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Database: UniProt/SWISS-PROT
Entry: BGAL_ALIAD
LinkDB: BGAL_ALIAD
Original site: BGAL_ALIAD 
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
//
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