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A3FEW8

- BGAL_ENTAG

UniProt

A3FEW8 - BGAL_ENTAG

Protein

Beta-galactosidase

Gene

lacZ

Organism
Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 30 (01 Oct 2014)
      Sequence version 2 (24 Mar 2009)
      Previous versions | rss
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    Functioni

    This beta-galactosidase is also able to catalyze glycosyl transfer to a series of acceptors, including hexose, pentose, beta- or alpha-disaccharides, hexahydroxy alcohol, cyclitol, and aromatic glycosides, resulting in the production of galacto-oligosaccharides (GOS).1 Publication

    Catalytic activityi

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

    Cofactori

    Binds 2 magnesium ions per monomer Probable. Can also use manganese and iron.Curated
    Binds 1 sodium ion per monomer Probable. Can also use potassium.Curated

    Enzyme regulationi

    Completely inhibited by Hg2+, Cu2+ Ag2+, and partially inhibited by Zn2+, imidazole and EDTA. Activated by Ca2+, Co2+, Ni2+.1 Publication

    Kineticsi

    1. KM=0.06 mM for o-nitrophenyl-beta-D-galactopyranoside (at 37 degrees Celsius)1 Publication
    2. KM=114 mM for lactose (at 37 degrees Celsius)1 Publication

    Vmax=0.43 mmol/min/mg enzyme for o-nitrophenyl-beta-D-galactopyranoside (at 37 degrees Celsius)1 Publication

    Vmax=2.9 mmol/min/mg enzyme for o-nitrophenyl-beta-D-galactopyranoside (at 37 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 7.5-8.0. Stable between 7.5-10.0.1 Publication

    Temperature dependencei

    Optimum temperature is 37-40 degrees Celsius. Stable below 37 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei104 – 1041SubstrateBy similarity
    Metal bindingi203 – 2031SodiumBy similarity
    Binding sitei203 – 2031SubstrateBy similarity
    Sitei359 – 3591Transition state stabilizerBy similarity
    Sitei393 – 3931Transition state stabilizerBy similarity
    Metal bindingi418 – 4181Magnesium 1By similarity
    Metal bindingi420 – 4201Magnesium 1By similarity
    Active sitei463 – 4631Proton donorBy similarity
    Metal bindingi463 – 4631Magnesium 1By similarity
    Binding sitei463 – 4631SubstrateBy similarity
    Active sitei539 – 5391NucleophileBy similarity
    Metal bindingi599 – 5991Magnesium 2By similarity
    Metal bindingi603 – 6031Sodium; via carbonyl oxygenBy similarity
    Metal bindingi606 – 6061SodiumBy similarity
    Binding sitei606 – 6061SubstrateBy similarity
    Binding sitei1004 – 10041SubstrateBy similarity
    Sitei1004 – 10041Important for ensuring that an appropriate proportion of lactose is converted to allolactoseBy similarity

    GO - Molecular functioni

    1. beta-galactosidase activity Source: UniProtKB-EC
    2. carbohydrate binding Source: InterPro
    3. magnesium ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Ligandi

    Magnesium, Metal-binding, Sodium

    Enzyme and pathway databases

    SABIO-RKA3FEW8.

    Protein family/group databases

    CAZyiGH2. Glycoside Hydrolase Family 2.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-galactosidase (EC:3.2.1.23)
    Short name:
    Beta-gal
    Short name:
    Bga
    Alternative name(s):
    Lactase
    Transglycosylating beta-galactosidase
    Gene namesi
    Name:lacZ
    OrganismiEnterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans)
    Taxonomic identifieri549 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePantoea

    Subcellular locationi

    GO - Cellular componenti

    1. beta-galactosidase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10281028Beta-galactosidasePRO_0000366982Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliA3FEW8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni539 – 5424Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 2 family.Curated

