ID Q64P21_BACFR Unreviewed; 628 AA.
AC Q64P21;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN OrderedLocusNames=BF4019 {ECO:0000313|EMBL:BAD50761.1};
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405 {ECO:0000313|EMBL:BAD50761.1, ECO:0000313|Proteomes:UP000002197};
RN [1] {ECO:0000313|EMBL:BAD50761.1, ECO:0000313|Proteomes:UP000002197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46 {ECO:0000313|EMBL:BAD50761.1,
RC ECO:0000313|Proteomes:UP000002197};
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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|RuleBase:RU000675};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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DR EMBL; AP006841; BAD50761.1; -; Genomic_DNA.
DR RefSeq; WP_011203551.1; NC_006347.1.
DR RefSeq; YP_101295.1; NC_006347.1.
DR AlphaFoldDB; Q64P21; -.
DR STRING; 295405.BF4019; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR KEGG; bfr:BF4019; -.
DR PATRIC; fig|295405.11.peg.3867; -.
DR HOGENOM; CLU_007853_7_1_10; -.
DR OrthoDB; 703126at2; -.
DR Proteomes; UP000002197; Chromosome.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR026283; B-gal_1-like.
DR InterPro; IPR048912; BetaGal1-like_ABD1.
DR InterPro; IPR048913; BetaGal_gal-bd.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR InterPro; IPR019801; Glyco_hydro_35_CS.
DR InterPro; IPR001944; Glycoside_Hdrlase_35.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR23421:SF165; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF21317; BetaGal_ABD_1; 1.
DR Pfam; PF21467; BetaGal_gal-bd; 1.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PIRSF; PIRSF006336; B-gal; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..628
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004267923"
FT DOMAIN 34..357
FT /note="Glycoside hydrolase 35 catalytic"
FT /evidence="ECO:0000259|Pfam:PF01301"
FT DOMAIN 401..511
FT /note="Beta-galactosidase 1-like first all-beta"
FT /evidence="ECO:0000259|Pfam:PF21317"
FT DOMAIN 541..599
FT /note="Beta-galactosidase galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21467"
FT ACT_SITE 181
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT ACT_SITE 265
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ SEQUENCE 628 AA; 71056 MW; 285A6EBE0EDEC775 CRC64;
MRTKSIFLLL LLAVMPLCVF SQSKSTFEIK NGHFYRNGKI TPVLSGEMHY ARIPHQYWRH
RLQMMKGMGL NTVATYVFWN LHEPEPGKWD FTGDKNLAEF IKTAGEEGMM VILRPGPYVC
AEWEFGGYPW WLQNVKGMEI RRDNPEFLKY TKAYIDRLYK EVGSLQCTKG GPIVMVQCEN
EFGSYVAQRK DIPLEEHRAY NAKIKQQLAD VGFNVPLFTS DGSWLFEGGA TPGALPTANG
ESDIENLKKV VDQYHDGKGP YMVAEFYPGW LSHWAEPFPQ IGASGIARQT EKYLQNDVSF
NFYMVHGGTN FGFTSGANYD KKRDIQPDMT SYDYDAPISE AGWVTPKYDS IRNVIKKYVK
YTIPEAPAPN PVIEIPSIQL NKVADVLAFA EKQKPVSSDT PLTFEQLNQG YGYVLYTRHF
NQPISGTLEI PGLRDYAVVY VDGEQVGVLN RNTKTYSMEI EVPFNATLQI LVENMGRINY
GSEIVHNTKG IISPVQIAGK EIVGGWDMYQ LPMDEMPDLT KLKADTHKNV PSEVAKLKGC
PVLYEGTFTL DKVGDTFMDM ESWGKGIVFV NGVNIGRYWK VGPQQTLYVP GVWLKKGENK
IVIFEQLNET PQTEVKTVKT PVLMKLKG
//
