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Protein

Beta-galactosidase

Gene

lacZ

Organism
Pseudoalteromonas haloplanktis (Alteromonas haloplanktis)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:

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

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Ligandi

    Magnesium, Metal-binding, Sodium

    Enzyme and pathway databases

    BRENDAi3.2.1.23. 5081.

    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

    Complete GO annotation...

    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

    Protein-protein interaction databases

    STRINGi722419.PH505_bt00220.

    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

            10         20         30         40         50
    MTSLQHIINR RDWENPITVQ VNQVKAHSPL NGFKTIEDAR ENTQSQKKSL
    60 70 80 90 100
    NGQWDFKLFD KPEAVDESLL YEKISKELSG DWQSITVPSN WQLHGFDKPI
    110 120 130 140 150
    YCNVKYPFAV NPPFVPSDNP TGCYRTEFTI TPEQLTQRNH IIFEGVNSAF
    160 170 180 190 200
    HLWCNGQWVG YSQDSRLPSE FDLSELLVVG TNRIAVMVIR WSDGSYLEDQ
    210 220 230 240 250
    DMWWLSGIFR DVNLLTKPQS QIRDVFITPD LDACYRDATL HIKTAINAPN
    260 270 280 290 300
    NYQVAVQIFD GKTSLCEPKI QSTNNKRVDE KGGWSDVVFQ TIAIRSPKKW
    310 320 330 340 350
    TAETPYLYRC VVSLLDEQGN TVDVEAYNIG FRKVEMLNGQ LCVNGKPLLI
    360 370 380 390 400
    RGVNRHEHHP ENGHAVSTAD MIEDIKLMKQ NNFNAVRTAH YPNHPLFYEL
    410 420 430 440 450
    CDELGLYVVD EANIETHGMF PMGRLASDPL WAGAFMSRYT QMVERDKNHA
    460 470 480 490 500
    SIIIWSLGNE CGHGANHDAM YGWSKSFDPS RPVQYEGGGA NTTATDIICP
    510 520 530 540 550
    MYSRVDTDIK DDAVPKYSIK KWLSLPGETR PLILCEYAHA MGNSLGSFDD
    560 570 580 590 600
    YWQAFREYPR LQGGFIWDWV DQGLSKIDEN GKHYWAYGGD FGDELNDRQF
    610 620 630 640 650
    CINGLLFPDR TPHPSLFEAK YSQQHLQFTL REQNQNQNQN QYSIDVFSDY
    660 670 680 690 700
    VFRHTDNEKL VWQLIQNGVC VEQGEMALNI APQSTHTLTI KTKTAFEHGA
    710 720 730 740 750
    QYYLNLDVAL INDSHFANAN HVMDSEQFKL INSNNLNSKS FASATEKSVI
    760 770 780 790 800
    SVNETDSHLS IENNTFKLVF NQQSGLIEQW LQDDTQVISS PLVDNFYRAP
    810 820 830 840 850
    LDNDIGVSEV DNLDPNAWEA RWSRAGIGQW QRTCSSINAV QSSVDVRITC
    860 870 880 890 900
    VFNYEFNGVL QAQTQWLYTL NNTGTISLNV DVNLNDTLPP MPRIGLSTTI
    910 920 930 940 950
    NKQSDTKVNW LGLGPFENYP DRKSAARFGY YSLSLNELYT PYIFPTDNGL
    960 970 980 990 1000
    RSDCQLLSIN NLIVTGAFLF AASEYSQNML TQAKHTNELI ADDCIHVHID
    1010 1020 1030
    HQHMGVGGDD SWSPSTHKEY LLEQKNYNYS LTLTGGITT
    Length:1,039
    Mass (Da):118,199
    Last modified:January 23, 2007 - v2
    Checksum:iD77713F653DE8231
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ131635 Genomic DNA. Translation: CAA10470.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ131635 Genomic DNA. Translation: CAA10470.1.

    3D structure databases

    ProteinModelPortaliP81650.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi722419.PH505_bt00220.

    Protein family/group databases

    CAZyiGH2. Glycoside Hydrolase Family 2.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BRENDAi3.2.1.23. 5081.

    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]
    ProtoNetiSearch...

    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: June 24, 2015
    This is version 80 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

    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.