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Protein

Beta-galactosidase

Gene
N/A
Organism
Arthrobacter sp.
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BRENDAi3.2.1.23. 457.

    Names & Taxonomyi

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

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    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

            10         20         30         40         50
    MGKRFPSGWF SPRVHPPRRQ RSPMTNQATP GTASVWNNIE GIGFGGDYNP
    60 70 80 90 100
    EQWPVSVRLE DLELMQEAGV NFLSVGIFSW ALLEPAEGQY DFGWLDDVMD
    110 120 130 140 150
    NLHGIGVKVA LATATAAPPA WLVRKHPEIL PVTADGTTLG PGSRRHYTPS
    160 170 180 190 200
    SAVYRKYAAG ITRVLAERYK DHPALALWHV DNELGCHVSE FYGEEDAAAF
    210 220 230 240 250
    RLWLERRYGT IDALNAAWGT AFWSQHYGSF EEILPPGVAP STLNPGQQLD
    260 270 280 290 300
    FQRFNSWALM DYYRSLVAVL REVTPAVPCT TNLMASSATK SMDYFSWAKD
    310 320 330 340 350
    LDVIANDHYL VAADPERHIE LAFSADLTRG IAGGDPWILM EHSTSAVNWQ
    360 370 380 390 400
    PRNQPKMPGE MLRNSLAHVA RGADAVMFFQ WRQSFAGSEK FHSAMVPHGG
    410 420 430 440 450
    RDTRVWREVV DLGAALQLLA PVRGSRVESR AAIVFDYEAW WASEIDSKPS
    460 470 480 490 500
    IDVRYLDLLR AFHRSLFLRG VSVDMVHPSA SLDGYDLVLV CTLYSVTDEA
    510 520 530 540 550
    AANIAAAAAG GATVLVSYFS GITDEKDHVR LGGYPGAFRE LLGVRVEEFH
    560 570 580 590 600
    PLLAGSQLKL SDGTVSSIWS EHVHLDGAEA FQTFTGYPLE GVPSLTRRAV
    610 620 630 640 650
    GTGAAWYLAT FPDRDGIESL VDRLLAESGV SPVAEADAGV ELTRRRSADG
    660 670 680 690
    GSFLFAINHT RAAASVRASG TDVLSGERFT GTVEAGSVAV IAED
    Length:694
    Mass (Da):75,915
    Last modified:September 22, 2009 - v1
    Checksum:i2A352EDCF797BE74
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    FJ609657 Genomic DNA. Translation: ACU00913.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    FJ609657 Genomic DNA. Translation: ACU00913.1.

    3D structure databases

    ProteinModelPortaliC7ASJ5.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BRENDAi3.2.1.23. 457.

    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.
    ProtoNetiSearch...

    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: June 24, 2015
    This is version 17 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.