ID C6J307_9BACL Unreviewed; 1044 AA.
AC C6J307;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
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=POTG_02756 {ECO:0000313|EMBL:EES72592.1};
OS Paenibacillus sp. oral taxon 786 str. D14.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=621372 {ECO:0000313|EMBL:EES72592.1, ECO:0000313|Proteomes:UP000003981};
RN [1] {ECO:0000313|EMBL:EES72592.1, ECO:0000313|Proteomes:UP000003981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D14 {ECO:0000313|EMBL:EES72592.1,
RC ECO:0000313|Proteomes:UP000003981};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA White J., Yandava C., Allen-Vercoe E., Strauss J., Sibley C., White A.,
RA Lander E., Nusbaum C., Galagan J., Birren B.;
RT "The Genome Sequence of Paenibacillus sp. D14.";
RL Submitted (MAR-2009) 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; GG695980; EES72592.1; -; Genomic_DNA.
DR AlphaFoldDB; C6J307; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_002346_0_2_9; -.
DR Proteomes; UP000003981; 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:UP000003981}.
FT DOMAIN 767..1037
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1044 AA; 120398 MW; 623B5C4226FAE648 CRC64;
METSALRIIC TFNTYNNIGV ITLLKIDKYW EDPHTLHINR EKPRAYYIPY ANAETAASRK
RGRSPYYQTL NGAWKFQYHS SVEDVCESFY EANFDAEDWS SLLVPSCWQN NGYDQMHYSN
LNYTIPCDPP FVPDDNPAGL YIRDFHISSE WSNKEKYVVF EGVNACFYVW VNGNFVGYSQ
GSRIPAEFRI SDHLVPGVNR MAVMVLKYCD GTYLEDQDLW RYTGIFRDVY MLARDKVHIR
DVFVRTSLLN DDKEAKLNIE IEMTGEAVVH AVLRDPSGNV IVEMQEEVRQ TGQLQMQVTE
PKLWNAEQPV LYELLLSSGE EIIRFNVGFR RVEIREGVFQ INGVPVKLKG VNRHDSHPSL
GQTIPLQHMI NDLQLMKQHN INTIRASHYP NDPRFLELCN EYGFYVVDEA DLECHGLAIA
ETWDNMAKGL GMQSYPAFHE LSNNPDWEEA FVDRAIRMVE RDKNNPCVVI WSMGNESGYG
HNHIAMAKWT RERDNSRLIH YEGAASLYLG NPDVSVLDME SRMYASVPEI EAYAKDKSND
KPLFLCEYSH AMGNSPGDLL DYWNVIYAEP KLMGGCVWEW CDHGIERTTE HGEVYYAYGG
DFGDKPNDGN FCIDGLVAPD RTPHTGLLEL KQVIAPVRIE AIELEKGRLF IRNLYDFIDL
SHLVFYWKVE REGVLLEEGE LRGLRTPPHS GEEVQLAFQS DKSAIGTICL TISCCLEKQN
IWAERGHEIM FQQFEYTASE ESLALNSYKN KASHVSIQVL EQDRMLRIDG FDFSHSFDLR
RGVPNQLTRH GVQLLEHPLS FNMWRAPLDN DRVIASRWEY EGLEHASMKV YHCDWEQPSE
EEVIVTTEFS LGIYTRKPIV RGVAKWHVDA QGAITVKTSV QVKEEIDFLP RFGLQLRMPA
AMNTVDYVGY GPHESYIDKR QSVRKGRYLQ RVDQMSECYI MPQENGSRWG TEWVIVSNEL
GMGMLMDSTA SFSFNVSNYL PQDLTAAKHT YELRKRKETI VQLDYKMSGV GSNSCGPKLM
EKYQLNEKQF DFQFTLRPVF KEDE
//
