Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

C8WV58

- BGAL_ALIAD

UniProt

C8WV58 - BGAL_ALIAD

Protein

Beta-galactosidase BglY

Gene

bglY

Organism
Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / 104-1A) (Bacillus acidocaldarius)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 30 (01 Oct 2014)
      Sequence version 1 (03 Nov 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Hydrolyzes o-nitrophenyl-beta-D-galactopyranoside (ONPG) and p-nitrophenyl-beta-D-fucopyranoside (PNPF), but not p-nitrophenyl-beta-D-glucopyranoside (PNPG), p-nitrophenyl-beta-D-xylopyranoside (PNPX) or p-nitrophenyl-beta-D-arabinopyranoside (PNPA). Also hydrolyzes lactose, including lactose in milk.1 Publication

    Catalytic activityi

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

    Enzyme regulationi

    Ca2+, Mg2+ and EDTA have little effect on enzyme activity at 1-10 mM. Zn2+ at 3, 5, 7 or 10 mM inhibits activity by 20%, 30%, 40% and 65%, respectively.1 Publication

    Kineticsi

    1. KM=6 mM for ONPG (at 60 degrees Celsius and pH 6.0)1 Publication
    2. KM=3.5 mM for PNPF (at 60 degrees Celsius and pH 6.0)1 Publication

    pH dependencei

    Optimum pH is 5.8. Approximately 80% of activity retained after incubating the enzyme for 40 minutes in buffers ranging from pH 5.0 to pH 10.5.1 Publication

    Temperature dependencei

    Optimum temperature is 70 degrees Celsius. Retains 90% of activity when heated at 70 degrees Celsius for 30 minutes. Approximately 48% of lactose in milk is hydrolyzed following treatment with enzyme at 65 degrees Celsius over 60 minutes.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei118 – 1181SubstrateBy similarity
    Metal bindingi122 – 1221ZincBy similarity
    Binding sitei156 – 1561SubstrateBy similarity
    Active sitei157 – 1571Proton donorBy similarity
    Metal bindingi162 – 1621ZincBy similarity
    Metal bindingi164 – 1641ZincBy similarity
    Metal bindingi167 – 1671ZincBy similarity
    Active sitei313 – 3131NucleophileBy similarity
    Binding sitei321 – 3211SubstrateBy 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

    BioCyciAACI521098:GCIO-2974-MONOMER.

    Protein family/group databases

    CAZyiGH42. Glycoside Hydrolase Family 42.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-galactosidase BglY (EC:3.2.1.23)
    Short name:
    Beta-galBy similarity
    Gene namesi
    Name:bglY
    Ordered Locus Names:Aaci_2891
    OrganismiAlicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / 104-1A) (Bacillus acidocaldarius)
    Taxonomic identifieri521098 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesAlicyclobacillaceaeAlicyclobacillus
    ProteomesiUP000001917: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. beta-galactosidase complex Source: InterPro

    Pathology & Biotechi

    Biotechnological usei

    Has potential use in hydrolyzing lactose in neutral pH dairy products such as whole milk or whey. Also could be used in milk lactose hydrolysis during pasteurization at high temperatures.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 688688Beta-galactosidase BglYPRO_0000407679Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi521098.Aaci_2891.

    Structurei

    3D structure databases

    ProteinModelPortaliC8WV58.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni361 – 3644Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 42 family.Sequence Analysis

    Phylogenomic databases

    eggNOGiCOG1874.
    HOGENOMiHOG000117811.
    KOiK12308.
    OMAiCFLGGFP.
    OrthoDBiEOG6GTZGG.

    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.

