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Database: UniProt
Entry: R6DFZ2_9BACE
LinkDB: R6DFZ2_9BACE
Original site: R6DFZ2_9BACE 
ID   R6DFZ2_9BACE            Unreviewed;      1014 AA.
AC   R6DFZ2;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN   ORFNames=BN772_01612 {ECO:0000313|EMBL:CDA83131.1};
OS   Bacteroides sp. CAG:754.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1262750 {ECO:0000313|EMBL:CDA83131.1, ECO:0000313|Proteomes:UP000017906};
RN   [1] {ECO:0000313|EMBL:CDA83131.1, ECO:0000313|Proteomes:UP000017906}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:754 {ECO:0000313|Proteomes:UP000017906};
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   -!- 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   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
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:CDA83131.1}.
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DR   EMBL; CBCP010000059; CDA83131.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6DFZ2; -.
DR   Proteomes; UP000017906; Unassembled WGS sequence.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR   Gene3D; 2.70.98.10; -; 1.
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; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR014718; GH-type_carb-bd.
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; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
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   PRINTS; PR00132; GLHYDRLASE2.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017906}.
FT   DOMAIN          44..203
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          206..316
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          319..606
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
SQ   SEQUENCE   1014 AA;  116335 MW;  800CF2A366070CA3 CRC64;
     MYKLNLMNQY FALFLLLIFP VLSIAQELEI PKQSVYQVRD KMELQTLNGK WKFKYIENKN
     IPSSLSGFVE SNFDDSTWDY ITVPSNWETE GFKTPQYGAD IVESWGLYRT TFKANPVWKN
     RHVILRFDGV QFGYEVYVNG HYAGRWGSSF NPCQFDITSF LHFDRPNVLA VKVSTRTKGW
     RFDLNDCWAL AGIFRDVELF SVPNLHLKDV TFVSKLEGNE RAALTFNVDV AAFKTLDDSE
     QYRAQVLFYD KTGRHLFSSS QPIVLKENGQ LLQFDWRLQN PHLWTAETPY LYRMEVRIMD
     SRNSVVQQIS ENVGVREVLV KDGILLVNNT PVLLRGTCHN EIDPVHGRAL TTADRLKQLQ
     MMKAANVNFI RTAHYPFHPE FHKMCDEMGF YVCCEVPFGY GDSNLYKEEY TTELCTRAEA
     TLTRDKNHPS IIMWTIGNEN PYTEVVEKVV QYVKQKDPTR PRALPMAGNY FLENRERLSD
     NLDIYAFHYQ SAQTVARIAD LKQKPVITTE YSHALGLAFD ALESQFDTIL SRKNIAGGAV
     WCWSDQALLR NRTKNDFMCD SVPMGVWLDS LRYLDSYNDK GTDGIVYADG YPQEDYWQLR
     KIYSPIVVLD KEFGIHEGKQ IIELTVENRF NFISLVGYRC NWQIRNLSKE LGNGSVQLSA
     LAGQQEKISL QCILPADIEN NDCMLYLEVT DNRGAPVYEK SIPLLVDNQR PDYLKLVGHL
     PEQKRFRIQK SSAMLSVQGE DYLFAVDKNG KLTIQDTDKR KVMDTYLYLR VGRKPSINIV
     NFLMRKKTFG WEPYLLTPEV KKFDCMEEKG KVSARLHCRW SRVDKAGEYI EGDVIFSVTK
     NGVMTVDYDL VPYHTTGTLW ECGPTFALHP SIETFRWLGN GPYTSTPGKT AYNERDTWAL
     HKDDMHFMGN RGLVDAAVLL DNENKGIGYI GSSSDLAVEK IGDAIYITDN AIVSSYGTKL
     SQPVVNNKAD KVKNIKGKFN LMLVGKAGNM LLTPLFSPYS EVLPNMHFLK SYGH
//
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