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O07012 (BGAL2_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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, yvfN
Ordered Locus Names:BSU34130
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length672 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Maximal activity with o-nitrophenyl-beta-D-galactopyranoside (ONPG) and p-nitrophenyl-beta-D-galactopyranoside (PNPG) as substrates, trace activity with p-nitrophenyl-alpha-L-arabinopyranoside and o-nitrophenyl-beta-D-fucopyranoside as substrates, but no activity with p-nitrophenyl-alpha-D-galactopyranoside, p-nitrophenyl-beta-D-glucopyranoside, o-nitrophenyl-beta-D-xylopyranoside, p-nitrophenyl-beta-D-mannopyranoside or p-nitrophenyl-alpha-L-arabinofuranoside as substrates. 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

Disruption phenotype

No chromogen 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-Gal) hydrolyzation. Reduces beta-galactosidase activity observed with polygalacturonic acid, citrus and apple pectins, galactan and soy flour. Ref.3

Sequence similarities

Belongs to the glycosyl hydrolase 42 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 6-0-6.5. Ref.3

Temperature dependence:

Optimum temperature is 50 degrees Celsius. Thermolabile above 50 degrees Celsius.

Sequence caution

The sequence CAB08008.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAB15418.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   LigandMetal-binding
Zinc
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processgalactose metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentbeta-galactosidase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionbeta-galactosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 672672Beta-galactosidase GanA
PRO_0000367026

Regions

Region356 – 3594Substrate binding By similarity

Sites

Active site1441Proton donor Potential
Active site3081Nucleophile Potential
Metal binding1091Zinc By similarity
Metal binding1491Zinc By similarity
Metal binding1511Zinc By similarity
Metal binding1541Zinc By similarity
Binding site1051Substrate By similarity
Binding site1431Substrate By similarity
Binding site3161Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
O07012 [UniParc].

Last modified March 24, 2009. Version 2.
Checksum: 324242C5D45E35BD

FASTA67277,499
        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 

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NOMENCLATURE, FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISRUPTION PHENOTYPE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z94043 Genomic DNA. Translation: CAB08008.1. Different initiation.
AL009126 Genomic DNA. Translation: CAB15418.1. Different initiation.
PIRB69649.
RefSeqNP_391293.1. NC_000964.3.

3D structure databases

ProteinModelPortalO07012.
SMRO07012. Positions 2-670.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU34130.

Protein family/group databases

CAZyGH42. Glycoside Hydrolase Family 42.

Proteomic databases

PaxDbO07012.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15418; CAB15418; BSU34130.
GeneID936313.
KEGGbsu:BSU34130.
PATRIC18978828. VBIBacSub10457_3577.

Organism-specific databases

GenoListBSU34130. [Micado]

Phylogenomic databases

eggNOGCOG1874.
HOGENOMHOG000117811.
KOK12308.
OrthoDBEOG6GTZGG.
ProtClustDBCLSK537148.

Enzyme and pathway databases

BioCycBSUB:BSU34130-MONOMER.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR013739. Beta_galactosidase_C.
IPR013738. Beta_galactosidase_Trimer.
IPR003476. Glyco_hydro_42.
IPR013529. Glyco_hydro_42_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF02449. Glyco_hydro_42. 1 hit.
PF08533. Glyco_hydro_42C. 1 hit.
PF08532. Glyco_hydro_42M. 1 hit.
[Graphical view]
PIRSFPIRSF001084. B-galactosidase. 1 hit.
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameBGAL2_BACSU
AccessionPrimary (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: November 13, 2013
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList