VIEEGELPPL PISPGDGELV AIPYRSVPSG RGEYWLHVSF
VLREHAAWAE AGHEVAWADV PLTRSGSTEA MHVPEVAAAM AAEAARAARE EAANAVVAKP
ESELSRTETG LSSTETGLSR TENELSLTEN DAALSVAGDG FALVFDKLAG EIVAWECRGA
SLLAKGPAIH LWRAPVDNDV HLAKRWREAG YHELTAYVRR VDSEIAEGGS AVRIEVESML
GVKGARMLFR TEQLYTIGGN GDVRLENRII PLKEDLPPLP RAGMRFAMAK SFDRFAWFGR
GPHECYPDRK ASGKLGVYEG KVSEQFVPYI KPQESGSKAD VRWATIAEAG GAGLLVAGAA
EGMLGQLGVN RYGTKALGET NHHADLVPSD EIEVLADWRQ SGLGNHSCGY APTLPSYLIS
AESMTYTVRL KPFWNDESRA AAIRRAHSSH KEG
//
