ID A0A089JQQ5_9BACL Unreviewed; 1037 AA.
AC A0A089JQQ5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=H70737_10875 {ECO:0000313|EMBL:AIQ23309.1};
OS Paenibacillus sp. FSL H7-0737.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1536775 {ECO:0000313|EMBL:AIQ23309.1, ECO:0000313|Proteomes:UP000029519};
RN [1] {ECO:0000313|EMBL:AIQ23309.1, ECO:0000313|Proteomes:UP000029519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL H7-0737 {ECO:0000313|EMBL:AIQ23309.1,
RC ECO:0000313|Proteomes:UP000029519};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-2014) 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; CP009279; AIQ23309.1; -; Genomic_DNA.
DR RefSeq; WP_042187037.1; NZ_CP009279.1.
DR AlphaFoldDB; A0A089JQQ5; -.
DR KEGG; paej:H70737_10875; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_002346_0_2_9; -.
DR Proteomes; UP000029519; Chromosome.
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:UP000029519}.
FT DOMAIN 763..1035
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1037 AA; 118723 MW; 8BFB253A8D18FECB CRC64;
MRAKFVYQPP ANGYPEWNNN PEIFELNRLD AHASMIPYSN LTQALVGDKE TSPYYKTLNG
IWKFSFSETP DLRVVDFYKA DFDCSNWATI PVPSHWQFHG YDYPQYTNVR YPWAESEPDL
KPPFAPTKYN PVGSYIRTFT VPESWNGQPV YLSFQGVESA FYVWVNGERV GYCEDTFTPS
EFDITPYLIA GDNKLAVEVY RWCDASWLED QDFWRLSGIF REVYLYTAPS VHVADFFVKT
ELDEAFVHAD LNVDIKVENY FNEKLNPYTL QMQLYNKEDQ PVWEAPVSTF TSFDQEGVQH
FKLSEHVEDP YKWSAETPYL YTLVLSMIDD KGNTTETVSC KVGFRTFEIK DGLMKINGKR
IVLKGVNRHE FSCDTGRALS KDDMIRDIKL MKTHNINAVR TSHYPNQSVW YELCDEYGLY
VIDETNLETH GTWQYGQQGI HEGNVPASKP EWRANVIDRC NSMMQRDKNH PSVIIWSLGN
ESYGGDNFIA MHDYLREADP TRPVHYEGIF HCRESEAASD IESTMYAKPH DVEKYALSHP
QKPYIICEYS HAMGNSCGGL HLYTDMFDKF DVFQGAFIWD WVDQAIRTKT SEGVPYLAYG
GDFGESPHDG NFSGNGLLFA DRSVTPKLFE VKKCYQNIKV TALNIREGLF QIRNNFLFTD
IEQYEFKWEV SLDGVTAQEG LLQISAAPGE IVECTIPYEL ISHRGDHEAI LNLSFIQRSE
TSWADADHEI AWEQFILSPR IVTKAPKTTN GKLHVQEHEG ALTVQGGNFT LNFNTTTGEL
NSYYAAGKEH LLEPVRPNFW RAVTDNDLGN GLPKRCAVWK QASNERNLLS MKYRTEGNLC
FVSTTYLLPT NPYSTLLIQY EIRPDGSLEI LQELNPGSSA LPEIPEFGMM FVLAGRLDTL
SWYGRGPHEN YWDRQTGAPL GRYTGKVSDQ FSPYLRPQEC GNKTDVRFAS ITDGNDGSGL
YFDSAIPMEI NALPWKPEEL EAHDHVYKLP VSNKSVLRVN YKQMGVGGDD SWGAPTHEEF
TLPANRPYAF RFTLSLL
//
