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Q9KI47

- BGAL_PLASS

UniProt

Q9KI47 - BGAL_PLASS

Protein

Beta-galactosidase BgaA

Gene

bgaA

Organism
Planococcus sp. (strain 'SOS Orange')
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 48 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Hydrolyzes o-nitrophenyl-beta-D-galactopyranoside (ONPG), p-nitrophenyl-beta-D-galactopyranoside (PNPG), 5-bromo-4-chloro-3-indoyl-beta-D-galactosde (X-gal), o-nitrophenyl-beta-D-fucopyranoside (ONPF) and p-nitrophenyl-beta-D-fucopyranoside (PNPF) with greatest activity towards ONPG and PNPG and low levels of activity with ONPF and PNPF. Detectable, but very low levels of activity towards p-nitrophenyl-beta-lactose (PNPL), p-nitrophenyl-beta-cellobiose (PNPC), p-nitrophenyl-alpha-galactopyranoside (PNP-alpha-G), and p-nitrophenyl-beta-xylopyranoside (PNPX).1 Publication

    Catalytic activityi

    Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.1 Publication

    Enzyme regulationi

    No activity is lost during treatment with 20 or 100 mM EDTA in Z buffer for 3 hours at 0 degrees Celsius, nor is activity greatly stimulated by the addition of cations. Inhibited by 1 mM zinc and 1 mM copper, the levels of activity decrease to 10% of the untreated control. Nickel, cobalt and manganese at concentrations of 10 mM decrease enzyme activity to either 40% (for nickel and cobalt) or 60% (for manganese) of the activity in untreated controls. No change in enzyme activity in the presence of calcium and magnesium at concentrations up to 50 mM. EDTA-treated enzyme exhibits a slight increase in relative specific activity when it is assayed in the presence of 50 mM NaCl or 50 mM KCl, it does not exhibit enhanced activity at concentrations greater than 250 mM. Maintains between 20 and 40% of activity in the presence of 4 M NaCl or 4 M KCl, and it is more active in the presence of KCl than in the presence of NaCl. Retains 50% of activity in the presence of 3 M KCl or 2.5 M NaCl.1 Publication

    Kineticsi

    1. KM=7.4 mM for ONPG (at 1.9 degrees Celsius and at pH 6.5)1 Publication
    2. KM=4.5 mM for ONPG (at 10 degrees Celsius and at pH 6.5)1 Publication
    3. KM=5.4 mM for ONPG (at 20 degrees Celsius and at pH 6.5)1 Publication
    4. KM=5.0 mM for ONPG (at 30 degrees Celsius and at pH 6.5)1 Publication
    5. KM=4.9 mM for ONPG (at 39 degrees Celsius and at pH 6.5)1 Publication

    Vmax=63 µmol/min/mg enzyme with ONPG as substrate (at 1.9 degrees Celsius and pH 6.5)1 Publication

    Vmax=80 µmol/min/mg enzyme with ONPG as substrate (at 10 degrees Celsius and pH 6.5)1 Publication

    Vmax=223 µmol/min/mg enzyme with ONPG as substrate (at 20 degrees Celsius and pH 6.5)1 Publication

    Vmax=392 µmol/min/mg enzyme with ONPG as substrate (at 30 degrees Celsius and pH 6.5)1 Publication

    Vmax=467 µmol/min/mg enzyme with ONPG as substrate (at 39 degrees Celsius and pH 6.5)1 Publication

    pH dependencei

    Optimum pH is 6.5.1 Publication

    Temperature dependencei

    Optimum temperature is 42 degrees Celsius. Thermostable at temperatures at or below the optimal temperature for activity, but it is rapidly denatured at temperatures above 42 degrees Celsius. Irreversibly inactivated within 10 minutes at 55 degrees Celsius. Stable during storage at 5 degrees Celsius and loses no activity during storage for 4 months. Retains 10% of activity at 0 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei112 – 1121SubstrateBy similarity
    Metal bindingi116 – 1161ZincBy similarity
    Binding sitei150 – 1501SubstrateBy similarity
    Active sitei151 – 1511Proton donorBy similarity
    Metal bindingi156 – 1561ZincBy similarity
    Metal bindingi158 – 1581ZincBy similarity
    Metal bindingi161 – 1611ZincBy similarity
    Active sitei309 – 3091NucleophileBy similarity
    Binding sitei317 – 3171SubstrateBy 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

    BRENDAi3.2.1.23. 4880.

