ID F8ASV2_BIFLN Unreviewed; 710 AA.
AC F8ASV2;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 47.
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=BLNIAS_02287 {ECO:0000313|EMBL:AEI98104.1};
OS Bifidobacterium longum subsp. longum KACC 91563.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1035817 {ECO:0000313|EMBL:AEI98104.1, ECO:0000313|Proteomes:UP000008938};
RN [1] {ECO:0000313|EMBL:AEI98104.1, ECO:0000313|Proteomes:UP000008938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC 91563 {ECO:0000313|EMBL:AEI98104.1,
RC ECO:0000313|Proteomes:UP000008938};
RX PubMed=21742881; DOI=10.1128/JB.05620-11;
RA Ham J.S., Lee T., Byun M.J., Lee K.T., Kim M.K., Han G.S., Jeong S.G.,
RA Oh M.H., Kim D.H., Kim H.;
RT "Complete Genome Sequence of Bifidobacterium longum subsp. longum KACC
RT 91563.";
RL J. Bacteriol. 193:5044-5044(2011).
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; CP002794; AEI98104.1; -; Genomic_DNA.
DR RefSeq; WP_014485870.1; NC_017221.1.
DR AlphaFoldDB; F8ASV2; -.
DR KEGG; blk:BLNIAS_02287; -.
DR PATRIC; fig|1035817.4.peg.1520; -.
DR HOGENOM; CLU_012430_1_1_11; -.
DR Proteomes; UP000008938; 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..397
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 411..622
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; 79122 MW; B3F2605FDD804750 CRC64;
MTTRRAFRWP SLLTPNGRGI AFGGDYNPDQ WPEETLDEDI HLMTQAGVNT VALAIFSWDK
IEPREGEFTF EWLDHVIDKL GAASIAVDLA SATATAPLWL YERHPEVLPI DRYGHVVNAG
SRQSWQPTSP VLKEYALRLC RKLAEHYKDN PYVTAWHMGN EYGWNNRYDY SDNALAAFRT
WCEAKYGTVD ALNEAWGTAF WSQHVNSFDE VLLPRHMGGD SMVNPPQQLD YERFGNDMLL
DFYKAERDAI EEICPGKPFT TNFMVSTDQC TMDYAQWANE VDFVSNDHYF HEGESHLDEL
ACSDALMDSL ALGKPWYVME HSTSAVQWKP LNTRKRAGEL MRDSLAHVAM GADAINFFQW
RQSASGAEAF HSAMVPHAGS DTKLFRGVCE LGAALKTLSD AGVQDTELKR ADTAILFSAE
SEWATRSETL PSMKLNHWHD VRDWYRGYLD AGARADVVPL AYDWSGYQTI VLPTVIALSD
EDTRRIADFA ENGGTVIVGY ATGLIDEHFH IGLGGYPGAG NGLLRDMLGI RSEEFNILGE
EAEDEPAEIG LSNGLTTRLW QNDVTSVAPD TCVLATYVGT AAADWELDGV PAITSRTYGN
GTAIYVGCDL GRHDIARLLK EFGSCWRELS AQPTEGGQTP TYPTTDPRIL HTIRRSADGS
TRFDFYLNRS NQPVAVNGIE GEPIIAYRCE ADTTGYTLNR NAILIAKTSC
//