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Beta-galactosidase GanA (Beta-gal) (EC 3.2.1.23) (Beta-1,4-galactooligomerase) (Galactooligomerase)

 BGAL2_BACLD             Reviewed;         673 AA.
Q65CX4; Q62NE9;
24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
24-MAR-2009, sequence version 2.
23-MAY-2018, entry version 88.
RecName: Full=Beta-galactosidase GanA;
Short=Beta-gal;
EC=3.2.1.23;
AltName: Full=Beta-1,4-galactooligomerase;
AltName: Full=Galactooligomerase;
Name=ganA; Synonyms=galO, lacA; OrderedLocusNames=BLi04277, BL00264;
Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / NBRC
12200 / NCIMB 9375 / NRRL NRS-1264 / Gibson 46).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=279010;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / NBRC 12200 / NCIMB 9375 / NRRL
NRS-1264 / Gibson 46;
PubMed=15383718; DOI=10.1159/000079829;
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H.,
Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R.,
Ehrenreich A., Gottschalk G.;
"The complete genome sequence of Bacillus licheniformis DSM13, an
organism with great industrial potential.";
J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / NBRC 12200 / NCIMB 9375 / NRRL
NRS-1264 / Gibson 46;
PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G.,
Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L.,
Larsen T.S., Sorokin A., Bolotin A., Lapidus A., Galleron N.,
Ehrlich S.D., Berka R.M.;
"Complete genome sequence of the industrial bacterium Bacillus
licheniformis and comparisons with closely related Bacillus species.";
Genome Biol. 5:R77.1-R77.12(2004).
[3]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME
REGULATION, SUBUNIT, AND BIOTECHNOLOGY.
PubMed=20852995; DOI=10.1007/s00253-010-2862-2;
Juajun O., Nguyen T.H., Maischberger T., Iqbal S., Haltrich D.,
Yamabhai M.;
"Cloning, purification, and characterization of beta-galactosidase
from Bacillus licheniformis DSM 13.";
Appl. Microbiol. Biotechnol. 89:645-654(2011).
-!- FUNCTION: Hydrolyzes oligosaccharides released by the endo-1,4-
beta-galactosidase GalA from arabinogalactan type I, a pectic
plant polysaccharide. It is unable to use lactose as a sole carbon
source (By similarity). Catalyzes the hydrolysis of lactose to its
constituent monosaccharides glucose and galactose. Possesses a low
level of transgalactosylation activity for the production of
galacto-oligosaccharides (GOS) from lactose. {ECO:0000250,
ECO:0000269|PubMed:20852995}.
-!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D-
galactose residues in beta-D-galactosides.
{ECO:0000269|PubMed:20852995}.
-!- ENZYME REGULATION: Inhibited by hydrolysis end products D-
galactose and D-glucose. The hydrolysis of o-nitrophenyl-beta-D-
galactopyranoside (ONPG) is slightly activated by monovalent ions,
Na(+) and K(+). Concentrations of these ions in the range of 1-100
mM exert the stimulating effects. The presence of 1 mM Mn(2+)
together with the presence of 10 mM Na(+) slightly stimulates the
activity, while presence of 10 mM Mn(2+) inhibits the activity by
about 40%. {ECO:0000269|PubMed:20852995}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=13.7 mM for ONPG (at 30 degrees Celsius and pH 6.5)
{ECO:0000269|PubMed:20852995};
KM=169 mM for lactose (at 30 degrees Celsius and pH 6.5)
{ECO:0000269|PubMed:20852995};
Vmax=299 umol/min/mg enzyme with ONPG as substrate (at 30
degrees Celsius and pH 6.5) {ECO:0000269|PubMed:20852995};
Vmax=13 umol/min/mg enzyme with lactose as substrate (at 30
degrees Celsius and pH 6.5) {ECO:0000269|PubMed:20852995};
pH dependence:
Optimum pH is 6.5 for both lactose and ONPG hydrolysis. Stable
at pH 5-8 and most stable at 6.5, retaining more than 90% and
80% of its activity when incubated at pH 6.5 and 37 degrees
Celsius for 5 days and 1 month, respectively.
{ECO:0000269|PubMed:20852995};
Temperature dependence:
Optimum temperature of the activity is 50 degrees Celsius when
using both lactose and ONPG as substrates under 10 minutes assay
conditions. Stable over a wide range of temperatures (4-42
degrees Celsius), and when kept at these temperatures up to 1
month. Most stable at 37 degrees Celsius, retaining 90% of its
activity after 1 month at this temperature. Half-life time of
activity of approximately 7 days, 5 hours, and 30 minutes at 55,
60 and 65 degrees Celsius, respectively. Approximately 45% of
lactose is hydrolyzed within the first 3 hours of the reaction
at 60 degrees Celsius, while about 20% is cleaved at 37 degrees
Celsius when employing initial lactose concentration of 50 g/l
at pH 6.5. For initial lactose concentrations of 200 and 50 g/l
and at temperature of 60 degrees Celsius, the maximum GOS yields
are approximately 12% and 7%, respectively. At the initial
lactose concentration of 200 g/l, the GOS yields obtained at 60
degrees Celsius are significantly higher than at 37 degrees
Celsius, with approximately 12% and 5% of total sugars,
respectively. {ECO:0000269|PubMed:20852995};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20852995}.
