ID   BGAL_THEBO              Reviewed;         645 AA.
AC   Q9X6C6;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   28-JUN-2023, entry version 64.
DE   RecName: Full=Beta-galactosidase BgaT;
DE            Short=Beta-gal {ECO:0000250|UniProtKB:O69315};
DE            EC=3.2.1.23;
GN   Name=bgaT {ECO:0000312|EMBL:AAD33667.1};
OS   Thermus brockianus.
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=56956;
RN   [1] {ECO:0000312|EMBL:AAD33667.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ITI360 {ECO:0000312|EMBL:AAD33667.1};
RX   PubMed=10473401; DOI=10.1128/aem.65.9.3955-3963.1999;
RA   Fridjonsson O., Watzlawick H., Gehweiler A., Rohrhirsch T., Mattes R.;
RT   "Cloning of the gene encoding a novel thermostable alpha-galactosidase from
RT   Thermus brockianus ITI360.";
RL   Appl. Environ. Microbiol. 65:3955-3963(1999).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:AAD33667.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RC   STRAIN=ITI360 {ECO:0000312|EMBL:AAD33667.1};
RX   PubMed=10741834; DOI=10.1007/s007920050004;
RA   Fridjonsson O., Watzlawick H., Mattes R.;
RT   "The structure of the alpha-galactosidase gene loci in Thermus brockianus
RT   ITI360 and Thermus thermophilus TH125.";
RL   Extremophiles 4:23-33(2000).
CC   -!- FUNCTION: Hydrolyzes pNP-beta-galactoside. Also possesses activity
CC       against galactose, and to a lesser extent towards melibiose and
CC       lactose. {ECO:0000269|PubMed:10741834}.
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:0000269|PubMed:10741834};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family. {ECO:0000255}.
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DR   EMBL; AF135398; AAD33667.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9X6C6; -.
DR   SMR; Q9X6C6; -.
DR   STRING; 56956.A0O31_01573; -.
DR   CAZy; GH42; Glycoside Hydrolase Family 42.
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:SF2; BETA-GALACTOSIDASE YESZ; 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.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   1: Evidence at protein level;
KW   Glycosidase; Hydrolase; Metal-binding; Zinc.
FT   CHAIN           1..645
FT                   /note="Beta-galactosidase BgaT"
FT                   /id="PRO_0000407694"
FT   ACT_SITE        141
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   ACT_SITE        312
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   BINDING         102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   BINDING         106
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   BINDING         140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   BINDING         150
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   BINDING         152
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   BINDING         155
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   BINDING         320
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   BINDING         360..363
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
SQ   SEQUENCE   645 AA;  73421 MW;  C79A9E1C0020EC40 CRC64;
     MLGVCYYPEH WPRERWSEDA RRMRELGLAY VRVGEFAWAL LEPEPGRLDW AWLDEAVAVL
     AQAGLKVVLG TPTATPPKWL VDRYPEILPV DREGRRRRFG GRRHYCFSSP VYHEETRRIV
     TLLGERYGKH PAVAGFQTDN EYGCHGTVRC YCERCQDAFR KWLEERYGSI DVLNEAWGTV
     FWSQRYRTFQ EVELPNLTVA EANPSHLLDY YRFASEQVRR YNRLQVEILR AHAPGKFVTH
     NFMGFFTDLN PFPLGEDLDF ASWDSYPLGF TDLMPLPEEE KLRYARTGHP DVAAFHHDLY
     RAVGRGRFWV MEQQPGPVNW APHNPNPAPG MVRLWTWEAL ANGAEVVSYF RWRQVPFAQE
     QMHAGLHRPD YAPDAAFFEV QRVVEELGAL SLPPPGQAPV ALVYDPEAPW VYEVQPHGAE
     WNYLALVFLF YSVARRLGLD VDIVPPGAAL QGYRLVLVPS LPIVREKALN AFREADGIVL
     FGPRSGSKNE NFHIPQGLPP GPLQALLPLK VVRVESLPPG LREEVEGPWG RFSSGLWREW
     VETDLSPLLR FADGLGALFR AGRYLYLAAW PSPELLGALL VGLAQEGGLS PKPLPSGLRL
     RWRGHLVFAF NYGPEEVVLP VPSGVRFRLG GPRLSPYEVA VWEEG
//