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Q8VNN2 (BGAL_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-galactosidase

Short name=Beta-gal
EC=3.2.1.23
Alternative name(s):
Lactase
Gene names
Name:lacZ
Encoded onPlasmid pMH11
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length1029 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. HAMAP-Rule MF_01687

Cofactor

Binds 2 magnesium ions per monomer By similarity. HAMAP-Rule MF_01687

Binds 1 sodium ion per monomer By similarity. HAMAP-Rule MF_01687

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_01687

Sequence similarities

Belongs to the glycosyl hydrolase 2 family.

Ontologies

Keywords
   LigandMagnesium
Metal-binding
Sodium
   Molecular functionGlycosidase
Hydrolase
   Technical termPlasmid
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentbeta-galactosidase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionbeta-galactosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

carbohydrate binding

Inferred from electronic annotation. Source: InterPro

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10291029Beta-galactosidase HAMAP-Rule MF_01687
PRO_0000366988

Regions

Region543 – 5464Substrate binding By similarity

Sites

Active site4671Proton donor By similarity
Active site5431Nucleophile By similarity
Metal binding2071Sodium By similarity
Metal binding4221Magnesium 1 By similarity
Metal binding4241Magnesium 1 By similarity
Metal binding4671Magnesium 1 By similarity
Metal binding6031Magnesium 2 By similarity
Metal binding6071Sodium; via carbonyl oxygen By similarity
Metal binding6101Sodium By similarity
Binding site1081Substrate By similarity
Binding site2071Substrate By similarity
Binding site4671Substrate By similarity
Binding site6101Substrate By similarity
Binding site10051Substrate By similarity
Site3631Transition state stabilizer By similarity
Site3971Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8VNN2 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 46C5DF38322A2F26

FASTA1,029116,967
        10         20         30         40         50         60 
MTMITPSFPG NSLAVVLQRR DWENPGVTQL NRLAAHPPFA SWRNSEEART DRPSQQLRSL 

        70         80         90        100        110        120 
NGEWRFAWFP APEAVPESWL ECDLPEADTV VVPSNWQMHG YDAPIYTNVT YPITVNPPFV 

       130        140        150        160        170        180 
PTENPTGCYS LTFNVDESWL QEGQTRIIFD GVNSAFHLWC NGRWVGYGQD SRLPSEFDLS 

       190        200        210        220        230        240 
AFLRAGENRL AVMVLRWSDG SYLEDQDMWR MSGIFRDVSL LHKPTTQISD FHVATRFNDD 

       250        260        270        280        290        300 
FSRAVLEAEV QMCGELRDYL RVTVSLWQGE TQVASGTAPF GGEIIDERGG YADRVTLRLN 

       310        320        330        340        350        360 
VENPKLWSAE IPNLYRAVVE LHTADGTLIE AEACDVGFRE VRIENGLLLL NGKPLLIRGV 

       370        380        390        400        410        420 
NRHEHHPLHG QVMDEQTMVQ DILLMKQNNF NAVRCSHYPN HPLWYTLCDR YGLYVVDEAN 

       430        440        450        460        470        480 
IETHGMVPMN RLTDDPRWLP AMSERVTRMV QRDRNHPSVI IWSLGNESGH GANHDALYRW 

       490        500        510        520        530        540 
IKSVDPSRPV QYEGGGADTT ATDIICPMYA RVDEDQPFPA VPKWSIKKWL SLPGETRPLI 

       550        560        570        580        590        600 
LCEYAHAMGN SLGGFAKYWQ AFRQYPRLQG GFVWDWVDQS LIKYDENGNP WSAYGGDFGD 

       610        620        630        640        650        660 
TPNDRQFCMN GLVFADRTPH PALTEAKHQQ QFFQFRLSGQ TIEVTSEYLF RHSDNELLHW 

       670        680        690        700        710        720 
MVALDGKPLA SGEVPLDVAP QGKQLIELPE LPQPESAGQL WLTVRVVQPN ATAWSEAGHI 

       730        740        750        760        770        780 
SAWQQWRLAE NLSVTLPAAS HAIPHLTTSE MDFCIELGNK RWQFNRQSGF LSQMWIGDKK 

       790        800        810        820        830        840 
QLLTPLRDQF TRAPLDNDIG VSEATRIDPN AWVERWKAAG HYQAEAALLQ CTADTLADAV 

       850        860        870        880        890        900 
LITTAHAWQH QGKTLFISRK TYRIDGSGQM AITVDVEVAS DTPHPARIGL NCQLAQVAER 

       910        920        930        940        950        960 
VNWLGLGPQE NYPDRLTAAC FDRWDLPLSD MYTPYVFPSE NGLRCGTREL NYGPHQWRGD 

       970        980        990       1000       1010       1020 
FQFNISRYSQ QQLMETSHRH LLHAEEGTWL NIDGFHMGIG GDDSWSPSVS AEFQLSAGRY 


HYQLVWCQK 

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References

[1]"pMH11, A tool for gene disruption and expression analysis in Azorhizobium caulinodans."
D'Haeze W., Verplancke C., Mironov V., Holsters M.
Plasmid 47:88-93(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ308295 Genomic DNA. Translation: CAC87491.1.

3D structure databases

ProteinModelPortalQ8VNN2.
SMRQ8VNN2. Positions 19-1029.
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL1293264.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG3250.

Family and domain databases

Gene3D2.60.120.260. 1 hit.
2.60.40.320. 2 hits.
2.70.98.10. 1 hit.
3.20.20.80. 1 hit.
HAMAPMF_01687. Beta_gal.
InterProIPR004199. 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]
PfamPF02929. 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]
PRINTSPR00132. GLHYDRLASE2.
SMARTSM01038. Bgal_small_N. 1 hit.
[Graphical view]
SUPFAMSSF49303. SSF49303. 2 hits.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF74650. SSF74650. 1 hit.
PROSITEPS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBGAL_ECOLX
AccessionPrimary (citable) accession number: Q8VNN2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 1, 2002
Last modified: February 19, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries