ID D2Q7B1_BIFDB Unreviewed; 668 AA.
AC D2Q7B1;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Beta-glucuronidase {ECO:0000256|ARBA:ARBA00016205};
DE EC=3.2.1.31 {ECO:0000256|ARBA:ARBA00012761};
GN Name=lacZ1 {ECO:0000313|EMBL:ADB10673.1};
GN OrderedLocusNames=BDP_2112 {ECO:0000313|EMBL:ADB10673.1};
OS Bifidobacterium dentium (strain ATCC 27534 / DSM 20436 / JCM 1195 / Bd1).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=401473 {ECO:0000313|EMBL:ADB10673.1, ECO:0000313|Proteomes:UP000008693};
RN [1] {ECO:0000313|EMBL:ADB10673.1, ECO:0000313|Proteomes:UP000008693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27534 / DSM 20436 / JCM 1195 / Bd1
RC {ECO:0000313|Proteomes:UP000008693};
RX PubMed=20041198; DOI=10.1371/journal.pgen.1000785;
RA Ventura M., Turroni F., Zomer A., Foroni E., Giubellini V., Bottacini F.,
RA Canchaya C., Claesson M.J., He F., Mantzourani M., Mulas L., Ferrarini A.,
RA Gao B., Delledonne M., Henrissat B., Coutinho P., Oggioni M., Gupta R.S.,
RA Zhang Z., Beighton D., Fitzgerald G.F., O'Toole P.W., van Sinderen D.;
RT "The Bifidobacterium dentium Bd1 genome sequence reflects its genetic
RT adaptation to the human oral cavity.";
RL PLoS Genet. 5:E1000785-E1000785(2009).
RN [2] {ECO:0007829|PDB:6LD0, ECO:0007829|PDB:6LD6}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
RX PubMed=33664385; DOI=10.1038/s42003-021-01815-w;
RA Lin H.Y., Chen C.Y., Lin T.C., Yeh L.F., Hsieh W.C., Gao S., Burnouf P.A.,
RA Chen B.M., Hsieh T.J., Dashnyam P., Kuo Y.H., Tu Z., Roffler S.R.,
RA Lin C.H.;
RT "Entropy-driven binding of gut bacterial beta-glucuronidase inhibitors
RT ameliorates irinotecan-induced toxicity.";
RL Commun. Biol. 4:280-280(2021).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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DR EMBL; CP001750; ADB10673.1; -; Genomic_DNA.
DR RefSeq; WP_012902563.1; NC_013714.1.
DR PDB; 6LD0; X-ray; 1.90 A; A/B/C/D=1-668.
DR PDB; 6LD6; X-ray; 2.20 A; A/B/C/D=1-668.
DR PDB; 6LDB; X-ray; 1.65 A; A/B/C/D=1-668.
DR PDB; 6LDC; X-ray; 2.18 A; A/B/C/D=1-668.
DR PDB; 6LDD; X-ray; 2.21 A; A/B/C/D=1-668.
DR AlphaFoldDB; D2Q7B1; -.
DR SMR; D2Q7B1; -.
DR STRING; 401473.BDP_2112; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR GeneID; 69535771; -.
DR KEGG; bde:BDP_2112; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_006501_6_1_11; -.
DR Proteomes; UP000008693; 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; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR023232; Glyco_hydro_2_AS.
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 PANTHER; PTHR10066; BETA-GLUCURONIDASE; 1.
DR PANTHER; PTHR10066:SF67; BETA-GLUCURONIDASE; 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 PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:6LD0, ECO:0007829|PDB:6LD6};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154};
KW Reference proteome {ECO:0000313|Proteomes:UP000008693}.
FT DOMAIN 15..196
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 269..355
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 357..661
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT REGION 237..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 668 AA; 74342 MW; 609BBE4E857FE48C CRC64;
MLYPQSNDSR IVFPLDGVWD FRTAGEDSYP AEWADAPLPE PLPMAVPGSY NDQNDELNLR
AHYGWVVYQR SFAVPSRLVA GQRMILRFDA ATHAADVYLN GQLLGSHFGG FLPFEFDVTS
ALHAGENLLT VAVDNRIGSS TLPVGNDAGT AFMGSDNANV PAVAEAKKHA RRQNLPNFDF
FNFAGLNRHV ELYTTPADAY IADIAITTER LDHIAGDACT AANALIAYDV TFGGDFPSNP
TDPNTPIQPS DPAINHADSS ESAESDIQRA TTYGRQVRIS ILDGEGTVVA GVTADIERSG
DGTAKASGEI AIRDAKLWNP GAAYLYTAVA ELLPEGGAES SSRIIDAYRQ TFGIRTVEVS
GTTFLINGKP FYFKGFGKHE DSYFHGRGTD DVLNVKDVSL IHWLHANSFR TSHYPYAESM
YDLCDREGIV IIDEVPAVGM SWLQYANPLV AERHREAIRG MIARDKNHPC IVMWSIANEP
GLDGDGERPR QAYDYFRPLY ELAHASDPQN RPVTLVCCQN DYTTDITERT MDVVCINRYY
GWYNLSGDLD AACHALNIEL DFWENIGKPV MFTEYGADTI EGIHGTHGEM FSEEFQRDYY
ARINAEIDKR PWFIGEQLWN FADFATFQGI IRVEGNRKGI LTRDRQPKMA AHWLRERWAG
IPDYGYKG
//
