ID   D6ZY97_BIFLJ            Unreviewed;       710 AA.
AC   D6ZY97;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 59.
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=BLJ_0417 {ECO:0000313|EMBL:ADG99893.1};
OS   Bifidobacterium longum subsp. longum (strain JDM301).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=759350 {ECO:0000313|EMBL:ADG99893.1, ECO:0000313|Proteomes:UP000006740};
RN   [1] {ECO:0000313|EMBL:ADG99893.1, ECO:0000313|Proteomes:UP000006740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JDM301 {ECO:0000313|EMBL:ADG99893.1,
RC   ECO:0000313|Proteomes:UP000006740};
RX   PubMed=20525832; DOI=10.1128/JB.00538-10;
RA   Wei Y.X., Zhang Z.Y., Liu C., Zhu Y.Z., Zhu Y.Q., Zheng H., Zhao G.P.,
RA   Wang S., Guo X.K.;
RT   "Complete genome sequence of Bifidobacterium longum JDM301.";
RL   J. Bacteriol. 192:4076-4077(2010).
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; CP002010; ADG99893.1; -; Genomic_DNA.
DR   RefSeq; WP_008782890.1; NC_014169.1.
DR   AlphaFoldDB; D6ZY97; -.
DR   CAZy; GH42; Glycoside Hydrolase Family 42.
DR   KEGG; bll:BLJ_0417; -.
DR   HOGENOM; CLU_012430_1_1_11; -.
DR   Proteomes; UP000006740; 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};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001084}.
FT   DOMAIN          25..398
FT                   /note="Glycoside hydrolase family 42 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02449"
FT   DOMAIN          411..625
FT                   /note="Beta-galactosidase trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08532"
FT   DOMAIN          650..707
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   710 AA;  78964 MW;  DCD7578DB5849763 CRC64;
     MTTHRAFRWP SLLTESGRGI AFGGDYNPDQ WPEETLDEDI RLMGEAGVNV VSLAIFSWDK
     IEPVEGAFTF EWLDHVIDRL GRAGIAVDLA SATAAAPLWL YESHPEVLPV DRYGHTVNAG
     SRQSWQPTSP VFKEYALRLC RKLAEHYKDN PYVTAWHMGN EYGWNNRYDY SDNALAAFRT
     WCEAKYGTID ALNEAWGTAF WSQHVNSFDE VLLPRHMGGD AMVNPSQQLD YERFGNDMLL
     DFYKAERDAI EQICPDKPFT TNFMVSTDQC VMNYAKWADE VDFVSNDHYF HEGESHLDEL
     ACSDALMDSL ALGKPWYVME HSTSAVQWKP LNTRKRAGEL MRDSLAHVAM GADAICFFQW
     RQSKSGAEAF HSAMLPHAGA DSKVFRGVCE LGKALKTLSD AGLQGTELER AGTAILFSAE
     SEWATRSETL PSMKLNHWHD VRDWYRGFLD AGLRADVVPL AYDWTGYKTI VLPTVLSLSD
     EDVLRIADFA KAGGTVIVGY AAGLIDEHFH IGLGGYPGAG NGLLRDMLGI RSEEFNILGE
     EAEGEPSEIS LSNGLTTRLW QNDVTSVAAD TTVLASYAGE SAADWELERT PAITSRPYGN
     GTAIYVGCDL NRHDIAQLLK ALGSRWQELS AQPTESGQTP TYPTTDPRIL HTIRRSADGS
     TRFDFYLNRS NQPVAINGVE GDPIIAHRCE TDAVGYTLNR NAILIAKTSC
//