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P81650

- BGAL_PSEHA

UniProt

P81650 - BGAL_PSEHA

Protein

Beta-galactosidase

Gene

lacZ

Organism
Pseudoalteromonas haloplanktis (Alteromonas haloplanktis)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    Binds 2 magnesium ions per monomer.1 Publication
    Binds 1 sodium ion per monomer.By similarity

    Enzyme regulationi

    Inhibited by zinc, copper and nickel ions. Activated by 2-mercaptoethanol and inhibited by EDTA in vitro.

    Kineticsi

    1. KM=2.4 mM for lactose (at pH 7.5 and at 25 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 8.5.1 Publication

    Temperature dependencei

    Optimum temperature is 4 degrees Celsius. It does not grow at temperatures higher than 25 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei103 – 1031SubstrateBy similarity
    Metal bindingi201 – 2011SodiumBy similarity
    Binding sitei201 – 2011SubstrateBy similarity
    Sitei356 – 3561Transition state stabilizerBy similarity
    Sitei390 – 3901Transition state stabilizerBy similarity
    Metal bindingi415 – 4151Magnesium 1By similarity
    Metal bindingi417 – 4171Magnesium 1By similarity
    Active sitei460 – 4601Proton donorBy similarity
    Metal bindingi460 – 4601Magnesium 1By similarity
    Binding sitei460 – 4601SubstrateBy similarity
    Active sitei536 – 5361NucleophileBy similarity
    Metal bindingi596 – 5961Magnesium 2By similarity
    Metal bindingi600 – 6001Sodium; via carbonyl oxygenBy similarity
    Metal bindingi603 – 6031SodiumBy similarity
    Binding sitei603 – 6031SubstrateBy similarity
    Binding sitei1012 – 10121SubstrateBy similarity
    Sitei1012 – 10121Important 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

    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
    Alternative name(s):
    Beta-D-galactoside galactohydrolase
    Lactase
    Gene namesi
    Name:lacZ
    OrganismiPseudoalteromonas haloplanktis (Alteromonas haloplanktis)
    Taxonomic identifieri228 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPseudoalteromonadaceaePseudoalteromonas

    Subcellular locationi

    GO - Cellular componenti

    1. beta-galactosidase complex Source: InterPro

    Pathology & Biotechi

    Biotechnological usei

    This cold-adapted beta-galactosidase could be used to hydrolyze lactose in milk and dairy products processed in refrigerated plants. It is in fact superior to the current commercial enzyme from K.marxiamus with respect to lactose removal, especially at low temperatures.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 10391038Beta-galactosidasePRO_0000057656Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliP81650.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni536 – 5394Substrate 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.

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

    P81650-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTSLQHIINR RDWENPITVQ VNQVKAHSPL NGFKTIEDAR ENTQSQKKSL     50
    NGQWDFKLFD KPEAVDESLL YEKISKELSG DWQSITVPSN WQLHGFDKPI 100
    YCNVKYPFAV NPPFVPSDNP TGCYRTEFTI TPEQLTQRNH IIFEGVNSAF 150
    HLWCNGQWVG YSQDSRLPSE FDLSELLVVG TNRIAVMVIR WSDGSYLEDQ 200
    DMWWLSGIFR DVNLLTKPQS QIRDVFITPD LDACYRDATL HIKTAINAPN 250
    NYQVAVQIFD GKTSLCEPKI QSTNNKRVDE KGGWSDVVFQ TIAIRSPKKW 300
    TAETPYLYRC VVSLLDEQGN TVDVEAYNIG FRKVEMLNGQ LCVNGKPLLI 350
    RGVNRHEHHP ENGHAVSTAD MIEDIKLMKQ NNFNAVRTAH YPNHPLFYEL 400
    CDELGLYVVD EANIETHGMF PMGRLASDPL WAGAFMSRYT QMVERDKNHA 450
    SIIIWSLGNE CGHGANHDAM YGWSKSFDPS RPVQYEGGGA NTTATDIICP 500
    MYSRVDTDIK DDAVPKYSIK KWLSLPGETR PLILCEYAHA MGNSLGSFDD 550
    YWQAFREYPR LQGGFIWDWV DQGLSKIDEN GKHYWAYGGD FGDELNDRQF 600
    CINGLLFPDR TPHPSLFEAK YSQQHLQFTL REQNQNQNQN QYSIDVFSDY 650
    VFRHTDNEKL VWQLIQNGVC VEQGEMALNI APQSTHTLTI KTKTAFEHGA 700
    QYYLNLDVAL INDSHFANAN HVMDSEQFKL INSNNLNSKS FASATEKSVI 750
    SVNETDSHLS IENNTFKLVF NQQSGLIEQW LQDDTQVISS PLVDNFYRAP 800
    LDNDIGVSEV DNLDPNAWEA RWSRAGIGQW QRTCSSINAV QSSVDVRITC 850
    VFNYEFNGVL QAQTQWLYTL NNTGTISLNV DVNLNDTLPP MPRIGLSTTI 900
    NKQSDTKVNW LGLGPFENYP DRKSAARFGY YSLSLNELYT PYIFPTDNGL 950
    RSDCQLLSIN NLIVTGAFLF AASEYSQNML TQAKHTNELI ADDCIHVHID 1000
    HQHMGVGGDD SWSPSTHKEY LLEQKNYNYS LTLTGGITT 1039
    Length:1,039
    Mass (Da):118,199
    Last modified:January 23, 2007 - v2
    Checksum:iD77713F653DE8231
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ131635 Genomic DNA. Translation: CAA10470.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ131635 Genomic DNA. Translation: CAA10470.1 .

    3D structure databases

    ProteinModelPortali P81650.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH2. Glycoside Hydrolase Family 2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "Cold-adapted beta-galactosidase from the Antarctic psychrophile Pseudoalteromonas haloplanktis."
      Hoyoux A., Jennes I., Dubois P., Genicot S., Dubail F., Francois J.M., Baise E., Feller G., Gerday C.
      Appl. Environ. Microbiol. 67:1529-1535(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: TAE 79.

    Entry informationi

    Entry nameiBGAL_PSEHA
    AccessioniPrimary (citable) accession number: P81650
    Secondary accession number(s): Q9ZEM8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 77 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