ID R6ZSW6_9BACE Unreviewed; 1037 AA.
AC R6ZSW6;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU361154};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU361154};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230, ECO:0000256|RuleBase:RU361154};
GN ORFNames=BN800_00198 {ECO:0000313|EMBL:CDD51593.1};
OS Bacteroides sp. CAG:875.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1262752 {ECO:0000313|EMBL:CDD51593.1, ECO:0000313|Proteomes:UP000018287};
RN [1] {ECO:0000313|EMBL:CDD51593.1, 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 -!- 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 ECO:0000256|RuleBase:RU361154};
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, ECO:0000256|RuleBase:RU361154}.
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:CDD51593.1}.
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DR EMBL; CBHD010000182; CDD51593.1; -; Genomic_DNA.
DR AlphaFoldDB; R6ZSW6; -.
DR Proteomes; UP000018287; Unassembled WGS sequence.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
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; IPR004199; B-gal_small/dom_5.
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; IPR023230; Glyco_hydro_2_CS.
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; IPR032312; LacZ_4.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR Pfam; PF02929; Bgal_small_N; 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 Pfam; PF16353; LacZ_4; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
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; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1037
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004427006"
FT DOMAIN 753..1028
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1037 AA; 118074 MW; 7678E0CD48209205 CRC64;
MKKQLVLGIL GACVLSASAQ TFKEWQDPEV NAINRAPMHA NFFAYENAEM ATKAVKEDSK
NFMSLNGTWK FFWVRNADAR PTDFWKVGFN DKGWDNLQVP GVWETQGYGD PIYVNVGYGW
RGRFANNPPY VPTEQNHVGS YRREIMVPAD WSGKDIIAHF GAVSSNMYLW VNGKFVGYSE
DSKLEAEFNL TPYLKPGQKN LIAFQVFRWC DGSYLEDQDF FRYTGVARDC YLYTRNKKRI
DDIRVTPDLD SEYKNGSLAI TLNLKGNGNV SLELLDAKNQ TVASTEVKGS GKVAATLQVE
NPQKWSAETP YLYTLRATLK DGSKTSEVVP VKVGFRKIEL KNAQILVNGQ PVLFKGADRH
EMDPDGGYVV SRARMIQDIQ IMKQLNINAV RTCHYPDDNF WYDLCDKYGI YVVAEANIES
HGMGYGEETL AKEPSYKKAH LERNQRNVQR GFNHPSIIFW SLGNEAGYGP NFEAAYDWVK
AEDPSRAVQY EQARIDGKTD IYCPMYADYK WCEEYSKNDK YQKPLIQCEY AHAMGNSEGG
FKEYWDLIRK YPKYQGGFIW DFVDQSIRWT GKNGKMIYAY AGDFNRMDDS GDKNFCDNGL
ISPDRKPNPH AYEVQYFYQN IWTTAGDLSK GEIKVYNENF FRDLSAYALE WEVLKDGKAI
RSGRVDNLNV APHQTATVKL DLGKTCQCGE WLLNVKYIQK NREGLLPAGS VVAKDQLVLN
PYKAPAMDLK NVTATNQQVV EPQINPNYPD YIAVEGDGFY MEFSKRNGYL DKYDVNGVSM
LKEGEALTPN FWRAPTDNDF GAGLQNKYAA WKNPGIKLTD FNYKVENGLA VVNSTYDLTE
VSAKLYLTYQ INNEGAVKVT QKMVADKNAK VSPMFRFGMQ MVMPKSFEKI SYYGRGPIEN
YIDRNHCTDL GIYNQNVSDQ FYPYIRPQET GTKTNIRWWR QLNMAGNGLM FVAEAPFSAS
ALHYTIASLD DGTEKKQSHS FEVEEADLTN LLIDKAQMGL GCVNSWGALP EAQYMLPYGD
YEFTFIMTPV KGYIACE
//
