Q65CX4 (BGAL2_BACLD) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-galactosidase ganA
Short name=Beta-gal
EC=3.2.1.23

Alternative name(s):
Beta-1,4-galactooligomerase
Galactooligomerase

Gene names

Name:	ganA
Synonyms:	galO, lacA
Ordered Locus Names:	BLi04277, BL00264

Organism

Bacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]

Taxonomic identifier

279010 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	673 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.3
Catalytic activity	Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. Ref.3
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 Mn2+ together with the presence of 10 mM Na+ slightly stimulates the activity, while presence of 10 mM Mn2+ inhibits the activity by about 40%. Ref.3
Subunit structure	Homodimer. Ref.3
Biotechnological use	Has potential for partial lactose removal in food products and improving the quality of dairy products by increasing their solubility and sweetness. Ref.3
Sequence similarities	Belongs to the glycosyl hydrolase 42 family.
Biophysicochemical properties	Kinetic parameters: KM=13.7 mM for ONPG (at 30 degrees Celsius and pH 6.5) Ref.3 KM=169 mM for lactose (at 30 degrees Celsius and pH 6.5) Vmax=299 µmol/min/mg enzyme with ONPG as substrate (at 30 degrees Celsius and pH 6.5) Vmax=13 µmol/min/mg enzyme with lactose as substrate (at 30 degrees Celsius and pH 6.5) 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. 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.

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	beta-galactosidase complex Inferred from electronic annotation. Source: InterPro
Molecular function	beta-galactosidase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 673	673	Beta-galactosidase ganA		PRO_0000367027
Regions
	Region	356 – 359	4	Substrate binding By similarity
Sites
	Active site	144	1	Proton donor By similarity
	Active site	308	1	Nucleophile By similarity
	Metal binding	109	1	Zinc By similarity
	Metal binding	149	1	Zinc By similarity
	Metal binding	151	1	Zinc By similarity
	Metal binding	154	1	Zinc By similarity
	Binding site	105	1	Substrate By similarity
	Binding site	143	1	Substrate By similarity
	Binding site	316	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q65CX4 [UniParc]. Last modified March 24, 2009. Version 2. Checksum: D21163244C361A34	FASTA	673	77,497
	10 20 30 40 50 60 MLHGGDYNPD QWLDRPDILA DDIKLMKLAH TNTFSVGIFS WSALEPEEGV YTFEWLDDIF 70 80 90 100 110 120 ESIHRNGGRI ILATPSGARP AWLSQKYPEV LRVNAERVKQ LHGGRHNHCF TSYVYREKTK 130 140 150 160 170 180 EINRMLAERY GSQHALLMWH VSNEYGGECH CDQCQHAFRD WLKKKYNHDI KSLNDAWWTP 190 200 210 220 230 240 FWSHTFNDWS QIESPSPIGE NAVHGLNLDW RRFVTDQTIS FFQNEIVPLK EITPNIPITT 250 260 270 280 290 300 NFMADTHDLI PFQGLDYSKF AKHLDVISWD AYPAWHNDWE STADLAMKVG FINDLYRSLK 310 320 330 340 350 360 QQPFLLMEST PSAVNWHDFN KAKRPGMHLL SSVQMIAHGS DSILYFQWRK SRGSSEKFHG 370 380 390 400 410 420 AVVGHDNCSE NRVFKEVAKV GQTLEALSEV TGTIRPADVA ILYDWENHWA LQDAQGFGMK 430 440 450 460 470 480 TKRYPQTLHE HYRAFWERDI PVDVITKEQD FSSYRLLIVP MLYLASEETI ARLKAFAANG 490 500 510 520 530 540 GTLVMTYISG IVNESDLTYL GGWPKDLQEM FGMEPVETDT LYPGDKNAVR YQNRSYELKD 550 560 570 580 590 600 YATVLKLSTA DPEGFYEDDF YADTTAVTSH PYKQGKTYYI GARLSSQFHR DFYGTLIKEL 610 620 630 640 650 660 AIQPALDVKH QPGVSVQVRQ DEENDYIFIM NFTEKRQPVV LASAVKDMLT GETLAGEVTL 670 EKYEARIAVK AKE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential." 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. J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580.
[2]	"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species." 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. Genome Biol. 5:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580.
[3]	"Cloning, purification, and characterization of beta-galactosidase from Bacillus licheniformis DSM 13." Juajun O., Nguyen T.H., Maischberger T., Iqbal S., Haltrich D., Yamabhai M. Appl. Microbiol. Biotechnol. 89:645-654(2011) [PubMed: 20852995] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT, BIOTECHNOLOGY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000002 Genomic DNA. Translation: AAU25712.1. AE017333 Genomic DNA. Translation: AAU43090.1.
RefSeq	YP_081350.1. NC_006270.3. YP_093783.1. NC_006322.1.
3D structure databases
ProteinModelPortal	Q65CX4.
ModBase	Search...
Protein-protein interaction databases
STRING	Q65CX4.
Protein family/group databases
CAZy	GH42. Glycoside Hydrolase Family 42.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000055485; EBBACP00000054016; EBBACG00000055476. EBBACT00000062095; EBBACP00000060528; EBBACG00000062086.
GeneID	3029925. 3098321.
GenomeReviews	Gene locus BLi04277 in contig AE017333_GR. Gene locus BL00264 in contig CP000002_GR.
KEGG	bld:BLi04277. bli:BL00264.
NMPDR	fig|279010.5.peg.3516.
PATRIC	18954384. VBIBacLic203714_4367.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1874.
GeneTree	EBGT00050000006111.
HOGENOM	HBG476453.
OMA	AKRPGMH.
ProtClustDB	CLSK537148.
Enzyme and pathway databases
BioCyc	BLIC279010-1:BLI04277-MONOMER. BLIC279010:BL00264-MONOMER.
Family and domain databases
InterPro	IPR013739. Beta_galactosidase_C. IPR013738. Beta_galactosidase_Trimer. IPR013780. Glyco_hydro_13_b. IPR003476. Glyco_hydro_42. IPR013529. Glyco_hydro_42_N. IPR013781. Glyco_hydro_subgr_catalytic. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Gene3D	G3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
KO	K12308.
Pfam	PF02449. Glyco_hydro_42. 1 hit. PF08533. Glyco_hydro_42C. 1 hit. PF08532. Glyco_hydro_42M. 1 hit. [Graphical view]
PIRSF	PIRSF001084. B-galactosidase. 1 hit.
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...

Entry information

Entry name

BGAL2_BACLD

Accession

Primary (citable) accession number: Q65CX4
Secondary accession number(s): Q62NE9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	March 24, 2009
Last modified:	January 25, 2012
This is version 57 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program