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Database: UniProt
Entry: A0A1M3M8U6_9BACT
LinkDB: A0A1M3M8U6_9BACT
Original site: A0A1M3M8U6_9BACT 
ID   A0A1M3M8U6_9BACT        Unreviewed;       796 AA.
AC   A0A1M3M8U6;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:OJX88028.1};
GN   ORFNames=BGP01_06995 {ECO:0000313|EMBL:OJX88028.1};
OS   Paludibacter sp. 47-17.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Paludibacteraceae;
OC   Paludibacter.
OX   NCBI_TaxID=1895899 {ECO:0000313|EMBL:OJX88028.1, ECO:0000313|Proteomes:UP000183960};
RN   [1] {ECO:0000313|EMBL:OJX88028.1, ECO:0000313|Proteomes:UP000183960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=47-17 {ECO:0000313|EMBL:OJX88028.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:OJX88028.1}.
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DR   EMBL; MKVT01000023; OJX88028.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3M8U6; -.
DR   STRING; 1895899.BGP01_06995; -.
DR   Proteomes; UP000183960; 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; 3.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR032311; DUF4982.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR040605; Glyco_hydro2_dom5.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR023232; Glyco_hydro_2_AS.
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; PTHR42732; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR   Pfam; PF16355; DUF4982; 1.
DR   Pfam; PF18565; Glyco_hydro2_C5; 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   PRINTS; PR00132; GLHYDRLASE2.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..796
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009895216"
FT   DOMAIN          27..172
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          183..290
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          300..453
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
FT   DOMAIN          614..677
FT                   /note="DUF4982"
FT                   /evidence="ECO:0000259|Pfam:PF16355"
FT   DOMAIN          690..790
FT                   /note="Glycoside hydrolase family 2"
FT                   /evidence="ECO:0000259|Pfam:PF18565"
SQ   SEQUENCE   796 AA;  89616 MW;  23A721564A7A0ACD CRC64;
     MKKHIGLLLL ILAVSAQAGE VRITQLFNFG WKFHYGDIND AQVPAFDDTA WRGLDLPHDF
     QFEQPWDEKS SPARGFKPMG VGWYRKTFKA DEAWKGRRVL LDVEGIMLIG DVWLNGTKVG
     STDYGYLGFE TDISKYLNYD GDNVLAVRAS TGETGGSRWY TGGGLYRDVH IVVKNQVAIA
     RHGVFVTTPL ITDAMAEVSV QVDIEGFRGK ADDLEIKAEI FGPDGRKVAE VKDLAPKRAN
     RWIEEVKLPL TKVDHPQLWS CETPNLYTAV VTLTLEGKPV DRFTEKFGIR TIEFSKEFGF
     KLNGKKVFLK GISNHHDMGP VGAAAYDAAA ARQMDVLKKF GYNHIRTSHN PYSKAFLRLA
     DEKGFIVVDE LYDKWSNRSY WGGRKPWTGL WFEHLTEWIK RDRNHPSVVL WSLGNELQMR
     EDLAGYPTGD WGVTTYRIMD VVAKRLDPTR KTTVAMFPAR AGGIGKNHPD FNTKIIPPEL
     ATVTDVSSFN YRWMNYPNYL EHAPDMIIYQ SEATTNELVA PFYGMDRERM VGLAYWGAIE
     YWGESHGWPR KGWNYSFFNH ALEPFPQAYL IKSIFSDEPL VHIGVVDSKT DTLTWNDIVV
     GLQPVSSHWN RTAGKKYSLF TYTNAEEVEL LVNGKSVGVK KNDATDVDKR NMVLWQNVSY
     APGRITAIAR TKGKEVARHQ LETTGKAVAL RMEVENAGWK ADGMDLQYVK VYAVDSKGRV
     VPEAAGEVVF DVAGAGRIIA VANGDHSSND LFDGNKRQLH KGFAMVVIRS HQQPGEVKVK
     ASVKGLRPAE KKMITQ
//
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