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Database: UniProt
Entry: R7A7G3_9BACE
LinkDB: R7A7G3_9BACE
Original site: R7A7G3_9BACE 
ID   R7A7G3_9BACE            Unreviewed;       834 AA.
AC   R7A7G3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:CDD51434.1};
GN   ORFNames=BN800_02556 {ECO:0000313|EMBL:CDD51434.1};
OS   Bacteroides sp. CAG:875.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1262752 {ECO:0000313|EMBL:CDD51434.1, ECO:0000313|Proteomes:UP000018287};
RN   [1] {ECO:0000313|EMBL:CDD51434.1, ECO:0000313|Proteomes:UP000018287}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:875 {ECO:0000313|Proteomes:UP000018287};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDD51434.1}.
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DR   EMBL; CBHD010000177; CDD51434.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7A7G3; -.
DR   Proteomes; UP000018287; 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   InterPro; IPR008964; Invasin/intimin_cell_adhesion.
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   SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 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..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..834
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004427462"
FT   DOMAIN          34..181
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          191..295
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          303..545
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
FT   DOMAIN          656..714
FT                   /note="DUF4982"
FT                   /evidence="ECO:0000259|Pfam:PF16355"
FT   DOMAIN          728..830
FT                   /note="Glycoside hydrolase family 2"
FT                   /evidence="ECO:0000259|Pfam:PF18565"
SQ   SEQUENCE   834 AA;  94479 MW;  B79FC8F9D3E35E4C CRC64;
     MKKLLLFLHV FCCSCFMVFS TTVSTCRERI NLGDCWRFHN GDEPEAVDAN FEDTGWQLLD
     LPHDWAIEGN FSKDNPSGTG GGALPGGIGW YRKTFVPEKA DSDMKFRIVF DGVYMNSEVY
     LNGILLGRRP YGYITFSYDL TPHLKWGEKN VLAVRVDNSE QPNSRWYSGC GIYRNVWLVK
     TEAVHVGEWG TYVTAPVVNK SKAIVRVQTT VSNETDVDAK VTVCSSLFDA EGKCVAKTDT
     LCQVGGQADA VAVQQLSVAD PHRWDIESPY LYTLVTELMD GEHCIDRYET ITGIRSFKFD
     AQKGFVLNGK PTKINGVCMH HDLGCLGAAV NMRAIERQLE ILKEMGCNGI RCSHNPPAPE
     LLDLCDQMGF IVMDEAFDMW RKKKTAHDYA RYFNDWHERD LHDFIMRDRN HPSIFMWSIG
     NEVLEQWSHA NADTLSLEEA NLILNFGHSK NMLAKEEEMS VNSLLTKKLA DIVRELDPTR
     PVTAGCNEPN PFNHLFKSGA LDIIGYNYHN INILDVPKNF PSKPFIITES NSTLATRGYY
     KMPSDKEFIW PERWDKPFYD PSFSCSSYDN CHAPWGNTHE ETLKLIRDND FISGQYVWTG
     FDYIGEPTPF GWPARSSYFG IVDLAGFPKD TYYLYQSEWS EEQVLHLFPH WNWKPGQVVD
     MWCYYNKADE VELFVNGKSQ GVKSKTPDCL HAMWRVEYEP GSVKVIARKN GKVVGEKEIR
     TAGEPVQIRL TPDRSQLTAN GKDLSFITVE ILDKDGNLCP NADNLVNFKV EGDIFIAGVD
     NGSPISMEHF KANKRRAFYG KCLVVIQNQG KQGTAHLVAT SNGLQSANVK ITID
//
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