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Database: UniProt
Entry: A0A1M3QTY2_9SPHI
LinkDB: A0A1M3QTY2_9SPHI
Original site: A0A1M3QTY2_9SPHI 
ID   A0A1M3QTY2_9SPHI        Unreviewed;       611 AA.
AC   A0A1M3QTY2;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:OJY88223.1};
GN   ORFNames=BGP13_06720 {ECO:0000313|EMBL:OJY88223.1};
OS   Sphingobacteriales bacterium 40-81.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX   NCBI_TaxID=1895835 {ECO:0000313|EMBL:OJY88223.1, ECO:0000313|Proteomes:UP000184064};
RN   [1] {ECO:0000313|EMBL:OJY88223.1, ECO:0000313|Proteomes:UP000184064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=40-81 {ECO:0000313|EMBL:OJY88223.1};
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:OJY88223.1}.
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DR   EMBL; MKWF01000046; OJY88223.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3QTY2; -.
DR   STRING; 1895835.BGP13_06720; -.
DR   Proteomes; UP000184064; 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; PTHR42732; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR42732:SF2; BETA-MANNOSIDASE; 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.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   DOMAIN          103..179
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          247..310
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          354..481
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
SQ   SEQUENCE   611 AA;  69262 MW;  CBCB57BC608B731F CRC64;
     MKYSFLFLMF FVSVTGFTQS QWQPVAGKIS TEWAAKVDPA NVLAEYPRPQ LTRSNNWINL
     NGLWEYSIQP RQDVEEFPSA FQGNILVPFA VESSLSGVGK TVGKDNVLWY KRKIDVPLTY
     RKGRVLLHFG AVDWAADVFV NGKKAGNHQG GYDPFSFDIT DLLKKGTSQE IAVRVWDPSD
     EGPQPRGKQV KKPEGIWYTP VTGIWQTVWI EGVPQTYIAA TRQTPDIDSK KLTLGVNVLN
     LAAGDELKAT AWDGSQLVAE VSGTANTLID LNIPNPKLWS PASPFLYNLK IAVIRKGKVV
     DEVGSYFAMR KSSLAKDAEG ISRMMLNNQF MFQYGPLDQG WWPDGLYTAP TDEALKFDIV
     KTKELGFNMI RKHVKVEPAR WYYHCDKEGI LVWQDMPSGD MGGNAWDMRA GQITGRQLDK
     DRTPVSEEIY RKEWKAIMDA CHNFPSIVAW VPFNEAWGQF KTKEIVDWTM QMDPSRLVNE
     SSGGNFFGSG HILDIHHYPD PEMPDPRVFG DKPQALVLGE FGGLGLPLEG HTWQDTKNWG
     YQSFKNKDEL FNKYAEFINR LPKLIKMGLS AAVYTQTTDV EIETNGFFTY DRKVLKIPVE
     KAQQVHRQLY Q
//
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