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A3FEW8

- BGAL_ENTAG

UniProt

A3FEW8 - BGAL_ENTAG

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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

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.UniRule annotation

Cofactori

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

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)

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

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

pH dependencei

Optimum pH is 7.5-8.0. Stable between 7.5-10.0.

Temperature dependencei

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei104 – 1041Substrate By similarity
Metal bindingi203 – 2031Sodium By similarity
Binding sitei203 – 2031Substrate By similarity
Sitei359 – 3591Transition state stabilizer By similarity
Sitei393 – 3931Transition state stabilizer By similarity
Metal bindingi418 – 4181Magnesium 1 By similarity
Metal bindingi420 – 4201Magnesium 1 By similarity
Active sitei463 – 4631Proton donor By similarity
Metal bindingi463 – 4631Magnesium 1 By similarity
Binding sitei463 – 4631Substrate By similarity
Active sitei539 – 5391Nucleophile By similarity
Metal bindingi599 – 5991Magnesium 2 By similarity
Metal bindingi603 – 6031Sodium; via carbonyl oxygen By similarity
Metal bindingi606 – 6061Sodium By similarity
Binding sitei606 – 6061Substrate By similarity
Binding sitei1004 – 10041Substrate By similarity
Sitei1004 – 10041Important 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

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-galactosidaseUniRule annotation
PRO_0000366982Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliA3FEW8.

Family & Domainsi

Region

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

A3FEW8-1 [UniParc]FASTAAdd to Basket

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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...

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: February 19, 2014
This is version 29 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

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