ID D2Q6C3_BIFDB Unreviewed; 700 AA.
AC D2Q6C3;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|PIRNR:PIRNR001084};
DE Short=Beta-gal {ECO:0000256|PIRNR:PIRNR001084};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|PIRNR:PIRNR001084};
GN OrderedLocusNames=BDP_1908 {ECO:0000313|EMBL:ADB10488.1};
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:ADB10488.1, ECO:0000313|Proteomes:UP000008693};
RN [1] {ECO:0000313|EMBL:ADB10488.1, 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).
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|PIRNR:PIRNR001084};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family.
CC {ECO:0000256|ARBA:ARBA00005940, ECO:0000256|PIRNR:PIRNR001084}.
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DR EMBL; CP001750; ADB10488.1; -; Genomic_DNA.
DR RefSeq; WP_012902492.1; NC_013714.1.
DR AlphaFoldDB; D2Q6C3; -.
DR STRING; 401473.BDP_1908; -.
DR CAZy; GH42; Glycoside Hydrolase Family 42.
DR KEGG; bde:BDP_1908; -.
DR eggNOG; COG1874; Bacteria.
DR HOGENOM; CLU_012430_1_1_11; -.
DR OMA; IGYLPRP; -.
DR Proteomes; UP000008693; Chromosome.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd03143; A4_beta-galactosidase_middle_domain; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR013738; Beta_galactosidase_Trimer.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR003476; Glyco_hydro_42.
DR InterPro; IPR013529; Glyco_hydro_42_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR36447; BETA-GALACTOSIDASE GANA; 1.
DR PANTHER; PTHR36447:SF1; BETA-GALACTOSIDASE GANA; 1.
DR Pfam; PF02449; Glyco_hydro_42; 1.
DR Pfam; PF08532; Glyco_hydro_42M; 1.
DR PIRSF; PIRSF001084; B-galactosidase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:ADB10488.1};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:ADB10488.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008693}.
FT DOMAIN 25..397
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 412..625
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT ACT_SITE 161
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 320
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 328
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 700 AA; 78202 MW; 6E66AF4CEC6F5E51 CRC64;
MTTRRTFSWP RLLTRNGGGI AFGGDYNPDQ WSEEIWDDDI RLMKQAGVNT VALAIFSWDR
IQPTEDRWNF GWLDRIIDKL GKAGIAVDLA SATATAPLWL YESHPEVLPR DKYGHQVNAG
SRQSWSPTSP VFKTYALTMC RKLAERYGDN PYVTAWHMGN EYGWNNREDY SDNALAAFRK
WCERKYGTVD ALNAAWGTTF WGQEMNGFDE VLIPRFMGTD SMVNPGQKLD FERFGNDMLL
DFYKAERDAI AEICPDKPFT TNFMVSTDQC CMDYADWAEE VDFVSNDHYF HEGESHLDEL
ACSDALMDSL ALGKPWYVME HSTSAVQWKP LNIRKRKGEI VRDSLAHVAM GADAINFFQW
RASAFGSEAF HSAMLPHAGE DTRVFRQVCE LGSVLKDLSA AGMQGSTLER SDTAILFSAE
SEWATRSETL PSMKLSHWHD VRDWYRAFLD AGQRADVVPL KYDWSAYSVV VLPSVLMLSA
ADTQRLADFT AAGGQVVIGY ATGLIDEHFH TWLGGYPGAG NGLLRKMLGI RGEEFNILGC
EAEGEPCEIE LGGGMDGAVT RLWQNDVNVE GPDTEVLATY SGKSADEWEL DGTAAITRNP
YGAGAAYFVG CDLNVADLTR FVRANLTTSG GEDDPRYGDV LHTVRKSADA TFDFYMPRGK
QEVTLRGIEG EPICQFHSEA GPEGPGSYVI HRNGMLITRR
//