SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P81650

- BGAL_PSEHA

UniProt

P81650 - BGAL_PSEHA

(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)

Protein
Beta-galactosidase
Gene
lacZ
Organism
Pseudoalteromonas haloplanktis (Alteromonas haloplanktis)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

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

Enzyme regulationi

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

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.

Temperature dependencei

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei103 – 1031Substrate By similarity
Metal bindingi201 – 2011Sodium By similarity
Binding sitei201 – 2011Substrate By similarity
Sitei356 – 3561Transition state stabilizer By similarity
Sitei390 – 3901Transition state stabilizer By similarity
Metal bindingi415 – 4151Magnesium 1 By similarity
Metal bindingi417 – 4171Magnesium 1 By similarity
Active sitei460 – 4601Proton donor By similarity
Metal bindingi460 – 4601Magnesium 1 By similarity
Binding sitei460 – 4601Substrate By similarity
Active sitei536 – 5361Nucleophile By similarity
Metal bindingi596 – 5961Magnesium 2 By similarity
Metal bindingi600 – 6001Sodium; via carbonyl oxygen By similarity
Metal bindingi603 – 6031Sodium By similarity
Binding sitei603 – 6031Substrate By similarity
Binding sitei1012 – 10121Substrate By similarity
Sitei1012 – 10121Important for ensuring that an appropriate proportion of lactose is converted to allolactose By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

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
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.UniRule annotation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 10391038Beta-galactosidaseUniRule annotation
PRO_0000057656Add
BLAST

Interactioni

Subunit structurei

Homotetramer Inferred.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP81650.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni536 – 5394Substrate binding By similarity

Sequence similaritiesi

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...

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: February 19, 2014
This is version 76 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