Reviewed, UniProtKB/Swiss-Prot O07012 (BGAL2_BACSU)

Names and origin

Protein names

Recommended name:
    Beta-galactosidase galO
      Short name=Beta-gal
    EC=3.2.1.23
Alternative name(s):
    Beta-1,4-galactooligomerase
    Galactooligomerase

Gene names

Name:	galO
Synonyms:	lacA, yvfN
Ordered Locus Names:	BSU34130

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	672 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. Ref.3
Catalytic activity	Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.
Enzyme regulation	Inhibited by zinc, cobalt and copper ions. Ref.3
Subunit structure	Homotrimer. Ref.3
Sequence similarities	Belongs to the glycosyl hydrolase 42 family.
biophysicochemical properties	pH dependence: Optimum pH is 6-0-6.5. Temperature dependence: Optimum temperature is 50 degrees Celsius. Thermolabile above 50 degrees Celsius.

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
Molecular function	beta-galactosidase activity Inferred from electronic annotation. Source: EC zinc 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 – 672	672	Beta-galactosidase galO		PRO_0000367026
Regions
	Region	356 – 359	4	Substrate binding By similarity
Sites
	Active site	144	1	Proton donor Potential
	Active site	308	1	Nucleophile Potential
	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)
	O07012-1 [UniParc]. Last modified March 24, 2009. Version 2. Checksum: 324242C5D45E35BD	FASTA	672	77,499
	10 20 30 40 50 60 MLHGGDYNPD QWLDRPDILA DDIKLMKLSH TNTFSVGIFA WSALEPEEGV YQFEWLDDIF 70 80 90 100 110 120 ERIHSIGGRV ILATPSGARP AWLSQTYPEV LRVNASRVKQ LHGGRHNHCL TSKVYREKTR 130 140 150 160 170 180 HINRLLAERY GHHPALLMWH ISNEYGGDCH CDLCQHAFRE WLKSKYDNSL KTLNHAWWTP 190 200 210 220 230 240 FWSHTFNDWS QIESPSPIGE NGLHGLNLDW RRFVTDQTIS FYENEIIPLK ELTPDIPITT 250 260 270 280 290 300 NFMADTPDLI PYQGLDYSKF AKHVDAISWD AYPVWHNDWE STADLAMKVG FINDLYRSLK 310 320 330 340 350 360 QQPFLLMECT PSAVNWHNVN KAKRPGMNLL SSMQMIAHGS DSVLYFQYRK SRGSSEKLHG 370 380 390 400 410 420 AVVDHDNSPK NRVFQEVAKV GETLERLSEV VGTKRPAQTA ILYDWENHWA LEDAQGFAKA 430 440 450 460 470 480 TKRYPQTLQQ HYRTFWEHDI PVDVITKEQD FSPYKLLIVP MLYLISEDTV SRLKAFTADG 490 500 510 520 530 540 GTLVMTYISG VVNEHDLTYT GGWHPDLQAI FGVEPLETDT LYPKDRNAVS YRSQIYEMKD 550 560 570 580 590 600 YATVIDVKTA SVEAVYQEDF YARTPAVTSH EYQQGKAYFI GARLEDQFQR DFYEGLITDL 610 620 630 640 650 660 SLSPVFPVRH GKGVSVQARQ DQDNDYIFVM NFTEEKQLVT FDQSVKDIMT GDILSGDLTM 670 EKYEVRIVVN TH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of the lacA gene encoding beta-galactosidase in Bacillus subtilis and a regulator gene, lacR." Daniel R.A., Haiech J., Denizot F., Errington J. J. Bacteriol. 179:5636-5638(1997) [PubMed: 9287030] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"Bioinformatic, genetic, and biochemical evidence that some glycoside hydrolase family 42 beta-galactosidases are arabinogalactan type I oligomer hydrolases." Shipkowski S., Brenchley J.E. Appl. Environ. Microbiol. 72:7730-7738(2006) [PubMed: 17056685] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, NOMENCLATURE, ENZYME REGULATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z94043 Genomic DNA. Translation: CAB08008.1. Different initiation. AL009126 Genomic DNA. Translation: CAB15418.1. Different initiation.
PIR	B69649.
RefSeq	NP_391293.1.
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GH42. Glycoside Hydrolase Family 42.
Genome annotation databases
GeneID	936313.
GenomeReviews	Gene locus BSU34130 in contig AL009126_GR.
KEGG	bsu:BSU34130.
NMPDR	fig|224308.1.peg.3419.
Organism-specific databases
SubtiList	BG12439. galO. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	O07012.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU3410-MON.
Family and domain databases
InterPro	IPR013739. Beta_Galactosidase_C. IPR013738. Beta_Galactosidase_Trimer. IPR003476. Glyco_hydro_42. IPR013529. Glyco_hydro_42_N. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
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.
ProtoNet	Search...

Entry information

Entry name

BGAL2_BACSU

Accession

Primary (citable) accession number: O07012
Secondary accession number(s): Q795J9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	March 24, 2009
Last modified:	June 16, 2009
This is version 56 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)