ID I3WJ66_BIFBI Unreviewed; 689 AA.
AC I3WJ66;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
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 Name=bgaB {ECO:0000313|EMBL:AFL04929.1};
GN ORFNames=BBB_1337 {ECO:0000313|EMBL:AFL04929.1};
OS Bifidobacterium bifidum BGN4.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=484020 {ECO:0000313|EMBL:AFL04929.1, ECO:0000313|Proteomes:UP000006173};
RN [1] {ECO:0000313|EMBL:AFL04929.1, ECO:0000313|Proteomes:UP000006173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGN4 {ECO:0000313|EMBL:AFL04929.1,
RC ECO:0000313|Proteomes:UP000006173};
RX PubMed=22887663; DOI=10.1128/JB.00988-12;
RA Yu D.S., Jeong H., Lee D.H., Kwon S.K., Song J.Y., Kim B.K., Park M.S.,
RA Ji G.E., Oh T.K., Kim J.F.;
RT "Complete Genome Sequence of the Probiotic Bacterium Bifidobacterium
RT bifidum Strain BGN4.";
RL J. Bacteriol. 194:4757-4758(2012).
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; CP001361; AFL04929.1; -; Genomic_DNA.
DR RefSeq; WP_013363739.1; NC_017999.1.
DR AlphaFoldDB; I3WJ66; -.
DR SMR; I3WJ66; -.
DR KEGG; bbf:BBB_1337; -.
DR PATRIC; fig|484020.3.peg.1322; -.
DR HOGENOM; CLU_012430_1_1_11; -.
DR Proteomes; UP000006173; 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:0006012; P:galactose 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 Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR013739; Beta_galactosidase_C.
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; IPR013780; Glyco_hydro_b.
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; PF08533; Glyco_hydro_42C; 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:AFL04929.1};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:AFL04929.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006173}.
FT DOMAIN 25..396
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 412..622
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 642..689
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
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 689 AA; 77190 MW; B31954A162218846 CRC64;
MSKRRKHSWP QPLKGAESRL WYGGDYNPDQ WPEEVWDDDI RLMKKAGVNL VSVGIFSWAK
IEPEEGKYDF DWLDRAIDKL GKAGIAVDLA SATASPPMWL TQAHPEVLWK DERGDTVWPG
AREHWRPTSP VFREYALNLC RRMAEHYKGN PYVVAWHVSN EYGCHNRFDY SDDAMRAFQK
WCKKRYKTID AVNEAWGTAF WAQHMNDFSE IIPPRYIGDG NFMNPGKLLD YKRFSSDALK
ELYIAERDVL ESITPGLPLT TNFMVSAGGS MLDYDDWGAE VDFVSNDHYF TPGEAHFDEV
AYAASLMDGI SRKEPWFQME HSTSAVNWRP INYRAEPGSV VRDSLAQVAM GADAICYFQW
RQSKAGAEKW HSSMVPHAGE DSQIFRDVCE LGADLGRLSD EGLMGTKTVK SKVAVVFDYE
SQWATEYTAN PTQQVDHWTE PLDWFRALAD NGITADVVPV RSDWDSYEIA VLPCVYLLSE
ETSRRVREFV ANGGKLFVTY YTGLSDENDH IWLGGYPGSI RDVVGVRVEE FAPMGNDMPG
ALDHLDLDNG TVAHDFADVI TSTADTSTVL ASYKAERWTG MNEVPAIVAN GYGDGRTVYV
GCRLGRQGLA KSLPAMLGSM GLSDLAGDGR VLRVERADAA AASHFEFVFN RTHEPVTVDV
EGEAIAASLA HVDDGRATID PTGVVVLRR
//
