ID A0A1I6UY93_9BACL Unreviewed; 1039 AA.
AC A0A1I6UY93;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=SAMN05428962_4092 {ECO:0000313|EMBL:SFT06396.1};
OS Paenibacillus sp. BC26.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1881032 {ECO:0000313|EMBL:SFT06396.1, ECO:0000313|Proteomes:UP000199637};
RN [1] {ECO:0000313|EMBL:SFT06396.1, ECO:0000313|Proteomes:UP000199637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC26 {ECO:0000313|EMBL:SFT06396.1,
RC ECO:0000313|Proteomes:UP000199637};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FPAD01000002; SFT06396.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6UY93; -.
DR STRING; 1881032.SAMN05428962_4092; -.
DR Proteomes; UP000199637; 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 767..1037
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1039 AA; 116758 MW; F54C5F2020E22A2A CRC64;
MKSKFTYTPP ANGYPEWNNN PEIFELNRMK AHATLMPFDS IEEALNGDRH ASRSSLSLNG
KWKFAFAETP EKRIANFYEE NYDASSWDEI AVPGHWQLQG YDYPQYTNIR YPWEVSEPDL
KPPFAPTKYN PVGSYVRSFS VPDEWQGQPV FISFQGVESA FYVWVNGELV GYSEDTFTPA
EFDLTPYLRA GDNKLAVEVY RWCDASWLED QDFWRMSGIF REVYLYTTPK AHIYDFFVTT
ELDDAYRDAE LKLKATIMNY WEADLGTVTV EAQLYDSKRQ PVLAQPIVVT TTLGSSEAEV
EIEASVQVAN PLKWSAEQPN LYTLVISLKD AEQKQLETIS TQTGFRKFEI KNGLMLINGQ
RIVFKGTNRH EFSCHTGRAL GLEDMITDVK LMKTHNINAV RTSHYPNHPL WYELCNQYGL
YVIDETNLET HGSWAYDQME LLPHNVPASN PAWTANVLDR ANSMMQRDKN HPSIIIWSLG
NESFGGDNFV KMHDFLREAD PSRLVHYEGV TMWRESADAT DMESFMYAKP HKLAEYAHDH
RPKKPYILCE YSHAMGNSCG GLHIYTELFD KHPVLQGGFI WDWVDQAIWT TGEDGVSYMA
YGGDFGEQPH DGNFCGNGLI FADRSISPKL LEVKKCYQNI AITEVDGKQG LYRIQNKNLF
TNLDAYTLQW LVAIDGVRSA EGSLIVSVAP GEAGEITLPL PVRENQAGEA VLTISFVTTA
AAEWAAAGHE VAFEQFVLAA SKQALAGSVR AESSGAVEVK ELDDVLEVKG AGFSACFDQT
TGSLVSYKVG GTELLKSALA PNFWRAYTDN DRGNKHHERC ATWRSAGEER VLHALRYEAL
ADRVIVHAEY LLPTTVESAC SITYTVMGNG AIQVLQQLAP GEGLPEIPEI GMMLVMDGSF
ENLEWYGKGP HESYWDRQGS AKLGLYQGTP AEQFVPYLRP QECGNKMGVR RAAIGNGSGA
TLHITGAPSF ELNVLPYTPF ELEAHDHVYK LPASEKTVVR INYKQMGVGG DDSWGAMPHP
QYLLQANKTY AFSFTLQGK
//