    Protein family/group databases

    CAZyiGH42. Glycoside Hydrolase Family 42.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-galactosidase BgaA (EC:3.2.1.23)
    Short name:
    Beta-galBy similarity
    Gene namesi
    Name:bgaA1 Publication
    OrganismiPlanococcus sp. (strain 'SOS Orange')
    Taxonomic identifieri128803 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesPlanococcaceaePlanococcus

    Subcellular locationi

    GO - Cellular componenti

    1. beta-galactosidase complex Source: InterPro

    Pathology & Biotechi

    Biotechnological usei

    Possible reporter enzyme for halotolerant and halophilic organisms. May also be used in the food industry to digest plant polysaccharides in high-salt processes.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 677677Beta-galactosidase BgaAPRO_0000407692Add
    BLAST

    Interactioni

    Subunit structurei

    Dimer.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ9KI47.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni357 – 3604Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 42 family.Sequence Analysis

    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.

    Q9KI47-1 [UniParc]FASTAAdd to Basket

    « Hide

    MINDKLPKIW HGGDYNPEQW DSKEIWDEDV RMFKLAGIDV ATLNVFSWAL    50
    NQPNEDTYNF DWLDEKINRL YENGIYTCLA TSTAAHPAWM AKKYPDVLRV 100
    DFYGRKRKFG SRHNSCPNSP TYRKYSERIA ETLAERYKDH PAVLIWHVSN 150
    EYGGYCYCDN CQDAFRNWLS DKYGTLEKLN KAWNTGFWGH TFYEWDEIVA 200
    PNMLSEKRED NVSDFQGISL DYRRFQSDRL LDCYKLEYNA IRKHVPTSIP 250
    ITTNLMGTYP MLDYFKWAKE MDVVSWDNYP SIDTPFSYTA MTHDLMRGLK 300
    GGKPFMLMEQ TPSQQNWQPY NSLKRPGVMR LWSYQAIGRG ADTILYFQLR 350
    RSVGACEKYH GAVIEHVGHE HTRVFNEVAQ LGQELNGLSD TLLDARVNAK 400
    VAIVFDWENR WATELSSGPS VSLDYVNEVH KYYDALYKLN VQVDMIGVEE 450
    DLSKYDVVIA PVLYMVKEGY AAKVEKFVEN GGTFLTTFFS GIVNETDIVT 500
    LGGYPGELRK VLGIWAEEID ALHPDETNQI VVKGSRGILS GKYSCNLLFD 550
    LIHTEGAEAV AEYGSDFYKG MPVLTVNKFG KGKAWYVASS PDAEFLVDFL 600
    QTVCEEAGVE PLLDVPAGVE TTERVKDGQT YLFVLNHNND EVTIELHGSQ 650
    YREVLTDEQV SGNLVLKEKG VLILAKV 677
    Length:677
    Mass (Da):77,484
    Last modified:October 1, 2000 - v1
    Checksum:i2A1928DADC945E55
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF242542 Genomic DNA. Translation: AAF75984.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF242542 Genomic DNA. Translation: AAF75984.1 .

    3D structure databases

    ProteinModelPortali Q9KI47.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH42. Glycoside Hydrolase Family 42.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BRENDAi 3.2.1.23. 4880.

    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. "Characterization of a salt-tolerant family 42 beta-galactosidase from a psychrophilic antarctic Planococcus isolate."
      Sheridan P.P., Brenchley J.E.
      Appl. Environ. Microbiol. 66:2438-2444(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-8, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, BIOTECHNOLOGY.
      Strain: SOS OrangeImported.

    Entry informationi

    Entry nameiBGAL_PLASS
    AccessioniPrimary (citable) accession number: Q9KI47
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 48 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