BGAL_HALL2
ID BGAL_HALL2 Reviewed; 663 AA.
AC P94804;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Beta-galactosidase BgaH;
DE Short=Beta-gal {ECO:0000250|UniProtKB:O69315};
DE EC=3.2.1.23;
GN Name=bgaH {ECO:0000312|EMBL:AAB40123.2};
OS Haloferax lucentense (strain DSM 14919 / JCM 9276 / NCIMB 13854 / Aa 2.2)
OS (Haloferax alicantei).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=1230452;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAB40123.2}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND INDUCTION.
RC STRAIN=Aa 2.2 / SB1;
RX PubMed=10760168; DOI=10.1046/j.1365-2958.2000.01832.x;
RA Holmes M.L., Dyall-Smith M.L.;
RT "Sequence and expression of a halobacterial beta-galactosidase gene.";
RL Mol. Microbiol. 36:114-122(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAB40123.2}
RP SEQUENCE REVISION TO C-TERMINUS.
RA Holmes M.L., Dyall-Smith M.L.;
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAB40123.2}
RP PROTEIN SEQUENCE OF 2-26; 286-300; 410-424; 425-431 AND 493-512, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC STRAIN=Aa 2.2 / SB1;
RX PubMed=9048905; DOI=10.1016/s0167-4838(96)00174-4;
RA Holmes M.L., Scopes R.K., Moritz R.L., Simpson R.J., Englert C.,
RA Pfeifer F., Dyall-Smith M.L.;
RT "Purification and analysis of an extremely halophilic beta-galactosidase
RT from Haloferax alicantei.";
RL Biochim. Biophys. Acta 1337:276-286(1997).
CC -!- FUNCTION: When overexpressed, cleaves several different substrates
CC including o-nitrophenyl-beta-D-galactopyranoside (ONPG), chromogen 5-
CC bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-Gal) and
CC lactulose, but not lactose. Has also beta-D-fucosidase activity. No
CC beta-L-fucosidase, beta-glucosidase, beta-arabinosidase or beta-
CC xylosidase activity. {ECO:0000269|PubMed:10760168,
CC ECO:0000269|PubMed:9048905}.
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:10760168, ECO:0000269|PubMed:9048905};
CC -!- ACTIVITY REGULATION: Requires 4 M NaCl for maximal activity. Loss of
CC activity if DTT or beta-mercaptoethanol is omitted from buffers.
CC Addition of 5-20 mM EDTA, 1 mM Cu(2+) or 1 mM Zn(2+) results in loss of
CC activity. {ECO:0000269|PubMed:9048905}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.87 mM for ONPG (in the presence of 2.5 M NaCl, at room
CC temperature and pH 7.2) {ECO:0000269|PubMed:9048905};
CC Vmax=110 umol/min/mg enzyme with ONPG as substrate (in the presence
CC of 2.5 M NaCl, at room temperature and pH 7.2)
CC {ECO:0000269|PubMed:9048905};
CC Temperature dependence:
CC Stable in 3 M NaCl for several days at room temperature, but
CC approximately 18% and 50% of specific activity is lost when samples
CC are stored overnight at 4 and -20 degrees Celsius, respectively.
CC Activity is irreversibly lost within minutes in low salt buffers.
CC Activity low, but detectable in 30% sorbitol in the complete absence
CC of salt and it is stable in 30% sorbitol for at least four months at
CC -20 degrees Celsius, but at room temperature approximately 20% of
CC specific activity is lost after 48 hours.
CC {ECO:0000269|PubMed:9048905};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9048905}.
CC -!- INDUCTION: Highest expression in cells grown on galactose. Glucose or
CC glycerol, alone or in combination with galactose, gives an intermediate
CC level of expression and peptone-containing media gives very low levels
CC of expression. {ECO:0000269|PubMed:10760168}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family. {ECO:0000255}.
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DR EMBL; U70664; AAB40123.2; -; Genomic_DNA.
DR PIR; T44793; T44793.
DR AlphaFoldDB; P94804; -.
DR SMR; P94804; -.
DR CAZy; GH42; Glycoside Hydrolase Family 42.
DR PRIDE; P94804; -.
DR BRENDA; 3.2.1.23; 13661.
DR BRENDA; 3.2.1.38; 13661.
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 Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.40.50.880; -; 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; PTHR36447; 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; SSF51445; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycosidase; Hydrolase; Metal-binding; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9048905"
FT CHAIN 2..663
FT /note="Beta-galactosidase BgaH"
FT /id="PRO_0000407697"
FT ACT_SITE 142
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT ACT_SITE 311
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 359..362
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT CONFLICT 21
FT /note="I -> F (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 663 AA; 74460 MW; 7ADF7634C5D13BE9 CRC64;
MTVGVCYFPE HWSRERWETD ISQMAEAGIE YVRMGEFAWR RIEPERGTFD FAWLDEAVEL
IGKFGMKAVL CTPTATPPKW LVDEHPDVRQ REQDGTPREW GSRRFTCFNS PTYRSETERI
VSVLTDRYAD NPHVAGWQTD NEFGCHETVT CYCEDCGEAF SEWLADRYES VADLNDAWGT
TFWSQQYDDF ESIDPPKPTP AANHPSRVLA YERFSNDSVA EYNRLHAALI REANDEWFVT
HNFMGGFSLD AFRLAADLDF LSWDSYPTGF VQDRQPDTPT VDELRAGNPD QVSMNHDLQR
GAKGKPFWVM EQQPGDINWP PQSPQPADGA MRLWAHHAVA HGADAVVYFR WRRCRQGQEQ
YHAGLRRQDG SPDRGYREAS TAADELFDLD SVDASVALVH DYESLWATRS QPLSPDWDYW
NHLRTYYDAL RARGVQVDIV SPEATLERYD AVVAPTLYLV GDELSTALTD YVDSGGCLLL
GARTGEKDPY NRLHESLAPG PLTALTGAQV ARHETLPDHV ETRLSYDGAT YEFRTWASWL
APEVGVPRGE YRTGEAAGNT AIVRNAAGDG SVTYCGCWPG DDLADALVTE LLDAAGVEYT
ERFPDGVRVM ERDGYTWALN FTSDPVTLTV PDSTGFLLGE STVDAFDTAV LDGSIRGVGL
ASE
