ID A0A1Q9Q3X6_9BACI Unreviewed; 686 AA.
AC A0A1Q9Q3X6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=BTR25_05485 {ECO:0000313|EMBL:OLS41310.1};
OS Bacillus sp. MRMR6.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1928617 {ECO:0000313|EMBL:OLS41310.1, ECO:0000313|Proteomes:UP000185615};
RN [1] {ECO:0000313|EMBL:OLS41310.1, ECO:0000313|Proteomes:UP000185615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRMR6 {ECO:0000313|EMBL:OLS41310.1,
RC ECO:0000313|Proteomes:UP000185615};
RA Thomas J.M., Ghebrendrias N., Rawat M.;
RT "Mendota Genome Annoucement.";
RL Submitted (DEC-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}.
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:OLS41310.1}.
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DR EMBL; MSLS01000003; OLS41310.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q9Q3X6; -.
DR STRING; 1928617.BTR25_05485; -.
DR Proteomes; UP000185615; 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: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};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000185615};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 20..401
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 412..616
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 627..684
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 158
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 322
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 330
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 686 AA; 79353 MW; B8914D42F53FCDB5 CRC64;
MSKHEKTYTT KANFMLHGGD YNPDQWLDRP DILEDDIKLM QLSHTNTFSV GIFAWAALEP
EEGIYHFEWL DKVIDDIYKI NGRVILATPS GARPAWMSQK YPEVLRVNGA RVKQLHGGRH
NHCFTSPVYR EKTQKINRML AERYGSHPAL LMWHISNEYG GECHCDLCQD AFREWLKNKY
NHNLKALNDA WWGPFWSHTF TEWSQIESPS SIGESMVHGL NLDWRRFVTD QTIDFFENEI
VPIKELTPEV PITTNFMADT HELIPFQALD YSKFAKHLDV ISWDAYPAWH NDWESTADLA
IRVGFIDDLY RSLKQQPFLL MESTPSMVNW HPVNKTKRPG MHMLASMQMV AHGSDSILYF
QWRKSRGSSE KFHGAVVDHD NSPNNRVFQE VAEVGKTLEK LADVVGTNRP SDVAILYDWE
SNWAINDAQG FGLETKRYPQ TLVEHYRAFW EKDIPVDVIT KEQDFSNYKL LIIPMLYLVS
EETIARLQSF VATGGRLVTT YISGLVNEHD LTYTGGWHKK LQDIFGINPI ETDTYYPSDR
NAVQFRNQSY ELKDYATVIE VNSATVEASY EDDFYAGTPA VTSHEYEKGK AYYIGGRLEA
DFQRDFYQEI IHDLALESVF DIKHNKGVSV QVRQAPESDY IFVMNFTEEE QPITIEVPVK
DVVTGEELQG ELTLERYAVR IVEKIK
//
