ID A0A087E9H5_9BIFI Unreviewed; 722 AA.
AC A0A087E9H5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=BITS_1288 {ECO:0000313|EMBL:KFJ04426.1};
OS Bifidobacterium tsurumiense.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=356829 {ECO:0000313|EMBL:KFJ04426.1, ECO:0000313|Proteomes:UP000029080};
RN [1] {ECO:0000313|EMBL:KFJ04426.1, ECO:0000313|Proteomes:UP000029080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13495 {ECO:0000313|EMBL:KFJ04426.1,
RC ECO:0000313|Proteomes:UP000029080};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family.
CC {ECO:0000256|ARBA:ARBA00005940}.
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:KFJ04426.1}.
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DR EMBL; JGZU01000018; KFJ04426.1; -; Genomic_DNA.
DR RefSeq; WP_026642355.1; NZ_JGZU01000018.1.
DR AlphaFoldDB; A0A087E9H5; -.
DR STRING; 356829.BITS_1288; -.
DR eggNOG; COG1874; Bacteria.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000029080; 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: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:0000313|EMBL:KFJ04426.1};
KW Hydrolase {ECO:0000313|EMBL:KFJ04426.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029080}.
FT DOMAIN 25..396
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 413..623
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 722 AA; 80351 MW; B488B70657CA8624 CRC64;
MSMQRKHTWP SLLTANGKGI AFGGDYNPDQ WPEEVWDEDI RLMKQAKVNV VALGIFSWDR
IQPAEGEWDF AWLDRIINKL GDAGISVDLA SATASAPIWL YNKYPEVLPQ DKYGHVINAG
SRQSWRPTSP VFKRFALALC KALAERYADN PTVTAWHIGN EYGWNNREDY SDDALREFRL
WCARKYGSID ALNKAWGSSF WSQEVHSFDD VLLPRHMGPD SMVNPSQQLD FERFGNDMLL
EFYKAERDVI AEISPDKPCT TNFMISTDQC AMDYAQWGRE VDFVSNDHYF HEGESHLDEL
ACSDSLVSSI AERNPWYLME HSTSAVQWKP LNARKRHGEL LRDSLAHVAM GADAINFFQW
RQSAFGAEAF HSAMLPHAGE HSKLFERVCE LGEALDMLSS AGVPGSTLVS SGTAILFSAQ
SEWATRCQTL PSNKLNHWHD VRDWYRAFLD AGSRADVVPL SAHWEGYSTV VLPTMLVLSN
EDAYRLKTFA AAGGTVIVGY ASGLVDEQFH VGLGGYPGAG DGVLRDMLGI RGEEFNILGD
EAQGETREIS LSNGMVTRLW QNDIDVVPDA DVLATYEGEG AEEWELQGVP AITSHAYGDG
KAIFVGCDLK CEDIARLISK ELSEVLTNTS SSIDYATSEF EDIDAGANRS VNNAILHTVR
KGENGIFDFY IVRGNSPVEV SVEAGTVLVA QHCTQADSSA QPDHQTRYAL QRNGILITKR
QA
//
