ID C6J324_9BACL Unreviewed; 170 AA.
AC C6J324;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=POTG_02773 {ECO:0000313|EMBL:EES72609.1};
OS Paenibacillus sp. oral taxon 786 str. D14.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=621372 {ECO:0000313|EMBL:EES72609.1, ECO:0000313|Proteomes:UP000003981};
RN [1] {ECO:0000313|EMBL:EES72609.1, ECO:0000313|Proteomes:UP000003981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D14 {ECO:0000313|EMBL:EES72609.1,
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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DR EMBL; GG695980; EES72609.1; -; Genomic_DNA.
DR AlphaFoldDB; C6J324; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_1569169_0_0_9; -.
DR Proteomes; UP000003981; Unassembled WGS sequence.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
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; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EES72609.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003981}.
FT DOMAIN 16..83
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 86..164
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
SQ SEQUENCE 170 AA; 19320 MW; 2CC4D0A1E2F0B333 CRC64;
MLPSDLSEGK LRSEIETTGS LTVQAELRDP AGKLIGRHEA QIDGKEAIEL DVPQPQLWNA
EQPRLYELIL TAGQEVLRFR VGFKKVEITD GIFRINGRAV KLKGVNRHDS HPELGQTIPV
NHMIADLKLM KRHNINTIRT SHYPNDPKFL DLCDEFGVYV IDERIWSAMV
//
