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 28-FEB-2018, entry version 46.
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
OS 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 /
OS 104-1A) (Bacillus acidocaldarius).
OC Bacteria; Firmicutes; 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
RP AND 637-649, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 /
RC NRRL B-14509 / 104-1A {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 / JCM 5260 / NBRC 15652 / NCIMB 11725 /
RC NRRL B-14509 / 104-1A {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.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA Ivanova N., Ovchinnikova G., Chertkov O., Sims D., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R., Klenk H.-P.,
RA 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)
CC and p-nitrophenyl-beta-D-fucopyranoside (PNPF), but not p-
CC nitrophenyl-beta-D-glucopyranoside (PNPG), p-nitrophenyl-beta-D-
CC xylopyranoside (PNPX) or p-nitrophenyl-beta-D-arabinopyranoside
CC (PNPA). Also hydrolyzes lactose, including lactose in milk.
CC {ECO:0000269|PubMed:17914606}.
CC -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D-
CC galactose residues in beta-D-galactosides.
CC {ECO:0000269|PubMed:17914606}.
CC -!- ENZYME 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
CC 5.0 to pH 10.5. {ECO:0000269|PubMed:17914606};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius. Retains 90% of
CC activity when heated at 70 degrees Celsius for 30 minutes.
CC Approximately 48% of lactose in milk is hydrolyzed following
CC treatment with enzyme at 65 degrees Celsius over 60 minutes.
CC {ECO:0000269|PubMed:17914606};
CC -!- BIOTECHNOLOGY: Has potential use in hydrolyzing lactose in neutral
CC pH dairy products such as whole milk or whey. Also could be used
CC in milk lactose hydrolysis during pasteurization at high
CC temperatures. {ECO:0000269|PubMed:17914606}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family.
CC {ECO:0000255}.
DR EMBL; DQ887754; ABI84370.1; -; Genomic_DNA.
DR EMBL; CP001727; ACV59895.1; -; Genomic_DNA.
DR RefSeq; WP_012812096.1; NC_013205.1.
DR ProteinModelPortal; C8WV58; -.
DR SMR; C8WV58; -.
DR STRING; 521098.Aaci_2891; -.
DR CAZy; GH42; Glycoside Hydrolase Family 42.
DR EnsemblBacteria; ACV59895; ACV59895; Aaci_2891.
DR KEGG; aac:Aaci_2891; -.
DR eggNOG; ENOG4105C4C; Bacteria.
DR eggNOG; COG1874; LUCA.
DR HOGENOM; HOG000117811; -.
DR KO; K12308; -.
DR OMA; MLHGADY; -.
DR OrthoDB; POG091H0719; -.
DR BioCyc; AACI521098:G1GFZ-2928-MONOMER; -.
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 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 Complete proteome; Direct protein sequencing; Glycosidase; Hydrolase;
KW Metal-binding; Reference proteome; Zinc.
FT CHAIN 1 688 Beta-galactosidase BglY.
FT /FTId=PRO_0000407679.
FT REGION 361 364 Substrate binding.
FT {ECO:0000250|UniProtKB:O69315}.
FT ACT_SITE 157 157 Proton donor.
FT {ECO:0000250|UniProtKB:O69315}.
FT ACT_SITE 313 313 Nucleophile.
FT {ECO:0000250|UniProtKB:O69315}.
FT METAL 122 122 Zinc. {ECO:0000250|UniProtKB:O69315}.
FT METAL 162 162 Zinc. {ECO:0000250|UniProtKB:O69315}.
FT METAL 164 164 Zinc. {ECO:0000250|UniProtKB:O69315}.
FT METAL 167 167 Zinc. {ECO:0000250|UniProtKB:O69315}.
FT BINDING 118 118 Substrate.
FT {ECO:0000250|UniProtKB:O69315}.
FT BINDING 156 156 Substrate.
FT {ECO:0000250|UniProtKB:O69315}.
FT BINDING 321 321 Substrate.
FT {ECO:0000250|UniProtKB:O69315}.
FT CONFLICT 543 544 Missing (in Ref. 1; AA sequence).
FT {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
//