-!- BIOTECHNOLOGY: Has potential for partial lactose removal in food
products and improving the quality of dairy products by increasing
their solubility and sweetness. {ECO:0000269|PubMed:20852995}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family.
{ECO:0000305}.
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EMBL; CP000002; AAU25712.1; -; Genomic_DNA.
EMBL; AE017333; AAU43090.1; -; Genomic_DNA.
ProteinModelPortal; Q65CX4; -.
SMR; Q65CX4; -.
STRING; 279010.BLi04277; -.
CAZy; GH42; Glycoside Hydrolase Family 42.
PRIDE; Q65CX4; -.
EnsemblBacteria; AAU25712; AAU25712; BL00264.
EnsemblBacteria; AAU43090; AAU43090; BLi04277.
KEGG; bld:BLi04277; -.
KEGG; bli:BL00264; -.
eggNOG; COG1874; LUCA.
HOGENOM; HOG000117811; -.
KO; K12308; -.
Proteomes; UP000000606; Chromosome.
GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006012; P:galactose metabolic process; IEA:InterPro.
Gene3D; 2.60.40.1180; -; 1.
Gene3D; 3.40.50.880; -; 1.
InterPro; IPR013739; Beta_galactosidase_C.
InterPro; IPR013738; Beta_galactosidase_Trimer.
InterPro; IPR029062; Class_I_gatase-like.
InterPro; IPR003476; Glyco_hydro_42.
InterPro; IPR013529; Glyco_hydro_42_N.
InterPro; IPR013780; Glyco_hydro_b.
InterPro; IPR017853; Glycoside_hydrolase_SF.
PANTHER; PTHR36447; PTHR36447; 1.
Pfam; PF02449; Glyco_hydro_42; 1.
Pfam; PF08533; Glyco_hydro_42C; 1.
Pfam; PF08532; Glyco_hydro_42M; 1.
PIRSF; PIRSF001084; B-galactosidase; 1.
SUPFAM; SSF51445; SSF51445; 1.
SUPFAM; SSF52317; SSF52317; 1.
1: Evidence at protein level;
Complete proteome; Glycosidase; Hydrolase; Metal-binding;
Reference proteome; Zinc.
CHAIN 1 673 Beta-galactosidase GanA.
/FTId=PRO_0000367027.
REGION 356 359 Substrate binding. {ECO:0000250}.
ACT_SITE 144 144 Proton donor. {ECO:0000250}.
ACT_SITE 308 308 Nucleophile. {ECO:0000250}.
METAL 109 109 Zinc. {ECO:0000250}.
METAL 149 149 Zinc. {ECO:0000250}.
METAL 151 151 Zinc. {ECO:0000250}.
METAL 154 154 Zinc. {ECO:0000250}.
BINDING 105 105 Substrate. {ECO:0000250}.
BINDING 143 143 Substrate. {ECO:0000250}.
BINDING 316 316 Substrate. {ECO:0000250}.
SEQUENCE 673 AA; 77497 MW; D21163244C361A34 CRC64;
MLHGGDYNPD QWLDRPDILA DDIKLMKLAH TNTFSVGIFS WSALEPEEGV YTFEWLDDIF
ESIHRNGGRI ILATPSGARP AWLSQKYPEV LRVNAERVKQ LHGGRHNHCF TSYVYREKTK
EINRMLAERY GSQHALLMWH VSNEYGGECH CDQCQHAFRD WLKKKYNHDI KSLNDAWWTP
FWSHTFNDWS QIESPSPIGE NAVHGLNLDW RRFVTDQTIS FFQNEIVPLK EITPNIPITT
NFMADTHDLI PFQGLDYSKF AKHLDVISWD AYPAWHNDWE STADLAMKVG FINDLYRSLK
QQPFLLMEST PSAVNWHDFN KAKRPGMHLL SSVQMIAHGS DSILYFQWRK SRGSSEKFHG
AVVGHDNCSE NRVFKEVAKV GQTLEALSEV TGTIRPADVA ILYDWENHWA LQDAQGFGMK
TKRYPQTLHE HYRAFWERDI PVDVITKEQD FSSYRLLIVP MLYLASEETI ARLKAFAANG
GTLVMTYISG IVNESDLTYL GGWPKDLQEM FGMEPVETDT LYPGDKNAVR YQNRSYELKD
YATVLKLSTA DPEGFYEDDF YADTTAVTSH PYKQGKTYYI GARLSSQFHR DFYGTLIKEL
AIQPALDVKH QPGVSVQVRQ DEENDYIFIM NFTEKRQPVV LASAVKDMLT GETLAGEVTL
EKYEARIAVK AKE


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