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Database: UniProt
Entry: W4UVS1_9BACE
LinkDB: W4UVS1_9BACE
Original site: W4UVS1_9BACE 
ID   W4UVS1_9BACE            Unreviewed;       846 AA.
AC   W4UVS1;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:GAE84604.1};
GN   ORFNames=JCM10512_2961 {ECO:0000313|EMBL:GAE84604.1};
OS   Bacteroides reticulotermitis JCM 10512.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1445607 {ECO:0000313|EMBL:GAE84604.1, ECO:0000313|Proteomes:UP000019131};
RN   [1] {ECO:0000313|EMBL:GAE84604.1, ECO:0000313|Proteomes:UP000019131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10512 {ECO:0000313|EMBL:GAE84604.1,
RC   ECO:0000313|Proteomes:UP000019131};
RA   Yuki M., Oshima K., Suda W., Sakamoto M., Iida T., Hattori M., Ohkuma M.;
RT   "Draft Genome Sequence of Bacteroides reticulotermitis Strain JCM 10512T,
RT   Isolated from the Gut of a Termite.";
RL   Genome Announc. 2:e00072-14(2014).
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:GAE84604.1}.
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DR   EMBL; BAIV01000018; GAE84604.1; -; Genomic_DNA.
DR   AlphaFoldDB; W4UVS1; -.
DR   STRING; 1445607.JCM10512_2961; -.
DR   Proteomes; UP000019131; 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; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR006103; Glyco_hydro_2_cat.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR006104; Glyco_hydro_2_N.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
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; 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; SSF75005; Arabinanase/levansucrase/invertase; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019131}.
FT   DOMAIN          334..438
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          483..580
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          592..727
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
SQ   SEQUENCE   846 AA;  96950 MW;  3CD0CEF529205251 CRC64;
     MTYVVYNGKG GTDGRGYETW LAESDNLLEW RTLGRVLSFR DGTWDANQRG GFPALPDMEW
     GGSYELQSYK GRHWMTYIGG EGTGYEAVKA PLYVGLAWTK DNIATAHEWE SLDKPILSIH
     DKDAQWWEKL TQYKSTIYWD KDKTLGAPFV MYYNAGGRHP ETDLKGERVG IALSKDMKKW
     KRYAGNPVFA HEVDGTITGD AHIQKMGDVY VMFYFSAFEP SRKYKAYNTF AASYDLVHWT
     DWTGADLIIP SKNYDELFAH KSYVIKHDGV IYHFYCAVNN AEQRGIAVAT SKPMGRSAVR
     FPKPEVKNRR ILTELNKDWK TWITEATHLK GNFMMPAQTV DIPHNWDDYY GYRQLTHGNM
     HGTAMYVKDF NIEVEAGKEY FLHFEGVGTY ATVKLNGQDF GRHPAGRTTL TLDVTKALKQ
     GANRLEVKAE HPEMIADMPW VCGGCSSEWG FSEGSQPLGI FRPVVLEATD LIRIEPFGVH
     IWNDEKAANV YVETEVKNYG KTTESIEVVN KLSNADGKQV FRLVEQVTLA PGETKTIRQQ
     APVESPILWS NDNPYLHKLA SMIKRGTATT DEVSTPFGIR TISWPVKRND GDGRFYLNNK
     PVFLNGVCEY EHQFGQSHAF STEQVASRVK QMRAAGFNAF RDAHQPHHLD YQNYWDKEGV
     LFWTQFSAHV WYDTPEFREN FKKLLRQWVK ERRNSPSVVI WGLQNESTLP REFAQECSDI
     IREMDPTARN MRIITTCNGG EGTDWNVIQN WSGTYGGNVF KYANELAQPN QLLNGEYGAW
     RSIDLHTEPG AFEADGVWSE ERMCQLMETK IRLAEQVRDS VCGQFQWIYS SHDNPGRRQP
     DEAYRR
//
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