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P94804

- BGAL_HALL2

UniProt

P94804 - BGAL_HALL2

Protein

Beta-galactosidase BgaH

Gene

bgaH

Organism
Haloferax lucentense (strain DSM 14919 / JCM 9276 / NCIMB 13854 / Aa 2.2) (Haloferax alicantei)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 2 (01 Oct 2001)
      Previous versions | rss
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    Functioni

    When overexpressed, cleaves several different substrates including o-nitrophenyl-beta-D-galactopyranoside (ONPG), chromogen 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-Gal) and lactulose, but not lactose. Has also beta-D-fucosidase activity. No beta-L-fucosidase, beta-glucosidase, beta-arabinosidase or beta-xylosidase activity.2 Publications

    Catalytic activityi

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

    Enzyme regulationi

    Requires 4 M NaCl for maximal activity. Loss of activity if DTT or beta-mercaptoethanol is omitted from buffers. Addition of 5-20 mM EDTA, 1 mM Cu2+ or 1 mM Zn2+ results in loss of activity.1 Publication

    Kineticsi

    1. KM=0.87 mM for ONPG (in the presence of 2.5 M NaCl, at room temperature and pH 7.2)1 Publication

    Vmax=110 µmol/min/mg enzyme with ONPG as substrate (in the presence of 2.5 M NaCl, at room temperature and pH 7.2)1 Publication

    Temperature dependencei

    Stable in 3 M NaCl for several days at room temperature, but approximately 18% and 50% of specific activity is lost when samples are stored overnight at 4 and -20 degrees Celsius, respectively. Activity is irreversibly lost within minutes in low salt buffers. Activity low, but detectable in 30% sorbitol in the complete absence of salt and it is stable in 30% sorbitol for at least four months at -20 degrees Celsius, but at room temperature approximately 20% of specific activity is lost after 48 hours.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei103 – 1031SubstrateBy similarity
    Metal bindingi107 – 1071ZincBy similarity
    Binding sitei141 – 1411SubstrateBy similarity
    Active sitei142 – 1421Proton donorBy similarity
    Metal bindingi151 – 1511ZincBy similarity
    Metal bindingi153 – 1531ZincBy similarity
    Metal bindingi156 – 1561ZincBy similarity
    Active sitei311 – 3111NucleophileBy similarity
    Binding sitei319 – 3191SubstrateBy 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 BgaH (EC:3.2.1.23)
    Short name:
    Beta-galBy similarity
    Gene namesi
    Name:bgaHImported
    OrganismiHaloferax lucentense (strain DSM 14919 / JCM 9276 / NCIMB 13854 / Aa 2.2) (Haloferax alicantei)
    Taxonomic identifieri1230452 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloferax

    Subcellular locationi

    GO - Cellular componenti

    1. beta-galactosidase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 663662Beta-galactosidase BgaHPRO_0000407697Add
    BLAST

    Expressioni

    Inductioni

    Highest expression in cells grown on galactose. Glucose or glycerol, alone or in combination with galactose, gives an intermediate level of expression and peptone-containing media gives very low levels of expression.1 Publication

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliP94804.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni359 – 3624Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 42 family.Sequence Analysis

    Family and domain databases

    Gene3Di2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    3.40.50.880. 1 hit.
    InterProiIPR013739. Beta_galactosidase_C.
    IPR013738. Beta_galactosidase_Trimer.
    IPR029062. Class_I_gatase-like.
    IPR013780. Glyco_hydro_13_b.
    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P94804-1 [UniParc]FASTAAdd to Basket

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    MTVGVCYFPE HWSRERWETD ISQMAEAGIE YVRMGEFAWR RIEPERGTFD    50
    FAWLDEAVEL IGKFGMKAVL CTPTATPPKW LVDEHPDVRQ REQDGTPREW 100
    GSRRFTCFNS PTYRSETERI VSVLTDRYAD NPHVAGWQTD NEFGCHETVT 150
    CYCEDCGEAF SEWLADRYES VADLNDAWGT TFWSQQYDDF ESIDPPKPTP 200
    AANHPSRVLA YERFSNDSVA EYNRLHAALI REANDEWFVT HNFMGGFSLD 250
    AFRLAADLDF LSWDSYPTGF VQDRQPDTPT VDELRAGNPD QVSMNHDLQR 300
    GAKGKPFWVM EQQPGDINWP PQSPQPADGA MRLWAHHAVA HGADAVVYFR 350
    WRRCRQGQEQ YHAGLRRQDG SPDRGYREAS TAADELFDLD SVDASVALVH 400
    DYESLWATRS QPLSPDWDYW NHLRTYYDAL RARGVQVDIV SPEATLERYD 450
    AVVAPTLYLV GDELSTALTD YVDSGGCLLL GARTGEKDPY NRLHESLAPG 500
    PLTALTGAQV ARHETLPDHV ETRLSYDGAT YEFRTWASWL APEVGVPRGE 550
    YRTGEAAGNT AIVRNAAGDG SVTYCGCWPG DDLADALVTE LLDAAGVEYT 600
    ERFPDGVRVM ERDGYTWALN FTSDPVTLTV PDSTGFLLGE STVDAFDTAV 650
    LDGSIRGVGL ASE 663
    Length:663
    Mass (Da):74,460
    Last modified:October 1, 2001 - v2
    Checksum:i7ADF7634C5D13BE9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti21 – 211I → F AA sequence (PubMed:9048905)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U70664 Genomic DNA. Translation: AAB40123.2.
    PIRiT44793.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U70664 Genomic DNA. Translation: AAB40123.2 .
    PIRi T44793.

    3D structure databases

    ProteinModelPortali P94804.
    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 2.60.40.1180. 1 hit.
    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.
    IPR013780. Glyco_hydro_13_b.
    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. "Sequence and expression of a halobacterial beta-galactosidase gene."
      Holmes M.L., Dyall-Smith M.L.
      Mol. Microbiol. 36:114-122(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, INDUCTION.
      Strain: Aa 2.2 / SB1.
    2. Holmes M.L., Dyall-Smith M.L.
      Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO C-TERMINUS.
    3. "Purification and analysis of an extremely halophilic beta-galactosidase from Haloferax alicantei."
      Holmes M.L., Scopes R.K., Moritz R.L., Simpson R.J., Englert C., Pfeifer F., Dyall-Smith M.L.
      Biochim. Biophys. Acta 1337:276-286(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-26; 286-300; 410-424; 425-431 AND 493-512, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT.
      Strain: Aa 2.2 / SB1.

    Entry informationi

    Entry nameiBGAL_HALL2
    AccessioniPrimary (citable) accession number: P94804
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: October 1, 2001
    Last modified: October 1, 2014
    This is version 56 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

    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