ID BGAL_ALIAD Reviewed; 688 AA.
AC C8WV58; Q06GJ1;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Beta-galactosidase BglY;
DE Short=Beta-gal {ECO:0000250|UniProtKB:Q65CX4};
DE EC=3.2.1.23;
GN Name=bglY; OrderedLocusNames=Aaci_2891;
OS Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 /
OS DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC 15652 / NCIMB 11725 /
OS NRRL B-14509 / 104-IA) (Bacillus acidocaldarius).
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=521098;
RN [1] {ECO:0000312|EMBL:ABI84370.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-8; 536-551 AND
RP 637-649, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 27009 / DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC
RC 15652 / NCIMB 11725 / NRRL B-14509 / 104-IA {ECO:0000312|EMBL:ABI84370.1};
RX PubMed=17914606; DOI=10.1007/s10529-007-9551-y;
RA Yuan T., Yang P., Wang Y., Meng K., Luo H., Zhang W., Wu N., Fan Y.,
RA Yao B.;
RT "Heterologous expression of a gene encoding a thermostable beta-
RT galactosidase from Alicyclobacillus acidocaldarius.";
RL Biotechnol. Lett. 30:343-348(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27009 / DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC
RC 15652 / NCIMB 11725 / NRRL B-14509 / 104-IA {ECO:0000312|EMBL:ACV59895.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Ovchinnikova G., Chertkov O., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Pukall R., Klenk H.-P., Eisen J.A.;
RT "The complete chromosome of Alicyclobacillus acidocaldarius subsp.
RT acidocaldarius DSM 446.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolyzes o-nitrophenyl-beta-D-galactopyranoside (ONPG) and
CC p-nitrophenyl-beta-D-fucopyranoside (PNPF), but not p-nitrophenyl-beta-
CC D-glucopyranoside (PNPG), p-nitrophenyl-beta-D-xylopyranoside (PNPX) or
CC p-nitrophenyl-beta-D-arabinopyranoside (PNPA). Also hydrolyzes lactose,
CC including lactose in milk. {ECO:0000269|PubMed:17914606}.
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:17914606};
CC -!- ACTIVITY REGULATION: Ca(2+), Mg(2+) and EDTA have little effect on
CC enzyme activity at 1-10 mM. Zn(2+) at 3, 5, 7 or 10 mM inhibits
CC activity by 20%, 30%, 40% and 65%, respectively.
CC {ECO:0000269|PubMed:17914606}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6 mM for ONPG (at 60 degrees Celsius and pH 6.0)
CC {ECO:0000269|PubMed:17914606};
CC KM=3.5 mM for PNPF (at 60 degrees Celsius and pH 6.0)
CC {ECO:0000269|PubMed:17914606};
CC pH dependence:
CC Optimum pH is 5.8. Approximately 80% of activity retained after
CC incubating the enzyme for 40 minutes in buffers ranging from pH 5.0
CC to pH 10.5. {ECO:0000269|PubMed:17914606};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius. Retains 90% of activity
CC when heated at 70 degrees Celsius for 30 minutes. Approximately 48%
CC of lactose in milk is hydrolyzed following treatment with enzyme at
CC 65 degrees Celsius over 60 minutes. {ECO:0000269|PubMed:17914606};
CC -!- BIOTECHNOLOGY: Has potential use in hydrolyzing lactose in neutral pH
CC dairy products such as whole milk or whey. Also could be used in milk
CC lactose hydrolysis during pasteurization at high temperatures.
CC {ECO:0000269|PubMed:17914606}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family. {ECO:0000255}.
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DR EMBL; DQ887754; ABI84370.1; -; Genomic_DNA.
DR EMBL; CP001727; ACV59895.1; -; Genomic_DNA.
DR RefSeq; WP_012812096.1; NC_013205.1.
DR AlphaFoldDB; C8WV58; -.
DR SMR; C8WV58; -.
DR STRING; 521098.Aaci_2891; -.
DR CAZy; GH42; Glycoside Hydrolase Family 42.
DR KEGG; aac:Aaci_2891; -.
DR eggNOG; COG1874; Bacteria.
DR HOGENOM; CLU_012430_1_1_9; -.
DR Proteomes; UP000001917; Chromosome.
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 1: Evidence at protein level;
KW Direct protein sequencing; Glycosidase; Hydrolase; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..688
FT /note="Beta-galactosidase BglY"
FT /id="PRO_0000407679"
FT ACT_SITE 157
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT ACT_SITE 313
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 321
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 361..364
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT CONFLICT 543..544
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 688 AA; 77869 MW; 686AFEA665822767 CRC64;
MAKHAPIFPN VQGFLHGGDY NPDQWLAYPD VLEQDVQLMR EAKWNVVSLG IFSWVSLEPE
EGLFTFEWLD EAIERLTHAG VRILLATPSG ARPAWLSAKY PEVLRVGPDG RRNRHGGRHN
HCYTSPIYRE KVRIINRKLA ERYAHHPGVI GWHVSNEYGG ECHCPLCQEA FREWLKRKYK
TLDALNHAWW TPFWSHTYTD WSQIESPMPH GETSIHGLNL DWKRFVTDQT VDFCRHEIEP
LKQVNPNLPV TTNFMGTYPG LNYWRFRDVL DVISWDSYPR WHAHETLVPE AVHTAMVHDL
NRSILKKPFL LMESTPSVTN WQAVSKQKRP GVHVLVSLQA VAHGADSVQY FQWRKSRGSY
EKFHGAVVDH VGHANTRVFR DVQAVGEMLE RLAPMAGAEV KADAAVIFDW ENRWALEDAK
GPRNIGMHYE ETVVNHYAAL WRMGVPMDVI DEEQPLDGYK LVVAPMLYMV RPGVAERMKA
FVERGGSLVL TYWSGIVDEN DLVFLGGFPG PLRELAGVWA EEIDALYDGE RVPVRVADGN
PLGLAGHYEA RELCEVVHLE GAEPIAVYGA DYYEGMPAAT VHRVGKGKVY YVAARLEDAF
LRDFFARVAA EAGVARAIER ELPDGVSAMV RSGDGVEYVM LMNFTPEARE VALDEAEYKP
LYGEAPTDGA VRLPAYGVSV LERPARNG
//
