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O07012

- BGAL2_BACSU

UniProt

O07012 - BGAL2_BACSU

Protein

Beta-galactosidase GanA

Gene

ganA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 2 (24 Mar 2009)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Catalytic activityi

    Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.

    Enzyme regulationi

    Inhibited by zinc, cobalt and copper ions.1 Publication

    pH dependencei

    Optimum pH is 6-0-6.5.1 Publication

    Temperature dependencei

    Optimum temperature is 50 degrees Celsius. Thermolabile above 50 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei105 – 1051SubstrateBy similarity
    Metal bindingi109 – 1091ZincBy similarity
    Binding sitei143 – 1431SubstrateBy similarity
    Active sitei144 – 1441Proton donorSequence Analysis
    Metal bindingi149 – 1491ZincBy similarity
    Metal bindingi151 – 1511ZincBy similarity
    Metal bindingi154 – 1541ZincBy similarity
    Active sitei308 – 3081NucleophileSequence Analysis
    Binding sitei316 – 3161SubstrateBy similarity

    GO - Molecular functioni

    1. beta-galactosidase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. galactose metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciBSUB:BSU34130-MONOMER.

    Protein family/group databases

    CAZyiGH42. Glycoside Hydrolase Family 42.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-galactosidase GanA (EC:3.2.1.23)
    Short name:
    Beta-gal
    Alternative name(s):
    Beta-1,4-galactooligomerase
    Galactooligomerase
    Gene namesi
    Name:ganA
    Synonyms:galO, lacA, yvfN
    Ordered Locus Names:BSU34130
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU34130. [Micado]

    Subcellular locationi

    GO - Cellular componenti

    1. beta-galactosidase complex Source: InterPro

    Pathology & Biotechi

    Disruption phenotypei

    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.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 672672Beta-galactosidase GanAPRO_0000367026Add
    BLAST

    Proteomic databases

    PaxDbiO07012.

    Interactioni

    Subunit structurei

    Homotrimer.1 Publication

    Protein-protein interaction databases

    STRINGi224308.BSU34130.

    Structurei

    3D structure databases

    ProteinModelPortaliO07012.
    SMRiO07012. Positions 2-670.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni356 – 3594Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 42 family.Curated

    Phylogenomic databases

    eggNOGiCOG1874.
    HOGENOMiHOG000117811.
    KOiK12308.
    OrthoDBiEOG6GTZGG.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    3.40.50.880. 1 hit.
    InterProiIPR013739. Beta_galactosidase_C.
    IPR013738. Beta_galactosidase_Trimer.
    IPR029062. Class_I_gatase-like.
    IPR003476. Glyco_hydro_42.
    IPR013529. Glyco_hydro_42_N.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF02449. Glyco_hydro_42. 1 hit.
    PF08533. Glyco_hydro_42C. 1 hit.
    PF08532. Glyco_hydro_42M. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001084. B-galactosidase. 1 hit.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF52317. SSF52317. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O07012-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLHGGDYNPD QWLDRPDILA DDIKLMKLSH TNTFSVGIFA WSALEPEEGV    50
    YQFEWLDDIF ERIHSIGGRV ILATPSGARP AWLSQTYPEV LRVNASRVKQ 100
    LHGGRHNHCL TSKVYREKTR HINRLLAERY GHHPALLMWH ISNEYGGDCH 150
    CDLCQHAFRE WLKSKYDNSL KTLNHAWWTP FWSHTFNDWS QIESPSPIGE 200
    NGLHGLNLDW RRFVTDQTIS FYENEIIPLK ELTPDIPITT NFMADTPDLI 250
    PYQGLDYSKF AKHVDAISWD AYPVWHNDWE STADLAMKVG FINDLYRSLK 300
    QQPFLLMECT PSAVNWHNVN KAKRPGMNLL SSMQMIAHGS DSVLYFQYRK 350
    SRGSSEKLHG AVVDHDNSPK NRVFQEVAKV GETLERLSEV VGTKRPAQTA 400
    ILYDWENHWA LEDAQGFAKA TKRYPQTLQQ HYRTFWEHDI PVDVITKEQD 450
    FSPYKLLIVP MLYLISEDTV SRLKAFTADG GTLVMTYISG VVNEHDLTYT 500
    GGWHPDLQAI FGVEPLETDT LYPKDRNAVS YRSQIYEMKD YATVIDVKTA 550
    SVEAVYQEDF YARTPAVTSH EYQQGKAYFI GARLEDQFQR DFYEGLITDL 600
    SLSPVFPVRH GKGVSVQARQ DQDNDYIFVM NFTEEKQLVT FDQSVKDIMT 650
    GDILSGDLTM EKYEVRIVVN TH 672
    Length:672
    Mass (Da):77,499
    Last modified:March 24, 2009 - v2
    Checksum:i324242C5D45E35BD
    GO

    Sequence cautioni

    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.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z94043 Genomic DNA. Translation: CAB08008.1. Different initiation.
    AL009126 Genomic DNA. Translation: CAB15418.1. Different initiation.
    PIRiB69649.
    RefSeqiNP_391293.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB15418; CAB15418; BSU34130.
    GeneIDi936313.
    KEGGibsu:BSU34130.
    PATRICi18978828. VBIBacSub10457_3577.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z94043 Genomic DNA. Translation: CAB08008.1 . Different initiation.
    AL009126 Genomic DNA. Translation: CAB15418.1 . Different initiation.
    PIRi B69649.
    RefSeqi NP_391293.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali O07012.
    SMRi O07012. Positions 2-670.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU34130.

    Protein family/group databases

    CAZyi GH42. Glycoside Hydrolase Family 42.

    Proteomic databases

    PaxDbi O07012.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB15418 ; CAB15418 ; BSU34130 .
    GeneIDi 936313.
    KEGGi bsu:BSU34130.
    PATRICi 18978828. VBIBacSub10457_3577.

    Organism-specific databases

    GenoListi BSU34130. [Micado ]

    Phylogenomic databases

    eggNOGi COG1874.
    HOGENOMi HOG000117811.
    KOi K12308.
    OrthoDBi EOG6GTZGG.

    Enzyme and pathway databases

    BioCyci BSUB:BSU34130-MONOMER.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    3.40.50.880. 1 hit.
    InterProi IPR013739. Beta_galactosidase_C.
    IPR013738. Beta_galactosidase_Trimer.
    IPR029062. Class_I_gatase-like.
    IPR003476. Glyco_hydro_42.
    IPR013529. Glyco_hydro_42_N.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF02449. Glyco_hydro_42. 1 hit.
    PF08533. Glyco_hydro_42C. 1 hit.
    PF08532. Glyco_hydro_42M. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001084. B-galactosidase. 1 hit.
    SUPFAMi SSF51445. SSF51445. 1 hit.
    SSF52317. SSF52317. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiBGAL2_BACSU
    AccessioniPrimary (citable) accession number: O07012
    Secondary accession number(s): Q795J9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: March 24, 2009
    Last modified: October 1, 2014
    This is version 90 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3