ID A0A1G0PDY3_9BACT Unreviewed; 781 AA.
AC A0A1G0PDY3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, 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};
DE Flags: Fragment;
GN ORFNames=A2068_02805 {ECO:0000313|EMBL:OGU33907.1};
OS Ignavibacteria bacterium GWB2_35_6b.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1798424 {ECO:0000313|EMBL:OGU33907.1, ECO:0000313|Proteomes:UP000178800};
RN [1] {ECO:0000313|EMBL:OGU33907.1, ECO:0000313|Proteomes:UP000178800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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, ECO:0000256|RuleBase:RU361154}.
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:OGU33907.1}.
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DR EMBL; MGZW01000244; OGU33907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0PDY3; -.
DR Proteomes; UP000178800; 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; 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; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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; 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 SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..781
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009566760"
FT DOMAIN 61..231
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 233..347
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 349..634
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 644..732
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|Pfam:PF16353"
FT NON_TER 781
FT /evidence="ECO:0000313|EMBL:OGU33907.1"
SQ SEQUENCE 781 AA; 89722 MW; 979D7A26099BB3E3 CRC64;
MIKTILILSA LFSLSLTAQN DWENHKIFNI GKEEPHAEII SYESFYKAVQ GEIYESRFTK
LLNGTWKFKW VNKPADRPVD FYKDDYNVSG WADIPVPSDW QMHGYGIPIY TNSIYPFSPN
NPTPPNIPHE YNPVGSYKRN FTVPDEWENR QIILHFGGVN SAMYVWINGE AVGYSQDSKT
PAEFNITKYL REGKNSLAVE VYRWCDGSYL EDQDFWRLSG IERDVYLYSV PQVHIKDYFA
HPDLDSEYID GIFSLTAKVK NYLTEDVKNC SVSVDLLDAD NQSILNKKLM KKISIDKNTE
TNIDFETTIK NPLKWTAETP NLYKLIITLQ DDKGENTEFV LAKIGFRKVE IKDGRLTING
IPITLKGVNR HEHDPLTGHV VSEESMITDI KLMKQFNINA VRTSHYPNDP LWYKLCNEYG
LYLIDEANIE SHGMGYNPER TLANNPDWME AHVDRTQRMV ERDKNHPSVI IWSLGNEAGD
GVNFSATYKW IHQKDNSRPV QYEGARKGEN TDIYCPMYPS INHITEYAGT TQDRPLIMCE
YSHSMGNSTG NLQDYWDAIE SHKQLQGGFI WDWVDQGFLK KDSLGKSFWA YGGDYGPAGT
PSDSNFCFNG LVSPDRQPHP ALWEVKKVYQ YIKILPEDLL AGKIKIINKY DFQNLDFVDI
LWQLYGEGKV LEEGKFPALK INPKEEREIT IPIKKPELSA GAEYFLKIFL ALNKDESWAD
KGHVVAWEQF MIPFEVPETV EENINSMPQL TYTNSDAGIN VKGNNFELLI GNNTGALEHF
I
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