ID A0A1C3S8T1_9BACI Unreviewed; 652 AA.
AC A0A1C3S8T1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=lacA2 {ECO:0000313|EMBL:SCA84282.1};
GN ORFNames=BGLY_0459 {ECO:0000313|EMBL:SCA84282.1};
OS Bacillus glycinifermentans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1664069 {ECO:0000313|EMBL:SCA84282.1, ECO:0000313|Proteomes:UP000093092};
RN [1] {ECO:0000313|Proteomes:UP000093092}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) 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}.
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DR EMBL; LT603683; SCA84282.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C3S8T1; -.
DR KEGG; bgy:BGLY_0459; -.
DR PATRIC; fig|1664069.6.peg.487; -.
DR Proteomes; UP000093092; Chromosome 1.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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, ECO:0000313|EMBL:SCA84282.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 1..356
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 367..578
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 589..647
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 119
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 277
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 285
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 652 AA; 74331 MW; C2039172042607CC CRC64;
MKLSRCNVMS VGIFSWVSLE PEEGRFTFDW LDRVLDAFKD NGIYAFLATP SGAKPAWMSK
KYPEVLRTDA NRVRSLHGKR HAHCYTSPVY RRKTAVINGK LAERYAHHPA VIGWHISNEY
SGECHCDLCQ AKFREWLLAK YKTLDQLNHA WWTGFWSHTY TDWDEVESPA PHGEDAVHGL
NLDWKRFVTD QTVDFCRHEI AHVRSFHPEL PVTTNFMGTF PGLNYWKFAD LLDVISWDSY
PAWHNNRQTD NELGAEIAFV HDINRSLKGG KPFMLMESTP SMTNWHDVSK LKRPGMHELS
SLQAVAHGSD TVQYFQWRKS RGSSEKLHGA VVDHEGSEHT RVFQDVKKLG EKLDKLDEIA
GTTAEPEVVL IFDWENRWAL EDAQGPRNIG LHYERTVKSF YQPFWQEGVP VDVIHMDGDF
SKYKLVIAPM LYMLKQDTAE RIERFVQEGG TFVATYWSGI VDENDLAFLG GFPGGLRKML
GIWSEEIDAL HDGQKNAIVM DADNRLGLSG RYEAAELCDL IHLEGAEALA FYEEDFYAGR
PALTVNLYGA GKAYYIASRN ETSFQKDFVS KLIEGTGIAK VLDTDLPDGV TAQMRTDGKH
DYIFLLNFTE ENENVALPDE AFTDVLKGTR KKGTVKLPPY GTAILRRSHR AE
//
