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Database: UniProt
Entry: A0A0S8ACY9_9BACT
LinkDB: A0A0S8ACY9_9BACT
Original site: A0A0S8ACY9_9BACT 
ID   A0A0S8ACY9_9BACT        Unreviewed;       601 AA.
AC   A0A0S8ACY9;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Beta-galactosidase {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=AMS20_17245 {ECO:0000313|EMBL:KPJ97249.1};
OS   Gemmatimonas sp. SG8_28.
OC   Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC   Gemmatimonadaceae; Gemmatimonas.
OX   NCBI_TaxID=1703357 {ECO:0000313|EMBL:KPJ97249.1, ECO:0000313|Proteomes:UP000051120};
RN   [1] {ECO:0000313|EMBL:KPJ97249.1, ECO:0000313|Proteomes:UP000051120}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_28 {ECO:0000313|EMBL:KPJ97249.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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:KPJ97249.1}.
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DR   EMBL; LJNQ01000402; KPJ97249.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8ACY9; -.
DR   PATRIC; fig|1703357.3.peg.2818; -.
DR   Proteomes; UP000051120; 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; 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; 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; 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   PRINTS; PR00132; GLHYDRLASE2.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE   3: Inferred from homology;
FT   DOMAIN          5..74
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          81..272
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
FT   DOMAIN          395..473
FT                   /note="DUF4982"
FT                   /evidence="ECO:0000259|Pfam:PF16355"
FT   DOMAIN          486..587
FT                   /note="Glycoside hydrolase family 2"
FT                   /evidence="ECO:0000259|Pfam:PF18565"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KPJ97249.1"
SQ   SEQUENCE   601 AA;  66131 MW;  DBDE3974BF95E1FC CRC64;
     LVLAILDTAG GEVARVEAPF TLAAGAATEV TQSLTVDAPA FWSPATPVLY TLRTTVLDAT
     GRAVDGTDTP FGIREIVYDA DRGFLLNGDR VKMLGVNLHH DGGPVGAAVP EAVWERRLIL
     LKQMGVNAIR TAHNPPAPEF LDLCDRLGLL VMDEAFDEWT HGKVEYGYHR YFAEWADRDL
     VDFIRRDRNH PSVVLWSLGN EIGEQHAAGG DTVLRALRDI AHREDPTRPV TTGNDHIYAD
     DGATTVEFMQ LLDVVGYNYV DRWHERRELY ATADRHAHPD WKFIGTESGS VWGTRGEYSL
     GSDPERVQPS YTAGMIRAEQ LWRFVALNDW FAGDFMWTGI DYLGEAFWPR KNSTSGVLDL
     VGFPDDGYFF YQSRWTEAPM VHLLPHWNWP GREDQLVPVL AYTNCDAVEL SLNGRFLGEK
     RLEFPRQGTS GGWNSYERPQ VFPTTADLHL SWDVPYEPGL LRAVGKRGGE VVAIAEVRTA
     GPAASLRLSV DRAGIRAGER DVAHVRVEIV DAAGVVVPGA NDLVRFTVDG PARLLAVGNG
     DPTDHSSYQD PERHAFHGLL LAMIQSTDEA GTVTVTAHAE GLAPASIAIT VVPGEGATRL
     P
//
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