ID E0I7Q0_9BACL Unreviewed; 1039 AA.
AC E0I7Q0;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
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=PaecuDRAFT_1651 {ECO:0000313|EMBL:EFM11205.1};
OS Paenibacillus curdlanolyticus YK9.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=717606 {ECO:0000313|EMBL:EFM11205.1, ECO:0000313|Proteomes:UP000005387};
RN [1] {ECO:0000313|EMBL:EFM11205.1, ECO:0000313|Proteomes:UP000005387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YK9 {ECO:0000313|EMBL:EFM11205.1,
RC ECO:0000313|Proteomes:UP000005387};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., Anderson I.J.,
RA Johnson E., Loganathan U., Mulhopadhyay B., Kyrpides N., Woyke T.J.;
RT "The draft genome of Paenibacillus curdlanolyticus YK9.";
RL Submitted (JUL-2010) 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; AEDD01000004; EFM11205.1; -; Genomic_DNA.
DR RefSeq; WP_006037662.1; NZ_AEDD01000004.1.
DR AlphaFoldDB; E0I7Q0; -.
DR STRING; 717606.PaecuDRAFT_1651; -.
DR eggNOG; COG3250; Bacteria.
DR Proteomes; UP000005387; 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:UP000005387}.
FT DOMAIN 764..1037
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1039 AA; 117614 MW; EBC767A5544D814A CRC64;
MRDKWTYQPP ANGYPEWNNN PEIFQLNRLD AHASLMPFPS VQDALRGEHA ASPFYYSLNG
IWKFAFAETP DKRIRDFYET GFDSSGWADM PVPSHWQFQG YDYPHYTNVR YPWAESEPEL
QPPFAPTRYN PVGSYVRTFN VPDAWQGQPV YISFQGVESA FYVWLNGELV GYSEDTFTPA
EFDLTPYLIA GDNKLAVEVY RWCDASWLED QDFWRLSGIF RDVYLYATPP LHIADFFVRT
VLDEAYCDAE LQLDLKVENY VNHAGATCRV EAQLYDGQGK PVWKEALGDD VSFRHGELAQ
LSFAAAVRSP RLWSAESPNL YTLVLSLKDA SGALLETASC RVGFRSFELK DGLMRINGKR
IVFKGVNRHE FSCETGRALG KEDMIRDIVL MKRHNINAVR TSHYPNQSIW YELCDEYGLY
VIDETNLETH GSWSYGQKDL LARTVPASHP EWRANVLDRC NSMFQRDKNH PSIVIWSLGN
ESFGGDNFLA MYDFLKACDP TRLVHYEGIF HYRPSEAASD IESTMYIKPH EVEAYALSEP
AKPYILCEYA HAMGNSCGGL HKYTELFDKY DRLQGGFIWD WVDQAIRTTT ADGVTYLAYG
GDFGESPHDG NFSGNGLLFG DRTVTPKLHE VNKCYQSIAI EAVNLAEKQV RVSNKLLFTD
LSTYVLHWEV LQDGEVVEQG IRQLSLPAGE QDVVELPYQT AYAPAHEYVL TVSFKLRSDT
AWAAAGHEIA WEQFVLSPRL VQAAAAAGAT KAPLRITEQG DLFTVAGNKL TVSFSRRSGD
LVSYKDGGLE RLLEPVRPNF WRAVTDNDLG NKLQERCGVW KDAGAYRKLA SFRWQMEGER
CVVQAAYILP TVPVSSAVTV RYDITADGRM TVQQELIPGS DRLPDIPEIG MLFVLDGQLD
TIEWYGRGPH ESYWDRKSGA RLGRYVGTVQ GQFVPYLRPQ ECGNKTDVRF ASVSNGIDGA
GMRFESTTAM EINALPWTPS ELEACDHAYK LPITNRTVVR INDKQMGVGG DDSWGARTHP
EYTLPANRPY SFRFTITLV
//
