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Protein

Beta-galactosidase

Gene

lacZ

Organism
Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Protein has several cofactor binding sites:
  • Mg2+Curated, Mn2+Curated, Fe cationCuratedNote: Binds 2 magnesium ions per monomer. Can also use manganese and iron.Curated
  • Na(+)Curated, K(+)CuratedNote: Binds 1 sodium ion per monomer. 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
Complete GO annotation...

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
Complete GO annotation...

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

        10         20         30         40         50
MFTASPMSLS KILARRDWEN PGVTQWHRLP AHAPFNSWRD EASARADDNA
60 70 80 90 100
SRKRSLNGDW QFSYYAAPEQ VPDSWVTEDC ADAVTTPVPS NWQMQGFDTP
110 120 130 140 150
IYTNDTYPIP VNPPFVPAEN PTGCYSLTFE VDEQWLESGQ TRIVFDGVNS
160 170 180 190 200
AFYLWCNGKW MGYSQDSRLP AEFDLSAVLR PGTNRLAVLV LRWCDGSYLE
210 220 230 240 250
DQDMWRMSGI FRDVSLLHKP HTHIADYHAV TELNADYDRA KLQVEVALAG
260 270 280 290 300
EQFADCEVAV TLWRDGLSVA TVSAKPGSAI IDERGNWAER LNVTLPVKDP
310 320 330 340 350
ALWSAETPEL YRLTFALRDG QGEILDVEAC DVGFRCVEIS NGLLKVNGKP
360 370 380 390 400
LLIRGVNRHE HHPENGQVMD EATMCRDIEL MKQHNFNAVR CSHYPNHPLW
410 420 430 440 450
YTLCDRYGLY VVDEANIETH GMVPMSRLAD DPRWLPAMSE RVTRMVLRDR
460 470 480 490 500
NHPSIIIWSL GNESGHGANH DALYRWVKTT DPTRPVQYEG GGANTAATDI
510 520 530 540 550
VCPMYARVDQ DQPFEAVPKW SLKKWIGMPD ETRPLILCEY AHAMGNSFGG
560 570 580 590 600
FAKYWQAFRN HPRLQGGFVW DWVDQALTKK DDNGNAFWAY GGDFGDTPND
610 620 630 640 650
RQFCLNGLVF PDRTPHPALF EAQRAQQFFT FTLVSTSPLV IDVHSDYLFR
660 670 680 690 700
QCDNEQLRWN IARDGEVLAS GEVALTIAPQ QTQRIEIDAP EFAAAAGEIW
710 720 730 740 750
LNVDIVQTAA TAWSPADHRC AWDQWQLPAP LYIAPPVEGT AKPDLKVKED
760 770 780 790 800
VLEVSHQSQR WHFDRASGNL TQWWNNGTAT LLAPLSDNFT RAPLDNDIGV
810 820 830 840 850
SEATRIDPNA WVERWKAAGM YNLTPRLLLC EGEQLAQAVT ITTLHAWESN
860 870 880 890 900
GKALFLSRKV WKIDRAGVLH GDVQVQVAND IPQPARIGLS CQLAQTPQTA
910 920 930 940 950
SWLGLGPDEN YPDRKLAARQ GRWTLPLDAL HTAYIFPTDN GLRCDTRELT
960 970 980 990 1000
FDTHQMQGDF HFSLSRYSQQ QLRDTSHHHL LEAEPGCWLN IDAFHMGVGG
1010 1020
DDSWSPSVSP EFILQRREMR YAFSWRQD
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. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF371803 Genomic DNA. Translation: ABN42680.1. Different initiation.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF371803 Genomic DNA. Translation: ABN42680.1. Different initiation.

3D structure databases

ProteinModelPortaliA3FEW8.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH2. Glycoside Hydrolase Family 2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKA3FEW8.

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. "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: November 26, 2014
This is version 31 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.