ID A0A0E9LV77_9BACT Unreviewed; 665 AA.
AC A0A0E9LV77;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=JCM15548_11660 {ECO:0000313|EMBL:GAO29472.1};
OS Geofilum rubicundum JCM 15548.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC Geofilum.
OX NCBI_TaxID=1236989 {ECO:0000313|EMBL:GAO29472.1, ECO:0000313|Proteomes:UP000032900};
RN [1] {ECO:0000313|EMBL:GAO29472.1, ECO:0000313|Proteomes:UP000032900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15548 {ECO:0000313|EMBL:GAO29472.1};
RX PubMed=25736980;
RA Inoue J., Oshima K., Suda W., Sakamoto M., Iino T., Noda S., Hongoh Y.,
RA Hattori M., Ohkuma M.;
RT "Distribution and evolution of nitrogen fixation genes in the phylum
RT bacteroidetes.";
RL Microbes Environ. 30:44-50(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAO29472.1}.
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DR EMBL; BAZW01000009; GAO29472.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E9LV77; -.
DR STRING; 1236989.JCM15548_11660; -.
DR Proteomes; UP000032900; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; 1.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
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 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 Pfam; PF02837; Glyco_hydro_2_N; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000032900}.
FT DOMAIN 25..202
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 220..329
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 336..483
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
SQ SEQUENCE 665 AA; 75628 MW; E08EABD91015B711 CRC64;
MRHLVVLLLM VLIASCGQRD NFVLDLAGEW QFQMDSADRG MDESWYAGEL GERMVLPGSL
MEAGIGHEIT LETQWTGSIY DSSWFFNPHT EPYRQPGNLM FPFWLTPDVY YVGAAWYQKE
VEVPNNWDER RIILHLERPH WESQVWVNGS HAGMQNSLSV PHEFDLTGLL KPGSNTISVR
VDNRVKDINP GPDSHSITDH TQGNWNGIVG EMKLIARPHV YVKNVQVYPD VETGRVKLLS
DMVNETGEVF SGEIEVHIEL FNVDVKAKAQ KMRFPVSVEK GDQTIELVVN MGDDVQLWDE
FHPALYKLSV DLHGDKGVSD VFETQFGFRS FEADGTRFKI NGRPVYLRGT VECAAHPLTG
YAPMDKAYWR SLYQKAMTYG VNHFRFHSWN PPRAAFEAAD ELGIYLQPEG PFWTNHGTAV
GDGLPVDQYI KDECDRLLET YGNHPSFVMF AYGNEPAGRH QIAFLNEMVE YWMEKDDRRL
YTHAAIGGSW PLAPSNEFII RAESRGLPWD SRPESMFDYS EKIAPYEVPY VAHEMGQYCV
FPDFEEIPKY TGVYKAKNFE MFKAELERKN MGDQARDFFM ASGTFQAICY KNEIEASLRT
PGNGGTQLLA LNDFPGQGTA LVGVTDVFGM RRTISHPQNS VAFLHQPCPW PGFPSLSLPT
MRCCL
//
