ID R7CUF7_9BACE Unreviewed; 977 AA.
AC R7CUF7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=BN666_00958 {ECO:0000313|EMBL:CDD81521.1};
OS Bacteroides sp. CAG:462.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1262740 {ECO:0000313|EMBL:CDD81521.1, ECO:0000313|Proteomes:UP000018063};
RN [1] {ECO:0000313|EMBL:CDD81521.1, ECO:0000313|Proteomes:UP000018063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:462 {ECO:0000313|Proteomes:UP000018063};
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:CDD81521.1}.
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DR EMBL; CBHU010000010; CDD81521.1; -; Genomic_DNA.
DR AlphaFoldDB; R7CUF7; -.
DR STRING; 1262740.BN666_00958; -.
DR Proteomes; UP000018063; 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; 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 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; 2.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 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:UP000018063}.
FT DOMAIN 69..202
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 214..314
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 323..530
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT REGION 533..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 977 AA; 110563 MW; 084887A9D0B2625D CRC64;
MNSLQRHFAY PVITMKQTLL TGLMLLGATL GLRAQAPHPE RIYLSGTGID DTKTWEFFCS
KGQNSGSWKP IEVPCCWETQ GFGEYTYGRW YTVKGARPSD ETGTYRHTFK APRTENGQRV
KLFFDGVMTD AEVRVNGQPA GDIHRGAFYR FSYDITDLLR PGKKNTLEVK VAKQSADKSV
NNAERRADWW LFGGIFRPVW LEVVPAVNMA HIILDADQHG RLRAQVRMEG DAQGYALTTS
LRRLSDGTPV RNASGSDSQT VRIADNRAEQ LIDSRWEDID AWTPESPTLY VARVELKSPD
GKVIQAREFR TGFRTVEFFP QDGLYLNGTR LVLKGINRHS FSTDGGRTTS AAMSREDAKL
IKQMNMNAVR SHYPPDEHFL DMCDSLGLVY IDELAGWHGK YDTKVGTRLV REMVERDVNH
PCIVIWSNGN EGGWNTRLDT LFATHDVFQR RHVIHPWADF NDLDTHHYPA YLTGVARFTN
GYKVFMPTEF MHAMYDQGGG AGLRDFWDRW CTNPLFAGGF IWAFCDEAPK RSDRGGVLDS
DKSNAPDGVL GPRREKEGSF HAVRAQWSPV QLRPLFITDH FDGSFQVTNE YLYTRLSACR
MTWKVLLCAT PLLERNPRAE VLAEGTVTLP DIAPGETGTA HFSLPDAFRN GDVLELEAFD
RDGHSLCQWT YPIKNARTYY EEKLAFTPQT LEWTEPATAV RRDGTVTLKS DRVTVAFDDS
TGIIRRVTTD GVEVPLTNGP LPVGMKMRYN ADRSYVRRAA DGAVFCARYQ GGADSIVWKL
TDNGLLYMDA LLLNRASGGG GFDDAFMDTK VYNLGLTFDY PEQLCTGMQW LGRGPYRVWK
NRIPGTNYNI WQKDYNNTIT GESFENLVYP EFKGYHANLY WAGIRSDKAP FTVYSRTDGI
FFRVFTPEEP KGGDGRTMPR FPDGDLSFLL DIPAIRSFKP TEQQGPNSQP GNIRIKSGDE
GLHIDLVFDF RHTDKEH
//
