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Database: UniProt
Entry: D4BMY8_BIFBR
LinkDB: D4BMY8_BIFBR
Original site: D4BMY8_BIFBR 
ID   D4BMY8_BIFBR            Unreviewed;       691 AA.
AC   D4BMY8;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-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   ORFNames=BIFBRE_03435 {ECO:0000313|EMBL:EFE89025.1};
OS   Bifidobacterium breve DSM 20213 = JCM 1192.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=518634 {ECO:0000313|EMBL:EFE89025.1, ECO:0000313|Proteomes:UP000003191};
RN   [1] {ECO:0000313|EMBL:EFE89025.1, ECO:0000313|Proteomes:UP000003191}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20213 {ECO:0000313|EMBL:EFE89025.1,
RC   ECO:0000313|Proteomes:UP000003191};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFE89025.1}.
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DR   EMBL; ACCG02000009; EFE89025.1; -; Genomic_DNA.
DR   RefSeq; WP_003828493.1; NZ_JDUD01000004.1.
DR   AlphaFoldDB; D4BMY8; -.
DR   SMR; D4BMY8; -.
DR   STRING; 1685.RY69_1497; -.
DR   KEGG; bbrd:BBBR_0453; -.
DR   PATRIC; fig|518634.20.peg.478; -.
DR   HOGENOM; CLU_012430_1_1_11; -.
DR   Proteomes; UP000003191; Unassembled WGS sequence.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003191}.
FT   DOMAIN          24..396
FT                   /note="Glycoside hydrolase family 42 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02449"
FT   DOMAIN          410..620
FT                   /note="Beta-galactosidase trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08532"
FT   DOMAIN          632..690
FT                   /note="Beta-galactosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08533"
FT   ACT_SITE        160
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   ACT_SITE        318
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         326
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ   SEQUENCE   691 AA;  77346 MW;  7A998DCDC816284A CRC64;
     MEHREFKWPQ PLAGGKPRIW YGGDYNPDQW PEEVWDEDVA LMQKAGVNLV SVAIFSWAKL
     EPEEGVYDFD WLDRVIDKLG KAGIAVDLAS GTASPPMWMT QAHPEILWVD YRGDVCQPGA
     RQHWRATSPV FLDYALNLCR KMAEHYKDNP YVVSWHVSNE YGCHNRFDYS EDAERAFQKW
     CEKKYGTIDA VNDAWGTAFW AQRMNNFSEI IPPRFIGDGN FMNPGKLLDW KRFSSDALLD
     FYKAERDALL EIAPKPQTTN FMVSAGGAGI DYDKWGYDVD FVSNDHYFTP GEAHFDELAY
     SASLCDGIAR KNPWFLMEHS SSAVNWRPIN YRVEPGELVR DSLAHLAMGS DAICYFQWRQ
     SKAGAEKWHS SMVPHAGPDS QIFRDVCELG ADLNKLADEG LLSTKLVKSK VAVVFDYESQ
     WATEHTATPT QEVRHWTEPL AWFRALADNG LTADVVPVRG PWDEYEAVVL PSLTILSEET
     TRRVREYVAN GGKLFVTYYT GLVDDKDHVW LGGYPGSIRD VVGVRVEEFA PMGNDFPGAI
     DHLDLDNGTV AHDFADVITS VADTAHVVAA FKADKWTGFD GAPAITVNDF GDGKAAYIGA
     RLGREGLAKS LPALLEELGI ETSAEDDRGE VLRVERADET GENHFVFLFN RTHDVAIVDV
     DGEPLVASLA QVNESEHTAA IQPNGVLVVK L
//
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