ID A0A2V3WV55_9BACI Unreviewed; 685 AA.
AC A0A2V3WV55;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
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=DES38_10162 {ECO:0000313|EMBL:PXW92982.1};
OS Streptohalobacillus salinus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Streptohalobacillus.
OX NCBI_TaxID=621096 {ECO:0000313|EMBL:PXW92982.1, ECO:0000313|Proteomes:UP000247922};
RN [1] {ECO:0000313|EMBL:PXW92982.1, ECO:0000313|Proteomes:UP000247922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22440 {ECO:0000313|EMBL:PXW92982.1,
RC ECO:0000313|Proteomes:UP000247922};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-2018) 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:PXW92982.1}.
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DR EMBL; QJJR01000001; PXW92982.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V3WV55; -.
DR Proteomes; UP000247922; 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:UP000247922};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 18..392
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 403..614
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 625..681
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 156
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 313
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 321
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 685 AA; 78378 MW; 2B7EADACFDEFD2E0 CRC64;
MMFKPLTEKL PKLLHGADYN PEQWLDYPEI FEQDLTLMQE AHVNVMSVGI FSWAKLEPEE
GVFDFAWMDT VIDRLYENGV SVFLATPTGA RPTWMSEKYP EVLRVSETRV RNLHGMRHNH
CYTSPIYREK TTIINQKLAE RYSDHPGVIG WHISNEYGGE CHCDLCQAAF RDWLKEKYQT
LDALNQAWWT TFWSHTYTAW SQLESPAPHG EQFVHGQTLD WKRFVTDQTL DFFRHEVKPL
KAKNQALPVT ANFMELFEGL NYDKFKDDLD IVSWDSYPTW HNATDDQEVA AYTAMNHDWF
RALKDGQPFL LMESTPSLTN WQPLSKLKKP GMHRLSSLQA VAHGSDSVQY FQWRKSRGSS
EKFHGAVVDH VGHSQTRVFK EVSDVGQTLE QLTELAGSSV KPEVAIIFDT ENRWAINDAE
GPRNAGVYYE RTVLEHYRAF WEQGVPVDII SEDRELSPYT LVVAPMLYMV REGIGEKIEA
FVEQGGTLVS TYWSGIVNET DLTYLGGFPG PLRKTLGIWS EEIDALADNE YNQATAKPGN
PLQLNGRFKI KELADLAHTE TAETLMTYDE DFYQGYPALT KNTLGSGSAY YQAARFDLDF
QRVFYKQLAK TLGLTHVWDT ALPSGVTVQK RENDTVRHLF IMNFNNSDQT LATAKTGLRD
ALSHALVATR IVVPAYGVRI LIEQK
//
