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P19668

- BGAL_GEOKU

UniProt

P19668 - BGAL_GEOKU

Protein

Beta-galactosidase bgaB

Gene

bgaB

Organism
Geobacillus kaustophilus
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      Previous versions | rss
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    Functioni

    Hydrolyzes 6-bromo-2-naphthyl-beta-D-galactopyranoside and o-nitrophenyl-beta-D-galactopyranoside (ONPG). Possesses a high level of transgalactosylation activity. Hydrolyzes lactose in milk.1 Publication

    Catalytic activityi

    Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.2 Publications

    Enzyme regulationi

    By divalent metal ions. Fe2+, Zn2+, Cu2+, Pb2+ and Sn2+ inhibit 52, 76.6, 85.3, 100 and 100% of the enzyme activity, respectively. Other metal cations and EDTA do not inhibit this enzyme. Thiol reagents 2-mercaptoethanol and dithiothreitol have no effect on the activity. Sulfhydryl group-blocking reagents p-chloromercuribenzoic acid and iodoacetic acid inhibit 86.2 and 74% of the enzyme activity, respectively.1 Publication

    Kineticsi

    1. KM=2.96 mM for ONPG (at 55 degrees Celsius and pH 7.0)2 Publications

    Vmax=6.62 µmol/min/mg enzyme with ONPG as substrate (at 55 degrees Celsius and pH 7.0)2 Publications

    pH dependencei

    Optimum pH is 7.0. Retains more than 80% of the activity at a pH range of 6.0-7.5.2 Publications

    Temperature dependencei

    Optimum temperature for the activity is 70 degrees Celsius using ONPG as substrate. Stable up to 70 degrees Celsius (PubMed:3086288). Retains 80% of the activity at 75 degrees Celsius (PubMed:18420605). Kinetics of thermal inactivation and half-life times at 60, 65 and 70 degrees Celsius are 120, 50 and 9 hours, respectively.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei109 – 1091SubstrateBy similarity
    Metal bindingi113 – 1131ZincBy similarity
    Binding sitei147 – 1471SubstrateBy similarity
    Active sitei148 – 1481Proton donorBy similarity
    Metal bindingi156 – 1561ZincBy similarity
    Metal bindingi158 – 1581ZincBy similarity
    Metal bindingi161 – 1611ZincBy similarity
    Active sitei303 – 3031NucleophileBy similarity
    Binding sitei311 – 3111SubstrateBy 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

    Protein family/group databases

    CAZyiGH42. Glycoside Hydrolase Family 42.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-galactosidase bgaB (EC:3.2.1.23)
    Short name:
    Beta-gal
    Alternative name(s):
    Beta-galactosidase I
    Lactase
    Gene namesi
    Name:bgaB
    OrganismiGeobacillus kaustophilus
    Taxonomic identifieri1462 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

    Subcellular locationi

    GO - Cellular componenti

    1. beta-galactosidase complex Source: InterPro

    Pathology & Biotechi

    Biotechnological usei

    Has potential for enzyme application in low-lactose milk production during milk pasteurization.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 672672Beta-galactosidase bgaBPRO_0000057691Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP19668.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni351 – 3544Substrate binding

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 42 family.Curated

    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.

    P19668-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNVLSSICYG GDYNPEQWPE EIWYEDAKLM QKAGVNLVSL GIFSWSKIEP    50
    SDGVFDFEWL DKVIDILYDH GVYINLGTAT ATTPAWFVKK YPDSLPIDES 100
    GVILSFGSRQ HYCPNHPQLI THIKRLVRAI AERYKNHPAL KMWHVNNEYA 150
    CHVSKCFCEN CAVAFRKWLK ERYKTIDELN ERWGTNFWGQ RYNHWDEINP 200
    PRKAPTFINP SQELDYYRFM NDSILKLFLT EKEILREVTP DIPVSTNFMG 250
    SFKPLNYFQW AQHVDIVTWD SYPDPREGLP IQHAMMNDLM RSLRKGQPFI 300
    LMEQVTSHVN WRDINVPKPP GVMRLWSYAT IARGADGIMF FQWRQSRAGA 350
    EKFHGAMVPH FLNENNRIYR EVTQLGQELK KLDCLVGSRI KAEVAIIFDW 400
    ENWWAVELSS KPHNKLRYIP IVEAYYRELY KRNIAVDFVR PSDDLTKYKV 450
    VIAPMLYMVK EGEDENLRQF VANGGTLIVS FFSGIVDEND RVHLGGYPGP 500
    LRDILGIFVE EFVPYPETKV NKIYSNDGEY DCTTWADIIR LEGAEPLATF 550
    KGDWYAGLPA VTRNCYGKGE GIYVGTYPDS NYLGRLLEQV FAKHHINPIL 600
    EVAENVEVQQ RETDEWKYLI IINHNDYEVT LSLPEDKIYQ NMIDGKCFRG 650
    GELRIQGVDV AVLREHDEAG KV 672
    Length:672
    Mass (Da):78,053
    Last modified:February 1, 1991 - v1
    Checksum:iFF611FFBEF68F09A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13466 Genomic DNA. Translation: AAA22262.1.
    PIRiA29836.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13466 Genomic DNA. Translation: AAA22262.1 .
    PIRi A29836.

    3D structure databases

    ProteinModelPortali P19668.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH42. Glycoside Hydrolase Family 42.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "Structure of a beta-galactosidase gene of Bacillus stearothermophilus."
      Hirata H., Fukazawa T., Negoro S., Okada H.
      J. Bacteriol. 166:722-727(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: ATCC 8005 / DSM 7263 / JCM 20319 / NCIMB 8547 / NRRL NRS-81 / IAM 11001.
    2. "Molecular basis of isozyme formation of beta-galactosidases in Bacillus stearothermophilus: isolation of two beta-galactosidase genes, bgaA and bgaB."
      Hirata H., Negoro S., Okada H.
      J. Bacteriol. 160:9-14(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY.
      Strain: ATCC 8005 / DSM 7263 / JCM 20319 / NCIMB 8547 / NRRL NRS-81 / IAM 11001.
    3. "Production, purification, and characterization of a potential thermostable galactosidase for milk lactose hydrolysis from Bacillus stearothermophilus."
      Chen W., Chen H., Xia Y., Zhao J., Tian F., Zhang H.
      J. Dairy Sci. 91:1751-1758(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, BIOTECHNOLOGY.
      Strain: ATCC 8005 / DSM 7263 / JCM 20319 / NCIMB 8547 / NRRL NRS-81 / IAM 11001.

    Entry informationi

    Entry nameiBGAL_GEOKU
    AccessioniPrimary (citable) accession number: P19668
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 75 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3