    Family and domain databases

    Gene3Di2.60.120.260. 1 hit.
    2.60.40.320. 2 hits.
    2.70.98.10. 1 hit.
    3.20.20.80. 1 hit.
    HAMAPiMF_01687. Beta_gal.
    InterProiIPR004199. B-gal_small/dom_5.
    IPR011013. Gal_mutarotase_SF_dom.
    IPR008979. Galactose-bd-like.
    IPR014718. Glyco_hydro-type_carb-bd_sub.
    IPR006101. Glyco_hydro_2.
    IPR013812. Glyco_hydro_2/20_Ig-like.
    IPR023232. Glyco_hydro_2_AS.
    IPR023933. Glyco_hydro_2_beta_Galsidase.
    IPR023230. Glyco_hydro_2_CS.
    IPR006102. Glyco_hydro_2_Ig-like.
    IPR006104. Glyco_hydro_2_N.
    IPR006103. Glyco_hydro_2_TIM.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF02929. Bgal_small_N. 1 hit.
    PF00703. Glyco_hydro_2. 1 hit.
    PF02836. Glyco_hydro_2_C. 1 hit.
    PF02837. Glyco_hydro_2_N. 1 hit.
    [Graphical view]
    PRINTSiPR00132. GLHYDRLASE2.
    SMARTiSM01038. Bgal_small_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF49303. SSF49303. 2 hits.
    SSF49785. SSF49785. 1 hit.
    SSF51445. SSF51445. 1 hit.
    SSF74650. SSF74650. 1 hit.
    PROSITEiPS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
    PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    A3FEW8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFTASPMSLS KILARRDWEN PGVTQWHRLP AHAPFNSWRD EASARADDNA     50
    SRKRSLNGDW QFSYYAAPEQ VPDSWVTEDC ADAVTTPVPS NWQMQGFDTP 100
    IYTNDTYPIP VNPPFVPAEN PTGCYSLTFE VDEQWLESGQ TRIVFDGVNS 150
    AFYLWCNGKW MGYSQDSRLP AEFDLSAVLR PGTNRLAVLV LRWCDGSYLE 200
    DQDMWRMSGI FRDVSLLHKP HTHIADYHAV TELNADYDRA KLQVEVALAG 250
    EQFADCEVAV TLWRDGLSVA TVSAKPGSAI IDERGNWAER LNVTLPVKDP 300
    ALWSAETPEL YRLTFALRDG QGEILDVEAC DVGFRCVEIS NGLLKVNGKP 350
    LLIRGVNRHE HHPENGQVMD EATMCRDIEL MKQHNFNAVR CSHYPNHPLW 400
    YTLCDRYGLY VVDEANIETH GMVPMSRLAD DPRWLPAMSE RVTRMVLRDR 450
    NHPSIIIWSL GNESGHGANH DALYRWVKTT DPTRPVQYEG GGANTAATDI 500
    VCPMYARVDQ DQPFEAVPKW SLKKWIGMPD ETRPLILCEY AHAMGNSFGG 550
    FAKYWQAFRN HPRLQGGFVW DWVDQALTKK DDNGNAFWAY GGDFGDTPND 600
    RQFCLNGLVF PDRTPHPALF EAQRAQQFFT FTLVSTSPLV IDVHSDYLFR 650
    QCDNEQLRWN IARDGEVLAS GEVALTIAPQ QTQRIEIDAP EFAAAAGEIW 700
    LNVDIVQTAA TAWSPADHRC AWDQWQLPAP LYIAPPVEGT AKPDLKVKED 750
    VLEVSHQSQR WHFDRASGNL TQWWNNGTAT LLAPLSDNFT RAPLDNDIGV 800
    SEATRIDPNA WVERWKAAGM YNLTPRLLLC EGEQLAQAVT ITTLHAWESN 850
    GKALFLSRKV WKIDRAGVLH GDVQVQVAND IPQPARIGLS CQLAQTPQTA 900
    SWLGLGPDEN YPDRKLAARQ GRWTLPLDAL HTAYIFPTDN GLRCDTRELT 950
    FDTHQMQGDF HFSLSRYSQQ QLRDTSHHHL LEAEPGCWLN IDAFHMGVGG 1000
    DDSWSPSVSP EFILQRREMR YAFSWRQD 1028
    Length:1,028
    Mass (Da):116,394
    Last modified:March 24, 2009 - v2
    Checksum:i5A72487AB243185D
    GO

    Sequence cautioni

    The sequence ABN42680.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF371803 Genomic DNA. Translation: ABN42680.1. Different initiation.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF371803 Genomic DNA. Translation: ABN42680.1 . Different initiation.

    3D structure databases

    ProteinModelPortali A3FEW8.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH2. Glycoside Hydrolase Family 2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK A3FEW8.

    Family and domain databases

    Gene3Di 2.60.120.260. 1 hit.
    2.60.40.320. 2 hits.
    2.70.98.10. 1 hit.
    3.20.20.80. 1 hit.
    HAMAPi MF_01687. Beta_gal.
    InterProi IPR004199. B-gal_small/dom_5.
    IPR011013. Gal_mutarotase_SF_dom.
    IPR008979. Galactose-bd-like.
    IPR014718. Glyco_hydro-type_carb-bd_sub.
    IPR006101. Glyco_hydro_2.
    IPR013812. Glyco_hydro_2/20_Ig-like.
    IPR023232. Glyco_hydro_2_AS.
    IPR023933. Glyco_hydro_2_beta_Galsidase.
    IPR023230. Glyco_hydro_2_CS.
    IPR006102. Glyco_hydro_2_Ig-like.
    IPR006104. Glyco_hydro_2_N.
    IPR006103. Glyco_hydro_2_TIM.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF02929. Bgal_small_N. 1 hit.
    PF00703. Glyco_hydro_2. 1 hit.
    PF02836. Glyco_hydro_2_C. 1 hit.
    PF02837. Glyco_hydro_2_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00132. GLHYDRLASE2.
    SMARTi SM01038. Bgal_small_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49303. SSF49303. 2 hits.
    SSF49785. SSF49785. 1 hit.
    SSF51445. SSF51445. 1 hit.
    SSF74650. SSF74650. 1 hit.
    PROSITEi PS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
    PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel beta-galactosidase capable of glycosyl transfer from Enterobacter agglomerans B1."
      Lu L., Xiao M., Xu X., Li Z., Li Y.
      Biochem. Biophys. Res. Commun. 356:78-84(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-9, FUNCTION AS TRANSGLYCOSYLATING BETA-GALACTOSIDASE, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.
      Strain: B1.

    Entry informationi

    Entry nameiBGAL_ENTAG
    AccessioniPrimary (citable) accession number: A3FEW8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: March 24, 2009
    Last modified: October 1, 2014
    This is version 30 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