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C7ASJ5

- BGAL2_ARTSP

UniProt

C7ASJ5 - BGAL2_ARTSP

Protein

Beta-galactosidase

Gene
N/A
Organism
Arthrobacter sp.
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 15 (01 Oct 2014)
      Sequence version 1 (22 Sep 2009)
      Previous versions | rss
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    Functioni

    Hydrolyzes p-nitrophenyl-beta-D-galactopyranoside (PNPG), o-nitrophenyl-beta-D-galactopyranoside (ONPG) and chromogen 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-gal), with highest activity against PNPG. Also acts on p-nitrophenyl-beta-D-glucopyranoside (PNPGlu) and o-nitrophenyl-beta-D-glucopyranoside (ONPGlu), but with significantly lower activity.1 Publication

    Catalytic activityi

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

    Enzyme regulationi

    Strongly inhibited by glucose. No activity is lost during treatment with 100 mM EDTA after 2 hours. Activity not considerably affected by metal ions (5 mM), including Na+, K+, Mg2+, Co2+ and Ca2+. Completely inhibited by Cu2+ and Zn2+ (5 mM) and is strongly inhibited by Mn2+ (11%), Fe2+ (25%) and Ni2+ (38%) in comparison with the activity in the absence of cations (100%). Activity not affected by dithiothreitol, beta-mercaptoethanol and L-cysteine whereas reduced glutathione almost completely inactivates it. With ONPG as substrate, the addition of ethanol up to 20% still slightly stimulates activity. The activity increases up to 120% in the presence of 8% v/v ethanol at pH 5.5.1 Publication

    Kineticsi

    1. KM=5.75 mM for ONPG (at 10 degrees Celsius)1 Publication
    2. KM=4.86 mM for ONPG (at 20 degrees Celsius)1 Publication
    3. KM=3.46 mM for ONPG (at 30 degrees Celsius)1 Publication
    4. KM=3.15 mM for ONPG (at 40 degrees Celsius)1 Publication
    5. KM=2.62 mM for ONPG (at 50 degrees Celsius)1 Publication
    6. KM=5.11 mM for ONPG (at 55 degrees Celsius)1 Publication
    7. KM=77.54 mM for lactose (at 10 degrees Celsius)1 Publication
    8. KM=67.82 mM for lactose (at 20 degrees Celsius)1 Publication
    9. KM=52.67 mM for lactose (at 30 degrees Celsius)1 Publication
    10. KM=44.31 mM for lactose (at 40 degrees Celsius)1 Publication
    11. KM=39.73 mM for lactose (at 50 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 6.5 with ONPG as substrate. Over 90% of activity in the pH range 6.5-8.5. Highly efficient at pH range 4.5-9.5.1 Publication

    Temperature dependencei

    Optimum temperature is 50 degrees Celsius with ONPG as substrate. Active at 4-8 degrees Celsius. 60% of the maximum activity is detected at 25 degrees Celsius and 15% at 0 degrees Celsius. Over 50% activity at 30 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei144 – 1441SubstrateBy similarity
    Binding sitei182 – 1821SubstrateBy similarity
    Active sitei183 – 1831Proton donorBy similarity
    Active sitei341 – 3411NucleophileBy similarity
    Binding sitei349 – 3491SubstrateBy similarity

    GO - Molecular functioni

    1. beta-galactosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. galactose metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-galactosidase (EC:3.2.1.23)
    Short name:
    Beta-galBy similarity
    OrganismiArthrobacter sp.
    Taxonomic identifieri1667 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter

    Subcellular locationi

    GO - Cellular componenti

    1. beta-galactosidase complex Source: InterPro

    Pathology & Biotechi

    Biotechnological usei

    Has potential use in lactose removal in milk and dairy products at low temperatures and for cheese whey bioremediation processes with simultaneous bio-ethanol production.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 694694Beta-galactosidasePRO_0000407681Add
    BLAST

    Interactioni

    Subunit structurei

    Homotrimer.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliC7ASJ5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni389 – 3924Substrate 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.

    C7ASJ5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGKRFPSGWF SPRVHPPRRQ RSPMTNQATP GTASVWNNIE GIGFGGDYNP    50
    EQWPVSVRLE DLELMQEAGV NFLSVGIFSW ALLEPAEGQY DFGWLDDVMD 100
    NLHGIGVKVA LATATAAPPA WLVRKHPEIL PVTADGTTLG PGSRRHYTPS 150
    SAVYRKYAAG ITRVLAERYK DHPALALWHV DNELGCHVSE FYGEEDAAAF 200
    RLWLERRYGT IDALNAAWGT AFWSQHYGSF EEILPPGVAP STLNPGQQLD 250
    FQRFNSWALM DYYRSLVAVL REVTPAVPCT TNLMASSATK SMDYFSWAKD 300
    LDVIANDHYL VAADPERHIE LAFSADLTRG IAGGDPWILM EHSTSAVNWQ 350
    PRNQPKMPGE MLRNSLAHVA RGADAVMFFQ WRQSFAGSEK FHSAMVPHGG 400
    RDTRVWREVV DLGAALQLLA PVRGSRVESR AAIVFDYEAW WASEIDSKPS 450
    IDVRYLDLLR AFHRSLFLRG VSVDMVHPSA SLDGYDLVLV CTLYSVTDEA 500
    AANIAAAAAG GATVLVSYFS GITDEKDHVR LGGYPGAFRE LLGVRVEEFH 550
    PLLAGSQLKL SDGTVSSIWS EHVHLDGAEA FQTFTGYPLE GVPSLTRRAV 600
    GTGAAWYLAT FPDRDGIESL VDRLLAESGV SPVAEADAGV ELTRRRSADG 650
    GSFLFAINHT RAAASVRASG TDVLSGERFT GTVEAGSVAV IAED 694
    Length:694
    Mass (Da):75,915
    Last modified:September 22, 2009 - v1
    Checksum:i2A352EDCF797BE74
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FJ609657 Genomic DNA. Translation: ACU00913.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FJ609657 Genomic DNA. Translation: ACU00913.1 .

    3D structure databases

    ProteinModelPortali C7ASJ5.
    ModBasei Search...
    MobiDBi Search...

    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. "A new cold-adapted beta-D-galactosidase from the Antarctic Arthrobacter sp. 32c - gene cloning, overexpression, purification and properties."
      Hildebrandt P., Wanarska M., Kur J.
      BMC Microbiol. 9:151-151(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, BIOTECHNOLOGY.
      Strain: 32cImported.

    Entry informationi

    Entry nameiBGAL2_ARTSP
    AccessioniPrimary (citable) accession number: C7ASJ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: September 22, 2009
    Last modified: October 1, 2014
    This is version 15 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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