    C8WV58-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKHAPIFPN VQGFLHGGDY NPDQWLAYPD VLEQDVQLMR EAKWNVVSLG    50
    IFSWVSLEPE EGLFTFEWLD EAIERLTHAG VRILLATPSG ARPAWLSAKY 100
    PEVLRVGPDG RRNRHGGRHN HCYTSPIYRE KVRIINRKLA ERYAHHPGVI 150
    GWHVSNEYGG ECHCPLCQEA FREWLKRKYK TLDALNHAWW TPFWSHTYTD 200
    WSQIESPMPH GETSIHGLNL DWKRFVTDQT VDFCRHEIEP LKQVNPNLPV 250
    TTNFMGTYPG LNYWRFRDVL DVISWDSYPR WHAHETLVPE AVHTAMVHDL 300
    NRSILKKPFL LMESTPSVTN WQAVSKQKRP GVHVLVSLQA VAHGADSVQY 350
    FQWRKSRGSY EKFHGAVVDH VGHANTRVFR DVQAVGEMLE RLAPMAGAEV 400
    KADAAVIFDW ENRWALEDAK GPRNIGMHYE ETVVNHYAAL WRMGVPMDVI 450
    DEEQPLDGYK LVVAPMLYMV RPGVAERMKA FVERGGSLVL TYWSGIVDEN 500
    DLVFLGGFPG PLRELAGVWA EEIDALYDGE RVPVRVADGN PLGLAGHYEA 550
    RELCEVVHLE GAEPIAVYGA DYYEGMPAAT VHRVGKGKVY YVAARLEDAF 600
    LRDFFARVAA EAGVARAIER ELPDGVSAMV RSGDGVEYVM LMNFTPEARE 650
    VALDEAEYKP LYGEAPTDGA VRLPAYGVSV LERPARNG 688
    Length:688
    Mass (Da):77,869
    Last modified:November 3, 2009 - v1
    Checksum:i686AFEA665822767
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti543 – 5442Missing AA sequence (PubMed:17914606)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ887754 Genomic DNA. Translation: ABI84370.1.
    CP001727 Genomic DNA. Translation: ACV59895.1.
    RefSeqiWP_012812096.1. NC_013205.1.
    YP_003186284.1. NC_013205.1.

    Genome annotation databases

    EnsemblBacteriaiACV59895; ACV59895; Aaci_2891.
    GeneIDi8426432.
    KEGGiaac:Aaci_2891.
    PATRICi20849346. VBIAliAci73240_2885.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ887754 Genomic DNA. Translation: ABI84370.1 .
    CP001727 Genomic DNA. Translation: ACV59895.1 .
    RefSeqi WP_012812096.1. NC_013205.1.
    YP_003186284.1. NC_013205.1.

    3D structure databases

    ProteinModelPortali C8WV58.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 521098.Aaci_2891.

    Protein family/group databases

    CAZyi GH42. Glycoside Hydrolase Family 42.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACV59895 ; ACV59895 ; Aaci_2891 .
    GeneIDi 8426432.
    KEGGi aac:Aaci_2891.
    PATRICi 20849346. VBIAliAci73240_2885.

    Phylogenomic databases

    eggNOGi COG1874.
    HOGENOMi HOG000117811.
    KOi K12308.
    OMAi CFLGGFP.
    OrthoDBi EOG6GTZGG.

    Enzyme and pathway databases

    BioCyci AACI521098:GCIO-2974-MONOMER.

    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. "Heterologous expression of a gene encoding a thermostable beta-galactosidase from Alicyclobacillus acidocaldarius."
      Yuan T., Yang P., Wang Y., Meng K., Luo H., Zhang W., Wu N., Fan Y., Yao B.
      Biotechnol. Lett. 30:343-348(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-8; 536-551 AND 637-649, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, BIOTECHNOLOGY.
      Strain: ATCC 27009 / DSM 446 / 104-1AImported.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 27009 / DSM 446 / 104-1AImported.

    Entry informationi

    Entry nameiBGAL_ALIAD
    AccessioniPrimary (citable) accession number: C8WV58
    Secondary accession number(s): Q06GJ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: November 3, 2009
    Last modified: October 1, 2014
    This is version 30 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

    Complete proteome, Direct protein sequencing, Reference proteome

    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